data_9GH0
# 
_entry.id   9GH0 
# 
_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   9GH0         pdb_00009gh0 10.2210/pdb9gh0/pdb 
WWPDB D_1292140430 ?            ?                   
# 
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                        9GH0 
_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 9GH1 PDB . 
unspecified 9GGW PDB . 
unspecified 9GGX PDB . 
unspecified 9GGU PDB . 
unspecified 9GGT PDB . 
unspecified 9GGV PDB . 
unspecified 9G0Y PDB . 
unspecified 9G4B PDB . 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              alexander.schuettelkopf@cancer.org.uk 
_pdbx_contact_author.name_first         Alexander 
_pdbx_contact_author.name_last          Schuettelkopf 
_pdbx_contact_author.name_mi            W. 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-9424-8730 
# 
_audit_author.name               'Schuettelkopf, A.W.' 
_audit_author.pdbx_ordinal       1 
_audit_author.identifier_ORCID   0000-0002-9424-8730 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            J.Med.Chem. 
_citation.journal_id_ASTM           JMCMAR 
_citation.journal_id_CSD            0151 
_citation.journal_id_ISSN           0022-2623 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            68 
_citation.language                  ? 
_citation.page_first                9129 
_citation.page_last                 9161 
_citation.title                     
'Reversible Small Molecule Multivariant Ras Inhibitors Display Tunable Affinity for the Active and Inactive Forms of Ras.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1021/acs.jmedchem.4c02929 
_citation.pdbx_database_id_PubMed   40162713 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Parry, C.W.'        1  ? 
primary 'Pellicano, F.'      2  ? 
primary 'Schuttelkopf, A.W.' 3  ? 
primary 'Beyer, K.S.'        4  ? 
primary 'Bower, J.'          5  ? 
primary 'Bryson, A.'         6  ? 
primary 'Cameron, K.'        7  ? 
primary 'Cerutti, N.M.'      8  ? 
primary 'Clark, J.P.'        9  ? 
primary 'Davidson, S.C.'     10 ? 
primary 'Davies, K.'         11 ? 
primary 'Drysdale, M.J.'     12 ? 
primary 'Engelman, J.'       13 ? 
primary 'Estevan-Barber, A.' 14 ? 
primary 'Gohlke, A.'         15 ? 
primary 'Gray, C.H.'         16 ? 
primary 'Guthy, D.A.'        17 ? 
primary 'Hong, M.'           18 ? 
primary 'Hopkins, A.'        19 ? 
primary 'Hutchinson, L.D.'   20 ? 
primary 'Konczal, J.'        21 ? 
primary 'Maira, M.'          22 ? 
primary 'McArthur, D.'       23 ? 
primary 'Mezna, M.'          24 ? 
primary 'McKinnon, H.'       25 ? 
primary 'Nepravishta, R.'    26 ? 
primary 'Ostermann, N.'      27 ? 
primary 'Pasquali, C.C.'     28 ? 
primary 'Pollock, K.'        29 ? 
primary 'Pugliese, A.'       30 ? 
primary 'Rooney, N.'         31 ? 
primary 'Schmiedeberg, N.'   32 ? 
primary 'Shaw, P.'           33 ? 
primary 'Velez-Vega, C.'     34 ? 
primary 'West, C.'           35 ? 
primary 'West, R.'           36 ? 
primary 'Zecri, F.'          37 ? 
primary 'Taylor, J.B.'       38 ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'GTPase KRas' 19607.078 1  3.6.5.2 C118S ? ? 
2 non-polymer syn 'PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER' 522.196   1  ?       ?     ? ? 
3 non-polymer syn 'MAGNESIUM ION' 24.305    1  ?       ?     ? ? 
4 non-polymer syn 'COBALT (II) ION' 58.933    2  ?       ?     ? ? 
5 non-polymer syn 
;(3Z)-18-(4-aminocyclohexyl)-7-chloro-10-hydroxy-2,2-dioxo-21-piperazin-1-yl-2-lambda-6,5-dithia-3,12,18,22-tetrazatetracyclo[18.3.1.04,12.06,11]tetracosa-1(23),3,6,8,10,20(24),21-heptaen-19-one
;
634.213   1  ?       ?     ? ? 
6 water       nat water 18.015    62 ?       ?     ? ? 
# 
_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 'PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER' GNP   
3 'MAGNESIUM ION' MG    
4 'COBALT (II) ION' CO    
5 
;(3Z)-18-(4-aminocyclohexyl)-7-chloro-10-hydroxy-2,2-dioxo-21-piperazin-1-yl-2-lambda-6,5-dithia-3,12,18,22-tetrazatetracyclo[18.3.1.04,12.06,11]tetracosa-1(23),3,6,8,10,20(24),21-heptaen-19-one
;
A1IMA 
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 
A1IMA non-polymer         . 
;(3Z)-18-(4-aminocyclohexyl)-7-chloro-10-hydroxy-2,2-dioxo-21-piperazin-1-yl-2-lambda-6,5-dithia-3,12,18,22-tetrazatetracyclo[18.3.1.04,12.06,11]tetracosa-1(23),3,6,8,10,20(24),21-heptaen-19-one
;
? 'C28 H36 Cl N7 O4 S2' 634.213 
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 
CO    non-polymer         . 'COBALT (II) ION' ? 'Co 2'                58.933  
CYS   'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S'        121.158 
GLN   'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3'        146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'          147.129 
GLY   'peptide linking'   y GLYCINE ? 'C2 H5 N O2'          75.067  
GNP   non-polymer         . 'PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER' ? 'C10 H17 N6 O13 P3'   522.196 
HIS   'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1'      156.162 
HOH   non-polymer         . WATER ? 'H2 O'                18.015  
ILE   'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2'         131.173 
LEU   'L-peptide linking' y LEUCINE ? 'C6 H13 N O2'         131.173 
LYS   'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1'      147.195 
MET   'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S'       149.211 
MG    non-polymer         . 'MAGNESIUM ION' ? 'Mg 2'                24.305  
PHE   'L-peptide linking' y PHENYLALANINE ? 'C9 H11 N O2'         165.189 
PRO   'L-peptide linking' y PROLINE ? 'C5 H9 N O2'          115.130 
SER   'L-peptide linking' y SERINE ? 'C3 H7 N O3'          105.093 
THR   'L-peptide linking' y THREONINE ? 'C4 H9 N O3'          119.119 
TYR   'L-peptide linking' y TYROSINE ? 'C9 H11 N O3'         181.189 
VAL   'L-peptide linking' y VALINE ? 'C5 H11 N O2'         117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   GLY 1   -2  ?   ?   ?   A . n 
A 1 2   GLY 2   -1  ?   ?   ?   A . n 
A 1 3   SER 3   0   ?   ?   ?   A . n 
A 1 4   MET 4   1   1   MET MET A . n 
A 1 5   THR 5   2   2   THR THR A . n 
A 1 6   GLU 6   3   3   GLU GLU A . n 
A 1 7   TYR 7   4   4   TYR TYR A . n 
A 1 8   LYS 8   5   5   LYS LYS A . n 
A 1 9   LEU 9   6   6   LEU LEU A . n 
A 1 10  VAL 10  7   7   VAL VAL A . n 
A 1 11  VAL 11  8   8   VAL VAL A . n 
A 1 12  VAL 12  9   9   VAL VAL A . n 
A 1 13  GLY 13  10  10  GLY GLY A . n 
A 1 14  ALA 14  11  11  ALA ALA A . n 
A 1 15  GLY 15  12  12  GLY GLY A . n 
A 1 16  GLY 16  13  13  GLY GLY A . n 
A 1 17  VAL 17  14  14  VAL VAL A . n 
A 1 18  GLY 18  15  15  GLY GLY A . n 
A 1 19  LYS 19  16  16  LYS LYS A . n 
A 1 20  SER 20  17  17  SER SER A . n 
A 1 21  ALA 21  18  18  ALA ALA A . n 
A 1 22  LEU 22  19  19  LEU LEU A . n 
A 1 23  THR 23  20  20  THR THR A . n 
A 1 24  ILE 24  21  21  ILE ILE A . n 
A 1 25  GLN 25  22  22  GLN GLN A . n 
A 1 26  LEU 26  23  23  LEU LEU A . n 
A 1 27  ILE 27  24  24  ILE ILE A . n 
A 1 28  GLN 28  25  25  GLN GLN A . n 
A 1 29  ASN 29  26  26  ASN ASN A . n 
A 1 30  HIS 30  27  27  HIS HIS A . n 
A 1 31  PHE 31  28  28  PHE PHE A . n 
A 1 32  VAL 32  29  29  VAL VAL A . n 
A 1 33  ASP 33  30  30  ASP ASP A . n 
A 1 34  GLU 34  31  31  GLU GLU A . n 
A 1 35  TYR 35  32  ?   ?   ?   A . n 
A 1 36  ASP 36  33  ?   ?   ?   A . n 
A 1 37  PRO 37  34  ?   ?   ?   A . n 
A 1 38  THR 38  35  ?   ?   ?   A . n 
A 1 39  ILE 39  36  ?   ?   ?   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  ?   ?   ?   A . n 
A 1 65  GLU 65  62  ?   ?   ?   A . n 
A 1 66  GLU 66  63  ?   ?   ?   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 GNP   1  201 1000 GNP   GNP A . 
C 3 MG    1  202 1001 MG    MG  A . 
D 4 CO    1  203 1    CO    CO  A . 
E 4 CO    1  204 2    CO    CO  A . 
F 5 A1IMA 1  205 1    A1IMA DRG A . 
G 6 HOH   1  301 1    HOH   HOH A . 
G 6 HOH   2  302 63   HOH   HOH A . 
G 6 HOH   3  303 2    HOH   HOH A . 
G 6 HOH   4  304 50   HOH   HOH A . 
G 6 HOH   5  305 64   HOH   HOH A . 
G 6 HOH   6  306 101  HOH   HOH A . 
G 6 HOH   7  307 132  HOH   HOH A . 
G 6 HOH   8  308 4    HOH   HOH A . 
G 6 HOH   9  309 87   HOH   HOH A . 
G 6 HOH   10 310 78   HOH   HOH A . 
G 6 HOH   11 311 109  HOH   HOH A . 
G 6 HOH   12 312 129  HOH   HOH A . 
G 6 HOH   13 313 52   HOH   HOH A . 
G 6 HOH   14 314 210  HOH   HOH A . 
G 6 HOH   15 315 113  HOH   HOH A . 
G 6 HOH   16 316 155  HOH   HOH A . 
G 6 HOH   17 317 9    HOH   HOH A . 
G 6 HOH   18 318 209  HOH   HOH A . 
G 6 HOH   19 319 141  HOH   HOH A . 
G 6 HOH   20 320 42   HOH   HOH A . 
G 6 HOH   21 321 120  HOH   HOH A . 
G 6 HOH   22 322 133  HOH   HOH A . 
G 6 HOH   23 323 5    HOH   HOH A . 
G 6 HOH   24 324 123  HOH   HOH A . 
G 6 HOH   25 325 61   HOH   HOH A . 
G 6 HOH   26 326 145  HOH   HOH A . 
G 6 HOH   27 327 201  HOH   HOH A . 
G 6 HOH   28 328 122  HOH   HOH A . 
G 6 HOH   29 329 202  HOH   HOH A . 
G 6 HOH   30 330 30   HOH   HOH A . 
G 6 HOH   31 331 102  HOH   HOH A . 
G 6 HOH   32 332 206  HOH   HOH A . 
G 6 HOH   33 333 127  HOH   HOH A . 
G 6 HOH   34 334 193  HOH   HOH A . 
G 6 HOH   35 335 112  HOH   HOH A . 
G 6 HOH   36 336 26   HOH   HOH A . 
G 6 HOH   37 337 3    HOH   HOH A . 
G 6 HOH   38 338 200  HOH   HOH A . 
G 6 HOH   39 339 100  HOH   HOH A . 
G 6 HOH   40 340 124  HOH   HOH A . 
G 6 HOH   41 341 126  HOH   HOH A . 
G 6 HOH   42 342 53   HOH   HOH A . 
G 6 HOH   43 343 157  HOH   HOH A . 
G 6 HOH   44 344 28   HOH   HOH A . 
G 6 HOH   45 345 207  HOH   HOH A . 
G 6 HOH   46 346 163  HOH   HOH A . 
G 6 HOH   47 347 205  HOH   HOH A . 
G 6 HOH   48 348 57   HOH   HOH A . 
G 6 HOH   49 349 208  HOH   HOH A . 
G 6 HOH   50 350 62   HOH   HOH A . 
G 6 HOH   51 351 142  HOH   HOH A . 
G 6 HOH   52 352 204  HOH   HOH A . 
G 6 HOH   53 353 134  HOH   HOH A . 
G 6 HOH   54 354 211  HOH   HOH A . 
G 6 HOH   55 355 45   HOH   HOH A . 
G 6 HOH   56 356 135  HOH   HOH A . 
G 6 HOH   57 357 139  HOH   HOH A . 
G 6 HOH   58 358 199  HOH   HOH A . 
G 6 HOH   59 359 140  HOH   HOH A . 
G 6 HOH   60 360 137  HOH   HOH A . 
G 6 HOH   61 361 148  HOH   HOH A . 
G 6 HOH   62 362 212  HOH   HOH A . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 0 A ARG 73  ? CG  ? A ARG 76  CG  
2  1 Y 0 A ARG 73  ? CD  ? A ARG 76  CD  
3  1 Y 0 A ARG 73  ? NE  ? A ARG 76  NE  
4  1 Y 0 A ARG 73  ? CZ  ? A ARG 76  CZ  
5  1 Y 0 A ARG 73  ? NH1 ? A ARG 76  NH1 
6  1 Y 0 A ARG 73  ? NH2 ? A ARG 76  NH2 
7  1 Y 0 A GLU 107 ? CG  ? A GLU 110 CG  
8  1 Y 0 A GLU 107 ? CD  ? A GLU 110 CD  
9  1 Y 0 A GLU 107 ? OE1 ? A GLU 110 OE1 
10 1 Y 0 A GLU 107 ? OE2 ? A GLU 110 OE2 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement        ? ? ? ? ? ? ? ? ? ? ? REFMAC      ? ? ? 5.8.0258 1 
? 'data scaling'    ? ? ? ? ? ? ? ? ? ? ? Aimless     ? ? ? 0.7.4    2 
? 'data extraction' ? ? ? ? ? ? ? ? ? ? ? PDB_EXTRACT ? ? ? 3.22     3 
? 'data reduction'  ? ? ? ? ? ? ? ? ? ? ? XDS         ? ? ? .        4 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   109.710 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9GH0 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     72.037 
_cell.length_a_esd                 ? 
_cell.length_b                     34.230 
_cell.length_b_esd                 ? 
_cell.length_c                     69.527 
_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                         9GH0 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                5 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'C 1 2 1' 
_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                   9GH0 
_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             2.06 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          40.23 
_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               0.220 
_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              7.5 
_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    '24% PEG 3350, 100 mM MgCl2, 10 mM CoCl2, 100 mM HEPES' 
_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 EIGER X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2020-12-11 
_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   0.9795 
_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        0.9795 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   I04 
_diffrn_source.pdbx_synchrotron_site       Diamond 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9GH0 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.570 
_reflns.d_resolution_low                               28.920 
_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                                     22125 
_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                           98.600 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                3.300 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          20.300 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.033 
_reflns.pdbx_Rpim_I_all                                0.018 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       73005 
_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                              0.028 
_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 
1.570 1.610  ? ? ? ? ? ? 1458 ? ? ? ? ? ? ? ? ? ? ? 2.600 ? ? ? 0.633 0.361 ? 1 1 0.923 ? ? 88.000 ? 0.515 ? ? ? ? ? ? ? ? ? 
7.030 28.920 ? ? ? ? ? ? 262  ? ? ? ? ? ? ? ? ? ? ? 3.100 ? ? ? 0.018 0.010 ? 2 1 1.000 ? ? 95.800 ? 0.015 ? ? ? ? ? ? ? ? ? 
# 
_refine.aniso_B[1][1]                            -0.5500 
_refine.aniso_B[1][2]                            0.0000 
_refine.aniso_B[1][3]                            0.9400 
_refine.aniso_B[2][2]                            2.9200 
_refine.aniso_B[2][3]                            0.0000 
_refine.aniso_B[3][3]                            -2.4200 
_refine.B_iso_max                                86.300 
_refine.B_iso_mean                               41.4790 
_refine.B_iso_min                                24.530 
_refine.correlation_coeff_Fo_to_Fc               0.9660 
_refine.correlation_coeff_Fo_to_Fc_free          0.9540 
_refine.details                                  'U VALUES      : WITH TLS ADDED HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9GH0 
_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                            1.5700 
_refine.ls_d_res_low                             28.9200 
_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                     20987 
_refine.ls_number_reflns_R_free                  1068 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    98.2000 
_refine.ls_percent_reflns_R_free                 4.8000 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2140 
_refine.ls_R_factor_R_free                       0.2403 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2127 
_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                       0.1040 
_refine.pdbx_overall_ESU_R_Free                  0.1010 
_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                             9.8040 
_refine.overall_SU_ML                            0.1310 
_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                       1.5700 
_refine_hist.d_res_low                        28.9200 
_refine_hist.number_atoms_solvent             62 
_refine_hist.number_atoms_total               1432 
_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       161 
_refine_hist.pdbx_B_iso_mean_ligand           44.63 
_refine_hist.pdbx_B_iso_mean_solvent          45.94 
_refine_hist.pdbx_number_atoms_protein        1293 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         77 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.019  0.013  1381 ? r_bond_refined_d       ? ? 
'X-RAY DIFFRACTION' ? 0.035  0.018  1270 ? r_bond_other_d         ? ? 
'X-RAY DIFFRACTION' ? 1.683  1.711  1873 ? r_angle_refined_deg    ? ? 
'X-RAY DIFFRACTION' ? 2.339  1.644  2941 ? r_angle_other_deg      ? ? 
'X-RAY DIFFRACTION' ? 4.226  5.000  158  ? r_dihedral_angle_1_deg ? ? 
'X-RAY DIFFRACTION' ? 31.276 21.867 75   ? r_dihedral_angle_2_deg ? ? 
'X-RAY DIFFRACTION' ? 14.155 15.000 238  ? r_dihedral_angle_3_deg ? ? 
'X-RAY DIFFRACTION' ? 13.064 15.000 11   ? r_dihedral_angle_4_deg ? ? 
'X-RAY DIFFRACTION' ? 0.127  0.200  181  ? r_chiral_restr         ? ? 
'X-RAY DIFFRACTION' ? 0.008  0.020  1501 ? r_gen_planes_refined   ? ? 
'X-RAY DIFFRACTION' ? 0.009  0.020  284  ? r_gen_planes_other     ? ? 
'X-RAY DIFFRACTION' ? 1.582  2.494  641  ? r_mcbond_it            ? ? 
'X-RAY DIFFRACTION' ? 1.571  2.489  640  ? r_mcbond_other         ? ? 
'X-RAY DIFFRACTION' ? 2.389  3.714  796  ? r_mcangle_it           ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.5730 
_refine_ls_shell.d_res_low                        1.6140 
_refine_ls_shell.number_reflns_all                1468 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             63 
_refine_ls_shell.number_reflns_R_work             1405 
_refine_ls_shell.percent_reflns_obs               89.3500 
_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                  0.3780 
_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                  0.3820 
# 
_struct.entry_id                     9GH0 
_struct.title                        'Human KRas4A (GMPPNP) in complex with compound 32' 
_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        9GH0 
_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              9GH0 
_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 9GH0 GLY A 1   ? UNP P01116 ?   ?   'expression tag'      -2  1 
1 9GH0 GLY A 2   ? UNP P01116 ?   ?   'expression tag'      -1  2 
1 9GH0 SER A 3   ? UNP P01116 ?   ?   'expression tag'      0   3 
1 9GH0 SER A 121 ? UNP P01116 CYS 118 'engineered mutation' 118 4 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 1850 ? 
1 MORE         -31  ? 
1 'SSA (A^2)'  8280 ? 
# 
_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 95  ? ASN A 86  ASP A 92  1 ? 7  
HELX_P HELX_P4 AA4 ASP A 95  ? LYS A 107 ? ASP A 92  LYS A 104 1 ? 13 
HELX_P HELX_P5 AA5 ASP A 129 ? GLY A 141 ? ASP A 126 GLY A 138 1 ? 13 
HELX_P HELX_P6 AA6 ARG A 154 ? 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 ? ? ? ? ? ? ? 2.074 ? ? 
metalc2  metalc ? ? A HIS 30  NE2 ? ? ? 1_555 D CO  . CO ? ? A HIS 27  A CO  203 1_555 ? ? ? ? ? ? ? 2.077 ? ? 
metalc3  metalc ? ? A HIS 97  NE2 ? ? ? 1_555 E CO  . CO ? ? A HIS 94  A CO  204 1_555 ? ? ? ? ? ? ? 2.384 ? ? 
metalc4  metalc ? ? A HIS 98  NE2 ? ? ? 1_555 E CO  . CO ? ? A HIS 95  A CO  204 2_655 ? ? ? ? ? ? ? 2.118 ? ? 
metalc5  metalc ? ? A GLU 101 OE1 ? ? ? 1_555 E CO  . CO ? ? A GLU 98  A CO  204 1_555 ? ? ? ? ? ? ? 2.139 ? ? 
metalc6  metalc ? ? B GNP .   O1G ? ? ? 1_555 C MG  . MG ? ? A GNP 201 A MG  202 1_555 ? ? ? ? ? ? ? 2.203 ? ? 
metalc7  metalc ? ? B GNP .   O2B ? ? ? 1_555 C MG  . MG ? ? A GNP 201 A MG  202 1_555 ? ? ? ? ? ? ? 2.192 ? ? 
metalc8  metalc ? ? C MG  .   MG  ? ? ? 1_555 G HOH . O  ? ? A MG  202 A HOH 304 1_555 ? ? ? ? ? ? ? 2.027 ? ? 
metalc9  metalc ? ? C MG  .   MG  ? ? ? 1_555 G HOH . O  ? ? A MG  202 A HOH 306 1_555 ? ? ? ? ? ? ? 2.160 ? ? 
metalc10 metalc ? ? C MG  .   MG  ? ? ? 1_555 G HOH . O  ? ? A MG  202 A HOH 338 1_555 ? ? ? ? ? ? ? 1.891 ? ? 
metalc11 metalc ? ? D CO  .   CO  ? ? ? 1_555 G HOH . O  ? ? A CO  203 A HOH 327 1_555 ? ? ? ? ? ? ? 1.881 ? ? 
metalc12 metalc ? ? D CO  .   CO  ? ? ? 1_555 G HOH . O  ? ? A CO  203 A HOH 329 1_555 ? ? ? ? ? ? ? 1.777 ? ? 
metalc13 metalc ? ? E CO  .   CO  ? ? ? 1_555 G HOH . O  ? ? A CO  204 A HOH 332 1_555 ? ? ? ? ? ? ? 2.195 ? ? 
metalc14 metalc ? ? E CO  .   CO  ? ? ? 1_555 G HOH . O  ? ? A CO  204 A HOH 345 1_555 ? ? ? ? ? ? ? 2.102 ? ? 
metalc15 metalc ? ? E CO  .   CO  ? ? ? 1_555 G HOH . O  ? ? A CO  204 A HOH 347 2_655 ? ? ? ? ? ? ? 2.196 ? ? 
# 
_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 O1G ? B GNP .   ? A GNP 201 ? 1_555 174.2 ? 
2  OG  ? A SER 20  ? A SER 17  ? 1_555 MG ? C MG . ? A MG 202 ? 1_555 O2B ? B GNP .   ? A GNP 201 ? 1_555 87.0  ? 
3  O1G ? B GNP .   ? A GNP 201 ? 1_555 MG ? C MG . ? A MG 202 ? 1_555 O2B ? B GNP .   ? A GNP 201 ? 1_555 88.6  ? 
4  OG  ? A SER 20  ? A SER 17  ? 1_555 MG ? C MG . ? A MG 202 ? 1_555 O   ? G HOH .   ? A HOH 304 ? 1_555 86.5  ? 
5  O1G ? B GNP .   ? A GNP 201 ? 1_555 MG ? C MG . ? A MG 202 ? 1_555 O   ? G HOH .   ? A HOH 304 ? 1_555 90.3  ? 
6  O2B ? B GNP .   ? A GNP 201 ? 1_555 MG ? C MG . ? A MG 202 ? 1_555 O   ? G HOH .   ? A HOH 304 ? 1_555 95.5  ? 
7  OG  ? A SER 20  ? A SER 17  ? 1_555 MG ? C MG . ? A MG 202 ? 1_555 O   ? G HOH .   ? A HOH 306 ? 1_555 84.8  ? 
8  O1G ? B GNP .   ? A GNP 201 ? 1_555 MG ? C MG . ? A MG 202 ? 1_555 O   ? G HOH .   ? A HOH 306 ? 1_555 98.4  ? 
9  O2B ? B GNP .   ? A GNP 201 ? 1_555 MG ? C MG . ? A MG 202 ? 1_555 O   ? G HOH .   ? A HOH 306 ? 1_555 83.6  ? 
10 O   ? G HOH .   ? A HOH 304 ? 1_555 MG ? C MG . ? A MG 202 ? 1_555 O   ? G HOH .   ? A HOH 306 ? 1_555 171.3 ? 
11 OG  ? A SER 20  ? A SER 17  ? 1_555 MG ? C MG . ? A MG 202 ? 1_555 O   ? G HOH .   ? A HOH 338 ? 1_555 92.0  ? 
12 O1G ? B GNP .   ? A GNP 201 ? 1_555 MG ? C MG . ? A MG 202 ? 1_555 O   ? G HOH .   ? A HOH 338 ? 1_555 92.5  ? 
13 O2B ? B GNP .   ? A GNP 201 ? 1_555 MG ? C MG . ? A MG 202 ? 1_555 O   ? G HOH .   ? A HOH 338 ? 1_555 178.9 ? 
14 O   ? G HOH .   ? A HOH 304 ? 1_555 MG ? C MG . ? A MG 202 ? 1_555 O   ? G HOH .   ? A HOH 338 ? 1_555 85.0  ? 
15 O   ? G HOH .   ? A HOH 306 ? 1_555 MG ? C MG . ? A MG 202 ? 1_555 O   ? G HOH .   ? A HOH 338 ? 1_555 95.8  ? 
16 NE2 ? A HIS 30  ? A HIS 27  ? 1_555 CO ? D CO . ? A CO 203 ? 1_555 O   ? G HOH .   ? A HOH 327 ? 1_555 88.7  ? 
17 NE2 ? A HIS 30  ? A HIS 27  ? 1_555 CO ? D CO . ? A CO 203 ? 1_555 O   ? G HOH .   ? A HOH 329 ? 1_555 92.4  ? 
18 O   ? G HOH .   ? A HOH 327 ? 1_555 CO ? D CO . ? A CO 203 ? 1_555 O   ? G HOH .   ? A HOH 329 ? 1_555 177.3 ? 
19 NE2 ? A HIS 97  ? A HIS 94  ? 1_555 CO ? E CO . ? A CO 204 ? 1_555 NE2 ? A HIS 98  ? A HIS 95  ? 1_555 66.4  ? 
20 NE2 ? A HIS 97  ? A HIS 94  ? 1_555 CO ? E CO . ? A CO 204 ? 1_555 OE1 ? A GLU 101 ? A GLU 98  ? 1_555 82.0  ? 
21 NE2 ? A HIS 98  ? A HIS 95  ? 1_555 CO ? E CO . ? A CO 204 ? 1_555 OE1 ? A GLU 101 ? A GLU 98  ? 1_555 109.0 ? 
22 NE2 ? A HIS 97  ? A HIS 94  ? 1_555 CO ? E CO . ? A CO 204 ? 1_555 O   ? G HOH .   ? A HOH 332 ? 1_555 176.2 ? 
23 NE2 ? A HIS 98  ? A HIS 95  ? 1_555 CO ? E CO . ? A CO 204 ? 1_555 O   ? G HOH .   ? A HOH 332 ? 1_555 117.3 ? 
24 OE1 ? A GLU 101 ? A GLU 98  ? 1_555 CO ? E CO . ? A CO 204 ? 1_555 O   ? G HOH .   ? A HOH 332 ? 1_555 97.2  ? 
25 NE2 ? A HIS 97  ? A HIS 94  ? 1_555 CO ? E CO . ? A CO 204 ? 1_555 O   ? G HOH .   ? A HOH 345 ? 1_555 91.2  ? 
26 NE2 ? A HIS 98  ? A HIS 95  ? 1_555 CO ? E CO . ? A CO 204 ? 1_555 O   ? G HOH .   ? A HOH 345 ? 1_555 37.9  ? 
27 OE1 ? A GLU 101 ? A GLU 98  ? 1_555 CO ? E CO . ? A CO 204 ? 1_555 O   ? G HOH .   ? A HOH 345 ? 1_555 85.7  ? 
28 O   ? G HOH .   ? A HOH 332 ? 1_555 CO ? E CO . ? A CO 204 ? 1_555 O   ? G HOH .   ? A HOH 345 ? 1_555 92.4  ? 
29 NE2 ? A HIS 97  ? A HIS 94  ? 1_555 CO ? E CO . ? A CO 204 ? 1_555 O   ? G HOH .   ? A HOH 347 ? 2_655 87.7  ? 
30 NE2 ? A HIS 98  ? A HIS 95  ? 1_555 CO ? E CO . ? A CO 204 ? 1_555 O   ? G HOH .   ? A HOH 347 ? 2_655 146.7 ? 
31 OE1 ? A GLU 101 ? A GLU 98  ? 1_555 CO ? E CO . ? A CO 204 ? 1_555 O   ? G HOH .   ? A HOH 347 ? 2_655 86.3  ? 
32 O   ? G HOH .   ? A HOH 332 ? 1_555 CO ? E CO . ? A CO 204 ? 1_555 O   ? G HOH .   ? A HOH 347 ? 2_655 88.5  ? 
33 O   ? G HOH .   ? A HOH 345 ? 1_555 CO ? E CO . ? A CO 204 ? 1_555 O   ? G HOH .   ? A HOH 347 ? 2_655 172.0 ? 
# 
_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 ? THR A 147 ? PHE A 141 THR A 144 
# 
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 LYS A 45  ? N LYS A 42  O LEU A 56  ? O LEU A 53  
AA1 2 3 O ASP A 57  ? O ASP A 54  N TYR A 7   ? N TYR A 4   
AA1 3 4 N VAL A 12  ? N VAL A 9   O VAL A 84  ? O VAL A 81  
AA1 4 5 N PHE A 85  ? N PHE A 82  O ASN A 119 ? O ASN A 116 
AA1 5 6 N LEU A 116 ? N LEU A 113 O ILE A 145 ? O ILE A 142 
# 
_pdbx_entry_details.entry_id                   9GH0 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     ? 
_pdbx_entry_details.has_protein_modification   N 
# 
_pdbx_validate_torsion.id              1 
_pdbx_validate_torsion.PDB_model_num   1 
_pdbx_validate_torsion.auth_comp_id    LYS 
_pdbx_validate_torsion.auth_asym_id    A 
_pdbx_validate_torsion.auth_seq_id     117 
_pdbx_validate_torsion.PDB_ins_code    ? 
_pdbx_validate_torsion.label_alt_id    ? 
_pdbx_validate_torsion.phi             72.97 
_pdbx_validate_torsion.psi             34.64 
# 
_pdbx_refine_tls.id               1 
_pdbx_refine_tls.pdbx_refine_id   'X-RAY DIFFRACTION' 
_pdbx_refine_tls.details          ? 
_pdbx_refine_tls.method           refined 
_pdbx_refine_tls.origin_x         29.0170 
_pdbx_refine_tls.origin_y         -0.4770 
_pdbx_refine_tls.origin_z         15.4110 
_pdbx_refine_tls.T[1][1]          0.0356 
_pdbx_refine_tls.T[1][1]_esd      ? 
_pdbx_refine_tls.T[1][2]          0.0059 
_pdbx_refine_tls.T[1][2]_esd      ? 
_pdbx_refine_tls.T[1][3]          0.0437 
_pdbx_refine_tls.T[1][3]_esd      ? 
_pdbx_refine_tls.T[2][2]          0.0475 
_pdbx_refine_tls.T[2][2]_esd      ? 
_pdbx_refine_tls.T[2][3]          0.0181 
_pdbx_refine_tls.T[2][3]_esd      ? 
_pdbx_refine_tls.T[3][3]          0.0707 
_pdbx_refine_tls.T[3][3]_esd      ? 
_pdbx_refine_tls.L[1][1]          3.3807 
_pdbx_refine_tls.L[1][1]_esd      ? 
_pdbx_refine_tls.L[1][2]          0.0111 
_pdbx_refine_tls.L[1][2]_esd      ? 
_pdbx_refine_tls.L[1][3]          -0.3819 
_pdbx_refine_tls.L[1][3]_esd      ? 
_pdbx_refine_tls.L[2][2]          1.9584 
_pdbx_refine_tls.L[2][2]_esd      ? 
_pdbx_refine_tls.L[2][3]          0.0555 
_pdbx_refine_tls.L[2][3]_esd      ? 
_pdbx_refine_tls.L[3][3]          3.2551 
_pdbx_refine_tls.L[3][3]_esd      ? 
_pdbx_refine_tls.S[1][1]          0.0235 
_pdbx_refine_tls.S[1][1]_esd      ? 
_pdbx_refine_tls.S[1][2]          -0.2764 
_pdbx_refine_tls.S[1][2]_esd      ? 
_pdbx_refine_tls.S[1][3]          -0.1560 
_pdbx_refine_tls.S[1][3]_esd      ? 
_pdbx_refine_tls.S[2][1]          0.0232 
_pdbx_refine_tls.S[2][1]_esd      ? 
_pdbx_refine_tls.S[2][2]          0.0093 
_pdbx_refine_tls.S[2][2]_esd      ? 
_pdbx_refine_tls.S[2][3]          0.0745 
_pdbx_refine_tls.S[2][3]_esd      ? 
_pdbx_refine_tls.S[3][1]          -0.1418 
_pdbx_refine_tls.S[3][1]_esd      ? 
_pdbx_refine_tls.S[3][2]          -0.0675 
_pdbx_refine_tls.S[3][2]_esd      ? 
_pdbx_refine_tls.S[3][3]          -0.0328 
_pdbx_refine_tls.S[3][3]_esd      ? 
# 
_pdbx_refine_tls_group.id                  1 
_pdbx_refine_tls_group.pdbx_refine_id      'X-RAY DIFFRACTION' 
_pdbx_refine_tls_group.refine_tls_id       1 
_pdbx_refine_tls_group.beg_label_asym_id   ? 
_pdbx_refine_tls_group.beg_label_seq_id    ? 
_pdbx_refine_tls_group.beg_auth_asym_id    A 
_pdbx_refine_tls_group.beg_auth_seq_id     1 
_pdbx_refine_tls_group.beg_PDB_ins_code    ? 
_pdbx_refine_tls_group.end_label_asym_id   ? 
_pdbx_refine_tls_group.end_label_seq_id    ? 
_pdbx_refine_tls_group.end_auth_asym_id    A 
_pdbx_refine_tls_group.end_auth_seq_id     205 
_pdbx_refine_tls_group.end_PDB_ins_code    ? 
_pdbx_refine_tls_group.selection           ? 
_pdbx_refine_tls_group.selection_details   ? 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A GLY -2 ? A GLY 1  
2  1 Y 1 A GLY -1 ? A GLY 2  
3  1 Y 1 A SER 0  ? A SER 3  
4  1 Y 1 A TYR 32 ? A TYR 35 
5  1 Y 1 A ASP 33 ? A ASP 36 
6  1 Y 1 A PRO 34 ? A PRO 37 
7  1 Y 1 A THR 35 ? A THR 38 
8  1 Y 1 A ILE 36 ? A ILE 39 
9  1 Y 1 A GLN 61 ? A GLN 64 
10 1 Y 1 A GLU 62 ? A GLU 65 
11 1 Y 1 A GLU 63 ? A GLU 66 
# 
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 
A1IMA CBK    C  N N 1   
A1IMA CBL    C  N N 2   
A1IMA CBM    C  N N 3   
A1IMA NBP    N  N N 4   
A1IMA CBN    C  N N 5   
A1IMA CBO    C  N N 6   
A1IMA CBJ    C  N N 7   
A1IMA NAQ    N  N N 8   
A1IMA CAB    C  N N 9   
A1IMA OAA    O  N N 10  
A1IMA CAR    C  N N 11  
A1IMA CAS    C  N N 12  
A1IMA CAT    C  N N 13  
A1IMA CAU    C  N N 14  
A1IMA CAV    C  N N 15  
A1IMA NAW    N  N N 16  
A1IMA CAX    C  Y N 17  
A1IMA CAY    C  Y N 18  
A1IMA OBD    O  N N 19  
A1IMA CAZ    C  Y N 20  
A1IMA CBA    C  Y N 21  
A1IMA CBB    C  Y N 22  
A1IMA CLBC   CL N N 23  
A1IMA CBI    C  Y N 24  
A1IMA SBH    S  N N 25  
A1IMA CBG    C  N N 26  
A1IMA NBF    N  N N 27  
A1IMA SAH    S  N N 28  
A1IMA OAI    O  N N 29  
A1IMA OBE    O  N N 30  
A1IMA CAG    C  Y N 31  
A1IMA CAF    C  Y N 32  
A1IMA NAE    N  Y N 33  
A1IMA CAJ    C  Y N 34  
A1IMA CAC    C  Y N 35  
A1IMA CAD    C  Y N 36  
A1IMA NAK    N  N N 37  
A1IMA CAL    C  N N 38  
A1IMA CAM    C  N N 39  
A1IMA NAN    N  N N 40  
A1IMA CAO    C  N N 41  
A1IMA CAP    C  N N 42  
A1IMA H1     H  N N 43  
A1IMA H2     H  N N 44  
A1IMA H3     H  N N 45  
A1IMA H4     H  N N 46  
A1IMA H5     H  N N 47  
A1IMA H6     H  N N 48  
A1IMA H7     H  N N 49  
A1IMA H9     H  N N 50  
A1IMA H10    H  N N 51  
A1IMA H11    H  N N 52  
A1IMA H12    H  N N 53  
A1IMA H13    H  N N 54  
A1IMA H14    H  N N 55  
A1IMA H15    H  N N 56  
A1IMA H16    H  N N 57  
A1IMA H17    H  N N 58  
A1IMA H18    H  N N 59  
A1IMA H19    H  N N 60  
A1IMA H20    H  N N 61  
A1IMA H21    H  N N 62  
A1IMA H22    H  N N 63  
A1IMA H23    H  N N 64  
A1IMA H24    H  N N 65  
A1IMA H25    H  N N 66  
A1IMA H26    H  N N 67  
A1IMA H30    H  N N 68  
A1IMA H31    H  N N 69  
A1IMA H32    H  N N 70  
A1IMA H33    H  N N 71  
A1IMA H34    H  N N 72  
A1IMA H35    H  N N 73  
A1IMA H36    H  N N 74  
A1IMA H38    H  N N 75  
A1IMA H39    H  N N 76  
A1IMA H40    H  N N 77  
A1IMA H41    H  N N 78  
ALA   N      N  N N 79  
ALA   CA     C  N S 80  
ALA   C      C  N N 81  
ALA   O      O  N N 82  
ALA   CB     C  N N 83  
ALA   OXT    O  N N 84  
ALA   H      H  N N 85  
ALA   H2     H  N N 86  
ALA   HA     H  N N 87  
ALA   HB1    H  N N 88  
ALA   HB2    H  N N 89  
ALA   HB3    H  N N 90  
ALA   HXT    H  N N 91  
ARG   N      N  N N 92  
ARG   CA     C  N S 93  
ARG   C      C  N N 94  
ARG   O      O  N N 95  
ARG   CB     C  N N 96  
ARG   CG     C  N N 97  
ARG   CD     C  N N 98  
ARG   NE     N  N N 99  
ARG   CZ     C  N N 100 
ARG   NH1    N  N N 101 
ARG   NH2    N  N N 102 
ARG   OXT    O  N N 103 
ARG   H      H  N N 104 
ARG   H2     H  N N 105 
ARG   HA     H  N N 106 
ARG   HB2    H  N N 107 
ARG   HB3    H  N N 108 
ARG   HG2    H  N N 109 
ARG   HG3    H  N N 110 
ARG   HD2    H  N N 111 
ARG   HD3    H  N N 112 
ARG   HE     H  N N 113 
ARG   HH11   H  N N 114 
ARG   HH12   H  N N 115 
ARG   HH21   H  N N 116 
ARG   HH22   H  N N 117 
ARG   HXT    H  N N 118 
ASN   N      N  N N 119 
ASN   CA     C  N S 120 
ASN   C      C  N N 121 
ASN   O      O  N N 122 
ASN   CB     C  N N 123 
ASN   CG     C  N N 124 
ASN   OD1    O  N N 125 
ASN   ND2    N  N N 126 
ASN   OXT    O  N N 127 
ASN   H      H  N N 128 
ASN   H2     H  N N 129 
ASN   HA     H  N N 130 
ASN   HB2    H  N N 131 
ASN   HB3    H  N N 132 
ASN   HD21   H  N N 133 
ASN   HD22   H  N N 134 
ASN   HXT    H  N N 135 
ASP   N      N  N N 136 
ASP   CA     C  N S 137 
ASP   C      C  N N 138 
ASP   O      O  N N 139 
ASP   CB     C  N N 140 
ASP   CG     C  N N 141 
ASP   OD1    O  N N 142 
ASP   OD2    O  N N 143 
ASP   OXT    O  N N 144 
ASP   H      H  N N 145 
ASP   H2     H  N N 146 
ASP   HA     H  N N 147 
ASP   HB2    H  N N 148 
ASP   HB3    H  N N 149 
ASP   HD2    H  N N 150 
ASP   HXT    H  N N 151 
CO    CO     CO N N 152 
CYS   N      N  N N 153 
CYS   CA     C  N R 154 
CYS   C      C  N N 155 
CYS   O      O  N N 156 
CYS   CB     C  N N 157 
CYS   SG     S  N N 158 
CYS   OXT    O  N N 159 
CYS   H      H  N N 160 
CYS   H2     H  N N 161 
CYS   HA     H  N N 162 
CYS   HB2    H  N N 163 
CYS   HB3    H  N N 164 
CYS   HG     H  N N 165 
CYS   HXT    H  N N 166 
GLN   N      N  N N 167 
GLN   CA     C  N S 168 
GLN   C      C  N N 169 
GLN   O      O  N N 170 
GLN   CB     C  N N 171 
GLN   CG     C  N N 172 
GLN   CD     C  N N 173 
GLN   OE1    O  N N 174 
GLN   NE2    N  N N 175 
GLN   OXT    O  N N 176 
GLN   H      H  N N 177 
GLN   H2     H  N N 178 
GLN   HA     H  N N 179 
GLN   HB2    H  N N 180 
GLN   HB3    H  N N 181 
GLN   HG2    H  N N 182 
GLN   HG3    H  N N 183 
GLN   HE21   H  N N 184 
GLN   HE22   H  N N 185 
GLN   HXT    H  N N 186 
GLU   N      N  N N 187 
GLU   CA     C  N S 188 
GLU   C      C  N N 189 
GLU   O      O  N N 190 
GLU   CB     C  N N 191 
GLU   CG     C  N N 192 
GLU   CD     C  N N 193 
GLU   OE1    O  N N 194 
GLU   OE2    O  N N 195 
GLU   OXT    O  N N 196 
GLU   H      H  N N 197 
GLU   H2     H  N N 198 
GLU   HA     H  N N 199 
GLU   HB2    H  N N 200 
GLU   HB3    H  N N 201 
GLU   HG2    H  N N 202 
GLU   HG3    H  N N 203 
GLU   HE2    H  N N 204 
GLU   HXT    H  N N 205 
GLY   N      N  N N 206 
GLY   CA     C  N N 207 
GLY   C      C  N N 208 
GLY   O      O  N N 209 
GLY   OXT    O  N N 210 
GLY   H      H  N N 211 
GLY   H2     H  N N 212 
GLY   HA2    H  N N 213 
GLY   HA3    H  N N 214 
GLY   HXT    H  N N 215 
GNP   PG     P  N N 216 
GNP   O1G    O  N N 217 
GNP   O2G    O  N N 218 
GNP   O3G    O  N N 219 
GNP   N3B    N  N N 220 
GNP   PB     P  N R 221 
GNP   O1B    O  N N 222 
GNP   O2B    O  N N 223 
GNP   O3A    O  N N 224 
GNP   PA     P  N S 225 
GNP   O1A    O  N N 226 
GNP   O2A    O  N N 227 
GNP   "O5'"  O  N N 228 
GNP   "C5'"  C  N N 229 
GNP   "C4'"  C  N R 230 
GNP   "O4'"  O  N N 231 
GNP   "C3'"  C  N S 232 
GNP   "O3'"  O  N N 233 
GNP   "C2'"  C  N R 234 
GNP   "O2'"  O  N N 235 
GNP   "C1'"  C  N R 236 
GNP   N9     N  Y N 237 
GNP   C8     C  Y N 238 
GNP   N7     N  Y N 239 
GNP   C5     C  Y N 240 
GNP   C6     C  Y N 241 
GNP   O6     O  N N 242 
GNP   N1     N  Y N 243 
GNP   C2     C  Y N 244 
GNP   N2     N  N N 245 
GNP   N3     N  Y N 246 
GNP   C4     C  Y N 247 
GNP   HOG2   H  N N 248 
GNP   HOG3   H  N N 249 
GNP   HNB3   H  N N 250 
GNP   HOB2   H  N N 251 
GNP   HOA2   H  N N 252 
GNP   "H5'2" H  N N 253 
GNP   "H5'1" H  N N 254 
GNP   "H4'"  H  N N 255 
GNP   "H3'"  H  N N 256 
GNP   "HO3'" H  N N 257 
GNP   "H2'"  H  N N 258 
GNP   "HO2'" H  N N 259 
GNP   "H1'"  H  N N 260 
GNP   H8     H  N N 261 
GNP   HN1    H  N N 262 
GNP   HN21   H  N N 263 
GNP   HN22   H  N N 264 
HIS   N      N  N N 265 
HIS   CA     C  N S 266 
HIS   C      C  N N 267 
HIS   O      O  N N 268 
HIS   CB     C  N N 269 
HIS   CG     C  Y N 270 
HIS   ND1    N  Y N 271 
HIS   CD2    C  Y N 272 
HIS   CE1    C  Y N 273 
HIS   NE2    N  Y N 274 
HIS   OXT    O  N N 275 
HIS   H      H  N N 276 
HIS   H2     H  N N 277 
HIS   HA     H  N N 278 
HIS   HB2    H  N N 279 
HIS   HB3    H  N N 280 
HIS   HD1    H  N N 281 
HIS   HD2    H  N N 282 
HIS   HE1    H  N N 283 
HIS   HE2    H  N N 284 
HIS   HXT    H  N N 285 
HOH   O      O  N N 286 
HOH   H1     H  N N 287 
HOH   H2     H  N N 288 
ILE   N      N  N N 289 
ILE   CA     C  N S 290 
ILE   C      C  N N 291 
ILE   O      O  N N 292 
ILE   CB     C  N S 293 
ILE   CG1    C  N N 294 
ILE   CG2    C  N N 295 
ILE   CD1    C  N N 296 
ILE   OXT    O  N N 297 
ILE   H      H  N N 298 
ILE   H2     H  N N 299 
ILE   HA     H  N N 300 
ILE   HB     H  N N 301 
ILE   HG12   H  N N 302 
ILE   HG13   H  N N 303 
ILE   HG21   H  N N 304 
ILE   HG22   H  N N 305 
ILE   HG23   H  N N 306 
ILE   HD11   H  N N 307 
ILE   HD12   H  N N 308 
ILE   HD13   H  N N 309 
ILE   HXT    H  N N 310 
LEU   N      N  N N 311 
LEU   CA     C  N S 312 
LEU   C      C  N N 313 
LEU   O      O  N N 314 
LEU   CB     C  N N 315 
LEU   CG     C  N N 316 
LEU   CD1    C  N N 317 
LEU   CD2    C  N N 318 
LEU   OXT    O  N N 319 
LEU   H      H  N N 320 
LEU   H2     H  N N 321 
LEU   HA     H  N N 322 
LEU   HB2    H  N N 323 
LEU   HB3    H  N N 324 
LEU   HG     H  N N 325 
LEU   HD11   H  N N 326 
LEU   HD12   H  N N 327 
LEU   HD13   H  N N 328 
LEU   HD21   H  N N 329 
LEU   HD22   H  N N 330 
LEU   HD23   H  N N 331 
LEU   HXT    H  N N 332 
LYS   N      N  N N 333 
LYS   CA     C  N S 334 
LYS   C      C  N N 335 
LYS   O      O  N N 336 
LYS   CB     C  N N 337 
LYS   CG     C  N N 338 
LYS   CD     C  N N 339 
LYS   CE     C  N N 340 
LYS   NZ     N  N N 341 
LYS   OXT    O  N N 342 
LYS   H      H  N N 343 
LYS   H2     H  N N 344 
LYS   HA     H  N N 345 
LYS   HB2    H  N N 346 
LYS   HB3    H  N N 347 
LYS   HG2    H  N N 348 
LYS   HG3    H  N N 349 
LYS   HD2    H  N N 350 
LYS   HD3    H  N N 351 
LYS   HE2    H  N N 352 
LYS   HE3    H  N N 353 
LYS   HZ1    H  N N 354 
LYS   HZ2    H  N N 355 
LYS   HZ3    H  N N 356 
LYS   HXT    H  N N 357 
MET   N      N  N N 358 
MET   CA     C  N S 359 
MET   C      C  N N 360 
MET   O      O  N N 361 
MET   CB     C  N N 362 
MET   CG     C  N N 363 
MET   SD     S  N N 364 
MET   CE     C  N N 365 
MET   OXT    O  N N 366 
MET   H      H  N N 367 
MET   H2     H  N N 368 
MET   HA     H  N N 369 
MET   HB2    H  N N 370 
MET   HB3    H  N N 371 
MET   HG2    H  N N 372 
MET   HG3    H  N N 373 
MET   HE1    H  N N 374 
MET   HE2    H  N N 375 
MET   HE3    H  N N 376 
MET   HXT    H  N N 377 
MG    MG     MG N N 378 
PHE   N      N  N N 379 
PHE   CA     C  N S 380 
PHE   C      C  N N 381 
PHE   O      O  N N 382 
PHE   CB     C  N N 383 
PHE   CG     C  Y N 384 
PHE   CD1    C  Y N 385 
PHE   CD2    C  Y N 386 
PHE   CE1    C  Y N 387 
PHE   CE2    C  Y N 388 
PHE   CZ     C  Y N 389 
PHE   OXT    O  N N 390 
PHE   H      H  N N 391 
PHE   H2     H  N N 392 
PHE   HA     H  N N 393 
PHE   HB2    H  N N 394 
PHE   HB3    H  N N 395 
PHE   HD1    H  N N 396 
PHE   HD2    H  N N 397 
PHE   HE1    H  N N 398 
PHE   HE2    H  N N 399 
PHE   HZ     H  N N 400 
PHE   HXT    H  N N 401 
PRO   N      N  N N 402 
PRO   CA     C  N S 403 
PRO   C      C  N N 404 
PRO   O      O  N N 405 
PRO   CB     C  N N 406 
PRO   CG     C  N N 407 
PRO   CD     C  N N 408 
PRO   OXT    O  N N 409 
PRO   H      H  N N 410 
PRO   HA     H  N N 411 
PRO   HB2    H  N N 412 
PRO   HB3    H  N N 413 
PRO   HG2    H  N N 414 
PRO   HG3    H  N N 415 
PRO   HD2    H  N N 416 
PRO   HD3    H  N N 417 
PRO   HXT    H  N N 418 
SER   N      N  N N 419 
SER   CA     C  N S 420 
SER   C      C  N N 421 
SER   O      O  N N 422 
SER   CB     C  N N 423 
SER   OG     O  N N 424 
SER   OXT    O  N N 425 
SER   H      H  N N 426 
SER   H2     H  N N 427 
SER   HA     H  N N 428 
SER   HB2    H  N N 429 
SER   HB3    H  N N 430 
SER   HG     H  N N 431 
SER   HXT    H  N N 432 
THR   N      N  N N 433 
THR   CA     C  N S 434 
THR   C      C  N N 435 
THR   O      O  N N 436 
THR   CB     C  N R 437 
THR   OG1    O  N N 438 
THR   CG2    C  N N 439 
THR   OXT    O  N N 440 
THR   H      H  N N 441 
THR   H2     H  N N 442 
THR   HA     H  N N 443 
THR   HB     H  N N 444 
THR   HG1    H  N N 445 
THR   HG21   H  N N 446 
THR   HG22   H  N N 447 
THR   HG23   H  N N 448 
THR   HXT    H  N N 449 
TYR   N      N  N N 450 
TYR   CA     C  N S 451 
TYR   C      C  N N 452 
TYR   O      O  N N 453 
TYR   CB     C  N N 454 
TYR   CG     C  Y N 455 
TYR   CD1    C  Y N 456 
TYR   CD2    C  Y N 457 
TYR   CE1    C  Y N 458 
TYR   CE2    C  Y N 459 
TYR   CZ     C  Y N 460 
TYR   OH     O  N N 461 
TYR   OXT    O  N N 462 
TYR   H      H  N N 463 
TYR   H2     H  N N 464 
TYR   HA     H  N N 465 
TYR   HB2    H  N N 466 
TYR   HB3    H  N N 467 
TYR   HD1    H  N N 468 
TYR   HD2    H  N N 469 
TYR   HE1    H  N N 470 
TYR   HE2    H  N N 471 
TYR   HH     H  N N 472 
TYR   HXT    H  N N 473 
VAL   N      N  N N 474 
VAL   CA     C  N S 475 
VAL   C      C  N N 476 
VAL   O      O  N N 477 
VAL   CB     C  N N 478 
VAL   CG1    C  N N 479 
VAL   CG2    C  N N 480 
VAL   OXT    O  N N 481 
VAL   H      H  N N 482 
VAL   H2     H  N N 483 
VAL   HA     H  N N 484 
VAL   HB     H  N N 485 
VAL   HG11   H  N N 486 
VAL   HG12   H  N N 487 
VAL   HG13   H  N N 488 
VAL   HG21   H  N N 489 
VAL   HG22   H  N N 490 
VAL   HG23   H  N N 491 
VAL   HXT    H  N N 492 
# 
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 
A1IMA CBK   CBL    sing N N 1   
A1IMA CBK   CBJ    sing N N 2   
A1IMA CBL   CBM    sing N N 3   
A1IMA CBM   NBP    sing N N 4   
A1IMA CBM   CBN    sing N N 5   
A1IMA CBN   CBO    sing N N 6   
A1IMA CBO   CBJ    sing N N 7   
A1IMA CBJ   NAQ    sing N N 8   
A1IMA NAQ   CAB    sing N N 9   
A1IMA NAQ   CAR    sing N N 10  
A1IMA CAB   OAA    doub N N 11  
A1IMA CAB   CAC    sing N N 12  
A1IMA CAR   CAS    sing N N 13  
A1IMA CAS   CAT    sing N N 14  
A1IMA CAT   CAU    sing N N 15  
A1IMA CAU   CAV    sing N N 16  
A1IMA CAV   NAW    sing N N 17  
A1IMA NAW   CAX    sing N N 18  
A1IMA NAW   CBG    sing N N 19  
A1IMA CAX   CAY    sing Y N 20  
A1IMA CAX   CBI    doub Y N 21  
A1IMA CAY   OBD    sing N N 22  
A1IMA CAY   CAZ    doub Y N 23  
A1IMA CAZ   CBA    sing Y N 24  
A1IMA CBA   CBB    doub Y N 25  
A1IMA CBB   CLBC   sing N N 26  
A1IMA CBB   CBI    sing Y N 27  
A1IMA CBI   SBH    sing N N 28  
A1IMA SBH   CBG    sing N N 29  
A1IMA CBG   NBF    doub N N 30  
A1IMA NBF   SAH    sing N N 31  
A1IMA SAH   OAI    doub N N 32  
A1IMA SAH   OBE    doub N N 33  
A1IMA SAH   CAG    sing N N 34  
A1IMA CAG   CAF    doub Y N 35  
A1IMA CAG   CAJ    sing Y N 36  
A1IMA CAF   NAE    sing Y N 37  
A1IMA NAE   CAD    doub Y N 38  
A1IMA CAJ   CAC    doub Y N 39  
A1IMA CAC   CAD    sing Y N 40  
A1IMA CAD   NAK    sing N N 41  
A1IMA NAK   CAL    sing N N 42  
A1IMA NAK   CAP    sing N N 43  
A1IMA CAL   CAM    sing N N 44  
A1IMA CAM   NAN    sing N N 45  
A1IMA NAN   CAO    sing N N 46  
A1IMA CAO   CAP    sing N N 47  
A1IMA CBK   H1     sing N N 48  
A1IMA CBK   H2     sing N N 49  
A1IMA CBL   H3     sing N N 50  
A1IMA CBL   H4     sing N N 51  
A1IMA CBM   H5     sing N N 52  
A1IMA NBP   H6     sing N N 53  
A1IMA NBP   H7     sing N N 54  
A1IMA CBN   H9     sing N N 55  
A1IMA CBN   H10    sing N N 56  
A1IMA CBO   H11    sing N N 57  
A1IMA CBO   H12    sing N N 58  
A1IMA CBJ   H13    sing N N 59  
A1IMA CAR   H14    sing N N 60  
A1IMA CAR   H15    sing N N 61  
A1IMA CAS   H16    sing N N 62  
A1IMA CAS   H17    sing N N 63  
A1IMA CAT   H18    sing N N 64  
A1IMA CAT   H19    sing N N 65  
A1IMA CAU   H20    sing N N 66  
A1IMA CAU   H21    sing N N 67  
A1IMA CAV   H22    sing N N 68  
A1IMA CAV   H23    sing N N 69  
A1IMA OBD   H24    sing N N 70  
A1IMA CAZ   H25    sing N N 71  
A1IMA CBA   H26    sing N N 72  
A1IMA CAF   H30    sing N N 73  
A1IMA CAJ   H31    sing N N 74  
A1IMA CAL   H32    sing N N 75  
A1IMA CAL   H33    sing N N 76  
A1IMA CAM   H34    sing N N 77  
A1IMA CAM   H35    sing N N 78  
A1IMA NAN   H36    sing N N 79  
A1IMA CAO   H38    sing N N 80  
A1IMA CAO   H39    sing N N 81  
A1IMA CAP   H40    sing N N 82  
A1IMA CAP   H41    sing N N 83  
ALA   N     CA     sing N N 84  
ALA   N     H      sing N N 85  
ALA   N     H2     sing N N 86  
ALA   CA    C      sing N N 87  
ALA   CA    CB     sing N N 88  
ALA   CA    HA     sing N N 89  
ALA   C     O      doub N N 90  
ALA   C     OXT    sing N N 91  
ALA   CB    HB1    sing N N 92  
ALA   CB    HB2    sing N N 93  
ALA   CB    HB3    sing N N 94  
ALA   OXT   HXT    sing N N 95  
ARG   N     CA     sing N N 96  
ARG   N     H      sing N N 97  
ARG   N     H2     sing N N 98  
ARG   CA    C      sing N N 99  
ARG   CA    CB     sing N N 100 
ARG   CA    HA     sing N N 101 
ARG   C     O      doub N N 102 
ARG   C     OXT    sing N N 103 
ARG   CB    CG     sing N N 104 
ARG   CB    HB2    sing N N 105 
ARG   CB    HB3    sing N N 106 
ARG   CG    CD     sing N N 107 
ARG   CG    HG2    sing N N 108 
ARG   CG    HG3    sing N N 109 
ARG   CD    NE     sing N N 110 
ARG   CD    HD2    sing N N 111 
ARG   CD    HD3    sing N N 112 
ARG   NE    CZ     sing N N 113 
ARG   NE    HE     sing N N 114 
ARG   CZ    NH1    sing N N 115 
ARG   CZ    NH2    doub N N 116 
ARG   NH1   HH11   sing N N 117 
ARG   NH1   HH12   sing N N 118 
ARG   NH2   HH21   sing N N 119 
ARG   NH2   HH22   sing N N 120 
ARG   OXT   HXT    sing N N 121 
ASN   N     CA     sing N N 122 
ASN   N     H      sing N N 123 
ASN   N     H2     sing N N 124 
ASN   CA    C      sing N N 125 
ASN   CA    CB     sing N N 126 
ASN   CA    HA     sing N N 127 
ASN   C     O      doub N N 128 
ASN   C     OXT    sing N N 129 
ASN   CB    CG     sing N N 130 
ASN   CB    HB2    sing N N 131 
ASN   CB    HB3    sing N N 132 
ASN   CG    OD1    doub N N 133 
ASN   CG    ND2    sing N N 134 
ASN   ND2   HD21   sing N N 135 
ASN   ND2   HD22   sing N N 136 
ASN   OXT   HXT    sing N N 137 
ASP   N     CA     sing N N 138 
ASP   N     H      sing N N 139 
ASP   N     H2     sing N N 140 
ASP   CA    C      sing N N 141 
ASP   CA    CB     sing N N 142 
ASP   CA    HA     sing N N 143 
ASP   C     O      doub N N 144 
ASP   C     OXT    sing N N 145 
ASP   CB    CG     sing N N 146 
ASP   CB    HB2    sing N N 147 
ASP   CB    HB3    sing N N 148 
ASP   CG    OD1    doub N N 149 
ASP   CG    OD2    sing N N 150 
ASP   OD2   HD2    sing N N 151 
ASP   OXT   HXT    sing N N 152 
CYS   N     CA     sing N N 153 
CYS   N     H      sing N N 154 
CYS   N     H2     sing N N 155 
CYS   CA    C      sing N N 156 
CYS   CA    CB     sing N N 157 
CYS   CA    HA     sing N N 158 
CYS   C     O      doub N N 159 
CYS   C     OXT    sing N N 160 
CYS   CB    SG     sing N N 161 
CYS   CB    HB2    sing N N 162 
CYS   CB    HB3    sing N N 163 
CYS   SG    HG     sing N N 164 
CYS   OXT   HXT    sing N N 165 
GLN   N     CA     sing N N 166 
GLN   N     H      sing N N 167 
GLN   N     H2     sing N N 168 
GLN   CA    C      sing N N 169 
GLN   CA    CB     sing N N 170 
GLN   CA    HA     sing N N 171 
GLN   C     O      doub N N 172 
GLN   C     OXT    sing N N 173 
GLN   CB    CG     sing N N 174 
GLN   CB    HB2    sing N N 175 
GLN   CB    HB3    sing N N 176 
GLN   CG    CD     sing N N 177 
GLN   CG    HG2    sing N N 178 
GLN   CG    HG3    sing N N 179 
GLN   CD    OE1    doub N N 180 
GLN   CD    NE2    sing N N 181 
GLN   NE2   HE21   sing N N 182 
GLN   NE2   HE22   sing N N 183 
GLN   OXT   HXT    sing N N 184 
GLU   N     CA     sing N N 185 
GLU   N     H      sing N N 186 
GLU   N     H2     sing N N 187 
GLU   CA    C      sing N N 188 
GLU   CA    CB     sing N N 189 
GLU   CA    HA     sing N N 190 
GLU   C     O      doub N N 191 
GLU   C     OXT    sing N N 192 
GLU   CB    CG     sing N N 193 
GLU   CB    HB2    sing N N 194 
GLU   CB    HB3    sing N N 195 
GLU   CG    CD     sing N N 196 
GLU   CG    HG2    sing N N 197 
GLU   CG    HG3    sing N N 198 
GLU   CD    OE1    doub N N 199 
GLU   CD    OE2    sing N N 200 
GLU   OE2   HE2    sing N N 201 
GLU   OXT   HXT    sing N N 202 
GLY   N     CA     sing N N 203 
GLY   N     H      sing N N 204 
GLY   N     H2     sing N N 205 
GLY   CA    C      sing N N 206 
GLY   CA    HA2    sing N N 207 
GLY   CA    HA3    sing N N 208 
GLY   C     O      doub N N 209 
GLY   C     OXT    sing N N 210 
GLY   OXT   HXT    sing N N 211 
GNP   PG    O1G    doub N N 212 
GNP   PG    O2G    sing N N 213 
GNP   PG    O3G    sing N N 214 
GNP   PG    N3B    sing N N 215 
GNP   O2G   HOG2   sing N N 216 
GNP   O3G   HOG3   sing N N 217 
GNP   N3B   PB     sing N N 218 
GNP   N3B   HNB3   sing N N 219 
GNP   PB    O1B    doub N N 220 
GNP   PB    O2B    sing N N 221 
GNP   PB    O3A    sing N N 222 
GNP   O2B   HOB2   sing N N 223 
GNP   O3A   PA     sing N N 224 
GNP   PA    O1A    doub N N 225 
GNP   PA    O2A    sing N N 226 
GNP   PA    "O5'"  sing N N 227 
GNP   O2A   HOA2   sing N N 228 
GNP   "O5'" "C5'"  sing N N 229 
GNP   "C5'" "C4'"  sing N N 230 
GNP   "C5'" "H5'2" sing N N 231 
GNP   "C5'" "H5'1" sing N N 232 
GNP   "C4'" "O4'"  sing N N 233 
GNP   "C4'" "C3'"  sing N N 234 
GNP   "C4'" "H4'"  sing N N 235 
GNP   "O4'" "C1'"  sing N N 236 
GNP   "C3'" "O3'"  sing N N 237 
GNP   "C3'" "C2'"  sing N N 238 
GNP   "C3'" "H3'"  sing N N 239 
GNP   "O3'" "HO3'" sing N N 240 
GNP   "C2'" "O2'"  sing N N 241 
GNP   "C2'" "C1'"  sing N N 242 
GNP   "C2'" "H2'"  sing N N 243 
GNP   "O2'" "HO2'" sing N N 244 
GNP   "C1'" N9     sing N N 245 
GNP   "C1'" "H1'"  sing N N 246 
GNP   N9    C8     sing Y N 247 
GNP   N9    C4     sing Y N 248 
GNP   C8    N7     doub Y N 249 
GNP   C8    H8     sing N N 250 
GNP   N7    C5     sing Y N 251 
GNP   C5    C6     sing Y N 252 
GNP   C5    C4     doub Y N 253 
GNP   C6    O6     doub N N 254 
GNP   C6    N1     sing Y N 255 
GNP   N1    C2     sing Y N 256 
GNP   N1    HN1    sing N N 257 
GNP   C2    N2     sing N N 258 
GNP   C2    N3     doub Y N 259 
GNP   N2    HN21   sing N N 260 
GNP   N2    HN22   sing N N 261 
GNP   N3    C4     sing Y N 262 
HIS   N     CA     sing N N 263 
HIS   N     H      sing N N 264 
HIS   N     H2     sing N N 265 
HIS   CA    C      sing N N 266 
HIS   CA    CB     sing N N 267 
HIS   CA    HA     sing N N 268 
HIS   C     O      doub N N 269 
HIS   C     OXT    sing N N 270 
HIS   CB    CG     sing N N 271 
HIS   CB    HB2    sing N N 272 
HIS   CB    HB3    sing N N 273 
HIS   CG    ND1    sing Y N 274 
HIS   CG    CD2    doub Y N 275 
HIS   ND1   CE1    doub Y N 276 
HIS   ND1   HD1    sing N N 277 
HIS   CD2   NE2    sing Y N 278 
HIS   CD2   HD2    sing N N 279 
HIS   CE1   NE2    sing Y N 280 
HIS   CE1   HE1    sing N N 281 
HIS   NE2   HE2    sing N N 282 
HIS   OXT   HXT    sing N N 283 
HOH   O     H1     sing N N 284 
HOH   O     H2     sing N N 285 
ILE   N     CA     sing N N 286 
ILE   N     H      sing N N 287 
ILE   N     H2     sing N N 288 
ILE   CA    C      sing N N 289 
ILE   CA    CB     sing N N 290 
ILE   CA    HA     sing N N 291 
ILE   C     O      doub N N 292 
ILE   C     OXT    sing N N 293 
ILE   CB    CG1    sing N N 294 
ILE   CB    CG2    sing N N 295 
ILE   CB    HB     sing N N 296 
ILE   CG1   CD1    sing N N 297 
ILE   CG1   HG12   sing N N 298 
ILE   CG1   HG13   sing N N 299 
ILE   CG2   HG21   sing N N 300 
ILE   CG2   HG22   sing N N 301 
ILE   CG2   HG23   sing N N 302 
ILE   CD1   HD11   sing N N 303 
ILE   CD1   HD12   sing N N 304 
ILE   CD1   HD13   sing N N 305 
ILE   OXT   HXT    sing N N 306 
LEU   N     CA     sing N N 307 
LEU   N     H      sing N N 308 
LEU   N     H2     sing N N 309 
LEU   CA    C      sing N N 310 
LEU   CA    CB     sing N N 311 
LEU   CA    HA     sing N N 312 
LEU   C     O      doub N N 313 
LEU   C     OXT    sing N N 314 
LEU   CB    CG     sing N N 315 
LEU   CB    HB2    sing N N 316 
LEU   CB    HB3    sing N N 317 
LEU   CG    CD1    sing N N 318 
LEU   CG    CD2    sing N N 319 
LEU   CG    HG     sing N N 320 
LEU   CD1   HD11   sing N N 321 
LEU   CD1   HD12   sing N N 322 
LEU   CD1   HD13   sing N N 323 
LEU   CD2   HD21   sing N N 324 
LEU   CD2   HD22   sing N N 325 
LEU   CD2   HD23   sing N N 326 
LEU   OXT   HXT    sing N N 327 
LYS   N     CA     sing N N 328 
LYS   N     H      sing N N 329 
LYS   N     H2     sing N N 330 
LYS   CA    C      sing N N 331 
LYS   CA    CB     sing N N 332 
LYS   CA    HA     sing N N 333 
LYS   C     O      doub N N 334 
LYS   C     OXT    sing N N 335 
LYS   CB    CG     sing N N 336 
LYS   CB    HB2    sing N N 337 
LYS   CB    HB3    sing N N 338 
LYS   CG    CD     sing N N 339 
LYS   CG    HG2    sing N N 340 
LYS   CG    HG3    sing N N 341 
LYS   CD    CE     sing N N 342 
LYS   CD    HD2    sing N N 343 
LYS   CD    HD3    sing N N 344 
LYS   CE    NZ     sing N N 345 
LYS   CE    HE2    sing N N 346 
LYS   CE    HE3    sing N N 347 
LYS   NZ    HZ1    sing N N 348 
LYS   NZ    HZ2    sing N N 349 
LYS   NZ    HZ3    sing N N 350 
LYS   OXT   HXT    sing N N 351 
MET   N     CA     sing N N 352 
MET   N     H      sing N N 353 
MET   N     H2     sing N N 354 
MET   CA    C      sing N N 355 
MET   CA    CB     sing N N 356 
MET   CA    HA     sing N N 357 
MET   C     O      doub N N 358 
MET   C     OXT    sing N N 359 
MET   CB    CG     sing N N 360 
MET   CB    HB2    sing N N 361 
MET   CB    HB3    sing N N 362 
MET   CG    SD     sing N N 363 
MET   CG    HG2    sing N N 364 
MET   CG    HG3    sing N N 365 
MET   SD    CE     sing N N 366 
MET   CE    HE1    sing N N 367 
MET   CE    HE2    sing N N 368 
MET   CE    HE3    sing N N 369 
MET   OXT   HXT    sing N N 370 
PHE   N     CA     sing N N 371 
PHE   N     H      sing N N 372 
PHE   N     H2     sing N N 373 
PHE   CA    C      sing N N 374 
PHE   CA    CB     sing N N 375 
PHE   CA    HA     sing N N 376 
PHE   C     O      doub N N 377 
PHE   C     OXT    sing N N 378 
PHE   CB    CG     sing N N 379 
PHE   CB    HB2    sing N N 380 
PHE   CB    HB3    sing N N 381 
PHE   CG    CD1    doub Y N 382 
PHE   CG    CD2    sing Y N 383 
PHE   CD1   CE1    sing Y N 384 
PHE   CD1   HD1    sing N N 385 
PHE   CD2   CE2    doub Y N 386 
PHE   CD2   HD2    sing N N 387 
PHE   CE1   CZ     doub Y N 388 
PHE   CE1   HE1    sing N N 389 
PHE   CE2   CZ     sing Y N 390 
PHE   CE2   HE2    sing N N 391 
PHE   CZ    HZ     sing N N 392 
PHE   OXT   HXT    sing N N 393 
PRO   N     CA     sing N N 394 
PRO   N     CD     sing N N 395 
PRO   N     H      sing N N 396 
PRO   CA    C      sing N N 397 
PRO   CA    CB     sing N N 398 
PRO   CA    HA     sing N N 399 
PRO   C     O      doub N N 400 
PRO   C     OXT    sing N N 401 
PRO   CB    CG     sing N N 402 
PRO   CB    HB2    sing N N 403 
PRO   CB    HB3    sing N N 404 
PRO   CG    CD     sing N N 405 
PRO   CG    HG2    sing N N 406 
PRO   CG    HG3    sing N N 407 
PRO   CD    HD2    sing N N 408 
PRO   CD    HD3    sing N N 409 
PRO   OXT   HXT    sing N N 410 
SER   N     CA     sing N N 411 
SER   N     H      sing N N 412 
SER   N     H2     sing N N 413 
SER   CA    C      sing N N 414 
SER   CA    CB     sing N N 415 
SER   CA    HA     sing N N 416 
SER   C     O      doub N N 417 
SER   C     OXT    sing N N 418 
SER   CB    OG     sing N N 419 
SER   CB    HB2    sing N N 420 
SER   CB    HB3    sing N N 421 
SER   OG    HG     sing N N 422 
SER   OXT   HXT    sing N N 423 
THR   N     CA     sing N N 424 
THR   N     H      sing N N 425 
THR   N     H2     sing N N 426 
THR   CA    C      sing N N 427 
THR   CA    CB     sing N N 428 
THR   CA    HA     sing N N 429 
THR   C     O      doub N N 430 
THR   C     OXT    sing N N 431 
THR   CB    OG1    sing N N 432 
THR   CB    CG2    sing N N 433 
THR   CB    HB     sing N N 434 
THR   OG1   HG1    sing N N 435 
THR   CG2   HG21   sing N N 436 
THR   CG2   HG22   sing N N 437 
THR   CG2   HG23   sing N N 438 
THR   OXT   HXT    sing N N 439 
TYR   N     CA     sing N N 440 
TYR   N     H      sing N N 441 
TYR   N     H2     sing N N 442 
TYR   CA    C      sing N N 443 
TYR   CA    CB     sing N N 444 
TYR   CA    HA     sing N N 445 
TYR   C     O      doub N N 446 
TYR   C     OXT    sing N N 447 
TYR   CB    CG     sing N N 448 
TYR   CB    HB2    sing N N 449 
TYR   CB    HB3    sing N N 450 
TYR   CG    CD1    doub Y N 451 
TYR   CG    CD2    sing Y N 452 
TYR   CD1   CE1    sing Y N 453 
TYR   CD1   HD1    sing N N 454 
TYR   CD2   CE2    doub Y N 455 
TYR   CD2   HD2    sing N N 456 
TYR   CE1   CZ     doub Y N 457 
TYR   CE1   HE1    sing N N 458 
TYR   CE2   CZ     sing Y N 459 
TYR   CE2   HE2    sing N N 460 
TYR   CZ    OH     sing N N 461 
TYR   OH    HH     sing N N 462 
TYR   OXT   HXT    sing N N 463 
VAL   N     CA     sing N N 464 
VAL   N     H      sing N N 465 
VAL   N     H2     sing N N 466 
VAL   CA    C      sing N N 467 
VAL   CA    CB     sing N N 468 
VAL   CA    HA     sing N N 469 
VAL   C     O      doub N N 470 
VAL   C     OXT    sing N N 471 
VAL   CB    CG1    sing N N 472 
VAL   CB    CG2    sing N N 473 
VAL   CB    HB     sing N N 474 
VAL   CG1   HG11   sing N N 475 
VAL   CG1   HG12   sing N N 476 
VAL   CG1   HG13   sing N N 477 
VAL   CG2   HG21   sing N N 478 
VAL   CG2   HG22   sing N N 479 
VAL   CG2   HG23   sing N N 480 
VAL   OXT   HXT    sing N N 481 
# 
_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                    9GH0 
_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]   0.013882 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.004973 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.029214 
_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]   0.015278 
_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 
CO 
MG 
N  
O  
P  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N     . MET   A 1 4   ? 7.067  2.175   24.287 1.00 62.41 ? 1   MET   A N     1 
ATOM   2    C  CA    . MET   A 1 4   ? 8.386  2.855   24.217 1.00 59.93 ? 1   MET   A CA    1 
ATOM   3    C  C     . MET   A 1 4   ? 9.210  2.203   23.102 1.00 55.09 ? 1   MET   A C     1 
ATOM   4    O  O     . MET   A 1 4   ? 9.293  0.994   23.077 1.00 54.18 ? 1   MET   A O     1 
ATOM   5    C  CB    . MET   A 1 4   ? 9.132  2.704   25.536 1.00 62.22 ? 1   MET   A CB    1 
ATOM   6    C  CG    . MET   A 1 4   ? 10.535 3.222   25.465 1.00 60.97 ? 1   MET   A CG    1 
ATOM   7    S  SD    . MET   A 1 4   ? 11.391 2.671   26.921 1.00 62.64 ? 1   MET   A SD    1 
ATOM   8    C  CE    . MET   A 1 4   ? 10.473 3.539   28.185 1.00 60.71 ? 1   MET   A CE    1 
ATOM   9    N  N     . THR   A 1 5   ? 9.777  3.016   22.222 1.00 50.93 ? 2   THR   A N     1 
ATOM   10   C  CA    . THR   A 1 5   ? 10.525 2.508   21.044 1.00 49.41 ? 2   THR   A CA    1 
ATOM   11   C  C     . THR   A 1 5   ? 11.806 1.774   21.445 1.00 47.47 ? 2   THR   A C     1 
ATOM   12   O  O     . THR   A 1 5   ? 12.589 2.328   22.209 1.00 45.51 ? 2   THR   A O     1 
ATOM   13   C  CB    . THR   A 1 5   ? 10.862 3.647   20.079 1.00 49.94 ? 2   THR   A CB    1 
ATOM   14   O  OG1   . THR   A 1 5   ? 9.637  4.200   19.602 1.00 51.78 ? 2   THR   A OG1   1 
ATOM   15   C  CG2   . THR   A 1 5   ? 11.705 3.189   18.912 1.00 48.90 ? 2   THR   A CG2   1 
ATOM   16   N  N     . GLU   A 1 6   ? 11.999 0.589   20.874 1.00 46.42 ? 3   GLU   A N     1 
ATOM   17   C  CA    . GLU   A 1 6   ? 13.209 -0.229  21.089 1.00 44.07 ? 3   GLU   A CA    1 
ATOM   18   C  C     . GLU   A 1 6   ? 14.022 -0.205  19.792 1.00 41.69 ? 3   GLU   A C     1 
ATOM   19   O  O     . GLU   A 1 6   ? 13.422 -0.037  18.743 1.00 41.11 ? 3   GLU   A O     1 
ATOM   20   C  CB    . GLU   A 1 6   ? 12.838 -1.671  21.420 1.00 47.10 ? 3   GLU   A CB    1 
ATOM   21   C  CG    . GLU   A 1 6   ? 11.920 -1.812  22.615 1.00 53.30 ? 3   GLU   A CG    1 
ATOM   22   C  CD    . GLU   A 1 6   ? 11.816 -3.234  23.133 1.00 54.79 ? 3   GLU   A CD    1 
ATOM   23   O  OE1   . GLU   A 1 6   ? 12.720 -4.036  22.838 1.00 55.01 ? 3   GLU   A OE1   1 
ATOM   24   O  OE2   . GLU   A 1 6   ? 10.824 -3.536  23.815 1.00 62.08 ? 3   GLU   A OE2   1 
ATOM   25   N  N     . TYR   A 1 7   ? 15.346 -0.272  19.907 1.00 37.99 ? 4   TYR   A N     1 
ATOM   26   C  CA    . TYR   A 1 7   ? 16.263 -0.302  18.743 1.00 35.12 ? 4   TYR   A CA    1 
ATOM   27   C  C     . TYR   A 1 7   ? 17.219 -1.487  18.909 1.00 35.29 ? 4   TYR   A C     1 
ATOM   28   O  O     . TYR   A 1 7   ? 17.895 -1.554  19.916 1.00 35.41 ? 4   TYR   A O     1 
ATOM   29   C  CB    . TYR   A 1 7   ? 17.074 0.991   18.668 1.00 34.04 ? 4   TYR   A CB    1 
ATOM   30   C  CG    . TYR   A 1 7   ? 16.275 2.239   18.398 1.00 34.63 ? 4   TYR   A CG    1 
ATOM   31   C  CD1   . TYR   A 1 7   ? 15.666 2.440   17.177 1.00 37.08 ? 4   TYR   A CD1   1 
ATOM   32   C  CD2   . TYR   A 1 7   ? 16.136 3.223   19.356 1.00 36.00 ? 4   TYR   A CD2   1 
ATOM   33   C  CE1   . TYR   A 1 7   ? 14.928 3.578   16.915 1.00 37.20 ? 4   TYR   A CE1   1 
ATOM   34   C  CE2   . TYR   A 1 7   ? 15.407 4.368   19.111 1.00 37.04 ? 4   TYR   A CE2   1 
ATOM   35   C  CZ    . TYR   A 1 7   ? 14.803 4.548   17.885 1.00 37.41 ? 4   TYR   A CZ    1 
ATOM   36   O  OH    . TYR   A 1 7   ? 14.081 5.669   17.635 1.00 40.57 ? 4   TYR   A OH    1 
ATOM   37   N  N     . LYS   A 1 8   ? 17.214 -2.401  17.957 1.00 33.66 ? 5   LYS   A N     1 
ATOM   38   C  CA    . LYS   A 1 8   ? 18.147 -3.538  18.038 1.00 33.10 ? 5   LYS   A CA    1 
ATOM   39   C  C     . LYS   A 1 8   ? 19.452 -3.105  17.364 1.00 32.02 ? 5   LYS   A C     1 
ATOM   40   O  O     . LYS   A 1 8   ? 19.418 -2.925  16.163 1.00 30.82 ? 5   LYS   A O     1 
ATOM   41   C  CB    . LYS   A 1 8   ? 17.531 -4.771  17.386 1.00 35.42 ? 5   LYS   A CB    1 
ATOM   42   C  CG    . LYS   A 1 8   ? 16.304 -5.314  18.105 1.00 38.61 ? 5   LYS   A CG    1 
ATOM   43   C  CD    . LYS   A 1 8   ? 16.347 -6.799  18.302 1.00 42.40 ? 5   LYS   A CD    1 
ATOM   44   C  CE    . LYS   A 1 8   ? 15.133 -7.346  19.016 1.00 46.11 ? 5   LYS   A CE    1 
ATOM   45   N  NZ    . LYS   A 1 8   ? 13.918 -6.562  18.706 1.00 48.55 ? 5   LYS   A NZ    1 
ATOM   46   N  N     . LEU   A 1 9   ? 20.510 -2.910  18.152 1.00 30.89 ? 6   LEU   A N     1 
ATOM   47   C  CA    . LEU   A 1 9   ? 21.824 -2.496  17.657 1.00 30.85 ? 6   LEU   A CA    1 
ATOM   48   C  C     . LEU   A 1 9   ? 22.743 -3.713  17.661 1.00 30.84 ? 6   LEU   A C     1 
ATOM   49   O  O     . LEU   A 1 9   ? 22.627 -4.537  18.564 1.00 29.95 ? 6   LEU   A O     1 
ATOM   50   C  CB    . LEU   A 1 9   ? 22.398 -1.399  18.560 1.00 30.73 ? 6   LEU   A CB    1 
ATOM   51   C  CG    . LEU   A 1 9   ? 21.498 -0.191  18.802 1.00 33.13 ? 6   LEU   A CG    1 
ATOM   52   C  CD1   . LEU   A 1 9   ? 22.264 0.905   19.546 1.00 35.03 ? 6   LEU   A CD1   1 
ATOM   53   C  CD2   . LEU   A 1 9   ? 20.959 0.335   17.480 1.00 32.71 ? 6   LEU   A CD2   1 
ATOM   54   N  N     . VAL   A 1 10  ? 23.611 -3.848  16.637 1.00 29.28 ? 7   VAL   A N     1 
ATOM   55   C  CA    . VAL   A 1 10  ? 24.541 -4.977  16.544 1.00 28.28 ? 7   VAL   A CA    1 
ATOM   56   C  C     . VAL   A 1 10  ? 25.949 -4.409  16.362 1.00 28.45 ? 7   VAL   A C     1 
ATOM   57   O  O     . VAL   A 1 10  ? 26.146 -3.490  15.566 1.00 28.33 ? 7   VAL   A O     1 
ATOM   58   C  CB    . VAL   A 1 10  ? 24.165 -5.963  15.423 1.00 28.68 ? 7   VAL   A CB    1 
ATOM   59   C  CG1   . VAL   A 1 10  ? 25.045 -7.216  15.391 1.00 30.85 ? 7   VAL   A CG1   1 
ATOM   60   C  CG2   . VAL   A 1 10  ? 22.685 -6.347  15.496 1.00 31.15 ? 7   VAL   A CG2   1 
ATOM   61   N  N     . VAL   A 1 11  ? 26.896 -4.906  17.165 1.00 28.63 ? 8   VAL   A N     1 
ATOM   62   C  CA    . VAL   A 1 11  ? 28.279 -4.460  17.074 1.00 28.79 ? 8   VAL   A CA    1 
ATOM   63   C  C     . VAL   A 1 11  ? 29.041 -5.585  16.380 1.00 27.57 ? 8   VAL   A C     1 
ATOM   64   O  O     . VAL   A 1 11  ? 29.053 -6.700  16.893 1.00 28.35 ? 8   VAL   A O     1 
ATOM   65   C  CB    . VAL   A 1 11  ? 28.877 -4.128  18.455 1.00 30.42 ? 8   VAL   A CB    1 
ATOM   66   C  CG1   . VAL   A 1 11  ? 30.324 -3.644  18.321 1.00 31.12 ? 8   VAL   A CG1   1 
ATOM   67   C  CG2   . VAL   A 1 11  ? 28.043 -3.127  19.266 1.00 32.01 ? 8   VAL   A CG2   1 
ATOM   68   N  N     . VAL   A 1 12  ? 29.602 -5.302  15.185 1.00 27.13 ? 9   VAL   A N     1 
ATOM   69   C  CA    . VAL   A 1 12  ? 30.292 -6.305  14.373 1.00 26.85 ? 9   VAL   A CA    1 
ATOM   70   C  C     . VAL   A 1 12  ? 31.715 -5.809  14.116 1.00 26.22 ? 9   VAL   A C     1 
ATOM   71   O  O     . VAL   A 1 12  ? 31.989 -4.621  14.253 1.00 26.94 ? 9   VAL   A O     1 
ATOM   72   C  CB    . VAL   A 1 12  ? 29.564 -6.561  13.029 1.00 26.12 ? 9   VAL   A CB    1 
ATOM   73   C  CG1   . VAL   A 1 12  ? 28.136 -7.074  13.194 1.00 27.58 ? 9   VAL   A CG1   1 
ATOM   74   C  CG2   . VAL   A 1 12  ? 29.621 -5.350  12.100 1.00 25.87 ? 9   VAL   A CG2   1 
ATOM   75   N  N     . GLY   A 1 13  ? 32.604 -6.716  13.685 1.00 26.99 ? 10  GLY   A N     1 
ATOM   76   C  CA    . GLY   A 1 13  ? 33.982 -6.343  13.389 1.00 28.45 ? 10  GLY   A CA    1 
ATOM   77   C  C     . GLY   A 1 13  ? 34.963 -7.467  13.703 1.00 28.12 ? 10  GLY   A C     1 
ATOM   78   O  O     . GLY   A 1 13  ? 34.647 -8.373  14.470 1.00 30.38 ? 10  GLY   A O     1 
ATOM   79   N  N     . ALA   A 1 14  ? 36.171 -7.387  13.114 1.00 28.26 ? 11  ALA   A N     1 
ATOM   80   C  CA    . ALA   A 1 14  ? 37.192 -8.416  13.276 1.00 29.25 ? 11  ALA   A CA    1 
ATOM   81   C  C     . ALA   A 1 14  ? 37.555 -8.637  14.745 1.00 30.54 ? 11  ALA   A C     1 
ATOM   82   O  O     . ALA   A 1 14  ? 37.346 -7.772  15.595 1.00 30.33 ? 11  ALA   A O     1 
ATOM   83   C  CB    . ALA   A 1 14  ? 38.420 -8.079  12.462 1.00 30.40 ? 11  ALA   A CB    1 
ATOM   84   N  N     . GLY   A 1 15  ? 38.098 -9.834  15.018 1.00 31.84 ? 12  GLY   A N     1 
ATOM   85   C  CA    . GLY   A 1 15  ? 38.614 -10.191 16.327 1.00 33.43 ? 12  GLY   A CA    1 
ATOM   86   C  C     . GLY   A 1 15  ? 39.526 -9.125  16.921 1.00 33.19 ? 12  GLY   A C     1 
ATOM   87   O  O     . GLY   A 1 15  ? 40.414 -8.618  16.251 1.00 33.43 ? 12  GLY   A O     1 
ATOM   88   N  N     . GLY   A 1 16  ? 39.302 -8.816  18.204 1.00 32.12 ? 13  GLY   A N     1 
ATOM   89   C  CA    . GLY   A 1 16  ? 40.183 -7.973  18.985 1.00 33.64 ? 13  GLY   A CA    1 
ATOM   90   C  C     . GLY   A 1 16  ? 40.110 -6.471  18.715 1.00 33.11 ? 13  GLY   A C     1 
ATOM   91   O  O     . GLY   A 1 16  ? 40.928 -5.728  19.268 1.00 35.90 ? 13  GLY   A O     1 
ATOM   92   N  N     . VAL   A 1 17  ? 39.125 -6.006  17.928 1.00 33.28 ? 14  VAL   A N     1 
ATOM   93   C  CA    . VAL   A 1 17  ? 39.049 -4.583  17.591 1.00 31.23 ? 14  VAL   A CA    1 
ATOM   94   C  C     . VAL   A 1 17  ? 38.506 -3.768  18.764 1.00 31.38 ? 14  VAL   A C     1 
ATOM   95   O  O     . VAL   A 1 17  ? 38.697 -2.557  18.795 1.00 29.60 ? 14  VAL   A O     1 
ATOM   96   C  CB    . VAL   A 1 17  ? 38.209 -4.302  16.327 1.00 29.80 ? 14  VAL   A CB    1 
ATOM   97   C  CG1   . VAL   A 1 17  ? 38.821 -4.955  15.097 1.00 30.06 ? 14  VAL   A CG1   1 
ATOM   98   C  CG2   . VAL   A 1 17  ? 36.738 -4.700  16.503 1.00 29.53 ? 14  VAL   A CG2   1 
ATOM   99   N  N     . GLY   A 1 18  ? 37.771 -4.425  19.671 1.00 30.47 ? 15  GLY   A N     1 
ATOM   100  C  CA    . GLY   A 1 18  ? 37.228 -3.786  20.865 1.00 31.18 ? 15  GLY   A CA    1 
ATOM   101  C  C     . GLY   A 1 18  ? 35.690 -3.682  20.874 1.00 28.62 ? 15  GLY   A C     1 
ATOM   102  O  O     . GLY   A 1 18  ? 35.151 -2.758  21.485 1.00 29.81 ? 15  GLY   A O     1 
ATOM   103  N  N     . LYS   A 1 19  ? 35.025 -4.588  20.175 1.00 28.22 ? 16  LYS   A N     1 
ATOM   104  C  CA    . LYS   A 1 19  ? 33.547 -4.602  20.145 1.00 28.12 ? 16  LYS   A CA    1 
ATOM   105  C  C     . LYS   A 1 19  ? 33.017 -4.661  21.583 1.00 29.64 ? 16  LYS   A C     1 
ATOM   106  O  O     . LYS   A 1 19  ? 32.186 -3.853  21.931 1.00 29.47 ? 16  LYS   A O     1 
ATOM   107  C  CB    . LYS   A 1 19  ? 33.053 -5.804  19.347 1.00 29.14 ? 16  LYS   A CB    1 
ATOM   108  C  CG    . LYS   A 1 19  ? 33.342 -5.755  17.857 1.00 29.67 ? 16  LYS   A CG    1 
ATOM   109  C  CD    . LYS   A 1 19  ? 32.983 -7.017  17.127 1.00 27.34 ? 16  LYS   A CD    1 
ATOM   110  C  CE    . LYS   A 1 19  ? 33.720 -8.234  17.621 1.00 30.06 ? 16  LYS   A CE    1 
ATOM   111  N  NZ    . LYS   A 1 19  ? 35.145 -8.204  17.244 1.00 31.31 ? 16  LYS   A NZ    1 
ATOM   112  N  N     . SER   A 1 20  ? 33.515 -5.605  22.367 1.00 30.93 ? 17  SER   A N     1 
ATOM   113  C  CA    . SER   A 1 20  ? 33.045 -5.797  23.760 1.00 32.35 ? 17  SER   A CA    1 
ATOM   114  C  C     . SER   A 1 20  ? 33.383 -4.609  24.642 1.00 34.58 ? 17  SER   A C     1 
ATOM   115  O  O     . SER   A 1 20  ? 32.510 -4.164  25.363 1.00 33.38 ? 17  SER   A O     1 
ATOM   116  C  CB    . SER   A 1 20  ? 33.629 -7.027  24.324 1.00 34.95 ? 17  SER   A CB    1 
ATOM   117  O  OG    . SER   A 1 20  ? 33.233 -8.114  23.554 1.00 35.22 ? 17  SER   A OG    1 
ATOM   118  N  N     . ALA   A 1 21  ? 34.618 -4.123  24.542 1.00 32.79 ? 18  ALA   A N     1 
ATOM   119  C  CA    . ALA   A 1 21  ? 35.048 -2.972  25.352 1.00 33.22 ? 18  ALA   A CA    1 
ATOM   120  C  C     . ALA   A 1 21  ? 34.171 -1.770  25.024 1.00 31.81 ? 18  ALA   A C     1 
ATOM   121  O  O     . ALA   A 1 21  ? 33.883 -1.026  25.924 1.00 33.60 ? 18  ALA   A O     1 
ATOM   122  C  CB    . ALA   A 1 21  ? 36.499 -2.677  25.093 1.00 33.80 ? 18  ALA   A CB    1 
ATOM   123  N  N     . LEU   A 1 22  ? 33.797 -1.597  23.762 1.00 30.92 ? 19  LEU   A N     1 
ATOM   124  C  CA    . LEU   A 1 22  ? 32.948 -0.457  23.417 1.00 30.59 ? 19  LEU   A CA    1 
ATOM   125  C  C     . LEU   A 1 22  ? 31.561 -0.633  24.043 1.00 32.33 ? 19  LEU   A C     1 
ATOM   126  O  O     . LEU   A 1 22  ? 30.977 0.300   24.579 1.00 32.77 ? 19  LEU   A O     1 
ATOM   127  C  CB    . LEU   A 1 22  ? 32.833 -0.350  21.890 1.00 31.72 ? 19  LEU   A CB    1 
ATOM   128  C  CG    . LEU   A 1 22  ? 33.968 0.397   21.178 1.00 29.93 ? 19  LEU   A CG    1 
ATOM   129  C  CD1   . LEU   A 1 22  ? 33.860 0.177   19.676 1.00 30.02 ? 19  LEU   A CD1   1 
ATOM   130  C  CD2   . LEU   A 1 22  ? 33.941 1.881   21.482 1.00 31.33 ? 19  LEU   A CD2   1 
ATOM   131  N  N     . THR   A 1 23  ? 30.999 -1.819  23.904 1.00 33.92 ? 20  THR   A N     1 
ATOM   132  C  CA    . THR   A 1 23  ? 29.639 -2.078  24.427 1.00 34.41 ? 20  THR   A CA    1 
ATOM   133  C  C     . THR   A 1 23  ? 29.598 -1.903  25.952 1.00 37.04 ? 20  THR   A C     1 
ATOM   134  O  O     . THR   A 1 23  ? 28.741 -1.209  26.438 1.00 35.62 ? 20  THR   A O     1 
ATOM   135  C  CB    . THR   A 1 23  ? 29.163 -3.460  23.999 1.00 34.32 ? 20  THR   A CB    1 
ATOM   136  O  OG1   . THR   A 1 23  ? 29.199 -3.492  22.577 1.00 32.67 ? 20  THR   A OG1   1 
ATOM   137  C  CG2   . THR   A 1 23  ? 27.767 -3.751  24.495 1.00 35.37 ? 20  THR   A CG2   1 
ATOM   138  N  N     . ILE   A 1 24  ? 30.549 -2.509  26.657 1.00 36.05 ? 21  ILE   A N     1 
ATOM   139  C  CA    . ILE   A 1 24  ? 30.637 -2.433  28.145 1.00 38.90 ? 21  ILE   A CA    1 
ATOM   140  C  C     . ILE   A 1 24  ? 30.890 -0.997  28.589 1.00 39.46 ? 21  ILE   A C     1 
ATOM   141  O  O     . ILE   A 1 24  ? 30.391 -0.613  29.621 1.00 39.83 ? 21  ILE   A O     1 
ATOM   142  C  CB    . ILE   A 1 24  ? 31.696 -3.406  28.678 1.00 40.57 ? 21  ILE   A CB    1 
ATOM   143  C  CG1   . ILE   A 1 24  ? 31.367 -4.845  28.298 1.00 40.46 ? 21  ILE   A CG1   1 
ATOM   144  C  CG2   . ILE   A 1 24  ? 31.879 -3.245  30.170 1.00 43.17 ? 21  ILE   A CG2   1 
ATOM   145  C  CD1   . ILE   A 1 24  ? 30.001 -5.253  28.699 1.00 44.05 ? 21  ILE   A CD1   1 
ATOM   146  N  N     . GLN   A 1 25  ? 31.661 -0.240  27.819 1.00 38.19 ? 22  GLN   A N     1 
ATOM   147  C  CA    . GLN   A 1 25  ? 31.924 1.180   28.145 1.00 39.68 ? 22  GLN   A CA    1 
ATOM   148  C  C     . GLN   A 1 25  ? 30.585 1.934   28.129 1.00 40.43 ? 22  GLN   A C     1 
ATOM   149  O  O     . GLN   A 1 25  ? 30.367 2.759   29.038 1.00 39.77 ? 22  GLN   A O     1 
ATOM   150  C  CB    . GLN   A 1 25  ? 32.987 1.688   27.171 1.00 40.09 ? 22  GLN   A CB    1 
ATOM   151  C  CG    . GLN   A 1 25  ? 33.552 3.069   27.474 1.00 42.70 ? 22  GLN   A CG    1 
ATOM   152  C  CD    . GLN   A 1 25  ? 34.107 3.212   28.870 1.00 45.73 ? 22  GLN   A CD    1 
ATOM   153  O  OE1   . GLN   A 1 25  ? 33.462 3.771   29.741 1.00 45.14 ? 22  GLN   A OE1   1 
ATOM   154  N  NE2   . GLN   A 1 25  ? 35.313 2.723   29.103 1.00 43.44 ? 22  GLN   A NE2   1 
ATOM   155  N  N     . LEU   A 1 26  ? 29.728 1.637   27.169 1.00 38.15 ? 23  LEU   A N     1 
ATOM   156  C  CA    . LEU   A 1 26  ? 28.413 2.313   27.137 1.00 38.94 ? 23  LEU   A CA    1 
ATOM   157  C  C     . LEU   A 1 26  ? 27.575 1.793   28.308 1.00 38.52 ? 23  LEU   A C     1 
ATOM   158  O  O     . LEU   A 1 26  ? 26.975 2.595   28.953 1.00 42.28 ? 23  LEU   A O     1 
ATOM   159  C  CB    . LEU   A 1 26  ? 27.707 2.028   25.810 1.00 37.12 ? 23  LEU   A CB    1 
ATOM   160  C  CG    . LEU   A 1 26  ? 26.447 2.855   25.556 1.00 37.68 ? 23  LEU   A CG    1 
ATOM   161  C  CD1   . LEU   A 1 26  ? 26.790 4.231   25.037 1.00 38.36 ? 23  LEU   A CD1   1 
ATOM   162  C  CD2   . LEU   A 1 26  ? 25.505 2.145   24.603 1.00 36.36 ? 23  LEU   A CD2   1 
ATOM   163  N  N     . ILE   A 1 27  ? 27.535 0.484   28.512 1.00 37.68 ? 24  ILE   A N     1 
ATOM   164  C  CA    . ILE   A 1 27  ? 26.683 -0.109  29.582 1.00 39.09 ? 24  ILE   A CA    1 
ATOM   165  C  C     . ILE   A 1 27  ? 27.164 0.218   31.004 1.00 41.92 ? 24  ILE   A C     1 
ATOM   166  O  O     . ILE   A 1 27  ? 26.366 0.764   31.749 1.00 42.72 ? 24  ILE   A O     1 
ATOM   167  C  CB    . ILE   A 1 27  ? 26.512 -1.616  29.340 1.00 39.11 ? 24  ILE   A CB    1 
ATOM   168  C  CG1   . ILE   A 1 27  ? 25.798 -1.871  28.017 1.00 39.23 ? 24  ILE   A CG1   1 
ATOM   169  C  CG2   . ILE   A 1 27  ? 25.795 -2.294  30.487 1.00 41.09 ? 24  ILE   A CG2   1 
ATOM   170  C  CD1   . ILE   A 1 27  ? 24.496 -1.133  27.865 1.00 38.84 ? 24  ILE   A CD1   1 
ATOM   171  N  N     . GLN   A 1 28  ? 28.440 0.019   31.312 1.00 41.43 ? 25  GLN   A N     1 
ATOM   172  C  CA    . GLN   A 1 28  ? 28.885 0.202   32.715 1.00 44.14 ? 25  GLN   A CA    1 
ATOM   173  C  C     . GLN   A 1 28  ? 29.709 1.460   32.947 1.00 45.09 ? 25  GLN   A C     1 
ATOM   174  O  O     . GLN   A 1 28  ? 30.039 1.689   34.091 1.00 45.97 ? 25  GLN   A O     1 
ATOM   175  C  CB    . GLN   A 1 28  ? 29.804 -0.949  33.096 1.00 44.98 ? 25  GLN   A CB    1 
ATOM   176  C  CG    . GLN   A 1 28  ? 29.194 -2.307  32.878 1.00 45.90 ? 25  GLN   A CG    1 
ATOM   177  C  CD    . GLN   A 1 28  ? 30.114 -3.412  33.316 1.00 48.09 ? 25  GLN   A CD    1 
ATOM   178  O  OE1   . GLN   A 1 28  ? 31.188 -3.173  33.822 1.00 53.19 ? 25  GLN   A OE1   1 
ATOM   179  N  NE2   . GLN   A 1 28  ? 29.692 -4.642  33.136 1.00 49.78 ? 25  GLN   A NE2   1 
ATOM   180  N  N     . ASN   A 1 29  ? 30.152 2.144   31.886 1.00 44.47 ? 26  ASN   A N     1 
ATOM   181  C  CA    . ASN   A 1 29  ? 31.093 3.302   31.941 1.00 47.16 ? 26  ASN   A CA    1 
ATOM   182  C  C     . ASN   A 1 29  ? 32.455 2.864   32.454 1.00 44.56 ? 26  ASN   A C     1 
ATOM   183  O  O     . ASN   A 1 29  ? 33.148 3.691   32.979 1.00 45.70 ? 26  ASN   A O     1 
ATOM   184  C  CB    . ASN   A 1 29  ? 30.597 4.539   32.778 1.00 53.67 ? 26  ASN   A CB    1 
ATOM   185  C  CG    . ASN   A 1 29  ? 29.655 5.407   31.989 1.00 57.77 ? 26  ASN   A CG    1 
ATOM   186  O  OD1   . ASN   A 1 29  ? 28.680 4.924   31.446 1.00 66.06 ? 26  ASN   A OD1   1 
ATOM   187  N  ND2   . ASN   A 1 29  ? 29.938 6.691   31.927 1.00 63.60 ? 26  ASN   A ND2   1 
ATOM   188  N  N     . HIS   A 1 30  ? 32.803 1.610   32.240 1.00 42.66 ? 27  HIS   A N     1 
ATOM   189  C  CA    . HIS   A 1 30  ? 34.039 1.007   32.755 1.00 45.23 ? 27  HIS   A CA    1 
ATOM   190  C  C     . HIS   A 1 30  ? 34.716 0.297   31.596 1.00 43.12 ? 27  HIS   A C     1 
ATOM   191  O  O     . HIS   A 1 30  ? 34.024 -0.259  30.770 1.00 41.36 ? 27  HIS   A O     1 
ATOM   192  C  CB    . HIS   A 1 30  ? 33.704 0.009   33.870 1.00 46.32 ? 27  HIS   A CB    1 
ATOM   193  C  CG    . HIS   A 1 30  ? 34.890 -0.473  34.630 1.00 48.68 ? 27  HIS   A CG    1 
ATOM   194  N  ND1   . HIS   A 1 30  ? 35.630 0.353   35.428 1.00 50.47 ? 27  HIS   A ND1   1 
ATOM   195  C  CD2   . HIS   A 1 30  ? 35.463 -1.686  34.717 1.00 49.61 ? 27  HIS   A CD2   1 
ATOM   196  C  CE1   . HIS   A 1 30  ? 36.614 -0.327  35.953 1.00 53.14 ? 27  HIS   A CE1   1 
ATOM   197  N  NE2   . HIS   A 1 30  ? 36.533 -1.572  35.544 1.00 52.64 ? 27  HIS   A NE2   1 
ATOM   198  N  N     . PHE   A 1 31  ? 36.033 0.346   31.600 1.00 44.98 ? 28  PHE   A N     1 
ATOM   199  C  CA    . PHE   A 1 31  ? 36.876 -0.293  30.596 1.00 44.10 ? 28  PHE   A CA    1 
ATOM   200  C  C     . PHE   A 1 31  ? 37.241 -1.703  31.049 1.00 46.85 ? 28  PHE   A C     1 
ATOM   201  O  O     . PHE   A 1 31  ? 37.854 -1.877  32.098 1.00 47.55 ? 28  PHE   A O     1 
ATOM   202  C  CB    . PHE   A 1 31  ? 38.153 0.524   30.362 1.00 44.90 ? 28  PHE   A CB    1 
ATOM   203  C  CG    . PHE   A 1 31  ? 39.105 -0.040  29.329 1.00 43.50 ? 28  PHE   A CG    1 
ATOM   204  C  CD1   . PHE   A 1 31  ? 38.720 -0.208  28.003 1.00 42.10 ? 28  PHE   A CD1   1 
ATOM   205  C  CD2   . PHE   A 1 31  ? 40.403 -0.390  29.672 1.00 46.58 ? 28  PHE   A CD2   1 
ATOM   206  C  CE1   . PHE   A 1 31  ? 39.600 -0.728  27.065 1.00 40.97 ? 28  PHE   A CE1   1 
ATOM   207  C  CE2   . PHE   A 1 31  ? 41.276 -0.921  28.734 1.00 44.66 ? 28  PHE   A CE2   1 
ATOM   208  C  CZ    . PHE   A 1 31  ? 40.881 -1.074  27.427 1.00 42.04 ? 28  PHE   A CZ    1 
ATOM   209  N  N     . VAL   A 1 32  ? 36.858 -2.673  30.235 1.00 49.63 ? 29  VAL   A N     1 
ATOM   210  C  CA    . VAL   A 1 32  ? 37.107 -4.106  30.514 1.00 55.42 ? 29  VAL   A CA    1 
ATOM   211  C  C     . VAL   A 1 32  ? 38.606 -4.363  30.520 1.00 59.95 ? 29  VAL   A C     1 
ATOM   212  O  O     . VAL   A 1 32  ? 39.331 -3.760  29.752 1.00 61.85 ? 29  VAL   A O     1 
ATOM   213  C  CB    . VAL   A 1 32  ? 36.431 -5.004  29.468 1.00 55.67 ? 29  VAL   A CB    1 
ATOM   214  C  CG1   . VAL   A 1 32  ? 34.928 -5.002  29.601 1.00 56.51 ? 29  VAL   A CG1   1 
ATOM   215  C  CG2   . VAL   A 1 32  ? 36.869 -4.651  28.059 1.00 55.21 ? 29  VAL   A CG2   1 
ATOM   216  N  N     . ASP   A 1 33  ? 39.006 -5.318  31.342 1.00 65.29 ? 30  ASP   A N     1 
ATOM   217  C  CA    . ASP   A 1 33  ? 40.422 -5.738  31.405 1.00 67.58 ? 30  ASP   A CA    1 
ATOM   218  C  C     . ASP   A 1 33  ? 40.483 -7.252  31.187 1.00 69.91 ? 30  ASP   A C     1 
ATOM   219  O  O     . ASP   A 1 33  ? 39.444 -7.853  30.881 1.00 65.96 ? 30  ASP   A O     1 
ATOM   220  C  CB    . ASP   A 1 33  ? 41.031 -5.285  32.730 1.00 71.75 ? 30  ASP   A CB    1 
ATOM   221  C  CG    . ASP   A 1 33  ? 40.237 -5.774  33.921 1.00 71.81 ? 30  ASP   A CG    1 
ATOM   222  O  OD1   . ASP   A 1 33  ? 39.540 -6.777  33.776 1.00 71.26 ? 30  ASP   A OD1   1 
ATOM   223  O  OD2   . ASP   A 1 33  ? 40.310 -5.138  34.953 1.00 74.52 ? 30  ASP   A OD2   1 
ATOM   224  N  N     . GLU   A 1 34  ? 41.675 -7.830  31.340 1.00 74.35 ? 31  GLU   A N     1 
ATOM   225  C  CA    . GLU   A 1 34  ? 41.915 -9.289  31.180 1.00 77.36 ? 31  GLU   A CA    1 
ATOM   226  C  C     . GLU   A 1 34  ? 40.851 -10.070 31.942 1.00 80.12 ? 31  GLU   A C     1 
ATOM   227  O  O     . GLU   A 1 34  ? 40.276 -10.963 31.317 1.00 82.09 ? 31  GLU   A O     1 
ATOM   228  C  CB    . GLU   A 1 34  ? 43.249 -9.674  31.812 1.00 79.89 ? 31  GLU   A CB    1 
ATOM   229  C  CG    . GLU   A 1 34  ? 43.496 -9.020  33.170 1.00 82.69 ? 31  GLU   A CG    1 
ATOM   230  C  CD    . GLU   A 1 34  ? 42.876 -9.641  34.414 1.00 82.04 ? 31  GLU   A CD    1 
ATOM   231  O  OE1   . GLU   A 1 34  ? 42.311 -8.900  35.210 1.00 78.53 ? 31  GLU   A OE1   1 
ATOM   232  O  OE2   . GLU   A 1 34  ? 42.992 -10.855 34.583 1.00 83.21 ? 31  GLU   A OE2   1 
ATOM   233  N  N     . GLU   A 1 40  ? 30.105 -13.244 24.068 1.00 63.17 ? 37  GLU   A N     1 
ATOM   234  C  CA    . GLU   A 1 40  ? 28.949 -12.931 23.181 1.00 63.09 ? 37  GLU   A CA    1 
ATOM   235  C  C     . GLU   A 1 40  ? 27.673 -12.806 24.014 1.00 58.96 ? 37  GLU   A C     1 
ATOM   236  O  O     . GLU   A 1 40  ? 27.196 -13.836 24.494 1.00 58.43 ? 37  GLU   A O     1 
ATOM   237  C  CB    . GLU   A 1 40  ? 28.753 -14.001 22.109 1.00 66.64 ? 37  GLU   A CB    1 
ATOM   238  C  CG    . GLU   A 1 40  ? 29.511 -13.722 20.830 1.00 66.35 ? 37  GLU   A CG    1 
ATOM   239  C  CD    . GLU   A 1 40  ? 29.089 -14.604 19.671 1.00 67.31 ? 37  GLU   A CD    1 
ATOM   240  O  OE1   . GLU   A 1 40  ? 28.763 -15.761 19.926 1.00 69.27 ? 37  GLU   A OE1   1 
ATOM   241  O  OE2   . GLU   A 1 40  ? 29.091 -14.140 18.527 1.00 58.27 ? 37  GLU   A OE2   1 
ATOM   242  N  N     . ASP   A 1 41  ? 27.166 -11.582 24.155 1.00 52.22 ? 38  ASP   A N     1 
ATOM   243  C  CA    . ASP   A 1 41  ? 25.935 -11.366 24.935 1.00 50.93 ? 38  ASP   A CA    1 
ATOM   244  C  C     . ASP   A 1 41  ? 25.194 -10.122 24.427 1.00 45.24 ? 38  ASP   A C     1 
ATOM   245  O  O     . ASP   A 1 41  ? 25.672 -9.467  23.512 1.00 39.15 ? 38  ASP   A O     1 
ATOM   246  C  CB    . ASP   A 1 41  ? 26.242 -11.303 26.427 1.00 54.28 ? 38  ASP   A CB    1 
ATOM   247  C  CG    . ASP   A 1 41  ? 25.138 -11.914 27.283 1.00 59.25 ? 38  ASP   A CG    1 
ATOM   248  O  OD1   . ASP   A 1 41  ? 24.042 -12.098 26.762 1.00 58.69 ? 38  ASP   A OD1   1 
ATOM   249  O  OD2   . ASP   A 1 41  ? 25.396 -12.188 28.457 1.00 64.18 ? 38  ASP   A OD2   1 
ATOM   250  N  N     . SER   A 1 42  ? 24.039 -9.869  25.032 1.00 44.10 ? 39  SER   A N     1 
ATOM   251  C  CA    . SER   A 1 42  ? 23.162 -8.725  24.728 1.00 42.68 ? 39  SER   A CA    1 
ATOM   252  C  C     . SER   A 1 42  ? 23.031 -7.846  25.967 1.00 41.75 ? 39  SER   A C     1 
ATOM   253  O  O     . SER   A 1 42  ? 23.266 -8.348  27.047 1.00 42.82 ? 39  SER   A O     1 
ATOM   254  C  CB    . SER   A 1 42  ? 21.845 -9.105  24.167 1.00 43.32 ? 39  SER   A CB    1 
ATOM   255  O  OG    . SER   A 1 42  ? 21.063 -9.768  25.126 1.00 44.25 ? 39  SER   A OG    1 
ATOM   256  N  N     . TYR   A 1 43  ? 22.853 -6.546  25.747 1.00 41.10 ? 40  TYR   A N     1 
ATOM   257  C  CA    . TYR   A 1 43  ? 22.799 -5.517  26.811 1.00 42.66 ? 40  TYR   A CA    1 
ATOM   258  C  C     . TYR   A 1 43  ? 21.589 -4.630  26.564 1.00 43.78 ? 40  TYR   A C     1 
ATOM   259  O  O     . TYR   A 1 43  ? 21.172 -4.528  25.427 1.00 40.26 ? 40  TYR   A O     1 
ATOM   260  C  CB    . TYR   A 1 43  ? 24.086 -4.694  26.822 1.00 43.61 ? 40  TYR   A CB    1 
ATOM   261  C  CG    . TYR   A 1 43  ? 25.305 -5.550  27.004 1.00 45.07 ? 40  TYR   A CG    1 
ATOM   262  C  CD1   . TYR   A 1 43  ? 25.936 -6.155  25.935 1.00 43.96 ? 40  TYR   A CD1   1 
ATOM   263  C  CD2   . TYR   A 1 43  ? 25.814 -5.790  28.263 1.00 48.53 ? 40  TYR   A CD2   1 
ATOM   264  C  CE1   . TYR   A 1 43  ? 27.011 -7.000  26.113 1.00 45.55 ? 40  TYR   A CE1   1 
ATOM   265  C  CE2   . TYR   A 1 43  ? 26.910 -6.601  28.455 1.00 49.03 ? 40  TYR   A CE2   1 
ATOM   266  C  CZ    . TYR   A 1 43  ? 27.514 -7.209  27.377 1.00 48.75 ? 40  TYR   A CZ    1 
ATOM   267  O  OH    . TYR   A 1 43  ? 28.582 -8.021  27.576 1.00 48.96 ? 40  TYR   A OH    1 
ATOM   268  N  N     . ARG   A 1 44  ? 21.069 -4.025  27.628 1.00 46.15 ? 41  ARG   A N     1 
ATOM   269  C  CA    . ARG   A 1 44  ? 19.878 -3.152  27.523 1.00 48.17 ? 41  ARG   A CA    1 
ATOM   270  C  C     . ARG   A 1 44  ? 20.116 -1.851  28.261 1.00 47.65 ? 41  ARG   A C     1 
ATOM   271  O  O     . ARG   A 1 44  ? 20.682 -1.862  29.323 1.00 48.63 ? 41  ARG   A O     1 
ATOM   272  C  CB    . ARG   A 1 44  ? 18.630 -3.866  28.027 1.00 53.40 ? 41  ARG   A CB    1 
ATOM   273  C  CG    . ARG   A 1 44  ? 17.983 -4.710  26.947 1.00 56.88 ? 41  ARG   A CG    1 
ATOM   274  C  CD    . ARG   A 1 44  ? 17.286 -5.865  27.605 1.00 60.93 ? 41  ARG   A CD    1 
ATOM   275  N  NE    . ARG   A 1 44  ? 15.877 -5.604  27.780 1.00 64.09 ? 41  ARG   A NE    1 
ATOM   276  C  CZ    . ARG   A 1 44  ? 14.992 -5.806  26.832 1.00 65.59 ? 41  ARG   A CZ    1 
ATOM   277  N  NH1   . ARG   A 1 44  ? 15.388 -6.214  25.642 1.00 62.65 ? 41  ARG   A NH1   1 
ATOM   278  N  NH2   . ARG   A 1 44  ? 13.719 -5.565  27.065 1.00 66.71 ? 41  ARG   A NH2   1 
ATOM   279  N  N     . LYS   A 1 45  ? 19.609 -0.782  27.691 1.00 46.73 ? 42  LYS   A N     1 
ATOM   280  C  CA    . LYS   A 1 45  ? 19.797 0.555   28.270 1.00 48.21 ? 42  LYS   A CA    1 
ATOM   281  C  C     . LYS   A 1 45  ? 18.742 1.505   27.714 1.00 46.48 ? 42  LYS   A C     1 
ATOM   282  O  O     . LYS   A 1 45  ? 18.542 1.558   26.506 1.00 44.68 ? 42  LYS   A O     1 
ATOM   283  C  CB    . LYS   A 1 45  ? 21.222 1.028   27.974 1.00 46.99 ? 42  LYS   A CB    1 
ATOM   284  C  CG    . LYS   A 1 45  ? 21.663 2.304   28.664 1.00 49.56 ? 42  LYS   A CG    1 
ATOM   285  C  CD    . LYS   A 1 45  ? 22.995 2.774   28.165 1.00 50.92 ? 42  LYS   A CD    1 
ATOM   286  C  CE    . LYS   A 1 45  ? 23.344 4.190   28.554 1.00 53.98 ? 42  LYS   A CE    1 
ATOM   287  N  NZ    . LYS   A 1 45  ? 24.335 4.243   29.646 1.00 56.00 ? 42  LYS   A NZ    1 
ATOM   288  N  N     . GLN   A 1 46  ? 18.101 2.236   28.611 1.00 46.64 ? 43  GLN   A N     1 
ATOM   289  C  CA    . GLN   A 1 46  ? 17.095 3.195   28.201 1.00 46.36 ? 43  GLN   A CA    1 
ATOM   290  C  C     . GLN   A 1 46  ? 17.764 4.558   28.216 1.00 46.84 ? 43  GLN   A C     1 
ATOM   291  O  O     . GLN   A 1 46  ? 18.459 4.895   29.174 1.00 47.49 ? 43  GLN   A O     1 
ATOM   292  C  CB    . GLN   A 1 46  ? 15.885 3.125   29.130 1.00 48.79 ? 43  GLN   A CB    1 
ATOM   293  C  CG    . GLN   A 1 46  ? 14.770 4.074   28.732 1.00 49.90 ? 43  GLN   A CG    1 
ATOM   294  C  CD    . GLN   A 1 46  ? 13.697 4.185   29.785 1.00 51.81 ? 43  GLN   A CD    1 
ATOM   295  O  OE1   . GLN   A 1 46  ? 13.066 3.200   30.143 1.00 51.41 ? 43  GLN   A OE1   1 
ATOM   296  N  NE2   . GLN   A 1 46  ? 13.468 5.402   30.256 1.00 54.01 ? 43  GLN   A NE2   1 
ATOM   297  N  N     . VAL   A 1 47  ? 17.612 5.298   27.114 1.00 45.44 ? 44  VAL   A N     1 
ATOM   298  C  CA    . VAL   A 1 47  ? 18.281 6.571   26.965 1.00 46.11 ? 44  VAL   A CA    1 
ATOM   299  C  C     . VAL   A 1 47  ? 17.289 7.550   26.359 1.00 47.63 ? 44  VAL   A C     1 
ATOM   300  O  O     . VAL   A 1 47  ? 16.297 7.151   25.749 1.00 48.98 ? 44  VAL   A O     1 
ATOM   301  C  CB    . VAL   A 1 47  ? 19.554 6.448   26.103 1.00 45.75 ? 44  VAL   A CB    1 
ATOM   302  C  CG1   . VAL   A 1 47  ? 20.513 5.400   26.650 1.00 44.66 ? 44  VAL   A CG1   1 
ATOM   303  C  CG2   . VAL   A 1 47  ? 19.222 6.151   24.641 1.00 44.29 ? 44  VAL   A CG2   1 
ATOM   304  N  N     . VAL   A 1 48  ? 17.570 8.829   26.565 1.00 50.32 ? 45  VAL   A N     1 
ATOM   305  C  CA    . VAL   A 1 48  ? 16.873 9.906   25.896 1.00 51.86 ? 45  VAL   A CA    1 
ATOM   306  C  C     . VAL   A 1 48  ? 17.841 10.448  24.848 1.00 50.80 ? 45  VAL   A C     1 
ATOM   307  O  O     . VAL   A 1 48  ? 18.967 10.811  25.185 1.00 51.82 ? 45  VAL   A O     1 
ATOM   308  C  CB    . VAL   A 1 48  ? 16.465 11.002  26.905 1.00 55.17 ? 45  VAL   A CB    1 
ATOM   309  C  CG1   . VAL   A 1 48  ? 16.074 12.303  26.212 1.00 57.10 ? 45  VAL   A CG1   1 
ATOM   310  C  CG2   . VAL   A 1 48  ? 15.387 10.540  27.884 1.00 58.03 ? 45  VAL   A CG2   1 
ATOM   311  N  N     . ILE   A 1 49  ? 17.394 10.475  23.586 1.00 50.28 ? 46  ILE   A N     1 
ATOM   312  C  CA    . ILE   A 1 49  ? 18.117 11.108  22.487 1.00 47.20 ? 46  ILE   A CA    1 
ATOM   313  C  C     . ILE   A 1 49  ? 17.145 12.070  21.813 1.00 48.37 ? 46  ILE   A C     1 
ATOM   314  O  O     . ILE   A 1 49  ? 16.046 11.662  21.414 1.00 47.25 ? 46  ILE   A O     1 
ATOM   315  C  CB    . ILE   A 1 49  ? 18.606 10.036  21.492 1.00 45.66 ? 46  ILE   A CB    1 
ATOM   316  C  CG1   . ILE   A 1 49  ? 19.569 9.033   22.131 1.00 44.19 ? 46  ILE   A CG1   1 
ATOM   317  C  CG2   . ILE   A 1 49  ? 19.181 10.666  20.228 1.00 45.38 ? 46  ILE   A CG2   1 
ATOM   318  C  CD1   . ILE   A 1 49  ? 19.584 7.673   21.464 1.00 43.31 ? 46  ILE   A CD1   1 
ATOM   319  N  N     . ASP   A 1 50  ? 17.554 13.340  21.713 1.00 50.55 ? 47  ASP   A N     1 
ATOM   320  C  CA    . ASP   A 1 50  ? 16.765 14.392  21.081 1.00 52.13 ? 47  ASP   A CA    1 
ATOM   321  C  C     . ASP   A 1 50  ? 15.334 14.350  21.617 1.00 54.77 ? 47  ASP   A C     1 
ATOM   322  O  O     . ASP   A 1 50  ? 14.380 14.477  20.850 1.00 55.40 ? 47  ASP   A O     1 
ATOM   323  C  CB    . ASP   A 1 50  ? 16.814 14.298  19.547 1.00 51.43 ? 47  ASP   A CB    1 
ATOM   324  C  CG    . ASP   A 1 50  ? 18.228 14.352  19.001 1.00 49.55 ? 47  ASP   A CG    1 
ATOM   325  O  OD1   . ASP   A 1 50  ? 19.040 15.103  19.565 1.00 53.15 ? 47  ASP   A OD1   1 
ATOM   326  O  OD2   . ASP   A 1 50  ? 18.508 13.636  18.022 1.00 46.75 ? 47  ASP   A OD2   1 
ATOM   327  N  N     . GLY   A 1 51  ? 15.202 14.109  22.929 1.00 56.45 ? 48  GLY   A N     1 
ATOM   328  C  CA    . GLY   A 1 51  ? 13.932 14.246  23.629 1.00 59.68 ? 48  GLY   A CA    1 
ATOM   329  C  C     . GLY   A 1 51  ? 12.947 13.118  23.334 1.00 59.09 ? 48  GLY   A C     1 
ATOM   330  O  O     . GLY   A 1 51  ? 11.789 13.185  23.746 1.00 62.35 ? 48  GLY   A O     1 
ATOM   331  N  N     . GLU   A 1 52  ? 13.404 12.093  22.604 1.00 57.44 ? 49  GLU   A N     1 
ATOM   332  C  CA    . GLU   A 1 52  ? 12.639 10.861  22.470 1.00 57.49 ? 49  GLU   A CA    1 
ATOM   333  C  C     . GLU   A 1 52  ? 13.288 9.812   23.375 1.00 55.36 ? 49  GLU   A C     1 
ATOM   334  O  O     . GLU   A 1 52  ? 14.515 9.676   23.391 1.00 56.45 ? 49  GLU   A O     1 
ATOM   335  C  CB    . GLU   A 1 52  ? 12.547 10.374  21.016 1.00 57.99 ? 49  GLU   A CB    1 
ATOM   336  C  CG    . GLU   A 1 52  ? 11.925 11.355  20.021 1.00 61.39 ? 49  GLU   A CG    1 
ATOM   337  C  CD    . GLU   A 1 52  ? 10.448 11.721  20.134 1.00 67.47 ? 49  GLU   A CD    1 
ATOM   338  O  OE1   . GLU   A 1 52  ? 9.669  10.953  20.739 1.00 71.90 ? 49  GLU   A OE1   1 
ATOM   339  O  OE2   . GLU   A 1 52  ? 10.076 12.785  19.608 1.00 69.69 ? 49  GLU   A OE2   1 
ATOM   340  N  N     . THR   A 1 53  ? 12.456 9.083   24.130 1.00 53.24 ? 50  THR   A N     1 
ATOM   341  C  CA    . THR   A 1 53  ? 12.921 8.010   24.997 1.00 52.50 ? 50  THR   A CA    1 
ATOM   342  C  C     . THR   A 1 53  ? 12.965 6.732   24.167 1.00 50.31 ? 50  THR   A C     1 
ATOM   343  O  O     . THR   A 1 53  ? 12.087 6.516   23.339 1.00 53.45 ? 50  THR   A O     1 
ATOM   344  C  CB    . THR   A 1 53  ? 12.023 7.866   26.243 1.00 54.33 ? 50  THR   A CB    1 
ATOM   345  O  OG1   . THR   A 1 53  ? 11.923 9.132   26.908 1.00 56.96 ? 50  THR   A OG1   1 
ATOM   346  C  CG2   . THR   A 1 53  ? 12.501 6.815   27.219 1.00 53.76 ? 50  THR   A CG2   1 
ATOM   347  N  N     . CYS   A 1 54  ? 13.987 5.891   24.382 1.00 48.75 ? 51  CYS   A N     1 
ATOM   348  C  CA    . CYS   A 1 54  ? 14.017 4.624   23.673 1.00 48.01 ? 51  CYS   A CA    1 
ATOM   349  C  C     . CYS   A 1 54  ? 14.813 3.575   24.443 1.00 46.06 ? 51  CYS   A C     1 
ATOM   350  O  O     . CYS   A 1 54  ? 15.645 3.907   25.277 1.00 46.04 ? 51  CYS   A O     1 
ATOM   351  C  CB    . CYS   A 1 54  ? 14.591 4.800   22.271 1.00 46.36 ? 51  CYS   A CB    1 
ATOM   352  S  SG    . CYS   A 1 54  ? 16.265 5.494   22.272 1.00 46.41 ? 51  CYS   A SG    1 
ATOM   353  N  N     . LEU   A 1 55  ? 14.547 2.306   24.135 1.00 44.21 ? 52  LEU   A N     1 
ATOM   354  C  CA    . LEU   A 1 55  ? 15.266 1.204   24.749 1.00 44.25 ? 52  LEU   A CA    1 
ATOM   355  C  C     . LEU   A 1 55  ? 16.296 0.682   23.745 1.00 41.08 ? 52  LEU   A C     1 
ATOM   356  O  O     . LEU   A 1 55  ? 15.916 0.239   22.660 1.00 39.49 ? 52  LEU   A O     1 
ATOM   357  C  CB    . LEU   A 1 55  ? 14.234 0.135   25.108 1.00 47.09 ? 52  LEU   A CB    1 
ATOM   358  C  CG    . LEU   A 1 55  ? 14.738 -1.151  25.774 1.00 48.85 ? 52  LEU   A CG    1 
ATOM   359  C  CD1   . LEU   A 1 55  ? 15.600 -0.853  26.989 1.00 49.88 ? 52  LEU   A CD1   1 
ATOM   360  C  CD2   . LEU   A 1 55  ? 13.548 -2.003  26.190 1.00 52.39 ? 52  LEU   A CD2   1 
ATOM   361  N  N     . LEU   A 1 56  ? 17.576 0.738   24.119 1.00 40.69 ? 53  LEU   A N     1 
ATOM   362  C  CA    . LEU   A 1 56  ? 18.667 0.210   23.257 1.00 37.63 ? 53  LEU   A CA    1 
ATOM   363  C  C     . LEU   A 1 56  ? 18.859 -1.267  23.590 1.00 37.77 ? 53  LEU   A C     1 
ATOM   364  O  O     . LEU   A 1 56  ? 19.058 -1.565  24.760 1.00 38.16 ? 53  LEU   A O     1 
ATOM   365  C  CB    . LEU   A 1 56  ? 19.973 0.959   23.519 1.00 36.81 ? 53  LEU   A CB    1 
ATOM   366  C  CG    . LEU   A 1 56  ? 19.947 2.456   23.253 1.00 37.77 ? 53  LEU   A CG    1 
ATOM   367  C  CD1   . LEU   A 1 56  ? 21.353 2.986   23.101 1.00 38.61 ? 53  LEU   A CD1   1 
ATOM   368  C  CD2   . LEU   A 1 56  ? 19.124 2.777   22.028 1.00 38.80 ? 53  LEU   A CD2   1 
ATOM   369  N  N     . ASP   A 1 57  ? 18.746 -2.136  22.602 1.00 35.66 ? 54  ASP   A N     1 
ATOM   370  C  CA    . ASP   A 1 57  ? 18.938 -3.596  22.748 1.00 36.42 ? 54  ASP   A CA    1 
ATOM   371  C  C     . ASP   A 1 57  ? 20.182 -3.963  21.929 1.00 35.83 ? 54  ASP   A C     1 
ATOM   372  O  O     . ASP   A 1 57  ? 20.059 -4.129  20.749 1.00 33.10 ? 54  ASP   A O     1 
ATOM   373  C  CB    . ASP   A 1 57  ? 17.683 -4.340  22.318 1.00 38.95 ? 54  ASP   A CB    1 
ATOM   374  C  CG    . ASP   A 1 57  ? 17.754 -5.811  22.612 1.00 40.98 ? 54  ASP   A CG    1 
ATOM   375  O  OD1   . ASP   A 1 57  ? 18.735 -6.218  23.170 1.00 40.93 ? 54  ASP   A OD1   1 
ATOM   376  O  OD2   . ASP   A 1 57  ? 16.837 -6.518  22.244 1.00 41.56 ? 54  ASP   A OD2   1 
ATOM   377  N  N     . ILE   A 1 58  ? 21.320 -4.146  22.583 1.00 34.92 ? 55  ILE   A N     1 
ATOM   378  C  CA    . ILE   A 1 58  ? 22.605 -4.273  21.836 1.00 32.77 ? 55  ILE   A CA    1 
ATOM   379  C  C     . ILE   A 1 58  ? 23.178 -5.679  21.885 1.00 32.98 ? 55  ILE   A C     1 
ATOM   380  O  O     . ILE   A 1 58  ? 23.376 -6.150  22.966 1.00 33.14 ? 55  ILE   A O     1 
ATOM   381  C  CB    . ILE   A 1 58  ? 23.596 -3.267  22.429 1.00 34.16 ? 55  ILE   A CB    1 
ATOM   382  C  CG1   . ILE   A 1 58  ? 23.000 -1.862  22.433 1.00 34.28 ? 55  ILE   A CG1   1 
ATOM   383  C  CG2   . ILE   A 1 58  ? 24.925 -3.339  21.704 1.00 33.46 ? 55  ILE   A CG2   1 
ATOM   384  C  CD1   . ILE   A 1 58  ? 23.696 -0.896  23.313 1.00 35.70 ? 55  ILE   A CD1   1 
ATOM   385  N  N     . LEU   A 1 59  ? 23.475 -6.236  20.718 1.00 30.70 ? 56  LEU   A N     1 
ATOM   386  C  CA    . LEU   A 1 59  ? 24.098 -7.569  20.592 1.00 31.50 ? 56  LEU   A CA    1 
ATOM   387  C  C     . LEU   A 1 59  ? 25.595 -7.383  20.336 1.00 30.13 ? 56  LEU   A C     1 
ATOM   388  O  O     . LEU   A 1 59  ? 25.948 -6.785  19.350 1.00 28.16 ? 56  LEU   A O     1 
ATOM   389  C  CB    . LEU   A 1 59  ? 23.458 -8.317  19.427 1.00 31.51 ? 56  LEU   A CB    1 
ATOM   390  C  CG    . LEU   A 1 59  ? 24.055 -9.682  19.112 1.00 32.25 ? 56  LEU   A CG    1 
ATOM   391  C  CD1   . LEU   A 1 59  ? 23.823 -10.654 20.252 1.00 34.77 ? 56  LEU   A CD1   1 
ATOM   392  C  CD2   . LEU   A 1 59  ? 23.475 -10.245 17.841 1.00 32.02 ? 56  LEU   A CD2   1 
ATOM   393  N  N     . ASP   A 1 60  ? 26.413 -7.920  21.218 1.00 31.22 ? 57  ASP   A N     1 
ATOM   394  C  CA    . ASP   A 1 60  ? 27.862 -7.831  21.052 1.00 32.63 ? 57  ASP   A CA    1 
ATOM   395  C  C     . ASP   A 1 60  ? 28.357 -9.120  20.391 1.00 33.30 ? 57  ASP   A C     1 
ATOM   396  O  O     . ASP   A 1 60  ? 28.386 -10.142 21.055 1.00 39.45 ? 57  ASP   A O     1 
ATOM   397  C  CB    . ASP   A 1 60  ? 28.519 -7.597  22.417 1.00 32.60 ? 57  ASP   A CB    1 
ATOM   398  C  CG    . ASP   A 1 60  ? 30.042 -7.697  22.379 1.00 32.75 ? 57  ASP   A CG    1 
ATOM   399  O  OD1   . ASP   A 1 60  ? 30.603 -7.476  21.288 1.00 31.60 ? 57  ASP   A OD1   1 
ATOM   400  O  OD2   . ASP   A 1 60  ? 30.641 -7.958  23.441 1.00 33.70 ? 57  ASP   A OD2   1 
ATOM   401  N  N     . THR   A 1 61  ? 28.739 -9.080  19.102 1.00 32.42 ? 58  THR   A N     1 
ATOM   402  C  CA    . THR   A 1 61  ? 29.077 -10.272 18.326 1.00 33.71 ? 58  THR   A CA    1 
ATOM   403  C  C     . THR   A 1 61  ? 30.580 -10.565 18.361 1.00 38.24 ? 58  THR   A C     1 
ATOM   404  O  O     . THR   A 1 61  ? 31.389 -9.710  18.735 1.00 41.85 ? 58  THR   A O     1 
ATOM   405  C  CB    . THR   A 1 61  ? 28.656 -10.165 16.848 1.00 31.52 ? 58  THR   A CB    1 
ATOM   406  O  OG1   . THR   A 1 61  ? 29.481 -9.233  16.130 1.00 29.18 ? 58  THR   A OG1   1 
ATOM   407  C  CG2   . THR   A 1 61  ? 27.185 -9.845  16.689 1.00 31.81 ? 58  THR   A CG2   1 
ATOM   408  N  N     . ALA   A 1 62  ? 30.928 -11.749 17.891 1.00 40.37 ? 59  ALA   A N     1 
ATOM   409  C  CA    . ALA   A 1 62  ? 32.347 -12.127 17.838 1.00 43.69 ? 59  ALA   A CA    1 
ATOM   410  C  C     . ALA   A 1 62  ? 32.882 -11.941 16.413 1.00 43.67 ? 59  ALA   A C     1 
ATOM   411  O  O     . ALA   A 1 62  ? 32.104 -11.938 15.468 1.00 38.70 ? 59  ALA   A O     1 
ATOM   412  C  CB    . ALA   A 1 62  ? 32.510 -13.548 18.319 1.00 47.50 ? 59  ALA   A CB    1 
ATOM   413  N  N     . GLY   A 1 63  ? 34.195 -11.725 16.323 1.00 44.52 ? 60  GLY   A N     1 
ATOM   414  C  CA    . GLY   A 1 63  ? 34.879 -11.533 15.038 1.00 49.18 ? 60  GLY   A CA    1 
ATOM   415  C  C     . GLY   A 1 63  ? 34.848 -12.828 14.276 1.00 53.49 ? 60  GLY   A C     1 
ATOM   416  O  O     . GLY   A 1 63  ? 34.604 -12.814 13.059 1.00 60.53 ? 60  GLY   A O     1 
ATOM   417  N  N     . TYR   A 1 67  ? 29.045 -19.661 11.636 1.00 61.34 ? 64  TYR   A N     1 
ATOM   418  C  CA    . TYR   A 1 67  ? 27.717 -20.278 11.378 1.00 61.46 ? 64  TYR   A CA    1 
ATOM   419  C  C     . TYR   A 1 67  ? 26.847 -19.259 10.650 1.00 59.91 ? 64  TYR   A C     1 
ATOM   420  O  O     . TYR   A 1 67  ? 26.242 -18.441 11.302 1.00 57.13 ? 64  TYR   A O     1 
ATOM   421  C  CB    . TYR   A 1 67  ? 27.082 -20.799 12.668 1.00 61.04 ? 64  TYR   A CB    1 
ATOM   422  C  CG    . TYR   A 1 67  ? 25.792 -21.562 12.491 1.00 59.04 ? 64  TYR   A CG    1 
ATOM   423  C  CD1   . TYR   A 1 67  ? 25.619 -22.433 11.439 1.00 59.19 ? 64  TYR   A CD1   1 
ATOM   424  C  CD2   . TYR   A 1 67  ? 24.744 -21.410 13.378 1.00 57.42 ? 64  TYR   A CD2   1 
ATOM   425  C  CE1   . TYR   A 1 67  ? 24.445 -23.143 11.281 1.00 60.91 ? 64  TYR   A CE1   1 
ATOM   426  C  CE2   . TYR   A 1 67  ? 23.554 -22.094 13.223 1.00 59.17 ? 64  TYR   A CE2   1 
ATOM   427  C  CZ    . TYR   A 1 67  ? 23.410 -22.974 12.175 1.00 60.21 ? 64  TYR   A CZ    1 
ATOM   428  O  OH    . TYR   A 1 67  ? 22.256 -23.650 11.995 1.00 63.78 ? 64  TYR   A OH    1 
ATOM   429  N  N     . SER   A 1 68  ? 26.694 -19.451 9.347  1.00 62.11 ? 65  SER   A N     1 
ATOM   430  C  CA    . SER   A 1 68  ? 25.980 -18.517 8.447  1.00 60.81 ? 65  SER   A CA    1 
ATOM   431  C  C     . SER   A 1 68  ? 24.525 -18.265 8.873  1.00 60.92 ? 65  SER   A C     1 
ATOM   432  O  O     . SER   A 1 68  ? 24.041 -17.167 8.588  1.00 58.52 ? 65  SER   A O     1 
ATOM   433  C  CB    . SER   A 1 68  ? 26.088 -18.961 7.008  1.00 63.49 ? 65  SER   A CB    1 
ATOM   434  O  OG    . SER   A 1 68  ? 27.444 -19.064 6.605  1.00 65.21 ? 65  SER   A OG    1 
ATOM   435  N  N     . ALA   A 1 69  ? 23.838 -19.254 9.451  1.00 58.53 ? 66  ALA   A N     1 
ATOM   436  C  CA    . ALA   A 1 69  ? 22.420 -19.103 9.840  1.00 57.94 ? 66  ALA   A CA    1 
ATOM   437  C  C     . ALA   A 1 69  ? 22.243 -18.182 11.056 1.00 55.54 ? 66  ALA   A C     1 
ATOM   438  O  O     . ALA   A 1 69  ? 21.267 -17.444 11.094 1.00 52.05 ? 66  ALA   A O     1 
ATOM   439  C  CB    . ALA   A 1 69  ? 21.858 -20.474 10.105 1.00 60.90 ? 66  ALA   A CB    1 
ATOM   440  N  N     . MET   A 1 70  ? 23.129 -18.289 12.036 1.00 54.77 ? 67  MET   A N     1 
ATOM   441  C  CA    . MET   A 1 70  ? 23.111 -17.469 13.267 1.00 53.54 ? 67  MET   A CA    1 
ATOM   442  C  C     . MET   A 1 70  ? 23.482 -16.043 12.848 1.00 49.58 ? 67  MET   A C     1 
ATOM   443  O  O     . MET   A 1 70  ? 22.737 -15.113 13.172 1.00 45.02 ? 67  MET   A O     1 
ATOM   444  C  CB    . MET   A 1 70  ? 24.139 -18.006 14.263 1.00 57.63 ? 67  MET   A CB    1 
ATOM   445  C  CG    . MET   A 1 70  ? 24.202 -17.223 15.539 1.00 60.03 ? 67  MET   A CG    1 
ATOM   446  S  SD    . MET   A 1 70  ? 22.642 -17.247 16.416 1.00 67.86 ? 67  MET   A SD    1 
ATOM   447  C  CE    . MET   A 1 70  ? 22.539 -18.970 16.882 1.00 66.16 ? 67  MET   A CE    1 
ATOM   448  N  N     . ARG   A 1 71  ? 24.570 -15.921 12.089 1.00 48.02 ? 68  ARG   A N     1 
ATOM   449  C  CA    . ARG   A 1 71  ? 25.058 -14.656 11.566 1.00 44.58 ? 68  ARG   A CA    1 
ATOM   450  C  C     . ARG   A 1 71  ? 23.939 -13.948 10.816 1.00 40.39 ? 68  ARG   A C     1 
ATOM   451  O  O     . ARG   A 1 71  ? 23.695 -12.778 11.071 1.00 36.71 ? 68  ARG   A O     1 
ATOM   452  C  CB    . ARG   A 1 71  ? 26.262 -14.885 10.650 1.00 46.56 ? 68  ARG   A CB    1 
ATOM   453  C  CG    . ARG   A 1 71  ? 27.086 -13.636 10.388 1.00 46.09 ? 68  ARG   A CG    1 
ATOM   454  C  CD    . ARG   A 1 71  ? 28.074 -13.909 9.270  1.00 49.83 ? 68  ARG   A CD    1 
ATOM   455  N  NE    . ARG   A 1 71  ? 27.391 -14.498 8.122  1.00 56.27 ? 68  ARG   A NE    1 
ATOM   456  C  CZ    . ARG   A 1 71  ? 27.997 -15.096 7.103  1.00 59.12 ? 68  ARG   A CZ    1 
ATOM   457  N  NH1   . ARG   A 1 71  ? 27.276 -15.629 6.131  1.00 63.05 ? 68  ARG   A NH1   1 
ATOM   458  N  NH2   . ARG   A 1 71  ? 29.316 -15.175 7.069  1.00 60.20 ? 68  ARG   A NH2   1 
ATOM   459  N  N     . ASP   A 1 72  ? 23.269 -14.681 9.915  1.00 43.58 ? 69  ASP   A N     1 
ATOM   460  C  CA    . ASP   A 1 72  ? 22.207 -14.150 9.075  1.00 42.94 ? 69  ASP   A CA    1 
ATOM   461  C  C     . ASP   A 1 72  ? 21.023 -13.694 9.917  1.00 42.19 ? 69  ASP   A C     1 
ATOM   462  O  O     . ASP   A 1 72  ? 20.375 -12.714 9.549  1.00 37.76 ? 69  ASP   A O     1 
ATOM   463  C  CB    . ASP   A 1 72  ? 21.825 -15.102 7.938  1.00 45.84 ? 69  ASP   A CB    1 
ATOM   464  C  CG    . ASP   A 1 72  ? 22.842 -15.102 6.807  1.00 46.55 ? 69  ASP   A CG    1 
ATOM   465  O  OD1   . ASP   A 1 72  ? 23.938 -14.491 6.974  1.00 45.13 ? 69  ASP   A OD1   1 
ATOM   466  O  OD2   . ASP   A 1 72  ? 22.530 -15.698 5.757  1.00 50.41 ? 69  ASP   A OD2   1 
ATOM   467  N  N     . GLN   A 1 73  ? 20.766 -14.379 11.028 1.00 42.88 ? 70  GLN   A N     1 
ATOM   468  C  CA    . GLN   A 1 73  ? 19.631 -14.044 11.918 1.00 43.23 ? 70  GLN   A CA    1 
ATOM   469  C  C     . GLN   A 1 73  ? 19.863 -12.688 12.576 1.00 39.84 ? 70  GLN   A C     1 
ATOM   470  O  O     . GLN   A 1 73  ? 18.956 -11.900 12.576 1.00 38.82 ? 70  GLN   A O     1 
ATOM   471  C  CB    . GLN   A 1 73  ? 19.405 -15.112 12.986 1.00 45.14 ? 70  GLN   A CB    1 
ATOM   472  C  CG    . GLN   A 1 73  ? 18.178 -14.847 13.839 1.00 46.94 ? 70  GLN   A CG    1 
ATOM   473  C  CD    . GLN   A 1 73  ? 16.936 -14.648 13.008 1.00 48.63 ? 70  GLN   A CD    1 
ATOM   474  O  OE1   . GLN   A 1 73  ? 16.647 -15.403 12.104 1.00 50.12 ? 70  GLN   A OE1   1 
ATOM   475  N  NE2   . GLN   A 1 73  ? 16.210 -13.591 13.283 1.00 47.17 ? 70  GLN   A NE2   1 
ATOM   476  N  N     . TYR   A 1 74  ? 21.035 -12.473 13.163 1.00 37.94 ? 71  TYR   A N     1 
ATOM   477  C  CA    . TYR   A 1 74  ? 21.294 -11.155 13.779 1.00 36.48 ? 71  TYR   A CA    1 
ATOM   478  C  C     . TYR   A 1 74  ? 21.338 -10.071 12.709 1.00 36.14 ? 71  TYR   A C     1 
ATOM   479  O  O     . TYR   A 1 74  ? 20.905 -8.980  12.986 1.00 36.72 ? 71  TYR   A O     1 
ATOM   480  C  CB    . TYR   A 1 74  ? 22.380 -11.184 14.847 1.00 36.26 ? 71  TYR   A CB    1 
ATOM   481  C  CG    . TYR   A 1 74  ? 23.796 -11.414 14.406 1.00 35.17 ? 71  TYR   A CG    1 
ATOM   482  C  CD1   . TYR   A 1 74  ? 24.442 -10.538 13.560 1.00 35.60 ? 71  TYR   A CD1   1 
ATOM   483  C  CD2   . TYR   A 1 74  ? 24.534 -12.445 14.951 1.00 37.06 ? 71  TYR   A CD2   1 
ATOM   484  C  CE1   . TYR   A 1 74  ? 25.770 -10.720 13.224 1.00 35.11 ? 71  TYR   A CE1   1 
ATOM   485  C  CE2   . TYR   A 1 74  ? 25.855 -12.653 14.618 1.00 37.74 ? 71  TYR   A CE2   1 
ATOM   486  C  CZ    . TYR   A 1 74  ? 26.477 -11.783 13.751 1.00 37.16 ? 71  TYR   A CZ    1 
ATOM   487  O  OH    . TYR   A 1 74  ? 27.776 -11.990 13.440 1.00 36.21 ? 71  TYR   A OH    1 
ATOM   488  N  N     . MET   A 1 75  ? 21.882 -10.374 11.541 1.00 33.74 ? 72  MET   A N     1 
ATOM   489  C  CA    . MET   A 1 75  ? 21.881 -9.341  10.489 1.00 34.78 ? 72  MET   A CA    1 
ATOM   490  C  C     . MET   A 1 75  ? 20.449 -9.062  10.019 1.00 36.85 ? 72  MET   A C     1 
ATOM   491  O  O     . MET   A 1 75  ? 20.176 -7.958  9.617  1.00 36.89 ? 72  MET   A O     1 
ATOM   492  C  CB    . MET   A 1 75  ? 22.817 -9.716  9.345  1.00 34.53 ? 72  MET   A CB    1 
ATOM   493  C  CG    . MET   A 1 75  ? 24.211 -9.937  9.854  1.00 33.56 ? 72  MET   A CG    1 
ATOM   494  S  SD    . MET   A 1 75  ? 25.381 -10.182 8.547  1.00 32.80 ? 72  MET   A SD    1 
ATOM   495  C  CE    . MET   A 1 75  ? 26.928 -9.839  9.371  1.00 32.96 ? 72  MET   A CE    1 
ATOM   496  N  N     . ARG   A 1 76  ? 19.557 -10.043 10.096 1.00 37.84 ? 73  ARG   A N     1 
ATOM   497  C  CA    . ARG   A 1 76  ? 18.158 -9.774  9.693  1.00 40.87 ? 73  ARG   A CA    1 
ATOM   498  C  C     . ARG   A 1 76  ? 17.438 -9.028  10.818 1.00 40.58 ? 73  ARG   A C     1 
ATOM   499  O  O     . ARG   A 1 76  ? 16.729 -8.093  10.520 1.00 42.90 ? 73  ARG   A O     1 
ATOM   500  C  CB    . ARG   A 1 76  ? 17.441 -11.066 9.309  1.00 43.56 ? 73  ARG   A CB    1 
ATOM   501  C  CG    . ARG   A 1 76  ? 16.040 -10.813 8.773  0.00 59.10 ? 73  ARG   A CG    1 
ATOM   502  C  CD    . ARG   A 1 76  ? 15.211 -12.012 8.402  0.00 61.71 ? 73  ARG   A CD    1 
ATOM   503  N  NE    . ARG   A 1 76  ? 15.960 -12.566 7.292  0.00 61.93 ? 73  ARG   A NE    1 
ATOM   504  C  CZ    . ARG   A 1 76  ? 15.849 -12.159 6.051  0.00 62.23 ? 73  ARG   A CZ    1 
ATOM   505  N  NH1   . ARG   A 1 76  ? 16.560 -12.751 5.113  0.00 62.68 ? 73  ARG   A NH1   1 
ATOM   506  N  NH2   . ARG   A 1 76  ? 15.020 -11.176 5.751  0.00 62.34 ? 73  ARG   A NH2   1 
ATOM   507  N  N     . THR   A 1 77  ? 17.656 -9.438  12.061 1.00 41.52 ? 74  THR   A N     1 
ATOM   508  C  CA    . THR   A 1 77  ? 17.068 -8.809  13.265 1.00 38.86 ? 74  THR   A CA    1 
ATOM   509  C  C     . THR   A 1 77  ? 17.634 -7.408  13.531 1.00 36.62 ? 74  THR   A C     1 
ATOM   510  O  O     . THR   A 1 77  ? 16.911 -6.566  14.006 1.00 33.96 ? 74  THR   A O     1 
ATOM   511  C  CB    . THR   A 1 77  ? 17.191 -9.755  14.454 1.00 39.83 ? 74  THR   A CB    1 
ATOM   512  O  OG1   . THR   A 1 77  ? 16.274 -10.773 14.099 1.00 41.89 ? 74  THR   A OG1   1 
ATOM   513  C  CG2   . THR   A 1 77  ? 16.768 -9.129  15.755 1.00 41.72 ? 74  THR   A CG2   1 
ATOM   514  N  N     . GLY   A 1 78  ? 18.923 -7.212  13.305 1.00 31.07 ? 75  GLY   A N     1 
ATOM   515  C  CA    . GLY   A 1 78  ? 19.532 -5.913  13.602 1.00 29.94 ? 75  GLY   A CA    1 
ATOM   516  C  C     . GLY   A 1 78  ? 18.926 -4.785  12.807 1.00 30.52 ? 75  GLY   A C     1 
ATOM   517  O  O     . GLY   A 1 78  ? 18.749 -4.927  11.625 1.00 30.25 ? 75  GLY   A O     1 
ATOM   518  N  N     . GLU   A 1 79  ? 18.689 -3.673  13.479 1.00 29.39 ? 76  GLU   A N     1 
ATOM   519  C  CA    . GLU   A 1 79  ? 18.139 -2.454  12.859 1.00 30.99 ? 76  GLU   A CA    1 
ATOM   520  C  C     . GLU   A 1 79  ? 19.264 -1.500  12.465 1.00 29.97 ? 76  GLU   A C     1 
ATOM   521  O  O     . GLU   A 1 79  ? 19.062 -0.761  11.532 1.00 29.91 ? 76  GLU   A O     1 
ATOM   522  C  CB    . GLU   A 1 79  ? 17.116 -1.810  13.784 1.00 31.84 ? 76  GLU   A CB    1 
ATOM   523  C  CG    . GLU   A 1 79  ? 15.868 -2.638  13.830 1.00 34.71 ? 76  GLU   A CG    1 
ATOM   524  C  CD    . GLU   A 1 79  ? 14.897 -2.380  14.952 1.00 38.76 ? 76  GLU   A CD    1 
ATOM   525  O  OE1   . GLU   A 1 79  ? 15.294 -1.878  15.972 1.00 37.00 ? 76  GLU   A OE1   1 
ATOM   526  O  OE2   . GLU   A 1 79  ? 13.741 -2.713  14.761 1.00 45.49 ? 76  GLU   A OE2   1 
ATOM   527  N  N     . GLY   A 1 80  ? 20.354 -1.507  13.218 1.00 29.74 ? 77  GLY   A N     1 
ATOM   528  C  CA    . GLY   A 1 80  ? 21.527 -0.644  12.998 1.00 29.10 ? 77  GLY   A CA    1 
ATOM   529  C  C     . GLY   A 1 80  ? 22.801 -1.391  13.327 1.00 28.16 ? 77  GLY   A C     1 
ATOM   530  O  O     . GLY   A 1 80  ? 22.773 -2.183  14.223 1.00 27.75 ? 77  GLY   A O     1 
ATOM   531  N  N     . PHE   A 1 81  ? 23.880 -1.137  12.594 1.00 25.84 ? 78  PHE   A N     1 
ATOM   532  C  CA    . PHE   A 1 81  ? 25.156 -1.864  12.817 1.00 26.07 ? 78  PHE   A CA    1 
ATOM   533  C  C     . PHE   A 1 81  ? 26.338 -0.922  13.059 1.00 25.18 ? 78  PHE   A C     1 
ATOM   534  O  O     . PHE   A 1 81  ? 26.563 -0.026  12.280 1.00 26.26 ? 78  PHE   A O     1 
ATOM   535  C  CB    . PHE   A 1 81  ? 25.442 -2.774  11.619 1.00 26.79 ? 78  PHE   A CB    1 
ATOM   536  C  CG    . PHE   A 1 81  ? 24.361 -3.789  11.374 1.00 27.12 ? 78  PHE   A CG    1 
ATOM   537  C  CD1   . PHE   A 1 81  ? 23.214 -3.449  10.694 1.00 28.23 ? 78  PHE   A CD1   1 
ATOM   538  C  CD2   . PHE   A 1 81  ? 24.477 -5.075  11.852 1.00 27.08 ? 78  PHE   A CD2   1 
ATOM   539  C  CE1   . PHE   A 1 81  ? 22.196 -4.360  10.517 1.00 28.99 ? 78  PHE   A CE1   1 
ATOM   540  C  CE2   . PHE   A 1 81  ? 23.456 -5.985  11.677 1.00 28.57 ? 78  PHE   A CE2   1 
ATOM   541  C  CZ    . PHE   A 1 81  ? 22.327 -5.628  11.003 1.00 30.15 ? 78  PHE   A CZ    1 
ATOM   542  N  N     . LEU   A 1 82  ? 27.032 -1.130  14.169 1.00 24.53 ? 79  LEU   A N     1 
ATOM   543  C  CA    . LEU   A 1 82  ? 28.307 -0.420  14.404 1.00 25.05 ? 79  LEU   A CA    1 
ATOM   544  C  C     . LEU   A 1 82  ? 29.363 -1.325  13.774 1.00 26.53 ? 79  LEU   A C     1 
ATOM   545  O  O     . LEU   A 1 82  ? 29.503 -2.429  14.228 1.00 24.90 ? 79  LEU   A O     1 
ATOM   546  C  CB    . LEU   A 1 82  ? 28.603 -0.281  15.893 1.00 27.41 ? 79  LEU   A CB    1 
ATOM   547  C  CG    . LEU   A 1 82  ? 28.091 0.950   16.628 1.00 31.93 ? 79  LEU   A CG    1 
ATOM   548  C  CD1   . LEU   A 1 82  ? 28.838 1.083   17.932 1.00 33.61 ? 79  LEU   A CD1   1 
ATOM   549  C  CD2   . LEU   A 1 82  ? 28.246 2.218   15.830 1.00 31.92 ? 79  LEU   A CD2   1 
ATOM   550  N  N     . CYS   A 1 83  ? 29.999 -0.870  12.707 1.00 26.93 ? 80  CYS   A N     1 
ATOM   551  C  CA    . CYS   A 1 83  ? 31.032 -1.681  12.028 1.00 26.41 ? 80  CYS   A CA    1 
ATOM   552  C  C     . CYS   A 1 83  ? 32.359 -1.183  12.561 1.00 24.89 ? 80  CYS   A C     1 
ATOM   553  O  O     . CYS   A 1 83  ? 32.776 -0.145  12.182 1.00 24.95 ? 80  CYS   A O     1 
ATOM   554  C  CB    . CYS   A 1 83  ? 30.915 -1.546  10.523 1.00 27.63 ? 80  CYS   A CB    1 
ATOM   555  S  SG    . CYS   A 1 83  ? 29.317 -2.141  9.938  1.00 30.76 ? 80  CYS   A SG    1 
ATOM   556  N  N     . VAL   A 1 84  ? 32.957 -1.975  13.422 1.00 25.76 ? 81  VAL   A N     1 
ATOM   557  C  CA    . VAL   A 1 84  ? 34.150 -1.506  14.146 1.00 25.19 ? 81  VAL   A CA    1 
ATOM   558  C  C     . VAL   A 1 84  ? 35.420 -2.103  13.562 1.00 26.50 ? 81  VAL   A C     1 
ATOM   559  O  O     . VAL   A 1 84  ? 35.456 -3.291  13.308 1.00 26.61 ? 81  VAL   A O     1 
ATOM   560  C  CB    . VAL   A 1 84  ? 34.043 -1.872  15.636 1.00 26.15 ? 81  VAL   A CB    1 
ATOM   561  C  CG1   . VAL   A 1 84  ? 35.162 -1.251  16.433 1.00 26.15 ? 81  VAL   A CG1   1 
ATOM   562  C  CG2   . VAL   A 1 84  ? 32.706 -1.473  16.222 1.00 26.61 ? 81  VAL   A CG2   1 
ATOM   563  N  N     . PHE   A 1 85  ? 36.377 -1.223  13.324 1.00 25.48 ? 82  PHE   A N     1 
ATOM   564  C  CA    . PHE   A 1 85  ? 37.773 -1.610  13.017 1.00 26.62 ? 82  PHE   A CA    1 
ATOM   565  C  C     . PHE   A 1 85  ? 38.658 -0.962  14.077 1.00 27.98 ? 82  PHE   A C     1 
ATOM   566  O  O     . PHE   A 1 85  ? 38.209 -0.126  14.815 1.00 29.46 ? 82  PHE   A O     1 
ATOM   567  C  CB    . PHE   A 1 85  ? 38.220 -1.235  11.603 1.00 25.29 ? 82  PHE   A CB    1 
ATOM   568  C  CG    . PHE   A 1 85  ? 38.443 0.232   11.380 1.00 26.81 ? 82  PHE   A CG    1 
ATOM   569  C  CD1   . PHE   A 1 85  ? 37.395 1.050   11.018 1.00 25.81 ? 82  PHE   A CD1   1 
ATOM   570  C  CD2   . PHE   A 1 85  ? 39.703 0.784   11.494 1.00 28.50 ? 82  PHE   A CD2   1 
ATOM   571  C  CE1   . PHE   A 1 85  ? 37.586 2.401   10.824 1.00 26.74 ? 82  PHE   A CE1   1 
ATOM   572  C  CE2   . PHE   A 1 85  ? 39.893 2.136   11.297 1.00 28.93 ? 82  PHE   A CE2   1 
ATOM   573  C  CZ    . PHE   A 1 85  ? 38.837 2.938   10.953 1.00 29.04 ? 82  PHE   A CZ    1 
ATOM   574  N  N     . ALA   A 1 86  ? 39.895 -1.424  14.174 1.00 28.67 ? 83  ALA   A N     1 
ATOM   575  C  CA    . ALA   A 1 86  ? 40.881 -0.828  15.079 1.00 29.14 ? 83  ALA   A CA    1 
ATOM   576  C  C     . ALA   A 1 86  ? 41.899 -0.076  14.236 1.00 29.78 ? 83  ALA   A C     1 
ATOM   577  O  O     . ALA   A 1 86  ? 42.296 -0.568  13.183 1.00 29.48 ? 83  ALA   A O     1 
ATOM   578  C  CB    . ALA   A 1 86  ? 41.553 -1.887  15.931 1.00 30.80 ? 83  ALA   A CB    1 
ATOM   579  N  N     . ILE   A 1 87  ? 42.294 1.118   14.695 1.00 31.56 ? 84  ILE   A N     1 
ATOM   580  C  CA    . ILE   A 1 87  ? 43.069 2.046   13.882 1.00 32.95 ? 84  ILE   A CA    1 
ATOM   581  C  C     . ILE   A 1 87  ? 44.504 1.530   13.731 1.00 34.89 ? 84  ILE   A C     1 
ATOM   582  O  O     . ILE   A 1 87  ? 45.266 2.055   12.926 1.00 36.56 ? 84  ILE   A O     1 
ATOM   583  C  CB    . ILE   A 1 87  ? 43.017 3.480   14.444 1.00 33.24 ? 84  ILE   A CB    1 
ATOM   584  C  CG1   . ILE   A 1 87  ? 43.632 3.549   15.853 1.00 37.00 ? 84  ILE   A CG1   1 
ATOM   585  C  CG2   . ILE   A 1 87  ? 41.593 4.049   14.394 1.00 33.55 ? 84  ILE   A CG2   1 
ATOM   586  C  CD1   . ILE   A 1 87  ? 44.305 4.879   16.205 1.00 39.86 ? 84  ILE   A CD1   1 
ATOM   587  N  N     . ASN   A 1 88  ? 44.845 0.499   14.491 1.00 33.91 ? 85  ASN   A N     1 
ATOM   588  C  CA    . ASN   A 1 88  ? 46.188 -0.117  14.459 1.00 35.74 ? 85  ASN   A CA    1 
ATOM   589  C  C     . ASN   A 1 88  ? 46.111 -1.474  13.762 1.00 35.15 ? 85  ASN   A C     1 
ATOM   590  O  O     . ASN   A 1 88  ? 47.053 -2.233  13.874 1.00 37.80 ? 85  ASN   A O     1 
ATOM   591  C  CB    . ASN   A 1 88  ? 46.756 -0.274  15.867 1.00 37.26 ? 85  ASN   A CB    1 
ATOM   592  C  CG    . ASN   A 1 88  ? 46.009 -1.267  16.724 1.00 38.09 ? 85  ASN   A CG    1 
ATOM   593  O  OD1   . ASN   A 1 88  ? 44.806 -1.420  16.595 1.00 36.65 ? 85  ASN   A OD1   1 
ATOM   594  N  ND2   . ASN   A 1 88  ? 46.723 -1.962  17.584 1.00 38.17 ? 85  ASN   A ND2   1 
ATOM   595  N  N     . ASN   A 1 89  ? 45.000 -1.784  13.109 1.00 33.60 ? 86  ASN   A N     1 
ATOM   596  C  CA    . ASN   A 1 89  ? 44.897 -3.098  12.431 1.00 33.55 ? 86  ASN   A CA    1 
ATOM   597  C  C     . ASN   A 1 89  ? 44.309 -2.872  11.043 1.00 33.03 ? 86  ASN   A C     1 
ATOM   598  O  O     . ASN   A 1 89  ? 43.118 -2.690  10.936 1.00 31.04 ? 86  ASN   A O     1 
ATOM   599  C  CB    . ASN   A 1 89  ? 44.163 -4.096  13.320 1.00 33.54 ? 86  ASN   A CB    1 
ATOM   600  C  CG    . ASN   A 1 89  ? 43.791 -5.408  12.675 1.00 33.89 ? 86  ASN   A CG    1 
ATOM   601  O  OD1   . ASN   A 1 89  ? 43.957 -5.613  11.495 1.00 35.67 ? 86  ASN   A OD1   1 
ATOM   602  N  ND2   . ASN   A 1 89  ? 43.226 -6.294  13.461 1.00 36.55 ? 86  ASN   A ND2   1 
ATOM   603  N  N     . THR   A 1 90  ? 45.148 -2.933  10.020 1.00 33.96 ? 87  THR   A N     1 
ATOM   604  C  CA    . THR   A 1 90  ? 44.695 -2.651  8.643  1.00 33.87 ? 87  THR   A CA    1 
ATOM   605  C  C     . THR   A 1 90  ? 43.760 -3.758  8.174  1.00 32.83 ? 87  THR   A C     1 
ATOM   606  O  O     . THR   A 1 90  ? 42.822 -3.439  7.474  1.00 32.07 ? 87  THR   A O     1 
ATOM   607  C  CB    . THR   A 1 90  ? 45.884 -2.447  7.702  1.00 36.80 ? 87  THR   A CB    1 
ATOM   608  O  OG1   . THR   A 1 90  ? 46.709 -3.583  7.887  1.00 41.75 ? 87  THR   A OG1   1 
ATOM   609  C  CG2   . THR   A 1 90  ? 46.675 -1.210  8.034  1.00 36.61 ? 87  THR   A CG2   1 
ATOM   610  N  N     . LYS   A 1 91  ? 44.013 -4.992  8.586  1.00 34.11 ? 88  LYS   A N     1 
ATOM   611  C  CA    . LYS   A 1 91  ? 43.140 -6.061  8.114  1.00 35.10 ? 88  LYS   A CA    1 
ATOM   612  C  C     . LYS   A 1 91  ? 41.709 -5.828  8.607  1.00 31.99 ? 88  LYS   A C     1 
ATOM   613  O  O     . LYS   A 1 91  ? 40.746 -6.140  7.911  1.00 29.89 ? 88  LYS   A O     1 
ATOM   614  C  CB    . LYS   A 1 91  ? 43.605 -7.447  8.568  1.00 37.98 ? 88  LYS   A CB    1 
ATOM   615  C  CG    . LYS   A 1 91  ? 42.754 -8.593  8.034  1.00 41.08 ? 88  LYS   A CG    1 
ATOM   616  C  CD    . LYS   A 1 91  ? 43.122 -9.957  8.591  1.00 43.38 ? 88  LYS   A CD    1 
ATOM   617  C  CE    . LYS   A 1 91  ? 42.345 -11.098 7.955  1.00 45.34 ? 88  LYS   A CE    1 
ATOM   618  N  NZ    . LYS   A 1 91  ? 40.946 -11.173 8.448  1.00 46.31 ? 88  LYS   A NZ    1 
ATOM   619  N  N     . SER   A 1 92  ? 41.582 -5.354  9.850  1.00 29.10 ? 89  SER   A N     1 
ATOM   620  C  CA    . SER   A 1 92  ? 40.249 -5.151  10.401 1.00 27.96 ? 89  SER   A CA    1 
ATOM   621  C  C     . SER   A 1 92  ? 39.515 -4.079  9.601  1.00 27.14 ? 89  SER   A C     1 
ATOM   622  O  O     . SER   A 1 92  ? 38.287 -4.131  9.423  1.00 25.04 ? 89  SER   A O     1 
ATOM   623  C  CB    . SER   A 1 92  ? 40.308 -4.859  11.904 1.00 27.16 ? 89  SER   A CB    1 
ATOM   624  O  OG    . SER   A 1 92  ? 40.714 -3.515  12.157 1.00 27.77 ? 89  SER   A OG    1 
ATOM   625  N  N     . PHE   A 1 93  ? 40.277 -3.087  9.125  1.00 27.74 ? 90  PHE   A N     1 
ATOM   626  C  CA    . PHE   A 1 93  ? 39.712 -1.994  8.344  1.00 26.17 ? 90  PHE   A CA    1 
ATOM   627  C  C     . PHE   A 1 93  ? 39.271 -2.509  6.970  1.00 27.79 ? 90  PHE   A C     1 
ATOM   628  O  O     . PHE   A 1 93  ? 38.162 -2.225  6.525  1.00 27.49 ? 90  PHE   A O     1 
ATOM   629  C  CB    . PHE   A 1 93  ? 40.710 -0.829  8.271  1.00 27.51 ? 90  PHE   A CB    1 
ATOM   630  C  CG    . PHE   A 1 93  ? 40.283 0.264   7.325  1.00 27.93 ? 90  PHE   A CG    1 
ATOM   631  C  CD1   . PHE   A 1 93  ? 39.217 1.085   7.653  1.00 26.19 ? 90  PHE   A CD1   1 
ATOM   632  C  CD2   . PHE   A 1 93  ? 40.933 0.469   6.112  1.00 28.97 ? 90  PHE   A CD2   1 
ATOM   633  C  CE1   . PHE   A 1 93  ? 38.789 2.084   6.798  1.00 26.46 ? 90  PHE   A CE1   1 
ATOM   634  C  CE2   . PHE   A 1 93  ? 40.509 1.479   5.253  1.00 30.52 ? 90  PHE   A CE2   1 
ATOM   635  C  CZ    . PHE   A 1 93  ? 39.422 2.265   5.588  1.00 28.66 ? 90  PHE   A CZ    1 
ATOM   636  N  N     . GLU   A 1 94  ? 40.134 -3.311  6.322  1.00 29.55 ? 91  GLU   A N     1 
ATOM   637  C  CA    . GLU   A 1 94  ? 39.826 -3.914  5.031  1.00 31.11 ? 91  GLU   A CA    1 
ATOM   638  C  C     . GLU   A 1 94  ? 38.596 -4.825  5.120  1.00 29.70 ? 91  GLU   A C     1 
ATOM   639  O  O     . GLU   A 1 94  ? 37.799 -4.860  4.174  1.00 28.79 ? 91  GLU   A O     1 
ATOM   640  C  CB    . GLU   A 1 94  ? 41.039 -4.669  4.467  1.00 32.44 ? 91  GLU   A CB    1 
ATOM   641  C  CG    . GLU   A 1 94  ? 42.088 -3.720  3.882  1.00 37.09 ? 91  GLU   A CG    1 
ATOM   642  C  CD    . GLU   A 1 94  ? 41.605 -2.816  2.749  1.00 39.10 ? 91  GLU   A CD    1 
ATOM   643  O  OE1   . GLU   A 1 94  ? 41.023 -3.325  1.772  1.00 44.84 ? 91  GLU   A OE1   1 
ATOM   644  O  OE2   . GLU   A 1 94  ? 41.822 -1.616  2.838  1.00 45.30 ? 91  GLU   A OE2   1 
ATOM   645  N  N     . ASP   A 1 95  ? 38.445 -5.536  6.249  1.00 29.32 ? 92  ASP   A N     1 
ATOM   646  C  CA    . ASP   A 1 95  ? 37.366 -6.499  6.395  1.00 29.91 ? 92  ASP   A CA    1 
ATOM   647  C  C     . ASP   A 1 95  ? 36.023 -5.786  6.563  1.00 26.56 ? 92  ASP   A C     1 
ATOM   648  O  O     . ASP   A 1 95  ? 34.992 -6.429  6.514  1.00 27.06 ? 92  ASP   A O     1 
ATOM   649  C  CB    . ASP   A 1 95  ? 37.581 -7.488  7.540  1.00 32.64 ? 92  ASP   A CB    1 
ATOM   650  C  CG    . ASP   A 1 95  ? 38.656 -8.523  7.254  1.00 35.06 ? 92  ASP   A CG    1 
ATOM   651  O  OD1   . ASP   A 1 95  ? 39.031 -8.671  6.079  1.00 38.36 ? 92  ASP   A OD1   1 
ATOM   652  O  OD2   . ASP   A 1 95  ? 39.120 -9.152  8.216  1.00 40.90 ? 92  ASP   A OD2   1 
ATOM   653  N  N     . ILE   A 1 96  ? 36.028 -4.471  6.753  1.00 25.34 ? 93  ILE   A N     1 
ATOM   654  C  CA    . ILE   A 1 96  ? 34.746 -3.763  6.848  1.00 25.93 ? 93  ILE   A CA    1 
ATOM   655  C  C     . ILE   A 1 96  ? 33.893 -3.985  5.594  1.00 25.64 ? 93  ILE   A C     1 
ATOM   656  O  O     . ILE   A 1 96  ? 32.659 -4.053  5.651  1.00 24.96 ? 93  ILE   A O     1 
ATOM   657  C  CB    . ILE   A 1 96  ? 34.946 -2.256  7.138  1.00 25.79 ? 93  ILE   A CB    1 
ATOM   658  C  CG1   . ILE   A 1 96  ? 35.597 -2.050  8.503  1.00 27.33 ? 93  ILE   A CG1   1 
ATOM   659  C  CG2   . ILE   A 1 96  ? 33.623 -1.494  7.035  1.00 25.88 ? 93  ILE   A CG2   1 
ATOM   660  C  CD1   . ILE   A 1 96  ? 34.702 -2.365  9.671  1.00 27.16 ? 93  ILE   A CD1   1 
ATOM   661  N  N     . HIS   A 1 97  ? 34.559 -4.062  4.436  1.00 26.52 ? 94  HIS   A N     1 
ATOM   662  C  CA    . HIS   A 1 97  ? 33.931 -4.439  3.184  1.00 26.05 ? 94  HIS   A CA    1 
ATOM   663  C  C     . HIS   A 1 97  ? 33.070 -5.687  3.377  1.00 28.54 ? 94  HIS   A C     1 
ATOM   664  O  O     . HIS   A 1 97  ? 31.902 -5.721  2.977  1.00 27.87 ? 94  HIS   A O     1 
ATOM   665  C  CB    . HIS   A 1 97  ? 35.025 -4.688  2.127  1.00 26.61 ? 94  HIS   A CB    1 
ATOM   666  C  CG    . HIS   A 1 97  ? 34.517 -5.354  0.888  1.00 28.13 ? 94  HIS   A CG    1 
ATOM   667  N  ND1   . HIS   A 1 97  ? 34.114 -4.638  -0.229 1.00 28.06 ? 94  HIS   A ND1   1 
ATOM   668  C  CD2   . HIS   A 1 97  ? 34.316 -6.667  0.600  1.00 28.30 ? 94  HIS   A CD2   1 
ATOM   669  C  CE1   . HIS   A 1 97  ? 33.681 -5.483  -1.164 1.00 30.04 ? 94  HIS   A CE1   1 
ATOM   670  N  NE2   . HIS   A 1 97  ? 33.835 -6.732  -0.684 1.00 33.34 ? 94  HIS   A NE2   1 
ATOM   671  N  N     . HIS   A 1 98  ? 33.693 -6.706  3.993  1.00 28.78 ? 95  HIS   A N     1 
ATOM   672  C  CA    . HIS   A 1 98  ? 33.074 -8.011  4.179  1.00 30.44 ? 95  HIS   A CA    1 
ATOM   673  C  C     . HIS   A 1 98  ? 31.836 -7.927  5.068  1.00 28.31 ? 95  HIS   A C     1 
ATOM   674  O  O     . HIS   A 1 98  ? 30.796 -8.492  4.719  1.00 29.91 ? 95  HIS   A O     1 
ATOM   675  C  CB    . HIS   A 1 98  ? 34.110 -9.035  4.659  1.00 32.06 ? 95  HIS   A CB    1 
ATOM   676  C  CG    . HIS   A 1 98  ? 35.185 -9.288  3.658  1.00 34.35 ? 95  HIS   A CG    1 
ATOM   677  N  ND1   . HIS   A 1 98  ? 35.093 -10.307 2.715  1.00 39.65 ? 95  HIS   A ND1   1 
ATOM   678  C  CD2   . HIS   A 1 98  ? 36.383 -8.695  3.459  1.00 35.67 ? 95  HIS   A CD2   1 
ATOM   679  C  CE1   . HIS   A 1 98  ? 36.185 -10.315 1.978  1.00 40.84 ? 95  HIS   A CE1   1 
ATOM   680  N  NE2   . HIS   A 1 98  ? 36.983 -9.334  2.416  1.00 35.61 ? 95  HIS   A NE2   1 
ATOM   681  N  N     . TYR   A 1 99  ? 31.938 -7.264  6.218  1.00 27.88 ? 96  TYR   A N     1 
ATOM   682  C  CA    . TYR   A 1 99  ? 30.778 -7.154  7.105  1.00 29.04 ? 96  TYR   A CA    1 
ATOM   683  C  C     . TYR   A 1 99  ? 29.628 -6.430  6.399  1.00 29.27 ? 96  TYR   A C     1 
ATOM   684  O  O     . TYR   A 1 99  ? 28.476 -6.881  6.431  1.00 28.14 ? 96  TYR   A O     1 
ATOM   685  C  CB    . TYR   A 1 99  ? 31.165 -6.478  8.427  1.00 29.14 ? 96  TYR   A CB    1 
ATOM   686  C  CG    . TYR   A 1 99  ? 32.130 -7.308  9.232  1.00 30.45 ? 96  TYR   A CG    1 
ATOM   687  C  CD1   . TYR   A 1 99  ? 31.672 -8.410  9.949  1.00 32.13 ? 96  TYR   A CD1   1 
ATOM   688  C  CD2   . TYR   A 1 99  ? 33.501 -7.051  9.219  1.00 30.47 ? 96  TYR   A CD2   1 
ATOM   689  C  CE1   . TYR   A 1 99  ? 32.535 -9.205  10.687 1.00 31.86 ? 96  TYR   A CE1   1 
ATOM   690  C  CE2   . TYR   A 1 99  ? 34.382 -7.875  9.912  1.00 31.28 ? 96  TYR   A CE2   1 
ATOM   691  C  CZ    . TYR   A 1 99  ? 33.897 -8.946  10.648 1.00 32.73 ? 96  TYR   A CZ    1 
ATOM   692  O  OH    . TYR   A 1 99  ? 34.747 -9.755  11.337 1.00 34.68 ? 96  TYR   A OH    1 
ATOM   693  N  N     . ARG   A 1 100 ? 29.942 -5.287  5.802  1.00 28.25 ? 97  ARG   A N     1 
ATOM   694  C  CA    . ARG   A 1 100 ? 28.934 -4.462  5.098  1.00 29.41 ? 97  ARG   A CA    1 
ATOM   695  C  C     . ARG   A 1 100 ? 28.295 -5.273  3.974  1.00 29.71 ? 97  ARG   A C     1 
ATOM   696  O  O     . ARG   A 1 100 ? 27.101 -5.219  3.842  1.00 29.06 ? 97  ARG   A O     1 
ATOM   697  C  CB    . ARG   A 1 100 ? 29.573 -3.171  4.582  1.00 30.91 ? 97  ARG   A CB    1 
ATOM   698  C  CG    . ARG   A 1 100 ? 28.681 -2.343  3.677  1.00 33.25 ? 97  ARG   A CG    1 
ATOM   699  C  CD    . ARG   A 1 100 ? 29.263 -1.000  3.310  1.00 35.07 ? 97  ARG   A CD    1 
ATOM   700  N  NE    . ARG   A 1 100 ? 28.556 -0.385  2.215  1.00 36.85 ? 97  ARG   A NE    1 
ATOM   701  C  CZ    . ARG   A 1 100 ? 28.715 -0.673  0.929  1.00 40.56 ? 97  ARG   A CZ    1 
ATOM   702  N  NH1   . ARG   A 1 100 ? 29.580 -1.588  0.551  1.00 38.93 ? 97  ARG   A NH1   1 
ATOM   703  N  NH2   . ARG   A 1 100 ? 28.010 -0.038  0.011  1.00 45.26 ? 97  ARG   A NH2   1 
ATOM   704  N  N     . GLU   A 1 101 ? 29.088 -6.031  3.225  1.00 28.27 ? 98  GLU   A N     1 
ATOM   705  C  CA    . GLU   A 1 101 ? 28.534 -6.810  2.130  1.00 30.93 ? 98  GLU   A CA    1 
ATOM   706  C  C     . GLU   A 1 101 ? 27.554 -7.856  2.668  1.00 31.66 ? 98  GLU   A C     1 
ATOM   707  O  O     . GLU   A 1 101 ? 26.507 -8.071  2.068  1.00 31.76 ? 98  GLU   A O     1 
ATOM   708  C  CB    . GLU   A 1 101 ? 29.645 -7.520  1.355  1.00 31.91 ? 98  GLU   A CB    1 
ATOM   709  C  CG    . GLU   A 1 101 ? 29.148 -8.462  0.272  1.00 35.09 ? 98  GLU   A CG    1 
ATOM   710  C  CD    . GLU   A 1 101 ? 30.282 -9.007  -0.588 1.00 37.38 ? 98  GLU   A CD    1 
ATOM   711  O  OE1   . GLU   A 1 101 ? 31.285 -8.260  -0.756 1.00 33.16 ? 98  GLU   A OE1   1 
ATOM   712  O  OE2   . GLU   A 1 101 ? 30.189 -10.183 -1.044 1.00 41.56 ? 98  GLU   A OE2   1 
ATOM   713  N  N     . GLN   A 1 102 ? 27.923 -8.526  3.757  1.00 31.57 ? 99  GLN   A N     1 
ATOM   714  C  CA    . GLN   A 1 102 ? 27.086 -9.607  4.342  1.00 32.88 ? 99  GLN   A CA    1 
ATOM   715  C  C     . GLN   A 1 102 ? 25.778 -9.022  4.865  1.00 29.50 ? 99  GLN   A C     1 
ATOM   716  O  O     . GLN   A 1 102 ? 24.752 -9.630  4.680  1.00 29.83 ? 99  GLN   A O     1 
ATOM   717  C  CB    . GLN   A 1 102 ? 27.830 -10.297 5.481  1.00 33.49 ? 99  GLN   A CB    1 
ATOM   718  C  CG    . GLN   A 1 102 ? 28.947 -11.198 4.998  1.00 40.23 ? 99  GLN   A CG    1 
ATOM   719  C  CD    . GLN   A 1 102 ? 29.863 -11.614 6.114  1.00 41.77 ? 99  GLN   A CD    1 
ATOM   720  O  OE1   . GLN   A 1 102 ? 29.694 -11.225 7.262  1.00 42.03 ? 99  GLN   A OE1   1 
ATOM   721  N  NE2   . GLN   A 1 102 ? 30.859 -12.406 5.771  1.00 44.85 ? 99  GLN   A NE2   1 
ATOM   722  N  N     . ILE   A 1 103 ? 25.855 -7.869  5.501  1.00 28.33 ? 100 ILE   A N     1 
ATOM   723  C  CA    . ILE   A 1 103 ? 24.656 -7.209  6.022  1.00 30.64 ? 100 ILE   A CA    1 
ATOM   724  C  C     . ILE   A 1 103 ? 23.698 -6.843  4.891  1.00 32.28 ? 100 ILE   A C     1 
ATOM   725  O  O     . ILE   A 1 103 ? 22.506 -7.137  4.966  1.00 31.90 ? 100 ILE   A O     1 
ATOM   726  C  CB    . ILE   A 1 103 ? 25.018 -5.999  6.916  1.00 27.78 ? 100 ILE   A CB    1 
ATOM   727  C  CG1   . ILE   A 1 103 ? 25.677 -6.470  8.216  1.00 27.44 ? 100 ILE   A CG1   1 
ATOM   728  C  CG2   . ILE   A 1 103 ? 23.814 -5.104  7.207  1.00 28.53 ? 100 ILE   A CG2   1 
ATOM   729  C  CD1   . ILE   A 1 103 ? 26.546 -5.420  8.882  1.00 26.15 ? 100 ILE   A CD1   1 
ATOM   730  N  N     . LYS   A 1 104 ? 24.235 -6.201  3.871  1.00 33.34 ? 101 LYS   A N     1 
ATOM   731  C  CA    . LYS   A 1 104 ? 23.439 -5.761  2.710  1.00 36.49 ? 101 LYS   A CA    1 
ATOM   732  C  C     . LYS   A 1 104 ? 22.787 -6.963  2.024  1.00 36.53 ? 101 LYS   A C     1 
ATOM   733  O  O     . LYS   A 1 104 ? 21.644 -6.839  1.645  1.00 35.34 ? 101 LYS   A O     1 
ATOM   734  C  CB    . LYS   A 1 104 ? 24.316 -4.931  1.773  1.00 40.20 ? 101 LYS   A CB    1 
ATOM   735  C  CG    . LYS   A 1 104 ? 24.607 -3.520  2.257  1.00 42.79 ? 101 LYS   A CG    1 
ATOM   736  C  CD    . LYS   A 1 104 ? 25.508 -2.731  1.327  1.00 46.82 ? 101 LYS   A CD    1 
ATOM   737  C  CE    . LYS   A 1 104 ? 25.034 -2.695  -0.106 1.00 52.89 ? 101 LYS   A CE    1 
ATOM   738  N  NZ    . LYS   A 1 104 ? 25.213 -1.356  -0.710 1.00 57.49 ? 101 LYS   A NZ    1 
ATOM   739  N  N     . ARG   A 1 105 ? 23.476 -8.098  1.958  1.00 35.47 ? 102 ARG   A N     1 
ATOM   740  C  CA    . ARG   A 1 105 ? 22.950 -9.268  1.275  1.00 39.91 ? 102 ARG   A CA    1 
ATOM   741  C  C     . ARG   A 1 105 ? 21.740 -9.799  2.056  1.00 40.66 ? 102 ARG   A C     1 
ATOM   742  O  O     . ARG   A 1 105 ? 20.707 -10.092 1.470  1.00 43.37 ? 102 ARG   A O     1 
ATOM   743  C  CB    . ARG   A 1 105 ? 24.056 -10.319 1.110  1.00 41.47 ? 102 ARG   A CB    1 
ATOM   744  C  CG    . ARG   A 1 105 ? 23.666 -11.500 0.236  1.00 47.40 ? 102 ARG   A CG    1 
ATOM   745  C  CD    . ARG   A 1 105 ? 24.765 -12.533 0.073  1.00 52.88 ? 102 ARG   A CD    1 
ATOM   746  N  NE    . ARG   A 1 105 ? 25.799 -12.030 -0.824 1.00 57.12 ? 102 ARG   A NE    1 
ATOM   747  C  CZ    . ARG   A 1 105 ? 27.054 -11.756 -0.476 1.00 56.85 ? 102 ARG   A CZ    1 
ATOM   748  N  NH1   . ARG   A 1 105 ? 27.892 -11.282 -1.381 1.00 57.26 ? 102 ARG   A NH1   1 
ATOM   749  N  NH2   . ARG   A 1 105 ? 27.468 -11.963 0.760  1.00 56.36 ? 102 ARG   A NH2   1 
ATOM   750  N  N     . VAL   A 1 106 ? 21.901 -9.929  3.379  1.00 41.25 ? 103 VAL   A N     1 
ATOM   751  C  CA    . VAL   A 1 106 ? 20.894 -10.400 4.324  1.00 42.79 ? 103 VAL   A CA    1 
ATOM   752  C  C     . VAL   A 1 106 ? 19.675 -9.479  4.300  1.00 42.23 ? 103 VAL   A C     1 
ATOM   753  O  O     . VAL   A 1 106 ? 18.546 -9.950  4.248  1.00 42.88 ? 103 VAL   A O     1 
ATOM   754  C  CB    . VAL   A 1 106 ? 21.499 -10.502 5.744  1.00 41.41 ? 103 VAL   A CB    1 
ATOM   755  C  CG1   . VAL   A 1 106 ? 20.448 -10.727 6.829  1.00 44.29 ? 103 VAL   A CG1   1 
ATOM   756  C  CG2   . VAL   A 1 106 ? 22.572 -11.583 5.804  1.00 42.06 ? 103 VAL   A CG2   1 
ATOM   757  N  N     . LYS   A 1 107 ? 19.902 -8.164  4.371  1.00 41.46 ? 104 LYS   A N     1 
ATOM   758  C  CA    . LYS   A 1 107 ? 18.802 -7.223  4.502  1.00 44.99 ? 104 LYS   A CA    1 
ATOM   759  C  C     . LYS   A 1 107 ? 18.289 -6.816  3.120  1.00 48.30 ? 104 LYS   A C     1 
ATOM   760  O  O     . LYS   A 1 107 ? 17.407 -5.964  3.008  1.00 49.88 ? 104 LYS   A O     1 
ATOM   761  C  CB    . LYS   A 1 107 ? 19.218 -6.054  5.405  1.00 43.65 ? 104 LYS   A CB    1 
ATOM   762  C  CG    . LYS   A 1 107 ? 19.531 -6.468  6.838  1.00 44.19 ? 104 LYS   A CG    1 
ATOM   763  C  CD    . LYS   A 1 107 ? 19.765 -5.329  7.809  1.00 42.17 ? 104 LYS   A CD    1 
ATOM   764  C  CE    . LYS   A 1 107 ? 18.484 -4.863  8.455  1.00 41.50 ? 104 LYS   A CE    1 
ATOM   765  N  NZ    . LYS   A 1 107 ? 17.918 -5.979  9.251  1.00 43.47 ? 104 LYS   A NZ    1 
ATOM   766  N  N     . ASP   A 1 108 ? 18.854 -7.413  2.062  1.00 51.97 ? 105 ASP   A N     1 
ATOM   767  C  CA    . ASP   A 1 108 ? 18.514 -7.126  0.634  1.00 55.22 ? 105 ASP   A CA    1 
ATOM   768  C  C     . ASP   A 1 108 ? 18.305 -5.628  0.402  1.00 57.68 ? 105 ASP   A C     1 
ATOM   769  O  O     . ASP   A 1 108 ? 17.244 -5.263  -0.112 1.00 59.42 ? 105 ASP   A O     1 
ATOM   770  C  CB    . ASP   A 1 108 ? 17.284 -7.890  0.143  1.00 59.06 ? 105 ASP   A CB    1 
ATOM   771  C  CG    . ASP   A 1 108 ? 17.010 -7.669  -1.339 1.00 62.69 ? 105 ASP   A CG    1 
ATOM   772  O  OD1   . ASP   A 1 108 ? 17.764 -6.927  -1.967 1.00 63.39 ? 105 ASP   A OD1   1 
ATOM   773  O  OD2   . ASP   A 1 108 ? 16.038 -8.237  -1.851 1.00 66.15 ? 105 ASP   A OD2   1 
ATOM   774  N  N     . SER   A 1 109 ? 19.228 -4.806  0.891  1.00 54.92 ? 106 SER   A N     1 
ATOM   775  C  CA    . SER   A 1 109 ? 19.074 -3.346  0.742  1.00 56.86 ? 106 SER   A CA    1 
ATOM   776  C  C     . SER   A 1 109 ? 20.438 -2.674  0.800  1.00 56.80 ? 106 SER   A C     1 
ATOM   777  O  O     . SER   A 1 109 ? 21.224 -3.013  1.666  1.00 52.13 ? 106 SER   A O     1 
ATOM   778  C  CB    . SER   A 1 109 ? 18.192 -2.817  1.816  1.00 56.86 ? 106 SER   A CB    1 
ATOM   779  O  OG    . SER   A 1 109 ? 17.999 -1.435  1.651  1.00 57.23 ? 106 SER   A OG    1 
ATOM   780  N  N     . GLU   A 1 110 ? 20.642 -1.719  -0.105 1.00 59.22 ? 107 GLU   A N     1 
ATOM   781  C  CA    . GLU   A 1 110 ? 21.863 -0.884  -0.194 1.00 60.30 ? 107 GLU   A CA    1 
ATOM   782  C  C     . GLU   A 1 110 ? 21.923 0.069   1.004  1.00 59.14 ? 107 GLU   A C     1 
ATOM   783  O  O     . GLU   A 1 110 ? 23.034 0.496   1.369  1.00 60.44 ? 107 GLU   A O     1 
ATOM   784  C  CB    . GLU   A 1 110 ? 21.883 -0.134  -1.530 1.00 61.52 ? 107 GLU   A CB    1 
ATOM   785  C  CG    . GLU   A 1 110 ? 22.003 -1.052  -2.733 0.00 56.91 ? 107 GLU   A CG    1 
ATOM   786  C  CD    . GLU   A 1 110 ? 22.000 -0.342  -4.076 0.00 58.75 ? 107 GLU   A CD    1 
ATOM   787  O  OE1   . GLU   A 1 110 ? 21.761 0.881   -4.096 0.00 59.09 ? 107 GLU   A OE1   1 
ATOM   788  O  OE2   . GLU   A 1 110 ? 22.236 -1.016  -5.099 0.00 60.08 ? 107 GLU   A OE2   1 
ATOM   789  N  N     . ASP   A 1 111 ? 20.750 0.456   1.502  1.00 55.36 ? 108 ASP   A N     1 
ATOM   790  C  CA    . ASP   A 1 111 ? 20.583 1.403   2.624  1.00 53.56 ? 108 ASP   A CA    1 
ATOM   791  C  C     . ASP   A 1 111 ? 20.203 0.658   3.907  1.00 49.51 ? 108 ASP   A C     1 
ATOM   792  O  O     . ASP   A 1 111 ? 19.077 0.173   4.001  1.00 52.69 ? 108 ASP   A O     1 
ATOM   793  C  CB    . ASP   A 1 111 ? 19.563 2.450   2.207  1.00 59.15 ? 108 ASP   A CB    1 
ATOM   794  C  CG    . ASP   A 1 111 ? 19.200 3.466   3.265  1.00 64.38 ? 108 ASP   A CG    1 
ATOM   795  O  OD1   . ASP   A 1 111 ? 20.077 3.852   4.061  1.00 68.30 ? 108 ASP   A OD1   1 
ATOM   796  O  OD2   . ASP   A 1 111 ? 18.047 3.883   3.253  1.00 70.36 ? 108 ASP   A OD2   1 
ATOM   797  N  N     . VAL   A 1 112 ? 21.159 0.527   4.809  1.00 39.38 ? 109 VAL   A N     1 
ATOM   798  C  CA    . VAL   A 1 112 ? 20.979 -0.094  6.149  1.00 36.86 ? 109 VAL   A CA    1 
ATOM   799  C  C     . VAL   A 1 112 ? 21.652 0.867   7.120  1.00 32.96 ? 109 VAL   A C     1 
ATOM   800  O  O     . VAL   A 1 112 ? 22.771 1.227   6.850  1.00 31.95 ? 109 VAL   A O     1 
ATOM   801  C  CB    . VAL   A 1 112 ? 21.668 -1.467  6.253  1.00 35.34 ? 109 VAL   A CB    1 
ATOM   802  C  CG1   . VAL   A 1 112 ? 21.716 -1.963  7.677  1.00 35.34 ? 109 VAL   A CG1   1 
ATOM   803  C  CG2   . VAL   A 1 112 ? 21.050 -2.500  5.339  1.00 38.86 ? 109 VAL   A CG2   1 
ATOM   804  N  N     . PRO   A 1 113 ? 21.031 1.266   8.241  1.00 30.39 ? 110 PRO   A N     1 
ATOM   805  C  CA    . PRO   A 1 113 ? 21.695 2.160   9.154  1.00 29.07 ? 110 PRO   A CA    1 
ATOM   806  C  C     . PRO   A 1 113 ? 22.979 1.485   9.646  1.00 29.29 ? 110 PRO   A C     1 
ATOM   807  O  O     . PRO   A 1 113 ? 22.930 0.396   10.060 1.00 29.11 ? 110 PRO   A O     1 
ATOM   808  C  CB    . PRO   A 1 113 ? 20.678 2.307   10.290 1.00 30.00 ? 110 PRO   A CB    1 
ATOM   809  C  CG    . PRO   A 1 113 ? 19.371 2.023   9.631  1.00 31.89 ? 110 PRO   A CG    1 
ATOM   810  C  CD    . PRO   A 1 113 ? 19.680 0.934   8.636  1.00 32.73 ? 110 PRO   A CD    1 
ATOM   811  N  N     . MET   A 1 114 ? 24.080 2.207   9.524  1.00 29.20 ? 111 MET   A N     1 
ATOM   812  C  CA    . MET   A 1 114 ? 25.418 1.740   9.916  1.00 27.42 ? 111 MET   A CA    1 
ATOM   813  C  C     . MET   A 1 114 ? 26.252 2.945   10.279 1.00 26.95 ? 111 MET   A C     1 
ATOM   814  O  O     . MET   A 1 114 ? 26.047 3.985   9.714  1.00 25.92 ? 111 MET   A O     1 
ATOM   815  C  CB    . MET   A 1 114 ? 26.163 1.115   8.740  1.00 30.48 ? 111 MET   A CB    1 
ATOM   816  C  CG    . MET   A 1 114 ? 25.644 -0.186  8.315  1.00 34.25 ? 111 MET   A CG    1 
ATOM   817  S  SD    . MET   A 1 114 ? 26.864 -0.950  7.244  1.00 38.81 ? 111 MET   A SD    1 
ATOM   818  C  CE    . MET   A 1 114 ? 25.756 -2.000  6.325  1.00 40.51 ? 111 MET   A CE    1 
ATOM   819  N  N     . VAL   A 1 115 ? 27.220 2.710   11.132 1.00 25.65 ? 112 VAL   A N     1 
ATOM   820  C  CA    . VAL   A 1 115 ? 28.205 3.745   11.491 1.00 25.20 ? 112 VAL   A CA    1 
ATOM   821  C  C     . VAL   A 1 115 ? 29.559 3.042   11.449 1.00 26.72 ? 112 VAL   A C     1 
ATOM   822  O  O     . VAL   A 1 115 ? 29.658 1.937   11.932 1.00 25.97 ? 112 VAL   A O     1 
ATOM   823  C  CB    . VAL   A 1 115 ? 27.908 4.375   12.866 1.00 26.55 ? 112 VAL   A CB    1 
ATOM   824  C  CG1   . VAL   A 1 115 ? 28.988 5.347   13.263 1.00 28.44 ? 112 VAL   A CG1   1 
ATOM   825  C  CG2   . VAL   A 1 115 ? 26.572 5.082   12.885 1.00 27.82 ? 112 VAL   A CG2   1 
ATOM   826  N  N     . LEU   A 1 116 ? 30.521 3.647   10.778 1.00 26.31 ? 113 LEU   A N     1 
ATOM   827  C  CA    . LEU   A 1 116 ? 31.886 3.145   10.794 1.00 26.26 ? 113 LEU   A CA    1 
ATOM   828  C  C     . LEU   A 1 116 ? 32.603 3.660   12.037 1.00 26.34 ? 113 LEU   A C     1 
ATOM   829  O  O     . LEU   A 1 116 ? 32.672 4.863   12.242 1.00 30.80 ? 113 LEU   A O     1 
ATOM   830  C  CB    . LEU   A 1 116 ? 32.636 3.647   9.555  1.00 27.39 ? 113 LEU   A CB    1 
ATOM   831  C  CG    . LEU   A 1 116 ? 34.028 3.029   9.382  1.00 26.08 ? 113 LEU   A CG    1 
ATOM   832  C  CD1   . LEU   A 1 116 ? 33.880 1.511   9.222  1.00 26.18 ? 113 LEU   A CD1   1 
ATOM   833  C  CD2   . LEU   A 1 116 ? 34.723 3.598   8.146  1.00 26.80 ? 113 LEU   A CD2   1 
ATOM   834  N  N     . VAL   A 1 117 ? 33.158 2.744   12.834 1.00 27.21 ? 114 VAL   A N     1 
ATOM   835  C  CA    . VAL   A 1 117 ? 33.891 3.140   14.014 1.00 25.70 ? 114 VAL   A CA    1 
ATOM   836  C  C     . VAL   A 1 117 ? 35.329 2.638   13.924 1.00 26.74 ? 114 VAL   A C     1 
ATOM   837  O  O     . VAL   A 1 117 ? 35.580 1.431   13.859 1.00 26.14 ? 114 VAL   A O     1 
ATOM   838  C  CB    . VAL   A 1 117 ? 33.241 2.565   15.276 1.00 26.51 ? 114 VAL   A CB    1 
ATOM   839  C  CG1   . VAL   A 1 117 ? 34.032 2.993   16.497 1.00 27.05 ? 114 VAL   A CG1   1 
ATOM   840  C  CG2   . VAL   A 1 117 ? 31.766 2.938   15.387 1.00 25.33 ? 114 VAL   A CG2   1 
ATOM   841  N  N     . GLY   A 1 118 ? 36.251 3.580   14.072 1.00 27.27 ? 115 GLY   A N     1 
ATOM   842  C  CA    . GLY   A 1 118 ? 37.679 3.257   14.190 1.00 26.41 ? 115 GLY   A CA    1 
ATOM   843  C  C     . GLY   A 1 118 ? 38.050 3.352   15.656 1.00 27.59 ? 115 GLY   A C     1 
ATOM   844  O  O     . GLY   A 1 118 ? 38.131 4.441   16.146 1.00 28.41 ? 115 GLY   A O     1 
ATOM   845  N  N     . ASN   A 1 119 ? 38.204 2.219   16.322 1.00 26.12 ? 116 ASN   A N     1 
ATOM   846  C  CA    . ASN   A 1 119 ? 38.484 2.143   17.777 1.00 29.02 ? 116 ASN   A CA    1 
ATOM   847  C  C     . ASN   A 1 119 ? 40.001 2.171   18.030 1.00 31.92 ? 116 ASN   A C     1 
ATOM   848  O  O     . ASN   A 1 119 ? 40.726 1.935   17.098 1.00 31.70 ? 116 ASN   A O     1 
ATOM   849  C  CB    . ASN   A 1 119 ? 37.868 0.860   18.351 1.00 28.35 ? 116 ASN   A CB    1 
ATOM   850  C  CG    . ASN   A 1 119 ? 37.672 0.861   19.853 1.00 29.29 ? 116 ASN   A CG    1 
ATOM   851  O  OD1   . ASN   A 1 119 ? 37.346 1.890   20.440 1.00 29.80 ? 116 ASN   A OD1   1 
ATOM   852  N  ND2   . ASN   A 1 119 ? 37.866 -0.287  20.481 1.00 28.83 ? 116 ASN   A ND2   1 
ATOM   853  N  N     . LYS   A 1 120 ? 40.405 2.368   19.290 1.00 32.82 ? 117 LYS   A N     1 
ATOM   854  C  CA    . LYS   A 1 120 ? 41.782 2.408   19.827 1.00 33.45 ? 117 LYS   A CA    1 
ATOM   855  C  C     . LYS   A 1 120 ? 42.470 3.704   19.404 1.00 35.66 ? 117 LYS   A C     1 
ATOM   856  O  O     . LYS   A 1 120 ? 43.645 3.664   19.137 1.00 36.52 ? 117 LYS   A O     1 
ATOM   857  C  CB    . LYS   A 1 120 ? 42.555 1.110   19.576 1.00 34.43 ? 117 LYS   A CB    1 
ATOM   858  C  CG    . LYS   A 1 120 ? 41.767 -0.180  19.723 1.00 32.78 ? 117 LYS   A CG    1 
ATOM   859  C  CD    . LYS   A 1 120 ? 42.625 -1.370  19.943 1.00 34.50 ? 117 LYS   A CD    1 
ATOM   860  C  CE    . LYS   A 1 120 ? 41.895 -2.686  19.952 1.00 33.33 ? 117 LYS   A CE    1 
ATOM   861  N  NZ    . LYS   A 1 120 ? 42.819 -3.818  20.146 1.00 35.47 ? 117 LYS   A NZ    1 
ATOM   862  N  N     . SER   A 1 121 ? 41.711 4.783   19.321 1.00 35.10 ? 118 SER   A N     1 
ATOM   863  C  CA    . SER   A 1 121 ? 42.261 6.100   18.941 1.00 37.31 ? 118 SER   A CA    1 
ATOM   864  C  C     . SER   A 1 121 ? 43.332 6.605   19.928 1.00 40.09 ? 118 SER   A C     1 
ATOM   865  O  O     . SER   A 1 121 ? 44.012 7.552   19.575 1.00 40.81 ? 118 SER   A O     1 
ATOM   866  C  CB    . SER   A 1 121 ? 41.167 7.073   18.733 1.00 37.59 ? 118 SER   A CB    1 
ATOM   867  O  OG    . SER   A 1 121 ? 40.492 7.311   19.941 1.00 38.42 ? 118 SER   A OG    1 
ATOM   868  N  N     . ASP   A 1 122 ? 43.459 5.942   21.071 1.00 40.38 ? 119 ASP   A N     1 
ATOM   869  C  CA    . ASP   A 1 122 ? 44.453 6.325   22.100 1.00 43.03 ? 119 ASP   A CA    1 
ATOM   870  C  C     . ASP   A 1 122 ? 45.808 5.693   21.761 1.00 44.61 ? 119 ASP   A C     1 
ATOM   871  O  O     . ASP   A 1 122 ? 46.795 6.036   22.412 1.00 46.50 ? 119 ASP   A O     1 
ATOM   872  C  CB    . ASP   A 1 122 ? 44.014 5.803   23.467 1.00 42.42 ? 119 ASP   A CB    1 
ATOM   873  C  CG    . ASP   A 1 122 ? 43.702 4.325   23.421 1.00 40.78 ? 119 ASP   A CG    1 
ATOM   874  O  OD1   . ASP   A 1 122 ? 42.675 3.963   22.868 1.00 40.24 ? 119 ASP   A OD1   1 
ATOM   875  O  OD2   . ASP   A 1 122 ? 44.507 3.567   23.881 1.00 41.75 ? 119 ASP   A OD2   1 
ATOM   876  N  N     . LEU   A 1 123 ? 45.840 4.771   20.806 1.00 42.14 ? 120 LEU   A N     1 
ATOM   877  C  CA    . LEU   A 1 123 ? 47.104 4.056   20.525 1.00 44.67 ? 120 LEU   A CA    1 
ATOM   878  C  C     . LEU   A 1 123 ? 47.990 4.840   19.558 1.00 47.62 ? 120 LEU   A C     1 
ATOM   879  O  O     . LEU   A 1 123 ? 47.462 5.393   18.597 1.00 45.79 ? 120 LEU   A O     1 
ATOM   880  C  CB    . LEU   A 1 123 ? 46.772 2.695   19.930 1.00 43.35 ? 120 LEU   A CB    1 
ATOM   881  C  CG    . LEU   A 1 123 ? 46.300 1.625   20.899 1.00 43.05 ? 120 LEU   A CG    1 
ATOM   882  C  CD1   . LEU   A 1 123 ? 46.070 0.336   20.156 1.00 42.76 ? 120 LEU   A CD1   1 
ATOM   883  C  CD2   . LEU   A 1 123 ? 47.307 1.409   21.997 1.00 45.55 ? 120 LEU   A CD2   1 
ATOM   884  N  N     . PRO   A 1 124 ? 49.314 4.909   19.818 1.00 49.53 ? 121 PRO   A N     1 
ATOM   885  C  CA    . PRO   A 1 124 ? 50.273 5.566   18.923 1.00 50.72 ? 121 PRO   A CA    1 
ATOM   886  C  C     . PRO   A 1 124 ? 50.642 4.692   17.714 1.00 52.70 ? 121 PRO   A C     1 
ATOM   887  O  O     . PRO   A 1 124 ? 50.997 5.196   16.692 1.00 54.79 ? 121 PRO   A O     1 
ATOM   888  C  CB    . PRO   A 1 124 ? 51.468 5.764   19.853 1.00 53.81 ? 121 PRO   A CB    1 
ATOM   889  C  CG    . PRO   A 1 124 ? 51.418 4.573   20.754 1.00 53.70 ? 121 PRO   A CG    1 
ATOM   890  C  CD    . PRO   A 1 124 ? 49.943 4.370   21.008 1.00 50.73 ? 121 PRO   A CD    1 
ATOM   891  N  N     . SER   A 1 125 ? 50.436 3.380   17.808 1.00 51.26 ? 122 SER   A N     1 
ATOM   892  C  CA    . SER   A 1 125 ? 50.791 2.455   16.701 1.00 50.88 ? 122 SER   A CA    1 
ATOM   893  C  C     . SER   A 1 125 ? 49.696 2.387   15.631 1.00 46.79 ? 122 SER   A C     1 
ATOM   894  O  O     . SER   A 1 125 ? 49.355 1.277   15.267 1.00 47.60 ? 122 SER   A O     1 
ATOM   895  C  CB    . SER   A 1 125 ? 51.063 1.086   17.268 1.00 51.40 ? 122 SER   A CB    1 
ATOM   896  O  OG    . SER   A 1 125 ? 49.963 0.600   18.017 1.00 49.44 ? 122 SER   A OG    1 
ATOM   897  N  N     . ARG   A 1 126 ? 49.318 3.524   15.053 1.00 44.77 ? 123 ARG   A N     1 
ATOM   898  C  CA    . ARG   A 1 126 ? 48.209 3.688   14.090 1.00 43.51 ? 123 ARG   A CA    1 
ATOM   899  C  C     . ARG   A 1 126 ? 48.635 3.278   12.690 1.00 43.36 ? 123 ARG   A C     1 
ATOM   900  O  O     . ARG   A 1 126 ? 49.669 3.748   12.226 1.00 46.70 ? 123 ARG   A O     1 
ATOM   901  C  CB    . ARG   A 1 126 ? 47.731 5.134   14.063 1.00 43.77 ? 123 ARG   A CB    1 
ATOM   902  C  CG    . ARG   A 1 126 ? 46.707 5.388   12.975 1.00 44.15 ? 123 ARG   A CG    1 
ATOM   903  C  CD    . ARG   A 1 126 ? 46.351 6.817   12.670 1.00 45.11 ? 123 ARG   A CD    1 
ATOM   904  N  NE    . ARG   A 1 126 ? 45.557 7.432   13.710 1.00 46.41 ? 123 ARG   A NE    1 
ATOM   905  C  CZ    . ARG   A 1 126 ? 44.238 7.544   13.720 1.00 46.09 ? 123 ARG   A CZ    1 
ATOM   906  N  NH1   . ARG   A 1 126 ? 43.656 8.124   14.749 1.00 46.46 ? 123 ARG   A NH1   1 
ATOM   907  N  NH2   . ARG   A 1 126 ? 43.508 7.073   12.729 1.00 41.91 ? 123 ARG   A NH2   1 
ATOM   908  N  N     . THR   A 1 127 ? 47.818 2.452   12.050 1.00 41.07 ? 124 THR   A N     1 
ATOM   909  C  CA    . THR   A 1 127 ? 48.106 1.995   10.669 1.00 40.69 ? 124 THR   A CA    1 
ATOM   910  C  C     . THR   A 1 127 ? 47.034 2.492   9.696  1.00 41.57 ? 124 THR   A C     1 
ATOM   911  O  O     . THR   A 1 127 ? 47.269 2.425   8.505  1.00 42.74 ? 124 THR   A O     1 
ATOM   912  C  CB    . THR   A 1 127 ? 48.402 0.495   10.638 1.00 40.80 ? 124 THR   A CB    1 
ATOM   913  O  OG1   . THR   A 1 127 ? 47.240 -0.241  11.003 1.00 38.65 ? 124 THR   A OG1   1 
ATOM   914  C  CG2   . THR   A 1 127 ? 49.539 0.121   11.556 1.00 41.89 ? 124 THR   A CG2   1 
ATOM   915  N  N     . VAL   A 1 128 ? 45.918 3.002   10.208 1.00 38.12 ? 125 VAL   A N     1 
ATOM   916  C  CA    . VAL   A 1 128 ? 44.813 3.510   9.357  1.00 37.22 ? 125 VAL   A CA    1 
ATOM   917  C  C     . VAL   A 1 128 ? 44.596 4.995   9.626  1.00 39.55 ? 125 VAL   A C     1 
ATOM   918  O  O     . VAL   A 1 128 ? 44.207 5.338   10.727 1.00 38.77 ? 125 VAL   A O     1 
ATOM   919  C  CB    . VAL   A 1 128 ? 43.513 2.719   9.585  1.00 36.76 ? 125 VAL   A CB    1 
ATOM   920  C  CG1   . VAL   A 1 128 ? 42.419 3.171   8.643  1.00 37.14 ? 125 VAL   A CG1   1 
ATOM   921  C  CG2   . VAL   A 1 128 ? 43.727 1.226   9.495  1.00 37.36 ? 125 VAL   A CG2   1 
ATOM   922  N  N     . ASP   A 1 129 ? 44.830 5.820   8.614  1.00 40.35 ? 126 ASP   A N     1 
ATOM   923  C  CA    . ASP   A 1 129 ? 44.678 7.262   8.676  1.00 43.00 ? 126 ASP   A CA    1 
ATOM   924  C  C     . ASP   A 1 129 ? 43.202 7.630   8.733  1.00 41.38 ? 126 ASP   A C     1 
ATOM   925  O  O     . ASP   A 1 129 ? 42.395 7.069   7.994  1.00 38.53 ? 126 ASP   A O     1 
ATOM   926  C  CB    . ASP   A 1 129 ? 45.234 7.941   7.420  1.00 49.64 ? 126 ASP   A CB    1 
ATOM   927  C  CG    . ASP   A 1 129 ? 46.744 7.915   7.352  1.00 54.54 ? 126 ASP   A CG    1 
ATOM   928  O  OD1   . ASP   A 1 129 ? 47.374 7.858   8.424  1.00 60.37 ? 126 ASP   A OD1   1 
ATOM   929  O  OD2   . ASP   A 1 129 ? 47.279 7.947   6.228  1.00 60.62 ? 126 ASP   A OD2   1 
ATOM   930  N  N     . THR   A 1 130 ? 42.882 8.625   9.576  1.00 39.05 ? 127 THR   A N     1 
ATOM   931  C  CA    . THR   A 1 130 ? 41.529 9.134   9.717  1.00 38.56 ? 127 THR   A CA    1 
ATOM   932  C  C     . THR   A 1 130 ? 40.949 9.440   8.333  1.00 39.13 ? 127 THR   A C     1 
ATOM   933  O  O     . THR   A 1 130 ? 39.815 9.075   8.029  1.00 35.39 ? 127 THR   A O     1 
ATOM   934  C  CB    . THR   A 1 130 ? 41.503 10.319  10.696 1.00 38.76 ? 127 THR   A CB    1 
ATOM   935  O  OG1   . THR   A 1 130 ? 42.103 9.847   11.903 1.00 39.03 ? 127 THR   A OG1   1 
ATOM   936  C  CG2   . THR   A 1 130 ? 40.113 10.787  11.056 1.00 40.27 ? 127 THR   A CG2   1 
ATOM   937  N  N     . LYS   A 1 131 ? 41.727 10.130  7.508  1.00 38.84 ? 128 LYS   A N     1 
ATOM   938  C  CA    . LYS   A 1 131 ? 41.249 10.541  6.169  1.00 41.07 ? 128 LYS   A CA    1 
ATOM   939  C  C     . LYS   A 1 131 ? 40.793 9.333   5.351  1.00 37.86 ? 128 LYS   A C     1 
ATOM   940  O  O     . LYS   A 1 131 ? 39.754 9.433   4.730  1.00 37.43 ? 128 LYS   A O     1 
ATOM   941  C  CB    . LYS   A 1 131 ? 42.347 11.275  5.403  1.00 46.09 ? 128 LYS   A CB    1 
ATOM   942  C  CG    . LYS   A 1 131 ? 42.126 11.303  3.899  1.00 50.58 ? 128 LYS   A CG    1 
ATOM   943  C  CD    . LYS   A 1 131 ? 42.427 12.627  3.261  1.00 55.27 ? 128 LYS   A CD    1 
ATOM   944  C  CE    . LYS   A 1 131 ? 41.958 12.699  1.827  1.00 57.42 ? 128 LYS   A CE    1 
ATOM   945  N  NZ    . LYS   A 1 131 ? 42.297 14.002  1.224  1.00 60.64 ? 128 LYS   A NZ    1 
ATOM   946  N  N     . GLN   A 1 132 ? 41.551 8.242   5.390  1.00 36.01 ? 129 GLN   A N     1 
ATOM   947  C  CA    . GLN   A 1 132 ? 41.273 7.041   4.607  1.00 35.51 ? 129 GLN   A CA    1 
ATOM   948  C  C     . GLN   A 1 132 ? 39.923 6.458   5.028  1.00 32.40 ? 129 GLN   A C     1 
ATOM   949  O  O     . GLN   A 1 132 ? 39.095 6.094   4.180  1.00 30.11 ? 129 GLN   A O     1 
ATOM   950  C  CB    . GLN   A 1 132 ? 42.399 6.020   4.783  1.00 37.49 ? 129 GLN   A CB    1 
ATOM   951  C  CG    . GLN   A 1 132 ? 42.176 4.685   4.084  1.00 40.00 ? 129 GLN   A CG    1 
ATOM   952  C  CD    . GLN   A 1 132 ? 43.306 3.702   4.308  1.00 44.41 ? 129 GLN   A CD    1 
ATOM   953  O  OE1   . GLN   A 1 132 ? 44.093 3.823   5.245  1.00 49.20 ? 129 GLN   A OE1   1 
ATOM   954  N  NE2   . GLN   A 1 132 ? 43.394 2.699   3.447  1.00 44.48 ? 129 GLN   A NE2   1 
ATOM   955  N  N     . ALA   A 1 133 ? 39.713 6.343   6.349  1.00 31.61 ? 130 ALA   A N     1 
ATOM   956  C  CA    . ALA   A 1 133 ? 38.431 5.831   6.829  1.00 29.83 ? 130 ALA   A CA    1 
ATOM   957  C  C     . ALA   A 1 133 ? 37.302 6.814   6.542  1.00 30.95 ? 130 ALA   A C     1 
ATOM   958  O  O     . ALA   A 1 133 ? 36.185 6.392   6.278  1.00 33.04 ? 130 ALA   A O     1 
ATOM   959  C  CB    . ALA   A 1 133 ? 38.499 5.500   8.307  1.00 30.42 ? 130 ALA   A CB    1 
ATOM   960  N  N     . GLN   A 1 134 ? 37.587 8.112   6.582  1.00 33.77 ? 131 GLN   A N     1 
ATOM   961  C  CA    . GLN   A 1 134 ? 36.525 9.113   6.302  1.00 35.84 ? 131 GLN   A CA    1 
ATOM   962  C  C     . GLN   A 1 134 ? 36.072 8.976   4.849  1.00 34.86 ? 131 GLN   A C     1 
ATOM   963  O  O     . GLN   A 1 134 ? 34.871 9.001   4.602  1.00 36.04 ? 131 GLN   A O     1 
ATOM   964  C  CB    . GLN   A 1 134 ? 37.032 10.541  6.507  1.00 40.41 ? 131 GLN   A CB    1 
ATOM   965  C  CG    . GLN   A 1 134 ? 37.306 10.910  7.956  1.00 44.79 ? 131 GLN   A CG    1 
ATOM   966  C  CD    . GLN   A 1 134 ? 37.927 12.277  8.113  1.00 48.20 ? 131 GLN   A CD    1 
ATOM   967  O  OE1   . GLN   A 1 134 ? 38.870 12.641  7.417  1.00 53.35 ? 131 GLN   A OE1   1 
ATOM   968  N  NE2   . GLN   A 1 134 ? 37.409 13.041  9.054  1.00 50.99 ? 131 GLN   A NE2   1 
ATOM   969  N  N     . ASP   A 1 135 ? 37.024 8.816   3.937  1.00 34.70 ? 132 ASP   A N     1 
ATOM   970  C  CA    . ASP   A 1 135 ? 36.735 8.701   2.516  1.00 33.51 ? 132 ASP   A CA    1 
ATOM   971  C  C     . ASP   A 1 135 ? 35.900 7.453   2.265  1.00 31.79 ? 132 ASP   A C     1 
ATOM   972  O  O     . ASP   A 1 135 ? 34.917 7.516   1.516  1.00 32.22 ? 132 ASP   A O     1 
ATOM   973  C  CB    . ASP   A 1 135 ? 38.011 8.739   1.668  1.00 34.85 ? 132 ASP   A CB    1 
ATOM   974  C  CG    . ASP   A 1 135 ? 38.647 10.121  1.639  1.00 36.43 ? 132 ASP   A CG    1 
ATOM   975  O  OD1   . ASP   A 1 135 ? 37.908 11.098  1.728  1.00 38.53 ? 132 ASP   A OD1   1 
ATOM   976  O  OD2   . ASP   A 1 135 ? 39.859 10.185  1.564  1.00 37.49 ? 132 ASP   A OD2   1 
ATOM   977  N  N     . LEU   A 1 136 ? 36.305 6.335   2.901  1.00 29.90 ? 133 LEU   A N     1 
ATOM   978  C  CA    . LEU   A 1 136 ? 35.538 5.105   2.740  1.00 29.67 ? 133 LEU   A CA    1 
ATOM   979  C  C     . LEU   A 1 136 ? 34.096 5.309   3.209  1.00 27.07 ? 133 LEU   A C     1 
ATOM   980  O  O     . LEU   A 1 136 ? 33.145 4.943   2.525  1.00 28.31 ? 133 LEU   A O     1 
ATOM   981  C  CB    . LEU   A 1 136 ? 36.223 3.913   3.435  1.00 29.16 ? 133 LEU   A CB    1 
ATOM   982  C  CG    . LEU   A 1 136 ? 35.535 2.553   3.204  1.00 30.06 ? 133 LEU   A CG    1 
ATOM   983  C  CD1   . LEU   A 1 136 ? 35.762 2.045   1.778  1.00 33.02 ? 133 LEU   A CD1   1 
ATOM   984  C  CD2   . LEU   A 1 136 ? 35.977 1.493   4.213  1.00 30.04 ? 133 LEU   A CD2   1 
ATOM   985  N  N     . ALA   A 1 137 ? 33.921 5.814   4.431  1.00 28.59 ? 134 ALA   A N     1 
ATOM   986  C  CA    . ALA   A 1 137 ? 32.584 6.019   4.955  1.00 27.71 ? 134 ALA   A CA    1 
ATOM   987  C  C     . ALA   A 1 137 ? 31.750 6.896   4.012  1.00 30.11 ? 134 ALA   A C     1 
ATOM   988  O  O     . ALA   A 1 137 ? 30.558 6.654   3.830  1.00 30.55 ? 134 ALA   A O     1 
ATOM   989  C  CB    . ALA   A 1 137 ? 32.716 6.658   6.321  1.00 27.57 ? 134 ALA   A CB    1 
ATOM   990  N  N     . ARG   A 1 138 ? 32.380 7.935   3.468  1.00 30.77 ? 135 ARG   A N     1 
ATOM   991  C  CA    . ARG   A 1 138 ? 31.712 8.848   2.509  1.00 35.63 ? 135 ARG   A CA    1 
ATOM   992  C  C     . ARG   A 1 138 ? 31.252 8.025   1.313  1.00 34.76 ? 135 ARG   A C     1 
ATOM   993  O  O     . ARG   A 1 138 ? 30.191 8.257   0.831  1.00 32.96 ? 135 ARG   A O     1 
ATOM   994  C  CB    . ARG   A 1 138 ? 32.689 9.903   1.989  1.00 41.38 ? 135 ARG   A CB    1 
ATOM   995  C  CG    . ARG   A 1 138 ? 32.705 11.199  2.776  1.00 47.23 ? 135 ARG   A CG    1 
ATOM   996  C  CD    . ARG   A 1 138 ? 33.339 12.357  2.028  1.00 52.43 ? 135 ARG   A CD    1 
ATOM   997  N  NE    . ARG   A 1 138 ? 34.775 12.399  2.189  1.00 55.66 ? 135 ARG   A NE    1 
ATOM   998  C  CZ    . ARG   A 1 138 ? 35.365 13.001  3.204  1.00 58.78 ? 135 ARG   A CZ    1 
ATOM   999  N  NH1   . ARG   A 1 138 ? 36.679 13.013  3.309  1.00 60.93 ? 135 ARG   A NH1   1 
ATOM   1000 N  NH2   . ARG   A 1 138 ? 34.632 13.592  4.126  1.00 61.87 ? 135 ARG   A NH2   1 
ATOM   1001 N  N     . SER   A 1 139 ? 32.090 7.087   0.886  1.00 32.84 ? 136 SER   A N     1 
ATOM   1002 C  CA    . SER   A 1 139 ? 31.781 6.184   -0.244 1.00 32.98 ? 136 SER   A CA    1 
ATOM   1003 C  C     . SER   A 1 139 ? 30.563 5.321   0.096  1.00 32.24 ? 136 SER   A C     1 
ATOM   1004 O  O     . SER   A 1 139 ? 29.731 5.134   -0.743 1.00 32.15 ? 136 SER   A O     1 
ATOM   1005 C  CB    . SER   A 1 139 ? 32.970 5.325   -0.513 1.00 34.69 ? 136 SER   A CB    1 
ATOM   1006 O  OG    . SER   A 1 139 ? 32.764 4.598   -1.693 1.00 37.96 ? 136 SER   A OG    1 
ATOM   1007 N  N     . TYR   A 1 140 ? 30.509 4.852   1.335  1.00 30.62 ? 137 TYR   A N     1 
ATOM   1008 C  CA    . TYR   A 1 140 ? 29.428 3.982   1.844  1.00 30.34 ? 137 TYR   A CA    1 
ATOM   1009 C  C     . TYR   A 1 140 ? 28.194 4.817   2.197  1.00 31.96 ? 137 TYR   A C     1 
ATOM   1010 O  O     . TYR   A 1 140 ? 27.135 4.245   2.329  1.00 33.89 ? 137 TYR   A O     1 
ATOM   1011 C  CB    . TYR   A 1 140 ? 29.909 3.276   3.110  1.00 28.74 ? 137 TYR   A CB    1 
ATOM   1012 C  CG    . TYR   A 1 140 ? 30.927 2.180   2.931  1.00 29.32 ? 137 TYR   A CG    1 
ATOM   1013 C  CD1   . TYR   A 1 140 ? 31.166 1.603   1.702  1.00 30.09 ? 137 TYR   A CD1   1 
ATOM   1014 C  CD2   . TYR   A 1 140 ? 31.605 1.673   4.018  1.00 28.77 ? 137 TYR   A CD2   1 
ATOM   1015 C  CE1   . TYR   A 1 140 ? 32.081 0.578   1.553  1.00 30.44 ? 137 TYR   A CE1   1 
ATOM   1016 C  CE2   . TYR   A 1 140 ? 32.515 0.644   3.893  1.00 30.48 ? 137 TYR   A CE2   1 
ATOM   1017 C  CZ    . TYR   A 1 140 ? 32.747 0.086   2.654  1.00 30.43 ? 137 TYR   A CZ    1 
ATOM   1018 O  OH    . TYR   A 1 140 ? 33.641 -0.924  2.541  1.00 32.26 ? 137 TYR   A OH    1 
ATOM   1019 N  N     . GLY   A 1 141 ? 28.366 6.122   2.355  1.00 31.34 ? 138 GLY   A N     1 
ATOM   1020 C  CA    . GLY   A 1 141 ? 27.260 7.012   2.737  1.00 32.68 ? 138 GLY   A CA    1 
ATOM   1021 C  C     . GLY   A 1 141 ? 26.877 6.813   4.191  1.00 31.71 ? 138 GLY   A C     1 
ATOM   1022 O  O     . GLY   A 1 141 ? 25.700 6.871   4.482  1.00 34.74 ? 138 GLY   A O     1 
ATOM   1023 N  N     . ILE   A 1 142 ? 27.856 6.579   5.058  1.00 28.33 ? 139 ILE   A N     1 
ATOM   1024 C  CA    . ILE   A 1 142 ? 27.595 6.349   6.483  1.00 27.55 ? 139 ILE   A CA    1 
ATOM   1025 C  C     . ILE   A 1 142 ? 28.495 7.258   7.305  1.00 29.34 ? 139 ILE   A C     1 
ATOM   1026 O  O     . ILE   A 1 142 ? 29.560 7.656   6.840  1.00 30.66 ? 139 ILE   A O     1 
ATOM   1027 C  CB    . ILE   A 1 142 ? 27.754 4.866   6.897  1.00 26.93 ? 139 ILE   A CB    1 
ATOM   1028 C  CG1   . ILE   A 1 142 ? 29.224 4.421   6.846  1.00 27.11 ? 139 ILE   A CG1   1 
ATOM   1029 C  CG2   . ILE   A 1 142 ? 26.821 3.968   6.096  1.00 26.26 ? 139 ILE   A CG2   1 
ATOM   1030 C  CD1   . ILE   A 1 142 ? 29.434 2.937   6.971  1.00 25.40 ? 139 ILE   A CD1   1 
ATOM   1031 N  N     . PRO   A 1 143 ? 28.096 7.620   8.557  1.00 29.46 ? 140 PRO   A N     1 
ATOM   1032 C  CA    . PRO   A 1 143 ? 28.958 8.398   9.447  1.00 28.50 ? 140 PRO   A CA    1 
ATOM   1033 C  C     . PRO   A 1 143 ? 30.217 7.633   9.846  1.00 28.47 ? 140 PRO   A C     1 
ATOM   1034 O  O     . PRO   A 1 143 ? 30.214 6.410   9.867  1.00 26.55 ? 140 PRO   A O     1 
ATOM   1035 C  CB    . PRO   A 1 143 ? 28.060 8.683   10.660 1.00 29.92 ? 140 PRO   A CB    1 
ATOM   1036 C  CG    . PRO   A 1 143 ? 26.646 8.542   10.119 1.00 30.03 ? 140 PRO   A CG    1 
ATOM   1037 C  CD    . PRO   A 1 143 ? 26.761 7.394   9.132  1.00 30.56 ? 140 PRO   A CD    1 
ATOM   1038 N  N     . PHE   A 1 144 ? 31.305 8.374   10.101 1.00 29.15 ? 141 PHE   A N     1 
ATOM   1039 C  CA    . PHE   A 1 144 ? 32.532 7.766   10.610 1.00 28.88 ? 141 PHE   A CA    1 
ATOM   1040 C  C     . PHE   A 1 144 ? 32.864 8.456   11.933 1.00 30.12 ? 141 PHE   A C     1 
ATOM   1041 O  O     . PHE   A 1 144 ? 32.797 9.687   12.035 1.00 31.40 ? 141 PHE   A O     1 
ATOM   1042 C  CB    . PHE   A 1 144 ? 33.684 7.870   9.601  1.00 29.96 ? 141 PHE   A CB    1 
ATOM   1043 C  CG    . PHE   A 1 144 ? 35.041 7.515   10.158 1.00 29.28 ? 141 PHE   A CG    1 
ATOM   1044 C  CD1   . PHE   A 1 144 ? 35.286 6.274   10.735 1.00 30.35 ? 141 PHE   A CD1   1 
ATOM   1045 C  CD2   . PHE   A 1 144 ? 36.086 8.427   10.115 1.00 32.39 ? 141 PHE   A CD2   1 
ATOM   1046 C  CE1   . PHE   A 1 144 ? 36.532 5.961   11.267 1.00 30.17 ? 141 PHE   A CE1   1 
ATOM   1047 C  CE2   . PHE   A 1 144 ? 37.330 8.113   10.641 1.00 32.57 ? 141 PHE   A CE2   1 
ATOM   1048 C  CZ    . PHE   A 1 144 ? 37.565 6.871   11.197 1.00 32.37 ? 141 PHE   A CZ    1 
ATOM   1049 N  N     . ILE   A 1 145 ? 33.232 7.664   12.938 1.00 30.95 ? 142 ILE   A N     1 
ATOM   1050 C  CA    . ILE   A 1 145 ? 33.618 8.228   14.228 1.00 31.09 ? 142 ILE   A CA    1 
ATOM   1051 C  C     . ILE   A 1 145 ? 34.792 7.416   14.763 1.00 29.40 ? 142 ILE   A C     1 
ATOM   1052 O  O     . ILE   A 1 145 ? 34.750 6.188   14.711 1.00 29.28 ? 142 ILE   A O     1 
ATOM   1053 C  CB    . ILE   A 1 145 ? 32.423 8.216   15.205 1.00 33.95 ? 142 ILE   A CB    1 
ATOM   1054 C  CG1   . ILE   A 1 145 ? 31.319 9.176   14.763 1.00 36.80 ? 142 ILE   A CG1   1 
ATOM   1055 C  CG2   . ILE   A 1 145 ? 32.859 8.443   16.652 1.00 37.42 ? 142 ILE   A CG2   1 
ATOM   1056 C  CD1   . ILE   A 1 145 ? 29.947 8.783   15.265 1.00 38.99 ? 142 ILE   A CD1   1 
ATOM   1057 N  N     . GLU   A 1 146 ? 35.811 8.115   15.286 1.00 30.44 ? 143 GLU   A N     1 
ATOM   1058 C  CA    . GLU   A 1 146 ? 36.942 7.469   15.928 1.00 31.48 ? 143 GLU   A CA    1 
ATOM   1059 C  C     . GLU   A 1 146 ? 36.729 7.434   17.438 1.00 31.78 ? 143 GLU   A C     1 
ATOM   1060 O  O     . GLU   A 1 146 ? 36.457 8.456   18.062 1.00 35.61 ? 143 GLU   A O     1 
ATOM   1061 C  CB    . GLU   A 1 146 ? 38.244 8.201   15.619 1.00 33.40 ? 143 GLU   A CB    1 
ATOM   1062 C  CG    . GLU   A 1 146 ? 38.692 7.970   14.188 1.00 34.78 ? 143 GLU   A CG    1 
ATOM   1063 C  CD    . GLU   A 1 146 ? 40.181 8.167   13.965 1.00 36.20 ? 143 GLU   A CD    1 
ATOM   1064 O  OE1   . GLU   A 1 146 ? 40.887 8.553   14.926 1.00 35.97 ? 143 GLU   A OE1   1 
ATOM   1065 O  OE2   . GLU   A 1 146 ? 40.639 7.872   12.844 1.00 37.57 ? 143 GLU   A OE2   1 
ATOM   1066 N  N     . THR   A 1 147 ? 36.895 6.239   18.005 1.00 30.25 ? 144 THR   A N     1 
ATOM   1067 C  CA    . THR   A 1 147 ? 36.616 6.037   19.419 1.00 30.97 ? 144 THR   A CA    1 
ATOM   1068 C  C     . THR   A 1 147 ? 37.815 5.454   20.166 1.00 32.90 ? 144 THR   A C     1 
ATOM   1069 O  O     . THR   A 1 147 ? 38.681 4.774   19.608 1.00 31.29 ? 144 THR   A O     1 
ATOM   1070 C  CB    . THR   A 1 147 ? 35.411 5.098   19.595 1.00 29.28 ? 144 THR   A CB    1 
ATOM   1071 O  OG1   . THR   A 1 147 ? 35.758 3.796   19.106 1.00 28.08 ? 144 THR   A OG1   1 
ATOM   1072 C  CG2   . THR   A 1 147 ? 34.164 5.570   18.879 1.00 29.87 ? 144 THR   A CG2   1 
ATOM   1073 N  N     . SER   A 1 148 ? 37.807 5.678   21.486 1.00 33.47 ? 145 SER   A N     1 
ATOM   1074 C  CA    . SER   A 1 148 ? 38.627 4.912   22.403 1.00 35.31 ? 145 SER   A CA    1 
ATOM   1075 C  C     . SER   A 1 148 ? 37.734 4.333   23.498 1.00 35.28 ? 145 SER   A C     1 
ATOM   1076 O  O     . SER   A 1 148 ? 37.160 5.088   24.282 1.00 35.15 ? 145 SER   A O     1 
ATOM   1077 C  CB    . SER   A 1 148 ? 39.723 5.743   23.009 1.00 38.07 ? 145 SER   A CB    1 
ATOM   1078 O  OG    . SER   A 1 148 ? 40.405 4.973   23.997 1.00 41.08 ? 145 SER   A OG    1 
ATOM   1079 N  N     . ALA   A 1 149 ? 37.596 3.005   23.511 1.00 34.86 ? 146 ALA   A N     1 
ATOM   1080 C  CA    . ALA   A 1 149 ? 36.947 2.326   24.624 1.00 37.92 ? 146 ALA   A CA    1 
ATOM   1081 C  C     . ALA   A 1 149 ? 37.746 2.521   25.917 1.00 41.14 ? 146 ALA   A C     1 
ATOM   1082 O  O     . ALA   A 1 149 ? 37.156 2.617   26.995 1.00 40.66 ? 146 ALA   A O     1 
ATOM   1083 C  CB    . ALA   A 1 149 ? 36.727 0.868   24.306 1.00 36.84 ? 146 ALA   A CB    1 
ATOM   1084 N  N     . LYS   A 1 150 ? 39.083 2.586   25.793 1.00 39.57 ? 147 LYS   A N     1 
ATOM   1085 C  CA    . LYS   A 1 150 ? 39.976 2.838   26.921 1.00 44.42 ? 147 LYS   A CA    1 
ATOM   1086 C  C     . LYS   A 1 150 ? 39.638 4.155   27.622 1.00 45.95 ? 147 LYS   A C     1 
ATOM   1087 O  O     . LYS   A 1 150 ? 39.474 4.167   28.838 1.00 45.32 ? 147 LYS   A O     1 
ATOM   1088 C  CB    . LYS   A 1 150 ? 41.459 2.720   26.524 1.00 45.28 ? 147 LYS   A CB    1 
ATOM   1089 C  CG    . LYS   A 1 150 ? 42.468 2.813   27.670 1.00 49.40 ? 147 LYS   A CG    1 
ATOM   1090 C  CD    . LYS   A 1 150 ? 43.858 2.292   27.317 1.00 51.72 ? 147 LYS   A CD    1 
ATOM   1091 C  CE    . LYS   A 1 150 ? 44.864 2.409   28.448 1.00 57.55 ? 147 LYS   A CE    1 
ATOM   1092 N  NZ    . LYS   A 1 150 ? 46.239 2.060   28.011 1.00 60.46 ? 147 LYS   A NZ    1 
ATOM   1093 N  N     . THR   A 1 151 ? 39.532 5.257   26.861 1.00 46.70 ? 148 THR   A N     1 
ATOM   1094 C  CA    . THR   A 1 151 ? 39.376 6.581   27.449 1.00 50.25 ? 148 THR   A CA    1 
ATOM   1095 C  C     . THR   A 1 151 ? 37.912 7.019   27.487 1.00 50.40 ? 148 THR   A C     1 
ATOM   1096 O  O     . THR   A 1 151 ? 37.600 7.983   28.174 1.00 50.94 ? 148 THR   A O     1 
ATOM   1097 C  CB    . THR   A 1 151 ? 40.298 7.614   26.786 1.00 51.08 ? 148 THR   A CB    1 
ATOM   1098 O  OG1   . THR   A 1 151 ? 39.696 8.137   25.599 1.00 54.01 ? 148 THR   A OG1   1 
ATOM   1099 C  CG2   . THR   A 1 151 ? 41.694 7.091   26.508 1.00 51.11 ? 148 THR   A CG2   1 
ATOM   1100 N  N     . ARG   A 1 152 ? 37.049 6.286   26.774 1.00 48.37 ? 149 ARG   A N     1 
ATOM   1101 C  CA    . ARG   A 1 152 ? 35.580 6.496   26.578 1.00 50.80 ? 149 ARG   A CA    1 
ATOM   1102 C  C     . ARG   A 1 152 ? 35.326 7.633   25.580 1.00 49.60 ? 149 ARG   A C     1 
ATOM   1103 O  O     . ARG   A 1 152 ? 34.184 8.034   25.450 1.00 49.84 ? 149 ARG   A O     1 
ATOM   1104 C  CB    . ARG   A 1 152 ? 34.750 6.581   27.873 1.00 56.67 ? 149 ARG   A CB    1 
ATOM   1105 C  CG    . ARG   A 1 152 ? 33.246 6.449   27.664 1.00 61.18 ? 149 ARG   A CG    1 
ATOM   1106 C  CD    . ARG   A 1 152 ? 32.293 6.658   28.840 1.00 67.52 ? 149 ARG   A CD    1 
ATOM   1107 N  NE    . ARG   A 1 152 ? 31.007 7.270   28.529 1.00 74.15 ? 149 ARG   A NE    1 
ATOM   1108 C  CZ    . ARG   A 1 152 ? 29.828 6.655   28.478 1.00 77.29 ? 149 ARG   A CZ    1 
ATOM   1109 N  NH1   . ARG   A 1 152 ? 28.744 7.342   28.169 1.00 74.28 ? 149 ARG   A NH1   1 
ATOM   1110 N  NH2   . ARG   A 1 152 ? 29.731 5.364   28.732 1.00 80.03 ? 149 ARG   A NH2   1 
ATOM   1111 N  N     . GLN   A 1 153 ? 36.352 8.080   24.861 1.00 46.57 ? 150 GLN   A N     1 
ATOM   1112 C  CA    . GLN   A 1 153 ? 36.195 9.160   23.866 1.00 46.13 ? 150 GLN   A CA    1 
ATOM   1113 C  C     . GLN   A 1 153 ? 35.307 8.703   22.712 1.00 40.74 ? 150 GLN   A C     1 
ATOM   1114 O  O     . GLN   A 1 153 ? 35.577 7.647   22.169 1.00 36.56 ? 150 GLN   A O     1 
ATOM   1115 C  CB    . GLN   A 1 153 ? 37.554 9.481   23.270 1.00 49.72 ? 150 GLN   A CB    1 
ATOM   1116 C  CG    . GLN   A 1 153 ? 37.519 10.708  22.396 1.00 54.68 ? 150 GLN   A CG    1 
ATOM   1117 C  CD    . GLN   A 1 153 ? 38.921 11.178  22.130 1.00 60.36 ? 150 GLN   A CD    1 
ATOM   1118 O  OE1   . GLN   A 1 153 ? 39.804 11.033  22.975 1.00 65.25 ? 150 GLN   A OE1   1 
ATOM   1119 N  NE2   . GLN   A 1 153 ? 39.125 11.721  20.942 1.00 58.15 ? 150 GLN   A NE2   1 
ATOM   1120 N  N     . ARG   A 1 154 ? 34.202 9.417   22.495 1.00 39.52 ? 151 ARG   A N     1 
ATOM   1121 C  CA    . ARG   A 1 154 ? 33.218 9.252   21.386 1.00 38.96 ? 151 ARG   A CA    1 
ATOM   1122 C  C     . ARG   A 1 154 ? 32.423 7.938   21.443 1.00 36.40 ? 151 ARG   A C     1 
ATOM   1123 O  O     . ARG   A 1 154 ? 31.734 7.668   20.489 1.00 34.05 ? 151 ARG   A O     1 
ATOM   1124 C  CB    . ARG   A 1 154 ? 33.883 9.493   20.031 1.00 37.41 ? 151 ARG   A CB    1 
ATOM   1125 C  CG    . ARG   A 1 154 ? 34.593 10.830  19.937 1.00 41.37 ? 151 ARG   A CG    1 
ATOM   1126 C  CD    . ARG   A 1 154 ? 34.485 11.442  18.565 1.00 43.30 ? 151 ARG   A CD    1 
ATOM   1127 N  NE    . ARG   A 1 154 ? 33.150 11.943  18.345 1.00 44.65 ? 151 ARG   A NE    1 
ATOM   1128 C  CZ    . ARG   A 1 154 ? 32.731 12.461  17.213 1.00 46.87 ? 151 ARG   A CZ    1 
ATOM   1129 N  NH1   . ARG   A 1 154 ? 33.553 12.541  16.183 1.00 47.22 ? 151 ARG   A NH1   1 
ATOM   1130 N  NH2   . ARG   A 1 154 ? 31.495 12.901  17.100 1.00 47.79 ? 151 ARG   A NH2   1 
ATOM   1131 N  N     . VAL   A 1 155 ? 32.457 7.214   22.556 1.00 34.85 ? 152 VAL   A N     1 
ATOM   1132 C  CA    . VAL   A 1 155 ? 31.722 5.929   22.654 1.00 34.26 ? 152 VAL   A CA    1 
ATOM   1133 C  C     . VAL   A 1 155 ? 30.235 6.244   22.587 1.00 34.61 ? 152 VAL   A C     1 
ATOM   1134 O  O     . VAL   A 1 155 ? 29.586 5.677   21.758 1.00 30.62 ? 152 VAL   A O     1 
ATOM   1135 C  CB    . VAL   A 1 155 ? 32.087 5.142   23.922 1.00 35.22 ? 152 VAL   A CB    1 
ATOM   1136 C  CG1   . VAL   A 1 155 ? 31.254 3.887   24.045 1.00 33.88 ? 152 VAL   A CG1   1 
ATOM   1137 C  CG2   . VAL   A 1 155 ? 33.561 4.793   23.959 1.00 34.89 ? 152 VAL   A CG2   1 
ATOM   1138 N  N     . GLU   A 1 156 ? 29.751 7.132   23.452 1.00 36.60 ? 153 GLU   A N     1 
ATOM   1139 C  CA    . GLU   A 1 156 ? 28.342 7.500   23.401 1.00 38.68 ? 153 GLU   A CA    1 
ATOM   1140 C  C     . GLU   A 1 156 ? 27.990 8.001   21.992 1.00 37.13 ? 153 GLU   A C     1 
ATOM   1141 O  O     . GLU   A 1 156 ? 27.002 7.567   21.396 1.00 34.81 ? 153 GLU   A O     1 
ATOM   1142 C  CB    . GLU   A 1 156 ? 28.046 8.561   24.459 1.00 41.66 ? 153 GLU   A CB    1 
ATOM   1143 C  CG    . GLU   A 1 156 ? 26.708 8.394   25.133 1.00 45.96 ? 153 GLU   A CG    1 
ATOM   1144 C  CD    . GLU   A 1 156 ? 26.479 9.478   26.180 1.00 48.92 ? 153 GLU   A CD    1 
ATOM   1145 O  OE1   . GLU   A 1 156 ? 26.249 10.641  25.774 1.00 51.10 ? 153 GLU   A OE1   1 
ATOM   1146 O  OE2   . GLU   A 1 156 ? 26.560 9.168   27.391 1.00 53.34 ? 153 GLU   A OE2   1 
ATOM   1147 N  N     . ASP   A 1 157 ? 28.831 8.900   21.470 1.00 37.21 ? 154 ASP   A N     1 
ATOM   1148 C  CA    . ASP   A 1 157 ? 28.691 9.489   20.148 1.00 35.30 ? 154 ASP   A CA    1 
ATOM   1149 C  C     . ASP   A 1 157 ? 28.423 8.427   19.084 1.00 31.79 ? 154 ASP   A C     1 
ATOM   1150 O  O     . ASP   A 1 157 ? 27.518 8.617   18.289 1.00 31.23 ? 154 ASP   A O     1 
ATOM   1151 C  CB    . ASP   A 1 157 ? 29.909 10.341  19.762 1.00 39.15 ? 154 ASP   A CB    1 
ATOM   1152 C  CG    . ASP   A 1 157 ? 29.940 11.732  20.380 1.00 41.94 ? 154 ASP   A CG    1 
ATOM   1153 O  OD1   . ASP   A 1 157 ? 28.897 12.163  20.932 1.00 44.42 ? 154 ASP   A OD1   1 
ATOM   1154 O  OD2   . ASP   A 1 157 ? 31.001 12.380  20.273 1.00 44.07 ? 154 ASP   A OD2   1 
ATOM   1155 N  N     . ALA   A 1 158 ? 29.188 7.330   19.086 1.00 29.80 ? 155 ALA   A N     1 
ATOM   1156 C  CA    . ALA   A 1 158 ? 29.040 6.270   18.086 1.00 29.79 ? 155 ALA   A CA    1 
ATOM   1157 C  C     . ALA   A 1 158 ? 27.683 5.572   18.206 1.00 29.47 ? 155 ALA   A C     1 
ATOM   1158 O  O     . ALA   A 1 158 ? 26.995 5.352   17.213 1.00 27.85 ? 155 ALA   A O     1 
ATOM   1159 C  CB    . ALA   A 1 158 ? 30.142 5.264   18.212 1.00 29.83 ? 155 ALA   A CB    1 
ATOM   1160 N  N     . PHE   A 1 159 ? 27.305 5.166   19.425 1.00 29.18 ? 156 PHE   A N     1 
ATOM   1161 C  CA    . PHE   A 1 159 ? 26.033 4.466   19.575 1.00 30.78 ? 156 PHE   A CA    1 
ATOM   1162 C  C     . PHE   A 1 159 ? 24.836 5.370   19.264 1.00 30.93 ? 156 PHE   A C     1 
ATOM   1163 O  O     . PHE   A 1 159 ? 23.873 4.931   18.628 1.00 30.13 ? 156 PHE   A O     1 
ATOM   1164 C  CB    . PHE   A 1 159 ? 25.909 3.841   20.976 1.00 31.97 ? 156 PHE   A CB    1 
ATOM   1165 C  CG    . PHE   A 1 159 ? 26.727 2.594   21.165 1.00 31.38 ? 156 PHE   A CG    1 
ATOM   1166 C  CD1   . PHE   A 1 159 ? 26.182 1.348   20.881 1.00 31.05 ? 156 PHE   A CD1   1 
ATOM   1167 C  CD2   . PHE   A 1 159 ? 28.037 2.662   21.636 1.00 30.18 ? 156 PHE   A CD2   1 
ATOM   1168 C  CE1   . PHE   A 1 159 ? 26.935 0.191   21.038 1.00 31.07 ? 156 PHE   A CE1   1 
ATOM   1169 C  CE2   . PHE   A 1 159 ? 28.788 1.503   21.789 1.00 28.96 ? 156 PHE   A CE2   1 
ATOM   1170 C  CZ    . PHE   A 1 159 ? 28.227 0.272   21.510 1.00 29.19 ? 156 PHE   A CZ    1 
ATOM   1171 N  N     . TYR   A 1 160 ? 24.889 6.627   19.719 1.00 31.73 ? 157 TYR   A N     1 
ATOM   1172 C  CA    . TYR   A 1 160 ? 23.779 7.557   19.563 1.00 33.22 ? 157 TYR   A CA    1 
ATOM   1173 C  C     . TYR   A 1 160 ? 23.678 8.047   18.111 1.00 31.55 ? 157 TYR   A C     1 
ATOM   1174 O  O     . TYR   A 1 160 ? 22.599 8.349   17.622 1.00 32.29 ? 157 TYR   A O     1 
ATOM   1175 C  CB    . TYR   A 1 160 ? 23.941 8.742   20.523 1.00 36.34 ? 157 TYR   A CB    1 
ATOM   1176 C  CG    . TYR   A 1 160 ? 23.625 8.446   21.976 1.00 40.67 ? 157 TYR   A CG    1 
ATOM   1177 C  CD1   . TYR   A 1 160 ? 23.436 7.146   22.426 1.00 40.51 ? 157 TYR   A CD1   1 
ATOM   1178 C  CD2   . TYR   A 1 160 ? 23.527 9.471   22.911 1.00 46.39 ? 157 TYR   A CD2   1 
ATOM   1179 C  CE1   . TYR   A 1 160 ? 23.152 6.869   23.758 1.00 46.27 ? 157 TYR   A CE1   1 
ATOM   1180 C  CE2   . TYR   A 1 160 ? 23.243 9.212   24.247 1.00 48.70 ? 157 TYR   A CE2   1 
ATOM   1181 C  CZ    . TYR   A 1 160 ? 23.052 7.908   24.672 1.00 50.02 ? 157 TYR   A CZ    1 
ATOM   1182 O  OH    . TYR   A 1 160 ? 22.764 7.636   25.983 1.00 53.16 ? 157 TYR   A OH    1 
ATOM   1183 N  N     . THR   A 1 161 ? 24.810 8.148   17.419 1.00 29.54 ? 158 THR   A N     1 
ATOM   1184 C  CA    . THR   A 1 161 ? 24.755 8.485   16.000 1.00 29.69 ? 158 THR   A CA    1 
ATOM   1185 C  C     . THR   A 1 161 ? 24.006 7.379   15.266 1.00 27.11 ? 158 THR   A C     1 
ATOM   1186 O  O     . THR   A 1 161 ? 23.229 7.662   14.358 1.00 28.35 ? 158 THR   A O     1 
ATOM   1187 C  CB    . THR   A 1 161 ? 26.161 8.702   15.420 1.00 28.37 ? 158 THR   A CB    1 
ATOM   1188 O  OG1   . THR   A 1 161 ? 26.783 9.769   16.129 1.00 31.02 ? 158 THR   A OG1   1 
ATOM   1189 C  CG2   . THR   A 1 161 ? 26.183 8.990   13.932 1.00 29.48 ? 158 THR   A CG2   1 
ATOM   1190 N  N     . LEU   A 1 162 ? 24.306 6.113   15.627 1.00 26.17 ? 159 LEU   A N     1 
ATOM   1191 C  CA    . LEU   A 1 162 ? 23.649 4.956   15.037 1.00 25.54 ? 159 LEU   A CA    1 
ATOM   1192 C  C     . LEU   A 1 162 ? 22.136 5.015   15.251 1.00 25.75 ? 159 LEU   A C     1 
ATOM   1193 O  O     . LEU   A 1 162 ? 21.386 4.771   14.324 1.00 27.22 ? 159 LEU   A O     1 
ATOM   1194 C  CB    . LEU   A 1 162 ? 24.245 3.653   15.595 1.00 26.13 ? 159 LEU   A CB    1 
ATOM   1195 C  CG    . LEU   A 1 162 ? 23.723 2.355   14.967 1.00 26.49 ? 159 LEU   A CG    1 
ATOM   1196 C  CD1   . LEU   A 1 162 ? 23.846 2.392   13.441 1.00 27.31 ? 159 LEU   A CD1   1 
ATOM   1197 C  CD2   . LEU   A 1 162 ? 24.479 1.147   15.536 1.00 27.14 ? 159 LEU   A CD2   1 
ATOM   1198 N  N     . VAL   A 1 163 ? 21.685 5.272   16.485 1.00 27.00 ? 160 VAL   A N     1 
ATOM   1199 C  CA    . VAL   A 1 163 ? 20.245 5.361   16.741 1.00 28.69 ? 160 VAL   A CA    1 
ATOM   1200 C  C     . VAL   A 1 163 ? 19.651 6.425   15.820 1.00 30.27 ? 160 VAL   A C     1 
ATOM   1201 O  O     . VAL   A 1 163 ? 18.605 6.208   15.198 1.00 31.29 ? 160 VAL   A O     1 
ATOM   1202 C  CB    . VAL   A 1 163 ? 19.942 5.751   18.206 1.00 29.65 ? 160 VAL   A CB    1 
ATOM   1203 C  CG1   . VAL   A 1 163 ? 18.449 6.040   18.383 1.00 31.57 ? 160 VAL   A CG1   1 
ATOM   1204 C  CG2   . VAL   A 1 163 ? 20.415 4.685   19.184 1.00 29.84 ? 160 VAL   A CG2   1 
ATOM   1205 N  N     . ARG   A 1 164 ? 20.346 7.572   15.734 1.00 30.85 ? 161 ARG   A N     1 
ATOM   1206 C  CA    . ARG   A 1 164 ? 19.889 8.668   14.887 1.00 32.52 ? 161 ARG   A CA    1 
ATOM   1207 C  C     . ARG   A 1 164 ? 19.768 8.221   13.430 1.00 31.19 ? 161 ARG   A C     1 
ATOM   1208 O  O     . ARG   A 1 164 ? 18.873 8.659   12.711 1.00 32.22 ? 161 ARG   A O     1 
ATOM   1209 C  CB    . ARG   A 1 164 ? 20.798 9.887   15.059 1.00 34.37 ? 161 ARG   A CB    1 
ATOM   1210 C  CG    . ARG   A 1 164 ? 20.457 10.681  16.314 1.00 37.61 ? 161 ARG   A CG    1 
ATOM   1211 C  CD    . ARG   A 1 164 ? 21.450 11.813  16.480 1.00 40.71 ? 161 ARG   A CD    1 
ATOM   1212 N  NE    . ARG   A 1 164 ? 21.140 12.647  17.638 1.00 43.89 ? 161 ARG   A NE    1 
ATOM   1213 C  CZ    . ARG   A 1 164 ? 21.888 12.748  18.738 1.00 46.34 ? 161 ARG   A CZ    1 
ATOM   1214 N  NH1   . ARG   A 1 164 ? 23.011 12.054  18.859 1.00 45.16 ? 161 ARG   A NH1   1 
ATOM   1215 N  NH2   . ARG   A 1 164 ? 21.509 13.558  19.713 1.00 48.86 ? 161 ARG   A NH2   1 
ATOM   1216 N  N     . GLU   A 1 165 ? 20.689 7.361   12.985 1.00 30.02 ? 162 GLU   A N     1 
ATOM   1217 C  CA    . GLU   A 1 165 ? 20.626 6.863   11.613 1.00 30.49 ? 162 GLU   A CA    1 
ATOM   1218 C  C     . GLU   A 1 165 ? 19.395 5.980   11.408 1.00 30.96 ? 162 GLU   A C     1 
ATOM   1219 O  O     . GLU   A 1 165 ? 18.807 5.966   10.337 1.00 30.68 ? 162 GLU   A O     1 
ATOM   1220 C  CB    . GLU   A 1 165 ? 21.912 6.119   11.240 1.00 29.56 ? 162 GLU   A CB    1 
ATOM   1221 C  CG    . GLU   A 1 165 ? 23.083 7.068   11.013 1.00 31.24 ? 162 GLU   A CG    1 
ATOM   1222 C  CD    . GLU   A 1 165 ? 22.963 7.913   9.749  1.00 31.97 ? 162 GLU   A CD    1 
ATOM   1223 O  OE1   . GLU   A 1 165 ? 23.134 7.350   8.651  1.00 33.94 ? 162 GLU   A OE1   1 
ATOM   1224 O  OE2   . GLU   A 1 165 ? 22.706 9.135   9.871  1.00 34.78 ? 162 GLU   A OE2   1 
ATOM   1225 N  N     . ILE   A 1 166 ? 19.073 5.196   12.427 1.00 31.49 ? 163 ILE   A N     1 
ATOM   1226 C  CA    . ILE   A 1 166 ? 17.903 4.282   12.363 1.00 32.33 ? 163 ILE   A CA    1 
ATOM   1227 C  C     . ILE   A 1 166 ? 16.652 5.154   12.246 1.00 35.33 ? 163 ILE   A C     1 
ATOM   1228 O  O     . ILE   A 1 166 ? 15.836 4.880   11.385 1.00 36.20 ? 163 ILE   A O     1 
ATOM   1229 C  CB    . ILE   A 1 166 ? 17.866 3.358   13.593 1.00 32.42 ? 163 ILE   A CB    1 
ATOM   1230 C  CG1   . ILE   A 1 166 ? 19.071 2.416   13.626 1.00 31.74 ? 163 ILE   A CG1   1 
ATOM   1231 C  CG2   . ILE   A 1 166 ? 16.559 2.593   13.643 1.00 34.04 ? 163 ILE   A CG2   1 
ATOM   1232 C  CD1   . ILE   A 1 166 ? 19.181 1.607   14.881 1.00 32.75 ? 163 ILE   A CD1   1 
ATOM   1233 N  N     . ARG   A 1 167 ? 16.565 6.205   13.058 1.00 37.63 ? 164 ARG   A N     1 
ATOM   1234 C  CA    . ARG   A 1 167 ? 15.407 7.125   13.015 1.00 41.07 ? 164 ARG   A CA    1 
ATOM   1235 C  C     . ARG   A 1 167 ? 15.337 7.791   11.644 1.00 42.81 ? 164 ARG   A C     1 
ATOM   1236 O  O     . ARG   A 1 167 ? 14.250 7.838   11.105 1.00 44.41 ? 164 ARG   A O     1 
ATOM   1237 C  CB    . ARG   A 1 167 ? 15.551 8.198   14.094 1.00 44.67 ? 164 ARG   A CB    1 
ATOM   1238 C  CG    . ARG   A 1 167 ? 15.177 7.718   15.485 1.00 47.69 ? 164 ARG   A CG    1 
ATOM   1239 C  CD    . ARG   A 1 167 ? 15.665 8.530   16.666 1.00 50.36 ? 164 ARG   A CD    1 
ATOM   1240 N  NE    . ARG   A 1 167 ? 14.964 8.036   17.837 1.00 53.00 ? 164 ARG   A NE    1 
ATOM   1241 C  CZ    . ARG   A 1 167 ? 15.024 8.535   19.068 1.00 57.10 ? 164 ARG   A CZ    1 
ATOM   1242 N  NH1   . ARG   A 1 167 ? 15.799 9.567   19.342 1.00 55.97 ? 164 ARG   A NH1   1 
ATOM   1243 N  NH2   . ARG   A 1 167 ? 14.304 7.979   20.024 1.00 56.18 ? 164 ARG   A NH2   1 
ATOM   1244 N  N     . GLN   A 1 168 ? 16.464 8.247   11.102 1.00 42.05 ? 165 GLN   A N     1 
ATOM   1245 C  CA    . GLN   A 1 168 ? 16.448 8.912   9.774  1.00 45.19 ? 165 GLN   A CA    1 
ATOM   1246 C  C     . GLN   A 1 168 ? 15.861 7.929   8.768  1.00 45.61 ? 165 GLN   A C     1 
ATOM   1247 O  O     . GLN   A 1 168 ? 15.014 8.319   7.971  1.00 45.85 ? 165 GLN   A O     1 
ATOM   1248 C  CB    . GLN   A 1 168 ? 17.860 9.224   9.284  1.00 47.53 ? 165 GLN   A CB    1 
ATOM   1249 C  CG    . GLN   A 1 168 ? 18.555 10.352  10.023 1.00 52.42 ? 165 GLN   A CG    1 
ATOM   1250 C  CD    . GLN   A 1 168 ? 17.802 11.657  9.968  1.00 59.10 ? 165 GLN   A CD    1 
ATOM   1251 O  OE1   . GLN   A 1 168 ? 17.444 12.160  8.905  1.00 65.41 ? 165 GLN   A OE1   1 
ATOM   1252 N  NE2   . GLN   A 1 168 ? 17.556 12.219  11.136 1.00 65.32 ? 165 GLN   A NE2   1 
ATOM   1253 N  N     . TYR   A 1 169 ? 16.328 6.692   8.838  1.00 42.54 ? 166 TYR   A N     1 
ATOM   1254 C  CA    . TYR   A 1 169 ? 15.896 5.632   7.939  1.00 45.21 ? 166 TYR   A CA    1 
ATOM   1255 C  C     . TYR   A 1 169 ? 14.400 5.370   8.084  1.00 47.72 ? 166 TYR   A C     1 
ATOM   1256 O  O     . TYR   A 1 169 ? 13.716 5.141   7.091  1.00 46.27 ? 166 TYR   A O     1 
ATOM   1257 C  CB    . TYR   A 1 169 ? 16.702 4.359   8.216  1.00 46.63 ? 166 TYR   A CB    1 
ATOM   1258 C  CG    . TYR   A 1 169 ? 16.377 3.163   7.359  1.00 50.52 ? 166 TYR   A CG    1 
ATOM   1259 C  CD1   . TYR   A 1 169 ? 16.757 3.123   6.027  1.00 51.80 ? 166 TYR   A CD1   1 
ATOM   1260 C  CD2   . TYR   A 1 169 ? 15.744 2.045   7.894  1.00 51.53 ? 166 TYR   A CD2   1 
ATOM   1261 C  CE1   . TYR   A 1 169 ? 16.479 2.020   5.232  1.00 55.31 ? 166 TYR   A CE1   1 
ATOM   1262 C  CE2   . TYR   A 1 169 ? 15.456 0.936   7.111  1.00 55.77 ? 166 TYR   A CE2   1 
ATOM   1263 C  CZ    . TYR   A 1 169 ? 15.824 0.927   5.774  1.00 55.70 ? 166 TYR   A CZ    1 
ATOM   1264 O  OH    . TYR   A 1 169 ? 15.562 -0.155  4.986  1.00 59.79 ? 166 TYR   A OH    1 
ATOM   1265 N  N     . ARG   A 1 170 ? 13.906 5.372   9.325  1.00 48.24 ? 167 ARG   A N     1 
ATOM   1266 C  CA    . ARG   A 1 170 ? 12.529 4.986   9.601  1.00 53.06 ? 167 ARG   A CA    1 
ATOM   1267 C  C     . ARG   A 1 170 ? 11.567 6.026   9.020  1.00 58.02 ? 167 ARG   A C     1 
ATOM   1268 O  O     . ARG   A 1 170 ? 10.384 5.742   8.823  1.00 61.46 ? 167 ARG   A O     1 
ATOM   1269 C  CB    . ARG   A 1 170 ? 12.331 4.714   11.098 1.00 52.97 ? 167 ARG   A CB    1 
ATOM   1270 C  CG    . ARG   A 1 170 ? 12.668 3.295   11.545 1.00 52.46 ? 167 ARG   A CG    1 
ATOM   1271 C  CD    . ARG   A 1 170 ? 12.573 3.182   13.062 1.00 53.47 ? 167 ARG   A CD    1 
ATOM   1272 N  NE    . ARG   A 1 170 ? 12.825 1.880   13.675 1.00 52.64 ? 167 ARG   A NE    1 
ATOM   1273 C  CZ    . ARG   A 1 170 ? 12.647 1.597   14.964 1.00 55.96 ? 167 ARG   A CZ    1 
ATOM   1274 N  NH1   . ARG   A 1 170 ? 12.182 2.523   15.787 1.00 58.93 ? 167 ARG   A NH1   1 
ATOM   1275 N  NH2   . ARG   A 1 170 ? 12.912 0.386   15.431 1.00 58.72 ? 167 ARG   A NH2   1 
ATOM   1276 N  N     . LEU   A 1 171 ? 12.091 7.214   8.705  1.00 62.32 ? 168 LEU   A N     1 
ATOM   1277 C  CA    . LEU   A 1 171 ? 11.257 8.313   8.151  1.00 69.77 ? 168 LEU   A CA    1 
ATOM   1278 C  C     . LEU   A 1 171 ? 11.421 8.421   6.629  1.00 72.94 ? 168 LEU   A C     1 
ATOM   1279 O  O     . LEU   A 1 171 ? 10.876 9.392   6.067  1.00 75.46 ? 168 LEU   A O     1 
ATOM   1280 C  CB    . LEU   A 1 171 ? 11.675 9.627   8.807  1.00 71.82 ? 168 LEU   A CB    1 
ATOM   1281 C  CG    . LEU   A 1 171 ? 11.686 9.644   10.332 1.00 73.02 ? 168 LEU   A CG    1 
ATOM   1282 C  CD1   . LEU   A 1 171 ? 11.846 11.062  10.842 1.00 74.74 ? 168 LEU   A CD1   1 
ATOM   1283 C  CD2   . LEU   A 1 171 ? 10.430 9.012   10.905 1.00 74.11 ? 168 LEU   A CD2   1 
ATOM   1284 N  N     . LYS   A 1 172 ? 12.111 7.456   6.005  1.00 72.69 ? 169 LYS   A N     1 
ATOM   1285 C  CA    . LYS   A 1 172 ? 12.390 7.456   4.573  1.00 75.58 ? 169 LYS   A CA    1 
ATOM   1286 C  C     . LYS   A 1 172 ? 11.162 6.996   3.773  1.00 79.66 ? 169 LYS   A C     1 
ATOM   1287 O  O     . LYS   A 1 172 ? 10.757 7.637   2.796  1.00 86.30 ? 169 LYS   A O     1 
ATOM   1288 C  CB    . LYS   A 1 172 ? 13.577 6.542   4.248  1.00 74.53 ? 169 LYS   A CB    1 
ATOM   1289 C  CG    . LYS   A 1 172 ? 14.938 7.048   4.704  1.00 74.73 ? 169 LYS   A CG    1 
ATOM   1290 C  CD    . LYS   A 1 172 ? 15.459 8.243   3.934  1.00 76.59 ? 169 LYS   A CD    1 
ATOM   1291 C  CE    . LYS   A 1 172 ? 16.626 8.926   4.619  1.00 77.20 ? 169 LYS   A CE    1 
ATOM   1292 N  NZ    . LYS   A 1 172 ? 17.648 7.960   5.093  1.00 76.30 ? 169 LYS   A NZ    1 
ATOM   1293 O  OXT   . LYS   A 1 172 ? 10.548 5.972   4.057  1.00 82.17 ? 169 LYS   A OXT   1 
HETATM 1294 P  PG    . GNP   B 2 .   ? 36.361 -10.533 20.001 1.00 37.71 ? 201 GNP   A PG    1 
HETATM 1295 O  O1G   . GNP   B 2 .   ? 35.106 -10.656 20.678 1.00 40.54 ? 201 GNP   A O1G   1 
HETATM 1296 O  O2G   . GNP   B 2 .   ? 37.069 -11.764 20.236 1.00 40.34 ? 201 GNP   A O2G   1 
HETATM 1297 O  O3G   . GNP   B 2 .   ? 36.121 -10.493 18.603 1.00 37.48 ? 201 GNP   A O3G   1 
HETATM 1298 N  N3B   . GNP   B 2 .   ? 37.140 -9.283  20.613 1.00 37.14 ? 201 GNP   A N3B   1 
HETATM 1299 P  PB    . GNP   B 2 .   ? 36.559 -7.802  20.719 1.00 35.38 ? 201 GNP   A PB    1 
HETATM 1300 O  O1B   . GNP   B 2 .   ? 36.510 -7.062  19.453 1.00 33.87 ? 201 GNP   A O1B   1 
HETATM 1301 O  O2B   . GNP   B 2 .   ? 35.359 -7.730  21.565 1.00 34.93 ? 201 GNP   A O2B   1 
HETATM 1302 O  O3A   . GNP   B 2 .   ? 37.584 -6.993  21.570 1.00 34.90 ? 201 GNP   A O3A   1 
HETATM 1303 P  PA    . GNP   B 2 .   ? 37.770 -6.713  23.109 1.00 35.73 ? 201 GNP   A PA    1 
HETATM 1304 O  O1A   . GNP   B 2 .   ? 37.752 -8.031  23.736 1.00 36.46 ? 201 GNP   A O1A   1 
HETATM 1305 O  O2A   . GNP   B 2 .   ? 36.865 -5.657  23.582 1.00 35.27 ? 201 GNP   A O2A   1 
HETATM 1306 O  "O5'" . GNP   B 2 .   ? 39.228 -6.130  23.154 1.00 37.13 ? 201 GNP   A "O5'" 1 
HETATM 1307 C  "C5'" . GNP   B 2 .   ? 40.338 -6.842  22.619 1.00 37.45 ? 201 GNP   A "C5'" 1 
HETATM 1308 C  "C4'" . GNP   B 2 .   ? 41.574 -6.200  23.183 1.00 38.74 ? 201 GNP   A "C4'" 1 
HETATM 1309 O  "O4'" . GNP   B 2 .   ? 41.582 -4.807  22.800 1.00 36.89 ? 201 GNP   A "O4'" 1 
HETATM 1310 C  "C3'" . GNP   B 2 .   ? 41.638 -6.206  24.711 1.00 40.79 ? 201 GNP   A "C3'" 1 
HETATM 1311 O  "O3'" . GNP   B 2 .   ? 42.970 -6.279  25.183 1.00 45.43 ? 201 GNP   A "O3'" 1 
HETATM 1312 C  "C2'" . GNP   B 2 .   ? 41.065 -4.838  25.064 1.00 39.99 ? 201 GNP   A "C2'" 1 
HETATM 1313 O  "O2'" . GNP   B 2 .   ? 41.473 -4.447  26.350 1.00 41.41 ? 201 GNP   A "O2'" 1 
HETATM 1314 C  "C1'" . GNP   B 2 .   ? 41.672 -4.005  23.949 1.00 38.59 ? 201 GNP   A "C1'" 1 
HETATM 1315 N  N9    . GNP   B 2 .   ? 40.994 -2.751  23.671 1.00 36.65 ? 201 GNP   A N9    1 
HETATM 1316 C  C8    . GNP   B 2 .   ? 39.675 -2.585  23.367 1.00 34.17 ? 201 GNP   A C8    1 
HETATM 1317 N  N7    . GNP   B 2 .   ? 39.349 -1.353  23.112 1.00 33.73 ? 201 GNP   A N7    1 
HETATM 1318 C  C5    . GNP   B 2 .   ? 40.530 -0.650  23.247 1.00 33.87 ? 201 GNP   A C5    1 
HETATM 1319 C  C6    . GNP   B 2 .   ? 40.789 0.731   23.085 1.00 36.00 ? 201 GNP   A C6    1 
HETATM 1320 O  O6    . GNP   B 2 .   ? 40.012 1.617   22.740 1.00 34.52 ? 201 GNP   A O6    1 
HETATM 1321 N  N1    . GNP   B 2 .   ? 42.128 1.034   23.297 1.00 36.27 ? 201 GNP   A N1    1 
HETATM 1322 C  C2    . GNP   B 2 .   ? 43.079 0.115   23.646 1.00 38.31 ? 201 GNP   A C2    1 
HETATM 1323 N  N2    . GNP   B 2 .   ? 44.314 0.581   23.838 1.00 39.62 ? 201 GNP   A N2    1 
HETATM 1324 N  N3    . GNP   B 2 .   ? 42.843 -1.183  23.805 1.00 38.10 ? 201 GNP   A N3    1 
HETATM 1325 C  C4    . GNP   B 2 .   ? 41.548 -1.502  23.596 1.00 36.36 ? 201 GNP   A C4    1 
HETATM 1326 MG MG    . MG    C 3 .   ? 34.143 -9.427  22.232 1.00 35.29 ? 202 MG    A MG    1 
HETATM 1327 CO CO    . CO    D 4 .   ? 37.998 -2.911  36.156 1.00 84.59 ? 203 CO    A CO    1 
HETATM 1328 CO CO    . CO    E 4 .   ? 33.157 -8.812  -1.632 1.00 38.47 ? 204 CO    A CO    1 
HETATM 1329 C  CBK   . A1IMA F 5 .   ? 22.203 -15.607 24.381 1.00 58.89 ? 205 A1IMA A CBK   1 
HETATM 1330 C  CBL   . A1IMA F 5 .   ? 22.383 -16.529 25.601 1.00 64.34 ? 205 A1IMA A CBL   1 
HETATM 1331 C  CBM   . A1IMA F 5 .   ? 23.826 -16.548 26.037 1.00 64.95 ? 205 A1IMA A CBM   1 
HETATM 1332 N  NBP   . A1IMA F 5 .   ? 24.215 -15.220 26.445 1.00 66.11 ? 205 A1IMA A NBP   1 
HETATM 1333 C  CBN   . A1IMA F 5 .   ? 24.693 -16.918 24.939 1.00 62.57 ? 205 A1IMA A CBN   1 
HETATM 1334 C  CBO   . A1IMA F 5 .   ? 24.540 -15.852 23.898 1.00 59.18 ? 205 A1IMA A CBO   1 
HETATM 1335 C  CBJ   . A1IMA F 5 .   ? 23.186 -16.018 23.347 1.00 57.80 ? 205 A1IMA A CBJ   1 
HETATM 1336 N  NAQ   . A1IMA F 5 .   ? 23.012 -15.312 22.068 1.00 52.12 ? 205 A1IMA A NAQ   1 
HETATM 1337 C  CAB   . A1IMA F 5 .   ? 22.549 -15.988 21.031 1.00 52.92 ? 205 A1IMA A CAB   1 
HETATM 1338 O  OAA   . A1IMA F 5 .   ? 22.266 -17.162 21.176 1.00 54.71 ? 205 A1IMA A OAA   1 
HETATM 1339 C  CAR   . A1IMA F 5 .   ? 23.278 -13.877 21.966 1.00 48.11 ? 205 A1IMA A CAR   1 
HETATM 1340 C  CAS   . A1IMA F 5 .   ? 22.188 -12.949 22.543 1.00 47.42 ? 205 A1IMA A CAS   1 
HETATM 1341 C  CAT   . A1IMA F 5 .   ? 20.935 -12.848 21.719 1.00 46.41 ? 205 A1IMA A CAT   1 
HETATM 1342 C  CAU   . A1IMA F 5 .   ? 20.046 -11.735 22.231 1.00 45.23 ? 205 A1IMA A CAU   1 
HETATM 1343 C  CAV   . A1IMA F 5 .   ? 18.759 -11.513 21.378 1.00 43.95 ? 205 A1IMA A CAV   1 
HETATM 1344 N  NAW   . A1IMA F 5 .   ? 19.005 -11.113 20.011 1.00 40.00 ? 205 A1IMA A NAW   1 
HETATM 1345 C  CAX   . A1IMA F 5 .   ? 19.329 -9.862  19.684 1.00 39.12 ? 205 A1IMA A CAX   1 
HETATM 1346 C  CAY   . A1IMA F 5 .   ? 19.482 -8.784  20.451 1.00 38.12 ? 205 A1IMA A CAY   1 
HETATM 1347 O  OBD   . A1IMA F 5 .   ? 19.282 -8.889  21.761 1.00 37.21 ? 205 A1IMA A OBD   1 
HETATM 1348 C  CAZ   . A1IMA F 5 .   ? 19.840 -7.548  19.951 1.00 35.87 ? 205 A1IMA A CAZ   1 
HETATM 1349 C  CBA   . A1IMA F 5 .   ? 20.042 -7.455  18.605 1.00 34.74 ? 205 A1IMA A CBA   1 
HETATM 1350 C  CBB   . A1IMA F 5 .   ? 19.898 -8.573  17.823 1.00 37.39 ? 205 A1IMA A CBB   1 
HETATM 1351 CL CLBC  . A1IMA F 5 .   ? 20.138 -8.431  16.228 1.00 37.84 ? 205 A1IMA A CLBC  1 
HETATM 1352 C  CBI   . A1IMA F 5 .   ? 19.522 -9.744  18.358 1.00 37.62 ? 205 A1IMA A CBI   1 
HETATM 1353 S  SBH   . A1IMA F 5 .   ? 19.278 -11.054 17.721 1.00 39.35 ? 205 A1IMA A SBH   1 
HETATM 1354 C  CBG   . A1IMA F 5 .   ? 18.950 -11.936 18.977 1.00 42.15 ? 205 A1IMA A CBG   1 
HETATM 1355 N  NBF   . A1IMA F 5 .   ? 18.636 -13.234 19.111 1.00 44.03 ? 205 A1IMA A NBF   1 
HETATM 1356 S  SAH   . A1IMA F 5 .   ? 19.017 -14.245 18.143 1.00 49.09 ? 205 A1IMA A SAH   1 
HETATM 1357 O  OAI   . A1IMA F 5 .   ? 18.668 -13.797 16.805 1.00 49.60 ? 205 A1IMA A OAI   1 
HETATM 1358 O  OBE   . A1IMA F 5 .   ? 18.273 -15.480 18.347 1.00 51.35 ? 205 A1IMA A OBE   1 
HETATM 1359 C  CAG   . A1IMA F 5 .   ? 20.588 -14.530 18.356 1.00 49.71 ? 205 A1IMA A CAG   1 
HETATM 1360 C  CAF   . A1IMA F 5 .   ? 21.570 -14.047 17.531 1.00 49.02 ? 205 A1IMA A CAF   1 
HETATM 1361 N  NAE   . A1IMA F 5 .   ? 22.885 -14.283 17.835 1.00 48.51 ? 205 A1IMA A NAE   1 
HETATM 1362 C  CAJ   . A1IMA F 5 .   ? 20.985 -15.138 19.518 1.00 50.73 ? 205 A1IMA A CAJ   1 
HETATM 1363 C  CAC   . A1IMA F 5 .   ? 22.306 -15.352 19.824 1.00 51.57 ? 205 A1IMA A CAC   1 
HETATM 1364 C  CAD   . A1IMA F 5 .   ? 23.283 -14.885 18.958 1.00 51.98 ? 205 A1IMA A CAD   1 
HETATM 1365 N  NAK   . A1IMA F 5 .   ? 24.610 -15.047 19.164 1.00 54.28 ? 205 A1IMA A NAK   1 
HETATM 1366 C  CAL   . A1IMA F 5 .   ? 25.257 -16.141 19.808 1.00 58.08 ? 205 A1IMA A CAL   1 
HETATM 1367 C  CAM   . A1IMA F 5 .   ? 25.850 -16.927 18.684 1.00 60.47 ? 205 A1IMA A CAM   1 
HETATM 1368 N  NAN   . A1IMA F 5 .   ? 26.779 -16.103 17.905 1.00 60.16 ? 205 A1IMA A NAN   1 
HETATM 1369 C  CAO   . A1IMA F 5 .   ? 26.143 -14.850 17.460 1.00 56.69 ? 205 A1IMA A CAO   1 
HETATM 1370 C  CAP   . A1IMA F 5 .   ? 25.551 -14.131 18.597 1.00 54.64 ? 205 A1IMA A CAP   1 
HETATM 1371 O  O     . HOH   G 6 .   ? 23.743 4.954   8.132  1.00 29.31 ? 301 HOH   A O     1 
HETATM 1372 O  O     . HOH   G 6 .   ? 29.801 -9.163  25.679 1.00 53.05 ? 302 HOH   A O     1 
HETATM 1373 O  O     . HOH   G 6 .   ? 34.851 -1.511  28.226 1.00 43.99 ? 303 HOH   A O     1 
HETATM 1374 O  O     . HOH   G 6 .   ? 32.589 -9.053  20.986 1.00 37.59 ? 304 HOH   A O     1 
HETATM 1375 O  O     . HOH   G 6 .   ? 31.647 8.603   25.455 1.00 42.82 ? 305 HOH   A O     1 
HETATM 1376 O  O     . HOH   G 6 .   ? 35.660 -9.603  23.759 1.00 37.83 ? 306 HOH   A O     1 
HETATM 1377 O  O     . HOH   G 6 .   ? 30.972 -3.776  0.980  1.00 33.37 ? 307 HOH   A O     1 
HETATM 1378 O  O     . HOH   G 6 .   ? 29.208 -10.198 12.149 1.00 36.18 ? 308 HOH   A O     1 
HETATM 1379 O  O     . HOH   G 6 .   ? 11.927 5.167   15.538 1.00 56.54 ? 309 HOH   A O     1 
HETATM 1380 O  O     . HOH   G 6 .   ? 30.435 9.913   5.712  1.00 37.59 ? 310 HOH   A O     1 
HETATM 1381 O  O     . HOH   G 6 .   ? 28.248 10.044  1.254  1.00 36.42 ? 311 HOH   A O     1 
HETATM 1382 O  O     . HOH   G 6 .   ? 34.468 -1.738  0.132  1.00 42.72 ? 312 HOH   A O     1 
HETATM 1383 O  O     . HOH   G 6 .   ? 26.463 11.527  21.886 1.00 45.70 ? 313 HOH   A O     1 
HETATM 1384 O  O     . HOH   G 6 .   ? 49.625 -2.054  17.694 1.00 48.49 ? 314 HOH   A O     1 
HETATM 1385 O  O     . HOH   G 6 .   ? 38.658 9.233   19.480 1.00 46.49 ? 315 HOH   A O     1 
HETATM 1386 O  O     . HOH   G 6 .   ? 7.663  9.394   19.800 1.00 67.46 ? 316 HOH   A O     1 
HETATM 1387 O  O     . HOH   G 6 .   ? 31.942 2.001   -1.789 1.00 36.94 ? 317 HOH   A O     1 
HETATM 1388 O  O     . HOH   G 6 .   ? 25.462 3.322   32.043 1.00 56.94 ? 318 HOH   A O     1 
HETATM 1389 O  O     . HOH   G 6 .   ? 24.361 8.511   6.502  1.00 46.51 ? 319 HOH   A O     1 
HETATM 1390 O  O     . HOH   G 6 .   ? 43.787 -3.881  17.217 1.00 37.98 ? 320 HOH   A O     1 
HETATM 1391 O  O     . HOH   G 6 .   ? 16.896 11.864  16.697 1.00 44.90 ? 321 HOH   A O     1 
HETATM 1392 O  O     . HOH   G 6 .   ? 42.229 8.880   1.989  1.00 37.26 ? 322 HOH   A O     1 
HETATM 1393 O  O     . HOH   G 6 .   ? 36.660 -4.976  11.461 1.00 28.26 ? 323 HOH   A O     1 
HETATM 1394 O  O     . HOH   G 6 .   ? 26.608 1.554   2.487  1.00 59.70 ? 324 HOH   A O     1 
HETATM 1395 O  O     . HOH   G 6 .   ? 33.891 11.725  23.978 1.00 48.80 ? 325 HOH   A O     1 
HETATM 1396 O  O     . HOH   G 6 .   ? 17.563 11.431  13.784 1.00 45.97 ? 326 HOH   A O     1 
HETATM 1397 O  O     . HOH   G 6 .   ? 39.124 -1.449  36.518 1.00 61.31 ? 327 HOH   A O     1 
HETATM 1398 O  O     . HOH   G 6 .   ? 24.281 1.647   4.546  1.00 40.66 ? 328 HOH   A O     1 
HETATM 1399 O  O     . HOH   G 6 .   ? 36.935 -4.311  35.895 1.00 78.95 ? 329 HOH   A O     1 
HETATM 1400 O  O     . HOH   G 6 .   ? 40.937 5.699   11.112 1.00 43.09 ? 330 HOH   A O     1 
HETATM 1401 O  O     . HOH   G 6 .   ? 25.091 11.889  16.995 1.00 46.13 ? 331 HOH   A O     1 
HETATM 1402 O  O     . HOH   G 6 .   ? 32.470 -10.652 -2.611 1.00 36.51 ? 332 HOH   A O     1 
HETATM 1403 O  O     . HOH   G 6 .   ? 25.881 -7.466  -0.620 1.00 41.92 ? 333 HOH   A O     1 
HETATM 1404 O  O     . HOH   G 6 .   ? 37.001 -5.557  33.497 1.00 73.23 ? 334 HOH   A O     1 
HETATM 1405 O  O     . HOH   G 6 .   ? 40.477 10.616  16.841 1.00 50.92 ? 335 HOH   A O     1 
HETATM 1406 O  O     . HOH   G 6 .   ? 37.091 -10.458 9.884  1.00 39.57 ? 336 HOH   A O     1 
HETATM 1407 O  O     . HOH   G 6 .   ? 31.344 -9.407  13.980 1.00 30.48 ? 337 HOH   A O     1 
HETATM 1408 O  O     . HOH   G 6 .   ? 33.090 -10.875 22.841 1.00 41.86 ? 338 HOH   A O     1 
HETATM 1409 O  O     . HOH   G 6 .   ? 42.224 -5.748  16.087 1.00 45.25 ? 339 HOH   A O     1 
HETATM 1410 O  O     . HOH   G 6 .   ? 24.338 4.276   2.943  1.00 41.88 ? 340 HOH   A O     1 
HETATM 1411 O  O     . HOH   G 6 .   ? 26.977 5.602   -1.378 1.00 51.39 ? 341 HOH   A O     1 
HETATM 1412 O  O     . HOH   G 6 .   ? 44.596 -3.234  22.319 1.00 41.28 ? 342 HOH   A O     1 
HETATM 1413 O  O     . HOH   G 6 .   ? 33.992 -13.203 21.408 1.00 53.22 ? 343 HOH   A O     1 
HETATM 1414 O  O     . HOH   G 6 .   ? 30.351 -11.736 10.019 1.00 43.23 ? 344 HOH   A O     1 
HETATM 1415 O  O     . HOH   G 6 .   ? 33.529 -9.811  0.180  1.00 45.53 ? 345 HOH   A O     1 
HETATM 1416 O  O     . HOH   G 6 .   ? 18.770 -8.077  25.633 1.00 57.70 ? 346 HOH   A O     1 
HETATM 1417 O  O     . HOH   G 6 .   ? 39.540 -7.691  3.401  1.00 36.82 ? 347 HOH   A O     1 
HETATM 1418 O  O     . HOH   G 6 .   ? 30.700 10.294  23.211 1.00 39.11 ? 348 HOH   A O     1 
HETATM 1419 O  O     . HOH   G 6 .   ? 46.950 3.923   25.429 1.00 45.97 ? 349 HOH   A O     1 
HETATM 1420 O  O     . HOH   G 6 .   ? 46.486 -1.069  24.973 1.00 48.52 ? 350 HOH   A O     1 
HETATM 1421 O  O     . HOH   G 6 .   ? 31.356 11.122  8.958  1.00 38.17 ? 351 HOH   A O     1 
HETATM 1422 O  O     . HOH   G 6 .   ? 48.112 -3.088  10.894 1.00 41.69 ? 352 HOH   A O     1 
HETATM 1423 O  O     . HOH   G 6 .   ? 39.089 -0.625  2.061  1.00 41.02 ? 353 HOH   A O     1 
HETATM 1424 O  O     . HOH   G 6 .   ? 50.000 -1.557  14.413 1.00 52.87 ? 354 HOH   A O     1 
HETATM 1425 O  O     . HOH   G 6 .   ? 12.953 -3.315  17.630 1.00 46.30 ? 355 HOH   A O     1 
HETATM 1426 O  O     . HOH   G 6 .   ? 37.344 -1.639  3.656  1.00 49.01 ? 356 HOH   A O     1 
HETATM 1427 O  O     . HOH   G 6 .   ? 23.268 4.768   5.550  1.00 40.93 ? 357 HOH   A O     1 
HETATM 1428 O  O     . HOH   G 6 .   ? 44.531 8.604   3.250  1.00 52.09 ? 358 HOH   A O     1 
HETATM 1429 O  O     . HOH   G 6 .   ? 26.365 10.104  6.321  1.00 50.98 ? 359 HOH   A O     1 
HETATM 1430 O  O     . HOH   G 6 .   ? 28.116 10.481  3.944  1.00 48.63 ? 360 HOH   A O     1 
HETATM 1431 O  O     . HOH   G 6 .   ? 14.248 12.795  16.752 1.00 54.02 ? 361 HOH   A O     1 
HETATM 1432 O  O     . HOH   G 6 .   ? 12.780 10.933  15.288 1.00 59.15 ? 362 HOH   A O     1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N  N     . MET   A 4   ? 0.4942 1.0835 0.7935 0.1126  0.1829  0.0193  1   MET   A N     
2    C  CA    . MET   A 4   ? 0.4985 1.0237 0.7550 0.1201  0.1754  0.0111  1   MET   A CA    
3    C  C     . MET   A 4   ? 0.4516 0.9376 0.7042 0.1036  0.1552  0.0185  1   MET   A C     
4    O  O     . MET   A 4   ? 0.4343 0.9274 0.6969 0.0792  0.1531  0.0310  1   MET   A O     
5    C  CB    . MET   A 4   ? 0.5429 1.0561 0.7651 0.1116  0.1884  0.0118  1   MET   A CB    
6    C  CG    . MET   A 4   ? 0.5605 1.0134 0.7428 0.1135  0.1793  0.0045  1   MET   A CG    
7    S  SD    . MET   A 4   ? 0.5946 1.0438 0.7418 0.0973  0.1903  0.0104  1   MET   A SD    
8    C  CE    . MET   A 4   ? 0.5580 1.0489 0.6999 0.1167  0.2139  -0.0036 1   MET   A CE    
9    N  N     . THR   A 5   ? 0.4172 0.8627 0.6554 0.1174  0.1423  0.0105  2   THR   A N     
10   C  CA    . THR   A 5   ? 0.4109 0.8217 0.6449 0.1047  0.1237  0.0156  2   THR   A CA    
11   C  C     . THR   A 5   ? 0.4070 0.7824 0.6144 0.0846  0.1227  0.0215  2   THR   A C     
12   O  O     . THR   A 5   ? 0.4000 0.7513 0.5779 0.0896  0.1288  0.0159  2   THR   A O     
13   C  CB    . THR   A 5   ? 0.4335 0.8094 0.6546 0.1250  0.1125  0.0073  2   THR   A CB    
14   O  OG1   . THR   A 5   ? 0.4356 0.8472 0.6848 0.1445  0.1111  0.0049  2   THR   A OG1   
15   C  CG2   . THR   A 5   ? 0.4350 0.7759 0.6470 0.1126  0.0956  0.0116  2   THR   A CG2   
16   N  N     . GLU   A 6   ? 0.3907 0.7632 0.6099 0.0636  0.1140  0.0312  3   GLU   A N     
17   C  CA    . GLU   A 6   ? 0.3788 0.7178 0.5778 0.0460  0.1112  0.0385  3   GLU   A CA    
18   C  C     . GLU   A 6   ? 0.3643 0.6649 0.5548 0.0450  0.0949  0.0350  3   GLU   A C     
19   O  O     . GLU   A 6   ? 0.3484 0.6581 0.5554 0.0499  0.0857  0.0315  3   GLU   A O     
20   C  CB    . GLU   A 6   ? 0.4035 0.7635 0.6225 0.0230  0.1154  0.0525  3   GLU   A CB    
21   C  CG    . GLU   A 6   ? 0.4635 0.8676 0.6942 0.0211  0.1327  0.0586  3   GLU   A CG    
22   C  CD    . GLU   A 6   ? 0.4750 0.8894 0.7175 -0.0037 0.1388  0.0760  3   GLU   A CD    
23   O  OE1   . GLU   A 6   ? 0.4926 0.8718 0.7258 -0.0165 0.1310  0.0830  3   GLU   A OE1   
24   O  OE2   . GLU   A 6   ? 0.5465 1.0038 0.8083 -0.0098 0.1521  0.0830  3   GLU   A OE2   
25   N  N     . TYR   A 7   ? 0.3388 0.6014 0.5032 0.0404  0.0919  0.0354  4   TYR   A N     
26   C  CA    . TYR   A 7   ? 0.3178 0.5446 0.4720 0.0382  0.0787  0.0325  4   TYR   A CA    
27   C  C     . TYR   A 7   ? 0.3278 0.5360 0.4769 0.0209  0.0770  0.0409  4   TYR   A C     
28   O  O     . TYR   A 7   ? 0.3369 0.5386 0.4699 0.0188  0.0832  0.0451  4   TYR   A O     
29   C  CB    . TYR   A 7   ? 0.3232 0.5198 0.4506 0.0525  0.0774  0.0232  4   TYR   A CB    
30   C  CG    . TYR   A 7   ? 0.3274 0.5312 0.4573 0.0726  0.0784  0.0153  4   TYR   A CG    
31   C  CD1   . TYR   A 7   ? 0.3523 0.5611 0.4956 0.0795  0.0687  0.0148  4   TYR   A CD1   
32   C  CD2   . TYR   A 7   ? 0.3482 0.5534 0.4662 0.0858  0.0888  0.0080  4   TYR   A CD2   
33   C  CE1   . TYR   A 7   ? 0.3506 0.5657 0.4972 0.1007  0.0690  0.0099  4   TYR   A CE1   
34   C  CE2   . TYR   A 7   ? 0.3594 0.5673 0.4808 0.1068  0.0905  0.0007  4   TYR   A CE2   
35   C  CZ    . TYR   A 7   ? 0.3575 0.5700 0.4940 0.1151  0.0804  0.0030  4   TYR   A CZ    
36   O  OH    . TYR   A 7   ? 0.3953 0.6102 0.5362 0.1384  0.0814  -0.0018 4   TYR   A OH    
37   N  N     . LYS   A 8   ? 0.3047 0.5066 0.4675 0.0097  0.0686  0.0429  5   LYS   A N     
38   C  CA    . LYS   A 8   ? 0.3062 0.4860 0.4654 -0.0040 0.0672  0.0503  5   LYS   A CA    
39   C  C     . LYS   A 8   ? 0.3110 0.4567 0.4489 0.0013  0.0599  0.0439  5   LYS   A C     
40   O  O     . LYS   A 8   ? 0.2980 0.4353 0.4376 0.0034  0.0516  0.0366  5   LYS   A O     
41   C  CB    . LYS   A 8   ? 0.3250 0.5113 0.5094 -0.0195 0.0632  0.0533  5   LYS   A CB    
42   C  CG    . LYS   A 8   ? 0.3458 0.5672 0.5542 -0.0291 0.0717  0.0615  5   LYS   A CG    
43   C  CD    . LYS   A 8   ? 0.3919 0.6046 0.6145 -0.0489 0.0742  0.0724  5   LYS   A CD    
44   C  CE    . LYS   A 8   ? 0.4190 0.6669 0.6662 -0.0613 0.0841  0.0822  5   LYS   A CE    
45   N  NZ    . LYS   A 8   ? 0.4306 0.7191 0.6952 -0.0544 0.0836  0.0735  5   LYS   A NZ    
46   N  N     . LEU   A 9   ? 0.3078 0.4395 0.4266 0.0032  0.0632  0.0467  6   LEU   A N     
47   C  CA    . LEU   A 9   ? 0.3224 0.4266 0.4231 0.0066  0.0579  0.0413  6   LEU   A CA    
48   C  C     . LEU   A 9   ? 0.3261 0.4160 0.4298 -0.0025 0.0559  0.0489  6   LEU   A C     
49   O  O     . LEU   A 9   ? 0.3100 0.4083 0.4198 -0.0085 0.0607  0.0604  6   LEU   A O     
50   C  CB    . LEU   A 9   ? 0.3288 0.4307 0.4083 0.0143  0.0622  0.0375  6   LEU   A CB    
51   C  CG    . LEU   A 9   ? 0.3566 0.4698 0.4324 0.0256  0.0666  0.0297  6   LEU   A CG    
52   C  CD1   . LEU   A 9   ? 0.3923 0.4942 0.4446 0.0313  0.0699  0.0220  6   LEU   A CD1   
53   C  CD2   . LEU   A 9   ? 0.3512 0.4581 0.4334 0.0323  0.0604  0.0236  6   LEU   A CD2   
54   N  N     . VAL   A 10  ? 0.3146 0.3835 0.4146 -0.0027 0.0497  0.0433  7   VAL   A N     
55   C  CA    . VAL   A 10  ? 0.3055 0.3593 0.4098 -0.0081 0.0483  0.0487  7   VAL   A CA    
56   C  C     . VAL   A 10  ? 0.3172 0.3578 0.4059 -0.0030 0.0460  0.0442  7   VAL   A C     
57   O  O     . VAL   A 10  ? 0.3211 0.3552 0.4001 0.0009  0.0436  0.0345  7   VAL   A O     
58   C  CB    . VAL   A 10  ? 0.3086 0.3527 0.4283 -0.0149 0.0443  0.0447  7   VAL   A CB    
59   C  CG1   . VAL   A 10  ? 0.3402 0.3653 0.4667 -0.0188 0.0443  0.0500  7   VAL   A CG1   
60   C  CG2   . VAL   A 10  ? 0.3280 0.3901 0.4655 -0.0222 0.0456  0.0468  7   VAL   A CG2   
61   N  N     . VAL   A 11  ? 0.3206 0.3601 0.4071 -0.0030 0.0471  0.0526  8   VAL   A N     
62   C  CA    . VAL   A 11  ? 0.3280 0.3616 0.4041 0.0004  0.0449  0.0489  8   VAL   A CA    
63   C  C     . VAL   A 11  ? 0.3133 0.3334 0.4009 0.0003  0.0429  0.0505  8   VAL   A C     
64   O  O     . VAL   A 11  ? 0.3202 0.3382 0.4186 -0.0006 0.0439  0.0617  8   VAL   A O     
65   C  CB    . VAL   A 11  ? 0.3475 0.3951 0.4131 0.0019  0.0459  0.0555  8   VAL   A CB    
66   C  CG1   . VAL   A 11  ? 0.3593 0.4055 0.4176 0.0034  0.0426  0.0503  8   VAL   A CG1   
67   C  CG2   . VAL   A 11  ? 0.3673 0.4279 0.4209 0.0027  0.0496  0.0523  8   VAL   A CG2   
68   N  N     . VAL   A 12  ? 0.3120 0.3217 0.3970 0.0015  0.0412  0.0395  9   VAL   A N     
69   C  CA    . VAL   A 12  ? 0.3094 0.3063 0.4045 0.0028  0.0407  0.0371  9   VAL   A CA    
70   C  C     . VAL   A 12  ? 0.3025 0.3021 0.3918 0.0067  0.0409  0.0327  9   VAL   A C     
71   O  O     . VAL   A 12  ? 0.3134 0.3202 0.3901 0.0055  0.0408  0.0291  9   VAL   A O     
72   C  CB    . VAL   A 12  ? 0.3030 0.2890 0.4006 -0.0005 0.0395  0.0260  9   VAL   A CB    
73   C  CG1   . VAL   A 12  ? 0.3176 0.3054 0.4251 -0.0066 0.0387  0.0288  9   VAL   A CG1   
74   C  CG2   . VAL   A 12  ? 0.3047 0.2917 0.3867 0.0005  0.0383  0.0159  9   VAL   A CG2   
75   N  N     . GLY   A 13  ? 0.3107 0.3041 0.4106 0.0109  0.0418  0.0321  10  GLY   A N     
76   C  CA    . GLY   A 13  ? 0.3268 0.3283 0.4258 0.0145  0.0428  0.0280  10  GLY   A CA    
77   C  C     . GLY   A 13  ? 0.3165 0.3198 0.4321 0.0230  0.0433  0.0347  10  GLY   A C     
78   O  O     . GLY   A 13  ? 0.3437 0.3421 0.4683 0.0260  0.0421  0.0465  10  GLY   A O     
79   N  N     . ALA   A 14  ? 0.3141 0.3254 0.4343 0.0275  0.0456  0.0284  11  ALA   A N     
80   C  CA    . ALA   A 14  ? 0.3191 0.3344 0.4578 0.0389  0.0465  0.0335  11  ALA   A CA    
81   C  C     . ALA   A 14  ? 0.3280 0.3596 0.4727 0.0437  0.0413  0.0506  11  ALA   A C     
82   O  O     . ALA   A 14  ? 0.3244 0.3707 0.4573 0.0371  0.0376  0.0550  11  ALA   A O     
83   C  CB    . ALA   A 14  ? 0.3275 0.3572 0.4705 0.0422  0.0507  0.0235  11  ALA   A CB    
84   N  N     . GLY   A 15  ? 0.3399 0.3676 0.5022 0.0563  0.0412  0.0602  12  GLY   A N     
85   C  CA    . GLY   A 15  ? 0.3520 0.3973 0.5208 0.0641  0.0356  0.0789  12  GLY   A CA    
86   C  C     . GLY   A 15  ? 0.3381 0.4210 0.5021 0.0612  0.0306  0.0784  12  GLY   A C     
87   O  O     . GLY   A 15  ? 0.3343 0.4324 0.5037 0.0608  0.0326  0.0670  12  GLY   A O     
88   N  N     . GLY   A 16  ? 0.3226 0.4215 0.4763 0.0581  0.0244  0.0906  13  GLY   A N     
89   C  CA    . GLY   A 16  ? 0.3308 0.4669 0.4805 0.0553  0.0177  0.0911  13  GLY   A CA    
90   C  C     . GLY   A 16  ? 0.3269 0.4705 0.4608 0.0394  0.0187  0.0740  13  GLY   A C     
91   O  O     . GLY   A 16  ? 0.3527 0.5264 0.4848 0.0344  0.0134  0.0711  13  GLY   A O     
92   N  N     . VAL   A 17  ? 0.3417 0.4586 0.4642 0.0312  0.0248  0.0634  14  VAL   A N     
93   C  CA    . VAL   A 17  ? 0.3203 0.4381 0.4281 0.0179  0.0266  0.0489  14  VAL   A CA    
94   C  C     . VAL   A 17  ? 0.3257 0.4516 0.4149 0.0105  0.0227  0.0497  14  VAL   A C     
95   O  O     . VAL   A 17  ? 0.3055 0.4358 0.3834 0.0000  0.0227  0.0384  14  VAL   A O     
96   C  CB    . VAL   A 17  ? 0.3142 0.4030 0.4150 0.0138  0.0335  0.0386  14  VAL   A CB    
97   C  CG1   . VAL   A 17  ? 0.3147 0.3977 0.4295 0.0198  0.0384  0.0337  14  VAL   A CG1   
98   C  CG2   . VAL   A 17  ? 0.3201 0.3881 0.4137 0.0146  0.0343  0.0433  14  VAL   A CG2   
99   N  N     . GLY   A 18  ? 0.3159 0.4408 0.4009 0.0153  0.0207  0.0625  15  GLY   A N     
100  C  CA    . GLY   A 18  ? 0.3276 0.4634 0.3938 0.0100  0.0183  0.0636  15  GLY   A CA    
101  C  C     . GLY   A 18  ? 0.3057 0.4208 0.3610 0.0080  0.0240  0.0634  15  GLY   A C     
102  O  O     . GLY   A 18  ? 0.3252 0.4440 0.3634 0.0025  0.0250  0.0565  15  GLY   A O     
103  N  N     . LYS   A 19  ? 0.3035 0.3986 0.3700 0.0122  0.0278  0.0690  16  LYS   A N     
104  C  CA    . LYS   A 19  ? 0.3087 0.3897 0.3700 0.0097  0.0328  0.0696  16  LYS   A CA    
105  C  C     . LYS   A 19  ? 0.3262 0.4238 0.3761 0.0094  0.0329  0.0805  16  LYS   A C     
106  O  O     . LYS   A 19  ? 0.3275 0.4275 0.3646 0.0058  0.0363  0.0736  16  LYS   A O     
107  C  CB    . LYS   A 19  ? 0.3227 0.3839 0.4005 0.0126  0.0353  0.0754  16  LYS   A CB    
108  C  CG    . LYS   A 19  ? 0.3324 0.3774 0.4175 0.0127  0.0364  0.0627  16  LYS   A CG    
109  C  CD    . LYS   A 19  ? 0.3042 0.3300 0.4047 0.0151  0.0383  0.0657  16  LYS   A CD    
110  C  CE    . LYS   A 19  ? 0.3345 0.3594 0.4484 0.0229  0.0372  0.0796  16  LYS   A CE    
111  N  NZ    . LYS   A 19  ? 0.3452 0.3788 0.4658 0.0300  0.0354  0.0754  16  LYS   A NZ    
112  N  N     . SER   A 20  ? 0.3372 0.4464 0.3914 0.0144  0.0298  0.0977  17  SER   A N     
113  C  CA    . SER   A 20  ? 0.3537 0.4807 0.3946 0.0143  0.0304  0.1116  17  SER   A CA    
114  C  C     . SER   A 20  ? 0.3813 0.5320 0.4006 0.0107  0.0274  0.1012  17  SER   A C     
115  O  O     . SER   A 20  ? 0.3687 0.5270 0.3726 0.0077  0.0321  0.0996  17  SER   A O     
116  C  CB    . SER   A 20  ? 0.3819 0.5147 0.4311 0.0217  0.0267  0.1340  17  SER   A CB    
117  O  OG    . SER   A 20  ? 0.3880 0.4941 0.4563 0.0240  0.0306  0.1416  17  SER   A OG    
118  N  N     . ALA   A 21  ? 0.3547 0.5170 0.3742 0.0102  0.0203  0.0927  18  ALA   A N     
119  C  CA    . ALA   A 21  ? 0.3597 0.5434 0.3592 0.0041  0.0164  0.0797  18  ALA   A CA    
120  C  C     . ALA   A 21  ? 0.3513 0.5182 0.3391 -0.0022 0.0233  0.0600  18  ALA   A C     
121  O  O     . ALA   A 21  ? 0.3767 0.5555 0.3444 -0.0056 0.0243  0.0518  18  ALA   A O     
122  C  CB    . ALA   A 21  ? 0.3595 0.5576 0.3672 0.0021  0.0081  0.0727  18  ALA   A CB    
123  N  N     . LEU   A 22  ? 0.3449 0.4855 0.3443 -0.0025 0.0277  0.0527  19  LEU   A N     
124  C  CA    . LEU   A 22  ? 0.3498 0.4735 0.3390 -0.0056 0.0338  0.0366  19  LEU   A CA    
125  C  C     . LEU   A 22  ? 0.3731 0.4998 0.3556 -0.0020 0.0406  0.0419  19  LEU   A C     
126  O  O     . LEU   A 22  ? 0.3832 0.5117 0.3501 -0.0026 0.0450  0.0304  19  LEU   A O     
127  C  CB    . LEU   A 22  ? 0.3683 0.4663 0.3706 -0.0053 0.0360  0.0313  19  LEU   A CB    
128  C  CG    . LEU   A 22  ? 0.3473 0.4390 0.3508 -0.0113 0.0332  0.0199  19  LEU   A CG    
129  C  CD1   . LEU   A 22  ? 0.3515 0.4220 0.3670 -0.0095 0.0357  0.0194  19  LEU   A CD1   
130  C  CD2   . LEU   A 22  ? 0.3734 0.4576 0.3594 -0.0178 0.0350  0.0032  19  LEU   A CD2   
131  N  N     . THR   A 23  ? 0.3889 0.5148 0.3850 0.0013  0.0427  0.0583  20  THR   A N     
132  C  CA    . THR   A 23  ? 0.3938 0.5257 0.3879 0.0027  0.0505  0.0649  20  THR   A CA    
133  C  C     . THR   A 23  ? 0.4253 0.5834 0.3987 0.0025  0.0523  0.0688  20  THR   A C     
134  O  O     . THR   A 23  ? 0.4090 0.5738 0.3707 0.0033  0.0593  0.0601  20  THR   A O     
135  C  CB    . THR   A 23  ? 0.3884 0.5132 0.4026 0.0031  0.0521  0.0822  20  THR   A CB    
136  O  OG1   . THR   A 23  ? 0.3698 0.4724 0.3990 0.0030  0.0502  0.0743  20  THR   A OG1   
137  C  CG2   . THR   A 23  ? 0.3978 0.5321 0.4139 0.0018  0.0608  0.0896  20  THR   A CG2   
138  N  N     . ILE   A 24  ? 0.4090 0.5831 0.3775 0.0025  0.0458  0.0813  21  ILE   A N     
139  C  CA    . ILE   A 24  ? 0.4432 0.6465 0.3883 0.0023  0.0457  0.0871  21  ILE   A CA    
140  C  C     . ILE   A 24  ? 0.4552 0.6657 0.3784 -0.0010 0.0448  0.0623  21  ILE   A C     
141  O  O     . ILE   A 24  ? 0.4608 0.6896 0.3628 -0.0011 0.0498  0.0585  21  ILE   A O     
142  C  CB    . ILE   A 24  ? 0.4587 0.6779 0.4049 0.0048  0.0365  0.1073  21  ILE   A CB    
143  C  CG1   . ILE   A 24  ? 0.4549 0.6604 0.4219 0.0084  0.0390  0.1317  21  ILE   A CG1   
144  C  CG2   . ILE   A 24  ? 0.4898 0.7424 0.4082 0.0045  0.0344  0.1125  21  ILE   A CG2   
145  C  CD1   . ILE   A 24  ? 0.5006 0.7070 0.4660 0.0062  0.0504  0.1425  21  ILE   A CD1   
146  N  N     . GLN   A 25  ? 0.4425 0.6379 0.3706 -0.0044 0.0395  0.0457  22  GLN   A N     
147  C  CA    . GLN   A 25  ? 0.4680 0.6626 0.3771 -0.0097 0.0391  0.0203  22  GLN   A CA    
148  C  C     . GLN   A 25  ? 0.4844 0.6655 0.3863 -0.0058 0.0509  0.0080  22  GLN   A C     
149  O  O     . GLN   A 25  ? 0.4805 0.6713 0.3595 -0.0068 0.0545  -0.0073 22  GLN   A O     
150  C  CB    . GLN   A 25  ? 0.4747 0.6531 0.3953 -0.0155 0.0324  0.0094  22  GLN   A CB    
151  C  CG    . GLN   A 25  ? 0.5144 0.6898 0.4183 -0.0246 0.0303  -0.0156 22  GLN   A CG    
152  C  CD    . GLN   A 25  ? 0.5489 0.7578 0.4310 -0.0295 0.0240  -0.0203 22  GLN   A CD    
153  O  OE1   . GLN   A 25  ? 0.5469 0.7615 0.4066 -0.0291 0.0293  -0.0316 22  GLN   A OE1   
154  N  NE2   . GLN   A 25  ? 0.5095 0.7437 0.3975 -0.0336 0.0124  -0.0125 22  GLN   A NE2   
155  N  N     . LEU   A 26  ? 0.4555 0.6179 0.3761 -0.0010 0.0564  0.0136  23  LEU   A N     
156  C  CA    . LEU   A 26  ? 0.4690 0.6238 0.3868 0.0051  0.0671  0.0035  23  LEU   A CA    
157  C  C     . LEU   A 26  ? 0.4572 0.6410 0.3653 0.0079  0.0750  0.0135  23  LEU   A C     
158  O  O     . LEU   A 26  ? 0.5079 0.6983 0.4003 0.0115  0.0828  -0.0006 23  LEU   A O     
159  C  CB    . LEU   A 26  ? 0.4447 0.5792 0.3864 0.0091  0.0691  0.0088  23  LEU   A CB    
160  C  CG    . LEU   A 26  ? 0.4540 0.5804 0.3971 0.0174  0.0780  -0.0025 23  LEU   A CG    
161  C  CD1   . LEU   A 26  ? 0.4749 0.5734 0.4092 0.0190  0.0771  -0.0224 23  LEU   A CD1   
162  C  CD2   . LEU   A 26  ? 0.4301 0.5538 0.3977 0.0209  0.0796  0.0090  23  LEU   A CD2   
163  N  N     . ILE   A 27  ? 0.4387 0.6366 0.3564 0.0065  0.0740  0.0373  24  ILE   A N     
164  C  CA    . ILE   A 27  ? 0.4501 0.6757 0.3596 0.0076  0.0832  0.0511  24  ILE   A CA    
165  C  C     . ILE   A 27  ? 0.4876 0.7402 0.3651 0.0061  0.0827  0.0474  24  ILE   A C     
166  O  O     . ILE   A 27  ? 0.4979 0.7660 0.3594 0.0091  0.0933  0.0378  24  ILE   A O     
167  C  CB    . ILE   A 27  ? 0.4431 0.6700 0.3728 0.0051  0.0827  0.0791  24  ILE   A CB    
168  C  CG1   . ILE   A 27  ? 0.4423 0.6473 0.4009 0.0055  0.0845  0.0788  24  ILE   A CG1   
169  C  CG2   . ILE   A 27  ? 0.4621 0.7170 0.3820 0.0038  0.0922  0.0975  24  ILE   A CG2   
170  C  CD1   . ILE   A 27  ? 0.4344 0.6440 0.3974 0.0098  0.0947  0.0660  24  ILE   A CD1   
171  N  N     . GLN   A 28  ? 0.4823 0.7414 0.3505 0.0023  0.0706  0.0513  25  GLN   A N     
172  C  CA    . GLN   A 28  ? 0.5166 0.8076 0.3528 0.0004  0.0684  0.0499  25  GLN   A CA    
173  C  C     . GLN   A 28  ? 0.5354 0.8251 0.3525 -0.0040 0.0615  0.0209  25  GLN   A C     
174  O  O     . GLN   A 28  ? 0.5468 0.8641 0.3356 -0.0065 0.0590  0.0159  25  GLN   A O     
175  C  CB    . GLN   A 28  ? 0.5214 0.8290 0.3586 -0.0005 0.0576  0.0766  25  GLN   A CB    
176  C  CG    . GLN   A 28  ? 0.5280 0.8315 0.3846 0.0020  0.0630  0.1073  25  GLN   A CG    
177  C  CD    . GLN   A 28  ? 0.5515 0.8679 0.4078 0.0038  0.0527  0.1347  25  GLN   A CD    
178  O  OE1   . GLN   A 28  ? 0.6148 0.9496 0.4566 0.0039  0.0408  0.1315  25  GLN   A OE1   
179  N  NE2   . GLN   A 28  ? 0.5703 0.8776 0.4436 0.0054  0.0570  0.1623  25  GLN   A NE2   
180  N  N     . ASN   A 29  ? 0.5326 0.7924 0.3648 -0.0065 0.0571  0.0047  26  ASN   A N     
181  C  CA    . ASN   A 29  ? 0.5732 0.8262 0.3924 -0.0143 0.0496  -0.0218 26  ASN   A CA    
182  C  C     . ASN   A 29  ? 0.5332 0.8132 0.3469 -0.0209 0.0345  -0.0141 26  ASN   A C     
183  O  O     . ASN   A 29  ? 0.5504 0.8400 0.3463 -0.0292 0.0282  -0.0347 26  ASN   A O     
184  C  CB    . ASN   A 29  ? 0.6649 0.9192 0.4551 -0.0150 0.0576  -0.0506 26  ASN   A CB    
185  C  CG    . ASN   A 29  ? 0.7255 0.9442 0.5253 -0.0087 0.0689  -0.0665 26  ASN   A CG    
186  O  OD1   . ASN   A 29  ? 0.8268 1.0387 0.6444 -0.0001 0.0769  -0.0530 26  ASN   A OD1   
187  N  ND2   . ASN   A 29  ? 0.8107 1.0066 0.5993 -0.0130 0.0693  -0.0948 26  ASN   A ND2   
188  N  N     . HIS   A 30  ? 0.5000 0.7900 0.3308 -0.0170 0.0288  0.0140  27  HIS   A N     
189  C  CA    . HIS   A 30  ? 0.5231 0.8434 0.3522 -0.0190 0.0142  0.0270  27  HIS   A CA    
190  C  C     . HIS   A 30  ? 0.4904 0.7951 0.3530 -0.0165 0.0084  0.0406  27  HIS   A C     
191  O  O     . HIS   A 30  ? 0.4699 0.7497 0.3516 -0.0110 0.0160  0.0514  27  HIS   A O     
192  C  CB    . HIS   A 30  ? 0.5319 0.8831 0.3449 -0.0127 0.0148  0.0530  27  HIS   A CB    
193  C  CG    . HIS   A 30  ? 0.5522 0.9406 0.3566 -0.0128 -0.0010 0.0658  27  HIS   A CG    
194  N  ND1   . HIS   A 30  ? 0.5735 0.9902 0.3541 -0.0209 -0.0109 0.0457  27  HIS   A ND1   
195  C  CD2   . HIS   A 30  ? 0.5551 0.9578 0.3721 -0.0050 -0.0093 0.0964  27  HIS   A CD2   
196  C  CE1   . HIS   A 30  ? 0.5959 1.0472 0.3759 -0.0181 -0.0256 0.0640  27  HIS   A CE1   
197  N  NE2   . HIS   A 30  ? 0.5852 1.0277 0.3871 -0.0071 -0.0246 0.0959  27  HIS   A NE2   
198  N  N     . PHE   A 31  ? 0.5058 0.8288 0.3745 -0.0207 -0.0048 0.0382  28  PHE   A N     
199  C  CA    . PHE   A 31  ? 0.4867 0.8024 0.3865 -0.0176 -0.0107 0.0491  28  PHE   A CA    
200  C  C     . PHE   A 31  ? 0.5115 0.8491 0.4193 -0.0062 -0.0173 0.0808  28  PHE   A C     
201  O  O     . PHE   A 31  ? 0.5128 0.8880 0.4058 -0.0052 -0.0276 0.0885  28  PHE   A O     
202  C  CB    . PHE   A 31  ? 0.4906 0.8191 0.3963 -0.0285 -0.0207 0.0298  28  PHE   A CB    
203  C  CG    . PHE   A 31  ? 0.4626 0.7891 0.4010 -0.0254 -0.0255 0.0385  28  PHE   A CG    
204  C  CD1   . PHE   A 31  ? 0.4505 0.7400 0.4090 -0.0224 -0.0164 0.0390  28  PHE   A CD1   
205  C  CD2   . PHE   A 31  ? 0.4852 0.8504 0.4343 -0.0248 -0.0391 0.0451  28  PHE   A CD2   
206  C  CE1   . PHE   A 31  ? 0.4269 0.7166 0.4134 -0.0189 -0.0193 0.0451  28  PHE   A CE1   
207  C  CE2   . PHE   A 31  ? 0.4499 0.8164 0.4305 -0.0200 -0.0419 0.0522  28  PHE   A CE2   
208  C  CZ    . PHE   A 31  ? 0.4237 0.7515 0.4221 -0.0174 -0.0312 0.0513  28  PHE   A CZ    
209  N  N     . VAL   A 32  ? 0.5476 0.8602 0.4779 0.0023  -0.0115 0.0982  29  VAL   A N     
210  C  CA    . VAL   A 32  ? 0.6143 0.9358 0.5556 0.0146  -0.0155 0.1299  29  VAL   A CA    
211  C  C     . VAL   A 32  ? 0.6577 1.0066 0.6135 0.0193  -0.0299 0.1347  29  VAL   A C     
212  O  O     . VAL   A 32  ? 0.6774 1.0247 0.6480 0.0138  -0.0328 0.1165  29  VAL   A O     
213  C  CB    . VAL   A 32  ? 0.6223 0.9052 0.5875 0.0205  -0.0060 0.1416  29  VAL   A CB    
214  C  CG1   . VAL   A 32  ? 0.6425 0.9072 0.5973 0.0172  0.0070  0.1432  29  VAL   A CG1   
215  C  CG2   . VAL   A 32  ? 0.6164 0.8767 0.6047 0.0182  -0.0051 0.1244  29  VAL   A CG2   
216  N  N     . ASP   A 33  ? 0.7180 1.0912 0.6713 0.0303  -0.0377 0.1614  30  ASP   A N     
217  C  CA    . ASP   A 33  ? 0.7309 1.1353 0.7017 0.0390  -0.0522 0.1707  30  ASP   A CA    
218  C  C     . ASP   A 33  ? 0.7586 1.1476 0.7501 0.0573  -0.0513 0.2028  30  ASP   A C     
219  O  O     . ASP   A 33  ? 0.7204 1.0722 0.7134 0.0590  -0.0392 0.2133  30  ASP   A O     
220  C  CB    . ASP   A 33  ? 0.7749 1.2311 0.7203 0.0357  -0.0661 0.1704  30  ASP   A CB    
221  C  CG    . ASP   A 33  ? 0.7826 1.2483 0.6975 0.0400  -0.0639 0.1923  30  ASP   A CG    
222  O  OD1   . ASP   A 33  ? 0.7827 1.2209 0.7039 0.0492  -0.0551 0.2164  30  ASP   A OD1   
223  O  OD2   . ASP   A 33  ? 0.8156 1.3154 0.7004 0.0328  -0.0704 0.1840  30  ASP   A OD2   
224  N  N     . GLU   A 34  ? 0.7996 1.2170 0.8083 0.0704  -0.0639 0.2171  31  GLU   A N     
225  C  CA    . GLU   A 34  ? 0.8354 1.2382 0.8657 0.0912  -0.0644 0.2483  31  GLU   A CA    
226  C  C     . GLU   A 34  ? 0.8834 1.2672 0.8935 0.0946  -0.0575 0.2755  31  GLU   A C     
227  O  O     . GLU   A 34  ? 0.9176 1.2578 0.9436 0.1004  -0.0471 0.2877  31  GLU   A O     
228  C  CB    . GLU   A 34  ? 0.8481 1.2996 0.8879 0.1061  -0.0819 0.2646  31  GLU   A CB    
229  C  CG    . GLU   A 34  ? 0.8768 1.3807 0.8841 0.0992  -0.0950 0.2650  31  GLU   A CG    
230  C  CD    . GLU   A 34  ? 0.8765 1.3881 0.8527 0.1055  -0.0963 0.2956  31  GLU   A CD    
231  O  OE1   . GLU   A 34  ? 0.8383 1.3659 0.7798 0.0917  -0.0954 0.2855  31  GLU   A OE1   
232  O  OE2   . GLU   A 34  ? 0.8911 1.3926 0.8778 0.1246  -0.0977 0.3295  31  GLU   A OE2   
233  N  N     . GLU   A 40  ? 0.7547 0.7742 0.8713 0.0126  0.0547  0.2179  37  GLU   A N     
234  C  CA    . GLU   A 40  ? 0.7535 0.7649 0.8786 -0.0003 0.0596  0.1989  37  GLU   A CA    
235  C  C     . GLU   A 40  ? 0.6975 0.7265 0.8163 -0.0120 0.0678  0.2092  37  GLU   A C     
236  O  O     . GLU   A 40  ? 0.6922 0.7089 0.8189 -0.0181 0.0738  0.2306  37  GLU   A O     
237  C  CB    . GLU   A 40  ? 0.8035 0.7768 0.9516 -0.0042 0.0613  0.1946  37  GLU   A CB    
238  C  CG    . GLU   A 40  ? 0.8018 0.7632 0.9559 0.0025  0.0560  0.1711  37  GLU   A CG    
239  C  CD    . GLU   A 40  ? 0.8190 0.7463 0.9921 -0.0040 0.0581  0.1599  37  GLU   A CD    
240  O  OE1   . GLU   A 40  ? 0.8479 0.7506 1.0334 -0.0085 0.0623  0.1749  37  GLU   A OE1   
241  O  OE2   . GLU   A 40  ? 0.7050 0.6296 0.8794 -0.0052 0.0557  0.1364  37  GLU   A OE2   
242  N  N     . ASP   A 41  ? 0.6075 0.6632 0.7135 -0.0144 0.0689  0.1943  38  ASP   A N     
243  C  CA    . ASP   A 41  ? 0.5853 0.6634 0.6863 -0.0237 0.0782  0.2015  38  ASP   A CA    
244  C  C     . ASP   A 41  ? 0.5085 0.6034 0.6071 -0.0255 0.0792  0.1769  38  ASP   A C     
245  O  O     . ASP   A 41  ? 0.4341 0.5206 0.5328 -0.0204 0.0726  0.1572  38  ASP   A O     
246  C  CB    . ASP   A 41  ? 0.6272 0.7295 0.7056 -0.0196 0.0805  0.2214  38  ASP   A CB    
247  C  CG    . ASP   A 41  ? 0.6861 0.7997 0.7656 -0.0304 0.0924  0.2427  38  ASP   A CG    
248  O  OD1   . ASP   A 41  ? 0.6739 0.7842 0.7718 -0.0417 0.0990  0.2372  38  ASP   A OD1   
249  O  OD2   . ASP   A 41  ? 0.7495 0.8778 0.8113 -0.0278 0.0950  0.2648  38  ASP   A OD2   
250  N  N     . SER   A 42  ? 0.4866 0.6048 0.5841 -0.0322 0.0883  0.1803  39  SER   A N     
251  C  CA    . SER   A 42  ? 0.4623 0.6000 0.5592 -0.0318 0.0911  0.1603  39  SER   A CA    
252  C  C     . SER   A 42  ? 0.4484 0.6168 0.5212 -0.0267 0.0971  0.1609  39  SER   A C     
253  O  O     . SER   A 42  ? 0.4627 0.6413 0.5231 -0.0278 0.1010  0.1802  39  SER   A O     
254  C  CB    . SER   A 42  ? 0.4609 0.6030 0.5821 -0.0426 0.0964  0.1584  39  SER   A CB    
255  O  OG    . SER   A 42  ? 0.4654 0.6249 0.5911 -0.0522 0.1075  0.1782  39  SER   A OG    
256  N  N     . TYR   A 43  ? 0.4398 0.6181 0.5036 -0.0198 0.0964  0.1394  40  TYR   A N     
257  C  CA    . TYR   A 43  ? 0.4597 0.6629 0.4984 -0.0135 0.1017  0.1327  40  TYR   A CA    
258  C  C     . TYR   A 43  ? 0.4660 0.6852 0.5122 -0.0104 0.1089  0.1169  40  TYR   A C     
259  O  O     . TYR   A 43  ? 0.4189 0.6264 0.4843 -0.0104 0.1051  0.1075  40  TYR   A O     
260  C  CB    . TYR   A 43  ? 0.4817 0.6752 0.5000 -0.0061 0.0922  0.1197  40  TYR   A CB    
261  C  CG    . TYR   A 43  ? 0.5050 0.6876 0.5200 -0.0068 0.0841  0.1349  40  TYR   A CG    
262  C  CD1   . TYR   A 43  ? 0.4940 0.6502 0.5263 -0.0071 0.0762  0.1356  40  TYR   A CD1   
263  C  CD2   . TYR   A 43  ? 0.5494 0.7506 0.5439 -0.0058 0.0844  0.1491  40  TYR   A CD2   
264  C  CE1   . TYR   A 43  ? 0.5168 0.6644 0.5496 -0.0051 0.0698  0.1504  40  TYR   A CE1   
265  C  CE2   . TYR   A 43  ? 0.5583 0.7526 0.5518 -0.0039 0.0762  0.1653  40  TYR   A CE2   
266  C  CZ    . TYR   A 43  ? 0.5570 0.7240 0.5712 -0.0027 0.0692  0.1659  40  TYR   A CZ    
267  O  OH    . TYR   A 43  ? 0.5611 0.7224 0.5768 0.0019  0.0618  0.1820  40  TYR   A OH    
268  N  N     . ARG   A 44  ? 0.4921 0.7391 0.5224 -0.0067 0.1190  0.1143  41  ARG   A N     
269  C  CA    . ARG   A 44  ? 0.5086 0.7747 0.5468 -0.0005 0.1277  0.0994  41  ARG   A CA    
270  C  C     . ARG   A 44  ? 0.5086 0.7829 0.5189 0.0106  0.1313  0.0813  41  ARG   A C     
271  O  O     . ARG   A 44  ? 0.5259 0.8105 0.5112 0.0096  0.1333  0.0857  41  ARG   A O     
272  C  CB    . ARG   A 44  ? 0.5588 0.8561 0.6141 -0.0082 0.1409  0.1141  41  ARG   A CB    
273  C  CG    . ARG   A 44  ? 0.5936 0.8837 0.6840 -0.0179 0.1377  0.1204  41  ARG   A CG    
274  C  CD    . ARG   A 44  ? 0.6336 0.9442 0.7372 -0.0324 0.1486  0.1434  41  ARG   A CD    
275  N  NE    . ARG   A 44  ? 0.6544 1.0035 0.7771 -0.0334 0.1610  0.1402  41  ARG   A NE    
276  C  CZ    . ARG   A 44  ? 0.6600 1.0163 0.8157 -0.0387 0.1589  0.1353  41  ARG   A CZ    
277  N  NH1   . ARG   A 44  ? 0.6287 0.9540 0.7977 -0.0431 0.1450  0.1314  41  ARG   A NH1   
278  N  NH2   . ARG   A 44  ? 0.6538 1.0516 0.8292 -0.0389 0.1705  0.1331  41  ARG   A NH2   
279  N  N     . LYS   A 45  ? 0.4967 0.7668 0.5122 0.0209  0.1321  0.0616  42  LYS   A N     
280  C  CA    . LYS   A 45  ? 0.5237 0.7936 0.5143 0.0321  0.1359  0.0405  42  LYS   A CA    
281  C  C     . LYS   A 45  ? 0.4960 0.7688 0.5011 0.0453  0.1414  0.0246  42  LYS   A C     
282  O  O     . LYS   A 45  ? 0.4720 0.7283 0.4973 0.0476  0.1339  0.0232  42  LYS   A O     
283  C  CB    . LYS   A 45  ? 0.5250 0.7631 0.4975 0.0311  0.1232  0.0313  42  LYS   A CB    
284  C  CG    . LYS   A 45  ? 0.5687 0.8020 0.5125 0.0378  0.1255  0.0094  42  LYS   A CG    
285  C  CD    . LYS   A 45  ? 0.5998 0.8020 0.5329 0.0342  0.1128  0.0003  42  LYS   A CD    
286  C  CE    . LYS   A 45  ? 0.6509 0.8391 0.5608 0.0395  0.1144  -0.0253 42  LYS   A CE    
287  N  NZ    . LYS   A 45  ? 0.6820 0.8815 0.5641 0.0318  0.1109  -0.0297 42  LYS   A NZ    
288  N  N     . GLN   A 46  ? 0.4946 0.7895 0.4880 0.0550  0.1544  0.0130  43  GLN   A N     
289  C  CA    . GLN   A 46  ? 0.4849 0.7843 0.4921 0.0714  0.1607  -0.0022 43  GLN   A CA    
290  C  C     . GLN   A 46  ? 0.5099 0.7767 0.4929 0.0822  0.1580  -0.0255 43  GLN   A C     
291  O  O     . GLN   A 46  ? 0.5290 0.7935 0.4820 0.0795  0.1605  -0.0345 43  GLN   A O     
292  C  CB    . GLN   A 46  ? 0.4981 0.8437 0.5118 0.0767  0.1787  -0.0012 43  GLN   A CB    
293  C  CG    . GLN   A 46  ? 0.5024 0.8586 0.5350 0.0966  0.1860  -0.0161 43  GLN   A CG    
294  C  CD    . GLN   A 46  ? 0.5099 0.9135 0.5450 0.1043  0.2061  -0.0194 43  GLN   A CD    
295  O  OE1   . GLN   A 46  ? 0.4868 0.9284 0.5383 0.0932  0.2139  -0.0019 43  GLN   A OE1   
296  N  NE2   . GLN   A 46  ? 0.5437 0.9446 0.5638 0.1235  0.2155  -0.0425 43  GLN   A NE2   
297  N  N     . VAL   A 47  ? 0.4971 0.7372 0.4922 0.0928  0.1518  -0.0341 44  VAL   A N     
298  C  CA    . VAL   A 47  ? 0.5254 0.7266 0.5001 0.1009  0.1488  -0.0540 44  VAL   A CA    
299  C  C     . VAL   A 47  ? 0.5419 0.7359 0.5318 0.1222  0.1534  -0.0645 44  VAL   A C     
300  O  O     . VAL   A 47  ? 0.5418 0.7584 0.5607 0.1283  0.1536  -0.0543 44  VAL   A O     
301  C  CB    . VAL   A 47  ? 0.5350 0.6992 0.5041 0.0891  0.1333  -0.0497 44  VAL   A CB    
302  C  CG1   . VAL   A 47  ? 0.5212 0.6956 0.4799 0.0709  0.1279  -0.0372 44  VAL   A CG1   
303  C  CG2   . VAL   A 47  ? 0.5115 0.6648 0.5063 0.0911  0.1243  -0.0389 44  VAL   A CG2   
304  N  N     . VAL   A 48  ? 0.5928 0.7559 0.5634 0.1334  0.1568  -0.0852 45  VAL   A N     
305  C  CA    . VAL   A 48  ? 0.6155 0.7583 0.5968 0.1554  0.1592  -0.0949 45  VAL   A CA    
306  C  C     . VAL   A 48  ? 0.6221 0.7127 0.5953 0.1511  0.1463  -0.0951 45  VAL   A C     
307  O  O     . VAL   A 48  ? 0.6527 0.7149 0.6014 0.1393  0.1434  -0.1048 45  VAL   A O     
308  C  CB    . VAL   A 48  ? 0.6639 0.8038 0.6287 0.1723  0.1744  -0.1190 45  VAL   A CB    
309  C  CG1   . VAL   A 48  ? 0.6995 0.8009 0.6690 0.1955  0.1756  -0.1308 45  VAL   A CG1   
310  C  CG2   . VAL   A 48  ? 0.6782 0.8743 0.6524 0.1790  0.1897  -0.1188 45  VAL   A CG2   
311  N  N     . ILE   A 49  ? 0.6114 0.6936 0.6054 0.1595  0.1386  -0.0839 46  ILE   A N     
312  C  CA    . ILE   A 49  ? 0.5908 0.6248 0.5779 0.1590  0.1285  -0.0825 46  ILE   A CA    
313  C  C     . ILE   A 49  ? 0.6057 0.6265 0.6054 0.1854  0.1306  -0.0843 46  ILE   A C     
314  O  O     . ILE   A 49  ? 0.5712 0.6273 0.5970 0.1970  0.1299  -0.0744 46  ILE   A O     
315  C  CB    . ILE   A 49  ? 0.5659 0.6054 0.5636 0.1424  0.1151  -0.0636 46  ILE   A CB    
316  C  CG1   . ILE   A 49  ? 0.5463 0.5986 0.5342 0.1193  0.1127  -0.0596 46  ILE   A CG1   
317  C  CG2   . ILE   A 49  ? 0.5786 0.5748 0.5707 0.1437  0.1059  -0.0596 46  ILE   A CG2   
318  C  CD1   . ILE   A 49  ? 0.5219 0.5958 0.5279 0.1067  0.1041  -0.0414 46  ILE   A CD1   
319  N  N     . ASP   A 50  ? 0.6560 0.6266 0.6382 0.1945  0.1330  -0.0967 47  ASP   A N     
320  C  CA    . ASP   A 50  ? 0.6808 0.6283 0.6715 0.2219  0.1350  -0.0976 47  ASP   A CA    
321  C  C     . ASP   A 50  ? 0.6915 0.6848 0.7047 0.2446  0.1450  -0.1011 47  ASP   A C     
322  O  O     . ASP   A 50  ? 0.6868 0.6950 0.7230 0.2645  0.1415  -0.0907 47  ASP   A O     
323  C  CB    . ASP   A 50  ? 0.6737 0.6067 0.6739 0.2232  0.1212  -0.0776 47  ASP   A CB    
324  C  CG    . ASP   A 50  ? 0.6707 0.5621 0.6499 0.2009  0.1135  -0.0740 47  ASP   A CG    
325  O  OD1   . ASP   A 50  ? 0.7363 0.5894 0.6937 0.1938  0.1190  -0.0888 47  ASP   A OD1   
326  O  OD2   . ASP   A 50  ? 0.6305 0.5302 0.6158 0.1902  0.1024  -0.0578 47  ASP   A OD2   
327  N  N     . GLY   A 51  ? 0.7057 0.7267 0.7123 0.2405  0.1571  -0.1147 48  GLY   A N     
328  C  CA    . GLY   A 51  ? 0.7271 0.7895 0.7511 0.2624  0.1708  -0.1225 48  GLY   A CA    
329  C  C     . GLY   A 51  ? 0.6870 0.8135 0.7449 0.2615  0.1680  -0.1044 48  GLY   A C     
330  O  O     . GLY   A 51  ? 0.7072 0.8755 0.7865 0.2800  0.1787  -0.1078 48  GLY   A O     
331  N  N     . GLU   A 52  ? 0.6612 0.7957 0.7254 0.2396  0.1541  -0.0863 49  GLU   A N     
332  C  CA    . GLU   A 52  ? 0.6328 0.8254 0.7261 0.2307  0.1517  -0.0711 49  GLU   A CA    
333  C  C     . GLU   A 52  ? 0.6045 0.8144 0.6847 0.2036  0.1551  -0.0685 49  GLU   A C     
334  O  O     . GLU   A 52  ? 0.6376 0.8137 0.6936 0.1862  0.1487  -0.0688 49  GLU   A O     
335  C  CB    . GLU   A 52  ? 0.6329 0.8259 0.7444 0.2265  0.1343  -0.0536 49  GLU   A CB    
336  C  CG    . GLU   A 52  ? 0.6771 0.8551 0.8001 0.2538  0.1283  -0.0517 49  GLU   A CG    
337  C  CD    . GLU   A 52  ? 0.7288 0.9514 0.8832 0.2814  0.1353  -0.0533 49  GLU   A CD    
338  O  OE1   . GLU   A 52  ? 0.7582 1.0382 0.9354 0.2763  0.1429  -0.0520 49  GLU   A OE1   
339  O  OE2   . GLU   A 52  ? 0.7635 0.9638 0.9204 0.3086  0.1337  -0.0550 49  GLU   A OE2   
340  N  N     . THR   A 53  ? 0.5538 0.8180 0.6512 0.2006  0.1655  -0.0647 50  THR   A N     
341  C  CA    . THR   A 53  ? 0.5409 0.8256 0.6281 0.1764  0.1694  -0.0577 50  THR   A CA    
342  C  C     . THR   A 53  ? 0.5019 0.8000 0.6096 0.1567  0.1568  -0.0374 50  THR   A C     
343  O  O     . THR   A 53  ? 0.5240 0.8448 0.6620 0.1625  0.1517  -0.0302 50  THR   A O     
344  C  CB    . THR   A 53  ? 0.5456 0.8804 0.6384 0.1817  0.1887  -0.0622 50  THR   A CB    
345  O  OG1   . THR   A 53  ? 0.5901 0.9098 0.6643 0.2029  0.2006  -0.0847 50  THR   A OG1   
346  C  CG2   . THR   A 53  ? 0.5366 0.8914 0.6146 0.1581  0.1937  -0.0527 50  THR   A CG2   
347  N  N     . CYS   A 54  ? 0.4921 0.7764 0.5837 0.1341  0.1514  -0.0291 51  CYS   A N     
348  C  CA    . CYS   A 54  ? 0.4729 0.7674 0.5838 0.1156  0.1413  -0.0117 51  CYS   A CA    
349  C  C     . CYS   A 54  ? 0.4527 0.7483 0.5492 0.0940  0.1428  -0.0013 51  CYS   A C     
350  O  O     . CYS   A 54  ? 0.4672 0.7473 0.5347 0.0923  0.1463  -0.0076 51  CYS   A O     
351  C  CB    . CYS   A 54  ? 0.4642 0.7219 0.5753 0.1156  0.1248  -0.0104 51  CYS   A CB    
352  S  SG    . CYS   A 54  ? 0.4968 0.6971 0.5696 0.1119  0.1188  -0.0190 51  CYS   A SG    
353  N  N     . LEU   A 55  ? 0.4162 0.7299 0.5338 0.0775  0.1392  0.0148  52  LEU   A N     
354  C  CA    . LEU   A 55  ? 0.4208 0.7324 0.5282 0.0582  0.1397  0.0284  52  LEU   A CA    
355  C  C     . LEU   A 55  ? 0.3937 0.6684 0.4987 0.0482  0.1240  0.0332  52  LEU   A C     
356  O  O     . LEU   A 55  ? 0.3665 0.6403 0.4936 0.0443  0.1157  0.0365  52  LEU   A O     
357  C  CB    . LEU   A 55  ? 0.4339 0.7873 0.5678 0.0463  0.1483  0.0432  52  LEU   A CB    
358  C  CG    . LEU   A 55  ? 0.4580 0.8121 0.5861 0.0263  0.1508  0.0622  52  LEU   A CG    
359  C  CD1   . LEU   A 55  ? 0.4852 0.8331 0.5770 0.0282  0.1566  0.0616  52  LEU   A CD1   
360  C  CD2   . LEU   A 55  ? 0.4794 0.8765 0.6347 0.0150  0.1626  0.0758  52  LEU   A CD2   
361  N  N     . LEU   A 56  ? 0.4064 0.6546 0.4850 0.0441  0.1203  0.0325  53  LEU   A N     
362  C  CA    . LEU   A 56  ? 0.3792 0.5952 0.4552 0.0352  0.1072  0.0369  53  LEU   A CA    
363  C  C     . LEU   A 56  ? 0.3758 0.5990 0.4603 0.0192  0.1074  0.0553  53  LEU   A C     
364  O  O     . LEU   A 56  ? 0.3807 0.6171 0.4521 0.0155  0.1147  0.0633  53  LEU   A O     
365  C  CB    . LEU   A 56  ? 0.3875 0.5762 0.4348 0.0380  0.1031  0.0278  53  LEU   A CB    
366  C  CG    . LEU   A 56  ? 0.4092 0.5812 0.4447 0.0522  0.1035  0.0097  53  LEU   A CG    
367  C  CD1   . LEU   A 56  ? 0.4377 0.5776 0.4518 0.0491  0.0964  0.0024  53  LEU   A CD1   
368  C  CD2   . LEU   A 56  ? 0.4168 0.5854 0.4721 0.0607  0.0993  0.0074  53  LEU   A CD2   
369  N  N     . ASP   A 57  ? 0.3452 0.5598 0.4501 0.0107  0.1002  0.0615  54  ASP   A N     
370  C  CA    . ASP   A 57  ? 0.3520 0.5643 0.4676 -0.0046 0.1000  0.0785  54  ASP   A CA    
371  C  C     . ASP   A 57  ? 0.3582 0.5353 0.4679 -0.0070 0.0885  0.0775  54  ASP   A C     
372  O  O     . ASP   A 57  ? 0.3233 0.4884 0.4458 -0.0086 0.0812  0.0716  54  ASP   A O     
373  C  CB    . ASP   A 57  ? 0.3668 0.5997 0.5135 -0.0141 0.1026  0.0838  54  ASP   A CB    
374  C  CG    . ASP   A 57  ? 0.3902 0.6186 0.5483 -0.0309 0.1050  0.1019  54  ASP   A CG    
375  O  OD1   . ASP   A 57  ? 0.4007 0.6120 0.5424 -0.0322 0.1046  0.1114  54  ASP   A OD1   
376  O  OD2   . ASP   A 57  ? 0.3846 0.6258 0.5687 -0.0425 0.1066  0.1060  54  ASP   A OD2   
377  N  N     . ILE   A 58  ? 0.3566 0.5221 0.4481 -0.0072 0.0874  0.0836  55  ILE   A N     
378  C  CA    . ILE   A 58  ? 0.3410 0.4776 0.4265 -0.0064 0.0775  0.0801  55  ILE   A CA    
379  C  C     . ILE   A 58  ? 0.3451 0.4689 0.4392 -0.0144 0.0755  0.0956  55  ILE   A C     
380  O  O     . ILE   A 58  ? 0.3464 0.4794 0.4335 -0.0164 0.0798  0.1099  55  ILE   A O     
381  C  CB    . ILE   A 58  ? 0.3679 0.5017 0.4281 0.0008  0.0761  0.0724  55  ILE   A CB    
382  C  CG1   . ILE   A 58  ? 0.3703 0.5105 0.4216 0.0094  0.0794  0.0566  55  ILE   A CG1   
383  C  CG2   . ILE   A 58  ? 0.3682 0.4785 0.4246 0.0010  0.0672  0.0689  55  ILE   A CG2   
384  C  CD1   . ILE   A 58  ? 0.3962 0.5377 0.4227 0.0139  0.0808  0.0481  55  ILE   A CD1   
385  N  N     . LEU   A 59  ? 0.3192 0.4215 0.4258 -0.0172 0.0690  0.0915  56  LEU   A N     
386  C  CA    . LEU   A 59  ? 0.3326 0.4156 0.4489 -0.0224 0.0670  0.1033  56  LEU   A CA    
387  C  C     . LEU   A 59  ? 0.3242 0.3916 0.4290 -0.0148 0.0606  0.0994  56  LEU   A C     
388  O  O     . LEU   A 59  ? 0.3032 0.3613 0.4056 -0.0115 0.0560  0.0846  56  LEU   A O     
389  C  CB    . LEU   A 59  ? 0.3299 0.3996 0.4675 -0.0306 0.0646  0.0977  56  LEU   A CB    
390  C  CG    . LEU   A 59  ? 0.3445 0.3873 0.4935 -0.0353 0.0629  0.1055  56  LEU   A CG    
391  C  CD1   . LEU   A 59  ? 0.3742 0.4182 0.5287 -0.0416 0.0699  0.1282  56  LEU   A CD1   
392  C  CD2   . LEU   A 59  ? 0.3403 0.3696 0.5067 -0.0437 0.0595  0.0935  56  LEU   A CD2   
393  N  N     . ASP   A 60  ? 0.3399 0.4075 0.4389 -0.0124 0.0606  0.1138  57  ASP   A N     
394  C  CA    . ASP   A 60  ? 0.3626 0.4221 0.4550 -0.0051 0.0545  0.1115  57  ASP   A CA    
395  C  C     . ASP   A 60  ? 0.3735 0.4087 0.4830 -0.0047 0.0526  0.1175  57  ASP   A C     
396  O  O     . ASP   A 60  ? 0.4511 0.4811 0.5666 -0.0052 0.0547  0.1360  57  ASP   A O     
397  C  CB    . ASP   A 60  ? 0.3613 0.4403 0.4372 -0.0009 0.0539  0.1228  57  ASP   A CB    
398  C  CG    . ASP   A 60  ? 0.3645 0.4416 0.4383 0.0063  0.0468  0.1238  57  ASP   A CG    
399  O  OD1   . ASP   A 60  ? 0.3519 0.4163 0.4323 0.0081  0.0436  0.1103  57  ASP   A OD1   
400  O  OD2   . ASP   A 60  ? 0.3743 0.4664 0.4397 0.0101  0.0445  0.1381  57  ASP   A OD2   
401  N  N     . THR   A 61  ? 0.3656 0.3846 0.4815 -0.0032 0.0493  0.1023  58  THR   A N     
402  C  CA    . THR   A 61  ? 0.3851 0.3787 0.5172 -0.0026 0.0488  0.1027  58  THR   A CA    
403  C  C     . THR   A 61  ? 0.4436 0.4332 0.5764 0.0086  0.0457  0.1061  58  THR   A C     
404  O  O     . THR   A 61  ? 0.4869 0.4949 0.6082 0.0137  0.0427  0.1040  58  THR   A O     
405  C  CB    . THR   A 61  ? 0.3598 0.3406 0.4973 -0.0068 0.0474  0.0829  58  THR   A CB    
406  O  OG1   . THR   A 61  ? 0.3323 0.3171 0.4592 -0.0010 0.0445  0.0689  58  THR   A OG1   
407  C  CG2   . THR   A 61  ? 0.3596 0.3495 0.4997 -0.0166 0.0488  0.0784  58  THR   A CG2   
408  N  N     . ALA   A 62  ? 0.4735 0.4391 0.6214 0.0119  0.0466  0.1091  59  ALA   A N     
409  C  CA    . ALA   A 62  ? 0.5146 0.4777 0.6678 0.0252  0.0443  0.1119  59  ALA   A CA    
410  C  C     . ALA   A 62  ? 0.5163 0.4701 0.6729 0.0279  0.0444  0.0900  59  ALA   A C     
411  O  O     . ALA   A 62  ? 0.4575 0.3986 0.6146 0.0199  0.0458  0.0759  59  ALA   A O     
412  C  CB    . ALA   A 62  ? 0.5653 0.5068 0.7326 0.0310  0.0461  0.1308  59  ALA   A CB    
413  N  N     . GLY   A 63  ? 0.5225 0.4882 0.6807 0.0386  0.0426  0.0879  60  GLY   A N     
414  C  CA    . GLY   A 63  ? 0.5820 0.5441 0.7427 0.0422  0.0444  0.0688  60  GLY   A CA    
415  C  C     . GLY   A 63  ? 0.6418 0.5730 0.8174 0.0469  0.0483  0.0637  60  GLY   A C     
416  O  O     . GLY   A 63  ? 0.7357 0.6551 0.9090 0.0429  0.0507  0.0447  60  GLY   A O     
417  N  N     . TYR   A 67  ? 0.7893 0.5064 1.0349 -0.0238 0.0630  0.0258  64  TYR   A N     
418  C  CA    . TYR   A 67  ? 0.7925 0.4937 1.0489 -0.0480 0.0627  0.0184  64  TYR   A CA    
419  C  C     . TYR   A 67  ? 0.7643 0.5023 1.0096 -0.0604 0.0558  0.0005  64  TYR   A C     
420  O  O     . TYR   A 67  ? 0.7194 0.4905 0.9608 -0.0653 0.0537  0.0137  64  TYR   A O     
421  C  CB    . TYR   A 67  ? 0.7856 0.4790 1.0544 -0.0580 0.0667  0.0481  64  TYR   A CB    
422  C  CG    . TYR   A 67  ? 0.7610 0.4365 1.0458 -0.0847 0.0679  0.0428  64  TYR   A CG    
423  C  CD1   . TYR   A 67  ? 0.7718 0.4116 1.0655 -0.0945 0.0679  0.0171  64  TYR   A CD1   
424  C  CD2   . TYR   A 67  ? 0.7312 0.4277 1.0227 -0.1012 0.0697  0.0622  64  TYR   A CD2   
425  C  CE1   . TYR   A 67  ? 0.7931 0.4178 1.1035 -0.1218 0.0685  0.0108  64  TYR   A CE1   
426  C  CE2   . TYR   A 67  ? 0.7513 0.4364 1.0607 -0.1279 0.0712  0.0575  64  TYR   A CE2   
427  C  CZ    . TYR   A 67  ? 0.7733 0.4217 1.0929 -0.1392 0.0701  0.0318  64  TYR   A CZ    
428  O  OH    . TYR   A 67  ? 0.8155 0.4538 1.1543 -0.1680 0.0708  0.0251  64  TYR   A OH    
429  N  N     . SER   A 68  ? 0.7962 0.5254 1.0382 -0.0662 0.0527  -0.0288 65  SER   A N     
430  C  CA    . SER   A 68  ? 0.7726 0.5360 1.0017 -0.0749 0.0447  -0.0474 65  SER   A CA    
431  C  C     . SER   A 68  ? 0.7625 0.5508 1.0015 -0.0947 0.0406  -0.0399 65  SER   A C     
432  O  O     . SER   A 68  ? 0.7230 0.5492 0.9510 -0.0949 0.0344  -0.0435 65  SER   A O     
433  C  CB    . SER   A 68  ? 0.8141 0.5614 1.0367 -0.0781 0.0423  -0.0798 65  SER   A CB    
434  O  OG    . SER   A 68  ? 0.8441 0.5761 1.0574 -0.0580 0.0476  -0.0870 65  SER   A OG    
435  N  N     . ALA   A 69  ? 0.7320 0.4998 0.9920 -0.1110 0.0442  -0.0307 66  ALA   A N     
436  C  CA    . ALA   A 69  ? 0.7109 0.5060 0.9847 -0.1317 0.0417  -0.0241 66  ALA   A CA    
437  C  C     . ALA   A 69  ? 0.6703 0.4996 0.9404 -0.1246 0.0445  0.0026  66  ALA   A C     
438  O  O     . ALA   A 69  ? 0.6123 0.4807 0.8847 -0.1322 0.0406  0.0023  66  ALA   A O     
439  C  CB    . ALA   A 69  ? 0.7521 0.5119 1.0497 -0.1524 0.0467  -0.0213 66  ALA   A CB    
440  N  N     . MET   A 70  ? 0.6667 0.4822 0.9323 -0.1104 0.0512  0.0245  67  MET   A N     
441  C  CA    . MET   A 70  ? 0.6435 0.4889 0.9020 -0.1025 0.0545  0.0488  67  MET   A CA    
442  C  C     . MET   A 70  ? 0.5896 0.4666 0.8274 -0.0880 0.0486  0.0387  67  MET   A C     
443  O  O     . MET   A 70  ? 0.5211 0.4337 0.7557 -0.0900 0.0471  0.0422  67  MET   A O     
444  C  CB    . MET   A 70  ? 0.7039 0.5254 0.9601 -0.0894 0.0609  0.0721  67  MET   A CB    
445  C  CG    . MET   A 70  ? 0.7278 0.5798 0.9733 -0.0817 0.0637  0.0952  67  MET   A CG    
446  S  SD    . MET   A 70  ? 0.8138 0.6924 1.0721 -0.1025 0.0694  0.1106  67  MET   A SD    
447  C  CE    . MET   A 70  ? 0.8013 0.6333 1.0794 -0.1160 0.0775  0.1294  67  MET   A CE    
448  N  N     . ARG   A 71  ? 0.5788 0.4413 0.8043 -0.0743 0.0463  0.0257  68  ARG   A N     
449  C  CA    . ARG   A 71  ? 0.5343 0.4197 0.7399 -0.0618 0.0418  0.0161  68  ARG   A CA    
450  C  C     . ARG   A 71  ? 0.4730 0.3853 0.6764 -0.0710 0.0351  0.0022  68  ARG   A C     
451  O  O     . ARG   A 71  ? 0.4204 0.3608 0.6136 -0.0651 0.0332  0.0065  68  ARG   A O     
452  C  CB    . ARG   A 71  ? 0.5692 0.4337 0.7661 -0.0503 0.0417  0.0013  68  ARG   A CB    
453  C  CG    . ARG   A 71  ? 0.5633 0.4479 0.7401 -0.0364 0.0400  -0.0017 68  ARG   A CG    
454  C  CD    . ARG   A 71  ? 0.6182 0.4870 0.7880 -0.0283 0.0409  -0.0195 68  ARG   A CD    
455  N  NE    . ARG   A 71  ? 0.7029 0.5605 0.8746 -0.0393 0.0376  -0.0408 68  ARG   A NE    
456  C  CZ    . ARG   A 71  ? 0.7467 0.5850 0.9147 -0.0357 0.0394  -0.0600 68  ARG   A CZ    
457  N  NH1   . ARG   A 71  ? 0.7991 0.6292 0.9675 -0.0479 0.0354  -0.0807 68  ARG   A NH1   
458  N  NH2   . ARG   A 71  ? 0.7642 0.5940 0.9290 -0.0203 0.0452  -0.0597 68  ARG   A NH2   
459  N  N     . ASP   A 72  ? 0.5130 0.4160 0.7267 -0.0849 0.0312  -0.0145 69  ASP   A N     
460  C  CA    . ASP   A 72  ? 0.4959 0.4265 0.7092 -0.0936 0.0227  -0.0289 69  ASP   A CA    
461  C  C     . ASP   A 72  ? 0.4711 0.4346 0.6974 -0.1011 0.0230  -0.0152 69  ASP   A C     
462  O  O     . ASP   A 72  ? 0.4060 0.4017 0.6270 -0.0981 0.0168  -0.0197 69  ASP   A O     
463  C  CB    . ASP   A 72  ? 0.5355 0.4503 0.7561 -0.1080 0.0175  -0.0519 69  ASP   A CB    
464  C  CG    . ASP   A 72  ? 0.5570 0.4542 0.7576 -0.0975 0.0158  -0.0708 69  ASP   A CG    
465  O  OD1   . ASP   A 72  ? 0.5452 0.4395 0.7300 -0.0798 0.0199  -0.0639 69  ASP   A OD1   
466  O  OD2   . ASP   A 72  ? 0.6086 0.4977 0.8093 -0.1078 0.0106  -0.0933 69  ASP   A OD2   
467  N  N     . GLN   A 73  ? 0.4768 0.4329 0.7193 -0.1093 0.0307  0.0022  70  GLN   A N     
468  C  CA    . GLN   A 73  ? 0.4655 0.4551 0.7219 -0.1173 0.0338  0.0159  70  GLN   A CA    
469  C  C     . GLN   A 73  ? 0.4198 0.4346 0.6593 -0.0996 0.0356  0.0260  70  GLN   A C     
470  O  O     . GLN   A 73  ? 0.3942 0.4435 0.6374 -0.0992 0.0331  0.0245  70  GLN   A O     
471  C  CB    . GLN   A 73  ? 0.4890 0.4629 0.7632 -0.1302 0.0436  0.0348  70  GLN   A CB    
472  C  CG    . GLN   A 73  ? 0.4937 0.5059 0.7838 -0.1406 0.0485  0.0478  70  GLN   A CG    
473  C  CD    . GLN   A 73  ? 0.4984 0.5437 0.8055 -0.1535 0.0406  0.0314  70  GLN   A CD    
474  O  OE1   . GLN   A 73  ? 0.5176 0.5501 0.8365 -0.1684 0.0345  0.0154  70  GLN   A OE1   
475  N  NE2   . GLN   A 73  ? 0.4650 0.5545 0.7730 -0.1467 0.0399  0.0340  70  GLN   A NE2   
476  N  N     . TYR   A 74  ? 0.4068 0.4048 0.6300 -0.0857 0.0400  0.0358  71  TYR   A N     
477  C  CA    . TYR   A 74  ? 0.3869 0.4062 0.5928 -0.0708 0.0414  0.0423  71  TYR   A CA    
478  C  C     . TYR   A 74  ? 0.3839 0.4135 0.5756 -0.0615 0.0335  0.0265  71  TYR   A C     
479  O  O     . TYR   A 74  ? 0.3856 0.4386 0.5709 -0.0539 0.0334  0.0282  71  TYR   A O     
480  C  CB    . TYR   A 74  ? 0.3922 0.3989 0.5865 -0.0613 0.0475  0.0579  71  TYR   A CB    
481  C  CG    . TYR   A 74  ? 0.3910 0.3709 0.5744 -0.0516 0.0455  0.0536  71  TYR   A CG    
482  C  CD1   . TYR   A 74  ? 0.4014 0.3820 0.5692 -0.0418 0.0408  0.0401  71  TYR   A CD1   
483  C  CD2   . TYR   A 74  ? 0.4210 0.3773 0.6097 -0.0508 0.0495  0.0656  71  TYR   A CD2   
484  C  CE1   . TYR   A 74  ? 0.4041 0.3659 0.5639 -0.0331 0.0407  0.0369  71  TYR   A CE1   
485  C  CE2   . TYR   A 74  ? 0.4385 0.3752 0.6204 -0.0397 0.0484  0.0624  71  TYR   A CE2   
486  C  CZ    . TYR   A 74  ? 0.4341 0.3757 0.6022 -0.0313 0.0444  0.0472  71  TYR   A CZ    
487  O  OH    . TYR   A 74  ? 0.4281 0.3557 0.5921 -0.0209 0.0446  0.0441  71  TYR   A OH    
488  N  N     . MET   A 75  ? 0.3618 0.3729 0.5475 -0.0612 0.0281  0.0121  72  MET   A N     
489  C  CA    . MET   A 75  ? 0.3766 0.3984 0.5464 -0.0529 0.0209  -0.0003 72  MET   A CA    
490  C  C     . MET   A 75  ? 0.3890 0.4406 0.5704 -0.0593 0.0141  -0.0062 72  MET   A C     
491  O  O     . MET   A 75  ? 0.3876 0.4561 0.5579 -0.0495 0.0096  -0.0086 72  MET   A O     
492  C  CB    . MET   A 75  ? 0.3851 0.3838 0.5431 -0.0509 0.0179  -0.0142 72  MET   A CB    
493  C  CG    . MET   A 75  ? 0.3826 0.3591 0.5333 -0.0428 0.0245  -0.0076 72  MET   A CG    
494  S  SD    . MET   A 75  ? 0.3846 0.3406 0.5210 -0.0373 0.0236  -0.0239 72  MET   A SD    
495  C  CE    . MET   A 75  ? 0.3919 0.3398 0.5206 -0.0243 0.0307  -0.0122 72  MET   A CE    
496  N  N     . ARG   A 76  ? 0.3916 0.4498 0.5962 -0.0755 0.0136  -0.0075 73  ARG   A N     
497  C  CA    . ARG   A 76  ? 0.4128 0.5074 0.6327 -0.0821 0.0064  -0.0129 73  ARG   A CA    
498  C  C     . ARG   A 76  ? 0.3963 0.5205 0.6250 -0.0763 0.0126  0.0013  73  ARG   A C     
499  O  O     . ARG   A 76  ? 0.4161 0.5692 0.6449 -0.0676 0.0074  -0.0010 73  ARG   A O     
500  C  CB    . ARG   A 76  ? 0.4391 0.5332 0.6827 -0.1044 0.0032  -0.0218 73  ARG   A CB    
501  C  CG    . ARG   A 76  ? 0.6156 0.7530 0.8769 -0.1122 -0.0063 -0.0294 73  ARG   A CG    
502  C  CD    . ARG   A 76  ? 0.6379 0.7811 0.9257 -0.1376 -0.0104 -0.0399 73  ARG   A CD    
503  N  NE    . ARG   A 76  ? 0.6567 0.7681 0.9282 -0.1404 -0.0167 -0.0581 73  ARG   A NE    
504  C  CZ    . ARG   A 76  ? 0.6607 0.7857 0.9181 -0.1364 -0.0293 -0.0744 73  ARG   A CZ    
505  N  NH1   . ARG   A 76  ? 0.6815 0.7770 0.9232 -0.1397 -0.0327 -0.0917 73  ARG   A NH1   
506  N  NH2   . ARG   A 76  ? 0.6471 0.8157 0.9057 -0.1282 -0.0382 -0.0730 73  ARG   A NH2   
507  N  N     . THR   A 77  ? 0.4090 0.5255 0.6432 -0.0795 0.0236  0.0157  74  THR   A N     
508  C  CA    . THR   A 77  ? 0.3644 0.5080 0.6039 -0.0742 0.0321  0.0289  74  THR   A CA    
509  C  C     . THR   A 77  ? 0.3440 0.4883 0.5593 -0.0530 0.0333  0.0301  74  THR   A C     
510  O  O     . THR   A 77  ? 0.3000 0.4718 0.5184 -0.0448 0.0362  0.0327  74  THR   A O     
511  C  CB    . THR   A 77  ? 0.3769 0.5108 0.6258 -0.0852 0.0433  0.0447  74  THR   A CB    
512  O  OG1   . THR   A 77  ? 0.3912 0.5335 0.6670 -0.1058 0.0417  0.0417  74  THR   A OG1   
513  C  CG2   . THR   A 77  ? 0.3923 0.5525 0.6404 -0.0789 0.0536  0.0580  74  THR   A CG2   
514  N  N     . GLY   A 78  ? 0.2913 0.4051 0.4842 -0.0452 0.0322  0.0281  75  GLY   A N     
515  C  CA    . GLY   A 78  ? 0.2854 0.3962 0.4559 -0.0286 0.0340  0.0288  75  GLY   A CA    
516  C  C     . GLY   A 78  ? 0.2893 0.4153 0.4550 -0.0175 0.0274  0.0210  75  GLY   A C     
517  O  O     . GLY   A 78  ? 0.2859 0.4112 0.4523 -0.0197 0.0185  0.0125  75  GLY   A O     
518  N  N     . GLU   A 79  ? 0.2737 0.4107 0.4322 -0.0049 0.0321  0.0239  76  GLU   A N     
519  C  CA    . GLU   A 79  ? 0.2924 0.4400 0.4453 0.0097  0.0271  0.0191  76  GLU   A CA    
520  C  C     . GLU   A 79  ? 0.2986 0.4163 0.4237 0.0198  0.0260  0.0164  76  GLU   A C     
521  O  O     . GLU   A 79  ? 0.3010 0.4172 0.4182 0.0288  0.0194  0.0132  76  GLU   A O     
522  C  CB    . GLU   A 79  ? 0.2897 0.4663 0.4539 0.0185  0.0340  0.0224  76  GLU   A CB    
523  C  CG    . GLU   A 79  ? 0.3038 0.5163 0.4986 0.0081  0.0335  0.0242  76  GLU   A CG    
524  C  CD    . GLU   A 79  ? 0.3385 0.5848 0.5493 0.0121  0.0440  0.0290  76  GLU   A CD    
525  O  OE1   . GLU   A 79  ? 0.3232 0.5624 0.5202 0.0190  0.0538  0.0318  76  GLU   A OE1   
526  O  OE2   . GLU   A 79  ? 0.4029 0.6851 0.6405 0.0074  0.0421  0.0290  76  GLU   A OE2   
527  N  N     . GLY   A 80  ? 0.3066 0.4046 0.4187 0.0179  0.0323  0.0189  77  GLY   A N     
528  C  CA    . GLY   A 80  ? 0.3153 0.3867 0.4036 0.0238  0.0327  0.0164  77  GLY   A CA    
529  C  C     . GLY   A 80  ? 0.3106 0.3657 0.3936 0.0151  0.0351  0.0182  77  GLY   A C     
530  O  O     . GLY   A 80  ? 0.2997 0.3625 0.3923 0.0090  0.0391  0.0237  77  GLY   A O     
531  N  N     . PHE   A 81  ? 0.2928 0.3277 0.3614 0.0152  0.0330  0.0147  78  PHE   A N     
532  C  CA    . PHE   A 81  ? 0.3002 0.3234 0.3669 0.0089  0.0349  0.0160  78  PHE   A CA    
533  C  C     . PHE   A 81  ? 0.2989 0.3093 0.3485 0.0114  0.0376  0.0145  78  PHE   A C     
534  O  O     . PHE   A 81  ? 0.3204 0.3199 0.3574 0.0146  0.0365  0.0107  78  PHE   A O     
535  C  CB    . PHE   A 81  ? 0.3106 0.3259 0.3815 0.0040  0.0307  0.0114  78  PHE   A CB    
536  C  CG    . PHE   A 81  ? 0.3051 0.3312 0.3940 -0.0021 0.0275  0.0106  78  PHE   A CG    
537  C  CD1   . PHE   A 81  ? 0.3135 0.3532 0.4059 -0.0004 0.0220  0.0069  78  PHE   A CD1   
538  C  CD2   . PHE   A 81  ? 0.3007 0.3239 0.4043 -0.0098 0.0296  0.0144  78  PHE   A CD2   
539  C  CE1   . PHE   A 81  ? 0.3119 0.3658 0.4236 -0.0086 0.0186  0.0052  78  PHE   A CE1   
540  C  CE2   . PHE   A 81  ? 0.3109 0.3423 0.4325 -0.0184 0.0274  0.0134  78  PHE   A CE2   
541  C  CZ    . PHE   A 81  ? 0.3237 0.3720 0.4500 -0.0189 0.0218  0.0078  78  PHE   A CZ    
542  N  N     . LEU   A 82  ? 0.2897 0.3032 0.3392 0.0090  0.0409  0.0183  79  LEU   A N     
543  C  CA    . LEU   A 82  ? 0.3032 0.3087 0.3400 0.0080  0.0423  0.0157  79  LEU   A CA    
544  C  C     . LEU   A 82  ? 0.3212 0.3225 0.3641 0.0046  0.0410  0.0161  79  LEU   A C     
545  O  O     . LEU   A 82  ? 0.2948 0.3018 0.3495 0.0033  0.0408  0.0217  79  LEU   A O     
546  C  CB    . LEU   A 82  ? 0.3305 0.3468 0.3642 0.0071  0.0448  0.0187  79  LEU   A CB    
547  C  CG    . LEU   A 82  ? 0.3916 0.4087 0.4131 0.0107  0.0480  0.0136  79  LEU   A CG    
548  C  CD1   . LEU   A 82  ? 0.4120 0.4393 0.4258 0.0073  0.0491  0.0136  79  LEU   A CD1   
549  C  CD2   . LEU   A 82  ? 0.4021 0.3996 0.4114 0.0128  0.0482  0.0059  79  LEU   A CD2   
550  N  N     . CYS   A 83  ? 0.3324 0.3235 0.3675 0.0039  0.0410  0.0108  80  CYS   A N     
551  C  CA    . CYS   A 83  ? 0.3244 0.3137 0.3653 0.0021  0.0415  0.0092  80  CYS   A CA    
552  C  C     . CYS   A 83  ? 0.3045 0.2987 0.3424 -0.0006 0.0437  0.0093  80  CYS   A C     
553  O  O     . CYS   A 83  ? 0.3110 0.2994 0.3377 -0.0036 0.0456  0.0056  80  CYS   A O     
554  C  CB    . CYS   A 83  ? 0.3454 0.3257 0.3788 0.0023  0.0412  0.0033  80  CYS   A CB    
555  S  SG    . CYS   A 83  ? 0.3829 0.3642 0.4216 0.0039  0.0362  0.0017  80  CYS   A SG    
556  N  N     . VAL   A 84  ? 0.3080 0.3137 0.3572 0.0002  0.0429  0.0143  81  VAL   A N     
557  C  CA    . VAL   A 84  ? 0.2969 0.3149 0.3453 -0.0027 0.0429  0.0147  81  VAL   A CA    
558  C  C     . VAL   A 84  ? 0.3073 0.3327 0.3669 -0.0016 0.0443  0.0136  81  VAL   A C     
559  O  O     . VAL   A 84  ? 0.3050 0.3293 0.3770 0.0042  0.0443  0.0165  81  VAL   A O     
560  C  CB    . VAL   A 84  ? 0.3033 0.3356 0.3548 -0.0012 0.0400  0.0225  81  VAL   A CB    
561  C  CG1   . VAL   A 84  ? 0.2988 0.3478 0.3471 -0.0056 0.0380  0.0209  81  VAL   A CG1   
562  C  CG2   . VAL   A 84  ? 0.3131 0.3419 0.3561 -0.0008 0.0405  0.0234  81  VAL   A CG2   
563  N  N     . PHE   A 85  ? 0.2938 0.3252 0.3491 -0.0077 0.0464  0.0087  82  PHE   A N     
564  C  CA    . PHE   A 85  ? 0.2982 0.3464 0.3668 -0.0074 0.0484  0.0076  82  PHE   A CA    
565  C  C     . PHE   A 85  ? 0.3077 0.3772 0.3783 -0.0139 0.0452  0.0080  82  PHE   A C     
566  O  O     . PHE   A 85  ? 0.3318 0.3976 0.3900 -0.0196 0.0429  0.0064  82  PHE   A O     
567  C  CB    . PHE   A 85  ? 0.2850 0.3269 0.3492 -0.0109 0.0551  0.0009  82  PHE   A CB    
568  C  CG    . PHE   A 85  ? 0.3110 0.3472 0.3606 -0.0226 0.0582  -0.0027 82  PHE   A CG    
569  C  CD1   . PHE   A 85  ? 0.3123 0.3249 0.3434 -0.0245 0.0585  -0.0033 82  PHE   A CD1   
570  C  CD2   . PHE   A 85  ? 0.3241 0.3784 0.3803 -0.0316 0.0609  -0.0051 82  PHE   A CD2   
571  C  CE1   . PHE   A 85  ? 0.3324 0.3335 0.3500 -0.0344 0.0619  -0.0052 82  PHE   A CE1   
572  C  CE2   . PHE   A 85  ? 0.3374 0.3815 0.3806 -0.0447 0.0644  -0.0081 82  PHE   A CE2   
573  C  CZ    . PHE   A 85  ? 0.3553 0.3697 0.3783 -0.0456 0.0653  -0.0077 82  PHE   A CZ    
574  N  N     . ALA   A 86  ? 0.3026 0.3966 0.3901 -0.0120 0.0447  0.0093  83  ALA   A N     
575  C  CA    . ALA   A 86  ? 0.2980 0.4193 0.3901 -0.0197 0.0404  0.0081  83  ALA   A CA    
576  C  C     . ALA   A 86  ? 0.3014 0.4321 0.3980 -0.0305 0.0465  0.0005  83  ALA   A C     
577  O  O     . ALA   A 86  ? 0.2943 0.4258 0.3999 -0.0259 0.0530  -0.0004 83  ALA   A O     
578  C  CB    . ALA   A 86  ? 0.3035 0.4529 0.4140 -0.0092 0.0340  0.0173  83  ALA   A CB    
579  N  N     . ILE   A 87  ? 0.3244 0.4610 0.4138 -0.0459 0.0453  -0.0056 84  ILE   A N     
580  C  CA    . ILE   A 87  ? 0.3413 0.4795 0.4311 -0.0606 0.0526  -0.0121 84  ILE   A CA    
581  C  C     . ILE   A 87  ? 0.3432 0.5227 0.4597 -0.0605 0.0537  -0.0118 84  ILE   A C     
582  O  O     . ILE   A 87  ? 0.3598 0.5475 0.4819 -0.0715 0.0619  -0.0157 84  ILE   A O     
583  C  CB    . ILE   A 87  ? 0.3538 0.4805 0.4286 -0.0786 0.0515  -0.0198 84  ILE   A CB    
584  C  CG1   . ILE   A 87  ? 0.3881 0.5470 0.4706 -0.0841 0.0413  -0.0231 84  ILE   A CG1   
585  C  CG2   . ILE   A 87  ? 0.3799 0.4647 0.4301 -0.0758 0.0527  -0.0203 84  ILE   A CG2   
586  C  CD1   . ILE   A 87  ? 0.4243 0.5872 0.5030 -0.1073 0.0413  -0.0346 84  ILE   A CD1   
587  N  N     . ASN   A 88  ? 0.3164 0.5224 0.4498 -0.0474 0.0461  -0.0059 85  ASN   A N     
588  C  CA    . ASN   A 88  ? 0.3150 0.5651 0.4778 -0.0423 0.0457  -0.0043 85  ASN   A CA    
589  C  C     . ASN   A 88  ? 0.3049 0.5504 0.4802 -0.0209 0.0503  0.0011  85  ASN   A C     
590  O  O     . ASN   A 88  ? 0.3189 0.5976 0.5197 -0.0098 0.0490  0.0044  85  ASN   A O     
591  C  CB    . ASN   A 88  ? 0.3182 0.6053 0.4922 -0.0413 0.0325  -0.0005 85  ASN   A CB    
592  C  CG    . ASN   A 88  ? 0.3330 0.6119 0.5023 -0.0236 0.0243  0.0108  85  ASN   A CG    
593  O  OD1   . ASN   A 88  ? 0.3336 0.5746 0.4844 -0.0194 0.0266  0.0130  85  ASN   A OD1   
594  N  ND2   . ASN   A 88  ? 0.3157 0.6320 0.5027 -0.0131 0.0147  0.0194  85  ASN   A ND2   
595  N  N     . ASN   A 89  ? 0.3041 0.5099 0.4626 -0.0149 0.0548  0.0013  86  ASN   A N     
596  C  CA    . ASN   A 89  ? 0.3026 0.5000 0.4720 0.0038  0.0592  0.0033  86  ASN   A CA    
597  C  C     . ASN   A 89  ? 0.3113 0.4796 0.4640 0.0002  0.0694  -0.0042 86  ASN   A C     
598  O  O     . ASN   A 89  ? 0.3035 0.4402 0.4359 -0.0018 0.0677  -0.0039 86  ASN   A O     
599  C  CB    . ASN   A 89  ? 0.3063 0.4912 0.4767 0.0176  0.0508  0.0133  86  ASN   A CB    
600  C  CG    . ASN   A 89  ? 0.3153 0.4793 0.4931 0.0342  0.0551  0.0143  86  ASN   A CG    
601  O  OD1   . ASN   A 89  ? 0.3400 0.4964 0.5190 0.0365  0.0643  0.0055  86  ASN   A OD1   
602  N  ND2   . ASN   A 89  ? 0.3520 0.5042 0.5326 0.0445  0.0488  0.0248  86  ASN   A ND2   
603  N  N     . THR   A 90  ? 0.3150 0.4982 0.4769 0.0006  0.0797  -0.0103 87  THR   A N     
604  C  CA    . THR   A 90  ? 0.3279 0.4885 0.4705 -0.0036 0.0897  -0.0171 87  THR   A CA    
605  C  C     . THR   A 90  ? 0.3259 0.4589 0.4626 0.0106  0.0893  -0.0195 87  THR   A C     
606  O  O     . THR   A 90  ? 0.3326 0.4393 0.4465 0.0060  0.0907  -0.0224 87  THR   A O     
607  C  CB    . THR   A 90  ? 0.3524 0.5404 0.5055 -0.0075 0.1024  -0.0228 87  THR   A CB    
608  O  OG1   . THR   A 90  ? 0.3967 0.6110 0.5787 0.0096  0.1034  -0.0238 87  THR   A OG1   
609  C  CG2   . THR   A 90  ? 0.3412 0.5521 0.4979 -0.0270 0.1038  -0.0212 87  THR   A CG2   
610  N  N     . LYS   A 91  ? 0.3333 0.4721 0.4905 0.0268  0.0867  -0.0177 88  LYS   A N     
611  C  CA    . LYS   A 91  ? 0.3573 0.4664 0.5100 0.0377  0.0869  -0.0217 88  LYS   A CA    
612  C  C     . LYS   A 91  ? 0.3333 0.4142 0.4678 0.0314  0.0783  -0.0165 88  LYS   A C     
613  O  O     . LYS   A 91  ? 0.3195 0.3754 0.4406 0.0313  0.0789  -0.0223 88  LYS   A O     
614  C  CB    . LYS   A 91  ? 0.3839 0.4970 0.5622 0.0567  0.0857  -0.0189 88  LYS   A CB    
615  C  CG    . LYS   A 91  ? 0.4358 0.5141 0.6109 0.0659  0.0870  -0.0251 88  LYS   A CG    
616  C  CD    . LYS   A 91  ? 0.4583 0.5317 0.6582 0.0848  0.0856  -0.0198 88  LYS   A CD    
617  C  CE    . LYS   A 91  ? 0.4966 0.5317 0.6943 0.0915  0.0885  -0.0292 88  LYS   A CE    
618  N  NZ    . LYS   A 91  ? 0.5227 0.5297 0.7073 0.0818  0.0803  -0.0226 88  LYS   A NZ    
619  N  N     . SER   A 92  ? 0.2939 0.3822 0.4295 0.0268  0.0701  -0.0065 89  SER   A N     
620  C  CA    . SER   A 92  ? 0.2917 0.3580 0.4125 0.0221  0.0633  -0.0016 89  SER   A CA    
621  C  C     . SER   A 92  ? 0.2944 0.3456 0.3914 0.0110  0.0657  -0.0073 89  SER   A C     
622  O  O     . SER   A 92  ? 0.2786 0.3091 0.3638 0.0101  0.0627  -0.0076 89  SER   A O     
623  C  CB    . SER   A 92  ? 0.2758 0.3558 0.4002 0.0202  0.0553  0.0090  89  SER   A CB    
624  O  OG    . SER   A 92  ? 0.2823 0.3755 0.3974 0.0076  0.0550  0.0068  89  SER   A OG    
625  N  N     . PHE   A 93  ? 0.3000 0.3629 0.3912 0.0024  0.0710  -0.0106 90  PHE   A N     
626  C  CA    . PHE   A 93  ? 0.2931 0.3404 0.3609 -0.0072 0.0738  -0.0130 90  PHE   A CA    
627  C  C     . PHE   A 93  ? 0.3212 0.3559 0.3787 -0.0028 0.0784  -0.0199 90  PHE   A C     
628  O  O     . PHE   A 93  ? 0.3294 0.3456 0.3696 -0.0042 0.0753  -0.0202 90  PHE   A O     
629  C  CB    . PHE   A 93  ? 0.3063 0.3674 0.3717 -0.0195 0.0791  -0.0129 90  PHE   A CB    
630  C  CG    . PHE   A 93  ? 0.3259 0.3684 0.3670 -0.0284 0.0839  -0.0130 90  PHE   A CG    
631  C  CD1   . PHE   A 93  ? 0.3171 0.3366 0.3414 -0.0315 0.0787  -0.0095 90  PHE   A CD1   
632  C  CD2   . PHE   A 93  ? 0.3393 0.3876 0.3739 -0.0325 0.0941  -0.0156 90  PHE   A CD2   
633  C  CE1   . PHE   A 93  ? 0.3345 0.3345 0.3365 -0.0371 0.0824  -0.0070 90  PHE   A CE1   
634  C  CE2   . PHE   A 93  ? 0.3735 0.4029 0.3831 -0.0400 0.0982  -0.0122 90  PHE   A CE2   
635  C  CZ    . PHE   A 93  ? 0.3637 0.3677 0.3574 -0.0414 0.0916  -0.0073 90  PHE   A CZ    
636  N  N     . GLU   A 94  ? 0.3355 0.3827 0.4044 0.0036  0.0854  -0.0264 91  GLU   A N     
637  C  CA    . GLU   A 94  ? 0.3620 0.3996 0.4204 0.0081  0.0902  -0.0363 91  GLU   A CA    
638  C  C     . GLU   A 94  ? 0.3514 0.3680 0.4092 0.0137  0.0826  -0.0391 91  GLU   A C     
639  O  O     . GLU   A 94  ? 0.3497 0.3541 0.3899 0.0121  0.0818  -0.0457 91  GLU   A O     
640  C  CB    . GLU   A 94  ? 0.3675 0.4238 0.4411 0.0159  0.1003  -0.0446 91  GLU   A CB    
641  C  CG    . GLU   A 94  ? 0.4209 0.4989 0.4896 0.0073  0.1108  -0.0442 91  GLU   A CG    
642  C  CD    . GLU   A 94  ? 0.4605 0.5275 0.4977 -0.0024 0.1152  -0.0446 91  GLU   A CD    
643  O  OE1   . GLU   A 94  ? 0.5422 0.5980 0.5636 0.0022  0.1165  -0.0531 91  GLU   A OE1   
644  O  OE2   . GLU   A 94  ? 0.5414 0.6105 0.5694 -0.0145 0.1170  -0.0364 91  GLU   A OE2   
645  N  N     . ASP   A 95  ? 0.3411 0.3554 0.4175 0.0190  0.0769  -0.0333 92  ASP   A N     
646  C  CA    . ASP   A 95  ? 0.3538 0.3488 0.4337 0.0224  0.0711  -0.0350 92  ASP   A CA    
647  C  C     . ASP   A 95  ? 0.3197 0.3049 0.3844 0.0146  0.0639  -0.0306 92  ASP   A C     
648  O  O     . ASP   A 95  ? 0.3298 0.3024 0.3959 0.0142  0.0593  -0.0330 92  ASP   A O     
649  C  CB    . ASP   A 95  ? 0.3811 0.3749 0.4841 0.0302  0.0682  -0.0271 92  ASP   A CB    
650  C  CG    . ASP   A 95  ? 0.4044 0.4020 0.5257 0.0423  0.0746  -0.0328 92  ASP   A CG    
651  O  OD1   . ASP   A 95  ? 0.4480 0.4459 0.5634 0.0444  0.0819  -0.0464 92  ASP   A OD1   
652  O  OD2   . ASP   A 95  ? 0.4707 0.4723 0.6111 0.0507  0.0726  -0.0231 92  ASP   A OD2   
653  N  N     . ILE   A 96  ? 0.3065 0.2976 0.3585 0.0085  0.0634  -0.0247 93  ILE   A N     
654  C  CA    . ILE   A 96  ? 0.3215 0.3036 0.3601 0.0043  0.0573  -0.0211 93  ILE   A CA    
655  C  C     . ILE   A 96  ? 0.3249 0.2991 0.3502 0.0040  0.0553  -0.0293 93  ILE   A C     
656  O  O     . ILE   A 96  ? 0.3185 0.2879 0.3420 0.0030  0.0486  -0.0287 93  ILE   A O     
657  C  CB    . ILE   A 96  ? 0.3233 0.3074 0.3490 -0.0011 0.0583  -0.0149 93  ILE   A CB    
658  C  CG1   . ILE   A 96  ? 0.3355 0.3295 0.3733 -0.0025 0.0578  -0.0088 93  ILE   A CG1   
659  C  CG2   . ILE   A 96  ? 0.3326 0.3064 0.3442 -0.0019 0.0530  -0.0119 93  ILE   A CG2   
660  C  CD1   . ILE   A 96  ? 0.3315 0.3242 0.3763 -0.0003 0.0518  -0.0032 93  ILE   A CD1   
661  N  N     . HIS   A 97  ? 0.3386 0.3152 0.3538 0.0044  0.0612  -0.0375 94  HIS   A N     
662  C  CA    . HIS   A 97  ? 0.3387 0.3114 0.3397 0.0042  0.0594  -0.0479 94  HIS   A CA    
663  C  C     . HIS   A 97  ? 0.3682 0.3329 0.3834 0.0050  0.0534  -0.0551 94  HIS   A C     
664  O  O     . HIS   A 97  ? 0.3626 0.3256 0.3708 0.0020  0.0458  -0.0582 94  HIS   A O     
665  C  CB    . HIS   A 97  ? 0.3463 0.3255 0.3394 0.0060  0.0693  -0.0577 94  HIS   A CB    
666  C  CG    . HIS   A 97  ? 0.3711 0.3475 0.3501 0.0064  0.0680  -0.0726 94  HIS   A CG    
667  N  ND1   . HIS   A 97  ? 0.3784 0.3589 0.3288 0.0035  0.0666  -0.0734 94  HIS   A ND1   
668  C  CD2   . HIS   A 97  ? 0.3726 0.3415 0.3610 0.0090  0.0672  -0.0876 94  HIS   A CD2   
669  C  CE1   . HIS   A 97  ? 0.4067 0.3865 0.3482 0.0038  0.0643  -0.0897 94  HIS   A CE1   
670  N  NE2   . HIS   A 97  ? 0.4436 0.4147 0.4086 0.0066  0.0653  -0.0999 94  HIS   A NE2   
671  N  N     . HIS   A 98  ? 0.3656 0.3261 0.4019 0.0091  0.0570  -0.0568 95  HIS   A N     
672  C  CA    . HIS   A 98  ? 0.3859 0.3332 0.4376 0.0090  0.0536  -0.0631 95  HIS   A CA    
673  C  C     . HIS   A 98  ? 0.3569 0.3026 0.4162 0.0037  0.0455  -0.0533 95  HIS   A C     
674  O  O     . HIS   A 98  ? 0.3782 0.3185 0.4398 -0.0018 0.0401  -0.0604 95  HIS   A O     
675  C  CB    . HIS   A 98  ? 0.4016 0.3424 0.4739 0.0171  0.0600  -0.0639 95  HIS   A CB    
676  C  CG    . HIS   A 98  ? 0.4312 0.3755 0.4985 0.0233  0.0690  -0.0771 95  HIS   A CG    
677  N  ND1   . HIS   A 98  ? 0.5032 0.4341 0.5692 0.0253  0.0717  -0.0960 95  HIS   A ND1   
678  C  CD2   . HIS   A 98  ? 0.4433 0.4044 0.5078 0.0276  0.0768  -0.0755 95  HIS   A CD2   
679  C  CE1   . HIS   A 98  ? 0.5168 0.4570 0.5780 0.0322  0.0816  -0.1054 95  HIS   A CE1   
680  N  NE2   . HIS   A 98  ? 0.4437 0.4040 0.5052 0.0332  0.0850  -0.0922 95  HIS   A NE2   
681  N  N     . TYR   A 99  ? 0.3475 0.3002 0.4117 0.0046  0.0451  -0.0385 96  TYR   A N     
682  C  CA    . TYR   A 99  ? 0.3592 0.3138 0.4302 0.0005  0.0395  -0.0294 96  TYR   A CA    
683  C  C     . TYR   A 99  ? 0.3644 0.3257 0.4221 -0.0034 0.0334  -0.0330 96  TYR   A C     
684  O  O     . TYR   A 99  ? 0.3468 0.3099 0.4127 -0.0084 0.0281  -0.0347 96  TYR   A O     
685  C  CB    . TYR   A 99  ? 0.3568 0.3196 0.4309 0.0027  0.0409  -0.0153 96  TYR   A CB    
686  C  CG    . TYR   A 99  ? 0.3690 0.3296 0.4584 0.0074  0.0444  -0.0093 96  TYR   A CG    
687  C  CD1   . TYR   A 99  ? 0.3877 0.3399 0.4932 0.0068  0.0435  -0.0028 96  TYR   A CD1   
688  C  CD2   . TYR   A 99  ? 0.3670 0.3348 0.4561 0.0125  0.0486  -0.0093 96  TYR   A CD2   
689  C  CE1   . TYR   A 99  ? 0.3809 0.3299 0.5000 0.0134  0.0460  0.0056  96  TYR   A CE1   
690  C  CE2   . TYR   A 99  ? 0.3713 0.3405 0.4767 0.0193  0.0505  -0.0030 96  TYR   A CE2   
691  C  CZ    . TYR   A 99  ? 0.3886 0.3471 0.5080 0.0208  0.0489  0.0052  96  TYR   A CZ    
692  O  OH    . TYR   A 99  ? 0.4081 0.3667 0.5427 0.0297  0.0501  0.0142  96  TYR   A OH    
693  N  N     . ARG   A 100 ? 0.3563 0.3223 0.3947 -0.0011 0.0342  -0.0327 97  ARG   A N     
694  C  CA    . ARG   A 100 ? 0.3737 0.3463 0.3974 -0.0015 0.0279  -0.0331 97  ARG   A CA    
695  C  C     . ARG   A 100 ? 0.3778 0.3522 0.3989 -0.0052 0.0224  -0.0462 97  ARG   A C     
696  O  O     . ARG   A 100 ? 0.3655 0.3494 0.3892 -0.0075 0.0145  -0.0467 97  ARG   A O     
697  C  CB    . ARG   A 100 ? 0.4002 0.3719 0.4021 0.0016  0.0313  -0.0287 97  ARG   A CB    
698  C  CG    . ARG   A 100 ? 0.4346 0.4107 0.4182 0.0039  0.0249  -0.0272 97  ARG   A CG    
699  C  CD    . ARG   A 100 ? 0.4668 0.4365 0.4294 0.0065  0.0292  -0.0190 97  ARG   A CD    
700  N  NE    . ARG   A 100 ? 0.4949 0.4679 0.4372 0.0101  0.0232  -0.0167 97  ARG   A NE    
701  C  CZ    . ARG   A 100 ? 0.5463 0.5239 0.4710 0.0090  0.0222  -0.0231 97  ARG   A CZ    
702  N  NH1   . ARG   A 100 ? 0.5250 0.5031 0.4513 0.0047  0.0282  -0.0344 97  ARG   A NH1   
703  N  NH2   . ARG   A 100 ? 0.6107 0.5937 0.5153 0.0134  0.0153  -0.0182 97  ARG   A NH2   
704  N  N     . GLU   A 101 ? 0.3631 0.3305 0.3805 -0.0058 0.0267  -0.0580 98  GLU   A N     
705  C  CA    . GLU   A 101 ? 0.3982 0.3664 0.4104 -0.0104 0.0216  -0.0741 98  GLU   A CA    
706  C  C     . GLU   A 101 ? 0.4008 0.3660 0.4363 -0.0179 0.0162  -0.0780 98  GLU   A C     
707  O  O     . GLU   A 101 ? 0.3991 0.3740 0.4335 -0.0243 0.0073  -0.0863 98  GLU   A O     
708  C  CB    . GLU   A 101 ? 0.4159 0.3750 0.4216 -0.0084 0.0295  -0.0881 98  GLU   A CB    
709  C  CG    . GLU   A 101 ? 0.4588 0.4158 0.4587 -0.0139 0.0251  -0.1091 98  GLU   A CG    
710  C  CD    . GLU   A 101 ? 0.4937 0.4437 0.4829 -0.0097 0.0348  -0.1246 98  GLU   A CD    
711  O  OE1   . GLU   A 101 ? 0.4422 0.3984 0.4192 -0.0035 0.0432  -0.1178 98  GLU   A OE1   
712  O  OE2   . GLU   A 101 ? 0.5489 0.4868 0.5435 -0.0129 0.0351  -0.1440 98  GLU   A OE2   
713  N  N     . GLN   A 102 ? 0.3967 0.3499 0.4530 -0.0179 0.0215  -0.0716 99  GLN   A N     
714  C  CA    . GLN   A 102 ? 0.4077 0.3540 0.4873 -0.0266 0.0187  -0.0727 99  GLN   A CA    
715  C  C     . GLN   A 102 ? 0.3562 0.3220 0.4426 -0.0313 0.0118  -0.0631 99  GLN   A C     
716  O  O     . GLN   A 102 ? 0.3546 0.3258 0.4530 -0.0414 0.0059  -0.0697 99  GLN   A O     
717  C  CB    . GLN   A 102 ? 0.4151 0.3451 0.5123 -0.0233 0.0263  -0.0625 99  GLN   A CB    
718  C  CG    . GLN   A 102 ? 0.5066 0.4167 0.6053 -0.0181 0.0330  -0.0735 99  GLN   A CG    
719  C  CD    . GLN   A 102 ? 0.5247 0.4244 0.6381 -0.0101 0.0396  -0.0597 99  GLN   A CD    
720  O  OE1   . GLN   A 102 ? 0.5232 0.4310 0.6429 -0.0097 0.0392  -0.0421 99  GLN   A OE1   
721  N  NE2   . GLN   A 102 ? 0.5674 0.4511 0.6856 -0.0025 0.0459  -0.0679 99  GLN   A NE2   
722  N  N     . ILE   A 103 ? 0.3400 0.3164 0.4200 -0.0240 0.0131  -0.0491 100 ILE   A N     
723  C  CA    . ILE   A 103 ? 0.3605 0.3568 0.4469 -0.0250 0.0082  -0.0405 100 ILE   A CA    
724  C  C     . ILE   A 103 ? 0.3781 0.3922 0.4562 -0.0266 -0.0019 -0.0491 100 ILE   A C     
725  O  O     . ILE   A 103 ? 0.3623 0.3937 0.4560 -0.0336 -0.0082 -0.0506 100 ILE   A O     
726  C  CB    . ILE   A 103 ? 0.3255 0.3255 0.4044 -0.0156 0.0127  -0.0265 100 ILE   A CB    
727  C  CG1   . ILE   A 103 ? 0.3205 0.3112 0.4109 -0.0157 0.0201  -0.0170 100 ILE   A CG1   
728  C  CG2   . ILE   A 103 ? 0.3274 0.3480 0.4087 -0.0124 0.0082  -0.0203 100 ILE   A CG2   
729  C  CD1   . ILE   A 103 ? 0.3085 0.2981 0.3868 -0.0079 0.0249  -0.0087 100 ILE   A CD1   
730  N  N     . LYS   A 104 ? 0.4002 0.4126 0.4541 -0.0205 -0.0034 -0.0536 101 LYS   A N     
731  C  CA    . LYS   A 104 ? 0.4385 0.4692 0.4787 -0.0198 -0.0140 -0.0597 101 LYS   A CA    
732  C  C     . LYS   A 104 ? 0.4336 0.4707 0.4836 -0.0324 -0.0214 -0.0770 101 LYS   A C     
733  O  O     . LYS   A 104 ? 0.4086 0.4702 0.4638 -0.0356 -0.0322 -0.0795 101 LYS   A O     
734  C  CB    . LYS   A 104 ? 0.4979 0.5221 0.5074 -0.0117 -0.0119 -0.0592 101 LYS   A CB    
735  C  CG    . LYS   A 104 ? 0.5353 0.5564 0.5342 -0.0011 -0.0078 -0.0427 101 LYS   A CG    
736  C  CD    . LYS   A 104 ? 0.5990 0.6115 0.5683 0.0040  -0.0041 -0.0404 101 LYS   A CD    
737  C  CE    . LYS   A 104 ? 0.6786 0.7044 0.6268 0.0045  -0.0131 -0.0471 101 LYS   A CE    
738  N  NZ    . LYS   A 104 ? 0.7465 0.7701 0.6678 0.0135  -0.0130 -0.0338 101 LYS   A NZ    
739  N  N     . ARG   A 105 ? 0.4254 0.4413 0.4808 -0.0392 -0.0157 -0.0885 102 ARG   A N     
740  C  CA    . ARG   A 105 ? 0.4793 0.4946 0.5425 -0.0525 -0.0217 -0.1080 102 ARG   A CA    
741  C  C     . ARG   A 105 ? 0.4744 0.5020 0.5684 -0.0645 -0.0262 -0.1046 102 ARG   A C     
742  O  O     . ARG   A 105 ? 0.4996 0.5479 0.6003 -0.0749 -0.0371 -0.1155 102 ARG   A O     
743  C  CB    . ARG   A 105 ? 0.5097 0.4938 0.5724 -0.0542 -0.0123 -0.1205 102 ARG   A CB    
744  C  CG    . ARG   A 105 ? 0.5861 0.5633 0.6516 -0.0674 -0.0174 -0.1454 102 ARG   A CG    
745  C  CD    . ARG   A 105 ? 0.6668 0.6099 0.7326 -0.0660 -0.0069 -0.1589 102 ARG   A CD    
746  N  NE    . ARG   A 105 ? 0.7299 0.6737 0.7668 -0.0544 -0.0018 -0.1655 102 ARG   A NE    
747  C  CZ    . ARG   A 105 ? 0.7316 0.6639 0.7644 -0.0417 0.0099  -0.1564 102 ARG   A CZ    
748  N  NH1   . ARG   A 105 ? 0.7436 0.6814 0.7506 -0.0337 0.0148  -0.1629 102 ARG   A NH1   
749  N  NH2   . ARG   A 105 ? 0.7229 0.6413 0.7773 -0.0377 0.0167  -0.1406 102 ARG   A NH2   
750  N  N     . VAL   A 106 ? 0.4792 0.4964 0.5915 -0.0636 -0.0175 -0.0893 103 VAL   A N     
751  C  CA    . VAL   A 106 ? 0.4856 0.5135 0.6269 -0.0746 -0.0177 -0.0817 103 VAL   A CA    
752  C  C     . VAL   A 106 ? 0.4636 0.5311 0.6099 -0.0725 -0.0265 -0.0758 103 VAL   A C     
753  O  O     . VAL   A 106 ? 0.4576 0.5469 0.6248 -0.0857 -0.0331 -0.0808 103 VAL   A O     
754  C  CB    . VAL   A 106 ? 0.4705 0.4813 0.6217 -0.0700 -0.0057 -0.0636 103 VAL   A CB    
755  C  CG1   . VAL   A 106 ? 0.4927 0.5204 0.6699 -0.0792 -0.0039 -0.0513 103 VAL   A CG1   
756  C  CG2   . VAL   A 106 ? 0.4905 0.4645 0.6431 -0.0715 0.0019  -0.0684 103 VAL   A CG2   
757  N  N     . LYS   A 107 ? 0.4565 0.5332 0.5856 -0.0559 -0.0262 -0.0648 104 LYS   A N     
758  C  CA    . LYS   A 107 ? 0.4875 0.5987 0.6231 -0.0495 -0.0327 -0.0567 104 LYS   A CA    
759  C  C     . LYS   A 107 ? 0.5270 0.6600 0.6481 -0.0467 -0.0467 -0.0665 104 LYS   A C     
760  O  O     . LYS   A 107 ? 0.5361 0.6991 0.6601 -0.0379 -0.0542 -0.0600 104 LYS   A O     
761  C  CB    . LYS   A 107 ? 0.4750 0.5816 0.6019 -0.0333 -0.0246 -0.0402 104 LYS   A CB    
762  C  CG    . LYS   A 107 ? 0.4811 0.5754 0.6226 -0.0368 -0.0127 -0.0301 104 LYS   A CG    
763  C  CD    . LYS   A 107 ? 0.4578 0.5525 0.5920 -0.0228 -0.0055 -0.0168 104 LYS   A CD    
764  C  CE    . LYS   A 107 ? 0.4325 0.5594 0.5850 -0.0198 -0.0060 -0.0104 104 LYS   A CE    
765  N  NZ    . LYS   A 107 ? 0.4455 0.5819 0.6244 -0.0351 -0.0013 -0.0078 104 LYS   A NZ    
766  N  N     . ASP   A 108 ? 0.5839 0.7027 0.6881 -0.0528 -0.0502 -0.0822 105 ASP   A N     
767  C  CA    . ASP   A 108 ? 0.6253 0.7638 0.7089 -0.0511 -0.0637 -0.0930 105 ASP   A CA    
768  C  C     . ASP   A 108 ? 0.6568 0.8119 0.7228 -0.0317 -0.0682 -0.0775 105 ASP   A C     
769  O  O     . ASP   A 108 ? 0.6658 0.8561 0.7358 -0.0290 -0.0816 -0.0772 105 ASP   A O     
770  C  CB    . ASP   A 108 ? 0.6569 0.8267 0.7603 -0.0672 -0.0773 -0.1075 105 ASP   A CB    
771  C  CG    . ASP   A 108 ? 0.7038 0.8957 0.7826 -0.0659 -0.0924 -0.1198 105 ASP   A CG    
772  O  OD1   . ASP   A 108 ? 0.7273 0.9084 0.7730 -0.0523 -0.0909 -0.1152 105 ASP   A OD1   
773  O  OD2   . ASP   A 108 ? 0.7331 0.9545 0.8255 -0.0795 -0.1056 -0.1337 105 ASP   A OD2   
774  N  N     . SER   A 109 ? 0.6348 0.7658 0.6860 -0.0190 -0.0572 -0.0642 106 SER   A N     
775  C  CA    . SER   A 109 ? 0.6624 0.8007 0.6972 -0.0007 -0.0596 -0.0485 106 SER   A CA    
776  C  C     . SER   A 109 ? 0.6812 0.7860 0.6910 0.0071  -0.0478 -0.0409 106 SER   A C     
777  O  O     . SER   A 109 ? 0.6267 0.7098 0.6443 0.0031  -0.0362 -0.0402 106 SER   A O     
778  C  CB    . SER   A 109 ? 0.6487 0.8037 0.7080 0.0063  -0.0585 -0.0369 106 SER   A CB    
779  O  OG    . SER   A 109 ? 0.6572 0.8154 0.7019 0.0254  -0.0608 -0.0230 106 SER   A OG    
780  N  N     . GLU   A 110 ? 0.7217 0.8255 0.7029 0.0178  -0.0514 -0.0338 107 GLU   A N     
781  C  CA    . GLU   A 110 ? 0.7533 0.8285 0.7094 0.0244  -0.0406 -0.0245 107 GLU   A CA    
782  C  C     . GLU   A 110 ? 0.7399 0.8016 0.7055 0.0335  -0.0327 -0.0105 107 GLU   A C     
783  O  O     . GLU   A 110 ? 0.7683 0.8044 0.7235 0.0334  -0.0213 -0.0060 107 GLU   A O     
784  C  CB    . GLU   A 110 ? 0.7782 0.8581 0.7010 0.0323  -0.0472 -0.0186 107 GLU   A CB    
785  C  CG    . GLU   A 110 ? 0.7210 0.8130 0.6283 0.0229  -0.0534 -0.0350 107 GLU   A CG    
786  C  CD    . GLU   A 110 ? 0.7537 0.8543 0.6242 0.0305  -0.0603 -0.0280 107 GLU   A CD    
787  O  OE1   . GLU   A 110 ? 0.7629 0.8600 0.6222 0.0443  -0.0619 -0.0082 107 GLU   A OE1   
788  O  OE2   . GLU   A 110 ? 0.7738 0.8834 0.6256 0.0231  -0.0636 -0.0423 107 GLU   A OE2   
789  N  N     . ASP   A 111 ? 0.6798 0.7606 0.6629 0.0414  -0.0388 -0.0047 108 ASP   A N     
790  C  CA    . ASP   A 111 ? 0.6571 0.7287 0.6492 0.0519  -0.0319 0.0062  108 ASP   A CA    
791  C  C     . ASP   A 111 ? 0.5923 0.6739 0.6149 0.0446  -0.0271 0.0014  108 ASP   A C     
792  O  O     . ASP   A 111 ? 0.6154 0.7268 0.6599 0.0428  -0.0342 -0.0017 108 ASP   A O     
793  C  CB    . ASP   A 111 ? 0.7241 0.8105 0.7126 0.0695  -0.0408 0.0169  108 ASP   A CB    
794  C  CG    . ASP   A 111 ? 0.7899 0.8683 0.7881 0.0833  -0.0344 0.0258  108 ASP   A CG    
795  O  OD1   . ASP   A 111 ? 0.8509 0.9005 0.8436 0.0813  -0.0224 0.0270  108 ASP   A OD1   
796  O  OD2   . ASP   A 111 ? 0.8532 0.9557 0.8643 0.0965  -0.0417 0.0306  108 ASP   A OD2   
797  N  N     . VAL   A 112 ? 0.4711 0.5308 0.4943 0.0392  -0.0157 0.0013  109 VAL   A N     
798  C  CA    . VAL   A 112 ? 0.4295 0.4948 0.4763 0.0330  -0.0092 0.0001  109 VAL   A CA    
799  C  C     . VAL   A 112 ? 0.3898 0.4347 0.4279 0.0397  0.0008  0.0064  109 VAL   A C     
800  O  O     . VAL   A 112 ? 0.3907 0.4127 0.4105 0.0384  0.0050  0.0069  109 VAL   A O     
801  C  CB    . VAL   A 112 ? 0.4101 0.4682 0.4645 0.0178  -0.0061 -0.0075 109 VAL   A CB    
802  C  CG1   . VAL   A 112 ? 0.4041 0.4623 0.4764 0.0128  0.0019  -0.0042 109 VAL   A CG1   
803  C  CG2   . VAL   A 112 ? 0.4466 0.5204 0.5097 0.0084  -0.0152 -0.0174 109 VAL   A CG2   
804  N  N     . PRO   A 113 ? 0.3499 0.4040 0.4006 0.0455  0.0052  0.0096  110 PRO   A N     
805  C  CA    . PRO   A 113 ? 0.3434 0.3775 0.3837 0.0504  0.0142  0.0122  110 PRO   A CA    
806  C  C     . PRO   A 113 ? 0.3520 0.3720 0.3889 0.0381  0.0200  0.0099  110 PRO   A C     
807  O  O     . PRO   A 113 ? 0.3415 0.3719 0.3926 0.0296  0.0206  0.0087  110 PRO   A O     
808  C  CB    . PRO   A 113 ? 0.3425 0.3971 0.4003 0.0564  0.0181  0.0132  110 PRO   A CB    
809  C  CG    . PRO   A 113 ? 0.3511 0.4353 0.4254 0.0606  0.0096  0.0137  110 PRO   A CG    
810  C  CD    . PRO   A 113 ? 0.3610 0.4468 0.4357 0.0474  0.0023  0.0098  110 PRO   A CD    
811  N  N     . MET   A 114 ? 0.3648 0.3613 0.3833 0.0381  0.0239  0.0103  111 MET   A N     
812  C  CA    . MET   A 114 ? 0.3468 0.3329 0.3622 0.0283  0.0288  0.0084  111 MET   A CA    
813  C  C     . MET   A 114 ? 0.3527 0.3189 0.3523 0.0296  0.0342  0.0088  111 MET   A C     
814  O  O     . MET   A 114 ? 0.3485 0.3011 0.3354 0.0362  0.0338  0.0109  111 MET   A O     
815  C  CB    . MET   A 114 ? 0.3893 0.3700 0.3988 0.0224  0.0266  0.0057  111 MET   A CB    
816  C  CG    . MET   A 114 ? 0.4280 0.4222 0.4513 0.0178  0.0218  0.0020  111 MET   A CG    
817  S  SD    . MET   A 114 ? 0.4916 0.4762 0.5069 0.0113  0.0231  -0.0044 111 MET   A SD    
818  C  CE    . MET   A 114 ? 0.5056 0.5038 0.5300 0.0081  0.0144  -0.0118 111 MET   A CE    
819  N  N     . VAL   A 115 ? 0.3362 0.3012 0.3373 0.0225  0.0384  0.0071  112 VAL   A N     
820  C  CA    . VAL   A 115 ? 0.3405 0.2886 0.3284 0.0192  0.0431  0.0051  112 VAL   A CA    
821  C  C     . VAL   A 115 ? 0.3574 0.3094 0.3485 0.0093  0.0445  0.0041  112 VAL   A C     
822  O  O     . VAL   A 115 ? 0.3387 0.3054 0.3428 0.0074  0.0433  0.0050  112 VAL   A O     
823  C  CB    . VAL   A 115 ? 0.3576 0.3065 0.3446 0.0218  0.0465  0.0019  112 VAL   A CB    
824  C  CG1   . VAL   A 115 ? 0.3913 0.3234 0.3658 0.0150  0.0505  -0.0029 112 VAL   A CG1   
825  C  CG2   . VAL   A 115 ? 0.3746 0.3215 0.3609 0.0343  0.0465  0.0022  112 VAL   A CG2   
826  N  N     . LEU   A 116 ? 0.3599 0.2993 0.3405 0.0041  0.0473  0.0034  113 LEU   A N     
827  C  CA    . LEU   A 116 ? 0.3550 0.3021 0.3408 -0.0044 0.0496  0.0018  113 LEU   A CA    
828  C  C     . LEU   A 116 ? 0.3546 0.3051 0.3410 -0.0106 0.0513  -0.0013 113 LEU   A C     
829  O  O     . LEU   A 116 ? 0.4201 0.3550 0.3951 -0.0137 0.0538  -0.0041 113 LEU   A O     
830  C  CB    . LEU   A 116 ? 0.3765 0.3130 0.3512 -0.0092 0.0535  0.0024  113 LEU   A CB    
831  C  CG    . LEU   A 116 ? 0.3524 0.3026 0.3359 -0.0165 0.0570  0.0003  113 LEU   A CG    
832  C  CD1   . LEU   A 116 ? 0.3441 0.3087 0.3418 -0.0111 0.0542  -0.0009 113 LEU   A CD1   
833  C  CD2   . LEU   A 116 ? 0.3684 0.3105 0.3396 -0.0221 0.0629  0.0016  113 LEU   A CD2   
834  N  N     . VAL   A 117 ? 0.3548 0.3250 0.3540 -0.0124 0.0496  -0.0008 114 VAL   A N     
835  C  CA    . VAL   A 117 ? 0.3325 0.3124 0.3317 -0.0186 0.0493  -0.0040 114 VAL   A CA    
836  C  C     . VAL   A 117 ? 0.3364 0.3333 0.3464 -0.0248 0.0493  -0.0038 114 VAL   A C     
837  O  O     . VAL   A 117 ? 0.3196 0.3305 0.3433 -0.0200 0.0476  0.0007  114 VAL   A O     
838  C  CB    . VAL   A 117 ? 0.3366 0.3307 0.3401 -0.0136 0.0464  -0.0014 114 VAL   A CB    
839  C  CG1   . VAL   A 117 ? 0.3401 0.3475 0.3400 -0.0203 0.0449  -0.0057 114 VAL   A CG1   
840  C  CG2   . VAL   A 117 ? 0.3270 0.3112 0.3243 -0.0062 0.0475  -0.0016 114 VAL   A CG2   
841  N  N     . GLY   A 118 ? 0.3446 0.3414 0.3502 -0.0355 0.0512  -0.0092 115 GLY   A N     
842  C  CA    . GLY   A 118 ? 0.3213 0.3421 0.3400 -0.0426 0.0507  -0.0100 115 GLY   A CA    
843  C  C     . GLY   A 118 ? 0.3289 0.3697 0.3495 -0.0464 0.0451  -0.0127 115 GLY   A C     
844  O  O     . GLY   A 118 ? 0.3456 0.3785 0.3553 -0.0558 0.0454  -0.0206 115 GLY   A O     
845  N  N     . ASN   A 119 ? 0.2987 0.3625 0.3312 -0.0386 0.0401  -0.0060 116 ASN   A N     
846  C  CA    . ASN   A 119 ? 0.3278 0.4152 0.3595 -0.0400 0.0334  -0.0058 116 ASN   A CA    
847  C  C     . ASN   A 119 ? 0.3496 0.4683 0.3947 -0.0480 0.0294  -0.0081 116 ASN   A C     
848  O  O     . ASN   A 119 ? 0.3408 0.4642 0.3993 -0.0488 0.0329  -0.0073 116 ASN   A O     
849  C  CB    . ASN   A 119 ? 0.3144 0.4107 0.3520 -0.0269 0.0302  0.0065  116 ASN   A CB    
850  C  CG    . ASN   A 119 ? 0.3235 0.4378 0.3517 -0.0266 0.0248  0.0088  116 ASN   A CG    
851  O  OD1   . ASN   A 119 ? 0.3371 0.4464 0.3486 -0.0335 0.0252  -0.0013 116 ASN   A OD1   
852  N  ND2   . ASN   A 119 ? 0.3079 0.4420 0.3453 -0.0181 0.0202  0.0221  116 ASN   A ND2   
853  N  N     . LYS   A 120 ? 0.3542 0.4972 0.3958 -0.0526 0.0221  -0.0106 117 LYS   A N     
854  C  CA    . LYS   A 120 ? 0.3448 0.5267 0.3992 -0.0605 0.0151  -0.0131 117 LYS   A CA    
855  C  C     . LYS   A 120 ? 0.3751 0.5520 0.4278 -0.0803 0.0185  -0.0277 117 LYS   A C     
856  O  O     . LYS   A 120 ? 0.3707 0.5750 0.4419 -0.0873 0.0172  -0.0288 117 LYS   A O     
857  C  CB    . LYS   A 120 ? 0.3400 0.5490 0.4192 -0.0479 0.0122  -0.0004 117 LYS   A CB    
858  C  CG    . LYS   A 120 ? 0.3212 0.5217 0.4025 -0.0294 0.0117  0.0147  117 LYS   A CG    
859  C  CD    . LYS   A 120 ? 0.3257 0.5559 0.4292 -0.0165 0.0063  0.0274  117 LYS   A CD    
860  C  CE    . LYS   A 120 ? 0.3148 0.5293 0.4224 0.0006  0.0074  0.0427  117 LYS   A CE    
861  N  NZ    . LYS   A 120 ? 0.3257 0.5657 0.4563 0.0152  0.0025  0.0556  117 LYS   A NZ    
862  N  N     . SER   A 121 ? 0.3865 0.5282 0.4191 -0.0881 0.0236  -0.0375 118 SER   A N     
863  C  CA    . SER   A 121 ? 0.4206 0.5480 0.4491 -0.1083 0.0281  -0.0506 118 SER   A CA    
864  C  C     . SER   A 121 ? 0.4429 0.6044 0.4759 -0.1255 0.0198  -0.0623 118 SER   A C     
865  O  O     . SER   A 121 ? 0.4530 0.6089 0.4889 -0.1451 0.0233  -0.0723 118 SER   A O     
866  C  CB    . SER   A 121 ? 0.4473 0.5275 0.4535 -0.1093 0.0347  -0.0571 118 SER   A CB    
867  O  OG    . SER   A 121 ? 0.4636 0.5426 0.4535 -0.1064 0.0303  -0.0643 118 SER   A OG    
868  N  N     . ASP   A 122 ? 0.4348 0.6310 0.4685 -0.1186 0.0092  -0.0595 119 ASP   A N     
869  C  CA    . ASP   A 122 ? 0.4539 0.6902 0.4907 -0.1338 -0.0015 -0.0706 119 ASP   A CA    
870  C  C     . ASP   A 122 ? 0.4478 0.7311 0.5161 -0.1356 -0.0061 -0.0635 119 ASP   A C     
871  O  O     . ASP   A 122 ? 0.4556 0.7783 0.5328 -0.1503 -0.0152 -0.0727 119 ASP   A O     
872  C  CB    . ASP   A 122 ? 0.4437 0.7022 0.4660 -0.1233 -0.0114 -0.0677 119 ASP   A CB    
873  C  CG    . ASP   A 122 ? 0.4151 0.6869 0.4477 -0.0994 -0.0133 -0.0451 119 ASP   A CG    
874  O  OD1   . ASP   A 122 ? 0.4213 0.6593 0.4483 -0.0870 -0.0051 -0.0370 119 ASP   A OD1   
875  O  OD2   . ASP   A 122 ? 0.4080 0.7227 0.4556 -0.0939 -0.0228 -0.0359 119 ASP   A OD2   
876  N  N     . LEU   A 123 ? 0.4113 0.6933 0.4967 -0.1203 -0.0003 -0.0488 120 LEU   A N     
877  C  CA    . LEU   A 123 ? 0.4168 0.7465 0.5342 -0.1173 -0.0038 -0.0418 120 LEU   A CA    
878  C  C     . LEU   A 123 ? 0.4478 0.7808 0.5806 -0.1371 0.0048  -0.0505 120 LEU   A C     
879  O  O     . LEU   A 123 ? 0.4430 0.7324 0.5646 -0.1422 0.0170  -0.0525 120 LEU   A O     
880  C  CB    . LEU   A 123 ? 0.3978 0.7227 0.5265 -0.0916 -0.0002 -0.0243 120 LEU   A CB    
881  C  CG    . LEU   A 123 ? 0.3916 0.7282 0.5160 -0.0716 -0.0095 -0.0106 120 LEU   A CG    
882  C  CD1   . LEU   A 123 ? 0.3867 0.7128 0.5253 -0.0494 -0.0042 0.0043  120 LEU   A CD1   
883  C  CD2   . LEU   A 123 ? 0.4003 0.7934 0.5369 -0.0725 -0.0241 -0.0086 120 LEU   A CD2   
884  N  N     . PRO   A 124 ? 0.4459 0.8321 0.6041 -0.1488 -0.0016 -0.0546 121 PRO   A N     
885  C  CA    . PRO   A 124 ? 0.4505 0.8487 0.6281 -0.1691 0.0076  -0.0613 121 PRO   A CA    
886  C  C     . PRO   A 124 ? 0.4652 0.8724 0.6649 -0.1535 0.0183  -0.0495 121 PRO   A C     
887  O  O     . PRO   A 124 ? 0.4926 0.8906 0.6984 -0.1661 0.0311  -0.0520 121 PRO   A O     
888  C  CB    . PRO   A 124 ? 0.4615 0.9227 0.6601 -0.1840 -0.0060 -0.0694 121 PRO   A CB    
889  C  CG    . PRO   A 124 ? 0.4474 0.9422 0.6509 -0.1583 -0.0199 -0.0572 121 PRO   A CG    
890  C  CD    . PRO   A 124 ? 0.4392 0.8799 0.6086 -0.1434 -0.0181 -0.0522 121 PRO   A CD    
891  N  N     . SER   A 125 ? 0.4404 0.8588 0.6483 -0.1253 0.0145  -0.0364 122 SER   A N     
892  C  CA    . SER   A 125 ? 0.4259 0.8524 0.6548 -0.1081 0.0248  -0.0278 122 SER   A CA    
893  C  C     . SER   A 125 ? 0.4012 0.7691 0.6076 -0.1007 0.0377  -0.0251 122 SER   A C     
894  O  O     . SER   A 125 ? 0.4125 0.7729 0.6232 -0.0777 0.0397  -0.0166 122 SER   A O     
895  C  CB    . SER   A 125 ? 0.4152 0.8745 0.6631 -0.0811 0.0152  -0.0157 122 SER   A CB    
896  O  OG    . SER   A 125 ? 0.4078 0.8377 0.6328 -0.0671 0.0076  -0.0081 122 SER   A OG    
897  N  N     . ARG   A 126 ? 0.3941 0.7263 0.5809 -0.1200 0.0465  -0.0321 123 ARG   A N     
898  C  CA    . ARG   A 126 ? 0.4049 0.6820 0.5665 -0.1154 0.0568  -0.0296 123 ARG   A CA    
899  C  C     . ARG   A 126 ? 0.3981 0.6792 0.5702 -0.1103 0.0706  -0.0266 123 ARG   A C     
900  O  O     . ARG   A 126 ? 0.4261 0.7341 0.6141 -0.1255 0.0781  -0.0299 123 ARG   A O     
901  C  CB    . ARG   A 126 ? 0.4289 0.6678 0.5662 -0.1371 0.0603  -0.0368 123 ARG   A CB    
902  C  CG    . ARG   A 126 ? 0.4587 0.6466 0.5721 -0.1323 0.0705  -0.0326 123 ARG   A CG    
903  C  CD    . ARG   A 126 ? 0.4916 0.6391 0.5833 -0.1516 0.0769  -0.0366 123 ARG   A CD    
904  N  NE    . ARG   A 126 ? 0.5225 0.6447 0.5962 -0.1539 0.0688  -0.0429 123 ARG   A NE    
905  C  CZ    . ARG   A 126 ? 0.5393 0.6215 0.5905 -0.1418 0.0681  -0.0406 123 ARG   A CZ    
906  N  NH1   . ARG   A 126 ? 0.5539 0.6198 0.5915 -0.1444 0.0619  -0.0484 123 ARG   A NH1   
907  N  NH2   . ARG   A 126 ? 0.4959 0.5577 0.5388 -0.1272 0.0734  -0.0318 123 ARG   A NH2   
908  N  N     . THR   A 127 ? 0.3810 0.6362 0.5432 -0.0909 0.0742  -0.0215 124 THR   A N     
909  C  CA    . THR   A 127 ? 0.3742 0.6305 0.5412 -0.0843 0.0877  -0.0206 124 THR   A CA    
910  C  C     . THR   A 127 ? 0.4122 0.6192 0.5478 -0.0867 0.0952  -0.0196 124 THR   A C     
911  O  O     . THR   A 127 ? 0.4284 0.6345 0.5610 -0.0866 0.1072  -0.0197 124 THR   A O     
912  C  CB    . THR   A 127 ? 0.3608 0.6399 0.5496 -0.0595 0.0862  -0.0179 124 THR   A CB    
913  O  OG1   . THR   A 127 ? 0.3485 0.5962 0.5237 -0.0434 0.0788  -0.0137 124 THR   A OG1   
914  C  CG2   . THR   A 127 ? 0.3463 0.6780 0.5672 -0.0565 0.0784  -0.0168 124 THR   A CG2   
915  N  N     . VAL   A 128 ? 0.3883 0.5591 0.5012 -0.0883 0.0883  -0.0186 125 VAL   A N     
916  C  CA    . VAL   A 128 ? 0.4015 0.5273 0.4853 -0.0884 0.0932  -0.0162 125 VAL   A CA    
917  C  C     . VAL   A 128 ? 0.4452 0.5456 0.5119 -0.1073 0.0938  -0.0172 125 VAL   A C     
918  O  O     . VAL   A 128 ? 0.4388 0.5320 0.5021 -0.1094 0.0850  -0.0202 125 VAL   A O     
919  C  CB    . VAL   A 128 ? 0.4067 0.5098 0.4802 -0.0701 0.0857  -0.0139 125 VAL   A CB    
920  C  CG1   . VAL   A 128 ? 0.4330 0.4983 0.4800 -0.0686 0.0895  -0.0114 125 VAL   A CG1   
921  C  CG2   . VAL   A 128 ? 0.4016 0.5244 0.4934 -0.0523 0.0844  -0.0135 125 VAL   A CG2   
922  N  N     . ASP   A 129 ? 0.4642 0.5498 0.5192 -0.1199 0.1049  -0.0145 126 ASP   A N     
923  C  CA    . ASP   A 129 ? 0.5137 0.5680 0.5520 -0.1381 0.1080  -0.0140 126 ASP   A CA    
924  C  C     . ASP   A 129 ? 0.5168 0.5259 0.5295 -0.1275 0.1032  -0.0110 126 ASP   A C     
925  O  O     . ASP   A 129 ? 0.4884 0.4858 0.4899 -0.1119 0.1034  -0.0058 126 ASP   A O     
926  C  CB    . ASP   A 129 ? 0.6029 0.6501 0.6331 -0.1523 0.1226  -0.0077 126 ASP   A CB    
927  C  CG    . ASP   A 129 ? 0.6413 0.7331 0.6978 -0.1684 0.1300  -0.0108 126 ASP   A CG    
928  O  OD1   . ASP   A 129 ? 0.6986 0.8188 0.7765 -0.1753 0.1224  -0.0186 126 ASP   A OD1   
929  O  OD2   . ASP   A 129 ? 0.7156 0.8168 0.7708 -0.1738 0.1433  -0.0054 126 ASP   A OD2   
930  N  N     . THR   A 130 ? 0.4982 0.4834 0.5022 -0.1367 0.0993  -0.0154 127 THR   A N     
931  C  CA    . THR   A 130 ? 0.5130 0.4568 0.4952 -0.1265 0.0958  -0.0135 127 THR   A CA    
932  C  C     . THR   A 130 ? 0.5363 0.4517 0.4986 -0.1210 0.1030  -0.0020 127 THR   A C     
933  O  O     . THR   A 130 ? 0.4972 0.3990 0.4484 -0.1033 0.0988  0.0024  127 THR   A O     
934  C  CB    . THR   A 130 ? 0.5254 0.4460 0.5012 -0.1399 0.0939  -0.0221 127 THR   A CB    
935  O  OG1   . THR   A 130 ? 0.5111 0.4676 0.5044 -0.1440 0.0859  -0.0323 127 THR   A OG1   
936  C  CG2   . THR   A 130 ? 0.5632 0.4463 0.5204 -0.1263 0.0901  -0.0225 127 THR   A CG2   
937  N  N     . LYS   A 131 ? 0.5363 0.4454 0.4942 -0.1369 0.1137  0.0036  128 LYS   A N     
938  C  CA    . LYS   A 131 ? 0.5811 0.4632 0.5160 -0.1331 0.1211  0.0171  128 LYS   A CA    
939  C  C     . LYS   A 131 ? 0.5348 0.4365 0.4674 -0.1146 0.1190  0.0202  128 LYS   A C     
940  O  O     . LYS   A 131 ? 0.5433 0.4225 0.4563 -0.1019 0.1165  0.0276  128 LYS   A O     
941  C  CB    . LYS   A 131 ? 0.6456 0.5271 0.5785 -0.1550 0.1347  0.0238  128 LYS   A CB    
942  C  CG    . LYS   A 131 ? 0.7131 0.5846 0.6242 -0.1502 0.1433  0.0386  128 LYS   A CG    
943  C  CD    . LYS   A 131 ? 0.7900 0.6268 0.6831 -0.1678 0.1550  0.0519  128 LYS   A CD    
944  C  CE    . LYS   A 131 ? 0.8313 0.6543 0.6960 -0.1591 0.1611  0.0691  128 LYS   A CE    
945  N  NZ    . LYS   A 131 ? 0.8902 0.6771 0.7366 -0.1770 0.1734  0.0854  128 LYS   A NZ    
946  N  N     . GLN   A 132 ? 0.4909 0.4333 0.4439 -0.1130 0.1195  0.0137  129 GLN   A N     
947  C  CA    . GLN   A 132 ? 0.4788 0.4391 0.4314 -0.0974 0.1189  0.0134  129 GLN   A CA    
948  C  C     . GLN   A 132 ? 0.4447 0.3930 0.3933 -0.0792 0.1068  0.0113  129 GLN   A C     
949  O  O     . GLN   A 132 ? 0.4234 0.3635 0.3571 -0.0679 0.1049  0.0146  129 GLN   A O     
950  C  CB    . GLN   A 132 ? 0.4805 0.4840 0.4600 -0.0979 0.1218  0.0055  129 GLN   A CB    
951  C  CG    . GLN   A 132 ? 0.5062 0.5257 0.4880 -0.0813 0.1217  0.0016  129 GLN   A CG    
952  C  CD    . GLN   A 132 ? 0.5392 0.5987 0.5496 -0.0787 0.1251  -0.0059 129 GLN   A CD    
953  O  OE1   . GLN   A 132 ? 0.5858 0.6657 0.6180 -0.0860 0.1231  -0.0083 129 GLN   A OE1   
954  N  NE2   . GLN   A 132 ? 0.5356 0.6078 0.5467 -0.0672 0.1299  -0.0106 129 GLN   A NE2   
955  N  N     . ALA   A 133 ? 0.4292 0.3803 0.3914 -0.0773 0.0985  0.0056  130 ALA   A N     
956  C  CA    . ALA   A 133 ? 0.4103 0.3527 0.3705 -0.0620 0.0886  0.0045  130 ALA   A CA    
957  C  C     . ALA   A 133 ? 0.4432 0.3512 0.3816 -0.0577 0.0868  0.0108  130 ALA   A C     
958  O  O     . ALA   A 133 ? 0.4732 0.3764 0.4059 -0.0444 0.0808  0.0126  130 ALA   A O     
959  C  CB    . ALA   A 133 ? 0.4077 0.3634 0.3848 -0.0613 0.0817  -0.0017 130 ALA   A CB    
960  N  N     . GLN   A 134 ? 0.4903 0.3747 0.4181 -0.0687 0.0919  0.0144  131 GLN   A N     
961  C  CA    . GLN   A 134 ? 0.5355 0.3835 0.4429 -0.0618 0.0907  0.0219  131 GLN   A CA    
962  C  C     . GLN   A 134 ? 0.5304 0.3739 0.4202 -0.0540 0.0920  0.0325  131 GLN   A C     
963  O  O     . GLN   A 134 ? 0.5520 0.3850 0.4324 -0.0393 0.0854  0.0369  131 GLN   A O     
964  C  CB    . GLN   A 134 ? 0.6064 0.4239 0.5051 -0.0764 0.0976  0.0242  131 GLN   A CB    
965  C  CG    . GLN   A 134 ? 0.6582 0.4747 0.5687 -0.0843 0.0951  0.0119  131 GLN   A CG    
966  C  CD    . GLN   A 134 ? 0.7142 0.4997 0.6174 -0.1024 0.1025  0.0112  131 GLN   A CD    
967  O  OE1   . GLN   A 134 ? 0.7803 0.5648 0.6818 -0.1186 0.1110  0.0169  131 GLN   A OE1   
968  N  NE2   . GLN   A 134 ? 0.7595 0.5193 0.6586 -0.1009 0.1000  0.0033  131 GLN   A NE2   
969  N  N     . ASP   A 135 ? 0.5257 0.3813 0.4116 -0.0635 0.1004  0.0359  132 ASP   A N     
970  C  CA    . ASP   A 135 ? 0.5178 0.3726 0.3830 -0.0579 0.1028  0.0453  132 ASP   A CA    
971  C  C     . ASP   A 135 ? 0.4879 0.3630 0.3570 -0.0426 0.0935  0.0389  132 ASP   A C     
972  O  O     . ASP   A 135 ? 0.5015 0.3691 0.3534 -0.0317 0.0879  0.0454  132 ASP   A O     
973  C  CB    . ASP   A 135 ? 0.5315 0.3999 0.3926 -0.0723 0.1158  0.0486  132 ASP   A CB    
974  C  CG    . ASP   A 135 ? 0.5635 0.4055 0.4153 -0.0891 0.1257  0.0588  132 ASP   A CG    
975  O  OD1   . ASP   A 135 ? 0.6070 0.4128 0.4443 -0.0854 0.1230  0.0679  132 ASP   A OD1   
976  O  OD2   . ASP   A 135 ? 0.5683 0.4264 0.4299 -0.1056 0.1360  0.0571  132 ASP   A OD2   
977  N  N     . LEU   A 136 ? 0.4477 0.3485 0.3400 -0.0424 0.0915  0.0266  133 LEU   A N     
978  C  CA    . LEU   A 136 ? 0.4376 0.3537 0.3361 -0.0303 0.0834  0.0195  133 LEU   A CA    
979  C  C     . LEU   A 136 ? 0.4094 0.3129 0.3063 -0.0193 0.0726  0.0219  133 LEU   A C     
980  O  O     . LEU   A 136 ? 0.4270 0.3334 0.3152 -0.0103 0.0659  0.0227  133 LEU   A O     
981  C  CB    . LEU   A 136 ? 0.4145 0.3545 0.3391 -0.0310 0.0836  0.0083  133 LEU   A CB    
982  C  CG    . LEU   A 136 ? 0.4196 0.3711 0.3516 -0.0208 0.0769  0.0003  133 LEU   A CG    
983  C  CD1   . LEU   A 136 ? 0.4591 0.4189 0.3767 -0.0195 0.0815  -0.0038 133 LEU   A CD1   
984  C  CD2   . LEU   A 136 ? 0.4053 0.3717 0.3643 -0.0190 0.0754  -0.0070 133 LEU   A CD2   
985  N  N     . ALA   A 137 ? 0.4283 0.3225 0.3356 -0.0200 0.0706  0.0212  134 ALA   A N     
986  C  CA    . ALA   A 137 ? 0.4195 0.3056 0.3278 -0.0088 0.0624  0.0226  134 ALA   A CA    
987  C  C     . ALA   A 137 ? 0.4632 0.3311 0.3498 -0.0005 0.0600  0.0335  134 ALA   A C     
988  O  O     . ALA   A 137 ? 0.4668 0.3405 0.3536 0.0113  0.0515  0.0347  134 ALA   A O     
989  C  CB    . ALA   A 137 ? 0.4181 0.2945 0.3352 -0.0121 0.0636  0.0196  134 ALA   A CB    
990  N  N     . ARG   A 138 ? 0.4843 0.3312 0.3537 -0.0071 0.0674  0.0424  135 ARG   A N     
991  C  CA    . ARG   A 138 ? 0.5606 0.3869 0.4063 0.0013  0.0659  0.0567  135 ARG   A CA    
992  C  C     . ARG   A 138 ? 0.5458 0.3937 0.3811 0.0078  0.0599  0.0581  135 ARG   A C     
993  O  O     . ARG   A 138 ? 0.5267 0.3733 0.3523 0.0205  0.0517  0.0653  135 ARG   A O     
994  C  CB    . ARG   A 138 ? 0.6475 0.4491 0.4757 -0.0107 0.0771  0.0674  135 ARG   A CB    
995  C  CG    . ARG   A 138 ? 0.7340 0.4994 0.5612 -0.0132 0.0811  0.0712  135 ARG   A CG    
996  C  CD    . ARG   A 138 ? 0.8177 0.5511 0.6234 -0.0230 0.0912  0.0865  135 ARG   A CD    
997  N  NE    . ARG   A 138 ? 0.8546 0.5931 0.6672 -0.0455 0.1022  0.0816  135 ARG   A NE    
998  C  CZ    . ARG   A 138 ? 0.8953 0.6184 0.7196 -0.0584 0.1068  0.0737  135 ARG   A CZ    
999  N  NH1   . ARG   A 138 ? 0.9160 0.6502 0.7491 -0.0797 0.1158  0.0692  135 ARG   A NH1   
1000 N  NH2   . ARG   A 138 ? 0.9412 0.6406 0.7691 -0.0500 0.1022  0.0689  135 ARG   A NH2   
1001 N  N     . SER   A 139 ? 0.5136 0.3823 0.3519 -0.0009 0.0643  0.0499  136 SER   A N     
1002 C  CA    . SER   A 139 ? 0.5117 0.4019 0.3394 0.0031  0.0597  0.0463  136 SER   A CA    
1003 C  C     . SER   A 139 ? 0.4918 0.3982 0.3348 0.0129  0.0467  0.0376  136 SER   A C     
1004 O  O     . SER   A 139 ? 0.4915 0.4078 0.3223 0.0202  0.0382  0.0394  136 SER   A O     
1005 C  CB    . SER   A 139 ? 0.5258 0.4331 0.3593 -0.0070 0.0686  0.0359  136 SER   A CB    
1006 O  OG    . SER   A 139 ? 0.5666 0.4907 0.3848 -0.0040 0.0662  0.0310  136 SER   A OG    
1007 N  N     . TYR   A 140 ? 0.4615 0.3716 0.3304 0.0118  0.0457  0.0292  137 TYR   A N     
1008 C  CA    . TYR   A 140 ? 0.4465 0.3723 0.3342 0.0180  0.0357  0.0214  137 TYR   A CA    
1009 C  C     . TYR   A 140 ? 0.4690 0.3885 0.3569 0.0295  0.0285  0.0298  137 TYR   A C     
1010 O  O     . TYR   A 140 ? 0.4836 0.4201 0.3839 0.0352  0.0196  0.0258  137 TYR   A O     
1011 C  CB    . TYR   A 140 ? 0.4161 0.3469 0.3290 0.0125  0.0391  0.0129  137 TYR   A CB    
1012 C  CG    . TYR   A 140 ? 0.4172 0.3585 0.3382 0.0053  0.0443  0.0033  137 TYR   A CG    
1013 C  CD1   . TYR   A 140 ? 0.4284 0.3777 0.3372 0.0042  0.0451  -0.0022 137 TYR   A CD1   
1014 C  CD2   . TYR   A 140 ? 0.4023 0.3474 0.3434 0.0012  0.0481  -0.0008 137 TYR   A CD2   
1015 C  CE1   . TYR   A 140 ? 0.4269 0.3849 0.3449 0.0001  0.0509  -0.0126 137 TYR   A CE1   
1016 C  CE2   . TYR   A 140 ? 0.4172 0.3721 0.3687 -0.0021 0.0526  -0.0087 137 TYR   A CE2   
1017 C  CZ    . TYR   A 140 ? 0.4184 0.3786 0.3592 -0.0021 0.0546  -0.0153 137 TYR   A CZ    
1018 O  OH    . TYR   A 140 ? 0.4350 0.4036 0.3873 -0.0031 0.0602  -0.0244 137 TYR   A OH    
1019 N  N     . GLY   A 141 ? 0.4731 0.3686 0.3492 0.0324  0.0331  0.0404  138 GLY   A N     
1020 C  CA    . GLY   A 141 ? 0.4929 0.3789 0.3700 0.0461  0.0280  0.0481  138 GLY   A CA    
1021 C  C     . GLY   A 141 ? 0.4710 0.3619 0.3720 0.0475  0.0285  0.0400  138 GLY   A C     
1022 O  O     . GLY   A 141 ? 0.5024 0.4040 0.4135 0.0592  0.0220  0.0408  138 GLY   A O     
1023 N  N     . ILE   A 142 ? 0.4267 0.3136 0.3362 0.0361  0.0359  0.0329  139 ILE   A N     
1024 C  CA    . ILE   A 142 ? 0.4081 0.3019 0.3366 0.0363  0.0369  0.0258  139 ILE   A CA    
1025 C  C     . ILE   A 142 ? 0.4399 0.3114 0.3637 0.0295  0.0451  0.0241  139 ILE   A C     
1026 O  O     . ILE   A 142 ? 0.4649 0.3226 0.3775 0.0197  0.0506  0.0264  139 ILE   A O     
1027 C  CB    . ILE   A 142 ? 0.3857 0.3045 0.3328 0.0294  0.0350  0.0177  139 ILE   A CB    
1028 C  CG1   . ILE   A 142 ? 0.3887 0.3064 0.3351 0.0169  0.0410  0.0141  139 ILE   A CG1   
1029 C  CG2   . ILE   A 142 ? 0.3688 0.3077 0.3215 0.0334  0.0266  0.0167  139 ILE   A CG2   
1030 C  CD1   . ILE   A 142 ? 0.3551 0.2922 0.3176 0.0126  0.0393  0.0078  139 ILE   A CD1   
1031 N  N     . PRO   A 143 ? 0.4394 0.3086 0.3714 0.0332  0.0467  0.0191  140 PRO   A N     
1032 C  CA    . PRO   A 143 ? 0.4347 0.2857 0.3625 0.0245  0.0535  0.0137  140 PRO   A CA    
1033 C  C     . PRO   A 143 ? 0.4266 0.2929 0.3621 0.0092  0.0556  0.0082  140 PRO   A C     
1034 O  O     . PRO   A 143 ? 0.3900 0.2808 0.3378 0.0085  0.0523  0.0072  140 PRO   A O     
1035 C  CB    . PRO   A 143 ? 0.4493 0.3032 0.3844 0.0340  0.0537  0.0075  140 PRO   A CB    
1036 C  CG    . PRO   A 143 ? 0.4455 0.3099 0.3855 0.0506  0.0481  0.0135  140 PRO   A CG    
1037 C  CD    . PRO   A 143 ? 0.4438 0.3289 0.3884 0.0458  0.0425  0.0176  140 PRO   A CD    
1038 N  N     . PHE   A 144 ? 0.4425 0.2936 0.3715 -0.0029 0.0611  0.0052  141 PHE   A N     
1039 C  CA    . PHE   A 144 ? 0.4296 0.2995 0.3684 -0.0164 0.0625  -0.0002 141 PHE   A CA    
1040 C  C     . PHE   A 144 ? 0.4472 0.3117 0.3856 -0.0230 0.0641  -0.0096 141 PHE   A C     
1041 O  O     . PHE   A 144 ? 0.4770 0.3124 0.4036 -0.0250 0.0679  -0.0123 141 PHE   A O     
1042 C  CB    . PHE   A 144 ? 0.4455 0.3129 0.3800 -0.0279 0.0672  0.0035  141 PHE   A CB    
1043 C  CG    . PHE   A 144 ? 0.4262 0.3137 0.3727 -0.0418 0.0693  -0.0023 141 PHE   A CG    
1044 C  CD1   . PHE   A 144 ? 0.4241 0.3418 0.3873 -0.0394 0.0651  -0.0050 141 PHE   A CD1   
1045 C  CD2   . PHE   A 144 ? 0.4703 0.3475 0.4129 -0.0574 0.0752  -0.0042 141 PHE   A CD2   
1046 C  CE1   . PHE   A 144 ? 0.4102 0.3501 0.3860 -0.0495 0.0657  -0.0090 141 PHE   A CE1   
1047 C  CE2   . PHE   A 144 ? 0.4595 0.3617 0.4162 -0.0702 0.0759  -0.0098 141 PHE   A CE2   
1048 C  CZ    . PHE   A 144 ? 0.4404 0.3757 0.4138 -0.0649 0.0707  -0.0119 141 PHE   A CZ    
1049 N  N     . ILE   A 145 ? 0.4449 0.3361 0.3950 -0.0262 0.0612  -0.0146 142 ILE   A N     
1050 C  CA    . ILE   A 145 ? 0.4471 0.3395 0.3948 -0.0336 0.0616  -0.0249 142 ILE   A CA    
1051 C  C     . ILE   A 145 ? 0.4110 0.3350 0.3712 -0.0436 0.0585  -0.0266 142 ILE   A C     
1052 O  O     . ILE   A 145 ? 0.3979 0.3447 0.3699 -0.0377 0.0552  -0.0204 142 ILE   A O     
1053 C  CB    . ILE   A 145 ? 0.4830 0.3784 0.4286 -0.0214 0.0603  -0.0287 142 ILE   A CB    
1054 C  CG1   . ILE   A 145 ? 0.5325 0.3979 0.4679 -0.0096 0.0635  -0.0282 142 ILE   A CG1   
1055 C  CG2   . ILE   A 145 ? 0.5239 0.4315 0.4664 -0.0286 0.0596  -0.0400 142 ILE   A CG2   
1056 C  CD1   . ILE   A 145 ? 0.5543 0.4327 0.4946 0.0062  0.0624  -0.0273 142 ILE   A CD1   
1057 N  N     . GLU   A 146 ? 0.4246 0.3492 0.3827 -0.0585 0.0593  -0.0351 143 GLU   A N     
1058 C  CA    . GLU   A 146 ? 0.4219 0.3813 0.3928 -0.0673 0.0550  -0.0373 143 GLU   A CA    
1059 C  C     . GLU   A 146 ? 0.4218 0.3971 0.3885 -0.0665 0.0500  -0.0448 143 GLU   A C     
1060 O  O     . GLU   A 146 ? 0.4807 0.4385 0.4337 -0.0710 0.0516  -0.0562 143 GLU   A O     
1061 C  CB    . GLU   A 146 ? 0.4453 0.4046 0.4192 -0.0863 0.0577  -0.0426 143 GLU   A CB    
1062 C  CG    . GLU   A 146 ? 0.4619 0.4180 0.4418 -0.0878 0.0632  -0.0336 143 GLU   A CG    
1063 C  CD    . GLU   A 146 ? 0.4690 0.4452 0.4612 -0.1057 0.0657  -0.0363 143 GLU   A CD    
1064 O  OE1   . GLU   A 146 ? 0.4592 0.4516 0.4561 -0.1186 0.0619  -0.0459 143 GLU   A OE1   
1065 O  OE2   . GLU   A 146 ? 0.4830 0.4635 0.4811 -0.1066 0.0713  -0.0293 143 GLU   A OE2   
1066 N  N     . THR   A 147 ? 0.3878 0.3959 0.3655 -0.0605 0.0445  -0.0381 144 THR   A N     
1067 C  CA    . THR   A 147 ? 0.3926 0.4199 0.3641 -0.0579 0.0399  -0.0415 144 THR   A CA    
1068 C  C     . THR   A 147 ? 0.4008 0.4670 0.3822 -0.0645 0.0323  -0.0403 144 THR   A C     
1069 O  O     . THR   A 147 ? 0.3689 0.4523 0.3676 -0.0651 0.0303  -0.0329 144 THR   A O     
1070 C  CB    . THR   A 147 ? 0.3697 0.4003 0.3425 -0.0421 0.0404  -0.0309 144 THR   A CB    
1071 O  OG1   . THR   A 147 ? 0.3433 0.3900 0.3335 -0.0367 0.0378  -0.0177 144 THR   A OG1   
1072 C  CG2   . THR   A 147 ? 0.3893 0.3899 0.3559 -0.0336 0.0463  -0.0310 144 THR   A CG2   
1073 N  N     . SER   A 148 ? 0.4063 0.4894 0.3761 -0.0673 0.0277  -0.0474 145 SER   A N     
1074 C  CA    . SER   A 148 ? 0.4134 0.5386 0.3898 -0.0680 0.0185  -0.0421 145 SER   A CA    
1075 C  C     . SER   A 148 ? 0.4130 0.5504 0.3771 -0.0571 0.0169  -0.0355 145 SER   A C     
1076 O  O     . SER   A 148 ? 0.4201 0.5513 0.3642 -0.0596 0.0188  -0.0476 145 SER   A O     
1077 C  CB    . SER   A 148 ? 0.4431 0.5870 0.4162 -0.0855 0.0126  -0.0572 145 SER   A CB    
1078 O  OG    . SER   A 148 ? 0.4646 0.6540 0.4422 -0.0836 0.0019  -0.0505 145 SER   A OG    
1079 N  N     . ALA   A 149 ? 0.3986 0.5512 0.3746 -0.0452 0.0147  -0.0165 146 ALA   A N     
1080 C  CA    . ALA   A 149 ? 0.4350 0.6050 0.4008 -0.0368 0.0130  -0.0062 146 ALA   A CA    
1081 C  C     . ALA   A 149 ? 0.4678 0.6740 0.4213 -0.0432 0.0037  -0.0106 146 ALA   A C     
1082 O  O     . ALA   A 149 ? 0.4648 0.6820 0.3980 -0.0415 0.0039  -0.0119 146 ALA   A O     
1083 C  CB    . ALA   A 149 ? 0.4146 0.5880 0.3971 -0.0246 0.0130  0.0159  146 ALA   A CB    
1084 N  N     . LYS   A 150 ? 0.4364 0.6645 0.4025 -0.0508 -0.0045 -0.0135 147 LYS   A N     
1085 C  CA    . LYS   A 150 ? 0.4877 0.7554 0.4446 -0.0589 -0.0157 -0.0197 147 LYS   A CA    
1086 C  C     . LYS   A 150 ? 0.5188 0.7780 0.4490 -0.0716 -0.0140 -0.0442 147 LYS   A C     
1087 O  O     . LYS   A 150 ? 0.5100 0.7929 0.4190 -0.0715 -0.0187 -0.0467 147 LYS   A O     
1088 C  CB    . LYS   A 150 ? 0.4816 0.7768 0.4621 -0.0655 -0.0243 -0.0196 147 LYS   A CB    
1089 C  CG    . LYS   A 150 ? 0.5185 0.8643 0.4943 -0.0728 -0.0388 -0.0235 147 LYS   A CG    
1090 C  CD    . LYS   A 150 ? 0.5254 0.9083 0.5314 -0.0726 -0.0478 -0.0156 147 LYS   A CD    
1091 C  CE    . LYS   A 150 ? 0.5815 1.0207 0.5845 -0.0800 -0.0643 -0.0196 147 LYS   A CE    
1092 N  NZ    . LYS   A 150 ? 0.5941 1.0722 0.6311 -0.0808 -0.0723 -0.0148 147 LYS   A NZ    
1093 N  N     . THR   A 151 ? 0.5403 0.7643 0.4700 -0.0820 -0.0068 -0.0622 148 THR   A N     
1094 C  CA    . THR   A 151 ? 0.5973 0.8079 0.5042 -0.0952 -0.0050 -0.0882 148 THR   A CA    
1095 C  C     . THR   A 151 ? 0.6170 0.7916 0.5063 -0.0856 0.0071  -0.0937 148 THR   A C     
1096 O  O     . THR   A 151 ? 0.6347 0.7991 0.5018 -0.0918 0.0097  -0.1148 148 THR   A O     
1097 C  CB    . THR   A 151 ? 0.6095 0.8056 0.5257 -0.1148 -0.0052 -0.1054 148 THR   A CB    
1098 O  OG1   . THR   A 151 ? 0.6614 0.8083 0.5822 -0.1128 0.0067  -0.1062 148 THR   A OG1   
1099 C  CG2   . THR   A 151 ? 0.5889 0.8230 0.5302 -0.1222 -0.0149 -0.0974 148 THR   A CG2   
1100 N  N     . ARG   A 152 ? 0.5931 0.7514 0.4932 -0.0705 0.0139  -0.0757 149 ARG   A N     
1101 C  CA    . ARG   A 152 ? 0.6365 0.7653 0.5284 -0.0585 0.0254  -0.0759 149 ARG   A CA    
1102 C  C     . ARG   A 152 ? 0.6359 0.7195 0.5291 -0.0623 0.0329  -0.0893 149 ARG   A C     
1103 O  O     . ARG   A 152 ? 0.6493 0.7089 0.5356 -0.0524 0.0415  -0.0928 149 ARG   A O     
1104 C  CB    . ARG   A 152 ? 0.7138 0.8574 0.5821 -0.0527 0.0287  -0.0818 149 ARG   A CB    
1105 C  CG    . ARG   A 152 ? 0.7769 0.9030 0.6447 -0.0380 0.0402  -0.0760 149 ARG   A CG    
1106 C  CD    . ARG   A 152 ? 0.8602 0.9996 0.7056 -0.0313 0.0472  -0.0836 149 ARG   A CD    
1107 N  NE    . ARG   A 152 ? 0.9533 1.0666 0.7974 -0.0204 0.0596  -0.0914 149 ARG   A NE    
1108 C  CZ    . ARG   A 152 ? 0.9883 1.1082 0.8401 -0.0079 0.0674  -0.0779 149 ARG   A CZ    
1109 N  NH1   . ARG   A 152 ? 0.9567 1.0559 0.8096 0.0025  0.0776  -0.0872 149 ARG   A NH1   
1110 N  NH2   . ARG   A 152 ? 1.0110 1.1585 0.8711 -0.0059 0.0651  -0.0549 149 ARG   A NH2   
1111 N  N     . GLN   A 153 ? 0.5973 0.6714 0.5007 -0.0753 0.0299  -0.0941 150 GLN   A N     
1112 C  CA    . GLN   A 153 ? 0.6069 0.6358 0.5102 -0.0799 0.0373  -0.1033 150 GLN   A CA    
1113 C  C     . GLN   A 153 ? 0.5419 0.5498 0.4562 -0.0651 0.0433  -0.0872 150 GLN   A C     
1114 O  O     . GLN   A 153 ? 0.4779 0.5030 0.4084 -0.0611 0.0401  -0.0708 150 GLN   A O     
1115 C  CB    . GLN   A 153 ? 0.6476 0.6785 0.5631 -0.0979 0.0335  -0.1063 150 GLN   A CB    
1116 C  CG    . GLN   A 153 ? 0.7274 0.7109 0.6393 -0.1062 0.0413  -0.1156 150 GLN   A CG    
1117 C  CD    . GLN   A 153 ? 0.7938 0.7843 0.7152 -0.1291 0.0382  -0.1226 150 GLN   A CD    
1118 O  OE1   . GLN   A 153 ? 0.8428 0.8699 0.7666 -0.1412 0.0296  -0.1305 150 GLN   A OE1   
1119 N  NE2   . GLN   A 153 ? 0.7744 0.7333 0.7017 -0.1354 0.0451  -0.1185 150 GLN   A NE2   
1120 N  N     . ARG   A 154 ? 0.5403 0.5159 0.4452 -0.0556 0.0511  -0.0926 151 ARG   A N     
1121 C  CA    . ARG   A 154 ? 0.5380 0.4916 0.4508 -0.0415 0.0563  -0.0805 151 ARG   A CA    
1122 C  C     . ARG   A 154 ? 0.4935 0.4726 0.4169 -0.0282 0.0551  -0.0643 151 ARG   A C     
1123 O  O     . ARG   A 154 ? 0.4648 0.4322 0.3968 -0.0191 0.0572  -0.0546 151 ARG   A O     
1124 C  CB    . ARG   A 154 ? 0.5224 0.4553 0.4439 -0.0487 0.0567  -0.0744 151 ARG   A CB    
1125 C  CG    . ARG   A 154 ? 0.5856 0.4889 0.4975 -0.0638 0.0595  -0.0887 151 ARG   A CG    
1126 C  CD    . ARG   A 154 ? 0.6221 0.4884 0.5347 -0.0631 0.0648  -0.0816 151 ARG   A CD    
1127 N  NE    . ARG   A 154 ? 0.6511 0.4895 0.5558 -0.0454 0.0697  -0.0806 151 ARG   A NE    
1128 C  CZ    . ARG   A 154 ? 0.6906 0.4971 0.5933 -0.0388 0.0736  -0.0719 151 ARG   A CZ    
1129 N  NH1   . ARG   A 154 ? 0.6971 0.4944 0.6027 -0.0498 0.0743  -0.0635 151 ARG   A NH1   
1130 N  NH2   . ARG   A 154 ? 0.7107 0.4971 0.6082 -0.0203 0.0770  -0.0709 151 ARG   A NH2   
1131 N  N     . VAL   A 155 ? 0.4638 0.4755 0.3848 -0.0277 0.0520  -0.0619 152 VAL   A N     
1132 C  CA    . VAL   A 155 ? 0.4455 0.4788 0.3772 -0.0175 0.0519  -0.0449 152 VAL   A CA    
1133 C  C     . VAL   A 155 ? 0.4545 0.4764 0.3843 -0.0047 0.0595  -0.0463 152 VAL   A C     
1134 O  O     . VAL   A 155 ? 0.4005 0.4191 0.3439 0.0021  0.0602  -0.0353 152 VAL   A O     
1135 C  CB    . VAL   A 155 ? 0.4473 0.5165 0.3742 -0.0197 0.0476  -0.0394 152 VAL   A CB    
1136 C  CG1   . VAL   A 155 ? 0.4215 0.5070 0.3589 -0.0106 0.0493  -0.0210 152 VAL   A CG1   
1137 C  CG2   . VAL   A 155 ? 0.4357 0.5215 0.3684 -0.0298 0.0388  -0.0368 152 VAL   A CG2   
1138 N  N     . GLU   A 156 ? 0.4863 0.5044 0.3998 -0.0017 0.0649  -0.0609 153 GLU   A N     
1139 C  CA    . GLU   A 156 ? 0.5149 0.5255 0.4292 0.0126  0.0729  -0.0632 153 GLU   A CA    
1140 C  C     . GLU   A 156 ? 0.5026 0.4820 0.4264 0.0187  0.0734  -0.0606 153 GLU   A C     
1141 O  O     . GLU   A 156 ? 0.4672 0.4512 0.4044 0.0290  0.0748  -0.0507 153 GLU   A O     
1142 C  CB    . GLU   A 156 ? 0.5611 0.5667 0.4551 0.0155  0.0796  -0.0834 153 GLU   A CB    
1143 C  CG    . GLU   A 156 ? 0.6091 0.6344 0.5030 0.0292  0.0885  -0.0831 153 GLU   A CG    
1144 C  CD    . GLU   A 156 ? 0.6559 0.6753 0.5276 0.0330  0.0963  -0.1064 153 GLU   A CD    
1145 O  OE1   . GLU   A 156 ? 0.6967 0.6804 0.5643 0.0395  0.1006  -0.1206 153 GLU   A OE1   
1146 O  OE2   . GLU   A 156 ? 0.7069 0.7557 0.5640 0.0294  0.0981  -0.1104 153 GLU   A OE2   
1147 N  N     . ASP   A 157 ? 0.5158 0.4657 0.4324 0.0109  0.0719  -0.0688 154 ASP   A N     
1148 C  CA    . ASP   A 157 ? 0.5010 0.4188 0.4216 0.0149  0.0724  -0.0651 154 ASP   A CA    
1149 C  C     . ASP   A 157 ? 0.4468 0.3767 0.3843 0.0183  0.0680  -0.0475 154 ASP   A C     
1150 O  O     . ASP   A 157 ? 0.4414 0.3610 0.3841 0.0300  0.0690  -0.0423 154 ASP   A O     
1151 C  CB    . ASP   A 157 ? 0.5618 0.4519 0.4738 0.0003  0.0712  -0.0725 154 ASP   A CB    
1152 C  CG    . ASP   A 157 ? 0.6128 0.4728 0.5080 -0.0015 0.0768  -0.0917 154 ASP   A CG    
1153 O  OD1   . ASP   A 157 ? 0.6475 0.5029 0.5373 0.0130  0.0825  -0.0994 154 ASP   A OD1   
1154 O  OD2   . ASP   A 157 ? 0.6481 0.4893 0.5370 -0.0176 0.0760  -0.0995 154 ASP   A OD2   
1155 N  N     . ALA   A 158 ? 0.4115 0.3634 0.3572 0.0091  0.0629  -0.0394 155 ALA   A N     
1156 C  CA    . ALA   A 158 ? 0.4034 0.3641 0.3642 0.0109  0.0591  -0.0258 155 ALA   A CA    
1157 C  C     . ALA   A 158 ? 0.3898 0.3682 0.3617 0.0216  0.0602  -0.0190 155 ALA   A C     
1158 O  O     . ALA   A 158 ? 0.3675 0.3425 0.3481 0.0277  0.0586  -0.0132 155 ALA   A O     
1159 C  CB    . ALA   A 158 ? 0.3955 0.3744 0.3636 0.0009  0.0546  -0.0201 155 ALA   A CB    
1160 N  N     . PHE   A 159 ? 0.3786 0.3796 0.3504 0.0226  0.0629  -0.0192 156 PHE   A N     
1161 C  CA    . PHE   A 159 ? 0.3879 0.4090 0.3727 0.0300  0.0653  -0.0119 156 PHE   A CA    
1162 C  C     . PHE   A 159 ? 0.3918 0.4056 0.3777 0.0435  0.0694  -0.0173 156 PHE   A C     
1163 O  O     . PHE   A 159 ? 0.3731 0.3973 0.3743 0.0494  0.0681  -0.0106 156 PHE   A O     
1164 C  CB    . PHE   A 159 ? 0.3945 0.4428 0.3772 0.0274  0.0688  -0.0087 156 PHE   A CB    
1165 C  CG    . PHE   A 159 ? 0.3810 0.4416 0.3698 0.0183  0.0640  0.0031  156 PHE   A CG    
1166 C  CD1   . PHE   A 159 ? 0.3670 0.4393 0.3735 0.0173  0.0633  0.0164  156 PHE   A CD1   
1167 C  CD2   . PHE   A 159 ? 0.3691 0.4300 0.3476 0.0110  0.0601  0.0008  156 PHE   A CD2   
1168 C  CE1   . PHE   A 159 ? 0.3632 0.4414 0.3761 0.0111  0.0595  0.0279  156 PHE   A CE1   
1169 C  CE2   . PHE   A 159 ? 0.3470 0.4199 0.3333 0.0060  0.0554  0.0131  156 PHE   A CE2   
1170 C  CZ    . PHE   A 159 ? 0.3424 0.4216 0.3452 0.0071  0.0556  0.0270  156 PHE   A CZ    
1171 N  N     . TYR   A 160 ? 0.4128 0.4092 0.3836 0.0486  0.0740  -0.0299 157 TYR   A N     
1172 C  CA    . TYR   A 160 ? 0.4342 0.4221 0.4060 0.0647  0.0790  -0.0355 157 TYR   A CA    
1173 C  C     . TYR   A 160 ? 0.4204 0.3834 0.3951 0.0707  0.0741  -0.0307 157 TYR   A C     
1174 O  O     . TYR   A 160 ? 0.4257 0.3916 0.4096 0.0853  0.0745  -0.0280 157 TYR   A O     
1175 C  CB    . TYR   A 160 ? 0.4853 0.4569 0.4386 0.0684  0.0862  -0.0523 157 TYR   A CB    
1176 C  CG    . TYR   A 160 ? 0.5321 0.5329 0.4802 0.0683  0.0930  -0.0584 157 TYR   A CG    
1177 C  CD1   . TYR   A 160 ? 0.5148 0.5514 0.4730 0.0621  0.0921  -0.0463 157 TYR   A CD1   
1178 C  CD2   . TYR   A 160 ? 0.6136 0.6045 0.5446 0.0739  0.1009  -0.0766 157 TYR   A CD2   
1179 C  CE1   . TYR   A 160 ? 0.5809 0.6455 0.5315 0.0615  0.0991  -0.0492 157 TYR   A CE1   
1180 C  CE2   . TYR   A 160 ? 0.6358 0.6563 0.5582 0.0738  0.1077  -0.0827 157 TYR   A CE2   
1181 C  CZ    . TYR   A 160 ? 0.6366 0.6954 0.5683 0.0676  0.1069  -0.0677 157 TYR   A CZ    
1182 O  OH    . TYR   A 160 ? 0.6698 0.7592 0.5907 0.0671  0.1145  -0.0710 157 TYR   A OH    
1183 N  N     . THR   A 161 ? 0.4049 0.3459 0.3715 0.0598  0.0696  -0.0289 158 THR   A N     
1184 C  CA    . THR   A 161 ? 0.4135 0.3344 0.3802 0.0641  0.0652  -0.0217 158 THR   A CA    
1185 C  C     . THR   A 161 ? 0.3661 0.3135 0.3503 0.0668  0.0593  -0.0112 158 THR   A C     
1186 O  O     . THR   A 161 ? 0.3813 0.3264 0.3696 0.0779  0.0559  -0.0060 158 THR   A O     
1187 C  CB    . THR   A 161 ? 0.4083 0.3061 0.3636 0.0498  0.0633  -0.0212 158 THR   A CB    
1188 O  OG1   . THR   A 161 ? 0.4546 0.3284 0.3955 0.0451  0.0684  -0.0327 158 THR   A OG1   
1189 C  CG2   . THR   A 161 ? 0.4296 0.3088 0.3815 0.0527  0.0597  -0.0121 158 THR   A CG2   
1190 N  N     . LEU   A 162 ? 0.3432 0.3143 0.3370 0.0559  0.0575  -0.0079 159 LEU   A N     
1191 C  CA    . LEU   A 162 ? 0.3217 0.3158 0.3330 0.0549  0.0525  -0.0002 159 LEU   A CA    
1192 C  C     . LEU   A 162 ? 0.3120 0.3288 0.3376 0.0670  0.0539  0.0007  159 LEU   A C     
1193 O  O     . LEU   A 162 ? 0.3236 0.3506 0.3600 0.0717  0.0481  0.0050  159 LEU   A O     
1194 C  CB    . LEU   A 162 ? 0.3213 0.3312 0.3401 0.0420  0.0521  0.0033  159 LEU   A CB    
1195 C  CG    . LEU   A 162 ? 0.3143 0.3412 0.3511 0.0375  0.0473  0.0097  159 LEU   A CG    
1196 C  CD1   . LEU   A 162 ? 0.3297 0.3443 0.3638 0.0381  0.0407  0.0098  159 LEU   A CD1   
1197 C  CD2   . LEU   A 162 ? 0.3185 0.3519 0.3609 0.0263  0.0478  0.0142  159 LEU   A CD2   
1198 N  N     . VAL   A 163 ? 0.3232 0.3529 0.3499 0.0715  0.0616  -0.0037 160 VAL   A N     
1199 C  CA    . VAL   A 163 ? 0.3303 0.3865 0.3732 0.0838  0.0648  -0.0034 160 VAL   A CA    
1200 C  C     . VAL   A 163 ? 0.3552 0.3976 0.3972 0.1008  0.0616  -0.0041 160 VAL   A C     
1201 O  O     . VAL   A 163 ? 0.3547 0.4198 0.4143 0.1088  0.0569  0.0007  160 VAL   A O     
1202 C  CB    . VAL   A 163 ? 0.3398 0.4083 0.3784 0.0886  0.0759  -0.0105 160 VAL   A CB    
1203 C  CG1   . VAL   A 163 ? 0.3488 0.4454 0.4053 0.1045  0.0808  -0.0114 160 VAL   A CG1   
1204 C  CG2   . VAL   A 163 ? 0.3364 0.4226 0.3748 0.0735  0.0789  -0.0065 160 VAL   A CG2   
1205 N  N     . ARG   A 164 ? 0.3818 0.3870 0.4034 0.1056  0.0636  -0.0093 161 ARG   A N     
1206 C  CA    . ARG   A 164 ? 0.4113 0.3956 0.4286 0.1228  0.0611  -0.0075 161 ARG   A CA    
1207 C  C     . ARG   A 164 ? 0.3916 0.3799 0.4135 0.1216  0.0499  0.0033  161 ARG   A C     
1208 O  O     . ARG   A 164 ? 0.4003 0.3949 0.4290 0.1376  0.0450  0.0087  161 ARG   A O     
1209 C  CB    . ARG   A 164 ? 0.4580 0.3960 0.4518 0.1235  0.0661  -0.0143 161 ARG   A CB    
1210 C  CG    . ARG   A 164 ? 0.5021 0.4351 0.4918 0.1334  0.0768  -0.0275 161 ARG   A CG    
1211 C  CD    . ARG   A 164 ? 0.5653 0.4497 0.5318 0.1294  0.0811  -0.0364 161 ARG   A CD    
1212 N  NE    . ARG   A 164 ? 0.6110 0.4860 0.5707 0.1391  0.0915  -0.0525 161 ARG   A NE    
1213 C  CZ    . ARG   A 164 ? 0.6481 0.5184 0.5941 0.1262  0.0970  -0.0667 161 ARG   A CZ    
1214 N  NH1   . ARG   A 164 ? 0.6331 0.5095 0.5732 0.1039  0.0924  -0.0650 161 ARG   A NH1   
1215 N  NH2   . ARG   A 164 ? 0.6857 0.5470 0.6239 0.1368  0.1067  -0.0834 161 ARG   A NH2   
1216 N  N     . GLU   A 165 ? 0.3792 0.3649 0.3964 0.1036  0.0455  0.0059  162 GLU   A N     
1217 C  CA    . GLU   A 165 ? 0.3830 0.3739 0.4016 0.1011  0.0355  0.0133  162 GLU   A CA    
1218 C  C     . GLU   A 165 ? 0.3669 0.3996 0.4099 0.1035  0.0295  0.0155  162 GLU   A C     
1219 O  O     . GLU   A 165 ? 0.3586 0.4021 0.4051 0.1098  0.0203  0.0204  162 GLU   A O     
1220 C  CB    . GLU   A 165 ? 0.3782 0.3577 0.3874 0.0824  0.0341  0.0132  162 GLU   A CB    
1221 C  CG    . GLU   A 165 ? 0.4197 0.3611 0.4061 0.0792  0.0380  0.0130  162 GLU   A CG    
1222 C  CD    . GLU   A 165 ? 0.4403 0.3617 0.4127 0.0885  0.0338  0.0210  162 GLU   A CD    
1223 O  OE1   . GLU   A 165 ? 0.4643 0.3924 0.4330 0.0837  0.0274  0.0257  162 GLU   A OE1   
1224 O  OE2   . GLU   A 165 ? 0.4866 0.3844 0.4503 0.1010  0.0372  0.0226  162 GLU   A OE2   
1225 N  N     . ILE   A 166 ? 0.3601 0.4173 0.4192 0.0963  0.0345  0.0123  163 ILE   A N     
1226 C  CA    . ILE   A 166 ? 0.3479 0.4469 0.4337 0.0944  0.0304  0.0141  163 ILE   A CA    
1227 C  C     . ILE   A 166 ? 0.3755 0.4937 0.4731 0.1157  0.0292  0.0154  163 ILE   A C     
1228 O  O     . ILE   A 166 ? 0.3734 0.5167 0.4852 0.1192  0.0195  0.0186  163 ILE   A O     
1229 C  CB    . ILE   A 166 ? 0.3385 0.4563 0.4371 0.0820  0.0385  0.0130  163 ILE   A CB    
1230 C  CG1   . ILE   A 166 ? 0.3386 0.4390 0.4284 0.0638  0.0381  0.0136  163 ILE   A CG1   
1231 C  CG2   . ILE   A 166 ? 0.3346 0.4959 0.4628 0.0797  0.0368  0.0151  163 ILE   A CG2   
1232 C  CD1   . ILE   A 166 ? 0.3447 0.4577 0.4420 0.0534  0.0461  0.0157  163 ILE   A CD1   
1233 N  N     . ARG   A 167 ? 0.4111 0.5166 0.5020 0.1300  0.0385  0.0120  164 ARG   A N     
1234 C  CA    . ARG   A 167 ? 0.4456 0.5666 0.5484 0.1544  0.0390  0.0127  164 ARG   A CA    
1235 C  C     . ARG   A 167 ? 0.4761 0.5809 0.5694 0.1670  0.0277  0.0203  164 ARG   A C     
1236 O  O     . ARG   A 167 ? 0.4796 0.6164 0.5914 0.1802  0.0202  0.0248  164 ARG   A O     
1237 C  CB    . ARG   A 167 ? 0.5023 0.6010 0.5937 0.1672  0.0521  0.0049  164 ARG   A CB    
1238 C  CG    . ARG   A 167 ? 0.5269 0.6547 0.6304 0.1622  0.0640  -0.0017 164 ARG   A CG    
1239 C  CD    . ARG   A 167 ? 0.5751 0.6784 0.6600 0.1669  0.0770  -0.0128 164 ARG   A CD    
1240 N  NE    . ARG   A 167 ? 0.5902 0.7338 0.6900 0.1657  0.0877  -0.0168 164 ARG   A NE    
1241 C  CZ    . ARG   A 167 ? 0.6465 0.7877 0.7353 0.1705  0.1009  -0.0279 164 ARG   A CZ    
1242 N  NH1   . ARG   A 167 ? 0.6555 0.7527 0.7185 0.1756  0.1047  -0.0383 164 ARG   A NH1   
1243 N  NH2   . ARG   A 167 ? 0.6159 0.7998 0.7189 0.1687  0.1108  -0.0289 164 ARG   A NH2   
1244 N  N     . GLN   A 168 ? 0.4905 0.5509 0.5564 0.1621  0.0264  0.0225  165 GLN   A N     
1245 C  CA    . GLN   A 168 ? 0.5405 0.5835 0.5930 0.1737  0.0165  0.0325  165 GLN   A CA    
1246 C  C     . GLN   A 168 ? 0.5285 0.6102 0.5943 0.1675  0.0027  0.0369  165 GLN   A C     
1247 O  O     . GLN   A 168 ? 0.5237 0.6231 0.5954 0.1841  -0.0071 0.0445  165 GLN   A O     
1248 C  CB    . GLN   A 168 ? 0.5957 0.5920 0.6181 0.1617  0.0179  0.0347  165 GLN   A CB    
1249 C  CG    . GLN   A 168 ? 0.6784 0.6297 0.6837 0.1659  0.0295  0.0305  165 GLN   A CG    
1250 C  CD    . GLN   A 168 ? 0.7692 0.7029 0.7734 0.1928  0.0313  0.0349  165 GLN   A CD    
1251 O  OE1   . GLN   A 168 ? 0.8535 0.7801 0.8516 0.2067  0.0233  0.0476  165 GLN   A OE1   
1252 N  NE2   . GLN   A 168 ? 0.8489 0.7751 0.8580 0.2016  0.0421  0.0244  165 GLN   A NE2   
1253 N  N     . TYR   A 169 ? 0.4843 0.5777 0.5544 0.1443  0.0019  0.0316  166 TYR   A N     
1254 C  CA    . TYR   A 169 ? 0.5035 0.6292 0.5851 0.1337  -0.0104 0.0317  166 TYR   A CA    
1255 C  C     . TYR   A 169 ? 0.5072 0.6845 0.6213 0.1421  -0.0157 0.0315  166 TYR   A C     
1256 O  O     . TYR   A 169 ? 0.4770 0.6825 0.5988 0.1450  -0.0293 0.0342  166 TYR   A O     
1257 C  CB    . TYR   A 169 ? 0.5223 0.6448 0.6047 0.1083  -0.0072 0.0247  166 TYR   A CB    
1258 C  CG    . TYR   A 169 ? 0.5593 0.7078 0.6524 0.0940  -0.0181 0.0211  166 TYR   A CG    
1259 C  CD1   . TYR   A 169 ? 0.5848 0.7248 0.6587 0.0921  -0.0280 0.0220  166 TYR   A CD1   
1260 C  CD2   . TYR   A 169 ? 0.5525 0.7322 0.6732 0.0805  -0.0176 0.0160  166 TYR   A CD2   
1261 C  CE1   . TYR   A 169 ? 0.6191 0.7816 0.7007 0.0782  -0.0380 0.0151  166 TYR   A CE1   
1262 C  CE2   . TYR   A 169 ? 0.5962 0.7957 0.7270 0.0652  -0.0275 0.0102  166 TYR   A CE2   
1263 C  CZ    . TYR   A 169 ? 0.6049 0.7957 0.7157 0.0644  -0.0381 0.0084  166 TYR   A CZ    
1264 O  OH    . TYR   A 169 ? 0.6482 0.8570 0.7664 0.0489  -0.0478 -0.0006 166 TYR   A OH    
1265 N  N     . ARG   A 170 ? 0.5020 0.6955 0.6353 0.1449  -0.0048 0.0278  167 ARG   A N     
1266 C  CA    . ARG   A 170 ? 0.5331 0.7813 0.7018 0.1491  -0.0071 0.0269  167 ARG   A CA    
1267 C  C     . ARG   A 170 ? 0.5871 0.8537 0.7635 0.1774  -0.0148 0.0334  167 ARG   A C     
1268 O  O     . ARG   A 170 ? 0.6034 0.9221 0.8097 0.1826  -0.0220 0.0341  167 ARG   A O     
1269 C  CB    . ARG   A 170 ? 0.5227 0.7835 0.7066 0.1440  0.0086  0.0222  167 ARG   A CB    
1270 C  CG    . ARG   A 170 ? 0.5105 0.7797 0.7030 0.1156  0.0119  0.0193  167 ARG   A CG    
1271 C  CD    . ARG   A 170 ? 0.5179 0.7956 0.7183 0.1128  0.0284  0.0175  167 ARG   A CD    
1272 N  NE    . ARG   A 170 ? 0.5019 0.7871 0.7110 0.0880  0.0335  0.0182  167 ARG   A NE    
1273 C  CZ    . ARG   A 170 ? 0.5368 0.8362 0.7533 0.0829  0.0473  0.0193  167 ARG   A CZ    
1274 N  NH1   . ARG   A 170 ? 0.5704 0.8812 0.7875 0.1008  0.0579  0.0169  167 ARG   A NH1   
1275 N  NH2   . ARG   A 170 ? 0.5688 0.8709 0.7916 0.0605  0.0511  0.0230  167 ARG   A NH2   
1276 N  N     . LEU   A 171 ? 0.6646 0.8886 0.8147 0.1954  -0.0138 0.0390  168 LEU   A N     
1277 C  CA    . LEU   A 171 ? 0.7545 0.9874 0.9089 0.2262  -0.0207 0.0480  168 LEU   A CA    
1278 C  C     . LEU   A 171 ? 0.8029 1.0299 0.9385 0.2288  -0.0377 0.0582  168 LEU   A C     
1279 O  O     . LEU   A 171 ? 0.8356 1.0627 0.9689 0.2556  -0.0445 0.0692  168 LEU   A O     
1280 C  CB    . LEU   A 171 ? 0.8025 0.9871 0.9392 0.2457  -0.0076 0.0485  168 LEU   A CB    
1281 C  CG    . LEU   A 171 ? 0.8148 0.9987 0.9610 0.2433  0.0103  0.0367  168 LEU   A CG    
1282 C  CD1   . LEU   A 171 ? 0.8559 0.9966 0.9875 0.2670  0.0212  0.0352  168 LEU   A CD1   
1283 C  CD2   . LEU   A 171 ? 0.7937 1.0428 0.9794 0.2454  0.0121  0.0327  168 LEU   A CD2   
1284 N  N     . LYS   A 172 ? 0.8053 1.0284 0.9280 0.2035  -0.0440 0.0548  169 LYS   A N     
1285 C  CA    . LYS   A 172 ? 0.8513 1.0690 0.9512 0.2025  -0.0586 0.0624  169 LYS   A CA    
1286 C  C     . LYS   A 172 ? 0.8751 1.1540 0.9978 0.2073  -0.0769 0.0639  169 LYS   A C     
1287 O  O     . LYS   A 172 ? 0.9596 1.2473 1.0721 0.2260  -0.0899 0.0758  169 LYS   A O     
1288 C  CB    . LYS   A 172 ? 0.8529 1.0468 0.9321 0.1742  -0.0569 0.0550  169 LYS   A CB    
1289 C  CG    . LYS   A 172 ? 0.8838 1.0195 0.9360 0.1688  -0.0425 0.0554  169 LYS   A CG    
1290 C  CD    . LYS   A 172 ? 0.9313 1.0273 0.9517 0.1836  -0.0435 0.0690  169 LYS   A CD    
1291 C  CE    . LYS   A 172 ? 0.9634 1.0053 0.9645 0.1795  -0.0279 0.0684  169 LYS   A CE    
1292 N  NZ    . LYS   A 172 ? 0.9553 0.9891 0.9547 0.1534  -0.0204 0.0567  169 LYS   A NZ    
1293 O  OXT   . LYS   A 172 ? 0.8826 1.2049 1.0344 0.1917  -0.0798 0.0539  169 LYS   A OXT   
1294 P  PG    . GNP   B .   ? 0.4134 0.4669 0.5526 0.0538  0.0271  0.1290  201 GNP   A PG    
1295 O  O1G   . GNP   B .   ? 0.4551 0.5013 0.5840 0.0457  0.0298  0.1390  201 GNP   A O1G   
1296 O  O2G   . GNP   B .   ? 0.4433 0.4900 0.5994 0.0685  0.0255  0.1455  201 GNP   A O2G   
1297 O  O3G   . GNP   B .   ? 0.4155 0.4477 0.5610 0.0503  0.0320  0.1103  201 GNP   A O3G   
1298 N  N3B   . GNP   B .   ? 0.3979 0.4888 0.5244 0.0510  0.0210  0.1233  201 GNP   A N3B   
1299 P  PB    . GNP   B .   ? 0.3793 0.4800 0.4849 0.0372  0.0216  0.1080  201 GNP   A PB    
1300 O  O1B   . GNP   B .   ? 0.3643 0.4527 0.4699 0.0311  0.0255  0.0877  201 GNP   A O1B   
1301 O  O2B   . GNP   B .   ? 0.3790 0.4779 0.4702 0.0315  0.0239  0.1160  201 GNP   A O2B   
1302 O  O3A   . GNP   B .   ? 0.3641 0.5005 0.4614 0.0363  0.0142  0.1068  201 GNP   A O3A   
1303 P  PA    . GNP   B .   ? 0.3696 0.5369 0.4511 0.0356  0.0073  0.1174  201 GNP   A PA    
1304 O  O1A   . GNP   B .   ? 0.3768 0.5430 0.4656 0.0471  0.0055  0.1422  201 GNP   A O1A   
1305 O  O2A   . GNP   B .   ? 0.3711 0.5392 0.4298 0.0244  0.0101  0.1071  201 GNP   A O2A   
1306 O  "O5'" . GNP   B .   ? 0.3748 0.5736 0.4624 0.0355  -0.0005 0.1092  201 GNP   A "O5'" 
1307 C  "C5'" . GNP   B .   ? 0.3679 0.5752 0.4798 0.0466  -0.0031 0.1139  201 GNP   A "C5'" 
1308 C  "C4'" . GNP   B .   ? 0.3692 0.6198 0.4831 0.0440  -0.0127 0.1095  201 GNP   A "C4'" 
1309 O  "O4'" . GNP   B .   ? 0.3491 0.6003 0.4522 0.0269  -0.0103 0.0868  201 GNP   A "O4'" 
1310 C  "C3'" . GNP   B .   ? 0.3904 0.6715 0.4880 0.0452  -0.0226 0.1228  201 GNP   A "C3'" 
1311 O  "O3'" . GNP   B .   ? 0.4303 0.7552 0.5406 0.0510  -0.0339 0.1274  201 GNP   A "O3'" 
1312 C  "C2'" . GNP   B .   ? 0.3886 0.6701 0.4606 0.0272  -0.0211 0.1040  201 GNP   A "C2'" 
1313 O  "O2'" . GNP   B .   ? 0.3995 0.7187 0.4553 0.0237  -0.0315 0.1062  201 GNP   A "O2'" 
1314 C  "C1'" . GNP   B .   ? 0.3684 0.6456 0.4521 0.0177  -0.0177 0.0829  201 GNP   A "C1'" 
1315 N  N9    . GNP   B .   ? 0.3566 0.6136 0.4222 0.0022  -0.0116 0.0632  201 GNP   A N9    
1316 C  C8    . GNP   B .   ? 0.3411 0.5634 0.3937 0.0005  -0.0028 0.0604  201 GNP   A C8    
1317 N  N7    . GNP   B .   ? 0.3444 0.5534 0.3837 -0.0117 0.0011  0.0422  201 GNP   A N7    
1318 C  C5    . GNP   B .   ? 0.3367 0.5705 0.3797 -0.0213 -0.0048 0.0315  201 GNP   A C5    
1319 C  C6    . GNP   B .   ? 0.3685 0.5973 0.4020 -0.0376 -0.0034 0.0113  201 GNP   A C6    
1320 O  O6    . GNP   B .   ? 0.3646 0.5631 0.3840 -0.0441 0.0037  -0.0004 201 GNP   A O6    
1321 N  N1    . GNP   B .   ? 0.3568 0.6196 0.4015 -0.0462 -0.0109 0.0055  201 GNP   A N1    
1322 C  C2    . GNP   B .   ? 0.3638 0.6647 0.4272 -0.0373 -0.0196 0.0184  201 GNP   A C2    
1323 N  N2    . GNP   B .   ? 0.3644 0.7015 0.4394 -0.0479 -0.0270 0.0101  201 GNP   A N2    
1324 N  N3    . GNP   B .   ? 0.3576 0.6610 0.4292 -0.0191 -0.0210 0.0386  201 GNP   A N3    
1325 C  C4    . GNP   B .   ? 0.3515 0.6186 0.4116 -0.0131 -0.0130 0.0439  201 GNP   A C4    
1326 MG MG    . MG    C .   ? 0.3884 0.4656 0.4869 0.0340  0.0292  0.1440  202 MG    A MG    
1327 CO CO    . CO    D .   ? 0.9717 1.4601 0.7820 0.0049  -0.0464 0.1335  203 CO    A CO    
1328 CO CO    . CO    E .   ? 0.5124 0.4675 0.4818 0.0056  0.0617  -0.1339 204 CO    A CO    
1329 C  CBK   . A1IMA F .   ? 0.6782 0.6954 0.8642 -0.0850 0.1076  0.2473  205 A1IMA A CBK   
1330 C  CBL   . A1IMA F .   ? 0.7523 0.7612 0.9312 -0.0872 0.1154  0.2832  205 A1IMA A CBL   
1331 C  CBM   . A1IMA F .   ? 0.7700 0.7685 0.9293 -0.0670 0.1076  0.2939  205 A1IMA A CBM   
1332 N  NBP   . A1IMA F .   ? 0.7802 0.8162 0.9155 -0.0549 0.1030  0.2815  205 A1IMA A NBP   
1333 C  CBN   . A1IMA F .   ? 0.7479 0.7105 0.9190 -0.0584 0.0984  0.2791  205 A1IMA A CBN   
1334 C  CBO   . A1IMA F .   ? 0.6995 0.6765 0.8724 -0.0572 0.0923  0.2446  205 A1IMA A CBO   
1335 C  CBJ   . A1IMA F .   ? 0.6748 0.6541 0.8673 -0.0764 0.0979  0.2347  205 A1IMA A CBJ   
1336 N  NAQ   . A1IMA F .   ? 0.5996 0.5820 0.7987 -0.0760 0.0908  0.2028  205 A1IMA A NAQ   
1337 C  CAB   . A1IMA F .   ? 0.6105 0.5693 0.8308 -0.0878 0.0895  0.1903  205 A1IMA A CAB   
1338 O  OAA   . A1IMA F .   ? 0.6369 0.5695 0.8723 -0.0997 0.0947  0.2043  205 A1IMA A OAA   
1339 C  CAR   . A1IMA F .   ? 0.5451 0.5563 0.7265 -0.0641 0.0857  0.1856  205 A1IMA A CAR   
1340 C  CAS   . A1IMA F .   ? 0.5243 0.5767 0.7008 -0.0688 0.0918  0.1834  205 A1IMA A CAS   
1341 C  CAT   . A1IMA F .   ? 0.5008 0.5645 0.6982 -0.0813 0.0927  0.1683  205 A1IMA A CAT   
1342 C  CAU   . A1IMA F .   ? 0.4734 0.5799 0.6651 -0.0793 0.0978  0.1633  205 A1IMA A CAU   
1343 C  CAV   . A1IMA F .   ? 0.4430 0.5690 0.6579 -0.0889 0.0971  0.1478  205 A1IMA A CAV   
1344 N  NAW   . A1IMA F .   ? 0.3966 0.5094 0.6137 -0.0837 0.0856  0.1254  205 A1IMA A NAW   
1345 C  CAX   . A1IMA F .   ? 0.3879 0.5095 0.5888 -0.0685 0.0803  0.1111  205 A1IMA A CAX   
1346 C  CAY   . A1IMA F .   ? 0.3755 0.5157 0.5574 -0.0561 0.0838  0.1111  205 A1IMA A CAY   
1347 O  OBD   . A1IMA F .   ? 0.3602 0.5179 0.5358 -0.0577 0.0939  0.1268  205 A1IMA A OBD   
1348 C  CAZ   . A1IMA F .   ? 0.3517 0.4924 0.5188 -0.0422 0.0780  0.0953  205 A1IMA A CAZ   
1349 C  CBA   . A1IMA F .   ? 0.3415 0.4659 0.5125 -0.0409 0.0684  0.0813  205 A1IMA A CBA   
1350 C  CBB   . A1IMA F .   ? 0.3744 0.4833 0.5629 -0.0530 0.0645  0.0805  205 A1IMA A CBB   
1351 CL CLBC  . A1IMA F .   ? 0.3854 0.4786 0.5739 -0.0511 0.0534  0.0623  205 A1IMA A CLBC  
1352 C  CBI   . A1IMA F .   ? 0.3729 0.4797 0.5770 -0.0668 0.0703  0.0941  205 A1IMA A CBI   
1353 S  SBH   . A1IMA F .   ? 0.3945 0.4815 0.6192 -0.0827 0.0683  0.0941  205 A1IMA A SBH   
1354 C  CBG   . A1IMA F .   ? 0.4262 0.5161 0.6594 -0.0938 0.0797  0.1173  205 A1IMA A CBG   
1355 N  NBF   . A1IMA F .   ? 0.4494 0.5225 0.7010 -0.1109 0.0841  0.1286  205 A1IMA A NBF   
1356 S  SAH   . A1IMA F .   ? 0.5228 0.5573 0.7851 -0.1189 0.0783  0.1202  205 A1IMA A SAH   
1357 O  OAI   . A1IMA F .   ? 0.5252 0.5668 0.7925 -0.1193 0.0681  0.0950  205 A1IMA A OAI   
1358 O  OBE   . A1IMA F .   ? 0.5470 0.5706 0.8334 -0.1412 0.0847  0.1309  205 A1IMA A OBE   
1359 C  CAG   . A1IMA F .   ? 0.5490 0.5476 0.7923 -0.1036 0.0768  0.1277  205 A1IMA A CAG   
1360 C  CAF   . A1IMA F .   ? 0.5493 0.5343 0.7789 -0.0893 0.0686  0.1117  205 A1IMA A CAF   
1361 N  NAE   . A1IMA F .   ? 0.5546 0.5169 0.7717 -0.0761 0.0681  0.1197  205 A1IMA A NAE   
1362 C  CAJ   . A1IMA F .   ? 0.5669 0.5550 0.8057 -0.1029 0.0844  0.1530  205 A1IMA A CAJ   
1363 C  CAC   . A1IMA F .   ? 0.5900 0.5549 0.8144 -0.0880 0.0824  0.1619  205 A1IMA A CAC   
1364 C  CAD   . A1IMA F .   ? 0.6022 0.5560 0.8169 -0.0741 0.0740  0.1439  205 A1IMA A CAD   
1365 N  NAK   . A1IMA F .   ? 0.6406 0.5773 0.8446 -0.0589 0.0715  0.1503  205 A1IMA A NAK   
1366 C  CAL   . A1IMA F .   ? 0.6964 0.6065 0.9041 -0.0551 0.0747  0.1722  205 A1IMA A CAL   
1367 C  CAM   . A1IMA F .   ? 0.7354 0.6072 0.9549 -0.0521 0.0714  0.1579  205 A1IMA A CAM   
1368 N  NAN   . A1IMA F .   ? 0.7326 0.6121 0.9410 -0.0378 0.0647  0.1379  205 A1IMA A NAN   
1369 C  CAO   . A1IMA F .   ? 0.6813 0.5920 0.8807 -0.0421 0.0615  0.1205  205 A1IMA A CAO   
1370 C  CAP   . A1IMA F .   ? 0.6477 0.5909 0.8376 -0.0445 0.0648  0.1342  205 A1IMA A CAP   
1371 O  O     . HOH   G .   ? 0.3894 0.3514 0.3727 0.0606  0.0216  0.0197  301 HOH   A O     
1372 O  O     . HOH   G .   ? 0.6163 0.7305 0.6688 0.0081  0.0518  0.1800  302 HOH   A O     
1373 O  O     . HOH   G .   ? 0.4972 0.7346 0.4395 -0.0047 0.0124  0.0677  303 HOH   A O     
1374 O  O     . HOH   G .   ? 0.4254 0.4768 0.5263 0.0217  0.0371  0.1247  304 HOH   A O     
1375 O  O     . HOH   G .   ? 0.5746 0.6021 0.4503 -0.0266 0.0592  -0.0970 305 HOH   A O     
1376 O  O     . HOH   G .   ? 0.4096 0.5265 0.5013 0.0463  0.0182  0.1649  306 HOH   A O     
1377 O  O     . HOH   G .   ? 0.4459 0.4202 0.4020 0.0004  0.0391  -0.0552 307 HOH   A O     
1378 O  O     . HOH   G .   ? 0.4319 0.3745 0.5685 -0.0071 0.0413  0.0235  308 HOH   A O     
1379 O  O     . HOH   G .   ? 0.5561 0.8390 0.7530 0.1503  0.0597  0.0093  309 HOH   A O     
1380 O  O     . HOH   G .   ? 0.5836 0.3842 0.4606 0.0136  0.0614  0.0425  310 HOH   A O     
1381 O  O     . HOH   G .   ? 0.5843 0.3959 0.4035 0.0486  0.0417  0.0837  311 HOH   A O     
1382 O  O     . HOH   G .   ? 0.5723 0.5529 0.4980 -0.0029 0.0702  -0.0412 312 HOH   A O     
1383 O  O     . HOH   G .   ? 0.6471 0.5434 0.5461 0.0457  0.0913  -0.0969 313 HOH   A O     
1384 O  O     . HOH   G .   ? 0.3910 0.8140 0.6375 -0.0141 0.0084  0.0172  314 HOH   A O     
1385 O  O     . HOH   G .   ? 0.6058 0.5992 0.5615 -0.1043 0.0439  -0.0778 315 HOH   A O     
1386 O  O     . HOH   G .   ? 0.6386 1.0343 0.8902 0.2716  0.1316  -0.0300 316 HOH   A O     
1387 O  O     . HOH   G .   ? 0.5341 0.4922 0.3771 0.0018  0.0533  -0.0001 317 HOH   A O     
1388 O  O     . HOH   G .   ? 0.6906 0.9456 0.5273 0.0192  0.1074  -0.0162 318 HOH   A O     
1389 O  O     . HOH   G .   ? 0.6525 0.5349 0.5798 0.0815  0.0265  0.0410  319 HOH   A O     
1390 O  O     . HOH   G .   ? 0.3539 0.5760 0.5133 0.0159  0.0213  0.0372  320 HOH   A O     
1391 O  O     . HOH   G .   ? 0.5639 0.5470 0.5952 0.1963  0.0869  -0.0305 321 HOH   A O     
1392 O  O     . HOH   G .   ? 0.5239 0.4585 0.4332 -0.1240 0.1477  0.0381  322 HOH   A O     
1393 O  O     . HOH   G .   ? 0.3207 0.3401 0.4130 0.0141  0.0509  0.0080  323 HOH   A O     
1394 O  O     . HOH   G .   ? 0.7870 0.7607 0.7208 0.0253  0.0116  0.0025  324 HOH   A O     
1395 O  O     . HOH   G .   ? 0.6832 0.6199 0.5510 -0.0646 0.0586  -0.1359 325 HOH   A O     
1396 O  O     . HOH   G .   ? 0.5873 0.5471 0.6121 0.1865  0.0609  -0.0017 326 HOH   A O     
1397 O  O     . HOH   G .   ? 0.6704 1.1922 0.4668 -0.0113 -0.0613 0.0941  327 HOH   A O     
1398 O  O     . HOH   G .   ? 0.5238 0.5205 0.5004 0.0359  0.0032  0.0065  328 HOH   A O     
1399 O  O     . HOH   G .   ? 0.9064 1.3641 0.7294 0.0173  -0.0325 0.1704  329 HOH   A O     
1400 O  O     . HOH   G .   ? 0.5356 0.5491 0.5528 -0.0861 0.0755  -0.0160 330 HOH   A O     
1401 O  O     . HOH   G .   ? 0.6617 0.4996 0.5917 0.0755  0.0802  -0.0492 331 HOH   A O     
1402 O  O     . HOH   G .   ? 0.4935 0.4300 0.4638 0.0012  0.0581  -0.1696 332 HOH   A O     
1403 O  O     . HOH   G .   ? 0.5352 0.5355 0.5221 -0.0254 -0.0063 -0.1075 333 HOH   A O     
1404 O  O     . HOH   G .   ? 0.8337 1.2216 0.7272 0.0279  -0.0251 0.1847  334 HOH   A O     
1405 O  O     . HOH   G .   ? 0.6694 0.6255 0.6398 -0.1374 0.0586  -0.0732 335 HOH   A O     
1406 O  O     . HOH   G .   ? 0.4634 0.4274 0.6126 0.0482  0.0605  -0.0034 336 HOH   A O     
1407 O  O     . HOH   G .   ? 0.3548 0.3196 0.4835 0.0090  0.0431  0.0447  337 HOH   A O     
1408 O  O     . HOH   G .   ? 0.4760 0.5330 0.5814 0.0330  0.0350  0.1698  338 HOH   A O     
1409 O  O     . HOH   G .   ? 0.4662 0.6266 0.6264 0.0364  0.0308  0.0445  339 HOH   A O     
1410 O  O     . HOH   G .   ? 0.5655 0.5329 0.4928 0.0556  0.0013  0.0281  340 HOH   A O     
1411 O  O     . HOH   G .   ? 0.7324 0.6647 0.5556 0.0461  0.0120  0.0512  341 HOH   A O     
1412 O  O     . HOH   G .   ? 0.3688 0.6969 0.5027 0.0088  -0.0204 0.0596  342 HOH   A O     
1413 O  O     . HOH   G .   ? 0.6250 0.6251 0.7719 0.0491  0.0367  0.1778  343 HOH   A O     
1414 O  O     . HOH   G .   ? 0.5310 0.4369 0.6748 -0.0017 0.0441  -0.0041 344 HOH   A O     
1415 O  O     . HOH   G .   ? 0.5931 0.5291 0.6080 0.0108  0.0638  -0.1237 345 HOH   A O     
1416 O  O     . HOH   G .   ? 0.6104 0.8395 0.7422 -0.0505 0.1239  0.1589  346 HOH   A O     
1417 O  O     . HOH   G .   ? 0.4367 0.4476 0.5146 0.0369  0.0972  -0.0702 347 HOH   A O     
1418 O  O     . HOH   G .   ? 0.5525 0.4961 0.4375 -0.0152 0.0700  -0.1025 348 HOH   A O     
1419 O  O     . HOH   G .   ? 0.4185 0.8414 0.4868 -0.1165 -0.0497 -0.0484 349 HOH   A O     
1420 O  O     . HOH   G .   ? 0.4297 0.8684 0.5452 -0.0270 -0.0513 0.0366  350 HOH   A O     
1421 O  O     . HOH   G .   ? 0.5933 0.3693 0.4878 -0.0032 0.0706  0.0166  351 HOH   A O     
1422 O  O     . HOH   G .   ? 0.3592 0.6431 0.5818 0.0032  0.0790  -0.0084 352 HOH   A O     
1423 O  O     . HOH   G .   ? 0.5218 0.5393 0.4973 -0.0175 0.1023  -0.0290 353 HOH   A O     
1424 O  O     . HOH   G .   ? 0.4547 0.8447 0.7095 -0.0251 0.0451  -0.0008 354 HOH   A O     
1425 O  O     . HOH   G .   ? 0.3929 0.7178 0.6483 -0.0033 0.0733  0.0463  355 HOH   A O     
1426 O  O     . HOH   G .   ? 0.6228 0.6219 0.6173 -0.0073 0.0823  -0.0289 356 HOH   A O     
1427 O  O     . HOH   G .   ? 0.5397 0.5111 0.5044 0.0653  0.0071  0.0266  357 HOH   A O     
1428 O  O     . HOH   G .   ? 0.6730 0.6693 0.6370 -0.1493 0.1547  0.0224  358 HOH   A O     
1429 O  O     . HOH   G .   ? 0.7406 0.5602 0.6361 0.0663  0.0412  0.0465  359 HOH   A O     
1430 O  O     . HOH   G .   ? 0.7324 0.5277 0.5877 0.0480  0.0471  0.0653  360 HOH   A O     
1431 O  O     . HOH   G .   ? 0.6497 0.6810 0.7219 0.2497  0.0935  -0.0307 361 HOH   A O     
1432 O  O     . HOH   G .   ? 0.6666 0.7919 0.7888 0.2435  0.0721  -0.0068 362 HOH   A O     
# 
