data_9GH2
# 
_entry.id   9GH2 
# 
_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   9GH2         pdb_00009gh2 10.2210/pdb9gh2/pdb 
WWPDB D_1292140389 ?            ?                   
# 
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                        9GH2 
_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 9GGZ PDB . 
unspecified 9GH0 PDB . 
unspecified 9GH1 PDB . 
unspecified 9GGW PDB . 
unspecified 9GGX PDB . 
unspecified 9GGU PDB . 
unspecified 9GGT PDB . 
unspecified 9GGV PDB . 
unspecified 9G0Y PDB . 
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)-21-[4-(4-amino-1-piperidyl)-1-piperidyl]-7-chloro-10-hydroxy-2,2-dioxo-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
;
731.371   1  ?       ?     ? ? 
6 water       nat water 18.015    58 ?       ?     ? ? 
# 
_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)-21-[4-(4-amino-1-piperidyl)-1-piperidyl]-7-chloro-10-hydroxy-2,2-dioxo-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
;
A1ILF 
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 
A1ILF non-polymer         . 
;(3Z)-18-(4-aminocyclohexyl)-21-[4-(4-amino-1-piperidyl)-1-piperidyl]-7-chloro-10-hydroxy-2,2-dioxo-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
;
? 'C34 H47 Cl N8 O4 S2' 731.371 
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  ?   ?   ?   A . n 
A 1 34  GLU 34  31  ?   ?   ?   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  ?   ?   ?   A . n 
A 1 68  SER 68  65  ?   ?   ?   A . n 
A 1 69  ALA 69  66  ?   ?   ?   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 A1ILF 1  205 1    A1ILF DRG A . 
G 6 HOH   1  301 134  HOH   HOH A . 
G 6 HOH   2  302 63   HOH   HOH A . 
G 6 HOH   3  303 4    HOH   HOH A . 
G 6 HOH   4  304 143  HOH   HOH A . 
G 6 HOH   5  305 64   HOH   HOH A . 
G 6 HOH   6  306 1    HOH   HOH A . 
G 6 HOH   7  307 78   HOH   HOH A . 
G 6 HOH   8  308 42   HOH   HOH A . 
G 6 HOH   9  309 50   HOH   HOH A . 
G 6 HOH   10 310 149  HOH   HOH A . 
G 6 HOH   11 311 124  HOH   HOH A . 
G 6 HOH   12 312 131  HOH   HOH A . 
G 6 HOH   13 313 132  HOH   HOH A . 
G 6 HOH   14 314 146  HOH   HOH A . 
G 6 HOH   15 315 87   HOH   HOH A . 
G 6 HOH   16 316 9    HOH   HOH A . 
G 6 HOH   17 317 91   HOH   HOH A . 
G 6 HOH   18 318 137  HOH   HOH A . 
G 6 HOH   19 319 2    HOH   HOH A . 
G 6 HOH   20 320 140  HOH   HOH A . 
G 6 HOH   21 321 109  HOH   HOH A . 
G 6 HOH   22 322 126  HOH   HOH A . 
G 6 HOH   23 323 101  HOH   HOH A . 
G 6 HOH   24 324 3    HOH   HOH A . 
G 6 HOH   25 325 5    HOH   HOH A . 
G 6 HOH   26 326 112  HOH   HOH A . 
G 6 HOH   27 327 100  HOH   HOH A . 
G 6 HOH   28 328 150  HOH   HOH A . 
G 6 HOH   29 329 80   HOH   HOH A . 
G 6 HOH   30 330 26   HOH   HOH A . 
G 6 HOH   31 331 130  HOH   HOH A . 
G 6 HOH   32 332 13   HOH   HOH A . 
G 6 HOH   33 333 127  HOH   HOH A . 
G 6 HOH   34 334 68   HOH   HOH A . 
G 6 HOH   35 335 129  HOH   HOH A . 
G 6 HOH   36 336 136  HOH   HOH A . 
G 6 HOH   37 337 11   HOH   HOH A . 
G 6 HOH   38 338 147  HOH   HOH A . 
G 6 HOH   39 339 30   HOH   HOH A . 
G 6 HOH   40 340 56   HOH   HOH A . 
G 6 HOH   41 341 75   HOH   HOH A . 
G 6 HOH   42 342 151  HOH   HOH A . 
G 6 HOH   43 343 57   HOH   HOH A . 
G 6 HOH   44 344 18   HOH   HOH A . 
G 6 HOH   45 345 152  HOH   HOH A . 
G 6 HOH   46 346 81   HOH   HOH A . 
G 6 HOH   47 347 142  HOH   HOH A . 
G 6 HOH   48 348 45   HOH   HOH A . 
G 6 HOH   49 349 148  HOH   HOH A . 
G 6 HOH   50 350 133  HOH   HOH A . 
G 6 HOH   51 351 53   HOH   HOH A . 
G 6 HOH   52 352 139  HOH   HOH A . 
G 6 HOH   53 353 144  HOH   HOH A . 
G 6 HOH   54 354 121  HOH   HOH A . 
G 6 HOH   55 355 138  HOH   HOH A . 
G 6 HOH   56 356 145  HOH   HOH A . 
G 6 HOH   57 357 141  HOH   HOH A . 
G 6 HOH   58 358 128  HOH   HOH A . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 0 A GLU 37  ? CG  ? A GLU 40  CG  
2  1 Y 0 A GLU 37  ? CD  ? A GLU 40  CD  
3  1 Y 0 A GLU 37  ? OE1 ? A GLU 40  OE1 
4  1 Y 0 A GLU 37  ? OE2 ? A GLU 40  OE2 
5  1 Y 0 A LYS 128 ? CG  ? A LYS 131 CG  
6  1 Y 0 A LYS 128 ? CD  ? A LYS 131 CD  
7  1 Y 0 A LYS 128 ? CE  ? A LYS 131 CE  
8  1 Y 0 A LYS 128 ? NZ  ? A LYS 131 NZ  
9  1 Y 0 A GLN 165 ? CG  ? A GLN 168 CG  
10 1 Y 0 A GLN 165 ? CD  ? A GLN 168 CD  
11 1 Y 0 A GLN 165 ? OE1 ? A GLN 168 OE1 
12 1 Y 0 A GLN 165 ? NE2 ? A GLN 168 NE2 
# 
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                   109.290 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9GH2 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     72.467 
_cell.length_a_esd                 ? 
_cell.length_b                     34.281 
_cell.length_b_esd                 ? 
_cell.length_c                     69.591 
_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                         9GH2 
_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                   9GH2 
_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             2.08 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          40.88 
_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, 150 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 PILATUS3 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2021-05-14 
_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   1.00 
_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 I24' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.00 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   I24 
_diffrn_source.pdbx_synchrotron_site       Diamond 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9GH2 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.350 
_reflns.d_resolution_low                               29.500 
_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                                     34806 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           97.600 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                3.000 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          10.300 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           3 
_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                                0.057 
_reflns.pdbx_Rpim_I_all                                0.031 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       103732 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.997 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.047 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
loop_
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_measured_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.number_unique_obs 
_reflns_shell.percent_possible_obs 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.meanI_over_sigI_gt 
_reflns_shell.meanI_over_uI_all 
_reflns_shell.meanI_over_uI_gt 
_reflns_shell.number_measured_gt 
_reflns_shell.number_unique_gt 
_reflns_shell.percent_possible_gt 
_reflns_shell.Rmerge_F_gt 
_reflns_shell.Rmerge_I_gt 
_reflns_shell.pdbx_redundancy 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_netI_over_sigmaI_all 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_rejects 
_reflns_shell.pdbx_ordinal 
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_CC_half 
_reflns_shell.pdbx_CC_star 
_reflns_shell.pdbx_R_split 
_reflns_shell.percent_possible_all 
_reflns_shell.Rmerge_I_all 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_percent_possible_ellipsoidal 
_reflns_shell.pdbx_percent_possible_spherical 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous 
_reflns_shell.pdbx_percent_possible_spherical_anomalous 
_reflns_shell.pdbx_redundancy_anomalous 
_reflns_shell.pdbx_CC_half_anomalous 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous 
_reflns_shell.pdbx_percent_possible_anomalous 
1.350 1.390  ? ? ? ? ? ? 2091 ? ? ? ? ? ? ? ? ? ? ? 2.400 ? ? ? 0.587 0.349 ? 1 1 0.891 ? ? 78.600 ? 0.469 ? ? ? ? ? ? ? ? ? 
6.040 29.500 ? ? ? ? ? ? 410  ? ? ? ? ? ? ? ? ? ? ? 2.900 ? ? ? 0.053 0.030 ? 2 1 0.993 ? ? 94.100 ? 0.043 ? ? ? ? ? ? ? ? ? 
# 
_refine.aniso_B[1][1]                            2.8500 
_refine.aniso_B[1][2]                            0.0000 
_refine.aniso_B[1][3]                            0.3600 
_refine.aniso_B[2][2]                            0.8200 
_refine.aniso_B[2][3]                            0.0000 
_refine.aniso_B[3][3]                            -3.1400 
_refine.B_iso_max                                75.580 
_refine.B_iso_mean                               30.2300 
_refine.B_iso_min                                17.740 
_refine.correlation_coeff_Fo_to_Fc               0.9720 
_refine.correlation_coeff_Fo_to_Fc_free          0.9650 
_refine.details                                  
'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS U VALUES      : REFINED INDIVIDUALLY' 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9GH2 
_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                            1.3500 
_refine.ls_d_res_low                             29.5000 
_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                     33076 
_refine.ls_number_reflns_R_free                  1729 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    97.4800 
_refine.ls_percent_reflns_R_free                 5.0000 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1838 
_refine.ls_R_factor_R_free                       0.2169 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1821 
_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                       0.0660 
_refine.pdbx_overall_ESU_R_Free                  0.0620 
_refine.pdbx_solvent_vdw_probe_radii             1.2000 
_refine.pdbx_solvent_ion_probe_radii             0.8000 
_refine.pdbx_solvent_shrinkage_radii             0.8000 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             4.2420 
_refine.overall_SU_ML                            0.0720 
_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                       1.3500 
_refine_hist.d_res_low                        29.5000 
_refine_hist.number_atoms_solvent             58 
_refine_hist.number_atoms_total               1395 
_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       156 
_refine_hist.pdbx_B_iso_mean_ligand           33.16 
_refine_hist.pdbx_B_iso_mean_solvent          40.51 
_refine_hist.pdbx_number_atoms_protein        1253 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         84 
_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  1365 ? r_bond_refined_d       ? ? 
'X-RAY DIFFRACTION' ? 0.034  0.018  1270 ? r_bond_other_d         ? ? 
'X-RAY DIFFRACTION' ? 1.703  1.720  1855 ? r_angle_refined_deg    ? ? 
'X-RAY DIFFRACTION' ? 2.310  1.664  2937 ? r_angle_other_deg      ? ? 
'X-RAY DIFFRACTION' ? 3.795  5.000  157  ? r_dihedral_angle_1_deg ? ? 
'X-RAY DIFFRACTION' ? 29.953 20.933 75   ? r_dihedral_angle_2_deg ? ? 
'X-RAY DIFFRACTION' ? 13.933 15.000 234  ? r_dihedral_angle_3_deg ? ? 
'X-RAY DIFFRACTION' ? 10.887 15.000 13   ? r_dihedral_angle_4_deg ? ? 
'X-RAY DIFFRACTION' ? 0.115  0.200  180  ? r_chiral_restr         ? ? 
'X-RAY DIFFRACTION' ? 0.010  0.020  1486 ? r_gen_planes_refined   ? ? 
'X-RAY DIFFRACTION' ? 0.009  0.020  289  ? r_gen_planes_other     ? ? 
'X-RAY DIFFRACTION' ? 1.985  2.934  631  ? r_mcbond_it            ? ? 
'X-RAY DIFFRACTION' ? 1.976  2.927  630  ? r_mcbond_other         ? ? 
'X-RAY DIFFRACTION' ? 2.352  4.388  787  ? r_mcangle_it           ? ? 
'X-RAY DIFFRACTION' ? 3.515  3.000  2635 ? r_rigid_bond_restr     ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.3510 
_refine_ls_shell.d_res_low                        1.3860 
_refine_ls_shell.number_reflns_all                2085 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             101 
_refine_ls_shell.number_reflns_R_work             1984 
_refine_ls_shell.percent_reflns_obs               78.5000 
_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                  0.3280 
_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                  0.3110 
# 
_struct.entry_id                     9GH2 
_struct.title                        'Human KRas4A (GMPPNP) in complex with compound 36' 
_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        9GH2 
_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              9GH2 
_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 9GH2 GLY A 1   ? UNP P01116 ?   ?   'expression tag'      -2  1 
1 9GH2 GLY A 2   ? UNP P01116 ?   ?   'expression tag'      -1  2 
1 9GH2 SER A 3   ? UNP P01116 ?   ?   'expression tag'      0   3 
1 9GH2 SER A 121 ? UNP P01116 CYS 118 'engineered mutation' 118 4 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 1890 ? 
1 MORE         -29  ? 
1 'SSA (A^2)'  7860 ? 
# 
_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 ARG A 71  ? GLY A 78  ? ARG A 68  GLY A 75  1 ? 8  
HELX_P HELX_P3 AA3 ASN A 89  ? ASP A 95  ? ASN A 86  ASP A 92  1 ? 7  
HELX_P HELX_P4 AA4 ASP A 95  ? ASP A 108 ? ASP A 92  ASP A 105 1 ? 14 
HELX_P HELX_P5 AA5 ASP A 129 ? GLY A 141 ? ASP A 126 GLY A 138 1 ? 13 
HELX_P HELX_P6 AA6 ARG A 154 ? 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 ? ? ? ? ? ? ? 2.101 ? ? 
metalc2  metalc ? ? A HIS 30  NE2 ? ? ? 1_555 D CO  . CO ? ? A HIS 27  A CO  203 1_555 ? ? ? ? ? ? ? 2.327 ? ? 
metalc3  metalc ? ? A HIS 97  NE2 ? ? ? 1_555 E CO  . CO ? ? A HIS 94  A CO  204 1_555 ? ? ? ? ? ? ? 2.285 ? ? 
metalc4  metalc ? ? A HIS 98  NE2 ? ? ? 1_555 E CO  . CO ? ? A HIS 95  A CO  204 2_655 ? ? ? ? ? ? ? 2.238 ? ? 
metalc5  metalc ? ? A GLU 101 OE1 ? ? ? 1_555 E CO  . CO ? ? A GLU 98  A CO  204 1_555 ? ? ? ? ? ? ? 2.050 ? ? 
metalc6  metalc ? ? B GNP .   O1G ? ? ? 1_555 C MG  . MG ? ? A GNP 201 A MG  202 1_555 ? ? ? ? ? ? ? 2.227 ? ? 
metalc7  metalc ? ? B GNP .   O2B ? ? ? 1_555 C MG  . MG ? ? A GNP 201 A MG  202 1_555 ? ? ? ? ? ? ? 2.193 ? ? 
metalc8  metalc ? ? C MG  .   MG  ? ? ? 1_555 G HOH . O  ? ? A MG  202 A HOH 309 1_555 ? ? ? ? ? ? ? 2.067 ? ? 
metalc9  metalc ? ? C MG  .   MG  ? ? ? 1_555 G HOH . O  ? ? A MG  202 A HOH 323 1_555 ? ? ? ? ? ? ? 2.063 ? ? 
metalc10 metalc ? ? C MG  .   MG  ? ? ? 1_555 G HOH . O  ? ? A MG  202 A HOH 340 1_555 ? ? ? ? ? ? ? 2.098 ? ? 
metalc11 metalc ? ? E CO  .   CO  ? ? ? 1_555 G HOH . O  ? ? A CO  204 A HOH 332 1_555 ? ? ? ? ? ? ? 2.094 ? ? 
metalc12 metalc ? ? E CO  .   CO  ? ? ? 1_555 G HOH . O  ? ? A CO  204 A HOH 341 2_655 ? ? ? ? ? ? ? 2.328 ? ? 
metalc13 metalc ? ? E CO  .   CO  ? ? ? 1_555 G HOH . O  ? ? A CO  204 A HOH 344 2_655 ? ? ? ? ? ? ? 2.250 ? ? 
# 
_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_555 174.3 ? 
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 88.9  ? 
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 92.2  ? 
4  OG  ? A SER 20  ? A SER 17  ? 1_555 MG ? C MG . ? A MG 202 ? 1_555 O   ? G HOH .   ? A HOH 309 ? 1_555 84.8  ? 
5  O1G ? B GNP .   ? A GNP 201 ? 1_555 MG ? C MG . ? A MG 202 ? 1_555 O   ? G HOH .   ? A HOH 309 ? 1_555 89.6  ? 
6  O2B ? B GNP .   ? A GNP 201 ? 1_555 MG ? C MG . ? A MG 202 ? 1_555 O   ? G HOH .   ? A HOH 309 ? 1_555 93.9  ? 
7  OG  ? A SER 20  ? A SER 17  ? 1_555 MG ? C MG . ? A MG 202 ? 1_555 O   ? G HOH .   ? A HOH 323 ? 1_555 88.6  ? 
8  O1G ? B GNP .   ? A GNP 201 ? 1_555 MG ? C MG . ? A MG 202 ? 1_555 O   ? G HOH .   ? A HOH 323 ? 1_555 97.0  ? 
9  O2B ? B GNP .   ? A GNP 201 ? 1_555 MG ? C MG . ? A MG 202 ? 1_555 O   ? G HOH .   ? A HOH 323 ? 1_555 89.8  ? 
10 O   ? G HOH .   ? A HOH 309 ? 1_555 MG ? C MG . ? A MG 202 ? 1_555 O   ? G HOH .   ? A HOH 323 ? 1_555 172.3 ? 
11 OG  ? A SER 20  ? A SER 17  ? 1_555 MG ? C MG . ? A MG 202 ? 1_555 O   ? G HOH .   ? A HOH 340 ? 1_555 89.8  ? 
12 O1G ? B GNP .   ? A GNP 201 ? 1_555 MG ? C MG . ? A MG 202 ? 1_555 O   ? G HOH .   ? A HOH 340 ? 1_555 89.6  ? 
13 O2B ? B GNP .   ? A GNP 201 ? 1_555 MG ? C MG . ? A MG 202 ? 1_555 O   ? G HOH .   ? A HOH 340 ? 1_555 175.4 ? 
14 O   ? G HOH .   ? A HOH 309 ? 1_555 MG ? C MG . ? A MG 202 ? 1_555 O   ? G HOH .   ? A HOH 340 ? 1_555 90.3  ? 
15 O   ? G HOH .   ? A HOH 323 ? 1_555 MG ? C MG . ? A MG 202 ? 1_555 O   ? G HOH .   ? A HOH 340 ? 1_555 85.7  ? 
16 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 65.1  ? 
17 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 89.6  ? 
18 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_555 114.2 ? 
19 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 94.6  ? 
20 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 41.2  ? 
21 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 87.6  ? 
22 NE2 ? A HIS 97  ? A HIS 94  ? 1_555 CO ? E CO . ? A CO 204 ? 1_555 O   ? G HOH .   ? A HOH 341 ? 2_655 86.7  ? 
23 NE2 ? A HIS 98  ? A HIS 95  ? 1_555 CO ? E CO . ? A CO 204 ? 1_555 O   ? G HOH .   ? A HOH 341 ? 2_655 143.8 ? 
24 OE1 ? A GLU 101 ? A GLU 98  ? 1_555 CO ? E CO . ? A CO 204 ? 1_555 O   ? G HOH .   ? A HOH 341 ? 2_655 86.3  ? 
25 O   ? G HOH .   ? A HOH 332 ? 1_555 CO ? E CO . ? A CO 204 ? 1_555 O   ? G HOH .   ? A HOH 341 ? 2_655 173.7 ? 
26 NE2 ? A HIS 97  ? A HIS 94  ? 1_555 CO ? E CO . ? A CO 204 ? 1_555 O   ? G HOH .   ? A HOH 344 ? 2_655 172.6 ? 
27 NE2 ? A HIS 98  ? A HIS 95  ? 1_555 CO ? E CO . ? A CO 204 ? 1_555 O   ? G HOH .   ? A HOH 344 ? 2_655 119.7 ? 
28 OE1 ? A GLU 101 ? A GLU 98  ? 1_555 CO ? E CO . ? A CO 204 ? 1_555 O   ? G HOH .   ? A HOH 344 ? 2_655 93.1  ? 
29 O   ? G HOH .   ? A HOH 332 ? 1_555 CO ? E CO . ? A CO 204 ? 1_555 O   ? G HOH .   ? A HOH 344 ? 2_655 92.4  ? 
30 O   ? G HOH .   ? A HOH 341 ? 2_655 CO ? E CO . ? A CO 204 ? 1_555 O   ? G HOH .   ? A HOH 344 ? 2_655 86.6  ? 
# 
_struct_sheet.id               AA1 
_struct_sheet.type             ? 
_struct_sheet.number_strands   6 
_struct_sheet.details          ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA1 4 5 ? parallel      
AA1 5 6 ? parallel      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 SER A 42  ? ILE A 49  ? SER A 39  ILE A 46  
AA1 2 GLU A 52  ? ASP A 60  ? GLU A 49  ASP A 57  
AA1 3 THR A 5   ? VAL A 12  ? THR A 2   VAL A 9   
AA1 4 GLY A 80  ? ALA A 86  ? GLY A 77  ALA A 83  
AA1 5 MET A 114 ? ASN A 119 ? MET A 111 ASN A 116 
AA1 6 PHE A 144 ? GLU A 146 ? PHE A 141 GLU A 143 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N LYS A 45  ? N LYS A 42  O LEU A 56  ? O LEU A 53  
AA1 2 3 O LEU A 59  ? O LEU A 56  N LEU A 9   ? N LEU A 6   
AA1 3 4 N VAL A 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 GLY A 118 ? N GLY A 115 O ILE A 145 ? O ILE A 142 
# 
_pdbx_entry_details.entry_id                   9GH2 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     ? 
_pdbx_entry_details.has_protein_modification   N 
# 
_pdbx_validate_rmsd_bond.id                        1 
_pdbx_validate_rmsd_bond.PDB_model_num             1 
_pdbx_validate_rmsd_bond.auth_atom_id_1            CD 
_pdbx_validate_rmsd_bond.auth_asym_id_1            A 
_pdbx_validate_rmsd_bond.auth_comp_id_1            GLU 
_pdbx_validate_rmsd_bond.auth_seq_id_1             76 
_pdbx_validate_rmsd_bond.PDB_ins_code_1            ? 
_pdbx_validate_rmsd_bond.label_alt_id_1            ? 
_pdbx_validate_rmsd_bond.auth_atom_id_2            OE1 
_pdbx_validate_rmsd_bond.auth_asym_id_2            A 
_pdbx_validate_rmsd_bond.auth_comp_id_2            GLU 
_pdbx_validate_rmsd_bond.auth_seq_id_2             76 
_pdbx_validate_rmsd_bond.PDB_ins_code_2            ? 
_pdbx_validate_rmsd_bond.label_alt_id_2            ? 
_pdbx_validate_rmsd_bond.bond_value                1.180 
_pdbx_validate_rmsd_bond.bond_target_value         1.252 
_pdbx_validate_rmsd_bond.bond_deviation            -0.072 
_pdbx_validate_rmsd_bond.bond_standard_deviation   0.011 
_pdbx_validate_rmsd_bond.linker_flag               N 
# 
_pdbx_validate_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             73.33 
_pdbx_validate_torsion.psi             33.00 
# 
loop_
_pdbx_validate_main_chain_plane.id 
_pdbx_validate_main_chain_plane.PDB_model_num 
_pdbx_validate_main_chain_plane.auth_comp_id 
_pdbx_validate_main_chain_plane.auth_asym_id 
_pdbx_validate_main_chain_plane.auth_seq_id 
_pdbx_validate_main_chain_plane.PDB_ins_code 
_pdbx_validate_main_chain_plane.label_alt_id 
_pdbx_validate_main_chain_plane.improper_torsion_angle 
1 1 SER A 136 ? A -10.64 
2 1 SER A 136 ? B -11.70 
# 
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 ASP 30 ? A ASP 33 
5  1 Y 1 A GLU 31 ? A GLU 34 
6  1 Y 1 A TYR 32 ? A TYR 35 
7  1 Y 1 A ASP 33 ? A ASP 36 
8  1 Y 1 A PRO 34 ? A PRO 37 
9  1 Y 1 A THR 35 ? A THR 38 
10 1 Y 1 A ILE 36 ? A ILE 39 
11 1 Y 1 A GLN 61 ? A GLN 64 
12 1 Y 1 A GLU 62 ? A GLU 65 
13 1 Y 1 A GLU 63 ? A GLU 66 
14 1 Y 1 A TYR 64 ? A TYR 67 
15 1 Y 1 A SER 65 ? A SER 68 
16 1 Y 1 A ALA 66 ? A ALA 69 
# 
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 
A1ILF CBK    C  N N 1   
A1ILF CBL    C  N N 2   
A1ILF CBM    C  N N 3   
A1ILF NBV    N  N N 4   
A1ILF CBN    C  N N 5   
A1ILF CBO    C  N N 6   
A1ILF CBJ    C  N N 7   
A1ILF NAQ    N  N N 8   
A1ILF CAB    C  N N 9   
A1ILF OAA    O  N N 10  
A1ILF CAR    C  N N 11  
A1ILF CAS    C  N N 12  
A1ILF CAT    C  N N 13  
A1ILF CAU    C  N N 14  
A1ILF CAV    C  N N 15  
A1ILF NAW    N  N N 16  
A1ILF CAX    C  Y N 17  
A1ILF CAY    C  Y N 18  
A1ILF OBD    O  N N 19  
A1ILF CAZ    C  Y N 20  
A1ILF CBA    C  Y N 21  
A1ILF CBB    C  Y N 22  
A1ILF CLBC   CL N N 23  
A1ILF CBI    C  Y N 24  
A1ILF SBH    S  N N 25  
A1ILF CBG    C  N N 26  
A1ILF NBF    N  N N 27  
A1ILF SAH    S  N N 28  
A1ILF OAI    O  N N 29  
A1ILF OBE    O  N N 30  
A1ILF CAG    C  Y N 31  
A1ILF CAF    C  Y N 32  
A1ILF NAE    N  Y N 33  
A1ILF CAJ    C  Y N 34  
A1ILF CAC    C  Y N 35  
A1ILF CAD    C  Y N 36  
A1ILF NAK    N  N N 37  
A1ILF CAP    C  N N 38  
A1ILF CAO    C  N N 39  
A1ILF CAL    C  N N 40  
A1ILF CAM    C  N N 41  
A1ILF CAN    C  N N 42  
A1ILF NBP    N  N N 43  
A1ILF CBQ    C  N N 44  
A1ILF CBR    C  N N 45  
A1ILF CBS    C  N N 46  
A1ILF NBW    N  N N 47  
A1ILF CBT    C  N N 48  
A1ILF CBU    C  N N 49  
A1ILF H1     H  N N 50  
A1ILF H2     H  N N 51  
A1ILF H3     H  N N 52  
A1ILF H4     H  N N 53  
A1ILF H5     H  N N 54  
A1ILF H6     H  N N 55  
A1ILF H7     H  N N 56  
A1ILF H9     H  N N 57  
A1ILF H10    H  N N 58  
A1ILF H11    H  N N 59  
A1ILF H12    H  N N 60  
A1ILF H13    H  N N 61  
A1ILF H14    H  N N 62  
A1ILF H15    H  N N 63  
A1ILF H16    H  N N 64  
A1ILF H17    H  N N 65  
A1ILF H18    H  N N 66  
A1ILF H19    H  N N 67  
A1ILF H20    H  N N 68  
A1ILF H21    H  N N 69  
A1ILF H22    H  N N 70  
A1ILF H23    H  N N 71  
A1ILF H24    H  N N 72  
A1ILF H25    H  N N 73  
A1ILF H26    H  N N 74  
A1ILF H30    H  N N 75  
A1ILF H31    H  N N 76  
A1ILF H32    H  N N 77  
A1ILF H33    H  N N 78  
A1ILF H34    H  N N 79  
A1ILF H35    H  N N 80  
A1ILF H36    H  N N 81  
A1ILF H37    H  N N 82  
A1ILF H38    H  N N 83  
A1ILF H39    H  N N 84  
A1ILF H40    H  N N 85  
A1ILF H42    H  N N 86  
A1ILF H43    H  N N 87  
A1ILF H44    H  N N 88  
A1ILF H45    H  N N 89  
A1ILF H46    H  N N 90  
A1ILF H47    H  N N 91  
A1ILF H48    H  N N 92  
A1ILF H50    H  N N 93  
A1ILF H51    H  N N 94  
A1ILF H52    H  N N 95  
A1ILF H53    H  N N 96  
ALA   N      N  N N 97  
ALA   CA     C  N S 98  
ALA   C      C  N N 99  
ALA   O      O  N N 100 
ALA   CB     C  N N 101 
ALA   OXT    O  N N 102 
ALA   H      H  N N 103 
ALA   H2     H  N N 104 
ALA   HA     H  N N 105 
ALA   HB1    H  N N 106 
ALA   HB2    H  N N 107 
ALA   HB3    H  N N 108 
ALA   HXT    H  N N 109 
ARG   N      N  N N 110 
ARG   CA     C  N S 111 
ARG   C      C  N N 112 
ARG   O      O  N N 113 
ARG   CB     C  N N 114 
ARG   CG     C  N N 115 
ARG   CD     C  N N 116 
ARG   NE     N  N N 117 
ARG   CZ     C  N N 118 
ARG   NH1    N  N N 119 
ARG   NH2    N  N N 120 
ARG   OXT    O  N N 121 
ARG   H      H  N N 122 
ARG   H2     H  N N 123 
ARG   HA     H  N N 124 
ARG   HB2    H  N N 125 
ARG   HB3    H  N N 126 
ARG   HG2    H  N N 127 
ARG   HG3    H  N N 128 
ARG   HD2    H  N N 129 
ARG   HD3    H  N N 130 
ARG   HE     H  N N 131 
ARG   HH11   H  N N 132 
ARG   HH12   H  N N 133 
ARG   HH21   H  N N 134 
ARG   HH22   H  N N 135 
ARG   HXT    H  N N 136 
ASN   N      N  N N 137 
ASN   CA     C  N S 138 
ASN   C      C  N N 139 
ASN   O      O  N N 140 
ASN   CB     C  N N 141 
ASN   CG     C  N N 142 
ASN   OD1    O  N N 143 
ASN   ND2    N  N N 144 
ASN   OXT    O  N N 145 
ASN   H      H  N N 146 
ASN   H2     H  N N 147 
ASN   HA     H  N N 148 
ASN   HB2    H  N N 149 
ASN   HB3    H  N N 150 
ASN   HD21   H  N N 151 
ASN   HD22   H  N N 152 
ASN   HXT    H  N N 153 
ASP   N      N  N N 154 
ASP   CA     C  N S 155 
ASP   C      C  N N 156 
ASP   O      O  N N 157 
ASP   CB     C  N N 158 
ASP   CG     C  N N 159 
ASP   OD1    O  N N 160 
ASP   OD2    O  N N 161 
ASP   OXT    O  N N 162 
ASP   H      H  N N 163 
ASP   H2     H  N N 164 
ASP   HA     H  N N 165 
ASP   HB2    H  N N 166 
ASP   HB3    H  N N 167 
ASP   HD2    H  N N 168 
ASP   HXT    H  N N 169 
CO    CO     CO N N 170 
CYS   N      N  N N 171 
CYS   CA     C  N R 172 
CYS   C      C  N N 173 
CYS   O      O  N N 174 
CYS   CB     C  N N 175 
CYS   SG     S  N N 176 
CYS   OXT    O  N N 177 
CYS   H      H  N N 178 
CYS   H2     H  N N 179 
CYS   HA     H  N N 180 
CYS   HB2    H  N N 181 
CYS   HB3    H  N N 182 
CYS   HG     H  N N 183 
CYS   HXT    H  N N 184 
GLN   N      N  N N 185 
GLN   CA     C  N S 186 
GLN   C      C  N N 187 
GLN   O      O  N N 188 
GLN   CB     C  N N 189 
GLN   CG     C  N N 190 
GLN   CD     C  N N 191 
GLN   OE1    O  N N 192 
GLN   NE2    N  N N 193 
GLN   OXT    O  N N 194 
GLN   H      H  N N 195 
GLN   H2     H  N N 196 
GLN   HA     H  N N 197 
GLN   HB2    H  N N 198 
GLN   HB3    H  N N 199 
GLN   HG2    H  N N 200 
GLN   HG3    H  N N 201 
GLN   HE21   H  N N 202 
GLN   HE22   H  N N 203 
GLN   HXT    H  N N 204 
GLU   N      N  N N 205 
GLU   CA     C  N S 206 
GLU   C      C  N N 207 
GLU   O      O  N N 208 
GLU   CB     C  N N 209 
GLU   CG     C  N N 210 
GLU   CD     C  N N 211 
GLU   OE1    O  N N 212 
GLU   OE2    O  N N 213 
GLU   OXT    O  N N 214 
GLU   H      H  N N 215 
GLU   H2     H  N N 216 
GLU   HA     H  N N 217 
GLU   HB2    H  N N 218 
GLU   HB3    H  N N 219 
GLU   HG2    H  N N 220 
GLU   HG3    H  N N 221 
GLU   HE2    H  N N 222 
GLU   HXT    H  N N 223 
GLY   N      N  N N 224 
GLY   CA     C  N N 225 
GLY   C      C  N N 226 
GLY   O      O  N N 227 
GLY   OXT    O  N N 228 
GLY   H      H  N N 229 
GLY   H2     H  N N 230 
GLY   HA2    H  N N 231 
GLY   HA3    H  N N 232 
GLY   HXT    H  N N 233 
GNP   PG     P  N N 234 
GNP   O1G    O  N N 235 
GNP   O2G    O  N N 236 
GNP   O3G    O  N N 237 
GNP   N3B    N  N N 238 
GNP   PB     P  N R 239 
GNP   O1B    O  N N 240 
GNP   O2B    O  N N 241 
GNP   O3A    O  N N 242 
GNP   PA     P  N S 243 
GNP   O1A    O  N N 244 
GNP   O2A    O  N N 245 
GNP   "O5'"  O  N N 246 
GNP   "C5'"  C  N N 247 
GNP   "C4'"  C  N R 248 
GNP   "O4'"  O  N N 249 
GNP   "C3'"  C  N S 250 
GNP   "O3'"  O  N N 251 
GNP   "C2'"  C  N R 252 
GNP   "O2'"  O  N N 253 
GNP   "C1'"  C  N R 254 
GNP   N9     N  Y N 255 
GNP   C8     C  Y N 256 
GNP   N7     N  Y N 257 
GNP   C5     C  Y N 258 
GNP   C6     C  Y N 259 
GNP   O6     O  N N 260 
GNP   N1     N  Y N 261 
GNP   C2     C  Y N 262 
GNP   N2     N  N N 263 
GNP   N3     N  Y N 264 
GNP   C4     C  Y N 265 
GNP   HOG2   H  N N 266 
GNP   HOG3   H  N N 267 
GNP   HNB3   H  N N 268 
GNP   HOB2   H  N N 269 
GNP   HOA2   H  N N 270 
GNP   "H5'2" H  N N 271 
GNP   "H5'1" H  N N 272 
GNP   "H4'"  H  N N 273 
GNP   "H3'"  H  N N 274 
GNP   "HO3'" H  N N 275 
GNP   "H2'"  H  N N 276 
GNP   "HO2'" H  N N 277 
GNP   "H1'"  H  N N 278 
GNP   H8     H  N N 279 
GNP   HN1    H  N N 280 
GNP   HN21   H  N N 281 
GNP   HN22   H  N N 282 
HIS   N      N  N N 283 
HIS   CA     C  N S 284 
HIS   C      C  N N 285 
HIS   O      O  N N 286 
HIS   CB     C  N N 287 
HIS   CG     C  Y N 288 
HIS   ND1    N  Y N 289 
HIS   CD2    C  Y N 290 
HIS   CE1    C  Y N 291 
HIS   NE2    N  Y N 292 
HIS   OXT    O  N N 293 
HIS   H      H  N N 294 
HIS   H2     H  N N 295 
HIS   HA     H  N N 296 
HIS   HB2    H  N N 297 
HIS   HB3    H  N N 298 
HIS   HD1    H  N N 299 
HIS   HD2    H  N N 300 
HIS   HE1    H  N N 301 
HIS   HE2    H  N N 302 
HIS   HXT    H  N N 303 
HOH   O      O  N N 304 
HOH   H1     H  N N 305 
HOH   H2     H  N N 306 
ILE   N      N  N N 307 
ILE   CA     C  N S 308 
ILE   C      C  N N 309 
ILE   O      O  N N 310 
ILE   CB     C  N S 311 
ILE   CG1    C  N N 312 
ILE   CG2    C  N N 313 
ILE   CD1    C  N N 314 
ILE   OXT    O  N N 315 
ILE   H      H  N N 316 
ILE   H2     H  N N 317 
ILE   HA     H  N N 318 
ILE   HB     H  N N 319 
ILE   HG12   H  N N 320 
ILE   HG13   H  N N 321 
ILE   HG21   H  N N 322 
ILE   HG22   H  N N 323 
ILE   HG23   H  N N 324 
ILE   HD11   H  N N 325 
ILE   HD12   H  N N 326 
ILE   HD13   H  N N 327 
ILE   HXT    H  N N 328 
LEU   N      N  N N 329 
LEU   CA     C  N S 330 
LEU   C      C  N N 331 
LEU   O      O  N N 332 
LEU   CB     C  N N 333 
LEU   CG     C  N N 334 
LEU   CD1    C  N N 335 
LEU   CD2    C  N N 336 
LEU   OXT    O  N N 337 
LEU   H      H  N N 338 
LEU   H2     H  N N 339 
LEU   HA     H  N N 340 
LEU   HB2    H  N N 341 
LEU   HB3    H  N N 342 
LEU   HG     H  N N 343 
LEU   HD11   H  N N 344 
LEU   HD12   H  N N 345 
LEU   HD13   H  N N 346 
LEU   HD21   H  N N 347 
LEU   HD22   H  N N 348 
LEU   HD23   H  N N 349 
LEU   HXT    H  N N 350 
LYS   N      N  N N 351 
LYS   CA     C  N S 352 
LYS   C      C  N N 353 
LYS   O      O  N N 354 
LYS   CB     C  N N 355 
LYS   CG     C  N N 356 
LYS   CD     C  N N 357 
LYS   CE     C  N N 358 
LYS   NZ     N  N N 359 
LYS   OXT    O  N N 360 
LYS   H      H  N N 361 
LYS   H2     H  N N 362 
LYS   HA     H  N N 363 
LYS   HB2    H  N N 364 
LYS   HB3    H  N N 365 
LYS   HG2    H  N N 366 
LYS   HG3    H  N N 367 
LYS   HD2    H  N N 368 
LYS   HD3    H  N N 369 
LYS   HE2    H  N N 370 
LYS   HE3    H  N N 371 
LYS   HZ1    H  N N 372 
LYS   HZ2    H  N N 373 
LYS   HZ3    H  N N 374 
LYS   HXT    H  N N 375 
MET   N      N  N N 376 
MET   CA     C  N S 377 
MET   C      C  N N 378 
MET   O      O  N N 379 
MET   CB     C  N N 380 
MET   CG     C  N N 381 
MET   SD     S  N N 382 
MET   CE     C  N N 383 
MET   OXT    O  N N 384 
MET   H      H  N N 385 
MET   H2     H  N N 386 
MET   HA     H  N N 387 
MET   HB2    H  N N 388 
MET   HB3    H  N N 389 
MET   HG2    H  N N 390 
MET   HG3    H  N N 391 
MET   HE1    H  N N 392 
MET   HE2    H  N N 393 
MET   HE3    H  N N 394 
MET   HXT    H  N N 395 
MG    MG     MG N N 396 
PHE   N      N  N N 397 
PHE   CA     C  N S 398 
PHE   C      C  N N 399 
PHE   O      O  N N 400 
PHE   CB     C  N N 401 
PHE   CG     C  Y N 402 
PHE   CD1    C  Y N 403 
PHE   CD2    C  Y N 404 
PHE   CE1    C  Y N 405 
PHE   CE2    C  Y N 406 
PHE   CZ     C  Y N 407 
PHE   OXT    O  N N 408 
PHE   H      H  N N 409 
PHE   H2     H  N N 410 
PHE   HA     H  N N 411 
PHE   HB2    H  N N 412 
PHE   HB3    H  N N 413 
PHE   HD1    H  N N 414 
PHE   HD2    H  N N 415 
PHE   HE1    H  N N 416 
PHE   HE2    H  N N 417 
PHE   HZ     H  N N 418 
PHE   HXT    H  N N 419 
PRO   N      N  N N 420 
PRO   CA     C  N S 421 
PRO   C      C  N N 422 
PRO   O      O  N N 423 
PRO   CB     C  N N 424 
PRO   CG     C  N N 425 
PRO   CD     C  N N 426 
PRO   OXT    O  N N 427 
PRO   H      H  N N 428 
PRO   HA     H  N N 429 
PRO   HB2    H  N N 430 
PRO   HB3    H  N N 431 
PRO   HG2    H  N N 432 
PRO   HG3    H  N N 433 
PRO   HD2    H  N N 434 
PRO   HD3    H  N N 435 
PRO   HXT    H  N N 436 
SER   N      N  N N 437 
SER   CA     C  N S 438 
SER   C      C  N N 439 
SER   O      O  N N 440 
SER   CB     C  N N 441 
SER   OG     O  N N 442 
SER   OXT    O  N N 443 
SER   H      H  N N 444 
SER   H2     H  N N 445 
SER   HA     H  N N 446 
SER   HB2    H  N N 447 
SER   HB3    H  N N 448 
SER   HG     H  N N 449 
SER   HXT    H  N N 450 
THR   N      N  N N 451 
THR   CA     C  N S 452 
THR   C      C  N N 453 
THR   O      O  N N 454 
THR   CB     C  N R 455 
THR   OG1    O  N N 456 
THR   CG2    C  N N 457 
THR   OXT    O  N N 458 
THR   H      H  N N 459 
THR   H2     H  N N 460 
THR   HA     H  N N 461 
THR   HB     H  N N 462 
THR   HG1    H  N N 463 
THR   HG21   H  N N 464 
THR   HG22   H  N N 465 
THR   HG23   H  N N 466 
THR   HXT    H  N N 467 
TYR   N      N  N N 468 
TYR   CA     C  N S 469 
TYR   C      C  N N 470 
TYR   O      O  N N 471 
TYR   CB     C  N N 472 
TYR   CG     C  Y N 473 
TYR   CD1    C  Y N 474 
TYR   CD2    C  Y N 475 
TYR   CE1    C  Y N 476 
TYR   CE2    C  Y N 477 
TYR   CZ     C  Y N 478 
TYR   OH     O  N N 479 
TYR   OXT    O  N N 480 
TYR   H      H  N N 481 
TYR   H2     H  N N 482 
TYR   HA     H  N N 483 
TYR   HB2    H  N N 484 
TYR   HB3    H  N N 485 
TYR   HD1    H  N N 486 
TYR   HD2    H  N N 487 
TYR   HE1    H  N N 488 
TYR   HE2    H  N N 489 
TYR   HH     H  N N 490 
TYR   HXT    H  N N 491 
VAL   N      N  N N 492 
VAL   CA     C  N S 493 
VAL   C      C  N N 494 
VAL   O      O  N N 495 
VAL   CB     C  N N 496 
VAL   CG1    C  N N 497 
VAL   CG2    C  N N 498 
VAL   OXT    O  N N 499 
VAL   H      H  N N 500 
VAL   H2     H  N N 501 
VAL   HA     H  N N 502 
VAL   HB     H  N N 503 
VAL   HG11   H  N N 504 
VAL   HG12   H  N N 505 
VAL   HG13   H  N N 506 
VAL   HG21   H  N N 507 
VAL   HG22   H  N N 508 
VAL   HG23   H  N N 509 
VAL   HXT    H  N N 510 
# 
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 
A1ILF CBK   CBL    sing N N 1   
A1ILF CBK   CBJ    sing N N 2   
A1ILF CBL   CBM    sing N N 3   
A1ILF CBM   NBV    sing N N 4   
A1ILF CBM   CBN    sing N N 5   
A1ILF CBN   CBO    sing N N 6   
A1ILF CBO   CBJ    sing N N 7   
A1ILF CBJ   NAQ    sing N N 8   
A1ILF NAQ   CAB    sing N N 9   
A1ILF NAQ   CAR    sing N N 10  
A1ILF CAB   OAA    doub N N 11  
A1ILF CAB   CAC    sing N N 12  
A1ILF CAR   CAS    sing N N 13  
A1ILF CAS   CAT    sing N N 14  
A1ILF CAT   CAU    sing N N 15  
A1ILF CAU   CAV    sing N N 16  
A1ILF CAV   NAW    sing N N 17  
A1ILF NAW   CAX    sing N N 18  
A1ILF NAW   CBG    sing N N 19  
A1ILF CAX   CAY    sing Y N 20  
A1ILF CAX   CBI    doub Y N 21  
A1ILF CAY   OBD    sing N N 22  
A1ILF CAY   CAZ    doub Y N 23  
A1ILF CAZ   CBA    sing Y N 24  
A1ILF CBA   CBB    doub Y N 25  
A1ILF CBB   CLBC   sing N N 26  
A1ILF CBB   CBI    sing Y N 27  
A1ILF CBI   SBH    sing N N 28  
A1ILF SBH   CBG    sing N N 29  
A1ILF CBG   NBF    doub N N 30  
A1ILF NBF   SAH    sing N N 31  
A1ILF SAH   OAI    doub N N 32  
A1ILF SAH   OBE    doub N N 33  
A1ILF SAH   CAG    sing N N 34  
A1ILF CAG   CAF    doub Y N 35  
A1ILF CAG   CAJ    sing Y N 36  
A1ILF CAF   NAE    sing Y N 37  
A1ILF NAE   CAD    doub Y N 38  
A1ILF CAJ   CAC    doub Y N 39  
A1ILF CAC   CAD    sing Y N 40  
A1ILF CAD   NAK    sing N N 41  
A1ILF NAK   CAP    sing N N 42  
A1ILF NAK   CAL    sing N N 43  
A1ILF CAP   CAO    sing N N 44  
A1ILF CAO   CAN    sing N N 45  
A1ILF CAL   CAM    sing N N 46  
A1ILF CAM   CAN    sing N N 47  
A1ILF CAN   NBP    sing N N 48  
A1ILF NBP   CBQ    sing N N 49  
A1ILF NBP   CBU    sing N N 50  
A1ILF CBQ   CBR    sing N N 51  
A1ILF CBR   CBS    sing N N 52  
A1ILF CBS   NBW    sing N N 53  
A1ILF CBS   CBT    sing N N 54  
A1ILF CBT   CBU    sing N N 55  
A1ILF CBK   H1     sing N N 56  
A1ILF CBK   H2     sing N N 57  
A1ILF CBL   H3     sing N N 58  
A1ILF CBL   H4     sing N N 59  
A1ILF CBM   H5     sing N N 60  
A1ILF NBV   H6     sing N N 61  
A1ILF NBV   H7     sing N N 62  
A1ILF CBN   H9     sing N N 63  
A1ILF CBN   H10    sing N N 64  
A1ILF CBO   H11    sing N N 65  
A1ILF CBO   H12    sing N N 66  
A1ILF CBJ   H13    sing N N 67  
A1ILF CAR   H14    sing N N 68  
A1ILF CAR   H15    sing N N 69  
A1ILF CAS   H16    sing N N 70  
A1ILF CAS   H17    sing N N 71  
A1ILF CAT   H18    sing N N 72  
A1ILF CAT   H19    sing N N 73  
A1ILF CAU   H20    sing N N 74  
A1ILF CAU   H21    sing N N 75  
A1ILF CAV   H22    sing N N 76  
A1ILF CAV   H23    sing N N 77  
A1ILF OBD   H24    sing N N 78  
A1ILF CAZ   H25    sing N N 79  
A1ILF CBA   H26    sing N N 80  
A1ILF CAF   H30    sing N N 81  
A1ILF CAJ   H31    sing N N 82  
A1ILF CAP   H32    sing N N 83  
A1ILF CAP   H33    sing N N 84  
A1ILF CAO   H34    sing N N 85  
A1ILF CAO   H35    sing N N 86  
A1ILF CAL   H36    sing N N 87  
A1ILF CAL   H37    sing N N 88  
A1ILF CAM   H38    sing N N 89  
A1ILF CAM   H39    sing N N 90  
A1ILF CAN   H40    sing N N 91  
A1ILF CBQ   H42    sing N N 92  
A1ILF CBQ   H43    sing N N 93  
A1ILF CBR   H44    sing N N 94  
A1ILF CBR   H45    sing N N 95  
A1ILF CBS   H46    sing N N 96  
A1ILF NBW   H47    sing N N 97  
A1ILF NBW   H48    sing N N 98  
A1ILF CBT   H50    sing N N 99  
A1ILF CBT   H51    sing N N 100 
A1ILF CBU   H52    sing N N 101 
A1ILF CBU   H53    sing N N 102 
ALA   N     CA     sing N N 103 
ALA   N     H      sing N N 104 
ALA   N     H2     sing N N 105 
ALA   CA    C      sing N N 106 
ALA   CA    CB     sing N N 107 
ALA   CA    HA     sing N N 108 
ALA   C     O      doub N N 109 
ALA   C     OXT    sing N N 110 
ALA   CB    HB1    sing N N 111 
ALA   CB    HB2    sing N N 112 
ALA   CB    HB3    sing N N 113 
ALA   OXT   HXT    sing N N 114 
ARG   N     CA     sing N N 115 
ARG   N     H      sing N N 116 
ARG   N     H2     sing N N 117 
ARG   CA    C      sing N N 118 
ARG   CA    CB     sing N N 119 
ARG   CA    HA     sing N N 120 
ARG   C     O      doub N N 121 
ARG   C     OXT    sing N N 122 
ARG   CB    CG     sing N N 123 
ARG   CB    HB2    sing N N 124 
ARG   CB    HB3    sing N N 125 
ARG   CG    CD     sing N N 126 
ARG   CG    HG2    sing N N 127 
ARG   CG    HG3    sing N N 128 
ARG   CD    NE     sing N N 129 
ARG   CD    HD2    sing N N 130 
ARG   CD    HD3    sing N N 131 
ARG   NE    CZ     sing N N 132 
ARG   NE    HE     sing N N 133 
ARG   CZ    NH1    sing N N 134 
ARG   CZ    NH2    doub N N 135 
ARG   NH1   HH11   sing N N 136 
ARG   NH1   HH12   sing N N 137 
ARG   NH2   HH21   sing N N 138 
ARG   NH2   HH22   sing N N 139 
ARG   OXT   HXT    sing N N 140 
ASN   N     CA     sing N N 141 
ASN   N     H      sing N N 142 
ASN   N     H2     sing N N 143 
ASN   CA    C      sing N N 144 
ASN   CA    CB     sing N N 145 
ASN   CA    HA     sing N N 146 
ASN   C     O      doub N N 147 
ASN   C     OXT    sing N N 148 
ASN   CB    CG     sing N N 149 
ASN   CB    HB2    sing N N 150 
ASN   CB    HB3    sing N N 151 
ASN   CG    OD1    doub N N 152 
ASN   CG    ND2    sing N N 153 
ASN   ND2   HD21   sing N N 154 
ASN   ND2   HD22   sing N N 155 
ASN   OXT   HXT    sing N N 156 
ASP   N     CA     sing N N 157 
ASP   N     H      sing N N 158 
ASP   N     H2     sing N N 159 
ASP   CA    C      sing N N 160 
ASP   CA    CB     sing N N 161 
ASP   CA    HA     sing N N 162 
ASP   C     O      doub N N 163 
ASP   C     OXT    sing N N 164 
ASP   CB    CG     sing N N 165 
ASP   CB    HB2    sing N N 166 
ASP   CB    HB3    sing N N 167 
ASP   CG    OD1    doub N N 168 
ASP   CG    OD2    sing N N 169 
ASP   OD2   HD2    sing N N 170 
ASP   OXT   HXT    sing N N 171 
CYS   N     CA     sing N N 172 
CYS   N     H      sing N N 173 
CYS   N     H2     sing N N 174 
CYS   CA    C      sing N N 175 
CYS   CA    CB     sing N N 176 
CYS   CA    HA     sing N N 177 
CYS   C     O      doub N N 178 
CYS   C     OXT    sing N N 179 
CYS   CB    SG     sing N N 180 
CYS   CB    HB2    sing N N 181 
CYS   CB    HB3    sing N N 182 
CYS   SG    HG     sing N N 183 
CYS   OXT   HXT    sing N N 184 
GLN   N     CA     sing N N 185 
GLN   N     H      sing N N 186 
GLN   N     H2     sing N N 187 
GLN   CA    C      sing N N 188 
GLN   CA    CB     sing N N 189 
GLN   CA    HA     sing N N 190 
GLN   C     O      doub N N 191 
GLN   C     OXT    sing N N 192 
GLN   CB    CG     sing N N 193 
GLN   CB    HB2    sing N N 194 
GLN   CB    HB3    sing N N 195 
GLN   CG    CD     sing N N 196 
GLN   CG    HG2    sing N N 197 
GLN   CG    HG3    sing N N 198 
GLN   CD    OE1    doub N N 199 
GLN   CD    NE2    sing N N 200 
GLN   NE2   HE21   sing N N 201 
GLN   NE2   HE22   sing N N 202 
GLN   OXT   HXT    sing N N 203 
GLU   N     CA     sing N N 204 
GLU   N     H      sing N N 205 
GLU   N     H2     sing N N 206 
GLU   CA    C      sing N N 207 
GLU   CA    CB     sing N N 208 
GLU   CA    HA     sing N N 209 
GLU   C     O      doub N N 210 
GLU   C     OXT    sing N N 211 
GLU   CB    CG     sing N N 212 
GLU   CB    HB2    sing N N 213 
GLU   CB    HB3    sing N N 214 
GLU   CG    CD     sing N N 215 
GLU   CG    HG2    sing N N 216 
GLU   CG    HG3    sing N N 217 
GLU   CD    OE1    doub N N 218 
GLU   CD    OE2    sing N N 219 
GLU   OE2   HE2    sing N N 220 
GLU   OXT   HXT    sing N N 221 
GLY   N     CA     sing N N 222 
GLY   N     H      sing N N 223 
GLY   N     H2     sing N N 224 
GLY   CA    C      sing N N 225 
GLY   CA    HA2    sing N N 226 
GLY   CA    HA3    sing N N 227 
GLY   C     O      doub N N 228 
GLY   C     OXT    sing N N 229 
GLY   OXT   HXT    sing N N 230 
GNP   PG    O1G    doub N N 231 
GNP   PG    O2G    sing N N 232 
GNP   PG    O3G    sing N N 233 
GNP   PG    N3B    sing N N 234 
GNP   O2G   HOG2   sing N N 235 
GNP   O3G   HOG3   sing N N 236 
GNP   N3B   PB     sing N N 237 
GNP   N3B   HNB3   sing N N 238 
GNP   PB    O1B    doub N N 239 
GNP   PB    O2B    sing N N 240 
GNP   PB    O3A    sing N N 241 
GNP   O2B   HOB2   sing N N 242 
GNP   O3A   PA     sing N N 243 
GNP   PA    O1A    doub N N 244 
GNP   PA    O2A    sing N N 245 
GNP   PA    "O5'"  sing N N 246 
GNP   O2A   HOA2   sing N N 247 
GNP   "O5'" "C5'"  sing N N 248 
GNP   "C5'" "C4'"  sing N N 249 
GNP   "C5'" "H5'2" sing N N 250 
GNP   "C5'" "H5'1" sing N N 251 
GNP   "C4'" "O4'"  sing N N 252 
GNP   "C4'" "C3'"  sing N N 253 
GNP   "C4'" "H4'"  sing N N 254 
GNP   "O4'" "C1'"  sing N N 255 
GNP   "C3'" "O3'"  sing N N 256 
GNP   "C3'" "C2'"  sing N N 257 
GNP   "C3'" "H3'"  sing N N 258 
GNP   "O3'" "HO3'" sing N N 259 
GNP   "C2'" "O2'"  sing N N 260 
GNP   "C2'" "C1'"  sing N N 261 
GNP   "C2'" "H2'"  sing N N 262 
GNP   "O2'" "HO2'" sing N N 263 
GNP   "C1'" N9     sing N N 264 
GNP   "C1'" "H1'"  sing N N 265 
GNP   N9    C8     sing Y N 266 
GNP   N9    C4     sing Y N 267 
GNP   C8    N7     doub Y N 268 
GNP   C8    H8     sing N N 269 
GNP   N7    C5     sing Y N 270 
GNP   C5    C6     sing Y N 271 
GNP   C5    C4     doub Y N 272 
GNP   C6    O6     doub N N 273 
GNP   C6    N1     sing Y N 274 
GNP   N1    C2     sing Y N 275 
GNP   N1    HN1    sing N N 276 
GNP   C2    N2     sing N N 277 
GNP   C2    N3     doub Y N 278 
GNP   N2    HN21   sing N N 279 
GNP   N2    HN22   sing N N 280 
GNP   N3    C4     sing Y N 281 
HIS   N     CA     sing N N 282 
HIS   N     H      sing N N 283 
HIS   N     H2     sing N N 284 
HIS   CA    C      sing N N 285 
HIS   CA    CB     sing N N 286 
HIS   CA    HA     sing N N 287 
HIS   C     O      doub N N 288 
HIS   C     OXT    sing N N 289 
HIS   CB    CG     sing N N 290 
HIS   CB    HB2    sing N N 291 
HIS   CB    HB3    sing N N 292 
HIS   CG    ND1    sing Y N 293 
HIS   CG    CD2    doub Y N 294 
HIS   ND1   CE1    doub Y N 295 
HIS   ND1   HD1    sing N N 296 
HIS   CD2   NE2    sing Y N 297 
HIS   CD2   HD2    sing N N 298 
HIS   CE1   NE2    sing Y N 299 
HIS   CE1   HE1    sing N N 300 
HIS   NE2   HE2    sing N N 301 
HIS   OXT   HXT    sing N N 302 
HOH   O     H1     sing N N 303 
HOH   O     H2     sing N N 304 
ILE   N     CA     sing N N 305 
ILE   N     H      sing N N 306 
ILE   N     H2     sing N N 307 
ILE   CA    C      sing N N 308 
ILE   CA    CB     sing N N 309 
ILE   CA    HA     sing N N 310 
ILE   C     O      doub N N 311 
ILE   C     OXT    sing N N 312 
ILE   CB    CG1    sing N N 313 
ILE   CB    CG2    sing N N 314 
ILE   CB    HB     sing N N 315 
ILE   CG1   CD1    sing N N 316 
ILE   CG1   HG12   sing N N 317 
ILE   CG1   HG13   sing N N 318 
ILE   CG2   HG21   sing N N 319 
ILE   CG2   HG22   sing N N 320 
ILE   CG2   HG23   sing N N 321 
ILE   CD1   HD11   sing N N 322 
ILE   CD1   HD12   sing N N 323 
ILE   CD1   HD13   sing N N 324 
ILE   OXT   HXT    sing N N 325 
LEU   N     CA     sing N N 326 
LEU   N     H      sing N N 327 
LEU   N     H2     sing N N 328 
LEU   CA    C      sing N N 329 
LEU   CA    CB     sing N N 330 
LEU   CA    HA     sing N N 331 
LEU   C     O      doub N N 332 
LEU   C     OXT    sing N N 333 
LEU   CB    CG     sing N N 334 
LEU   CB    HB2    sing N N 335 
LEU   CB    HB3    sing N N 336 
LEU   CG    CD1    sing N N 337 
LEU   CG    CD2    sing N N 338 
LEU   CG    HG     sing N N 339 
LEU   CD1   HD11   sing N N 340 
LEU   CD1   HD12   sing N N 341 
LEU   CD1   HD13   sing N N 342 
LEU   CD2   HD21   sing N N 343 
LEU   CD2   HD22   sing N N 344 
LEU   CD2   HD23   sing N N 345 
LEU   OXT   HXT    sing N N 346 
LYS   N     CA     sing N N 347 
LYS   N     H      sing N N 348 
LYS   N     H2     sing N N 349 
LYS   CA    C      sing N N 350 
LYS   CA    CB     sing N N 351 
LYS   CA    HA     sing N N 352 
LYS   C     O      doub N N 353 
LYS   C     OXT    sing N N 354 
LYS   CB    CG     sing N N 355 
LYS   CB    HB2    sing N N 356 
LYS   CB    HB3    sing N N 357 
LYS   CG    CD     sing N N 358 
LYS   CG    HG2    sing N N 359 
LYS   CG    HG3    sing N N 360 
LYS   CD    CE     sing N N 361 
LYS   CD    HD2    sing N N 362 
LYS   CD    HD3    sing N N 363 
LYS   CE    NZ     sing N N 364 
LYS   CE    HE2    sing N N 365 
LYS   CE    HE3    sing N N 366 
LYS   NZ    HZ1    sing N N 367 
LYS   NZ    HZ2    sing N N 368 
LYS   NZ    HZ3    sing N N 369 
LYS   OXT   HXT    sing N N 370 
MET   N     CA     sing N N 371 
MET   N     H      sing N N 372 
MET   N     H2     sing N N 373 
MET   CA    C      sing N N 374 
MET   CA    CB     sing N N 375 
MET   CA    HA     sing N N 376 
MET   C     O      doub N N 377 
MET   C     OXT    sing N N 378 
MET   CB    CG     sing N N 379 
MET   CB    HB2    sing N N 380 
MET   CB    HB3    sing N N 381 
MET   CG    SD     sing N N 382 
MET   CG    HG2    sing N N 383 
MET   CG    HG3    sing N N 384 
MET   SD    CE     sing N N 385 
MET   CE    HE1    sing N N 386 
MET   CE    HE2    sing N N 387 
MET   CE    HE3    sing N N 388 
MET   OXT   HXT    sing N N 389 
PHE   N     CA     sing N N 390 
PHE   N     H      sing N N 391 
PHE   N     H2     sing N N 392 
PHE   CA    C      sing N N 393 
PHE   CA    CB     sing N N 394 
PHE   CA    HA     sing N N 395 
PHE   C     O      doub N N 396 
PHE   C     OXT    sing N N 397 
PHE   CB    CG     sing N N 398 
PHE   CB    HB2    sing N N 399 
PHE   CB    HB3    sing N N 400 
PHE   CG    CD1    doub Y N 401 
PHE   CG    CD2    sing Y N 402 
PHE   CD1   CE1    sing Y N 403 
PHE   CD1   HD1    sing N N 404 
PHE   CD2   CE2    doub Y N 405 
PHE   CD2   HD2    sing N N 406 
PHE   CE1   CZ     doub Y N 407 
PHE   CE1   HE1    sing N N 408 
PHE   CE2   CZ     sing Y N 409 
PHE   CE2   HE2    sing N N 410 
PHE   CZ    HZ     sing N N 411 
PHE   OXT   HXT    sing N N 412 
PRO   N     CA     sing N N 413 
PRO   N     CD     sing N N 414 
PRO   N     H      sing N N 415 
PRO   CA    C      sing N N 416 
PRO   CA    CB     sing N N 417 
PRO   CA    HA     sing N N 418 
PRO   C     O      doub N N 419 
PRO   C     OXT    sing N N 420 
PRO   CB    CG     sing N N 421 
PRO   CB    HB2    sing N N 422 
PRO   CB    HB3    sing N N 423 
PRO   CG    CD     sing N N 424 
PRO   CG    HG2    sing N N 425 
PRO   CG    HG3    sing N N 426 
PRO   CD    HD2    sing N N 427 
PRO   CD    HD3    sing N N 428 
PRO   OXT   HXT    sing N N 429 
SER   N     CA     sing N N 430 
SER   N     H      sing N N 431 
SER   N     H2     sing N N 432 
SER   CA    C      sing N N 433 
SER   CA    CB     sing N N 434 
SER   CA    HA     sing N N 435 
SER   C     O      doub N N 436 
SER   C     OXT    sing N N 437 
SER   CB    OG     sing N N 438 
SER   CB    HB2    sing N N 439 
SER   CB    HB3    sing N N 440 
SER   OG    HG     sing N N 441 
SER   OXT   HXT    sing N N 442 
THR   N     CA     sing N N 443 
THR   N     H      sing N N 444 
THR   N     H2     sing N N 445 
THR   CA    C      sing N N 446 
THR   CA    CB     sing N N 447 
THR   CA    HA     sing N N 448 
THR   C     O      doub N N 449 
THR   C     OXT    sing N N 450 
THR   CB    OG1    sing N N 451 
THR   CB    CG2    sing N N 452 
THR   CB    HB     sing N N 453 
THR   OG1   HG1    sing N N 454 
THR   CG2   HG21   sing N N 455 
THR   CG2   HG22   sing N N 456 
THR   CG2   HG23   sing N N 457 
THR   OXT   HXT    sing N N 458 
TYR   N     CA     sing N N 459 
TYR   N     H      sing N N 460 
TYR   N     H2     sing N N 461 
TYR   CA    C      sing N N 462 
TYR   CA    CB     sing N N 463 
TYR   CA    HA     sing N N 464 
TYR   C     O      doub N N 465 
TYR   C     OXT    sing N N 466 
TYR   CB    CG     sing N N 467 
TYR   CB    HB2    sing N N 468 
TYR   CB    HB3    sing N N 469 
TYR   CG    CD1    doub Y N 470 
TYR   CG    CD2    sing Y N 471 
TYR   CD1   CE1    sing Y N 472 
TYR   CD1   HD1    sing N N 473 
TYR   CD2   CE2    doub Y N 474 
TYR   CD2   HD2    sing N N 475 
TYR   CE1   CZ     doub Y N 476 
TYR   CE1   HE1    sing N N 477 
TYR   CE2   CZ     sing Y N 478 
TYR   CE2   HE2    sing N N 479 
TYR   CZ    OH     sing N N 480 
TYR   OH    HH     sing N N 481 
TYR   OXT   HXT    sing N N 482 
VAL   N     CA     sing N N 483 
VAL   N     H      sing N N 484 
VAL   N     H2     sing N N 485 
VAL   CA    C      sing N N 486 
VAL   CA    CB     sing N N 487 
VAL   CA    HA     sing N N 488 
VAL   C     O      doub N N 489 
VAL   C     OXT    sing N N 490 
VAL   CB    CG1    sing N N 491 
VAL   CB    CG2    sing N N 492 
VAL   CB    HB     sing N N 493 
VAL   CG1   HG11   sing N N 494 
VAL   CG1   HG12   sing N N 495 
VAL   CG1   HG13   sing N N 496 
VAL   CG2   HG21   sing N N 497 
VAL   CG2   HG22   sing N N 498 
VAL   CG2   HG23   sing N N 499 
VAL   OXT   HXT    sing N N 500 
# 
_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                    9GH2 
_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]   0.013799 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.004831 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.029171 
_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]   0.015225 
_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   ? 7.684  2.961   24.413 1.00 59.94 ? 1   MET   A N     1 
ATOM   2    C  CA    . MET   A 1 4   ? 9.135  3.300   24.391 1.00 55.01 ? 1   MET   A CA    1 
ATOM   3    C  C     . MET   A 1 4   ? 9.832  2.520   23.276 1.00 46.68 ? 1   MET   A C     1 
ATOM   4    O  O     . MET   A 1 4   ? 9.870  1.309   23.340 1.00 46.06 ? 1   MET   A O     1 
ATOM   5    C  CB    . MET   A 1 4   ? 9.794  2.926   25.710 1.00 58.07 ? 1   MET   A CB    1 
ATOM   6    C  CG    . MET   A 1 4   ? 11.209 3.377   25.809 1.00 54.04 ? 1   MET   A CG    1 
ATOM   7    S  SD    . MET   A 1 4   ? 11.958 2.584   27.204 1.00 53.39 ? 1   MET   A SD    1 
ATOM   8    C  CE    . MET   A 1 4   ? 11.050 3.344   28.537 1.00 51.10 ? 1   MET   A CE    1 
ATOM   9    N  N     . THR   A 1 5   ? 10.320 3.241   22.285 1.00 44.13 ? 2   THR   A N     1 
ATOM   10   C  CA    . THR   A 1 5   ? 10.962 2.610   21.116 1.00 41.22 ? 2   THR   A CA    1 
ATOM   11   C  C     . THR   A 1 5   ? 12.194 1.820   21.561 1.00 38.44 ? 2   THR   A C     1 
ATOM   12   O  O     . THR   A 1 5   ? 12.975 2.347   22.360 1.00 39.46 ? 2   THR   A O     1 
ATOM   13   C  CB    . THR   A 1 5   ? 11.395 3.707   20.150 1.00 44.43 ? 2   THR   A CB    1 
ATOM   14   O  OG1   . THR   A 1 5   ? 10.259 4.554   20.004 1.00 49.46 ? 2   THR   A OG1   1 
ATOM   15   C  CG2   . THR   A 1 5   ? 11.833 3.176   18.809 1.00 46.42 ? 2   THR   A CG2   1 
ATOM   16   N  N     . GLU   A 1 6   ? 12.327 0.618   21.014 1.00 37.89 ? 3   GLU   A N     1 
ATOM   17   C  CA    . GLU   A 1 6   ? 13.472 -0.273  21.278 1.00 37.08 ? 3   GLU   A CA    1 
ATOM   18   C  C     . GLU   A 1 6   ? 14.269 -0.362  19.976 1.00 35.46 ? 3   GLU   A C     1 
ATOM   19   O  O     . GLU   A 1 6   ? 13.670 -0.479  18.936 1.00 38.49 ? 3   GLU   A O     1 
ATOM   20   C  CB    . GLU   A 1 6   ? 12.967 -1.630  21.747 1.00 45.35 ? 3   GLU   A CB    1 
ATOM   21   C  CG    . GLU   A 1 6   ? 13.867 -2.775  21.359 1.00 52.26 ? 3   GLU   A CG    1 
ATOM   22   C  CD    . GLU   A 1 6   ? 13.615 -4.038  22.145 1.00 55.45 ? 3   GLU   A CD    1 
ATOM   23   O  OE1   . GLU   A 1 6   ? 12.782 -3.988  23.075 1.00 51.73 ? 3   GLU   A OE1   1 
ATOM   24   O  OE2   . GLU   A 1 6   ? 14.263 -5.056  21.830 1.00 63.66 ? 3   GLU   A OE2   1 
ATOM   25   N  N     . TYR   A 1 7   ? 15.593 -0.265  20.083 1.00 30.29 ? 4   TYR   A N     1 
ATOM   26   C  CA    . TYR   A 1 7   ? 16.484 -0.345  18.905 1.00 30.03 ? 4   TYR   A CA    1 
ATOM   27   C  C     . TYR   A 1 7   ? 17.442 -1.515  19.081 1.00 28.94 ? 4   TYR   A C     1 
ATOM   28   O  O     . TYR   A 1 7   ? 18.089 -1.570  20.069 1.00 29.16 ? 4   TYR   A O     1 
ATOM   29   C  CB    . TYR   A 1 7   ? 17.304 0.936   18.791 1.00 27.06 ? 4   TYR   A CB    1 
ATOM   30   C  CG    . TYR   A 1 7   ? 16.498 2.184   18.555 1.00 28.63 ? 4   TYR   A CG    1 
ATOM   31   C  CD1   . TYR   A 1 7   ? 16.007 2.482   17.306 1.00 32.36 ? 4   TYR   A CD1   1 
ATOM   32   C  CD2   . TYR   A 1 7   ? 16.248 3.064   19.585 1.00 30.96 ? 4   TYR   A CD2   1 
ATOM   33   C  CE1   . TYR   A 1 7   ? 15.262 3.627   17.093 1.00 33.53 ? 4   TYR   A CE1   1 
ATOM   34   C  CE2   . TYR   A 1 7   ? 15.523 4.220   19.385 1.00 34.17 ? 4   TYR   A CE2   1 
ATOM   35   C  CZ    . TYR   A 1 7   ? 15.034 4.503   18.132 1.00 33.08 ? 4   TYR   A CZ    1 
ATOM   36   O  OH    . TYR   A 1 7   ? 14.324 5.644   17.937 1.00 37.30 ? 4   TYR   A OH    1 
ATOM   37   N  N     . LYS   A 1 8   ? 17.513 -2.390  18.104 1.00 25.18 ? 5   LYS   A N     1 
ATOM   38   C  CA    . LYS   A 1 8   ? 18.466 -3.511  18.207 1.00 26.24 ? 5   LYS   A CA    1 
ATOM   39   C  C     . LYS   A 1 8   ? 19.761 -3.096  17.508 1.00 22.92 ? 5   LYS   A C     1 
ATOM   40   O  O     . LYS   A 1 8   ? 19.750 -2.924  16.317 1.00 23.65 ? 5   LYS   A O     1 
ATOM   41   C  CB    . LYS   A 1 8   ? 17.878 -4.728  17.518 1.00 26.88 ? 5   LYS   A CB    1 
ATOM   42   C  CG    . LYS   A 1 8   ? 16.565 -5.208  18.106 1.00 33.04 ? 5   LYS   A CG    1 
ATOM   43   C  CD    . LYS   A 1 8   ? 16.669 -6.474  18.872 1.00 37.91 ? 5   LYS   A CD    1 
ATOM   44   C  CE    . LYS   A 1 8   ? 15.344 -7.205  18.997 1.00 42.97 ? 5   LYS   A CE    1 
ATOM   45   N  NZ    . LYS   A 1 8   ? 14.217 -6.256  19.107 1.00 47.37 ? 5   LYS   A NZ    1 
ATOM   46   N  N     . LEU   A 1 9   ? 20.831 -2.990  18.276 1.00 22.49 ? 6   LEU   A N     1 
ATOM   47   C  CA    . LEU   A 1 9   ? 22.156 -2.592  17.749 1.00 20.59 ? 6   LEU   A CA    1 
ATOM   48   C  C     . LEU   A 1 9   ? 23.080 -3.809  17.760 1.00 20.13 ? 6   LEU   A C     1 
ATOM   49   O  O     . LEU   A 1 9   ? 23.026 -4.560  18.701 1.00 22.82 ? 6   LEU   A O     1 
ATOM   50   C  CB    . LEU   A 1 9   ? 22.732 -1.516  18.657 1.00 22.67 ? 6   LEU   A CB    1 
ATOM   51   C  CG    . LEU   A 1 9   ? 21.833 -0.314  18.911 1.00 25.43 ? 6   LEU   A CG    1 
ATOM   52   C  CD1   . LEU   A 1 9   ? 22.606 0.779   19.608 1.00 27.57 ? 6   LEU   A CD1   1 
ATOM   53   C  CD2   . LEU   A 1 9   ? 21.248 0.202   17.610 1.00 26.71 ? 6   LEU   A CD2   1 
ATOM   54   N  N     . VAL   A 1 10  ? 23.874 -3.958  16.712 1.00 19.17 ? 7   VAL   A N     1 
ATOM   55   C  CA    . VAL   A 1 10  ? 24.850 -5.073  16.596 1.00 19.61 ? 7   VAL   A CA    1 
ATOM   56   C  C     . VAL   A 1 10  ? 26.237 -4.462  16.417 1.00 19.55 ? 7   VAL   A C     1 
ATOM   57   O  O     . VAL   A 1 10  ? 26.419 -3.568  15.574 1.00 19.74 ? 7   VAL   A O     1 
ATOM   58   C  CB    . VAL   A 1 10  ? 24.502 -6.030  15.444 1.00 20.70 ? 7   VAL   A CB    1 
ATOM   59   C  CG1   . VAL   A 1 10  ? 25.416 -7.255  15.455 1.00 22.18 ? 7   VAL   A CG1   1 
ATOM   60   C  CG2   . VAL   A 1 10  ? 23.044 -6.462  15.480 1.00 20.10 ? 7   VAL   A CG2   1 
ATOM   61   N  N     . VAL   A 1 11  ? 27.192 -4.967  17.192 1.00 18.85 ? 8   VAL   A N     1 
ATOM   62   C  CA    . VAL   A 1 11  ? 28.598 -4.496  17.126 1.00 19.28 ? 8   VAL   A CA    1 
ATOM   63   C  C     . VAL   A 1 11  ? 29.353 -5.600  16.392 1.00 19.29 ? 8   VAL   A C     1 
ATOM   64   O  O     . VAL   A 1 11  ? 29.324 -6.720  16.893 1.00 20.47 ? 8   VAL   A O     1 
ATOM   65   C  CB    . VAL   A 1 11  ? 29.161 -4.230  18.527 1.00 18.99 ? 8   VAL   A CB    1 
ATOM   66   C  CG1   . VAL   A 1 11  ? 30.562 -3.651  18.456 1.00 20.84 ? 8   VAL   A CG1   1 
ATOM   67   C  CG2   . VAL   A 1 11  ? 28.292 -3.314  19.346 1.00 21.55 ? 8   VAL   A CG2   1 
ATOM   68   N  N     . VAL   A 1 12  ? 29.905 -5.292  15.219 1.00 18.26 ? 9   VAL   A N     1 
ATOM   69   C  CA    . VAL   A 1 12  ? 30.587 -6.288  14.341 1.00 19.68 ? 9   VAL   A CA    1 
ATOM   70   C  C     . VAL   A 1 12  ? 32.007 -5.796  14.066 1.00 20.05 ? 9   VAL   A C     1 
ATOM   71   O  O     . VAL   A 1 12  ? 32.293 -4.583  14.219 1.00 19.47 ? 9   VAL   A O     1 
ATOM   72   C  CB    . VAL   A 1 12  ? 29.823 -6.524  13.029 1.00 20.00 ? 9   VAL   A CB    1 
ATOM   73   C  CG1   . VAL   A 1 12  ? 28.437 -7.078  13.296 1.00 21.89 ? 9   VAL   A CG1   1 
ATOM   74   C  CG2   . VAL   A 1 12  ? 29.766 -5.303  12.126 1.00 21.87 ? 9   VAL   A CG2   1 
ATOM   75   N  N     . GLY   A 1 13  ? 32.870 -6.710  13.628 1.00 20.07 ? 10  GLY   A N     1 
ATOM   76   C  CA    . GLY   A 1 13  ? 34.267 -6.355  13.353 1.00 20.96 ? 10  GLY   A CA    1 
ATOM   77   C  C     . GLY   A 1 13  ? 35.203 -7.503  13.624 1.00 21.02 ? 10  GLY   A C     1 
ATOM   78   O  O     . GLY   A 1 13  ? 34.806 -8.448  14.310 1.00 21.99 ? 10  GLY   A O     1 
ATOM   79   N  N     . ALA   A 1 14  ? 36.422 -7.378  13.108 1.00 20.48 ? 11  ALA   A N     1 
ATOM   80   C  CA    . ALA   A 1 14  ? 37.432 -8.448  13.170 1.00 23.57 ? 11  ALA   A CA    1 
ATOM   81   C  C     . ALA   A 1 14  ? 37.815 -8.729  14.625 1.00 23.03 ? 11  ALA   A C     1 
ATOM   82   O  O     . ALA   A 1 14  ? 37.531 -7.917  15.526 1.00 24.56 ? 11  ALA   A O     1 
ATOM   83   C  CB    . ALA   A 1 14  ? 38.619 -8.045  12.347 1.00 24.58 ? 11  ALA   A CB    1 
ATOM   84   N  N     . GLY   A 1 15  ? 38.475 -9.860  14.851 1.00 25.64 ? 12  GLY   A N     1 
ATOM   85   C  CA    . GLY   A 1 15  ? 38.917 -10.232 16.199 1.00 28.27 ? 12  GLY   A CA    1 
ATOM   86   C  C     . GLY   A 1 15  ? 39.781 -9.145  16.802 1.00 26.04 ? 12  GLY   A C     1 
ATOM   87   O  O     . GLY   A 1 15  ? 40.628 -8.579  16.080 1.00 28.26 ? 12  GLY   A O     1 
ATOM   88   N  N     . GLY   A 1 16  ? 39.544 -8.843  18.077 1.00 24.62 ? 13  GLY   A N     1 
ATOM   89   C  CA    . GLY   A 1 16  ? 40.399 -7.969  18.903 1.00 26.27 ? 13  GLY   A CA    1 
ATOM   90   C  C     . GLY   A 1 16  ? 40.274 -6.481  18.625 1.00 26.77 ? 13  GLY   A C     1 
ATOM   91   O  O     . GLY   A 1 16  ? 41.085 -5.705  19.180 1.00 28.09 ? 13  GLY   A O     1 
ATOM   92   N  N     . VAL   A 1 17  ? 39.293 -6.012  17.850 1.00 24.06 ? 14  VAL   A N     1 
ATOM   93   C  CA    . VAL   A 1 17  ? 39.220 -4.562  17.508 1.00 24.32 ? 14  VAL   A CA    1 
ATOM   94   C  C     . VAL   A 1 17  ? 38.627 -3.763  18.677 1.00 23.71 ? 14  VAL   A C     1 
ATOM   95   O  O     . VAL   A 1 17  ? 38.738 -2.528  18.663 1.00 23.86 ? 14  VAL   A O     1 
ATOM   96   C  CB    . VAL   A 1 17  ? 38.440 -4.302  16.212 1.00 23.06 ? 14  VAL   A CB    1 
ATOM   97   C  CG1   . VAL   A 1 17  ? 39.115 -4.957  15.022 1.00 23.09 ? 14  VAL   A CG1   1 
ATOM   98   C  CG2   . VAL   A 1 17  ? 36.972 -4.706  16.285 1.00 22.21 ? 14  VAL   A CG2   1 
ATOM   99   N  N     . GLY   A 1 18  ? 38.011 -4.445  19.649 1.00 23.74 ? 15  GLY   A N     1 
ATOM   100  C  CA    . GLY   A 1 18  ? 37.435 -3.798  20.842 1.00 24.38 ? 15  GLY   A CA    1 
ATOM   101  C  C     . GLY   A 1 18  ? 35.914 -3.750  20.809 1.00 22.76 ? 15  GLY   A C     1 
ATOM   102  O  O     . GLY   A 1 18  ? 35.351 -2.855  21.438 1.00 22.60 ? 15  GLY   A O     1 
ATOM   103  N  N     . LYS   A 1 19  ? 35.262 -4.682  20.113 1.00 20.53 ? 16  LYS   A N     1 
ATOM   104  C  CA    . LYS   A 1 19  ? 33.779 -4.766  20.109 1.00 20.06 ? 16  LYS   A CA    1 
ATOM   105  C  C     . LYS   A 1 19  ? 33.272 -4.858  21.551 1.00 21.50 ? 16  LYS   A C     1 
ATOM   106  O  O     . LYS   A 1 19  ? 32.381 -4.087  21.945 1.00 22.39 ? 16  LYS   A O     1 
ATOM   107  C  CB    . LYS   A 1 19  ? 33.322 -5.992  19.322 1.00 21.81 ? 16  LYS   A CB    1 
ATOM   108  C  CG    . LYS   A 1 19  ? 33.673 -5.963  17.848 1.00 22.30 ? 16  LYS   A CG    1 
ATOM   109  C  CD    . LYS   A 1 19  ? 33.244 -7.194  17.085 1.00 23.65 ? 16  LYS   A CD    1 
ATOM   110  C  CE    . LYS   A 1 19  ? 33.870 -8.478  17.565 1.00 23.77 ? 16  LYS   A CE    1 
ATOM   111  N  NZ    . LYS   A 1 19  ? 35.308 -8.549  17.220 1.00 23.43 ? 16  LYS   A NZ    1 
ATOM   112  N  N     . SER   A 1 20  ? 33.835 -5.769  22.330 1.00 21.99 ? 17  SER   A N     1 
ATOM   113  C  CA    . SER   A 1 20  ? 33.378 -6.013  23.717 1.00 22.37 ? 17  SER   A CA    1 
ATOM   114  C  C     . SER   A 1 20  ? 33.706 -4.801  24.591 1.00 22.75 ? 17  SER   A C     1 
ATOM   115  O  O     . SER   A 1 20  ? 32.849 -4.386  25.386 1.00 23.92 ? 17  SER   A O     1 
ATOM   116  C  CB    . SER   A 1 20  ? 33.984 -7.260  24.277 1.00 22.03 ? 17  SER   A CB    1 
ATOM   117  O  OG    . SER   A 1 20  ? 33.532 -8.395  23.571 1.00 24.52 ? 17  SER   A OG    1 
ATOM   118  N  N     . ALA   A 1 21  ? 34.945 -4.295  24.517 1.00 23.41 ? 18  ALA   A N     1 
ATOM   119  C  CA    . ALA   A 1 21  ? 35.382 -3.117  25.296 1.00 23.80 ? 18  ALA   A CA    1 
ATOM   120  C  C     . ALA   A 1 21  ? 34.461 -1.928  24.999 1.00 23.38 ? 18  ALA   A C     1 
ATOM   121  O  O     . ALA   A 1 21  ? 34.092 -1.225  25.931 1.00 25.65 ? 18  ALA   A O     1 
ATOM   122  C  CB    . ALA   A 1 21  ? 36.830 -2.811  24.997 1.00 25.75 ? 18  ALA   A CB    1 
ATOM   123  N  N     . LEU   A 1 22  ? 34.116 -1.689  23.740 1.00 23.25 ? 19  LEU   A N     1 
ATOM   124  C  CA    . LEU   A 1 22  ? 33.206 -0.566  23.398 1.00 22.95 ? 19  LEU   A CA    1 
ATOM   125  C  C     . LEU   A 1 22  ? 31.853 -0.771  24.079 1.00 24.14 ? 19  LEU   A C     1 
ATOM   126  O  O     . LEU   A 1 22  ? 31.288 0.188   24.631 1.00 24.44 ? 19  LEU   A O     1 
ATOM   127  C  CB    . LEU   A 1 22  ? 33.044 -0.484  21.884 1.00 23.03 ? 19  LEU   A CB    1 
ATOM   128  C  CG    . LEU   A 1 22  ? 34.214 0.202   21.190 1.00 24.24 ? 19  LEU   A CG    1 
ATOM   129  C  CD1   . LEU   A 1 22  ? 34.113 0.026   19.692 1.00 25.87 ? 19  LEU   A CD1   1 
ATOM   130  C  CD2   . LEU   A 1 22  ? 34.303 1.674   21.570 1.00 25.61 ? 19  LEU   A CD2   1 
ATOM   131  N  N     . THR   A 1 23  ? 31.288 -1.953  23.965 1.00 23.69 ? 20  THR   A N     1 
ATOM   132  C  CA    . THR   A 1 23  ? 29.952 -2.222  24.545 1.00 23.89 ? 20  THR   A CA    1 
ATOM   133  C  C     . THR   A 1 23  ? 29.965 -2.054  26.074 1.00 26.13 ? 20  THR   A C     1 
ATOM   134  O  O     . THR   A 1 23  ? 29.085 -1.413  26.585 1.00 27.95 ? 20  THR   A O     1 
ATOM   135  C  CB    . THR   A 1 23  ? 29.491 -3.610  24.113 1.00 25.04 ? 20  THR   A CB    1 
ATOM   136  O  OG1   . THR   A 1 23  ? 29.570 -3.688  22.698 1.00 25.92 ? 20  THR   A OG1   1 
ATOM   137  C  CG2   . THR   A 1 23  ? 28.085 -3.910  24.566 1.00 25.65 ? 20  THR   A CG2   1 
ATOM   138  N  N     . ILE   A 1 24  ? 30.970 -2.599  26.749 1.00 24.47 ? 21  ILE   A N     1 
ATOM   139  C  CA    . ILE   A 1 24  ? 31.074 -2.501  28.228 1.00 27.69 ? 21  ILE   A CA    1 
ATOM   140  C  C     . ILE   A 1 24  ? 31.314 -1.052  28.651 1.00 25.88 ? 21  ILE   A C     1 
ATOM   141  O  O     . ILE   A 1 24  ? 30.801 -0.649  29.650 1.00 27.73 ? 21  ILE   A O     1 
ATOM   142  C  CB    . ILE   A 1 24  ? 32.100 -3.508  28.759 1.00 28.89 ? 21  ILE   A CB    1 
ATOM   143  C  CG1   . ILE   A 1 24  ? 31.637 -4.921  28.433 1.00 31.41 ? 21  ILE   A CG1   1 
ATOM   144  C  CG2   . ILE   A 1 24  ? 32.333 -3.318  30.240 1.00 30.97 ? 21  ILE   A CG2   1 
ATOM   145  C  CD1   . ILE   A 1 24  ? 32.713 -5.939  28.456 1.00 37.20 ? 21  ILE   A CD1   1 
ATOM   146  N  N     . GLN   A 1 25  ? 32.054 -0.284  27.867 1.00 27.99 ? 22  GLN   A N     1 
ATOM   147  C  CA    . GLN   A 1 25  ? 32.267 1.150   28.160 1.00 31.84 ? 22  GLN   A CA    1 
ATOM   148  C  C     . GLN   A 1 25  ? 30.905 1.856   28.093 1.00 32.16 ? 22  GLN   A C     1 
ATOM   149  O  O     . GLN   A 1 25  ? 30.624 2.652   28.944 1.00 32.90 ? 22  GLN   A O     1 
ATOM   150  C  CB    . GLN   A 1 25  ? 33.327 1.662   27.188 1.00 35.29 ? 22  GLN   A CB    1 
ATOM   151  C  CG    . GLN   A 1 25  ? 33.930 3.021   27.465 1.00 38.19 ? 22  GLN   A CG    1 
ATOM   152  C  CD    . GLN   A 1 25  ? 34.536 3.258   28.820 1.00 36.16 ? 22  GLN   A CD    1 
ATOM   153  O  OE1   . GLN   A 1 25  ? 33.831 3.536   29.756 1.00 39.86 ? 22  GLN   A OE1   1 
ATOM   154  N  NE2   . GLN   A 1 25  ? 35.849 3.243   28.904 1.00 36.74 ? 22  GLN   A NE2   1 
ATOM   155  N  N     . LEU   A 1 26  ? 30.058 1.527   27.134 1.00 29.27 ? 23  LEU   A N     1 
ATOM   156  C  CA    . LEU   A 1 26  ? 28.738 2.196   27.081 1.00 30.66 ? 23  LEU   A CA    1 
ATOM   157  C  C     . LEU   A 1 26  ? 27.892 1.799   28.293 1.00 29.29 ? 23  LEU   A C     1 
ATOM   158  O  O     . LEU   A 1 26  ? 27.278 2.652   28.853 1.00 33.55 ? 23  LEU   A O     1 
ATOM   159  C  CB    . LEU   A 1 26  ? 28.001 1.799   25.803 1.00 30.28 ? 23  LEU   A CB    1 
ATOM   160  C  CG    . LEU   A 1 26  ? 26.701 2.569   25.577 1.00 31.94 ? 23  LEU   A CG    1 
ATOM   161  C  CD1   . LEU   A 1 26  ? 26.974 3.978   25.113 1.00 34.69 ? 23  LEU   A CD1   1 
ATOM   162  C  CD2   . LEU   A 1 26  ? 25.822 1.865   24.583 1.00 31.79 ? 23  LEU   A CD2   1 
ATOM   163  N  N     . ILE   A 1 27  ? 27.886 0.526   28.639 1.00 29.19 ? 24  ILE   A N     1 
ATOM   164  C  CA    . ILE   A 1 27  ? 27.044 -0.053  29.723 1.00 29.27 ? 24  ILE   A CA    1 
ATOM   165  C  C     . ILE   A 1 27  ? 27.563 0.282   31.124 1.00 31.13 ? 24  ILE   A C     1 
ATOM   166  O  O     . ILE   A 1 27  ? 26.807 0.865   31.888 1.00 35.34 ? 24  ILE   A O     1 
ATOM   167  C  CB    . ILE   A 1 27  ? 26.876 -1.567  29.517 1.00 29.17 ? 24  ILE   A CB    1 
ATOM   168  C  CG1   . ILE   A 1 27  ? 26.259 -1.876  28.160 1.00 29.52 ? 24  ILE   A CG1   1 
ATOM   169  C  CG2   . ILE   A 1 27  ? 26.066 -2.183  30.647 1.00 31.38 ? 24  ILE   A CG2   1 
ATOM   170  C  CD1   . ILE   A 1 27  ? 24.910 -1.253  27.981 1.00 31.04 ? 24  ILE   A CD1   1 
ATOM   171  N  N     . GLN   A 1 28  ? 28.792 -0.086  31.432 1.00 29.95 ? 25  GLN   A N     1 
ATOM   172  C  CA    . GLN   A 1 28  ? 29.285 0.110   32.813 1.00 33.45 ? 25  GLN   A CA    1 
ATOM   173  C  C     . GLN   A 1 28  ? 30.066 1.399   32.992 1.00 33.38 ? 25  GLN   A C     1 
ATOM   174  O  O     . GLN   A 1 28  ? 30.412 1.667   34.102 1.00 36.20 ? 25  GLN   A O     1 
ATOM   175  C  CB    . GLN   A 1 28  ? 30.270 -1.000  33.157 1.00 32.26 ? 25  GLN   A CB    1 
ATOM   176  C  CG    . GLN   A 1 28  ? 29.699 -2.377  32.960 1.00 34.33 ? 25  GLN   A CG    1 
ATOM   177  C  CD    . GLN   A 1 28  ? 30.645 -3.433  33.451 1.00 35.93 ? 25  GLN   A CD    1 
ATOM   178  O  OE1   . GLN   A 1 28  ? 31.712 -3.143  33.946 1.00 41.62 ? 25  GLN   A OE1   1 
ATOM   179  N  NE2   . GLN   A 1 28  ? 30.242 -4.671  33.321 1.00 41.39 ? 25  GLN   A NE2   1 
ATOM   180  N  N     . ASN   A 1 29  ? 30.438 2.085   31.909 1.00 33.66 ? 26  ASN   A N     1 
ATOM   181  C  CA    . ASN   A 1 29  ? 31.358 3.259   31.916 1.00 37.08 ? 26  ASN   A CA    1 
ATOM   182  C  C     . ASN   A 1 29  ? 32.718 2.835   32.466 1.00 35.37 ? 26  ASN   A C     1 
ATOM   183  O  O     . ASN   A 1 29  ? 33.348 3.634   33.083 1.00 39.60 ? 26  ASN   A O     1 
ATOM   184  C  CB    . ASN   A 1 29  ? 30.885 4.492   32.691 1.00 39.48 ? 26  ASN   A CB    1 
ATOM   185  C  CG    . ASN   A 1 29  ? 29.753 5.236   32.039 1.00 48.12 ? 26  ASN   A CG    1 
ATOM   186  O  OD1   . ASN   A 1 29  ? 28.785 4.635   31.607 1.00 57.26 ? 26  ASN   A OD1   1 
ATOM   187  N  ND2   . ASN   A 1 29  ? 29.855 6.549   31.995 1.00 54.22 ? 26  ASN   A ND2   1 
ATOM   188  N  N     . HIS   A 1 30  ? 33.136 1.613   32.199 1.00 32.34 ? 27  HIS   A N     1 
ATOM   189  C  CA    . HIS   A 1 30  ? 34.377 1.031   32.733 1.00 34.17 ? 27  HIS   A CA    1 
ATOM   190  C  C     . HIS   A 1 30  ? 35.091 0.310   31.593 1.00 33.17 ? 27  HIS   A C     1 
ATOM   191  O  O     . HIS   A 1 30  ? 34.442 -0.281  30.760 1.00 33.26 ? 27  HIS   A O     1 
ATOM   192  C  CB    . HIS   A 1 30  ? 34.020 0.065   33.864 1.00 34.45 ? 27  HIS   A CB    1 
ATOM   193  C  CG    . HIS   A 1 30  ? 35.198 -0.528  34.547 1.00 35.34 ? 27  HIS   A CG    1 
ATOM   194  N  ND1   . HIS   A 1 30  ? 36.008 0.206   35.346 1.00 38.17 ? 27  HIS   A ND1   1 
ATOM   195  C  CD2   . HIS   A 1 30  ? 35.693 -1.775  34.562 1.00 40.68 ? 27  HIS   A CD2   1 
ATOM   196  C  CE1   . HIS   A 1 30  ? 36.957 -0.558  35.815 1.00 39.36 ? 27  HIS   A CE1   1 
ATOM   197  N  NE2   . HIS   A 1 30  ? 36.791 -1.761  35.360 1.00 43.05 ? 27  HIS   A NE2   1 
ATOM   198  N  N     . PHE   A 1 31  ? 36.422 0.405   31.608 1.00 33.11 ? 28  PHE   A N     1 
ATOM   199  C  CA    . PHE   A 1 31  ? 37.302 -0.251  30.612 1.00 31.15 ? 28  PHE   A CA    1 
ATOM   200  C  C     . PHE   A 1 31  ? 37.655 -1.642  31.112 1.00 33.67 ? 28  PHE   A C     1 
ATOM   201  O  O     . PHE   A 1 31  ? 38.318 -1.777  32.101 1.00 38.68 ? 28  PHE   A O     1 
ATOM   202  C  CB    . PHE   A 1 31  ? 38.555 0.574   30.325 1.00 33.53 ? 28  PHE   A CB    1 
ATOM   203  C  CG    . PHE   A 1 31  ? 39.482 -0.035  29.308 1.00 35.24 ? 28  PHE   A CG    1 
ATOM   204  C  CD1   . PHE   A 1 31  ? 39.061 -0.302  28.022 1.00 33.81 ? 28  PHE   A CD1   1 
ATOM   205  C  CD2   . PHE   A 1 31  ? 40.790 -0.331  29.637 1.00 36.71 ? 28  PHE   A CD2   1 
ATOM   206  C  CE1   . PHE   A 1 31  ? 39.917 -0.875  27.104 1.00 35.50 ? 28  PHE   A CE1   1 
ATOM   207  C  CE2   . PHE   A 1 31  ? 41.648 -0.896  28.713 1.00 36.66 ? 28  PHE   A CE2   1 
ATOM   208  C  CZ    . PHE   A 1 31  ? 41.219 -1.155  27.443 1.00 36.30 ? 28  PHE   A CZ    1 
ATOM   209  N  N     . VAL   A 1 32  ? 37.192 -2.633  30.373 1.00 38.97 ? 29  VAL   A N     1 
ATOM   210  C  CA    . VAL   A 1 32  ? 37.366 -4.073  30.686 1.00 46.81 ? 29  VAL   A CA    1 
ATOM   211  C  C     . VAL   A 1 32  ? 38.792 -4.476  30.301 1.00 52.22 ? 29  VAL   A C     1 
ATOM   212  O  O     . VAL   A 1 32  ? 39.192 -4.130  29.189 1.00 57.85 ? 29  VAL   A O     1 
ATOM   213  C  CB    . VAL   A 1 32  ? 36.284 -4.893  29.961 1.00 50.07 ? 29  VAL   A CB    1 
ATOM   214  C  CG1   . VAL   A 1 32  ? 36.384 -4.801  28.453 1.00 50.55 ? 29  VAL   A CG1   1 
ATOM   215  C  CG2   . VAL   A 1 32  ? 36.225 -6.334  30.422 1.00 50.48 ? 29  VAL   A CG2   1 
ATOM   216  N  N     . GLU   A 1 40  ? 28.515 -11.240 29.314 1.00 49.89 ? 37  GLU   A N     1 
ATOM   217  C  CA    . GLU   A 1 40  ? 27.390 -11.656 28.438 1.00 46.64 ? 37  GLU   A CA    1 
ATOM   218  C  C     . GLU   A 1 40  ? 27.603 -11.085 27.036 1.00 40.83 ? 37  GLU   A C     1 
ATOM   219  O  O     . GLU   A 1 40  ? 28.471 -10.249 26.876 1.00 41.51 ? 37  GLU   A O     1 
ATOM   220  C  CB    . GLU   A 1 40  ? 26.054 -11.195 29.033 1.00 49.91 ? 37  GLU   A CB    1 
ATOM   221  C  CG    . GLU   A 1 40  ? 25.741 -11.827 30.377 0.00 50.37 ? 37  GLU   A CG    1 
ATOM   222  C  CD    . GLU   A 1 40  ? 25.510 -13.328 30.331 0.00 49.91 ? 37  GLU   A CD    1 
ATOM   223  O  OE1   . GLU   A 1 40  ? 25.189 -13.842 29.241 0.00 49.85 ? 37  GLU   A OE1   1 
ATOM   224  O  OE2   . GLU   A 1 40  ? 25.653 -13.979 31.385 0.00 49.71 ? 37  GLU   A OE2   1 
ATOM   225  N  N     . ASP   A 1 41  ? 26.873 -11.574 26.041 1.00 34.91 ? 38  ASP   A N     1 
ATOM   226  C  CA    . ASP   A 1 41  ? 27.066 -10.961 24.705 1.00 32.13 ? 38  ASP   A CA    1 
ATOM   227  C  C     . ASP   A 1 41  ? 25.904 -10.020 24.356 1.00 27.47 ? 38  ASP   A C     1 
ATOM   228  O  O     . ASP   A 1 41  ? 25.918 -9.494  23.295 1.00 29.69 ? 38  ASP   A O     1 
ATOM   229  C  CB    . ASP   A 1 41  ? 27.511 -11.959 23.645 1.00 40.38 ? 38  ASP   A CB    1 
ATOM   230  C  CG    . ASP   A 1 41  ? 26.825 -13.292 23.768 1.00 44.94 ? 38  ASP   A CG    1 
ATOM   231  O  OD1   . ASP   A 1 41  ? 25.827 -13.341 24.476 1.00 49.57 ? 38  ASP   A OD1   1 
ATOM   232  O  OD2   . ASP   A 1 41  ? 27.320 -14.246 23.175 1.00 48.58 ? 38  ASP   A OD2   1 
ATOM   233  N  N     . SER   A 1 42  ? 24.955 -9.815  25.255 1.00 28.66 ? 39  SER   A N     1 
ATOM   234  C  CA    . SER   A 1 42  ? 23.877 -8.841  24.952 1.00 29.52 ? 39  SER   A CA    1 
ATOM   235  C  C     . SER   A 1 42  ? 23.601 -8.005  26.181 1.00 29.09 ? 39  SER   A C     1 
ATOM   236  O  O     . SER   A 1 42  ? 23.758 -8.503  27.266 1.00 30.51 ? 39  SER   A O     1 
ATOM   237  C  CB    . SER   A 1 42  ? 22.639 -9.448  24.385 1.00 34.66 ? 39  SER   A CB    1 
ATOM   238  O  OG    . SER   A 1 42  ? 21.882 -10.045 25.398 1.00 39.37 ? 39  SER   A OG    1 
ATOM   239  N  N     . TYR   A 1 43  ? 23.345 -6.725  25.950 1.00 28.97 ? 40  TYR   A N     1 
ATOM   240  C  CA    . TYR   A 1 43  ? 23.174 -5.714  27.016 1.00 29.04 ? 40  TYR   A CA    1 
ATOM   241  C  C     . TYR   A 1 43  ? 22.001 -4.809  26.675 1.00 30.21 ? 40  TYR   A C     1 
ATOM   242  O  O     . TYR   A 1 43  ? 21.673 -4.701  25.527 1.00 30.70 ? 40  TYR   A O     1 
ATOM   243  C  CB    . TYR   A 1 43  ? 24.417 -4.835  27.111 1.00 33.07 ? 40  TYR   A CB    1 
ATOM   244  C  CG    . TYR   A 1 43  ? 25.699 -5.602  27.287 1.00 38.51 ? 40  TYR   A CG    1 
ATOM   245  C  CD1   . TYR   A 1 43  ? 26.384 -6.080  26.198 1.00 37.62 ? 40  TYR   A CD1   1 
ATOM   246  C  CD2   . TYR   A 1 43  ? 26.181 -5.911  28.535 1.00 42.01 ? 40  TYR   A CD2   1 
ATOM   247  C  CE1   . TYR   A 1 43  ? 27.532 -6.829  26.334 1.00 42.20 ? 40  TYR   A CE1   1 
ATOM   248  C  CE2   . TYR   A 1 43  ? 27.339 -6.643  28.694 1.00 43.77 ? 40  TYR   A CE2   1 
ATOM   249  C  CZ    . TYR   A 1 43  ? 28.022 -7.101  27.586 1.00 46.44 ? 40  TYR   A CZ    1 
ATOM   250  O  OH    . TYR   A 1 43  ? 29.176 -7.818  27.707 1.00 50.26 ? 40  TYR   A OH    1 
ATOM   251  N  N     . ARG   A 1 44  ? 21.422 -4.207  27.702 1.00 34.40 ? 41  ARG   A N     1 
ATOM   252  C  CA    . ARG   A 1 44  ? 20.258 -3.300  27.584 1.00 34.51 ? 41  ARG   A CA    1 
ATOM   253  C  C     . ARG   A 1 44  ? 20.534 -2.013  28.351 1.00 32.93 ? 41  ARG   A C     1 
ATOM   254  O  O     . ARG   A 1 44  ? 21.113 -2.076  29.397 1.00 35.39 ? 41  ARG   A O     1 
ATOM   255  C  CB    . ARG   A 1 44  ? 18.998 -4.057  27.995 1.00 40.65 ? 41  ARG   A CB    1 
ATOM   256  C  CG    . ARG   A 1 44  ? 18.473 -4.918  26.864 1.00 45.34 ? 41  ARG   A CG    1 
ATOM   257  C  CD    . ARG   A 1 44  ? 17.786 -6.193  27.243 1.00 51.88 ? 41  ARG   A CD    1 
ATOM   258  N  NE    . ARG   A 1 44  ? 18.715 -7.192  27.730 1.00 56.58 ? 41  ARG   A NE    1 
ATOM   259  C  CZ    . ARG   A 1 44  ? 19.335 -8.083  26.974 1.00 56.70 ? 41  ARG   A CZ    1 
ATOM   260  N  NH1   . ARG   A 1 44  ? 19.148 -8.091  25.668 1.00 53.58 ? 41  ARG   A NH1   1 
ATOM   261  N  NH2   . ARG   A 1 44  ? 20.152 -8.958  27.526 1.00 57.68 ? 41  ARG   A NH2   1 
ATOM   262  N  N     . LYS   A 1 45  ? 20.110 -0.886  27.798 1.00 31.63 ? 42  LYS   A N     1 
ATOM   263  C  CA    . LYS   A 1 45  ? 20.320 0.425   28.431 1.00 33.53 ? 42  LYS   A CA    1 
ATOM   264  C  C     . LYS   A 1 45  ? 19.265 1.399   27.915 1.00 30.56 ? 42  LYS   A C     1 
ATOM   265  O  O     . LYS   A 1 45  ? 19.136 1.555   26.736 1.00 33.83 ? 42  LYS   A O     1 
ATOM   266  C  CB    . LYS   A 1 45  ? 21.704 0.964   28.084 1.00 34.70 ? 42  LYS   A CB    1 
ATOM   267  C  CG    . LYS   A 1 45  ? 22.147 2.213   28.822 1.00 39.38 ? 42  LYS   A CG    1 
ATOM   268  C  CD    . LYS   A 1 45  ? 23.534 2.674   28.428 1.00 42.27 ? 42  LYS   A CD    1 
ATOM   269  C  CE    . LYS   A 1 45  ? 24.047 3.931   29.097 1.00 47.61 ? 42  LYS   A CE    1 
ATOM   270  N  NZ    . LYS   A 1 45  ? 24.662 3.696   30.416 1.00 51.02 ? 42  LYS   A NZ    1 
ATOM   271  N  N     . GLN   A 1 46  ? 18.542 2.026   28.827 1.00 33.98 ? 43  GLN   A N     1 
ATOM   272  C  CA    . GLN   A 1 46  ? 17.540 3.017   28.423 1.00 35.03 ? 43  GLN   A CA    1 
ATOM   273  C  C     . GLN   A 1 46  ? 18.232 4.366   28.370 1.00 36.33 ? 43  GLN   A C     1 
ATOM   274  O  O     . GLN   A 1 46  ? 18.903 4.706   29.307 1.00 39.34 ? 43  GLN   A O     1 
ATOM   275  C  CB    . GLN   A 1 46  ? 16.382 3.044   29.420 1.00 36.27 ? 43  GLN   A CB    1 
ATOM   276  C  CG    . GLN   A 1 46  ? 15.212 3.872   28.942 1.00 38.58 ? 43  GLN   A CG    1 
ATOM   277  C  CD    . GLN   A 1 46  ? 14.131 3.930   29.980 1.00 39.86 ? 43  GLN   A CD    1 
ATOM   278  O  OE1   . GLN   A 1 46  ? 13.512 2.951   30.290 1.00 41.94 ? 43  GLN   A OE1   1 
ATOM   279  N  NE2   . GLN   A 1 46  ? 13.908 5.104   30.505 1.00 45.77 ? 43  GLN   A NE2   1 
ATOM   280  N  N     . VAL   A 1 47  ? 18.055 5.088   27.283 1.00 34.79 ? 44  VAL   A N     1 
ATOM   281  C  CA    . VAL   A 1 47  ? 18.712 6.408   27.145 1.00 40.13 ? 44  VAL   A CA    1 
ATOM   282  C  C     . VAL   A 1 47  ? 17.717 7.388   26.530 1.00 37.22 ? 44  VAL   A C     1 
ATOM   283  O  O     . VAL   A 1 47  ? 16.747 6.954   25.958 1.00 41.08 ? 44  VAL   A O     1 
ATOM   284  C  CB    . VAL   A 1 47  ? 19.962 6.351   26.252 1.00 41.43 ? 44  VAL   A CB    1 
ATOM   285  C  CG1   . VAL   A 1 47  ? 21.143 5.630   26.869 1.00 41.67 ? 44  VAL   A CG1   1 
ATOM   286  C  CG2   . VAL   A 1 47  ? 19.645 5.791   24.882 1.00 42.20 ? 44  VAL   A CG2   1 
ATOM   287  N  N     . VAL   A 1 48  ? 18.008 8.666   26.678 1.00 42.40 ? 45  VAL   A N     1 
ATOM   288  C  CA    . VAL   A 1 48  ? 17.241 9.785   26.067 1.00 42.86 ? 45  VAL   A CA    1 
ATOM   289  C  C     . VAL   A 1 48  ? 18.127 10.388  24.972 1.00 44.52 ? 45  VAL   A C     1 
ATOM   290  O  O     . VAL   A 1 48  ? 19.236 10.854  25.298 1.00 47.31 ? 45  VAL   A O     1 
ATOM   291  C  CB    . VAL   A 1 48  ? 16.847 10.831  27.127 1.00 46.86 ? 45  VAL   A CB    1 
ATOM   292  C  CG1   . VAL   A 1 48  ? 16.112 12.005  26.504 1.00 50.83 ? 45  VAL   A CG1   1 
ATOM   293  C  CG2   . VAL   A 1 48  ? 16.025 10.214  28.240 1.00 49.52 ? 45  VAL   A CG2   1 
ATOM   294  N  N     . ILE   A 1 49  ? 17.671 10.319  23.727 1.00 44.55 ? 46  ILE   A N     1 
ATOM   295  C  CA    . ILE   A 1 49  ? 18.385 10.909  22.555 1.00 45.60 ? 46  ILE   A CA    1 
ATOM   296  C  C     . ILE   A 1 49  ? 17.418 11.879  21.870 1.00 45.17 ? 46  ILE   A C     1 
ATOM   297  O  O     . ILE   A 1 49  ? 16.338 11.463  21.496 1.00 43.47 ? 46  ILE   A O     1 
ATOM   298  C  CB    . ILE   A 1 49  ? 18.864 9.810   21.593 1.00 44.28 ? 46  ILE   A CB    1 
ATOM   299  C  CG1   . ILE   A 1 49  ? 19.792 8.824   22.298 1.00 45.05 ? 46  ILE   A CG1   1 
ATOM   300  C  CG2   . ILE   A 1 49  ? 19.536 10.422  20.375 1.00 44.19 ? 46  ILE   A CG2   1 
ATOM   301  C  CD1   . ILE   A 1 49  ? 20.209 7.667   21.466 1.00 44.36 ? 46  ILE   A CD1   1 
ATOM   302  N  N     . ASP   A 1 50  ? 17.780 13.148  21.807 1.00 46.46 ? 47  ASP   A N     1 
ATOM   303  C  CA    . ASP   A 1 50  ? 16.952 14.204  21.165 1.00 45.97 ? 47  ASP   A CA    1 
ATOM   304  C  C     . ASP   A 1 50  ? 15.528 14.214  21.747 1.00 46.20 ? 47  ASP   A C     1 
ATOM   305  O  O     . ASP   A 1 50  ? 14.599 14.257  20.971 1.00 40.92 ? 47  ASP   A O     1 
ATOM   306  C  CB    . ASP   A 1 50  ? 17.006 14.097  19.637 1.00 42.56 ? 47  ASP   A CB    1 
ATOM   307  C  CG    . ASP   A 1 50  ? 18.407 14.243  19.060 1.00 43.40 ? 47  ASP   A CG    1 
ATOM   308  O  OD1   . ASP   A 1 50  ? 19.120 15.146  19.494 1.00 47.00 ? 47  ASP   A OD1   1 
ATOM   309  O  OD2   . ASP   A 1 50  ? 18.758 13.450  18.179 1.00 43.87 ? 47  ASP   A OD2   1 
ATOM   310  N  N     . GLY   A 1 51  ? 15.405 14.141  23.074 1.00 48.79 ? 48  GLY   A N     1 
ATOM   311  C  CA    . GLY   A 1 51  ? 14.109 14.222  23.772 1.00 46.72 ? 48  GLY   A CA    1 
ATOM   312  C  C     . GLY   A 1 51  ? 13.273 12.980  23.621 1.00 42.49 ? 48  GLY   A C     1 
ATOM   313  O  O     . GLY   A 1 51  ? 12.132 12.984  24.074 1.00 45.77 ? 48  GLY   A O     1 
ATOM   314  N  N     . GLU   A 1 52  ? 13.834 11.936  23.036 1.00 41.51 ? 49  GLU   A N     1 
ATOM   315  C  CA    . GLU   A 1 52  ? 13.022 10.716  22.870 1.00 41.36 ? 49  GLU   A CA    1 
ATOM   316  C  C     . GLU   A 1 52  ? 13.666 9.601   23.681 1.00 42.70 ? 49  GLU   A C     1 
ATOM   317  O  O     . GLU   A 1 52  ? 14.860 9.374   23.529 1.00 45.30 ? 49  GLU   A O     1 
ATOM   318  C  CB    . GLU   A 1 52  ? 12.831 10.377  21.398 1.00 43.35 ? 49  GLU   A CB    1 
ATOM   319  C  CG    . GLU   A 1 52  ? 12.038 9.113   21.191 1.00 48.23 ? 49  GLU   A CG    1 
ATOM   320  C  CD    . GLU   A 1 52  ? 11.646 8.790   19.762 1.00 53.05 ? 49  GLU   A CD    1 
ATOM   321  O  OE1   . GLU   A 1 52  ? 12.246 9.346   18.849 1.00 59.29 ? 49  GLU   A OE1   1 
ATOM   322  O  OE2   . GLU   A 1 52  ? 10.733 7.982   19.578 1.00 62.14 ? 49  GLU   A OE2   1 
ATOM   323  N  N     . THR   A 1 53  ? 12.853 8.930   24.481 1.00 41.28 ? 50  THR   A N     1 
ATOM   324  C  CA    . THR   A 1 53  ? 13.309 7.823   25.335 1.00 43.43 ? 50  THR   A CA    1 
ATOM   325  C  C     . THR   A 1 53  ? 13.347 6.575   24.478 1.00 42.17 ? 50  THR   A C     1 
ATOM   326  O  O     . THR   A 1 53  ? 12.413 6.349   23.741 1.00 43.70 ? 50  THR   A O     1 
ATOM   327  C  CB    . THR   A 1 53  ? 12.351 7.627   26.513 1.00 44.90 ? 50  THR   A CB    1 
ATOM   328  O  OG1   . THR   A 1 53  ? 12.447 8.831   27.255 1.00 48.63 ? 50  THR   A OG1   1 
ATOM   329  C  CG2   . THR   A 1 53  ? 12.707 6.461   27.396 1.00 49.41 ? 50  THR   A CG2   1 
ATOM   330  N  N     . CYS   A 1 54  ? 14.406 5.791   24.620 1.00 39.61 ? 51  CYS   A N     1 
ATOM   331  C  CA    . CYS   A 1 54  ? 14.442 4.521   23.880 1.00 40.14 ? 51  CYS   A CA    1 
ATOM   332  C  C     . CYS   A 1 54  ? 15.294 3.523   24.646 1.00 35.79 ? 51  CYS   A C     1 
ATOM   333  O  O     . CYS   A 1 54  ? 16.051 3.918   25.503 1.00 38.04 ? 51  CYS   A O     1 
ATOM   334  C  CB    . CYS   A 1 54  ? 14.994 4.692   22.484 1.00 42.32 ? 51  CYS   A CB    1 
ATOM   335  S  SG    . CYS   A 1 54  ? 16.665 5.357   22.514 1.00 42.89 ? 51  CYS   A SG    1 
ATOM   336  N  N     . LEU   A 1 55  ? 15.065 2.274   24.341 1.00 32.67 ? 52  LEU   A N     1 
ATOM   337  C  CA    . LEU   A 1 55  ? 15.787 1.181   25.004 1.00 34.81 ? 52  LEU   A CA    1 
ATOM   338  C  C     . LEU   A 1 55  ? 16.748 0.631   23.962 1.00 33.18 ? 52  LEU   A C     1 
ATOM   339  O  O     . LEU   A 1 55  ? 16.286 0.246   22.912 1.00 31.70 ? 52  LEU   A O     1 
ATOM   340  C  CB    . LEU   A 1 55  ? 14.741 0.135   25.364 1.00 40.07 ? 52  LEU   A CB    1 
ATOM   341  C  CG    . LEU   A 1 55  ? 15.230 -1.095  26.105 1.00 43.04 ? 52  LEU   A CG    1 
ATOM   342  C  CD1   . LEU   A 1 55  ? 15.819 -0.724  27.437 1.00 44.77 ? 52  LEU   A CD1   1 
ATOM   343  C  CD2   . LEU   A 1 55  ? 14.072 -2.037  26.304 1.00 48.82 ? 52  LEU   A CD2   1 
ATOM   344  N  N     . LEU   A 1 56  ? 18.037 0.679   24.262 1.00 32.90 ? 53  LEU   A N     1 
ATOM   345  C  CA    . LEU   A 1 56  ? 19.046 0.118   23.340 1.00 30.07 ? 53  LEU   A CA    1 
ATOM   346  C  C     . LEU   A 1 56  ? 19.254 -1.332  23.730 1.00 27.99 ? 53  LEU   A C     1 
ATOM   347  O  O     . LEU   A 1 56  ? 19.465 -1.571  24.873 1.00 30.96 ? 53  LEU   A O     1 
ATOM   348  C  CB    . LEU   A 1 56  ? 20.354 0.887   23.491 1.00 30.62 ? 53  LEU   A CB    1 
ATOM   349  C  CG    . LEU   A 1 56  ? 20.310 2.386   23.250 1.00 33.76 ? 53  LEU   A CG    1 
ATOM   350  C  CD1   . LEU   A 1 56  ? 21.702 2.958   23.159 1.00 34.66 ? 53  LEU   A CD1   1 
ATOM   351  C  CD2   . LEU   A 1 56  ? 19.513 2.730   22.017 1.00 33.62 ? 53  LEU   A CD2   1 
ATOM   352  N  N     . ASP   A 1 57  ? 19.126 -2.241  22.783 1.00 28.44 ? 54  ASP   A N     1 
ATOM   353  C  CA    . ASP   A 1 57  ? 19.350 -3.684  22.995 1.00 27.90 ? 54  ASP   A CA    1 
ATOM   354  C  C     . ASP   A 1 57  ? 20.573 -4.018  22.145 1.00 26.18 ? 54  ASP   A C     1 
ATOM   355  O  O     . ASP   A 1 57  ? 20.418 -4.095  20.951 1.00 25.55 ? 54  ASP   A O     1 
ATOM   356  C  CB    . ASP   A 1 57  ? 18.094 -4.429  22.577 1.00 30.97 ? 54  ASP   A CB    1 
ATOM   357  C  CG    . ASP   A 1 57  ? 18.116 -5.899  22.884 1.00 35.31 ? 54  ASP   A CG    1 
ATOM   358  O  OD1   . ASP   A 1 57  ? 19.118 -6.363  23.377 1.00 34.85 ? 54  ASP   A OD1   1 
ATOM   359  O  OD2   . ASP   A 1 57  ? 17.126 -6.558  22.597 1.00 42.89 ? 54  ASP   A OD2   1 
ATOM   360  N  N     . ILE   A 1 58  ? 21.711 -4.260  22.783 1.00 24.32 ? 55  ILE   A N     1 
ATOM   361  C  CA    . ILE   A 1 58  ? 22.994 -4.357  22.031 1.00 22.90 ? 55  ILE   A CA    1 
ATOM   362  C  C     . ILE   A 1 58  ? 23.544 -5.779  22.007 1.00 21.06 ? 55  ILE   A C     1 
ATOM   363  O  O     . ILE   A 1 58  ? 23.661 -6.370  23.050 1.00 25.00 ? 55  ILE   A O     1 
ATOM   364  C  CB    . ILE   A 1 58  ? 23.994 -3.362  22.640 1.00 23.94 ? 55  ILE   A CB    1 
ATOM   365  C  CG1   . ILE   A 1 58  ? 23.434 -1.939  22.607 1.00 25.85 ? 55  ILE   A CG1   1 
ATOM   366  C  CG2   . ILE   A 1 58  ? 25.310 -3.452  21.919 1.00 24.60 ? 55  ILE   A CG2   1 
ATOM   367  C  CD1   . ILE   A 1 58  ? 24.206 -0.945  23.381 1.00 27.24 ? 55  ILE   A CD1   1 
ATOM   368  N  N     . LEU   A 1 59  ? 23.860 -6.254  20.810 1.00 21.24 ? 56  LEU   A N     1 
ATOM   369  C  CA    . LEU   A 1 59  ? 24.470 -7.590  20.624 1.00 22.98 ? 56  LEU   A CA    1 
ATOM   370  C  C     . LEU   A 1 59  ? 25.969 -7.455  20.307 1.00 22.96 ? 56  LEU   A C     1 
ATOM   371  O  O     . LEU   A 1 59  ? 26.307 -6.813  19.361 1.00 22.23 ? 56  LEU   A O     1 
ATOM   372  C  CB    . LEU   A 1 59  ? 23.757 -8.356  19.511 1.00 24.85 ? 56  LEU   A CB    1 
ATOM   373  C  CG    . LEU   A 1 59  ? 24.283 -9.766  19.256 1.00 24.40 ? 56  LEU   A CG    1 
ATOM   374  C  CD1   . LEU   A 1 59  ? 23.954 -10.698 20.404 1.00 25.22 ? 56  LEU   A CD1   1 
ATOM   375  C  CD2   . LEU   A 1 59  ? 23.747 -10.317 17.964 1.00 25.13 ? 56  LEU   A CD2   1 
ATOM   376  N  N     . ASP   A 1 60  ? 26.796 -8.148  21.078 1.00 24.22 ? 57  ASP   A N     1 
ATOM   377  C  CA    . ASP   A 1 60  ? 28.269 -8.211  20.891 1.00 25.92 ? 57  ASP   A CA    1 
ATOM   378  C  C     . ASP   A 1 60  ? 28.556 -9.499  20.102 1.00 25.45 ? 57  ASP   A C     1 
ATOM   379  O  O     . ASP   A 1 60  ? 28.112 -10.537 20.521 1.00 34.72 ? 57  ASP   A O     1 
ATOM   380  C  CB    . ASP   A 1 60  ? 28.934 -8.116  22.262 1.00 27.52 ? 57  ASP   A CB    1 
ATOM   381  C  CG    . ASP   A 1 60  ? 30.449 -8.069  22.236 1.00 28.85 ? 57  ASP   A CG    1 
ATOM   382  O  OD1   . ASP   A 1 60  ? 30.986 -7.709  21.216 1.00 29.68 ? 57  ASP   A OD1   1 
ATOM   383  O  OD2   . ASP   A 1 60  ? 31.045 -8.399  23.241 1.00 32.43 ? 57  ASP   A OD2   1 
ATOM   384  N  N     . THR   A 1 61  ? 29.253 -9.410  18.986 1.00 25.35 ? 58  THR   A N     1 
ATOM   385  C  CA    . THR   A 1 61  ? 29.462 -10.596 18.136 1.00 24.45 ? 58  THR   A CA    1 
ATOM   386  C  C     . THR   A 1 61  ? 30.924 -11.041 18.111 1.00 26.32 ? 58  THR   A C     1 
ATOM   387  O  O     . THR   A 1 61  ? 31.752 -10.410 18.712 1.00 27.49 ? 58  THR   A O     1 
ATOM   388  C  CB    . THR   A 1 61  ? 29.022 -10.256 16.709 1.00 23.76 ? 58  THR   A CB    1 
ATOM   389  O  OG1   . THR   A 1 61  ? 29.871 -9.223  16.223 1.00 24.30 ? 58  THR   A OG1   1 
ATOM   390  C  CG2   . THR   A 1 61  ? 27.595 -9.774  16.654 1.00 23.55 ? 58  THR   A CG2   1 
ATOM   391  N  N     . ALA   A 1 62  ? 31.176 -12.108 17.380 1.00 26.85 ? 59  ALA   A N     1 
ATOM   392  C  CA    . ALA   A 1 62  ? 32.553 -12.589 17.196 1.00 28.82 ? 59  ALA   A CA    1 
ATOM   393  C  C     . ALA   A 1 62  ? 33.025 -12.147 15.818 1.00 29.59 ? 59  ALA   A C     1 
ATOM   394  O  O     . ALA   A 1 62  ? 32.221 -11.939 14.966 1.00 31.15 ? 59  ALA   A O     1 
ATOM   395  C  CB    . ALA   A 1 62  ? 32.599 -14.089 17.300 1.00 31.29 ? 59  ALA   A CB    1 
ATOM   396  N  N     . GLY   A 1 63  ? 34.333 -12.138 15.568 1.00 32.44 ? 60  GLY   A N     1 
ATOM   397  C  CA    . GLY   A 1 63  ? 34.833 -11.828 14.215 1.00 34.06 ? 60  GLY   A CA    1 
ATOM   398  C  C     . GLY   A 1 63  ? 34.527 -12.910 13.179 1.00 38.41 ? 60  GLY   A C     1 
ATOM   399  O  O     . GLY   A 1 63  ? 34.158 -14.034 13.531 1.00 41.23 ? 60  GLY   A O     1 
ATOM   400  N  N     . MET   A 1 70  ? 24.393 -18.065 14.362 1.00 34.74 ? 67  MET   A N     1 
ATOM   401  C  CA    . MET   A 1 70  ? 23.326 -17.048 14.399 1.00 35.27 ? 67  MET   A CA    1 
ATOM   402  C  C     . MET   A 1 70  ? 23.655 -15.824 13.511 1.00 33.97 ? 67  MET   A C     1 
ATOM   403  O  O     . MET   A 1 70  ? 22.864 -14.912 13.524 1.00 33.23 ? 67  MET   A O     1 
ATOM   404  C  CB    . MET   A 1 70  ? 23.063 -16.649 15.849 1.00 39.94 ? 67  MET   A CB    1 
ATOM   405  C  CG    . MET   A 1 70  ? 22.592 -17.807 16.713 1.00 42.32 ? 67  MET   A CG    1 
ATOM   406  S  SD    . MET   A 1 70  ? 21.154 -18.697 16.054 1.00 51.90 ? 67  MET   A SD    1 
ATOM   407  C  CE    . MET   A 1 70  ? 19.841 -17.491 16.208 1.00 50.14 ? 67  MET   A CE    1 
ATOM   408  N  N     . ARG   A 1 71  ? 24.741 -15.848 12.735 1.00 32.72 ? 68  ARG   A N     1 
ATOM   409  C  CA    . ARG   A 1 71  ? 25.202 -14.683 11.909 1.00 31.13 ? 68  ARG   A CA    1 
ATOM   410  C  C     . ARG   A 1 71  ? 24.110 -14.120 11.002 1.00 28.40 ? 68  ARG   A C     1 
ATOM   411  O  O     . ARG   A 1 71  ? 23.838 -12.957 11.076 1.00 27.27 ? 68  ARG   A O     1 
ATOM   412  C  CB    . ARG   A 1 71  ? 26.409 -15.039 11.044 1.00 35.01 ? 68  ARG   A CB    1 
ATOM   413  C  CG    . ARG   A 1 71  ? 27.079 -13.835 10.401 1.00 42.19 ? 68  ARG   A CG    1 
ATOM   414  C  CD    . ARG   A 1 71  ? 28.148 -14.098 9.350  1.00 48.14 ? 68  ARG   A CD    1 
ATOM   415  N  NE    . ARG   A 1 71  ? 27.679 -14.920 8.249  1.00 55.72 ? 68  ARG   A NE    1 
ATOM   416  C  CZ    . ARG   A 1 71  ? 28.458 -15.511 7.357  1.00 57.15 ? 68  ARG   A CZ    1 
ATOM   417  N  NH1   . ARG   A 1 71  ? 29.767 -15.359 7.412  1.00 58.17 ? 68  ARG   A NH1   1 
ATOM   418  N  NH2   . ARG   A 1 71  ? 27.926 -16.265 6.419  1.00 61.36 ? 68  ARG   A NH2   1 
ATOM   419  N  N     . ASP   A 1 72  ? 23.507 -14.944 10.165 1.00 31.52 ? 69  ASP   A N     1 
ATOM   420  C  CA    . ASP   A 1 72  ? 22.454 -14.423 9.274  1.00 33.49 ? 69  ASP   A CA    1 
ATOM   421  C  C     . ASP   A 1 72  ? 21.260 -13.950 10.100 1.00 31.03 ? 69  ASP   A C     1 
ATOM   422  O  O     . ASP   A 1 72  ? 20.673 -12.976 9.710  1.00 30.12 ? 69  ASP   A O     1 
ATOM   423  C  CB    . ASP   A 1 72  ? 22.038 -15.451 8.233  1.00 39.22 ? 69  ASP   A CB    1 
ATOM   424  C  CG    . ASP   A 1 72  ? 23.001 -15.503 7.072  1.00 40.10 ? 69  ASP   A CG    1 
ATOM   425  O  OD1   . ASP   A 1 72  ? 24.151 -15.113 7.258  1.00 43.53 ? 69  ASP   A OD1   1 
ATOM   426  O  OD2   . ASP   A 1 72  ? 22.579 -15.906 5.990  1.00 50.92 ? 69  ASP   A OD2   1 
ATOM   427  N  N     . GLN   A 1 73  ? 20.978 -14.591 11.230 1.00 30.82 ? 70  GLN   A N     1 
ATOM   428  C  CA    . GLN   A 1 73  ? 19.833 -14.178 12.071 1.00 30.35 ? 70  GLN   A CA    1 
ATOM   429  C  C     . GLN   A 1 73  ? 20.104 -12.806 12.677 1.00 29.01 ? 70  GLN   A C     1 
ATOM   430  O  O     . GLN   A 1 73  ? 19.255 -11.981 12.565 1.00 29.46 ? 70  GLN   A O     1 
ATOM   431  C  CB    . GLN   A 1 73  ? 19.508 -15.201 13.156 1.00 31.67 ? 70  GLN   A CB    1 
ATOM   432  C  CG    . GLN   A 1 73  ? 18.311 -14.808 14.006 1.00 34.43 ? 70  GLN   A CG    1 
ATOM   433  C  CD    . GLN   A 1 73  ? 17.048 -14.580 13.208 1.00 33.36 ? 70  GLN   A CD    1 
ATOM   434  O  OE1   . GLN   A 1 73  ? 16.722 -15.335 12.312 1.00 34.48 ? 70  GLN   A OE1   1 
ATOM   435  N  NE2   . GLN   A 1 73  ? 16.340 -13.519 13.517 1.00 32.82 ? 70  GLN   A NE2   1 
ATOM   436  N  N     . TYR   A 1 74  ? 21.262 -12.586 13.300 1.00 26.04 ? 71  TYR   A N     1 
ATOM   437  C  CA    . TYR   A 1 74  ? 21.493 -11.236 13.870 1.00 23.96 ? 71  TYR   A CA    1 
ATOM   438  C  C     . TYR   A 1 74  ? 21.580 -10.177 12.778 1.00 21.95 ? 71  TYR   A C     1 
ATOM   439  O  O     . TYR   A 1 74  ? 21.238 -9.071  13.055 1.00 24.15 ? 71  TYR   A O     1 
ATOM   440  C  CB    . TYR   A 1 74  ? 22.532 -11.193 14.985 1.00 25.24 ? 71  TYR   A CB    1 
ATOM   441  C  CG    . TYR   A 1 74  ? 23.959 -11.452 14.603 1.00 26.60 ? 71  TYR   A CG    1 
ATOM   442  C  CD1   . TYR   A 1 74  ? 24.648 -10.606 13.760 1.00 26.02 ? 71  TYR   A CD1   1 
ATOM   443  C  CD2   . TYR   A 1 74  ? 24.636 -12.516 15.152 1.00 27.46 ? 71  TYR   A CD2   1 
ATOM   444  C  CE1   . TYR   A 1 74  ? 25.969 -10.827 13.442 1.00 26.30 ? 71  TYR   A CE1   1 
ATOM   445  C  CE2   . TYR   A 1 74  ? 25.959 -12.760 14.849 1.00 28.61 ? 71  TYR   A CE2   1 
ATOM   446  C  CZ    . TYR   A 1 74  ? 26.630 -11.904 13.997 1.00 29.25 ? 71  TYR   A CZ    1 
ATOM   447  O  OH    . TYR   A 1 74  ? 27.932 -12.131 13.703 1.00 31.48 ? 71  TYR   A OH    1 
ATOM   448  N  N     . MET   A 1 75  ? 22.127 -10.503 11.628 1.00 24.19 ? 72  MET   A N     1 
ATOM   449  C  CA    . MET   A 1 75  ? 22.149 -9.500  10.549 1.00 25.29 ? 72  MET   A CA    1 
ATOM   450  C  C     . MET   A 1 75  ? 20.719 -9.185  10.084 1.00 28.53 ? 72  MET   A C     1 
ATOM   451  O  O     . MET   A 1 75  ? 20.476 -8.071  9.711  1.00 31.67 ? 72  MET   A O     1 
ATOM   452  C  CB    . MET   A 1 75  ? 23.083 -9.910  9.414  1.00 26.83 ? 72  MET   A CB    1 
ATOM   453  C  CG    . MET   A 1 75  ? 24.516 -9.947  9.874  1.00 25.77 ? 72  MET   A CG    1 
ATOM   454  S  SD    . MET   A 1 75  ? 25.650 -10.321 8.543  1.00 27.98 ? 72  MET   A SD    1 
ATOM   455  C  CE    . MET   A 1 75  ? 27.223 -9.985  9.328  1.00 29.31 ? 72  MET   A CE    1 
ATOM   456  N  N     . ARG   A 1 76  ? 19.813 -10.159 10.111 1.00 29.74 ? 73  ARG   A N     1 
ATOM   457  C  CA    . ARG   A 1 76  ? 18.394 -9.890  9.779  1.00 33.27 ? 73  ARG   A CA    1 
ATOM   458  C  C     . ARG   A 1 76  ? 17.687 -9.087  10.891 1.00 30.21 ? 73  ARG   A C     1 
ATOM   459  O  O     . ARG   A 1 76  ? 17.005 -8.137  10.580 1.00 34.52 ? 73  ARG   A O     1 
ATOM   460  C  CB    . ARG   A 1 76  ? 17.758 -11.242 9.465  1.00 35.29 ? 73  ARG   A CB    1 
ATOM   461  C  CG    . ARG   A 1 76  ? 16.582 -11.187 8.506  1.00 44.19 ? 73  ARG   A CG    1 
ATOM   462  C  CD    . ARG   A 1 76  ? 16.179 -12.582 8.038  1.00 49.54 ? 73  ARG   A CD    1 
ATOM   463  N  NE    . ARG   A 1 76  ? 16.990 -13.125 6.957  1.00 56.71 ? 73  ARG   A NE    1 
ATOM   464  C  CZ    . ARG   A 1 76  ? 17.819 -14.159 7.064  1.00 56.61 ? 73  ARG   A CZ    1 
ATOM   465  N  NH1   . ARG   A 1 76  ? 18.490 -14.576 6.008  1.00 58.90 ? 73  ARG   A NH1   1 
ATOM   466  N  NH2   . ARG   A 1 76  ? 17.970 -14.765 8.222  1.00 54.28 ? 73  ARG   A NH2   1 
ATOM   467  N  N     . THR   A 1 77  ? 17.895 -9.436  12.147 1.00 30.36 ? 74  THR   A N     1 
ATOM   468  C  CA    . THR   A 1 77  ? 17.238 -8.775  13.296 1.00 29.05 ? 74  THR   A CA    1 
ATOM   469  C  C     . THR   A 1 77  ? 17.829 -7.398  13.621 1.00 26.27 ? 74  THR   A C     1 
ATOM   470  O  O     . THR   A 1 77  ? 17.094 -6.559  14.116 1.00 26.16 ? 74  THR   A O     1 
ATOM   471  C  CB    . THR   A 1 77  ? 17.336 -9.669  14.528 1.00 30.75 ? 74  THR   A CB    1 
ATOM   472  O  OG1   . THR   A 1 77  ? 16.498 -10.778 14.237 1.00 34.16 ? 74  THR   A OG1   1 
ATOM   473  C  CG2   . THR   A 1 77  ? 16.857 -8.988  15.784 1.00 31.84 ? 74  THR   A CG2   1 
ATOM   474  N  N     . GLY   A 1 78  ? 19.131 -7.225  13.404 1.00 22.25 ? 75  GLY   A N     1 
ATOM   475  C  CA    . GLY   A 1 78  ? 19.777 -5.955  13.743 1.00 23.71 ? 75  GLY   A CA    1 
ATOM   476  C  C     . GLY   A 1 78  ? 19.187 -4.784  12.990 1.00 21.74 ? 75  GLY   A C     1 
ATOM   477  O  O     . GLY   A 1 78  ? 19.056 -4.864  11.795 1.00 24.37 ? 75  GLY   A O     1 
ATOM   478  N  N     . GLU   A 1 79  ? 18.945 -3.695  13.694 1.00 21.31 ? 76  GLU   A N     1 
ATOM   479  C  CA    . GLU   A 1 79  ? 18.395 -2.505  13.011 1.00 23.55 ? 76  GLU   A CA    1 
ATOM   480  C  C     . GLU   A 1 79  ? 19.508 -1.549  12.593 1.00 22.56 ? 76  GLU   A C     1 
ATOM   481  O  O     . GLU   A 1 79  ? 19.292 -0.812  11.672 1.00 24.67 ? 76  GLU   A O     1 
ATOM   482  C  CB    . GLU   A 1 79  ? 17.380 -1.817  13.912 1.00 25.70 ? 76  GLU   A CB    1 
ATOM   483  C  CG    . GLU   A 1 79  ? 16.175 -2.698  14.089 1.00 28.53 ? 76  GLU   A CG    1 
ATOM   484  C  CD    . GLU   A 1 79  ? 15.233 -2.433  15.235 1.00 32.16 ? 76  GLU   A CD    1 
ATOM   485  O  OE1   . GLU   A 1 79  ? 15.607 -1.819  16.171 1.00 32.52 ? 76  GLU   A OE1   1 
ATOM   486  O  OE2   . GLU   A 1 79  ? 14.097 -2.862  15.123 1.00 42.04 ? 76  GLU   A OE2   1 
ATOM   487  N  N     . GLY   A 1 80  ? 20.653 -1.629  13.274 1.00 21.20 ? 77  GLY   A N     1 
ATOM   488  C  CA    . GLY   A 1 80  ? 21.813 -0.758  13.024 1.00 22.14 ? 77  GLY   A CA    1 
ATOM   489  C  C     . GLY   A 1 80  ? 23.087 -1.479  13.397 1.00 20.63 ? 77  GLY   A C     1 
ATOM   490  O  O     . GLY   A 1 80  ? 23.058 -2.241  14.306 1.00 19.37 ? 77  GLY   A O     1 
ATOM   491  N  N     . PHE   A 1 81  ? 24.147 -1.242  12.648 1.00 18.82 ? 78  PHE   A N     1 
ATOM   492  C  CA    . PHE   A 1 81  ? 25.420 -1.957  12.893 1.00 17.74 ? 78  PHE   A CA    1 
ATOM   493  C  C     . PHE   A 1 81  ? 26.579 -0.994  13.148 1.00 19.28 ? 78  PHE   A C     1 
ATOM   494  O  O     . PHE   A 1 81  ? 26.745 -0.059  12.397 1.00 18.90 ? 78  PHE   A O     1 
ATOM   495  C  CB    . PHE   A 1 81  ? 25.721 -2.839  11.680 1.00 18.59 ? 78  PHE   A CB    1 
ATOM   496  C  CG    . PHE   A 1 81  ? 24.649 -3.866  11.444 1.00 19.46 ? 78  PHE   A CG    1 
ATOM   497  C  CD1   . PHE   A 1 81  ? 23.492 -3.540  10.764 1.00 19.57 ? 78  PHE   A CD1   1 
ATOM   498  C  CD2   . PHE   A 1 81  ? 24.768 -5.127  11.981 1.00 19.58 ? 78  PHE   A CD2   1 
ATOM   499  C  CE1   . PHE   A 1 81  ? 22.483 -4.467  10.617 1.00 21.15 ? 78  PHE   A CE1   1 
ATOM   500  C  CE2   . PHE   A 1 81  ? 23.759 -6.054  11.829 1.00 19.66 ? 78  PHE   A CE2   1 
ATOM   501  C  CZ    . PHE   A 1 81  ? 22.615 -5.713  11.159 1.00 21.06 ? 78  PHE   A CZ    1 
ATOM   502  N  N     . LEU   A 1 82  ? 27.316 -1.251  14.223 1.00 18.23 ? 79  LEU   A N     1 
ATOM   503  C  CA    . LEU   A 1 82  ? 28.583 -0.526  14.458 1.00 18.99 ? 79  LEU   A CA    1 
ATOM   504  C  C     . LEU   A 1 82  ? 29.652 -1.406  13.818 1.00 19.83 ? 79  LEU   A C     1 
ATOM   505  O  O     . LEU   A 1 82  ? 29.866 -2.472  14.299 1.00 20.21 ? 79  LEU   A O     1 
ATOM   506  C  CB    . LEU   A 1 82  ? 28.900 -0.406  15.946 1.00 24.14 ? 79  LEU   A CB    1 
ATOM   507  C  CG    . LEU   A 1 82  ? 28.331 0.756   16.748 1.00 28.53 ? 79  LEU   A CG    1 
ATOM   508  C  CD1   . LEU   A 1 82  ? 29.070 0.853   18.069 1.00 30.38 ? 79  LEU   A CD1   1 
ATOM   509  C  CD2   . LEU   A 1 82  ? 28.420 2.079   16.021 1.00 24.83 ? 79  LEU   A CD2   1 
ATOM   510  N  N     . CYS   A 1 83  ? 30.209 -0.937  12.723 1.00 19.02 ? 80  CYS   A N     1 
ATOM   511  C  CA    . CYS   A 1 83  ? 31.274 -1.686  12.024 1.00 19.72 ? 80  CYS   A CA    1 
ATOM   512  C  C     . CYS   A 1 83  ? 32.601 -1.164  12.556 1.00 19.36 ? 80  CYS   A C     1 
ATOM   513  O  O     . CYS   A 1 83  ? 32.994 -0.085  12.191 1.00 20.23 ? 80  CYS   A O     1 
ATOM   514  C  CB    . CYS   A 1 83  ? 31.170 -1.481  10.531 1.00 21.34 ? 80  CYS   A CB    1 
ATOM   515  S  SG    . CYS   A 1 83  ? 29.618 -2.180  9.924  1.00 25.36 ? 80  CYS   A SG    1 
ATOM   516  N  N     . VAL   A 1 84  ? 33.213 -1.969  13.402 1.00 19.01 ? 81  VAL   A N     1 
ATOM   517  C  CA    . VAL   A 1 84  ? 34.415 -1.559  14.161 1.00 18.65 ? 81  VAL   A CA    1 
ATOM   518  C  C     . VAL   A 1 84  ? 35.699 -2.134  13.563 1.00 18.70 ? 81  VAL   A C     1 
ATOM   519  O  O     . VAL   A 1 84  ? 35.768 -3.295  13.312 1.00 20.44 ? 81  VAL   A O     1 
ATOM   520  C  CB    . VAL   A 1 84  ? 34.281 -1.985  15.636 1.00 19.31 ? 81  VAL   A CB    1 
ATOM   521  C  CG1   . VAL   A 1 84  ? 35.419 -1.422  16.474 1.00 20.13 ? 81  VAL   A CG1   1 
ATOM   522  C  CG2   . VAL   A 1 84  ? 32.939 -1.580  16.230 1.00 19.47 ? 81  VAL   A CG2   1 
ATOM   523  N  N     . PHE   A 1 85  ? 36.657 -1.248  13.370 1.00 19.55 ? 82  PHE   A N     1 
ATOM   524  C  CA    . PHE   A 1 85  ? 38.052 -1.634  13.046 1.00 20.19 ? 82  PHE   A CA    1 
ATOM   525  C  C     . PHE   A 1 85  ? 38.933 -0.956  14.094 1.00 21.83 ? 82  PHE   A C     1 
ATOM   526  O  O     . PHE   A 1 85  ? 38.501 -0.097  14.810 1.00 21.53 ? 82  PHE   A O     1 
ATOM   527  C  CB    . PHE   A 1 85  ? 38.492 -1.245  11.632 1.00 20.75 ? 82  PHE   A CB    1 
ATOM   528  C  CG    . PHE   A 1 85  ? 38.654 0.228   11.397 1.00 21.37 ? 82  PHE   A CG    1 
ATOM   529  C  CD1   . PHE   A 1 85  ? 37.574 1.012   11.053 1.00 20.90 ? 82  PHE   A CD1   1 
ATOM   530  C  CD2   . PHE   A 1 85  ? 39.893 0.828   11.497 1.00 22.70 ? 82  PHE   A CD2   1 
ATOM   531  C  CE1   . PHE   A 1 85  ? 37.709 2.369   10.857 1.00 21.76 ? 82  PHE   A CE1   1 
ATOM   532  C  CE2   . PHE   A 1 85  ? 40.026 2.181   11.287 1.00 23.04 ? 82  PHE   A CE2   1 
ATOM   533  C  CZ    . PHE   A 1 85  ? 38.942 2.948   10.963 1.00 22.87 ? 82  PHE   A CZ    1 
ATOM   534  N  N     . ALA   A 1 86  ? 40.151 -1.442  14.201 1.00 22.11 ? 83  ALA   A N     1 
ATOM   535  C  CA    . ALA   A 1 86  ? 41.169 -0.845  15.091 1.00 23.54 ? 83  ALA   A CA    1 
ATOM   536  C  C     . ALA   A 1 86  ? 42.152 -0.078  14.214 1.00 23.67 ? 83  ALA   A C     1 
ATOM   537  O  O     . ALA   A 1 86  ? 42.505 -0.589  13.149 1.00 25.37 ? 83  ALA   A O     1 
ATOM   538  C  CB    . ALA   A 1 86  ? 41.828 -1.910  15.908 1.00 23.94 ? 83  ALA   A CB    1 
ATOM   539  N  N     . ILE   A 1 87  ? 42.532 1.122   14.642 1.00 25.43 ? 84  ILE   A N     1 
ATOM   540  C  CA    . ILE   A 1 87  ? 43.327 2.099   13.830 1.00 29.43 ? 84  ILE   A CA    1 
ATOM   541  C  C     . ILE   A 1 87  ? 44.774 1.616   13.677 1.00 31.97 ? 84  ILE   A C     1 
ATOM   542  O  O     . ILE   A 1 87  ? 45.472 2.173   12.797 1.00 31.62 ? 84  ILE   A O     1 
ATOM   543  C  CB    . ILE   A 1 87  ? 43.240 3.511   14.433 1.00 29.43 ? 84  ILE   A CB    1 
ATOM   544  C  CG1   . ILE   A 1 87  ? 43.721 3.547   15.890 1.00 34.27 ? 84  ILE   A CG1   1 
ATOM   545  C  CG2   . ILE   A 1 87  ? 41.823 4.048   14.276 1.00 30.17 ? 84  ILE   A CG2   1 
ATOM   546  C  CD1   . ILE   A 1 87  ? 44.736 4.609   16.202 1.00 37.67 ? 84  ILE   A CD1   1 
ATOM   547  N  N     . ASN   A 1 88  ? 45.136 0.582   14.422 1.00 28.40 ? 85  ASN   A N     1 
ATOM   548  C  CA    . ASN   A 1 88  ? 46.475 -0.044  14.387 1.00 30.11 ? 85  ASN   A CA    1 
ATOM   549  C  C     . ASN   A 1 88  ? 46.403 -1.436  13.753 1.00 31.93 ? 85  ASN   A C     1 
ATOM   550  O  O     . ASN   A 1 88  ? 47.335 -2.184  13.889 1.00 35.02 ? 85  ASN   A O     1 
ATOM   551  C  CB    . ASN   A 1 88  ? 47.052 -0.102  15.796 1.00 33.78 ? 85  ASN   A CB    1 
ATOM   552  C  CG    . ASN   A 1 88  ? 46.308 -1.035  16.712 1.00 36.58 ? 85  ASN   A CG    1 
ATOM   553  O  OD1   . ASN   A 1 88  ? 45.118 -1.219  16.583 1.00 34.61 ? 85  ASN   A OD1   1 
ATOM   554  N  ND2   . ASN   A 1 88  ? 47.000 -1.647  17.645 1.00 37.27 ? 85  ASN   A ND2   1 
ATOM   555  N  N     . ASN   A 1 89  ? 45.330 -1.757  13.044 1.00 29.08 ? 86  ASN   A N     1 
ATOM   556  C  CA    . ASN   A 1 89  ? 45.163 -3.107  12.430 1.00 27.95 ? 86  ASN   A CA    1 
ATOM   557  C  C     . ASN   A 1 89  ? 44.586 -2.946  11.021 1.00 29.15 ? 86  ASN   A C     1 
ATOM   558  O  O     . ASN   A 1 89  ? 43.353 -2.799  10.874 1.00 25.77 ? 86  ASN   A O     1 
ATOM   559  C  CB    . ASN   A 1 89  ? 44.360 -4.059  13.323 1.00 29.50 ? 86  ASN   A CB    1 
ATOM   560  C  CG    . ASN   A 1 89  ? 44.064 -5.420  12.713 1.00 27.80 ? 86  ASN   A CG    1 
ATOM   561  O  OD1   . ASN   A 1 89  ? 44.390 -5.706  11.550 1.00 27.97 ? 86  ASN   A OD1   1 
ATOM   562  N  ND2   . ASN   A 1 89  ? 43.436 -6.283  13.500 1.00 32.51 ? 86  ASN   A ND2   1 
ATOM   563  N  N     . THR   A 1 90  ? 45.453 -2.944  10.016 1.00 27.75 ? 87  THR   A N     1 
ATOM   564  C  CA    . THR   A 1 90  ? 45.023 -2.682  8.628  1.00 27.53 ? 87  THR   A CA    1 
ATOM   565  C  C     . THR   A 1 90  ? 44.073 -3.766  8.143  1.00 24.56 ? 87  THR   A C     1 
ATOM   566  O  O     . THR   A 1 90  ? 43.152 -3.424  7.451  1.00 26.23 ? 87  THR   A O     1 
ATOM   567  C  CB    . THR   A 1 90  ? 46.219 -2.479  7.692  1.00 31.17 ? 87  THR   A CB    1 
ATOM   568  O  OG1   . THR   A 1 90  ? 47.008 -3.654  7.721  1.00 38.87 ? 87  THR   A OG1   1 
ATOM   569  C  CG2   . THR   A 1 90  ? 47.062 -1.290  8.075  1.00 32.07 ? 87  THR   A CG2   1 
ATOM   570  N  N     . LYS   A 1 91  ? 44.287 -5.008  8.545  1.00 24.90 ? 88  LYS   A N     1 
ATOM   571  C  CA    . LYS   A 1 91  ? 43.411 -6.110  8.087  1.00 26.31 ? 88  LYS   A CA    1 
ATOM   572  C  C     . LYS   A 1 91  ? 41.993 -5.863  8.619  1.00 24.41 ? 88  LYS   A C     1 
ATOM   573  O  O     . LYS   A 1 91  ? 41.063 -6.064  7.895  1.00 26.30 ? 88  LYS   A O     1 
ATOM   574  C  CB    . LYS   A 1 91  ? 43.970 -7.476  8.494  1.00 27.94 ? 88  LYS   A CB    1 
ATOM   575  C  CG    . LYS   A 1 91  ? 43.075 -8.671  8.183  1.00 31.55 ? 88  LYS   A CG    1 
ATOM   576  C  CD    . LYS   A 1 91  ? 43.555 -9.981  8.794  1.00 35.07 ? 88  LYS   A CD    1 
ATOM   577  C  CE    . LYS   A 1 91  ? 42.704 -11.179 8.440  1.00 38.28 ? 88  LYS   A CE    1 
ATOM   578  N  NZ    . LYS   A 1 91  ? 41.343 -11.054 9.000  1.00 40.12 ? 88  LYS   A NZ    1 
ATOM   579  N  N     . SER   A 1 92  ? 41.871 -5.419  9.857  1.00 23.40 ? 89  SER   A N     1 
ATOM   580  C  CA    . SER   A 1 92  ? 40.536 -5.146  10.432 1.00 21.25 ? 89  SER   A CA    1 
ATOM   581  C  C     . SER   A 1 92  ? 39.824 -4.049  9.632  1.00 22.40 ? 89  SER   A C     1 
ATOM   582  O  O     . SER   A 1 92  ? 38.635 -4.165  9.448  1.00 21.32 ? 89  SER   A O     1 
ATOM   583  C  CB    . SER   A 1 92  ? 40.619 -4.858  11.899 1.00 23.10 ? 89  SER   A CB    1 
ATOM   584  O  OG    . SER   A 1 92  ? 41.056 -3.550  12.151 1.00 23.12 ? 89  SER   A OG    1 
ATOM   585  N  N     . PHE   A 1 93  ? 40.579 -3.074  9.132  1.00 22.01 ? 90  PHE   A N     1 
ATOM   586  C  CA    . PHE   A 1 93  ? 40.006 -1.981  8.306  1.00 21.12 ? 90  PHE   A CA    1 
ATOM   587  C  C     . PHE   A 1 93  ? 39.593 -2.533  6.941  1.00 22.17 ? 90  PHE   A C     1 
ATOM   588  O  O     . PHE   A 1 93  ? 38.467 -2.298  6.520  1.00 21.98 ? 90  PHE   A O     1 
ATOM   589  C  CB    . PHE   A 1 93  ? 40.998 -0.821  8.195  1.00 22.23 ? 90  PHE   A CB    1 
ATOM   590  C  CG    . PHE   A 1 93  ? 40.515 0.263   7.271  1.00 22.65 ? 90  PHE   A CG    1 
ATOM   591  C  CD1   . PHE   A 1 93  ? 39.477 1.102   7.652  1.00 22.21 ? 90  PHE   A CD1   1 
ATOM   592  C  CD2   . PHE   A 1 93  ? 41.059 0.417   6.010  1.00 24.27 ? 90  PHE   A CD2   1 
ATOM   593  C  CE1   . PHE   A 1 93  ? 39.025 2.100   6.807  1.00 22.54 ? 90  PHE   A CE1   1 
ATOM   594  C  CE2   . PHE   A 1 93  ? 40.615 1.424   5.172  1.00 26.25 ? 90  PHE   A CE2   1 
ATOM   595  C  CZ    . PHE   A 1 93  ? 39.585 2.248   5.560  1.00 25.63 ? 90  PHE   A CZ    1 
ATOM   596  N  N     . GLU   A 1 94  ? 40.466 -3.281  6.266  1.00 22.95 ? 91  GLU   A N     1 
ATOM   597  C  CA    . GLU   A 1 94  ? 40.129 -3.889  4.953  1.00 23.83 ? 91  GLU   A CA    1 
ATOM   598  C  C     . GLU   A 1 94  ? 38.897 -4.785  5.123  1.00 23.36 ? 91  GLU   A C     1 
ATOM   599  O  O     . GLU   A 1 94  ? 38.042 -4.809  4.208  1.00 25.77 ? 91  GLU   A O     1 
ATOM   600  C  CB    . GLU   A 1 94  ? 41.341 -4.626  4.385  1.00 24.56 ? 91  GLU   A CB    1 
ATOM   601  C  CG    . GLU   A 1 94  ? 42.412 -3.667  3.901  1.00 29.33 ? 91  GLU   A CG    1 
ATOM   602  C  CD    . GLU   A 1 94  ? 41.999 -2.759  2.752  1.00 33.71 ? 91  GLU   A CD    1 
ATOM   603  O  OE1   . GLU   A 1 94  ? 41.222 -3.208  1.873  1.00 41.58 ? 91  GLU   A OE1   1 
ATOM   604  O  OE2   . GLU   A 1 94  ? 42.461 -1.603  2.725  1.00 42.20 ? 91  GLU   A OE2   1 
ATOM   605  N  N     . ASP   A 1 95  ? 38.806 -5.500  6.244  1.00 20.93 ? 92  ASP   A N     1 
ATOM   606  C  CA    . ASP   A 1 95  ? 37.714 -6.478  6.486  1.00 21.95 ? 92  ASP   A CA    1 
ATOM   607  C  C     . ASP   A 1 95  ? 36.352 -5.817  6.670  1.00 21.35 ? 92  ASP   A C     1 
ATOM   608  O  O     . ASP   A 1 95  ? 35.387 -6.492  6.550  1.00 20.48 ? 92  ASP   A O     1 
ATOM   609  C  CB    . ASP   A 1 95  ? 38.006 -7.410  7.651  1.00 25.04 ? 92  ASP   A CB    1 
ATOM   610  C  CG    . ASP   A 1 95  ? 39.012 -8.480  7.305  1.00 28.21 ? 92  ASP   A CG    1 
ATOM   611  O  OD1   . ASP   A 1 95  ? 39.323 -8.615  6.151  1.00 30.55 ? 92  ASP   A OD1   1 
ATOM   612  O  OD2   . ASP   A 1 95  ? 39.441 -9.131  8.200  1.00 32.12 ? 92  ASP   A OD2   1 
ATOM   613  N  N     . ILE   A 1 96  ? 36.303 -4.506  6.794  1.00 20.19 ? 93  ILE   A N     1 
ATOM   614  C  CA    . ILE   A 1 96  ? 34.987 -3.803  6.870  1.00 21.01 ? 93  ILE   A CA    1 
ATOM   615  C  C     . ILE   A 1 96  ? 34.178 -4.102  5.594  1.00 20.63 ? 93  ILE   A C     1 
ATOM   616  O  O     . ILE   A 1 96  ? 32.993 -4.251  5.694  1.00 21.46 ? 93  ILE   A O     1 
ATOM   617  C  CB    . ILE   A 1 96  ? 35.167 -2.291  7.098  1.00 21.47 ? 93  ILE   A CB    1 
ATOM   618  C  CG1   . ILE   A 1 96  ? 35.817 -1.983  8.450  1.00 21.99 ? 93  ILE   A CG1   1 
ATOM   619  C  CG2   . ILE   A 1 96  ? 33.838 -1.564  6.910  1.00 22.81 ? 93  ILE   A CG2   1 
ATOM   620  C  CD1   . ILE   A 1 96  ? 34.983 -2.298  9.651  1.00 22.75 ? 93  ILE   A CD1   1 
ATOM   621  N  N     . HIS   A 1 97  ? 34.838 -4.203  4.453  1.00 19.79 ? 94  HIS   A N     1 
ATOM   622  C  CA    . HIS   A 1 97  ? 34.154 -4.547  3.188  1.00 20.56 ? 94  HIS   A CA    1 
ATOM   623  C  C     . HIS   A 1 97  ? 33.338 -5.828  3.378  1.00 20.33 ? 94  HIS   A C     1 
ATOM   624  O  O     . HIS   A 1 97  ? 32.219 -5.878  2.914  1.00 21.13 ? 94  HIS   A O     1 
ATOM   625  C  CB    . HIS   A 1 97  ? 35.198 -4.718  2.080  1.00 20.29 ? 94  HIS   A CB    1 
ATOM   626  C  CG    . HIS   A 1 97  ? 34.701 -5.439  0.880  1.00 20.83 ? 94  HIS   A CG    1 
ATOM   627  N  ND1   . HIS   A 1 97  ? 34.225 -4.802  -0.218 1.00 21.42 ? 94  HIS   A ND1   1 
ATOM   628  C  CD2   . HIS   A 1 97  ? 34.611 -6.751  0.628  1.00 21.23 ? 94  HIS   A CD2   1 
ATOM   629  C  CE1   . HIS   A 1 97  ? 33.876 -5.698  -1.103 1.00 24.20 ? 94  HIS   A CE1   1 
ATOM   630  N  NE2   . HIS   A 1 97  ? 34.103 -6.887  -0.611 1.00 23.03 ? 94  HIS   A NE2   1 
ATOM   631  N  N     . HIS   A 1 98  ? 33.943 -6.819  4.024  1.00 21.22 ? 95  HIS   A N     1 
ATOM   632  C  CA    . HIS   A 1 98  ? 33.315 -8.140  4.260  1.00 22.03 ? 95  HIS   A CA    1 
ATOM   633  C  C     . HIS   A 1 98  ? 32.118 -8.037  5.202  1.00 20.06 ? 95  HIS   A C     1 
ATOM   634  O  O     . HIS   A 1 98  ? 31.109 -8.609  4.880  1.00 23.00 ? 95  HIS   A O     1 
ATOM   635  C  CB    . HIS   A 1 98  ? 34.352 -9.146  4.746  1.00 23.07 ? 95  HIS   A CB    1 
ATOM   636  C  CG    . HIS   A 1 98  ? 35.406 -9.374  3.727  1.00 28.70 ? 95  HIS   A CG    1 
ATOM   637  N  ND1   . HIS   A 1 98  ? 35.315 -10.356 2.792  1.00 32.93 ? 95  HIS   A ND1   1 
ATOM   638  C  CD2   . HIS   A 1 98  ? 36.534 -8.696  3.453  1.00 26.51 ? 95  HIS   A CD2   1 
ATOM   639  C  CE1   . HIS   A 1 98  ? 36.361 -10.305 2.008  1.00 34.89 ? 95  HIS   A CE1   1 
ATOM   640  N  NE2   . HIS   A 1 98  ? 37.123 -9.301  2.396  1.00 27.44 ? 95  HIS   A NE2   1 
ATOM   641  N  N     . TYR   A 1 99  ? 32.231 -7.292  6.285  1.00 20.50 ? 96  TYR   A N     1 
ATOM   642  C  CA    . TYR   A 1 99  ? 31.076 -7.140  7.200  1.00 21.73 ? 96  TYR   A CA    1 
ATOM   643  C  C     . TYR   A 1 99  ? 29.994 -6.327  6.480  1.00 21.34 ? 96  TYR   A C     1 
ATOM   644  O  O     . TYR   A 1 99  ? 28.873 -6.877  6.455  1.00 22.07 ? 96  TYR   A O     1 
ATOM   645  C  CB    . TYR   A 1 99  ? 31.515 -6.501  8.515  1.00 21.82 ? 96  TYR   A CB    1 
ATOM   646  C  CG    . TYR   A 1 99  ? 32.457 -7.384  9.285  1.00 22.96 ? 96  TYR   A CG    1 
ATOM   647  C  CD1   . TYR   A 1 99  ? 31.986 -8.449  10.024 1.00 24.38 ? 96  TYR   A CD1   1 
ATOM   648  C  CD2   . TYR   A 1 99  ? 33.819 -7.193  9.214  1.00 23.74 ? 96  TYR   A CD2   1 
ATOM   649  C  CE1   . TYR   A 1 99  ? 32.844 -9.287  10.708 1.00 25.01 ? 96  TYR   A CE1   1 
ATOM   650  C  CE2   . TYR   A 1 99  ? 34.689 -8.035  9.871  1.00 24.75 ? 96  TYR   A CE2   1 
ATOM   651  C  CZ    . TYR   A 1 99  ? 34.200 -9.081  10.620 1.00 24.24 ? 96  TYR   A CZ    1 
ATOM   652  O  OH    . TYR   A 1 99  ? 35.039 -9.912  11.273 1.00 27.05 ? 96  TYR   A OH    1 
ATOM   653  N  N     A ARG   A 1 100 ? 30.323 -5.257  5.781  0.50 21.23 ? 97  ARG   A N     1 
ATOM   654  N  N     B ARG   A 1 100 ? 30.287 -5.319  5.842  0.50 20.98 ? 97  ARG   A N     1 
ATOM   655  C  CA    A ARG   A 1 100 ? 29.265 -4.455  5.125  0.50 22.06 ? 97  ARG   A CA    1 
ATOM   656  C  CA    B ARG   A 1 100 ? 29.255 -4.496  5.165  0.50 22.34 ? 97  ARG   A CA    1 
ATOM   657  C  C     A ARG   A 1 100 ? 28.574 -5.277  4.036  0.50 21.56 ? 97  ARG   A C     1 
ATOM   658  C  C     B ARG   A 1 100 ? 28.565 -5.319  4.076  0.50 21.22 ? 97  ARG   A C     1 
ATOM   659  O  O     A ARG   A 1 100 ? 27.355 -5.333  4.059  0.50 22.45 ? 97  ARG   A O     1 
ATOM   660  O  O     B ARG   A 1 100 ? 27.346 -5.338  4.058  0.50 22.51 ? 97  ARG   A O     1 
ATOM   661  C  CB    A ARG   A 1 100 ? 29.875 -3.174  4.558  0.50 22.87 ? 97  ARG   A CB    1 
ATOM   662  C  CB    B ARG   A 1 100 ? 29.882 -3.231  4.579  0.50 23.86 ? 97  ARG   A CB    1 
ATOM   663  C  CG    A ARG   A 1 100 ? 28.930 -2.395  3.658  0.50 24.49 ? 97  ARG   A CG    1 
ATOM   664  C  CG    B ARG   A 1 100 ? 28.940 -2.439  3.686  0.50 26.65 ? 97  ARG   A CG    1 
ATOM   665  C  CD    A ARG   A 1 100 ? 29.456 -1.012  3.337  0.50 25.83 ? 97  ARG   A CD    1 
ATOM   666  C  CD    B ARG   A 1 100 ? 29.508 -1.089  3.301  0.50 29.57 ? 97  ARG   A CD    1 
ATOM   667  N  NE    A ARG   A 1 100 ? 28.719 -0.356  2.273  0.50 26.99 ? 97  ARG   A NE    1 
ATOM   668  N  NE    B ARG   A 1 100 ? 28.600 -0.270  2.520  0.50 33.63 ? 97  ARG   A NE    1 
ATOM   669  C  CZ    A ARG   A 1 100 ? 28.886 -0.598  0.977  0.50 26.60 ? 97  ARG   A CZ    1 
ATOM   670  C  CZ    B ARG   A 1 100 ? 27.604 0.438   3.048  0.50 34.71 ? 97  ARG   A CZ    1 
ATOM   671  N  NH1   A ARG   A 1 100 ? 29.757 -1.502  0.574  0.50 24.14 ? 97  ARG   A NH1   1 
ATOM   672  N  NH1   B ARG   A 1 100 ? 27.383 0.416   4.349  0.50 34.75 ? 97  ARG   A NH1   1 
ATOM   673  N  NH2   A ARG   A 1 100 ? 28.175 0.060   0.079  0.50 28.36 ? 97  ARG   A NH2   1 
ATOM   674  N  NH2   B ARG   A 1 100 ? 26.828 1.177   2.279  0.50 37.91 ? 97  ARG   A NH2   1 
ATOM   675  N  N     . GLU   A 1 101 ? 29.322 -6.135  3.350  1.00 21.45 ? 98  GLU   A N     1 
ATOM   676  C  CA    . GLU   A 1 101 ? 28.769 -6.963  2.254  1.00 24.50 ? 98  GLU   A CA    1 
ATOM   677  C  C     . GLU   A 1 101 ? 27.828 -8.041  2.799  1.00 23.64 ? 98  GLU   A C     1 
ATOM   678  O  O     . GLU   A 1 101 ? 26.798 -8.223  2.215  1.00 25.85 ? 98  GLU   A O     1 
ATOM   679  C  CB    . GLU   A 1 101 ? 29.904 -7.586  1.444  1.00 26.27 ? 98  GLU   A CB    1 
ATOM   680  C  CG    . GLU   A 1 101 ? 29.426 -8.524  0.367  1.00 28.74 ? 98  GLU   A CG    1 
ATOM   681  C  CD    . GLU   A 1 101 ? 30.529 -9.146  -0.463 1.00 30.69 ? 98  GLU   A CD    1 
ATOM   682  O  OE1   . GLU   A 1 101 ? 31.482 -8.456  -0.747 1.00 25.90 ? 98  GLU   A OE1   1 
ATOM   683  O  OE2   . GLU   A 1 101 ? 30.410 -10.305 -0.815 1.00 36.39 ? 98  GLU   A OE2   1 
ATOM   684  N  N     . GLN   A 1 102 ? 28.183 -8.695  3.887  1.00 24.34 ? 99  GLN   A N     1 
ATOM   685  C  CA    . GLN   A 1 102 ? 27.341 -9.774  4.458  1.00 25.27 ? 99  GLN   A CA    1 
ATOM   686  C  C     . GLN   A 1 102 ? 26.035 -9.161  4.978  1.00 23.49 ? 99  GLN   A C     1 
ATOM   687  O  O     . GLN   A 1 102 ? 24.994 -9.747  4.774  1.00 23.90 ? 99  GLN   A O     1 
ATOM   688  C  CB    . GLN   A 1 102 ? 28.094 -10.474 5.588  1.00 27.94 ? 99  GLN   A CB    1 
ATOM   689  C  CG    . GLN   A 1 102 ? 29.308 -11.255 5.123  1.00 33.52 ? 99  GLN   A CG    1 
ATOM   690  C  CD    . GLN   A 1 102 ? 30.283 -11.666 6.200  1.00 42.22 ? 99  GLN   A CD    1 
ATOM   691  O  OE1   . GLN   A 1 102 ? 30.146 -11.361 7.379  1.00 45.93 ? 99  GLN   A OE1   1 
ATOM   692  N  NE2   . GLN   A 1 102 ? 31.312 -12.376 5.785  1.00 49.29 ? 99  GLN   A NE2   1 
ATOM   693  N  N     . ILE   A 1 103 ? 26.114 -8.023  5.637  1.00 21.34 ? 100 ILE   A N     1 
ATOM   694  C  CA    . ILE   A 1 103 ? 24.920 -7.324  6.181  1.00 23.46 ? 100 ILE   A CA    1 
ATOM   695  C  C     . ILE   A 1 103 ? 23.981 -6.951  5.027  1.00 23.74 ? 100 ILE   A C     1 
ATOM   696  O  O     . ILE   A 1 103 ? 22.814 -7.281  5.106  1.00 26.47 ? 100 ILE   A O     1 
ATOM   697  C  CB    . ILE   A 1 103 ? 25.329 -6.103  7.027  1.00 21.32 ? 100 ILE   A CB    1 
ATOM   698  C  CG1   . ILE   A 1 103 ? 26.030 -6.539  8.313  1.00 22.68 ? 100 ILE   A CG1   1 
ATOM   699  C  CG2   . ILE   A 1 103 ? 24.127 -5.224  7.315  1.00 23.98 ? 100 ILE   A CG2   1 
ATOM   700  C  CD1   . ILE   A 1 103 ? 26.915 -5.486  8.931  1.00 21.85 ? 100 ILE   A CD1   1 
ATOM   701  N  N     . LYS   A 1 104 ? 24.495 -6.325  3.980  1.00 24.58 ? 101 LYS   A N     1 
ATOM   702  C  CA    . LYS   A 1 104 ? 23.663 -5.878  2.833  1.00 26.49 ? 101 LYS   A CA    1 
ATOM   703  C  C     . LYS   A 1 104 ? 23.025 -7.074  2.116  1.00 26.26 ? 101 LYS   A C     1 
ATOM   704  O  O     . LYS   A 1 104 ? 21.890 -6.946  1.692  1.00 29.46 ? 101 LYS   A O     1 
ATOM   705  C  CB    . LYS   A 1 104 ? 24.480 -4.984  1.902  1.00 27.93 ? 101 LYS   A CB    1 
ATOM   706  C  CG    . LYS   A 1 104 ? 24.819 -3.621  2.485  1.00 30.14 ? 101 LYS   A CG    1 
ATOM   707  C  CD    . LYS   A 1 104 ? 25.697 -2.743  1.621  1.00 37.65 ? 101 LYS   A CD    1 
ATOM   708  C  CE    . LYS   A 1 104 ? 25.407 -2.824  0.144  1.00 44.33 ? 101 LYS   A CE    1 
ATOM   709  N  NZ    . LYS   A 1 104 ? 26.632 -2.631  -0.661 1.00 49.37 ? 101 LYS   A NZ    1 
ATOM   710  N  N     . ARG   A 1 105 ? 23.727 -8.195  2.054  1.00 26.16 ? 102 ARG   A N     1 
ATOM   711  C  CA    . ARG   A 1 105 ? 23.233 -9.445  1.406  1.00 30.52 ? 102 ARG   A CA    1 
ATOM   712  C  C     . ARG   A 1 105 ? 22.032 -9.999  2.186  1.00 31.00 ? 102 ARG   A C     1 
ATOM   713  O  O     . ARG   A 1 105 ? 21.043 -10.359 1.534  1.00 35.26 ? 102 ARG   A O     1 
ATOM   714  C  CB    . ARG   A 1 105 ? 24.346 -10.492 1.314  1.00 32.44 ? 102 ARG   A CB    1 
ATOM   715  C  CG    . ARG   A 1 105 ? 23.940 -11.774 0.596  1.00 36.67 ? 102 ARG   A CG    1 
ATOM   716  C  CD    . ARG   A 1 105 ? 25.108 -12.723 0.391  1.00 42.15 ? 102 ARG   A CD    1 
ATOM   717  N  NE    . ARG   A 1 105 ? 26.036 -12.195 -0.606 1.00 48.13 ? 102 ARG   A NE    1 
ATOM   718  C  CZ    . ARG   A 1 105 ? 27.269 -11.731 -0.373 1.00 49.55 ? 102 ARG   A CZ    1 
ATOM   719  N  NH1   . ARG   A 1 105 ? 27.986 -11.262 -1.380 1.00 47.83 ? 102 ARG   A NH1   1 
ATOM   720  N  NH2   . ARG   A 1 105 ? 27.792 -11.744 0.842  1.00 52.51 ? 102 ARG   A NH2   1 
ATOM   721  N  N     . VAL   A 1 106 ? 22.139 -10.096 3.502  1.00 29.69 ? 103 VAL   A N     1 
ATOM   722  C  CA    . VAL   A 1 106 ? 21.083 -10.652 4.392  1.00 31.13 ? 103 VAL   A CA    1 
ATOM   723  C  C     . VAL   A 1 106 ? 19.891 -9.699  4.430  1.00 31.56 ? 103 VAL   A C     1 
ATOM   724  O  O     . VAL   A 1 106 ? 18.769 -10.167 4.437  1.00 35.97 ? 103 VAL   A O     1 
ATOM   725  C  CB    . VAL   A 1 106 ? 21.678 -10.824 5.793  1.00 33.72 ? 103 VAL   A CB    1 
ATOM   726  C  CG1   . VAL   A 1 106 ? 20.619 -11.110 6.835  1.00 36.86 ? 103 VAL   A CG1   1 
ATOM   727  C  CG2   . VAL   A 1 106 ? 22.742 -11.895 5.801  1.00 35.38 ? 103 VAL   A CG2   1 
ATOM   728  N  N     . LYS   A 1 107 ? 20.139 -8.403  4.421  1.00 29.96 ? 104 LYS   A N     1 
ATOM   729  C  CA    . LYS   A 1 107 ? 19.057 -7.402  4.525  1.00 33.07 ? 104 LYS   A CA    1 
ATOM   730  C  C     . LYS   A 1 107 ? 18.500 -7.071  3.145  1.00 35.42 ? 104 LYS   A C     1 
ATOM   731  O  O     . LYS   A 1 107 ? 17.507 -6.380  3.093  1.00 38.66 ? 104 LYS   A O     1 
ATOM   732  C  CB    . LYS   A 1 107 ? 19.533 -6.207  5.356  1.00 35.70 ? 104 LYS   A CB    1 
ATOM   733  C  CG    . LYS   A 1 107 ? 19.797 -6.576  6.803  1.00 39.53 ? 104 LYS   A CG    1 
ATOM   734  C  CD    . LYS   A 1 107 ? 20.015 -5.452  7.757  1.00 38.89 ? 104 LYS   A CD    1 
ATOM   735  C  CE    . LYS   A 1 107 ? 18.760 -5.047  8.480  1.00 37.66 ? 104 LYS   A CE    1 
ATOM   736  N  NZ    . LYS   A 1 107 ? 18.275 -6.082  9.406  1.00 38.79 ? 104 LYS   A NZ    1 
ATOM   737  N  N     . ASP   A 1 108 ? 19.121 -7.587  2.091  1.00 35.75 ? 105 ASP   A N     1 
ATOM   738  C  CA    . ASP   A 1 108 ? 18.692 -7.348  0.693  1.00 42.18 ? 105 ASP   A CA    1 
ATOM   739  C  C     . ASP   A 1 108 ? 18.416 -5.862  0.470  1.00 40.81 ? 105 ASP   A C     1 
ATOM   740  O  O     . ASP   A 1 108 ? 17.366 -5.547  -0.057 1.00 45.30 ? 105 ASP   A O     1 
ATOM   741  C  CB    . ASP   A 1 108 ? 17.450 -8.163  0.347  1.00 44.60 ? 105 ASP   A CB    1 
ATOM   742  C  CG    . ASP   A 1 108 ? 17.368 -8.557  -1.122 1.00 53.90 ? 105 ASP   A CG    1 
ATOM   743  O  OD1   . ASP   A 1 108 ? 18.144 -9.415  -1.536 1.00 55.09 ? 105 ASP   A OD1   1 
ATOM   744  O  OD2   . ASP   A 1 108 ? 16.487 -8.023  -1.826 1.00 60.90 ? 105 ASP   A OD2   1 
ATOM   745  N  N     . SER   A 1 109 ? 19.353 -5.016  0.894  1.00 41.65 ? 106 SER   A N     1 
ATOM   746  C  CA    . SER   A 1 109 ? 19.194 -3.556  0.779  1.00 43.84 ? 106 SER   A CA    1 
ATOM   747  C  C     . SER   A 1 109 ? 20.573 -2.904  0.786  1.00 47.07 ? 106 SER   A C     1 
ATOM   748  O  O     . SER   A 1 109 ? 21.387 -3.265  1.632  1.00 45.74 ? 106 SER   A O     1 
ATOM   749  C  CB    . SER   A 1 109 ? 18.358 -3.054  1.907  1.00 46.42 ? 106 SER   A CB    1 
ATOM   750  O  OG    . SER   A 1 109 ? 18.222 -1.656  1.856  1.00 45.07 ? 106 SER   A OG    1 
ATOM   751  N  N     . GLU   A 1 110 ? 20.755 -1.921  -0.097 1.00 51.49 ? 107 GLU   A N     1 
ATOM   752  C  CA    . GLU   A 1 110 ? 22.027 -1.166  -0.195 1.00 55.06 ? 107 GLU   A CA    1 
ATOM   753  C  C     . GLU   A 1 110 ? 22.000 -0.063  0.868  1.00 53.71 ? 107 GLU   A C     1 
ATOM   754  O  O     . GLU   A 1 110 ? 23.014 0.595   1.076  1.00 56.90 ? 107 GLU   A O     1 
ATOM   755  C  CB    . GLU   A 1 110 ? 22.259 -0.723  -1.647 1.00 62.77 ? 107 GLU   A CB    1 
ATOM   756  C  CG    . GLU   A 1 110 ? 22.575 -1.895  -2.574 1.00 67.45 ? 107 GLU   A CG    1 
ATOM   757  C  CD    . GLU   A 1 110 ? 23.096 -1.662  -3.983 1.00 68.49 ? 107 GLU   A CD    1 
ATOM   758  O  OE1   . GLU   A 1 110 ? 23.718 -0.622  -4.219 1.00 67.77 ? 107 GLU   A OE1   1 
ATOM   759  O  OE2   . GLU   A 1 110 ? 22.879 -2.544  -4.845 1.00 68.47 ? 107 GLU   A OE2   1 
ATOM   760  N  N     . ASP   A 1 111 ? 20.867 0.061   1.554  1.00 50.04 ? 108 ASP   A N     1 
ATOM   761  C  CA    . ASP   A 1 111 ? 20.638 1.083   2.598  1.00 44.38 ? 108 ASP   A CA    1 
ATOM   762  C  C     . ASP   A 1 111 ? 20.424 0.387   3.941  1.00 37.09 ? 108 ASP   A C     1 
ATOM   763  O  O     . ASP   A 1 111 ? 19.352 -0.131  4.137  1.00 39.75 ? 108 ASP   A O     1 
ATOM   764  C  CB    . ASP   A 1 111 ? 19.327 1.790   2.262  1.00 49.75 ? 108 ASP   A CB    1 
ATOM   765  C  CG    . ASP   A 1 111 ? 19.034 3.061   3.020  1.00 57.58 ? 108 ASP   A CG    1 
ATOM   766  O  OD1   . ASP   A 1 111 ? 19.921 3.543   3.723  1.00 65.65 ? 108 ASP   A OD1   1 
ATOM   767  O  OD2   . ASP   A 1 111 ? 17.923 3.560   2.873  1.00 64.31 ? 108 ASP   A OD2   1 
ATOM   768  N  N     . VAL   A 1 112 ? 21.425 0.359   4.810  1.00 28.72 ? 109 VAL   A N     1 
ATOM   769  C  CA    . VAL   A 1 112 ? 21.249 -0.242  6.159  1.00 25.72 ? 109 VAL   A CA    1 
ATOM   770  C  C     . VAL   A 1 112 ? 21.895 0.731   7.146  1.00 24.93 ? 109 VAL   A C     1 
ATOM   771  O  O     . VAL   A 1 112 ? 23.005 1.134   6.877  1.00 23.86 ? 109 VAL   A O     1 
ATOM   772  C  CB    . VAL   A 1 112 ? 21.897 -1.638  6.256  1.00 27.44 ? 109 VAL   A CB    1 
ATOM   773  C  CG1   . VAL   A 1 112 ? 21.865 -2.180  7.668  1.00 26.56 ? 109 VAL   A CG1   1 
ATOM   774  C  CG2   . VAL   A 1 112 ? 21.288 -2.631  5.289  1.00 29.52 ? 109 VAL   A CG2   1 
ATOM   775  N  N     . PRO   A 1 113 ? 21.252 1.125   8.264  1.00 21.94 ? 110 PRO   A N     1 
ATOM   776  C  CA    . PRO   A 1 113 ? 21.893 2.014   9.214  1.00 22.81 ? 110 PRO   A CA    1 
ATOM   777  C  C     . PRO   A 1 113 ? 23.210 1.392   9.696  1.00 22.40 ? 110 PRO   A C     1 
ATOM   778  O  O     . PRO   A 1 113 ? 23.198 0.342   10.181 1.00 20.34 ? 110 PRO   A O     1 
ATOM   779  C  CB    . PRO   A 1 113 ? 20.877 2.133   10.346 1.00 23.06 ? 110 PRO   A CB    1 
ATOM   780  C  CG    . PRO   A 1 113 ? 19.572 1.880   9.654  1.00 24.08 ? 110 PRO   A CG    1 
ATOM   781  C  CD    . PRO   A 1 113 ? 19.875 0.816   8.629  1.00 22.89 ? 110 PRO   A CD    1 
ATOM   782  N  N     . MET   A 1 114 ? 24.290 2.138   9.516  1.00 21.35 ? 111 MET   A N     1 
ATOM   783  C  CA    . MET   A 1 114 ? 25.645 1.680   9.904  1.00 20.96 ? 111 MET   A CA    1 
ATOM   784  C  C     . MET   A 1 114 ? 26.497 2.895   10.254 1.00 21.99 ? 111 MET   A C     1 
ATOM   785  O  O     . MET   A 1 114 ? 26.278 3.939   9.728  1.00 21.42 ? 111 MET   A O     1 
ATOM   786  C  CB    . MET   A 1 114 ? 26.373 0.960   8.758  1.00 25.81 ? 111 MET   A CB    1 
ATOM   787  C  CG    . MET   A 1 114 ? 25.787 -0.344  8.326  1.00 27.71 ? 111 MET   A CG    1 
ATOM   788  S  SD    . MET   A 1 114 ? 26.952 -1.203  7.248  1.00 35.16 ? 111 MET   A SD    1 
ATOM   789  C  CE    . MET   A 1 114 ? 25.888 -2.417  6.487  1.00 38.22 ? 111 MET   A CE    1 
ATOM   790  N  N     . VAL   A 1 115 ? 27.427 2.697   11.163 1.00 20.73 ? 112 VAL   A N     1 
ATOM   791  C  CA    . VAL   A 1 115 ? 28.436 3.715   11.528 1.00 20.36 ? 112 VAL   A CA    1 
ATOM   792  C  C     . VAL   A 1 115 ? 29.768 2.991   11.481 1.00 19.57 ? 112 VAL   A C     1 
ATOM   793  O  O     . VAL   A 1 115 ? 29.871 1.894   12.067 1.00 19.75 ? 112 VAL   A O     1 
ATOM   794  C  CB    . VAL   A 1 115 ? 28.192 4.365   12.907 1.00 20.07 ? 112 VAL   A CB    1 
ATOM   795  C  CG1   . VAL   A 1 115 ? 29.360 5.252   13.317 1.00 21.92 ? 112 VAL   A CG1   1 
ATOM   796  C  CG2   . VAL   A 1 115 ? 26.906 5.178   12.947 1.00 21.93 ? 112 VAL   A CG2   1 
ATOM   797  N  N     . LEU   A 1 116 ? 30.735 3.591   10.805 1.00 19.64 ? 113 LEU   A N     1 
ATOM   798  C  CA    . LEU   A 1 116 ? 32.123 3.088   10.798 1.00 19.89 ? 113 LEU   A CA    1 
ATOM   799  C  C     . LEU   A 1 116 ? 32.817 3.632   12.041 1.00 19.37 ? 113 LEU   A C     1 
ATOM   800  O  O     . LEU   A 1 116 ? 32.744 4.865   12.269 1.00 22.32 ? 113 LEU   A O     1 
ATOM   801  C  CB    . LEU   A 1 116 ? 32.826 3.526   9.515  1.00 20.70 ? 113 LEU   A CB    1 
ATOM   802  C  CG    . LEU   A 1 116 ? 34.250 2.997   9.362  1.00 20.99 ? 113 LEU   A CG    1 
ATOM   803  C  CD1   . LEU   A 1 116 ? 34.244 1.487   9.182  1.00 23.55 ? 113 LEU   A CD1   1 
ATOM   804  C  CD2   . LEU   A 1 116 ? 34.958 3.702   8.193  1.00 23.16 ? 113 LEU   A CD2   1 
ATOM   805  N  N     . VAL   A 1 117 ? 33.414 2.744   12.826 1.00 20.17 ? 114 VAL   A N     1 
ATOM   806  C  CA    . VAL   A 1 117 ? 34.074 3.105   14.102 1.00 20.77 ? 114 VAL   A CA    1 
ATOM   807  C  C     . VAL   A 1 117 ? 35.541 2.696   13.995 1.00 20.43 ? 114 VAL   A C     1 
ATOM   808  O  O     . VAL   A 1 117 ? 35.832 1.510   13.775 1.00 20.28 ? 114 VAL   A O     1 
ATOM   809  C  CB    . VAL   A 1 117 ? 33.360 2.468   15.304 1.00 21.92 ? 114 VAL   A CB    1 
ATOM   810  C  CG1   . VAL   A 1 117 ? 34.084 2.820   16.594 1.00 22.70 ? 114 VAL   A CG1   1 
ATOM   811  C  CG2   . VAL   A 1 117 ? 31.904 2.890   15.359 1.00 22.63 ? 114 VAL   A CG2   1 
ATOM   812  N  N     . GLY   A 1 118 ? 36.435 3.672   14.137 1.00 22.65 ? 115 GLY   A N     1 
ATOM   813  C  CA    . GLY   A 1 118 ? 37.875 3.397   14.220 1.00 23.16 ? 115 GLY   A CA    1 
ATOM   814  C  C     . GLY   A 1 118 ? 38.257 3.437   15.687 1.00 23.32 ? 115 GLY   A C     1 
ATOM   815  O  O     . GLY   A 1 118 ? 38.318 4.507   16.217 1.00 25.63 ? 115 GLY   A O     1 
ATOM   816  N  N     . ASN   A 1 119 ? 38.409 2.271   16.298 1.00 22.07 ? 116 ASN   A N     1 
ATOM   817  C  CA    . ASN   A 1 119 ? 38.697 2.143   17.750 1.00 24.55 ? 116 ASN   A CA    1 
ATOM   818  C  C     . ASN   A 1 119 ? 40.218 2.195   17.997 1.00 26.08 ? 116 ASN   A C     1 
ATOM   819  O  O     . ASN   A 1 119 ? 40.956 2.004   17.053 1.00 28.57 ? 116 ASN   A O     1 
ATOM   820  C  CB    . ASN   A 1 119 ? 37.989 0.900   18.319 1.00 23.79 ? 116 ASN   A CB    1 
ATOM   821  C  CG    . ASN   A 1 119 ? 37.910 0.832   19.828 1.00 25.25 ? 116 ASN   A CG    1 
ATOM   822  O  OD1   . ASN   A 1 119 ? 37.689 1.835   20.453 1.00 25.03 ? 116 ASN   A OD1   1 
ATOM   823  N  ND2   . ASN   A 1 119 ? 38.254 -0.298  20.387 1.00 22.95 ? 116 ASN   A ND2   1 
ATOM   824  N  N     . LYS   A 1 120 ? 40.606 2.393   19.268 1.00 26.16 ? 117 LYS   A N     1 
ATOM   825  C  CA    . LYS   A 1 120 ? 41.980 2.457   19.832 1.00 29.64 ? 117 LYS   A CA    1 
ATOM   826  C  C     . LYS   A 1 120 ? 42.626 3.779   19.423 1.00 31.24 ? 117 LYS   A C     1 
ATOM   827  O  O     . LYS   A 1 120 ? 43.790 3.776   19.183 1.00 34.81 ? 117 LYS   A O     1 
ATOM   828  C  CB    . LYS   A 1 120 ? 42.763 1.171   19.555 1.00 29.19 ? 117 LYS   A CB    1 
ATOM   829  C  CG    . LYS   A 1 120 ? 41.986 -0.130  19.727 1.00 26.93 ? 117 LYS   A CG    1 
ATOM   830  C  CD    . LYS   A 1 120 ? 42.854 -1.320  19.907 1.00 29.06 ? 117 LYS   A CD    1 
ATOM   831  C  CE    . LYS   A 1 120 ? 42.115 -2.629  19.931 1.00 26.97 ? 117 LYS   A CE    1 
ATOM   832  N  NZ    . LYS   A 1 120 ? 43.012 -3.790  20.043 1.00 30.22 ? 117 LYS   A NZ    1 
ATOM   833  N  N     . SER   A 1 121 ? 41.836 4.833   19.302 1.00 30.66 ? 118 SER   A N     1 
ATOM   834  C  CA    . SER   A 1 121 ? 42.330 6.163   18.882 1.00 33.95 ? 118 SER   A CA    1 
ATOM   835  C  C     . SER   A 1 121 ? 43.392 6.675   19.856 1.00 34.28 ? 118 SER   A C     1 
ATOM   836  O  O     . SER   A 1 121 ? 44.115 7.577   19.483 1.00 37.26 ? 118 SER   A O     1 
ATOM   837  C  CB    . SER   A 1 121 ? 41.219 7.126   18.744 1.00 35.85 ? 118 SER   A CB    1 
ATOM   838  O  OG    . SER   A 1 121 ? 40.713 7.454   20.016 1.00 37.45 ? 118 SER   A OG    1 
ATOM   839  N  N     . ASP   A 1 122 ? 43.425 6.122   21.059 1.00 33.49 ? 119 ASP   A N     1 
ATOM   840  C  CA    . ASP   A 1 122 ? 44.408 6.492   22.112 1.00 35.45 ? 119 ASP   A CA    1 
ATOM   841  C  C     . ASP   A 1 122 ? 45.806 5.965   21.755 1.00 35.03 ? 119 ASP   A C     1 
ATOM   842  O  O     . ASP   A 1 122 ? 46.773 6.495   22.328 1.00 40.25 ? 119 ASP   A O     1 
ATOM   843  C  CB    . ASP   A 1 122 ? 43.979 5.951   23.479 1.00 38.05 ? 119 ASP   A CB    1 
ATOM   844  C  CG    . ASP   A 1 122 ? 43.830 4.441   23.498 1.00 37.89 ? 119 ASP   A CG    1 
ATOM   845  O  OD1   . ASP   A 1 122 ? 42.808 3.941   22.942 1.00 35.14 ? 119 ASP   A OD1   1 
ATOM   846  O  OD2   . ASP   A 1 122 ? 44.716 3.776   24.042 1.00 38.92 ? 119 ASP   A OD2   1 
ATOM   847  N  N     . LEU   A 1 123 ? 45.913 4.951   20.898 1.00 36.74 ? 120 LEU   A N     1 
ATOM   848  C  CA    . LEU   A 1 123 ? 47.205 4.266   20.629 1.00 37.57 ? 120 LEU   A CA    1 
ATOM   849  C  C     . LEU   A 1 123 ? 48.135 5.063   19.715 1.00 41.06 ? 120 LEU   A C     1 
ATOM   850  O  O     . LEU   A 1 123 ? 47.659 5.679   18.786 1.00 37.71 ? 120 LEU   A O     1 
ATOM   851  C  CB    . LEU   A 1 123 ? 46.927 2.918   19.977 1.00 39.50 ? 120 LEU   A CB    1 
ATOM   852  C  CG    . LEU   A 1 123 ? 46.480 1.787   20.894 1.00 41.36 ? 120 LEU   A CG    1 
ATOM   853  C  CD1   . LEU   A 1 123 ? 46.472 0.488   20.124 1.00 40.06 ? 120 LEU   A CD1   1 
ATOM   854  C  CD2   . LEU   A 1 123 ? 47.390 1.666   22.098 1.00 40.63 ? 120 LEU   A CD2   1 
ATOM   855  N  N     . PRO   A 1 124 ? 49.470 5.025   19.922 1.00 39.68 ? 121 PRO   A N     1 
ATOM   856  C  CA    . PRO   A 1 124 ? 50.389 5.733   19.038 1.00 42.55 ? 121 PRO   A CA    1 
ATOM   857  C  C     . PRO   A 1 124 ? 50.705 4.972   17.742 1.00 42.76 ? 121 PRO   A C     1 
ATOM   858  O  O     . PRO   A 1 124 ? 51.013 5.576   16.778 1.00 50.95 ? 121 PRO   A O     1 
ATOM   859  C  CB    . PRO   A 1 124 ? 51.619 5.892   19.939 1.00 40.70 ? 121 PRO   A CB    1 
ATOM   860  C  CG    . PRO   A 1 124 ? 51.622 4.657   20.798 1.00 38.41 ? 121 PRO   A CG    1 
ATOM   861  C  CD    . PRO   A 1 124 ? 50.157 4.292   20.976 1.00 36.59 ? 121 PRO   A CD    1 
ATOM   862  N  N     . SER   A 1 125 ? 50.547 3.657   17.729 1.00 40.23 ? 122 SER   A N     1 
ATOM   863  C  CA    . SER   A 1 125 ? 50.892 2.866   16.526 1.00 40.08 ? 122 SER   A CA    1 
ATOM   864  C  C     . SER   A 1 125 ? 49.794 2.863   15.452 1.00 39.47 ? 122 SER   A C     1 
ATOM   865  O  O     . SER   A 1 125 ? 49.501 1.791   14.996 1.00 41.51 ? 122 SER   A O     1 
ATOM   866  C  CB    . SER   A 1 125 ? 51.240 1.466   16.939 1.00 45.15 ? 122 SER   A CB    1 
ATOM   867  O  OG    . SER   A 1 125 ? 50.305 0.951   17.871 1.00 50.61 ? 122 SER   A OG    1 
ATOM   868  N  N     . ARG   A 1 126 ? 49.361 4.023   14.964 1.00 39.62 ? 123 ARG   A N     1 
ATOM   869  C  CA    . ARG   A 1 126 ? 48.293 4.136   13.933 1.00 37.10 ? 123 ARG   A CA    1 
ATOM   870  C  C     . ARG   A 1 126 ? 48.805 3.690   12.557 1.00 36.67 ? 123 ARG   A C     1 
ATOM   871  O  O     . ARG   A 1 126 ? 49.810 4.237   12.099 1.00 39.81 ? 123 ARG   A O     1 
ATOM   872  C  CB    . ARG   A 1 126 ? 47.744 5.559   13.891 1.00 37.55 ? 123 ARG   A CB    1 
ATOM   873  C  CG    . ARG   A 1 126 ? 46.912 5.871   12.663 1.00 37.36 ? 123 ARG   A CG    1 
ATOM   874  C  CD    . ARG   A 1 126 ? 46.504 7.315   12.523 1.00 39.53 ? 123 ARG   A CD    1 
ATOM   875  N  NE    . ARG   A 1 126 ? 45.691 7.848   13.596 1.00 39.83 ? 123 ARG   A NE    1 
ATOM   876  C  CZ    . ARG   A 1 126 ? 44.377 7.731   13.684 1.00 39.83 ? 123 ARG   A CZ    1 
ATOM   877  N  NH1   . ARG   A 1 126 ? 43.706 7.085   12.759 1.00 38.65 ? 123 ARG   A NH1   1 
ATOM   878  N  NH2   . ARG   A 1 126 ? 43.735 8.250   14.705 1.00 43.07 ? 123 ARG   A NH2   1 
ATOM   879  N  N     . THR   A 1 127 ? 48.145 2.696   11.954 1.00 37.73 ? 124 THR   A N     1 
ATOM   880  C  CA    . THR   A 1 127 ? 48.446 2.166   10.597 1.00 36.65 ? 124 THR   A CA    1 
ATOM   881  C  C     . THR   A 1 127 ? 47.327 2.530   9.610  1.00 37.01 ? 124 THR   A C     1 
ATOM   882  O  O     . THR   A 1 127 ? 47.559 2.327   8.400  1.00 39.18 ? 124 THR   A O     1 
ATOM   883  C  CB    . THR   A 1 127 ? 48.676 0.649   10.617 1.00 37.97 ? 124 THR   A CB    1 
ATOM   884  O  OG1   . THR   A 1 127 ? 47.446 0.037   11.017 1.00 36.17 ? 124 THR   A OG1   1 
ATOM   885  C  CG2   . THR   A 1 127 ? 49.812 0.212   11.522 1.00 40.66 ? 124 THR   A CG2   1 
ATOM   886  N  N     . VAL   A 1 128 ? 46.174 3.026   10.085 1.00 33.87 ? 125 VAL   A N     1 
ATOM   887  C  CA    . VAL   A 1 128 ? 45.055 3.494   9.229  1.00 32.84 ? 125 VAL   A CA    1 
ATOM   888  C  C     . VAL   A 1 128 ? 44.807 4.985   9.451  1.00 31.58 ? 125 VAL   A C     1 
ATOM   889  O  O     . VAL   A 1 128 ? 44.347 5.357   10.574 1.00 33.80 ? 125 VAL   A O     1 
ATOM   890  C  CB    . VAL   A 1 128 ? 43.752 2.718   9.528  1.00 31.15 ? 125 VAL   A CB    1 
ATOM   891  C  CG1   . VAL   A 1 128 ? 42.612 3.194   8.658  1.00 30.87 ? 125 VAL   A CG1   1 
ATOM   892  C  CG2   . VAL   A 1 128 ? 43.958 1.224   9.389  1.00 32.61 ? 125 VAL   A CG2   1 
ATOM   893  N  N     . ASP   A 1 129 ? 45.011 5.790   8.401  1.00 33.72 ? 126 ASP   A N     1 
ATOM   894  C  CA    . ASP   A 1 129 ? 44.856 7.264   8.451  1.00 38.37 ? 126 ASP   A CA    1 
ATOM   895  C  C     . ASP   A 1 129 ? 43.385 7.615   8.661  1.00 36.18 ? 126 ASP   A C     1 
ATOM   896  O  O     . ASP   A 1 129 ? 42.529 7.009   8.000  1.00 34.40 ? 126 ASP   A O     1 
ATOM   897  C  CB    . ASP   A 1 129 ? 45.393 7.929   7.180  1.00 44.10 ? 126 ASP   A CB    1 
ATOM   898  C  CG    . ASP   A 1 129 ? 46.908 7.965   7.134  1.00 51.01 ? 126 ASP   A CG    1 
ATOM   899  O  OD1   . ASP   A 1 129 ? 47.528 7.465   8.094  1.00 57.26 ? 126 ASP   A OD1   1 
ATOM   900  O  OD2   . ASP   A 1 129 ? 47.452 8.496   6.147  1.00 57.23 ? 126 ASP   A OD2   1 
ATOM   901  N  N     . THR   A 1 130 ? 43.101 8.568   9.548  1.00 35.79 ? 127 THR   A N     1 
ATOM   902  C  CA    . THR   A 1 130 ? 41.735 9.146   9.701  1.00 36.49 ? 127 THR   A CA    1 
ATOM   903  C  C     . THR   A 1 130 ? 41.199 9.475   8.308  1.00 35.95 ? 127 THR   A C     1 
ATOM   904  O  O     . THR   A 1 130 ? 40.072 9.104   8.026  1.00 35.24 ? 127 THR   A O     1 
ATOM   905  C  CB    . THR   A 1 130 ? 41.726 10.374  10.617 1.00 38.05 ? 127 THR   A CB    1 
ATOM   906  O  OG1   . THR   A 1 130 ? 42.331 9.972   11.844 1.00 39.82 ? 127 THR   A OG1   1 
ATOM   907  C  CG2   . THR   A 1 130 ? 40.328 10.891  10.877 1.00 39.38 ? 127 THR   A CG2   1 
ATOM   908  N  N     . LYS   A 1 131 ? 41.986 10.123  7.448  1.00 34.16 ? 128 LYS   A N     1 
ATOM   909  C  CA    . LYS   A 1 131 ? 41.514 10.521  6.097  1.00 33.53 ? 128 LYS   A CA    1 
ATOM   910  C  C     . LYS   A 1 131 ? 41.066 9.287   5.299  1.00 31.47 ? 128 LYS   A C     1 
ATOM   911  O  O     . LYS   A 1 131 ? 39.983 9.361   4.676  1.00 32.42 ? 128 LYS   A O     1 
ATOM   912  C  CB    . LYS   A 1 131 ? 42.612 11.265  5.336  1.00 35.88 ? 128 LYS   A CB    1 
ATOM   913  C  CG    . LYS   A 1 131 ? 42.149 11.925  4.046  0.00 35.41 ? 128 LYS   A CG    1 
ATOM   914  C  CD    . LYS   A 1 131 ? 43.176 12.845  3.444  0.00 34.69 ? 128 LYS   A CD    1 
ATOM   915  C  CE    . LYS   A 1 131 ? 42.782 13.386  2.084  0.00 34.85 ? 128 LYS   A CE    1 
ATOM   916  N  NZ    . LYS   A 1 131 ? 43.900 14.113  1.445  0.00 34.61 ? 128 LYS   A NZ    1 
ATOM   917  N  N     . GLN   A 1 132 ? 41.836 8.211   5.324  1.00 30.82 ? 129 GLN   A N     1 
ATOM   918  C  CA    . GLN   A 1 132 ? 41.496 6.977   4.565  1.00 30.10 ? 129 GLN   A CA    1 
ATOM   919  C  C     . GLN   A 1 132 ? 40.119 6.452   4.993  1.00 27.51 ? 129 GLN   A C     1 
ATOM   920  O  O     . GLN   A 1 132 ? 39.321 6.147   4.126  1.00 26.14 ? 129 GLN   A O     1 
ATOM   921  C  CB    . GLN   A 1 132 ? 42.570 5.916   4.765  1.00 31.31 ? 129 GLN   A CB    1 
ATOM   922  C  CG    . GLN   A 1 132 ? 42.338 4.703   3.894  1.00 33.75 ? 129 GLN   A CG    1 
ATOM   923  C  CD    . GLN   A 1 132 ? 43.377 3.627   4.047  1.00 36.01 ? 129 GLN   A CD    1 
ATOM   924  O  OE1   . GLN   A 1 132 ? 44.133 3.609   4.986  1.00 44.39 ? 129 GLN   A OE1   1 
ATOM   925  N  NE2   . GLN   A 1 132 ? 43.360 2.674   3.139  1.00 42.34 ? 129 GLN   A NE2   1 
ATOM   926  N  N     . ALA   A 1 133 ? 39.896 6.368   6.300  1.00 26.47 ? 130 ALA   A N     1 
ATOM   927  C  CA    . ALA   A 1 133 ? 38.612 5.880   6.866  1.00 26.45 ? 130 ALA   A CA    1 
ATOM   928  C  C     . ALA   A 1 133 ? 37.472 6.858   6.556  1.00 26.20 ? 130 ALA   A C     1 
ATOM   929  O  O     . ALA   A 1 133 ? 36.378 6.392   6.203  1.00 26.23 ? 130 ALA   A O     1 
ATOM   930  C  CB    . ALA   A 1 133 ? 38.739 5.649   8.352  1.00 28.35 ? 130 ALA   A CB    1 
ATOM   931  N  N     . GLN   A 1 134 ? 37.723 8.167   6.637  1.00 26.67 ? 131 GLN   A N     1 
ATOM   932  C  CA    . GLN   A 1 134 ? 36.686 9.174   6.314  1.00 29.74 ? 131 GLN   A CA    1 
ATOM   933  C  C     . GLN   A 1 134 ? 36.248 9.006   4.859  1.00 29.32 ? 131 GLN   A C     1 
ATOM   934  O  O     . GLN   A 1 134 ? 35.076 9.002   4.625  1.00 30.55 ? 131 GLN   A O     1 
ATOM   935  C  CB    . GLN   A 1 134 ? 37.191 10.612  6.484  1.00 33.52 ? 131 GLN   A CB    1 
ATOM   936  C  CG    . GLN   A 1 134 ? 37.401 11.049  7.917  1.00 39.28 ? 131 GLN   A CG    1 
ATOM   937  C  CD    . GLN   A 1 134 ? 38.077 12.393  8.055  1.00 42.76 ? 131 GLN   A CD    1 
ATOM   938  O  OE1   . GLN   A 1 134 ? 39.193 12.612  7.614  1.00 50.78 ? 131 GLN   A OE1   1 
ATOM   939  N  NE2   . GLN   A 1 134 ? 37.414 13.294  8.735  1.00 46.42 ? 131 GLN   A NE2   1 
ATOM   940  N  N     . ASP   A 1 135 ? 37.200 8.899   3.937  1.00 29.54 ? 132 ASP   A N     1 
ATOM   941  C  CA    . ASP   A 1 135 ? 36.905 8.716   2.494  1.00 28.05 ? 132 ASP   A CA    1 
ATOM   942  C  C     . ASP   A 1 135 ? 36.132 7.418   2.273  1.00 26.58 ? 132 ASP   A C     1 
ATOM   943  O  O     . ASP   A 1 135 ? 35.204 7.440   1.540  1.00 26.34 ? 132 ASP   A O     1 
ATOM   944  C  CB    . ASP   A 1 135 ? 38.187 8.778   1.667  1.00 30.05 ? 132 ASP   A CB    1 
ATOM   945  C  CG    . ASP   A 1 135 ? 38.784 10.174  1.632  1.00 33.61 ? 132 ASP   A CG    1 
ATOM   946  O  OD1   . ASP   A 1 135 ? 38.030 11.119  1.726  1.00 37.90 ? 132 ASP   A OD1   1 
ATOM   947  O  OD2   . ASP   A 1 135 ? 40.000 10.271  1.540  1.00 40.01 ? 132 ASP   A OD2   1 
ATOM   948  N  N     . LEU   A 1 136 ? 36.535 6.337   2.913  1.00 23.86 ? 133 LEU   A N     1 
ATOM   949  C  CA    . LEU   A 1 136 ? 35.756 5.079   2.752  1.00 22.27 ? 133 LEU   A CA    1 
ATOM   950  C  C     . LEU   A 1 136 ? 34.326 5.299   3.256  1.00 22.05 ? 133 LEU   A C     1 
ATOM   951  O  O     . LEU   A 1 136 ? 33.383 4.841   2.576  1.00 22.76 ? 133 LEU   A O     1 
ATOM   952  C  CB    . LEU   A 1 136 ? 36.445 3.926   3.486  1.00 21.98 ? 133 LEU   A CB    1 
ATOM   953  C  CG    . LEU   A 1 136 ? 35.759 2.569   3.310  1.00 23.98 ? 133 LEU   A CG    1 
ATOM   954  C  CD1   . LEU   A 1 136 ? 35.912 2.071   1.889  1.00 24.14 ? 133 LEU   A CD1   1 
ATOM   955  C  CD2   . LEU   A 1 136 ? 36.277 1.543   4.311  1.00 24.84 ? 133 LEU   A CD2   1 
ATOM   956  N  N     . ALA   A 1 137 ? 34.171 5.887   4.438  1.00 22.84 ? 134 ALA   A N     1 
ATOM   957  C  CA    . ALA   A 1 137 ? 32.819 6.105   4.996  1.00 23.74 ? 134 ALA   A CA    1 
ATOM   958  C  C     . ALA   A 1 137 ? 31.996 6.978   4.048  1.00 26.01 ? 134 ALA   A C     1 
ATOM   959  O  O     . ALA   A 1 137 ? 30.840 6.732   3.906  1.00 27.03 ? 134 ALA   A O     1 
ATOM   960  C  CB    . ALA   A 1 137 ? 32.925 6.701   6.362  1.00 21.90 ? 134 ALA   A CB    1 
ATOM   961  N  N     . ARG   A 1 138 ? 32.630 7.959   3.418  1.00 25.09 ? 135 ARG   A N     1 
ATOM   962  C  CA    . ARG   A 1 138 ? 31.937 8.801   2.418  1.00 27.25 ? 135 ARG   A CA    1 
ATOM   963  C  C     . ARG   A 1 138 ? 31.571 7.925   1.221  1.00 26.57 ? 135 ARG   A C     1 
ATOM   964  O  O     . ARG   A 1 138 ? 30.449 8.065   0.779  1.00 28.15 ? 135 ARG   A O     1 
ATOM   965  C  CB    . ARG   A 1 138 ? 32.859 9.931   1.974  1.00 30.06 ? 135 ARG   A CB    1 
ATOM   966  C  CG    . ARG   A 1 138 ? 32.790 11.167  2.847  1.00 37.35 ? 135 ARG   A CG    1 
ATOM   967  C  CD    . ARG   A 1 138 ? 33.327 12.389  2.135  1.00 42.64 ? 135 ARG   A CD    1 
ATOM   968  N  NE    . ARG   A 1 138 ? 34.756 12.492  2.285  1.00 48.16 ? 135 ARG   A NE    1 
ATOM   969  C  CZ    . ARG   A 1 138 ? 35.343 13.046  3.333  1.00 54.09 ? 135 ARG   A CZ    1 
ATOM   970  N  NH1   . ARG   A 1 138 ? 34.611 13.524  4.323  1.00 57.97 ? 135 ARG   A NH1   1 
ATOM   971  N  NH2   . ARG   A 1 138 ? 36.657 13.123  3.400  1.00 56.38 ? 135 ARG   A NH2   1 
ATOM   972  N  N     A SER   A 1 139 ? 32.293 6.979   0.805  0.50 25.21 ? 136 SER   A N     1 
ATOM   973  N  N     B SER   A 1 139 ? 32.291 6.975   0.788  0.50 25.99 ? 136 SER   A N     1 
ATOM   974  C  CA    A SER   A 1 139 ? 31.967 6.091   -0.339 0.50 24.30 ? 136 SER   A CA    1 
ATOM   975  C  CA    B SER   A 1 139 ? 31.936 6.100   -0.364 0.50 25.25 ? 136 SER   A CA    1 
ATOM   976  C  C     A SER   A 1 139 ? 30.772 5.198   0.015  0.50 24.67 ? 136 SER   A C     1 
ATOM   977  C  C     B SER   A 1 139 ? 30.765 5.183   0.009  0.50 25.01 ? 136 SER   A C     1 
ATOM   978  O  O     A SER   A 1 139 ? 29.838 5.182   -0.763 0.50 28.62 ? 136 SER   A O     1 
ATOM   979  O  O     B SER   A 1 139 ? 29.822 5.165   -0.757 0.50 28.76 ? 136 SER   A O     1 
ATOM   980  C  CB    A SER   A 1 139 ? 33.153 5.250   -0.667 0.50 23.04 ? 136 SER   A CB    1 
ATOM   981  C  CB    B SER   A 1 139 ? 33.119 5.306   -0.847 0.50 25.70 ? 136 SER   A CB    1 
ATOM   982  O  OG    A SER   A 1 139 ? 32.918 4.545   -1.857 0.50 23.17 ? 136 SER   A OG    1 
ATOM   983  O  OG    B SER   A 1 139 ? 33.469 4.301   0.075  0.50 25.66 ? 136 SER   A OG    1 
ATOM   984  N  N     . TYR   A 1 140 ? 30.666 4.836   1.292  1.00 24.32 ? 137 TYR   A N     1 
ATOM   985  C  CA    . TYR   A 1 140 ? 29.560 3.996   1.804  1.00 24.69 ? 137 TYR   A CA    1 
ATOM   986  C  C     . TYR   A 1 140 ? 28.314 4.836   2.163  1.00 26.72 ? 137 TYR   A C     1 
ATOM   987  O  O     . TYR   A 1 140 ? 27.252 4.261   2.333  1.00 27.69 ? 137 TYR   A O     1 
ATOM   988  C  CB    . TYR   A 1 140 ? 30.027 3.270   3.070  1.00 24.20 ? 137 TYR   A CB    1 
ATOM   989  C  CG    . TYR   A 1 140 ? 31.075 2.187   2.928  1.00 24.68 ? 137 TYR   A CG    1 
ATOM   990  C  CD1   . TYR   A 1 140 ? 31.355 1.582   1.722  1.00 23.01 ? 137 TYR   A CD1   1 
ATOM   991  C  CD2   . TYR   A 1 140 ? 31.737 1.722   4.046  1.00 24.68 ? 137 TYR   A CD2   1 
ATOM   992  C  CE1   . TYR   A 1 140 ? 32.303 0.580   1.627  1.00 25.60 ? 137 TYR   A CE1   1 
ATOM   993  C  CE2   . TYR   A 1 140 ? 32.666 0.705   3.975  1.00 24.68 ? 137 TYR   A CE2   1 
ATOM   994  C  CZ    . TYR   A 1 140 ? 32.945 0.128   2.758  1.00 25.82 ? 137 TYR   A CZ    1 
ATOM   995  O  OH    . TYR   A 1 140 ? 33.868 -0.856  2.694  1.00 26.08 ? 137 TYR   A OH    1 
ATOM   996  N  N     . GLY   A 1 141 ? 28.487 6.149   2.336  1.00 25.47 ? 138 GLY   A N     1 
ATOM   997  C  CA    . GLY   A 1 141 ? 27.395 7.062   2.731  1.00 26.21 ? 138 GLY   A CA    1 
ATOM   998  C  C     . GLY   A 1 141 ? 27.023 6.889   4.193  1.00 27.06 ? 138 GLY   A C     1 
ATOM   999  O  O     . GLY   A 1 141 ? 25.809 6.964   4.518  1.00 28.68 ? 138 GLY   A O     1 
ATOM   1000 N  N     . ILE   A 1 142 ? 28.009 6.657   5.065  1.00 24.47 ? 139 ILE   A N     1 
ATOM   1001 C  CA    . ILE   A 1 142 ? 27.776 6.448   6.526  1.00 22.39 ? 139 ILE   A CA    1 
ATOM   1002 C  C     . ILE   A 1 142 ? 28.706 7.338   7.334  1.00 22.53 ? 139 ILE   A C     1 
ATOM   1003 O  O     . ILE   A 1 142 ? 29.780 7.710   6.875  1.00 25.45 ? 139 ILE   A O     1 
ATOM   1004 C  CB    . ILE   A 1 142 ? 27.947 4.971   6.925  1.00 23.97 ? 139 ILE   A CB    1 
ATOM   1005 C  CG1   . ILE   A 1 142 ? 29.390 4.492   6.798  1.00 22.24 ? 139 ILE   A CG1   1 
ATOM   1006 C  CG2   . ILE   A 1 142 ? 26.971 4.089   6.157  1.00 22.76 ? 139 ILE   A CG2   1 
ATOM   1007 C  CD1   . ILE   A 1 142 ? 29.580 3.054   7.196  1.00 22.22 ? 139 ILE   A CD1   1 
ATOM   1008 N  N     . PRO   A 1 143 ? 28.318 7.686   8.584  1.00 22.21 ? 140 PRO   A N     1 
ATOM   1009 C  CA    . PRO   A 1 143 ? 29.208 8.424   9.471  1.00 23.37 ? 140 PRO   A CA    1 
ATOM   1010 C  C     . PRO   A 1 143 ? 30.453 7.619   9.827  1.00 22.38 ? 140 PRO   A C     1 
ATOM   1011 O  O     . PRO   A 1 143 ? 30.429 6.360   9.862  1.00 22.85 ? 140 PRO   A O     1 
ATOM   1012 C  CB    . PRO   A 1 143 ? 28.351 8.689   10.724 1.00 24.80 ? 140 PRO   A CB    1 
ATOM   1013 C  CG    . PRO   A 1 143 ? 26.928 8.492   10.264 1.00 24.51 ? 140 PRO   A CG    1 
ATOM   1014 C  CD    . PRO   A 1 143 ? 27.014 7.416   9.201  1.00 23.43 ? 140 PRO   A CD    1 
ATOM   1015 N  N     . PHE   A 1 144 ? 31.524 8.352   10.106 1.00 25.01 ? 141 PHE   A N     1 
ATOM   1016 C  CA    . PHE   A 1 144 ? 32.782 7.789   10.632 1.00 24.49 ? 141 PHE   A CA    1 
ATOM   1017 C  C     . PHE   A 1 144 ? 33.105 8.510   11.935 1.00 23.70 ? 141 PHE   A C     1 
ATOM   1018 O  O     . PHE   A 1 144 ? 33.058 9.763   11.969 1.00 26.94 ? 141 PHE   A O     1 
ATOM   1019 C  CB    . PHE   A 1 144 ? 33.899 7.910   9.602  1.00 25.09 ? 141 PHE   A CB    1 
ATOM   1020 C  CG    . PHE   A 1 144 ? 35.251 7.602   10.180 1.00 26.04 ? 141 PHE   A CG    1 
ATOM   1021 C  CD1   . PHE   A 1 144 ? 35.482 6.381   10.791 1.00 26.17 ? 141 PHE   A CD1   1 
ATOM   1022 C  CD2   . PHE   A 1 144 ? 36.271 8.541   10.172 1.00 28.48 ? 141 PHE   A CD2   1 
ATOM   1023 C  CE1   . PHE   A 1 144 ? 36.716 6.076   11.339 1.00 24.57 ? 141 PHE   A CE1   1 
ATOM   1024 C  CE2   . PHE   A 1 144 ? 37.499 8.237   10.731 1.00 28.17 ? 141 PHE   A CE2   1 
ATOM   1025 C  CZ    . PHE   A 1 144 ? 37.730 7.004   11.295 1.00 29.18 ? 141 PHE   A CZ    1 
ATOM   1026 N  N     . ILE   A 1 145 ? 33.398 7.731   12.964 1.00 25.73 ? 142 ILE   A N     1 
ATOM   1027 C  CA    . ILE   A 1 145 ? 33.757 8.238   14.320 1.00 27.88 ? 142 ILE   A CA    1 
ATOM   1028 C  C     . ILE   A 1 145 ? 34.977 7.466   14.815 1.00 25.60 ? 142 ILE   A C     1 
ATOM   1029 O  O     . ILE   A 1 145 ? 34.989 6.235   14.702 1.00 26.86 ? 142 ILE   A O     1 
ATOM   1030 C  CB    . ILE   A 1 145 ? 32.560 8.116   15.283 1.00 30.91 ? 142 ILE   A CB    1 
ATOM   1031 C  CG1   . ILE   A 1 145 ? 31.341 8.885   14.771 1.00 35.57 ? 142 ILE   A CG1   1 
ATOM   1032 C  CG2   . ILE   A 1 145 ? 32.954 8.567   16.686 1.00 31.66 ? 142 ILE   A CG2   1 
ATOM   1033 C  CD1   . ILE   A 1 145 ? 30.058 8.501   15.438 1.00 38.33 ? 142 ILE   A CD1   1 
ATOM   1034 N  N     . GLU   A 1 146 ? 35.974 8.178   15.337 1.00 28.35 ? 143 GLU   A N     1 
ATOM   1035 C  CA    . GLU   A 1 146 ? 37.134 7.501   15.953 1.00 28.98 ? 143 GLU   A CA    1 
ATOM   1036 C  C     . GLU   A 1 146 ? 36.859 7.460   17.451 1.00 29.61 ? 143 GLU   A C     1 
ATOM   1037 O  O     . GLU   A 1 146 ? 36.461 8.475   18.003 1.00 31.29 ? 143 GLU   A O     1 
ATOM   1038 C  CB    . GLU   A 1 146 ? 38.460 8.191   15.660 1.00 33.03 ? 143 GLU   A CB    1 
ATOM   1039 C  CG    . GLU   A 1 146 ? 38.909 7.979   14.236 1.00 36.18 ? 143 GLU   A CG    1 
ATOM   1040 C  CD    . GLU   A 1 146 ? 40.370 8.283   14.009 1.00 37.77 ? 143 GLU   A CD    1 
ATOM   1041 O  OE1   . GLU   A 1 146 ? 40.996 8.751   14.937 1.00 38.59 ? 143 GLU   A OE1   1 
ATOM   1042 O  OE2   . GLU   A 1 146 ? 40.858 8.019   12.923 1.00 39.20 ? 143 GLU   A OE2   1 
ATOM   1043 N  N     . THR   A 1 147 ? 37.087 6.307   18.048 1.00 25.95 ? 144 THR   A N     1 
ATOM   1044 C  CA    . THR   A 1 147 ? 36.750 6.101   19.467 1.00 27.60 ? 144 THR   A CA    1 
ATOM   1045 C  C     . THR   A 1 147 ? 37.915 5.482   20.219 1.00 27.74 ? 144 THR   A C     1 
ATOM   1046 O  O     . THR   A 1 147 ? 38.841 5.020   19.618 1.00 26.64 ? 144 THR   A O     1 
ATOM   1047 C  CB    . THR   A 1 147 ? 35.604 5.087   19.630 1.00 25.09 ? 144 THR   A CB    1 
ATOM   1048 O  OG1   . THR   A 1 147 ? 36.008 3.833   19.097 1.00 25.20 ? 144 THR   A OG1   1 
ATOM   1049 C  CG2   . THR   A 1 147 ? 34.309 5.535   19.000 1.00 25.93 ? 144 THR   A CG2   1 
ATOM   1050 N  N     . SER   A 1 148 ? 37.821 5.555   21.533 1.00 29.00 ? 145 SER   A N     1 
ATOM   1051 C  CA    . SER   A 1 148 ? 38.748 4.818   22.407 1.00 29.49 ? 145 SER   A CA    1 
ATOM   1052 C  C     . SER   A 1 148 ? 37.936 4.216   23.559 1.00 26.94 ? 145 SER   A C     1 
ATOM   1053 O  O     . SER   A 1 148 ? 37.408 4.998   24.312 1.00 28.37 ? 145 SER   A O     1 
ATOM   1054 C  CB    . SER   A 1 148 ? 39.834 5.700   22.937 1.00 32.48 ? 145 SER   A CB    1 
ATOM   1055 O  OG    . SER   A 1 148 ? 40.595 4.992   23.878 1.00 31.78 ? 145 SER   A OG    1 
ATOM   1056 N  N     . ALA   A 1 149 ? 37.801 2.889   23.599 1.00 29.65 ? 146 ALA   A N     1 
ATOM   1057 C  CA    . ALA   A 1 149 ? 37.157 2.162   24.717 1.00 29.64 ? 146 ALA   A CA    1 
ATOM   1058 C  C     . ALA   A 1 149 ? 37.983 2.371   25.989 1.00 32.43 ? 146 ALA   A C     1 
ATOM   1059 O  O     . ALA   A 1 149 ? 37.395 2.404   27.080 1.00 35.28 ? 146 ALA   A O     1 
ATOM   1060 C  CB    . ALA   A 1 149 ? 36.993 0.700   24.373 1.00 29.58 ? 146 ALA   A CB    1 
ATOM   1061 N  N     . LYS   A 1 150 ? 39.280 2.578   25.837 1.00 32.50 ? 147 LYS   A N     1 
ATOM   1062 C  CA    . LYS   A 1 150 ? 40.150 2.758   27.018 1.00 34.12 ? 147 LYS   A CA    1 
ATOM   1063 C  C     . LYS   A 1 150 ? 39.865 4.084   27.725 1.00 36.16 ? 147 LYS   A C     1 
ATOM   1064 O  O     . LYS   A 1 150 ? 39.761 4.068   28.926 1.00 40.45 ? 147 LYS   A O     1 
ATOM   1065 C  CB    . LYS   A 1 150 ? 41.609 2.655   26.581 1.00 34.10 ? 147 LYS   A CB    1 
ATOM   1066 C  CG    . LYS   A 1 150 ? 42.595 3.087   27.640 1.00 36.60 ? 147 LYS   A CG    1 
ATOM   1067 C  CD    . LYS   A 1 150 ? 43.997 2.810   27.253 1.00 41.03 ? 147 LYS   A CD    1 
ATOM   1068 C  CE    . LYS   A 1 150 ? 44.437 1.450   27.724 1.00 46.37 ? 147 LYS   A CE    1 
ATOM   1069 N  NZ    . LYS   A 1 150 ? 45.644 1.537   28.569 1.00 48.27 ? 147 LYS   A NZ    1 
ATOM   1070 N  N     . THR   A 1 151 ? 39.678 5.178   27.012 1.00 40.01 ? 148 THR   A N     1 
ATOM   1071 C  CA    . THR   A 1 151 ? 39.463 6.508   27.625 1.00 39.33 ? 148 THR   A CA    1 
ATOM   1072 C  C     . THR   A 1 151 ? 38.000 6.954   27.570 1.00 41.94 ? 148 THR   A C     1 
ATOM   1073 O  O     . THR   A 1 151 ? 37.722 7.998   28.143 1.00 42.26 ? 148 THR   A O     1 
ATOM   1074 C  CB    . THR   A 1 151 ? 40.344 7.552   26.947 1.00 43.03 ? 148 THR   A CB    1 
ATOM   1075 O  OG1   . THR   A 1 151 ? 39.818 7.771   25.643 1.00 41.61 ? 148 THR   A OG1   1 
ATOM   1076 C  CG2   . THR   A 1 151 ? 41.775 7.095   26.825 1.00 42.99 ? 148 THR   A CG2   1 
ATOM   1077 N  N     . ARG   A 1 152 ? 37.158 6.190   26.867 1.00 37.35 ? 149 ARG   A N     1 
ATOM   1078 C  CA    . ARG   A 1 152 ? 35.702 6.426   26.657 1.00 38.96 ? 149 ARG   A CA    1 
ATOM   1079 C  C     . ARG   A 1 152 ? 35.453 7.563   25.657 1.00 42.05 ? 149 ARG   A C     1 
ATOM   1080 O  O     . ARG   A 1 152 ? 34.296 7.942   25.486 1.00 41.57 ? 149 ARG   A O     1 
ATOM   1081 C  CB    . ARG   A 1 152 ? 34.897 6.517   27.957 1.00 42.41 ? 149 ARG   A CB    1 
ATOM   1082 C  CG    . ARG   A 1 152 ? 33.390 6.441   27.755 1.00 47.52 ? 149 ARG   A CG    1 
ATOM   1083 C  CD    . ARG   A 1 152 ? 32.544 6.634   29.009 1.00 53.62 ? 149 ARG   A CD    1 
ATOM   1084 N  NE    . ARG   A 1 152 ? 31.185 6.116   28.911 1.00 59.30 ? 149 ARG   A NE    1 
ATOM   1085 C  CZ    . ARG   A 1 152 ? 30.102 6.848   28.644 1.00 62.83 ? 149 ARG   A CZ    1 
ATOM   1086 N  NH1   . ARG   A 1 152 ? 30.205 8.148   28.430 1.00 62.02 ? 149 ARG   A NH1   1 
ATOM   1087 N  NH2   . ARG   A 1 152 ? 28.915 6.276   28.571 1.00 64.04 ? 149 ARG   A NH2   1 
ATOM   1088 N  N     . GLN   A 1 153 ? 36.498 8.021   24.977 1.00 36.38 ? 150 GLN   A N     1 
ATOM   1089 C  CA    . GLN   A 1 153 ? 36.417 9.106   23.967 1.00 35.60 ? 150 GLN   A CA    1 
ATOM   1090 C  C     . GLN   A 1 153 ? 35.493 8.720   22.802 1.00 31.78 ? 150 GLN   A C     1 
ATOM   1091 O  O     . GLN   A 1 153 ? 35.776 7.728   22.161 1.00 31.68 ? 150 GLN   A O     1 
ATOM   1092 C  CB    . GLN   A 1 153 ? 37.802 9.350   23.386 1.00 38.59 ? 150 GLN   A CB    1 
ATOM   1093 C  CG    . GLN   A 1 153 ? 37.889 10.607  22.549 1.00 42.52 ? 150 GLN   A CG    1 
ATOM   1094 C  CD    . GLN   A 1 153 ? 38.039 11.803  23.451 1.00 50.05 ? 150 GLN   A CD    1 
ATOM   1095 O  OE1   . GLN   A 1 153 ? 38.905 11.835  24.316 1.00 58.70 ? 150 GLN   A OE1   1 
ATOM   1096 N  NE2   . GLN   A 1 153 ? 37.182 12.790  23.255 1.00 55.84 ? 150 GLN   A NE2   1 
ATOM   1097 N  N     . ARG   A 1 154 ? 34.384 9.441   22.652 1.00 33.10 ? 151 ARG   A N     1 
ATOM   1098 C  CA    . ARG   A 1 154 ? 33.382 9.325   21.558 1.00 30.94 ? 151 ARG   A CA    1 
ATOM   1099 C  C     . ARG   A 1 154 ? 32.639 7.982   21.555 1.00 29.78 ? 151 ARG   A C     1 
ATOM   1100 O  O     . ARG   A 1 154 ? 32.017 7.711   20.581 1.00 27.72 ? 151 ARG   A O     1 
ATOM   1101 C  CB    . ARG   A 1 154 ? 34.032 9.590   20.197 1.00 32.15 ? 151 ARG   A CB    1 
ATOM   1102 C  CG    . ARG   A 1 154 ? 34.715 10.945  20.075 1.00 35.52 ? 151 ARG   A CG    1 
ATOM   1103 C  CD    . ARG   A 1 154 ? 34.558 11.548  18.699 1.00 40.29 ? 151 ARG   A CD    1 
ATOM   1104 N  NE    . ARG   A 1 154 ? 33.211 12.032  18.498 1.00 43.31 ? 151 ARG   A NE    1 
ATOM   1105 C  CZ    . ARG   A 1 154 ? 32.768 12.564  17.383 1.00 45.29 ? 151 ARG   A CZ    1 
ATOM   1106 N  NH1   . ARG   A 1 154 ? 33.580 12.684  16.357 1.00 48.87 ? 151 ARG   A NH1   1 
ATOM   1107 N  NH2   . ARG   A 1 154 ? 31.522 12.952  17.274 1.00 45.05 ? 151 ARG   A NH2   1 
ATOM   1108 N  N     . VAL   A 1 155 ? 32.634 7.236   22.650 1.00 27.81 ? 152 VAL   A N     1 
ATOM   1109 C  CA    . VAL   A 1 155 ? 31.921 5.929   22.677 1.00 26.65 ? 152 VAL   A CA    1 
ATOM   1110 C  C     . VAL   A 1 155 ? 30.417 6.199   22.631 1.00 27.13 ? 152 VAL   A C     1 
ATOM   1111 O  O     . VAL   A 1 155 ? 29.738 5.593   21.855 1.00 25.46 ? 152 VAL   A O     1 
ATOM   1112 C  CB    . VAL   A 1 155 ? 32.328 5.080   23.893 1.00 26.65 ? 152 VAL   A CB    1 
ATOM   1113 C  CG1   . VAL   A 1 155 ? 31.509 3.815   23.972 1.00 26.54 ? 152 VAL   A CG1   1 
ATOM   1114 C  CG2   . VAL   A 1 155 ? 33.808 4.739   23.884 1.00 27.48 ? 152 VAL   A CG2   1 
ATOM   1115 N  N     . GLU   A 1 156 ? 29.925 7.092   23.467 1.00 27.43 ? 153 GLU   A N     1 
ATOM   1116 C  CA    . GLU   A 1 156 ? 28.484 7.416   23.423 1.00 30.40 ? 153 GLU   A CA    1 
ATOM   1117 C  C     . GLU   A 1 156 ? 28.114 7.978   22.042 1.00 28.46 ? 153 GLU   A C     1 
ATOM   1118 O  O     . GLU   A 1 156 ? 27.105 7.570   21.507 1.00 27.97 ? 153 GLU   A O     1 
ATOM   1119 C  CB    . GLU   A 1 156 ? 28.189 8.382   24.564 1.00 34.34 ? 153 GLU   A CB    1 
ATOM   1120 C  CG    . GLU   A 1 156 ? 26.739 8.541   24.861 1.00 40.08 ? 153 GLU   A CG    1 
ATOM   1121 C  CD    . GLU   A 1 156 ? 26.572 9.795   25.696 1.00 45.91 ? 153 GLU   A CD    1 
ATOM   1122 O  OE1   . GLU   A 1 156 ? 26.987 9.772   26.844 1.00 51.22 ? 153 GLU   A OE1   1 
ATOM   1123 O  OE2   . GLU   A 1 156 ? 26.108 10.808  25.146 1.00 52.69 ? 153 GLU   A OE2   1 
ATOM   1124 N  N     . ASP   A 1 157 ? 28.947 8.866   21.510 1.00 27.37 ? 154 ASP   A N     1 
ATOM   1125 C  CA    . ASP   A 1 157 ? 28.708 9.483   20.185 1.00 29.61 ? 154 ASP   A CA    1 
ATOM   1126 C  C     . ASP   A 1 157 ? 28.552 8.399   19.113 1.00 27.50 ? 154 ASP   A C     1 
ATOM   1127 O  O     . ASP   A 1 157 ? 27.684 8.538   18.289 1.00 27.47 ? 154 ASP   A O     1 
ATOM   1128 C  CB    . ASP   A 1 157 ? 29.815 10.456  19.780 1.00 34.56 ? 154 ASP   A CB    1 
ATOM   1129 C  CG    . ASP   A 1 157 ? 29.927 11.689  20.650 1.00 39.05 ? 154 ASP   A CG    1 
ATOM   1130 O  OD1   . ASP   A 1 157 ? 28.952 12.023  21.319 1.00 43.37 ? 154 ASP   A OD1   1 
ATOM   1131 O  OD2   . ASP   A 1 157 ? 31.005 12.266  20.658 1.00 45.13 ? 154 ASP   A OD2   1 
ATOM   1132 N  N     . ALA   A 1 158 ? 29.356 7.344   19.179 1.00 24.51 ? 155 ALA   A N     1 
ATOM   1133 C  CA    . ALA   A 1 158 ? 29.279 6.252   18.177 1.00 26.00 ? 155 ALA   A CA    1 
ATOM   1134 C  C     . ALA   A 1 158 ? 27.916 5.569   18.282 1.00 24.01 ? 155 ALA   A C     1 
ATOM   1135 O  O     . ALA   A 1 158 ? 27.239 5.477   17.280 1.00 24.20 ? 155 ALA   A O     1 
ATOM   1136 C  CB    . ALA   A 1 158 ? 30.398 5.268   18.348 1.00 26.31 ? 155 ALA   A CB    1 
ATOM   1137 N  N     . PHE   A 1 159 ? 27.516 5.110   19.468 1.00 21.85 ? 156 PHE   A N     1 
ATOM   1138 C  CA    . PHE   A 1 159 ? 26.235 4.381   19.640 1.00 21.75 ? 156 PHE   A CA    1 
ATOM   1139 C  C     . PHE   A 1 159 ? 25.061 5.332   19.353 1.00 22.74 ? 156 PHE   A C     1 
ATOM   1140 O  O     . PHE   A 1 159 ? 24.076 4.931   18.729 1.00 24.36 ? 156 PHE   A O     1 
ATOM   1141 C  CB    . PHE   A 1 159 ? 26.164 3.738   21.029 1.00 21.88 ? 156 PHE   A CB    1 
ATOM   1142 C  CG    . PHE   A 1 159 ? 27.008 2.499   21.200 1.00 22.29 ? 156 PHE   A CG    1 
ATOM   1143 C  CD1   . PHE   A 1 159 ? 26.497 1.257   20.858 1.00 21.84 ? 156 PHE   A CD1   1 
ATOM   1144 C  CD2   . PHE   A 1 159 ? 28.282 2.555   21.730 1.00 22.31 ? 156 PHE   A CD2   1 
ATOM   1145 C  CE1   . PHE   A 1 159 ? 27.235 0.103   21.053 1.00 23.04 ? 156 PHE   A CE1   1 
ATOM   1146 C  CE2   . PHE   A 1 159 ? 29.025 1.398   21.909 1.00 23.13 ? 156 PHE   A CE2   1 
ATOM   1147 C  CZ    . PHE   A 1 159 ? 28.502 0.176   21.567 1.00 23.27 ? 156 PHE   A CZ    1 
ATOM   1148 N  N     . TYR   A 1 160 ? 25.111 6.549   19.878 1.00 23.21 ? 157 TYR   A N     1 
ATOM   1149 C  CA    . TYR   A 1 160 ? 24.000 7.527   19.721 1.00 24.78 ? 157 TYR   A CA    1 
ATOM   1150 C  C     . TYR   A 1 160 ? 23.861 7.968   18.256 1.00 24.99 ? 157 TYR   A C     1 
ATOM   1151 O  O     . TYR   A 1 160 ? 22.765 8.126   17.796 1.00 26.35 ? 157 TYR   A O     1 
ATOM   1152 C  CB    . TYR   A 1 160 ? 24.258 8.679   20.680 1.00 30.30 ? 157 TYR   A CB    1 
ATOM   1153 C  CG    . TYR   A 1 160 ? 23.970 8.407   22.130 1.00 32.32 ? 157 TYR   A CG    1 
ATOM   1154 C  CD1   . TYR   A 1 160 ? 23.869 7.135   22.650 1.00 32.27 ? 157 TYR   A CD1   1 
ATOM   1155 C  CD2   . TYR   A 1 160 ? 23.823 9.471   22.985 1.00 37.84 ? 157 TYR   A CD2   1 
ATOM   1156 C  CE1   . TYR   A 1 160 ? 23.620 6.940   23.994 1.00 39.77 ? 157 TYR   A CE1   1 
ATOM   1157 C  CE2   . TYR   A 1 160 ? 23.573 9.295   24.323 1.00 41.03 ? 157 TYR   A CE2   1 
ATOM   1158 C  CZ    . TYR   A 1 160 ? 23.460 8.031   24.829 1.00 42.71 ? 157 TYR   A CZ    1 
ATOM   1159 O  OH    . TYR   A 1 160 ? 23.187 7.924   26.157 1.00 47.81 ? 157 TYR   A OH    1 
ATOM   1160 N  N     . THR   A 1 161 ? 24.975 8.125   17.552 1.00 26.66 ? 158 THR   A N     1 
ATOM   1161 C  CA    . THR   A 1 161 ? 24.944 8.420   16.100 1.00 23.77 ? 158 THR   A CA    1 
ATOM   1162 C  C     . THR   A 1 161 ? 24.232 7.268   15.394 1.00 21.17 ? 158 THR   A C     1 
ATOM   1163 O  O     . THR   A 1 161 ? 23.411 7.525   14.515 1.00 24.47 ? 158 THR   A O     1 
ATOM   1164 C  CB    . THR   A 1 161 ? 26.349 8.683   15.554 1.00 24.27 ? 158 THR   A CB    1 
ATOM   1165 O  OG1   . THR   A 1 161 ? 26.788 9.869   16.217 1.00 28.72 ? 158 THR   A OG1   1 
ATOM   1166 C  CG2   . THR   A 1 161 ? 26.397 8.871   14.054 1.00 27.20 ? 158 THR   A CG2   1 
ATOM   1167 N  N     . LEU   A 1 162 ? 24.538 6.029   15.777 1.00 21.52 ? 159 LEU   A N     1 
ATOM   1168 C  CA    . LEU   A 1 162 ? 23.922 4.853   15.125 1.00 20.08 ? 159 LEU   A CA    1 
ATOM   1169 C  C     . LEU   A 1 162 ? 22.411 4.906   15.372 1.00 21.13 ? 159 LEU   A C     1 
ATOM   1170 O  O     . LEU   A 1 162 ? 21.650 4.637   14.443 1.00 21.71 ? 159 LEU   A O     1 
ATOM   1171 C  CB    . LEU   A 1 162 ? 24.544 3.548   15.640 1.00 19.95 ? 159 LEU   A CB    1 
ATOM   1172 C  CG    . LEU   A 1 162 ? 23.936 2.284   15.037 1.00 19.48 ? 159 LEU   A CG    1 
ATOM   1173 C  CD1   . LEU   A 1 162 ? 24.019 2.294   13.519 1.00 21.81 ? 159 LEU   A CD1   1 
ATOM   1174 C  CD2   . LEU   A 1 162 ? 24.567 1.025   15.641 1.00 20.77 ? 159 LEU   A CD2   1 
ATOM   1175 N  N     . VAL   A 1 163 ? 21.983 5.225   16.592 1.00 21.94 ? 160 VAL   A N     1 
ATOM   1176 C  CA    . VAL   A 1 163 ? 20.523 5.345   16.879 1.00 23.10 ? 160 VAL   A CA    1 
ATOM   1177 C  C     . VAL   A 1 163 ? 19.942 6.464   16.001 1.00 23.02 ? 160 VAL   A C     1 
ATOM   1178 O  O     . VAL   A 1 163 ? 18.865 6.239   15.426 1.00 25.57 ? 160 VAL   A O     1 
ATOM   1179 C  CB    . VAL   A 1 163 ? 20.230 5.598   18.366 1.00 23.95 ? 160 VAL   A CB    1 
ATOM   1180 C  CG1   . VAL   A 1 163 ? 18.763 5.935   18.600 1.00 26.50 ? 160 VAL   A CG1   1 
ATOM   1181 C  CG2   . VAL   A 1 163 ? 20.648 4.417   19.217 1.00 26.90 ? 160 VAL   A CG2   1 
ATOM   1182 N  N     . ARG   A 1 164 ? 20.641 7.588   15.846 1.00 23.26 ? 161 ARG   A N     1 
ATOM   1183 C  CA    . ARG   A 1 164 ? 20.162 8.685   14.955 1.00 23.38 ? 161 ARG   A CA    1 
ATOM   1184 C  C     . ARG   A 1 164 ? 20.069 8.206   13.502 1.00 25.38 ? 161 ARG   A C     1 
ATOM   1185 O  O     . ARG   A 1 164 ? 19.131 8.629   12.802 1.00 28.84 ? 161 ARG   A O     1 
ATOM   1186 C  CB    . ARG   A 1 164 ? 21.049 9.921   15.081 1.00 28.36 ? 161 ARG   A CB    1 
ATOM   1187 C  CG    . ARG   A 1 164 ? 20.934 10.584  16.441 1.00 30.88 ? 161 ARG   A CG    1 
ATOM   1188 C  CD    . ARG   A 1 164 ? 21.681 11.899  16.459 1.00 35.80 ? 161 ARG   A CD    1 
ATOM   1189 N  NE    . ARG   A 1 164 ? 21.485 12.652  17.686 1.00 40.03 ? 161 ARG   A NE    1 
ATOM   1190 C  CZ    . ARG   A 1 164 ? 22.284 12.630  18.749 1.00 45.59 ? 161 ARG   A CZ    1 
ATOM   1191 N  NH1   . ARG   A 1 164 ? 23.369 11.872  18.772 1.00 47.10 ? 161 ARG   A NH1   1 
ATOM   1192 N  NH2   . ARG   A 1 164 ? 21.988 13.388  19.793 1.00 51.86 ? 161 ARG   A NH2   1 
ATOM   1193 N  N     . GLU   A 1 165 ? 20.971 7.332   13.056 1.00 23.83 ? 162 GLU   A N     1 
ATOM   1194 C  CA    . GLU   A 1 165 ? 20.937 6.781   11.673 1.00 25.30 ? 162 GLU   A CA    1 
ATOM   1195 C  C     . GLU   A 1 165 ? 19.716 5.874   11.513 1.00 25.60 ? 162 GLU   A C     1 
ATOM   1196 O  O     . GLU   A 1 165 ? 19.114 5.892   10.423 1.00 25.12 ? 162 GLU   A O     1 
ATOM   1197 C  CB    . GLU   A 1 165 ? 22.206 6.002   11.313 1.00 22.81 ? 162 GLU   A CB    1 
ATOM   1198 C  CG    . GLU   A 1 165 ? 23.400 6.907   11.047 1.00 25.17 ? 162 GLU   A CG    1 
ATOM   1199 C  CD    . GLU   A 1 165 ? 23.239 7.799   9.826  1.00 28.66 ? 162 GLU   A CD    1 
ATOM   1200 O  OE1   . GLU   A 1 165 ? 23.243 7.272   8.701  1.00 33.10 ? 162 GLU   A OE1   1 
ATOM   1201 O  OE2   . GLU   A 1 165 ? 23.095 9.015   10.003 1.00 34.67 ? 162 GLU   A OE2   1 
ATOM   1202 N  N     . ILE   A 1 166 ? 19.385 5.084   12.538 1.00 23.04 ? 163 ILE   A N     1 
ATOM   1203 C  CA    . ILE   A 1 166 ? 18.195 4.190   12.499 1.00 22.93 ? 163 ILE   A CA    1 
ATOM   1204 C  C     . ILE   A 1 166 ? 16.952 5.083   12.418 1.00 27.75 ? 163 ILE   A C     1 
ATOM   1205 O  O     . ILE   A 1 166 ? 16.082 4.805   11.584 1.00 28.56 ? 163 ILE   A O     1 
ATOM   1206 C  CB    . ILE   A 1 166 ? 18.151 3.226   13.700 1.00 24.01 ? 163 ILE   A CB    1 
ATOM   1207 C  CG1   . ILE   A 1 166 ? 19.343 2.267   13.677 1.00 22.03 ? 163 ILE   A CG1   1 
ATOM   1208 C  CG2   . ILE   A 1 166 ? 16.848 2.443   13.748 1.00 27.16 ? 163 ILE   A CG2   1 
ATOM   1209 C  CD1   . ILE   A 1 166 ? 19.570 1.553   14.980 1.00 24.43 ? 163 ILE   A CD1   1 
ATOM   1210 N  N     . ARG   A 1 167 ? 16.879 6.127   13.226 1.00 25.89 ? 164 ARG   A N     1 
ATOM   1211 C  CA    . ARG   A 1 167 ? 15.675 6.994   13.222 1.00 29.14 ? 164 ARG   A CA    1 
ATOM   1212 C  C     . ARG   A 1 167 ? 15.527 7.668   11.871 1.00 32.29 ? 164 ARG   A C     1 
ATOM   1213 O  O     . ARG   A 1 167 ? 14.429 7.746   11.394 1.00 36.54 ? 164 ARG   A O     1 
ATOM   1214 C  CB    . ARG   A 1 167 ? 15.788 8.066   14.296 1.00 32.78 ? 164 ARG   A CB    1 
ATOM   1215 C  CG    . ARG   A 1 167 ? 15.641 7.497   15.688 1.00 33.54 ? 164 ARG   A CG    1 
ATOM   1216 C  CD    . ARG   A 1 167 ? 15.933 8.530   16.734 1.00 40.18 ? 164 ARG   A CD    1 
ATOM   1217 N  NE    . ARG   A 1 167 ? 15.571 8.035   18.041 1.00 36.57 ? 164 ARG   A NE    1 
ATOM   1218 C  CZ    . ARG   A 1 167 ? 15.695 8.747   19.142 1.00 39.34 ? 164 ARG   A CZ    1 
ATOM   1219 N  NH1   . ARG   A 1 167 ? 15.334 8.236   20.300 1.00 41.67 ? 164 ARG   A NH1   1 
ATOM   1220 N  NH2   . ARG   A 1 167 ? 16.180 9.962   19.082 1.00 45.45 ? 164 ARG   A NH2   1 
ATOM   1221 N  N     . GLN   A 1 168 ? 16.623 8.131   11.304 1.00 32.78 ? 165 GLN   A N     1 
ATOM   1222 C  CA    . GLN   A 1 168 ? 16.570 8.815   9.980  1.00 33.27 ? 165 GLN   A CA    1 
ATOM   1223 C  C     . GLN   A 1 168 ? 16.114 7.823   8.907  1.00 33.04 ? 165 GLN   A C     1 
ATOM   1224 O  O     . GLN   A 1 168 ? 15.369 8.210   8.015  1.00 35.94 ? 165 GLN   A O     1 
ATOM   1225 C  CB    . GLN   A 1 168 ? 17.912 9.473   9.646  1.00 35.77 ? 165 GLN   A CB    1 
ATOM   1226 C  CG    . GLN   A 1 168 ? 17.868 10.300  8.379  0.00 34.97 ? 165 GLN   A CG    1 
ATOM   1227 C  CD    . GLN   A 1 168 ? 19.074 11.131  8.020  0.00 34.70 ? 165 GLN   A CD    1 
ATOM   1228 O  OE1   . GLN   A 1 168 ? 20.045 11.220  8.769  0.00 34.61 ? 165 GLN   A OE1   1 
ATOM   1229 N  NE2   . GLN   A 1 168 ? 19.044 11.703  6.823  0.00 34.70 ? 165 GLN   A NE2   1 
ATOM   1230 N  N     . TYR   A 1 169 ? 16.564 6.582   8.999  1.00 32.93 ? 166 TYR   A N     1 
ATOM   1231 C  CA    . TYR   A 1 169 ? 16.167 5.478   8.086  1.00 31.39 ? 166 TYR   A CA    1 
ATOM   1232 C  C     . TYR   A 1 169 ? 14.668 5.194   8.229  1.00 36.68 ? 166 TYR   A C     1 
ATOM   1233 O  O     . TYR   A 1 169 ? 14.013 4.994   7.193  1.00 39.81 ? 166 TYR   A O     1 
ATOM   1234 C  CB    . TYR   A 1 169 ? 17.028 4.241   8.366  1.00 32.51 ? 166 TYR   A CB    1 
ATOM   1235 C  CG    . TYR   A 1 169 ? 16.648 3.006   7.594  1.00 36.95 ? 166 TYR   A CG    1 
ATOM   1236 C  CD1   . TYR   A 1 169 ? 17.039 2.838   6.275  1.00 41.29 ? 166 TYR   A CD1   1 
ATOM   1237 C  CD2   . TYR   A 1 169 ? 15.922 1.989   8.192  1.00 42.18 ? 166 TYR   A CD2   1 
ATOM   1238 C  CE1   . TYR   A 1 169 ? 16.704 1.694   5.564  1.00 46.71 ? 166 TYR   A CE1   1 
ATOM   1239 C  CE2   . TYR   A 1 169 ? 15.576 0.842   7.497  1.00 47.29 ? 166 TYR   A CE2   1 
ATOM   1240 C  CZ    . TYR   A 1 169 ? 15.967 0.695   6.177  1.00 47.83 ? 166 TYR   A CZ    1 
ATOM   1241 O  OH    . TYR   A 1 169 ? 15.627 -0.431  5.483  1.00 50.53 ? 166 TYR   A OH    1 
ATOM   1242 N  N     . ARG   A 1 170 ? 14.167 5.222   9.461  1.00 38.06 ? 167 ARG   A N     1 
ATOM   1243 C  CA    . ARG   A 1 170 ? 12.746 4.896   9.758  1.00 39.11 ? 167 ARG   A CA    1 
ATOM   1244 C  C     . ARG   A 1 170 ? 11.821 5.993   9.208  1.00 44.83 ? 167 ARG   A C     1 
ATOM   1245 O  O     . ARG   A 1 170 ? 10.625 5.731   9.111  1.00 42.85 ? 167 ARG   A O     1 
ATOM   1246 C  CB    . ARG   A 1 170 ? 12.538 4.632   11.249 1.00 38.37 ? 167 ARG   A CB    1 
ATOM   1247 C  CG    . ARG   A 1 170 ? 12.809 3.202   11.694 1.00 40.78 ? 167 ARG   A CG    1 
ATOM   1248 C  CD    . ARG   A 1 170 ? 12.909 3.109   13.200 1.00 39.77 ? 167 ARG   A CD    1 
ATOM   1249 N  NE    . ARG   A 1 170 ? 13.198 1.799   13.757 1.00 41.58 ? 167 ARG   A NE    1 
ATOM   1250 C  CZ    . ARG   A 1 170 ? 13.168 1.524   15.050 1.00 45.60 ? 167 ARG   A CZ    1 
ATOM   1251 N  NH1   . ARG   A 1 170 ? 12.825 2.452   15.915 1.00 49.37 ? 167 ARG   A NH1   1 
ATOM   1252 N  NH2   . ARG   A 1 170 ? 13.438 0.312   15.487 1.00 50.34 ? 167 ARG   A NH2   1 
ATOM   1253 N  N     . LEU   A 1 171 ? 12.354 7.170   8.881  1.00 46.03 ? 168 LEU   A N     1 
ATOM   1254 C  CA    . LEU   A 1 171 ? 11.522 8.261   8.313  1.00 51.52 ? 168 LEU   A CA    1 
ATOM   1255 C  C     . LEU   A 1 171 ? 11.512 8.173   6.783  1.00 54.45 ? 168 LEU   A C     1 
ATOM   1256 O  O     . LEU   A 1 171 ? 10.815 8.980   6.159  1.00 56.93 ? 168 LEU   A O     1 
ATOM   1257 C  CB    . LEU   A 1 171 ? 12.046 9.609   8.799  1.00 54.99 ? 168 LEU   A CB    1 
ATOM   1258 C  CG    . LEU   A 1 171 ? 12.082 9.769   10.317 1.00 57.41 ? 168 LEU   A CG    1 
ATOM   1259 C  CD1   . LEU   A 1 171 ? 12.216 11.220  10.727 1.00 64.32 ? 168 LEU   A CD1   1 
ATOM   1260 C  CD2   . LEU   A 1 171 ? 10.864 9.150   10.981 1.00 56.59 ? 168 LEU   A CD2   1 
ATOM   1261 N  N     . LYS   A 1 172 ? 12.221 7.191   6.217  1.00 53.56 ? 169 LYS   A N     1 
ATOM   1262 C  CA    . LYS   A 1 172 ? 12.330 6.996   4.744  1.00 58.82 ? 169 LYS   A CA    1 
ATOM   1263 C  C     . LYS   A 1 172 ? 11.207 6.075   4.246  1.00 67.48 ? 169 LYS   A C     1 
ATOM   1264 O  O     . LYS   A 1 172 ? 11.072 5.905   3.055  1.00 72.10 ? 169 LYS   A O     1 
ATOM   1265 C  CB    . LYS   A 1 172 ? 13.720 6.464   4.369  1.00 58.01 ? 169 LYS   A CB    1 
ATOM   1266 C  CG    . LYS   A 1 172 ? 14.852 7.475   4.511  1.00 59.53 ? 169 LYS   A CG    1 
ATOM   1267 C  CD    . LYS   A 1 172 ? 16.253 7.009   4.129  1.00 60.84 ? 169 LYS   A CD    1 
ATOM   1268 C  CE    . LYS   A 1 172 ? 17.329 7.985   4.565  1.00 63.39 ? 169 LYS   A CE    1 
ATOM   1269 N  NZ    . LYS   A 1 172 ? 18.218 7.431   5.616  1.00 60.38 ? 169 LYS   A NZ    1 
ATOM   1270 O  OXT   . LYS   A 1 172 ? 10.474 5.549   5.091  1.00 75.58 ? 169 LYS   A OXT   1 
HETATM 1271 P  PG    . GNP   B 2 .   ? 36.816 -10.702 20.047 1.00 28.18 ? 201 GNP   A PG    1 
HETATM 1272 O  O1G   . GNP   B 2 .   ? 35.594 -10.969 20.777 1.00 29.50 ? 201 GNP   A O1G   1 
HETATM 1273 O  O2G   . GNP   B 2 .   ? 37.767 -11.838 20.327 1.00 30.73 ? 201 GNP   A O2G   1 
HETATM 1274 O  O3G   . GNP   B 2 .   ? 36.590 -10.693 18.650 1.00 28.43 ? 201 GNP   A O3G   1 
HETATM 1275 N  N3B   . GNP   B 2 .   ? 37.515 -9.346  20.595 1.00 27.41 ? 201 GNP   A N3B   1 
HETATM 1276 P  PB    . GNP   B 2 .   ? 36.852 -7.856  20.647 1.00 24.62 ? 201 GNP   A PB    1 
HETATM 1277 O  O1B   . GNP   B 2 .   ? 36.768 -7.237  19.327 1.00 22.77 ? 201 GNP   A O1B   1 
HETATM 1278 O  O2B   . GNP   B 2 .   ? 35.650 -7.869  21.500 1.00 24.87 ? 201 GNP   A O2B   1 
HETATM 1279 O  O3A   . GNP   B 2 .   ? 37.897 -6.952  21.450 1.00 24.65 ? 201 GNP   A O3A   1 
HETATM 1280 P  PA    . GNP   B 2 .   ? 38.122 -6.773  23.005 1.00 26.24 ? 201 GNP   A PA    1 
HETATM 1281 O  O1A   . GNP   B 2 .   ? 38.215 -8.091  23.617 1.00 29.36 ? 201 GNP   A O1A   1 
HETATM 1282 O  O2A   . GNP   B 2 .   ? 37.178 -5.799  23.565 1.00 26.38 ? 201 GNP   A O2A   1 
HETATM 1283 O  "O5'" . GNP   B 2 .   ? 39.556 -6.079  23.041 1.00 27.28 ? 201 GNP   A "O5'" 1 
HETATM 1284 C  "C5'" . GNP   B 2 .   ? 40.716 -6.731  22.505 1.00 30.70 ? 201 GNP   A "C5'" 1 
HETATM 1285 C  "C4'" . GNP   B 2 .   ? 41.923 -6.115  23.172 1.00 30.59 ? 201 GNP   A "C4'" 1 
HETATM 1286 O  "O4'" . GNP   B 2 .   ? 41.999 -4.714  22.837 1.00 29.04 ? 201 GNP   A "O4'" 1 
HETATM 1287 C  "C3'" . GNP   B 2 .   ? 41.905 -6.161  24.697 1.00 31.76 ? 201 GNP   A "C3'" 1 
HETATM 1288 O  "O3'" . GNP   B 2 .   ? 43.240 -6.313  25.158 1.00 36.98 ? 201 GNP   A "O3'" 1 
HETATM 1289 C  "C2'" . GNP   B 2 .   ? 41.333 -4.791  25.049 1.00 33.91 ? 201 GNP   A "C2'" 1 
HETATM 1290 O  "O2'" . GNP   B 2 .   ? 41.691 -4.390  26.341 1.00 36.48 ? 201 GNP   A "O2'" 1 
HETATM 1291 C  "C1'" . GNP   B 2 .   ? 41.990 -3.925  23.996 1.00 30.40 ? 201 GNP   A "C1'" 1 
HETATM 1292 N  N9    . GNP   B 2 .   ? 41.291 -2.687  23.691 1.00 28.28 ? 201 GNP   A N9    1 
HETATM 1293 C  C8    . GNP   B 2 .   ? 39.968 -2.564  23.362 1.00 26.04 ? 201 GNP   A C8    1 
HETATM 1294 N  N7    . GNP   B 2 .   ? 39.624 -1.346  23.078 1.00 26.29 ? 201 GNP   A N7    1 
HETATM 1295 C  C5    . GNP   B 2 .   ? 40.773 -0.600  23.246 1.00 27.44 ? 201 GNP   A C5    1 
HETATM 1296 C  C6    . GNP   B 2 .   ? 40.988 0.788   23.084 1.00 27.94 ? 201 GNP   A C6    1 
HETATM 1297 O  O6    . GNP   B 2 .   ? 40.217 1.669   22.725 1.00 29.07 ? 201 GNP   A O6    1 
HETATM 1298 N  N1    . GNP   B 2 .   ? 42.309 1.130   23.335 1.00 31.73 ? 201 GNP   A N1    1 
HETATM 1299 C  C2    . GNP   B 2 .   ? 43.267 0.237   23.719 1.00 32.07 ? 201 GNP   A C2    1 
HETATM 1300 N  N2    . GNP   B 2 .   ? 44.486 0.755   23.912 1.00 36.10 ? 201 GNP   A N2    1 
HETATM 1301 N  N3    . GNP   B 2 .   ? 43.081 -1.067  23.866 1.00 32.98 ? 201 GNP   A N3    1 
HETATM 1302 C  C4    . GNP   B 2 .   ? 41.800 -1.422  23.628 1.00 28.59 ? 201 GNP   A C4    1 
HETATM 1303 MG MG    . MG    C 3 .   ? 34.620 -9.642  22.277 1.00 23.02 ? 202 MG    A MG    1 
HETATM 1304 CO CO    . CO    D 4 .   ? 38.384 -3.395  35.813 1.00 71.93 ? 203 CO    A CO    1 
HETATM 1305 CO CO    . CO    E 4 .   ? 33.360 -8.877  -1.452 1.00 26.99 ? 204 CO    A CO    1 
HETATM 1306 C  CBK   . A1ILF F 5 .   ? 22.573 -15.533 24.732 1.00 45.94 ? 205 A1ILF A CBK   1 
HETATM 1307 C  CBL   . A1ILF F 5 .   ? 22.845 -16.364 26.022 1.00 46.61 ? 205 A1ILF A CBL   1 
HETATM 1308 C  CBM   . A1ILF F 5 .   ? 24.191 -17.092 26.032 1.00 46.68 ? 205 A1ILF A CBM   1 
HETATM 1309 N  NBV   . A1ILF F 5 .   ? 25.351 -16.225 26.194 1.00 48.63 ? 205 A1ILF A NBV   1 
HETATM 1310 C  CBN   . A1ILF F 5 .   ? 24.352 -17.799 24.778 1.00 45.21 ? 205 A1ILF A CBN   1 
HETATM 1311 C  CBO   . A1ILF F 5 .   ? 24.288 -16.756 23.671 1.00 45.14 ? 205 A1ILF A CBO   1 
HETATM 1312 C  CBJ   . A1ILF F 5 .   ? 22.910 -16.321 23.516 1.00 42.20 ? 205 A1ILF A CBJ   1 
HETATM 1313 N  NAQ   . A1ILF F 5 .   ? 22.819 -15.534 22.249 1.00 36.39 ? 205 A1ILF A NAQ   1 
HETATM 1314 C  CAB   . A1ILF F 5 .   ? 22.393 -16.150 21.136 1.00 35.62 ? 205 A1ILF A CAB   1 
HETATM 1315 O  OAA   . A1ILF F 5 .   ? 22.006 -17.306 21.248 1.00 39.68 ? 205 A1ILF A OAA   1 
HETATM 1316 C  CAR   . A1ILF F 5 .   ? 23.242 -14.121 22.213 1.00 34.07 ? 205 A1ILF A CAR   1 
HETATM 1317 C  CAS   . A1ILF F 5 .   ? 22.243 -13.137 22.776 1.00 34.45 ? 205 A1ILF A CAS   1 
HETATM 1318 C  CAT   . A1ILF F 5 .   ? 21.023 -12.888 21.879 1.00 30.91 ? 205 A1ILF A CAT   1 
HETATM 1319 C  CAU   . A1ILF F 5 .   ? 20.246 -11.711 22.390 1.00 31.32 ? 205 A1ILF A CAU   1 
HETATM 1320 C  CAV   . A1ILF F 5 .   ? 18.963 -11.422 21.616 1.00 32.23 ? 205 A1ILF A CAV   1 
HETATM 1321 N  NAW   . A1ILF F 5 .   ? 19.180 -11.036 20.242 1.00 29.58 ? 205 A1ILF A NAW   1 
HETATM 1322 C  CAX   . A1ILF F 5 .   ? 19.515 -9.777  19.927 1.00 30.01 ? 205 A1ILF A CAX   1 
HETATM 1323 C  CAY   . A1ILF F 5 .   ? 19.708 -8.701  20.715 1.00 31.23 ? 205 A1ILF A CAY   1 
HETATM 1324 O  OBD   . A1ILF F 5 .   ? 19.560 -8.808  22.038 1.00 33.64 ? 205 A1ILF A OBD   1 
HETATM 1325 C  CAZ   . A1ILF F 5 .   ? 20.081 -7.467  20.208 1.00 29.56 ? 205 A1ILF A CAZ   1 
HETATM 1326 C  CBA   . A1ILF F 5 .   ? 20.242 -7.346  18.864 1.00 28.51 ? 205 A1ILF A CBA   1 
HETATM 1327 C  CBB   . A1ILF F 5 .   ? 20.028 -8.438  18.080 1.00 29.68 ? 205 A1ILF A CBB   1 
HETATM 1328 CL CLBC  . A1ILF F 5 .   ? 20.258 -8.261  16.441 1.00 30.39 ? 205 A1ILF A CLBC  1 
HETATM 1329 C  CBI   . A1ILF F 5 .   ? 19.675 -9.619  18.603 1.00 31.04 ? 205 A1ILF A CBI   1 
HETATM 1330 S  SBH   . A1ILF F 5 .   ? 19.374 -10.936 17.876 1.00 30.19 ? 205 A1ILF A SBH   1 
HETATM 1331 C  CBG   . A1ILF F 5 .   ? 19.076 -11.847 19.200 1.00 33.01 ? 205 A1ILF A CBG   1 
HETATM 1332 N  NBF   . A1ILF F 5 .   ? 18.710 -13.140 19.326 1.00 31.63 ? 205 A1ILF A NBF   1 
HETATM 1333 S  SAH   . A1ILF F 5 .   ? 18.930 -14.140 18.264 1.00 35.32 ? 205 A1ILF A SAH   1 
HETATM 1334 O  OAI   . A1ILF F 5 .   ? 18.661 -13.595 16.941 1.00 35.97 ? 205 A1ILF A OAI   1 
HETATM 1335 O  OBE   . A1ILF F 5 .   ? 18.054 -15.284 18.550 1.00 38.01 ? 205 A1ILF A OBE   1 
HETATM 1336 C  CAG   . A1ILF F 5 .   ? 20.506 -14.519 18.491 1.00 32.63 ? 205 A1ILF A CAG   1 
HETATM 1337 C  CAF   . A1ILF F 5 .   ? 21.523 -14.047 17.679 1.00 32.44 ? 205 A1ILF A CAF   1 
HETATM 1338 N  NAE   . A1ILF F 5 .   ? 22.835 -14.341 17.963 1.00 33.98 ? 205 A1ILF A NAE   1 
HETATM 1339 C  CAJ   . A1ILF F 5 .   ? 20.879 -15.168 19.633 1.00 35.20 ? 205 A1ILF A CAJ   1 
HETATM 1340 C  CAC   . A1ILF F 5 .   ? 22.212 -15.456 19.927 1.00 35.66 ? 205 A1ILF A CAC   1 
HETATM 1341 C  CAD   . A1ILF F 5 .   ? 23.201 -14.998 19.058 1.00 34.01 ? 205 A1ILF A CAD   1 
HETATM 1342 N  NAK   . A1ILF F 5 .   ? 24.524 -15.191 19.195 1.00 34.49 ? 205 A1ILF A NAK   1 
HETATM 1343 C  CAP   . A1ILF F 5 .   ? 25.103 -16.333 19.869 1.00 35.00 ? 205 A1ILF A CAP   1 
HETATM 1344 C  CAO   . A1ILF F 5 .   ? 26.343 -15.989 20.652 1.00 33.54 ? 205 A1ILF A CAO   1 
HETATM 1345 C  CAL   . A1ILF F 5 .   ? 25.451 -14.266 18.539 1.00 34.43 ? 205 A1ILF A CAL   1 
HETATM 1346 C  CAM   . A1ILF F 5 .   ? 26.647 -13.929 19.405 1.00 33.97 ? 205 A1ILF A CAM   1 
HETATM 1347 C  CAN   . A1ILF F 5 .   ? 27.340 -15.164 19.881 1.00 35.24 ? 205 A1ILF A CAN   1 
HETATM 1348 N  NBP   . A1ILF F 5 .   ? 28.434 -14.823 20.782 1.00 35.05 ? 205 A1ILF A NBP   1 
HETATM 1349 C  CBQ   . A1ILF F 5 .   ? 29.176 -16.024 21.119 1.00 34.15 ? 205 A1ILF A CBQ   1 
HETATM 1350 C  CBR   . A1ILF F 5 .   ? 30.270 -15.691 22.076 1.00 34.06 ? 205 A1ILF A CBR   1 
HETATM 1351 C  CBS   . A1ILF F 5 .   ? 31.276 -14.790 21.415 1.00 32.80 ? 205 A1ILF A CBS   1 
HETATM 1352 N  NBW   . A1ILF F 5 .   ? 32.450 -14.519 22.266 1.00 36.68 ? 205 A1ILF A NBW   1 
HETATM 1353 C  CBT   . A1ILF F 5 .   ? 30.552 -13.538 21.066 1.00 35.87 ? 205 A1ILF A CBT   1 
HETATM 1354 C  CBU   . A1ILF F 5 .   ? 29.356 -13.897 20.145 1.00 34.54 ? 205 A1ILF A CBU   1 
HETATM 1355 O  O     . HOH   G 6 .   ? 26.564 11.565  21.978 1.00 50.00 ? 301 HOH   A O     1 
HETATM 1356 O  O     . HOH   G 6 .   ? 30.507 -9.976  25.134 1.00 50.55 ? 302 HOH   A O     1 
HETATM 1357 O  O     . HOH   G 6 .   ? 29.375 -10.565 12.348 1.00 29.89 ? 303 HOH   A O     1 
HETATM 1358 O  O     . HOH   G 6 .   ? 27.567 -16.325 24.586 1.00 47.16 ? 304 HOH   A O     1 
HETATM 1359 O  O     . HOH   G 6 .   ? 31.799 8.604   25.560 1.00 36.57 ? 305 HOH   A O     1 
HETATM 1360 O  O     . HOH   G 6 .   ? 24.170 4.905   8.164  1.00 24.98 ? 306 HOH   A O     1 
HETATM 1361 O  O     . HOH   G 6 .   ? 30.573 9.884   5.693  1.00 40.63 ? 307 HOH   A O     1 
HETATM 1362 O  O     . HOH   G 6 .   ? 44.259 -3.564  17.318 1.00 33.43 ? 308 HOH   A O     1 
HETATM 1363 O  O     . HOH   G 6 .   ? 32.998 -9.429  21.014 1.00 27.79 ? 309 HOH   A O     1 
HETATM 1364 O  O     . HOH   G 6 .   ? 17.004 -0.767  10.326 1.00 45.70 ? 310 HOH   A O     1 
HETATM 1365 O  O     . HOH   G 6 .   ? 34.122 -13.153 20.318 1.00 34.86 ? 311 HOH   A O     1 
HETATM 1366 O  O     . HOH   G 6 .   ? 42.341 9.019   1.962  1.00 36.48 ? 312 HOH   A O     1 
HETATM 1367 O  O     . HOH   G 6 .   ? 24.220 8.430   6.465  1.00 53.41 ? 313 HOH   A O     1 
HETATM 1368 O  O     . HOH   G 6 .   ? 36.357 -13.058 17.109 1.00 38.66 ? 314 HOH   A O     1 
HETATM 1369 O  O     . HOH   G 6 .   ? 12.529 5.788   15.909 1.00 48.31 ? 315 HOH   A O     1 
HETATM 1370 O  O     . HOH   G 6 .   ? 31.889 2.036   -1.809 1.00 42.41 ? 316 HOH   A O     1 
HETATM 1371 O  O     . HOH   G 6 .   ? 40.273 -12.010 19.262 1.00 39.94 ? 317 HOH   A O     1 
HETATM 1372 O  O     . HOH   G 6 .   ? 20.062 6.406   7.905  1.00 49.50 ? 318 HOH   A O     1 
HETATM 1373 O  O     . HOH   G 6 .   ? 35.201 -1.655  28.412 1.00 32.68 ? 319 HOH   A O     1 
HETATM 1374 O  O     . HOH   G 6 .   ? 44.867 -5.756  20.594 1.00 66.31 ? 320 HOH   A O     1 
HETATM 1375 O  O     . HOH   G 6 .   ? 28.551 10.006  1.274  1.00 46.40 ? 321 HOH   A O     1 
HETATM 1376 O  O     . HOH   G 6 .   ? 23.420 -8.236  30.003 1.00 51.40 ? 322 HOH   A O     1 
HETATM 1377 O  O     . HOH   G 6 .   ? 36.057 -9.825  23.746 1.00 28.89 ? 323 HOH   A O     1 
HETATM 1378 O  O     . HOH   G 6 .   ? 31.422 -9.489  13.869 1.00 21.97 ? 324 HOH   A O     1 
HETATM 1379 O  O     . HOH   G 6 .   ? 36.962 -5.161  11.465 1.00 23.38 ? 325 HOH   A O     1 
HETATM 1380 O  O     . HOH   G 6 .   ? 40.584 10.690  16.930 1.00 54.45 ? 326 HOH   A O     1 
HETATM 1381 O  O     . HOH   G 6 .   ? 42.495 -5.528  16.063 1.00 34.73 ? 327 HOH   A O     1 
HETATM 1382 O  O     . HOH   G 6 .   ? 48.274 -2.670  10.894 1.00 33.63 ? 328 HOH   A O     1 
HETATM 1383 O  O     . HOH   G 6 .   ? 44.302 11.584  8.202  1.00 44.42 ? 329 HOH   A O     1 
HETATM 1384 O  O     . HOH   G 6 .   ? 37.496 -10.323 9.899  1.00 31.67 ? 330 HOH   A O     1 
HETATM 1385 O  O     . HOH   G 6 .   ? 24.452 4.241   2.869  1.00 47.16 ? 331 HOH   A O     1 
HETATM 1386 O  O     . HOH   G 6 .   ? 33.690 -9.943  0.320  1.00 33.92 ? 332 HOH   A O     1 
HETATM 1387 O  O     . HOH   G 6 .   ? 34.558 -1.780  0.052  1.00 36.08 ? 333 HOH   A O     1 
HETATM 1388 O  O     . HOH   G 6 .   ? 37.498 2.612   33.155 1.00 40.94 ? 334 HOH   A O     1 
HETATM 1389 O  O     . HOH   G 6 .   ? 24.619 1.442   4.451  1.00 55.38 ? 335 HOH   A O     1 
HETATM 1390 O  O     . HOH   G 6 .   ? 17.050 11.671  16.584 1.00 47.84 ? 336 HOH   A O     1 
HETATM 1391 O  O     . HOH   G 6 .   ? 41.236 -3.820  -1.007 1.00 31.35 ? 337 HOH   A O     1 
HETATM 1392 O  O     . HOH   G 6 .   ? 38.743 -11.831 12.660 1.00 38.91 ? 338 HOH   A O     1 
HETATM 1393 O  O     . HOH   G 6 .   ? 41.290 5.682   11.158 1.00 42.21 ? 339 HOH   A O     1 
HETATM 1394 O  O     . HOH   G 6 .   ? 33.727 -11.323 23.160 1.00 31.36 ? 340 HOH   A O     1 
HETATM 1395 O  O     . HOH   G 6 .   ? 39.721 -7.687  3.356  1.00 28.03 ? 341 HOH   A O     1 
HETATM 1396 O  O     . HOH   G 6 .   ? 26.101 -7.322  -0.546 1.00 39.18 ? 342 HOH   A O     1 
HETATM 1397 O  O     . HOH   G 6 .   ? 30.825 10.324  23.366 1.00 32.54 ? 343 HOH   A O     1 
HETATM 1398 O  O     . HOH   G 6 .   ? 39.796 -10.720 2.544  1.00 30.21 ? 344 HOH   A O     1 
HETATM 1399 O  O     . HOH   G 6 .   ? 35.932 11.158  14.709 1.00 51.46 ? 345 HOH   A O     1 
HETATM 1400 O  O     . HOH   G 6 .   ? 45.446 10.334  10.411 1.00 43.57 ? 346 HOH   A O     1 
HETATM 1401 O  O     . HOH   G 6 .   ? 28.915 -13.858 16.268 1.00 27.19 ? 347 HOH   A O     1 
HETATM 1402 O  O     . HOH   G 6 .   ? 13.259 -3.428  18.196 1.00 48.35 ? 348 HOH   A O     1 
HETATM 1403 O  O     . HOH   G 6 .   ? 42.285 -9.134  13.508 1.00 50.41 ? 349 HOH   A O     1 
HETATM 1404 O  O     . HOH   G 6 .   ? 31.732 11.092  8.714  1.00 41.34 ? 350 HOH   A O     1 
HETATM 1405 O  O     . HOH   G 6 .   ? 45.054 -2.821  22.250 1.00 36.77 ? 351 HOH   A O     1 
HETATM 1406 O  O     . HOH   G 6 .   ? 45.545 -5.372  23.101 1.00 44.10 ? 352 HOH   A O     1 
HETATM 1407 O  O     . HOH   G 6 .   ? 35.177 -13.532 23.856 1.00 51.94 ? 353 HOH   A O     1 
HETATM 1408 O  O     . HOH   G 6 .   ? 23.391 4.310   5.652  1.00 42.83 ? 354 HOH   A O     1 
HETATM 1409 O  O     . HOH   G 6 .   ? 46.433 -5.148  16.674 1.00 45.22 ? 355 HOH   A O     1 
HETATM 1410 O  O     . HOH   G 6 .   ? 35.012 -10.286 26.375 1.00 49.76 ? 356 HOH   A O     1 
HETATM 1411 O  O     . HOH   G 6 .   ? 40.099 2.461   33.581 1.00 44.68 ? 357 HOH   A O     1 
HETATM 1412 O  O     . HOH   G 6 .   ? 33.475 -0.618  -2.121 1.00 36.93 ? 358 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   ? 0.6420 0.9038 0.7314 0.1334  0.1232  -0.0430 1   MET   A N     
2    C  CA    . MET   A 4   ? 0.6343 0.8349 0.6209 0.1304  0.0855  -0.0319 1   MET   A CA    
3    C  C     . MET   A 4   ? 0.3429 0.7393 0.6915 0.2014  0.0764  0.0476  1   MET   A C     
4    O  O     . MET   A 4   ? 0.2668 0.7483 0.7349 0.2182  0.1609  0.0491  1   MET   A O     
5    C  CB    . MET   A 4   ? 0.6795 0.8632 0.6633 0.0351  0.0013  -0.0094 1   MET   A CB    
6    C  CG    . MET   A 4   ? 0.6105 0.8721 0.5704 0.0428  0.1302  0.0666  1   MET   A CG    
7    S  SD    . MET   A 4   ? 0.3896 0.8740 0.7648 0.0863  0.2053  0.1158  1   MET   A SD    
8    C  CE    . MET   A 4   ? 0.1975 0.8663 0.8777 0.1879  0.2238  0.1785  1   MET   A CE    
9    N  N     . THR   A 5   ? 0.3315 0.7465 0.5988 0.2406  0.1177  -0.0216 2   THR   A N     
10   C  CA    . THR   A 5   ? 0.2149 0.7885 0.5625 0.1983  0.0593  -0.0439 2   THR   A CA    
11   C  C     . THR   A 5   ? 0.1586 0.7328 0.5690 0.0931  0.0177  -0.0195 2   THR   A C     
12   O  O     . THR   A 5   ? 0.1853 0.7768 0.5373 0.1590  0.0022  -0.0600 2   THR   A O     
13   C  CB    . THR   A 5   ? 0.2529 0.8199 0.6150 0.1953  -0.0040 0.0086  2   THR   A CB    
14   O  OG1   . THR   A 5   ? 0.2827 0.9317 0.6648 0.2423  -0.0256 0.0393  2   THR   A OG1   
15   C  CG2   . THR   A 5   ? 0.2810 0.8748 0.6080 0.1066  0.0247  0.0032  2   THR   A CG2   
16   N  N     . GLU   A 6   ? 0.1174 0.7311 0.5911 0.0717  0.0439  -0.0408 3   GLU   A N     
17   C  CA    . GLU   A 6   ? 0.2064 0.6791 0.5231 0.0990  0.0799  -0.0325 3   GLU   A CA    
18   C  C     . GLU   A 6   ? 0.1155 0.7029 0.5286 0.0317  0.0607  0.0127  3   GLU   A C     
19   O  O     . GLU   A 6   ? 0.1710 0.7280 0.5633 0.0417  0.0400  -0.0238 3   GLU   A O     
20   C  CB    . GLU   A 6   ? 0.3308 0.7475 0.6445 0.0102  0.0570  0.0175  3   GLU   A CB    
21   C  CG    . GLU   A 6   ? 0.4871 0.7650 0.7332 0.0728  0.0613  0.0128  3   GLU   A CG    
22   C  CD    . GLU   A 6   ? 0.4844 0.7727 0.8497 0.0363  0.1003  0.0279  3   GLU   A CD    
23   O  OE1   . GLU   A 6   ? 0.2087 0.9327 0.8241 0.0239  -0.0311 0.0814  3   GLU   A OE1   
24   O  OE2   . GLU   A 6   ? 0.7328 0.7176 0.9681 0.0871  0.0611  0.0296  3   GLU   A OE2   
25   N  N     . TYR   A 7   ? 0.1177 0.5723 0.4606 0.0662  0.0418  0.0386  4   TYR   A N     
26   C  CA    . TYR   A 7   ? 0.1811 0.5553 0.4042 0.0733  0.0285  0.0519  4   TYR   A CA    
27   C  C     . TYR   A 7   ? 0.2064 0.5177 0.3753 0.0495  0.0174  0.0436  4   TYR   A C     
28   O  O     . TYR   A 7   ? 0.1553 0.5632 0.3895 0.0839  0.0444  0.0158  4   TYR   A O     
29   C  CB    . TYR   A 7   ? 0.1231 0.5189 0.3861 0.1081  0.0350  0.0532  4   TYR   A CB    
30   C  CG    . TYR   A 7   ? 0.1244 0.5620 0.4013 0.1498  0.0370  0.0583  4   TYR   A CG    
31   C  CD1   . TYR   A 7   ? 0.3157 0.5319 0.3817 0.1920  0.0383  0.0544  4   TYR   A CD1   
32   C  CD2   . TYR   A 7   ? 0.2004 0.5373 0.4383 0.1415  0.0161  0.0330  4   TYR   A CD2   
33   C  CE1   . TYR   A 7   ? 0.2413 0.6045 0.4279 0.2211  -0.0359 0.0738  4   TYR   A CE1   
34   C  CE2   . TYR   A 7   ? 0.2727 0.5677 0.4576 0.1657  0.0038  0.0538  4   TYR   A CE2   
35   C  CZ    . TYR   A 7   ? 0.2479 0.5626 0.4463 0.1973  0.0467  0.0832  4   TYR   A CZ    
36   O  OH    . TYR   A 7   ? 0.1820 0.6257 0.6093 0.2235  -0.0761 0.0464  4   TYR   A OH    
37   N  N     . LYS   A 8   ? 0.0672 0.4982 0.3913 0.0661  0.0260  0.0417  5   LYS   A N     
38   C  CA    . LYS   A 8   ? 0.1603 0.4518 0.3849 0.0659  0.0586  0.0553  5   LYS   A CA    
39   C  C     . LYS   A 8   ? 0.0900 0.4252 0.3555 0.0504  -0.0075 0.0379  5   LYS   A C     
40   O  O     . LYS   A 8   ? 0.0757 0.4575 0.3651 0.0437  -0.0228 0.0178  5   LYS   A O     
41   C  CB    . LYS   A 8   ? 0.0969 0.5010 0.4233 0.0207  0.0117  0.0772  5   LYS   A CB    
42   C  CG    . LYS   A 8   ? 0.1601 0.5730 0.5223 -0.0217 0.0783  0.0668  5   LYS   A CG    
43   C  CD    . LYS   A 8   ? 0.2665 0.5844 0.5893 -0.0407 0.1001  0.0956  5   LYS   A CD    
44   C  CE    . LYS   A 8   ? 0.3342 0.6446 0.6536 -0.1115 0.1539  0.0894  5   LYS   A CE    
45   N  NZ    . LYS   A 8   ? 0.3657 0.7430 0.6910 -0.0467 0.1759  0.1019  5   LYS   A NZ    
46   N  N     . LEU   A 9   ? 0.0875 0.4105 0.3564 0.0325  0.0030  0.0506  6   LEU   A N     
47   C  CA    . LEU   A 9   ? 0.0902 0.3649 0.3273 0.0559  0.0314  0.0391  6   LEU   A CA    
48   C  C     . LEU   A 9   ? 0.1077 0.3237 0.3332 0.0190  0.0276  0.0326  6   LEU   A C     
49   O  O     . LEU   A 9   ? 0.0785 0.4128 0.3757 0.0278  0.0238  0.0753  6   LEU   A O     
50   C  CB    . LEU   A 9   ? 0.1305 0.3698 0.3609 0.0389  0.0226  0.0273  6   LEU   A CB    
51   C  CG    . LEU   A 9   ? 0.2317 0.3466 0.3877 0.0546  0.0460  0.0328  6   LEU   A CG    
52   C  CD1   . LEU   A 9   ? 0.2455 0.3723 0.4296 0.0406  0.0309  0.0370  6   LEU   A CD1   
53   C  CD2   . LEU   A 9   ? 0.2147 0.3790 0.4210 0.0651  0.0492  0.0644  6   LEU   A CD2   
54   N  N     . VAL   A 10  ? 0.0673 0.3185 0.3424 0.0225  0.0074  0.0390  7   VAL   A N     
55   C  CA    . VAL   A 10  ? 0.0569 0.2992 0.3887 0.0113  0.0195  0.0463  7   VAL   A CA    
56   C  C     . VAL   A 10  ? 0.0575 0.2938 0.3912 0.0157  0.0200  0.0523  7   VAL   A C     
57   O  O     . VAL   A 10  ? 0.0612 0.3080 0.3809 -0.0001 -0.0145 0.0402  7   VAL   A O     
58   C  CB    . VAL   A 10  ? 0.0740 0.3174 0.3949 -0.0016 0.0200  0.0326  7   VAL   A CB    
59   C  CG1   . VAL   A 10  ? 0.1466 0.2991 0.3969 0.0107  0.0104  0.0139  7   VAL   A CG1   
60   C  CG2   . VAL   A 10  ? 0.0791 0.3081 0.3765 -0.0064 -0.0014 0.0141  7   VAL   A CG2   
61   N  N     . VAL   A 11  ? 0.0594 0.2783 0.3785 0.0028  0.0063  0.0325  8   VAL   A N     
62   C  CA    . VAL   A 11  ? 0.0586 0.3096 0.3642 0.0011  0.0403  0.0287  8   VAL   A CA    
63   C  C     . VAL   A 11  ? 0.0660 0.3192 0.3477 0.0199  -0.0218 0.0194  8   VAL   A C     
64   O  O     . VAL   A 11  ? 0.0658 0.3250 0.3869 0.0312  0.0096  0.0144  8   VAL   A O     
65   C  CB    . VAL   A 11  ? 0.0720 0.2902 0.3594 0.0055  0.0255  0.0367  8   VAL   A CB    
66   C  CG1   . VAL   A 11  ? 0.0398 0.3663 0.3856 0.0187  -0.0071 0.0173  8   VAL   A CG1   
67   C  CG2   . VAL   A 11  ? 0.1341 0.3297 0.3550 0.0246  0.0308  0.0171  8   VAL   A CG2   
68   N  N     . VAL   A 12  ? 0.0557 0.2805 0.3576 0.0382  0.0104  0.0137  9   VAL   A N     
69   C  CA    . VAL   A 12  ? 0.0989 0.2905 0.3584 0.0165  0.0240  -0.0010 9   VAL   A CA    
70   C  C     . VAL   A 12  ? 0.0990 0.2862 0.3763 0.0212  0.0249  -0.0090 9   VAL   A C     
71   O  O     . VAL   A 12  ? 0.0570 0.2957 0.3870 0.0230  0.0091  0.0067  9   VAL   A O     
72   C  CB    . VAL   A 12  ? 0.0747 0.3106 0.3745 0.0031  0.0195  -0.0098 9   VAL   A CB    
73   C  CG1   . VAL   A 12  ? 0.0594 0.3865 0.3858 -0.0050 0.0017  0.0045  9   VAL   A CG1   
74   C  CG2   . VAL   A 12  ? 0.1048 0.3549 0.3709 0.0048  -0.0155 0.0189  9   VAL   A CG2   
75   N  N     . GLY   A 13  ? 0.0992 0.2780 0.3854 0.0073  0.0273  -0.0181 10  GLY   A N     
76   C  CA    . GLY   A 13  ? 0.0901 0.2962 0.4099 0.0110  0.0115  0.0104  10  GLY   A CA    
77   C  C     . GLY   A 13  ? 0.0825 0.3253 0.3908 0.0316  0.0472  0.0038  10  GLY   A C     
78   O  O     . GLY   A 13  ? 0.0696 0.3486 0.4170 0.0241  -0.0042 0.0175  10  GLY   A O     
79   N  N     . ALA   A 14  ? 0.0620 0.3083 0.4079 0.0137  0.0232  -0.0058 11  ALA   A N     
80   C  CA    . ALA   A 14  ? 0.1120 0.3442 0.4394 0.0578  0.0179  0.0144  11  ALA   A CA    
81   C  C     . ALA   A 14  ? 0.0469 0.3800 0.4478 0.0619  0.0149  0.0060  11  ALA   A C     
82   O  O     . ALA   A 14  ? 0.0732 0.4070 0.4527 0.0698  0.0002  -0.0014 11  ALA   A O     
83   C  CB    . ALA   A 14  ? 0.0664 0.4052 0.4620 0.0728  0.0250  0.0061  11  ALA   A CB    
84   N  N     . GLY   A 15  ? 0.1325 0.3818 0.4599 0.0847  -0.0023 0.0097  12  GLY   A N     
85   C  CA    . GLY   A 15  ? 0.2235 0.3982 0.4524 0.0718  0.0126  0.0186  12  GLY   A CA    
86   C  C     . GLY   A 15  ? 0.2079 0.3820 0.3996 0.0731  -0.0004 0.0404  12  GLY   A C     
87   O  O     . GLY   A 15  ? 0.1621 0.4542 0.4573 0.0987  0.0088  0.0689  12  GLY   A O     
88   N  N     . GLY   A 16  ? 0.0929 0.4161 0.4263 0.0670  -0.0212 -0.0122 13  GLY   A N     
89   C  CA    . GLY   A 16  ? 0.1021 0.4877 0.4081 0.0223  -0.0321 -0.0014 13  GLY   A CA    
90   C  C     . GLY   A 16  ? 0.1225 0.4966 0.3979 0.0352  -0.0391 -0.0075 13  GLY   A C     
91   O  O     . GLY   A 16  ? 0.0976 0.5355 0.4340 0.0377  -0.0536 -0.0238 13  GLY   A O     
92   N  N     . VAL   A 17  ? 0.0245 0.4686 0.4208 0.0089  -0.0085 -0.0076 14  VAL   A N     
93   C  CA    . VAL   A 17  ? 0.0584 0.4569 0.4086 -0.0309 0.0233  -0.0102 14  VAL   A CA    
94   C  C     . VAL   A 17  ? 0.1013 0.4168 0.3826 0.0593  0.0126  0.0375  14  VAL   A C     
95   O  O     . VAL   A 17  ? 0.0718 0.4451 0.3897 -0.0147 0.0078  -0.0053 14  VAL   A O     
96   C  CB    . VAL   A 17  ? 0.0701 0.3999 0.4061 -0.0385 0.0181  0.0021  14  VAL   A CB    
97   C  CG1   . VAL   A 17  ? 0.0632 0.3971 0.4168 0.0114  -0.0021 0.0088  14  VAL   A CG1   
98   C  CG2   . VAL   A 17  ? 0.0673 0.4064 0.3699 -0.0440 0.0082  -0.0309 14  VAL   A CG2   
99   N  N     . GLY   A 18  ? 0.0775 0.4349 0.3896 -0.0229 0.0031  0.0091  15  GLY   A N     
100  C  CA    . GLY   A 18  ? 0.0831 0.4415 0.4017 -0.0230 -0.0167 -0.0091 15  GLY   A CA    
101  C  C     . GLY   A 18  ? 0.0802 0.4038 0.3806 -0.0413 -0.0120 0.0075  15  GLY   A C     
102  O  O     . GLY   A 18  ? 0.0752 0.3985 0.3850 -0.0338 -0.0102 0.0165  15  GLY   A O     
103  N  N     . LYS   A 19  ? 0.0385 0.3597 0.3816 0.0077  -0.0054 0.0185  16  LYS   A N     
104  C  CA    . LYS   A 19  ? 0.0342 0.3669 0.3609 0.0367  0.0126  0.0237  16  LYS   A CA    
105  C  C     . LYS   A 19  ? 0.1285 0.3494 0.3391 0.0247  -0.0113 0.0236  16  LYS   A C     
106  O  O     . LYS   A 19  ? 0.0973 0.4095 0.3439 0.0341  0.0226  0.0431  16  LYS   A O     
107  C  CB    . LYS   A 19  ? 0.0896 0.3675 0.3715 0.0521  -0.0261 0.0167  16  LYS   A CB    
108  C  CG    . LYS   A 19  ? 0.0840 0.3721 0.3912 0.0183  0.0019  0.0317  16  LYS   A CG    
109  C  CD    . LYS   A 19  ? 0.1279 0.4054 0.3650 0.0010  0.0057  0.0030  16  LYS   A CD    
110  C  CE    . LYS   A 19  ? 0.0981 0.4070 0.3980 -0.0210 -0.0029 0.0010  16  LYS   A CE    
111  N  NZ    . LYS   A 19  ? 0.0936 0.3935 0.4031 0.0081  -0.0124 0.0003  16  LYS   A NZ    
112  N  N     . SER   A 20  ? 0.0511 0.4161 0.3682 0.0204  -0.0254 0.0481  17  SER   A N     
113  C  CA    . SER   A 20  ? 0.0947 0.3886 0.3667 0.0065  -0.0149 0.0511  17  SER   A CA    
114  C  C     . SER   A 20  ? 0.1080 0.4086 0.3476 -0.0179 0.0065  0.0344  17  SER   A C     
115  O  O     . SER   A 20  ? 0.1189 0.4370 0.3527 0.0237  -0.0025 0.0272  17  SER   A O     
116  C  CB    . SER   A 20  ? 0.0895 0.3861 0.3613 0.0116  0.0088  0.0572  17  SER   A CB    
117  O  OG    . SER   A 20  ? 0.1145 0.3778 0.4392 0.0443  -0.0464 0.0618  17  SER   A OG    
118  N  N     . ALA   A 21  ? 0.0835 0.4368 0.3691 0.0080  -0.0161 0.0334  18  ALA   A N     
119  C  CA    . ALA   A 21  ? 0.0770 0.4555 0.3718 0.0050  -0.0150 0.0292  18  ALA   A CA    
120  C  C     . ALA   A 21  ? 0.0785 0.4603 0.3495 -0.0112 -0.0083 0.0201  18  ALA   A C     
121  O  O     . ALA   A 21  ? 0.1317 0.4937 0.3489 -0.0169 0.0054  0.0094  18  ALA   A O     
122  C  CB    . ALA   A 21  ? 0.0573 0.4959 0.4251 0.0142  -0.0394 0.0174  18  ALA   A CB    
123  N  N     . LEU   A 22  ? 0.1081 0.4362 0.3389 0.0159  0.0002  0.0232  19  LEU   A N     
124  C  CA    . LEU   A 22  ? 0.1401 0.3815 0.3501 -0.0233 0.0136  0.0411  19  LEU   A CA    
125  C  C     . LEU   A 22  ? 0.1420 0.4273 0.3476 -0.0297 0.0152  0.0238  19  LEU   A C     
126  O  O     . LEU   A 22  ? 0.1502 0.4444 0.3339 -0.0319 0.0032  0.0175  19  LEU   A O     
127  C  CB    . LEU   A 22  ? 0.1243 0.3995 0.3510 -0.0292 0.0162  0.0271  19  LEU   A CB    
128  C  CG    . LEU   A 22  ? 0.1379 0.3937 0.3895 -0.0330 0.0312  0.0269  19  LEU   A CG    
129  C  CD1   . LEU   A 22  ? 0.1936 0.4027 0.3866 -0.0085 0.0249  0.0592  19  LEU   A CD1   
130  C  CD2   . LEU   A 22  ? 0.1990 0.3975 0.3763 -0.0594 0.0179  0.0467  19  LEU   A CD2   
131  N  N     . THR   A 23  ? 0.0950 0.4328 0.3721 -0.0112 0.0101  0.0186  20  THR   A N     
132  C  CA    . THR   A 23  ? 0.0671 0.4597 0.3810 -0.0124 -0.0107 0.0331  20  THR   A CA    
133  C  C     . THR   A 23  ? 0.1701 0.4449 0.3776 0.0164  -0.0197 0.0329  20  THR   A C     
134  O  O     . THR   A 23  ? 0.2030 0.5048 0.3538 0.0042  0.0465  0.0186  20  THR   A O     
135  C  CB    . THR   A 23  ? 0.1020 0.4642 0.3853 -0.0302 0.0186  0.0289  20  THR   A CB    
136  O  OG1   . THR   A 23  ? 0.1038 0.4718 0.4090 0.0029  0.0240  0.0168  20  THR   A OG1   
137  C  CG2   . THR   A 23  ? 0.0698 0.5158 0.3888 -0.0307 -0.0075 0.0135  20  THR   A CG2   
138  N  N     . ILE   A 24  ? 0.0783 0.4706 0.3806 0.0195  0.0384  0.0441  21  ILE   A N     
139  C  CA    . ILE   A 24  ? 0.1797 0.5060 0.3662 -0.0005 0.0649  0.0490  21  ILE   A CA    
140  C  C     . ILE   A 24  ? 0.1469 0.5229 0.3134 0.0036  0.0288  0.0412  21  ILE   A C     
141  O  O     . ILE   A 24  ? 0.1729 0.5402 0.3404 0.0043  0.0646  0.0248  21  ILE   A O     
142  C  CB    . ILE   A 24  ? 0.1902 0.5222 0.3853 0.0099  0.0640  0.0535  21  ILE   A CB    
143  C  CG1   . ILE   A 24  ? 0.2375 0.5325 0.4233 -0.0087 0.0635  0.0571  21  ILE   A CG1   
144  C  CG2   . ILE   A 24  ? 0.2261 0.5590 0.3913 0.0260  0.0535  0.0571  21  ILE   A CG2   
145  C  CD1   . ILE   A 24  ? 0.4023 0.5220 0.4890 0.0540  0.0442  0.0632  21  ILE   A CD1   
146  N  N     . GLN   A 25  ? 0.2056 0.5174 0.3404 -0.0385 0.0448  0.0072  22  GLN   A N     
147  C  CA    . GLN   A 25  ? 0.3099 0.5365 0.3634 -0.0403 0.0491  -0.0297 22  GLN   A CA    
148  C  C     . GLN   A 25  ? 0.3486 0.5155 0.3576 -0.0256 0.0455  -0.0152 22  GLN   A C     
149  O  O     . GLN   A 25  ? 0.3490 0.5293 0.3715 -0.0439 0.0755  -0.0088 22  GLN   A O     
150  C  CB    . GLN   A 25  ? 0.4073 0.5760 0.3574 -0.0678 0.0713  0.0015  22  GLN   A CB    
151  C  CG    . GLN   A 25  ? 0.4552 0.6396 0.3560 -0.1109 0.0852  -0.0287 22  GLN   A CG    
152  C  CD    . GLN   A 25  ? 0.3169 0.6900 0.3670 -0.1144 0.0870  0.0191  22  GLN   A CD    
153  O  OE1   . GLN   A 25  ? 0.3407 0.7360 0.4376 -0.1046 0.1124  -0.0200 22  GLN   A OE1   
154  N  NE2   . GLN   A 25  ? 0.3311 0.5804 0.4843 -0.1942 -0.0381 -0.0335 22  GLN   A NE2   
155  N  N     . LEU   A 26  ? 0.2434 0.5145 0.3540 0.0111  0.0853  -0.0310 23  LEU   A N     
156  C  CA    . LEU   A 26  ? 0.3131 0.4942 0.3575 0.0489  0.0664  0.0092  23  LEU   A CA    
157  C  C     . LEU   A 26  ? 0.2718 0.4822 0.3587 0.0361  0.0648  -0.0083 23  LEU   A C     
158  O  O     . LEU   A 26  ? 0.3362 0.5620 0.3762 0.0926  0.0625  -0.0424 23  LEU   A O     
159  C  CB    . LEU   A 26  ? 0.2691 0.4924 0.3887 0.0533  0.0543  -0.0062 23  LEU   A CB    
160  C  CG    . LEU   A 26  ? 0.2994 0.5006 0.4134 0.0575  0.0373  0.0264  23  LEU   A CG    
161  C  CD1   . LEU   A 26  ? 0.3996 0.4768 0.4416 0.0419  0.0309  -0.0252 23  LEU   A CD1   
162  C  CD2   . LEU   A 26  ? 0.2295 0.5583 0.4198 0.0475  0.0599  0.0255  23  LEU   A CD2   
163  N  N     . ILE   A 27  ? 0.2101 0.4989 0.3998 0.0696  0.0928  0.0171  24  ILE   A N     
164  C  CA    . ILE   A 27  ? 0.1994 0.5365 0.3759 0.0222  0.0630  0.0125  24  ILE   A CA    
165  C  C     . ILE   A 27  ? 0.2619 0.5522 0.3685 0.0666  0.0406  0.0296  24  ILE   A C     
166  O  O     . ILE   A 27  ? 0.3194 0.6100 0.4133 0.0405  0.0914  -0.0101 24  ILE   A O     
167  C  CB    . ILE   A 27  ? 0.1665 0.5238 0.4179 0.0442  0.0352  0.0370  24  ILE   A CB    
168  C  CG1   . ILE   A 27  ? 0.1488 0.5321 0.4405 0.0083  0.0277  0.0237  24  ILE   A CG1   
169  C  CG2   . ILE   A 27  ? 0.2754 0.4741 0.4428 0.0090  0.0485  0.0528  24  ILE   A CG2   
170  C  CD1   . ILE   A 27  ? 0.1826 0.5451 0.4516 0.0584  0.0448  -0.0104 24  ILE   A CD1   
171  N  N     . GLN   A 28  ? 0.2024 0.5631 0.3724 -0.0021 0.0618  0.0267  25  GLN   A N     
172  C  CA    . GLN   A 28  ? 0.2980 0.5930 0.3799 0.0168  0.0266  0.0170  25  GLN   A CA    
173  C  C     . GLN   A 28  ? 0.2917 0.6280 0.3485 -0.0121 0.0863  0.0059  25  GLN   A C     
174  O  O     . GLN   A 28  ? 0.3160 0.6934 0.3657 -0.0336 0.0236  0.0199  25  GLN   A O     
175  C  CB    . GLN   A 28  ? 0.2503 0.5893 0.3860 0.0166  0.0699  -0.0227 25  GLN   A CB    
176  C  CG    . GLN   A 28  ? 0.3300 0.5754 0.3987 0.0279  0.0638  -0.0138 25  GLN   A CG    
177  C  CD    . GLN   A 28  ? 0.4020 0.5770 0.3861 0.0163  0.0376  0.0419  25  GLN   A CD    
178  O  OE1   . GLN   A 28  ? 0.3472 0.7310 0.5032 0.0614  0.0674  0.0121  25  GLN   A OE1   
179  N  NE2   . GLN   A 28  ? 0.5233 0.5666 0.4826 0.0305  0.0487  0.0085  25  GLN   A NE2   
180  N  N     . ASN   A 29  ? 0.3180 0.5794 0.3813 -0.0048 0.0641  0.0155  26  ASN   A N     
181  C  CA    . ASN   A 29  ? 0.4262 0.5928 0.3897 -0.0425 0.0798  -0.0056 26  ASN   A CA    
182  C  C     . ASN   A 29  ? 0.3855 0.6165 0.3418 -0.0476 0.1108  -0.0366 26  ASN   A C     
183  O  O     . ASN   A 29  ? 0.4453 0.6297 0.4296 -0.1223 0.0930  -0.0005 26  ASN   A O     
184  C  CB    . ASN   A 29  ? 0.4843 0.5929 0.4226 -0.0681 0.0919  -0.0201 26  ASN   A CB    
185  C  CG    . ASN   A 29  ? 0.5995 0.6399 0.5888 -0.0154 0.0181  -0.0033 26  ASN   A CG    
186  O  OD1   . ASN   A 29  ? 0.7049 0.6870 0.7834 -0.1095 -0.0116 -0.0144 26  ASN   A OD1   
187  N  ND2   . ASN   A 29  ? 0.7084 0.6618 0.6899 -0.0953 -0.0120 -0.0020 26  ASN   A ND2   
188  N  N     . HIS   A 30  ? 0.2713 0.5705 0.3868 -0.0896 0.0553  -0.0001 27  HIS   A N     
189  C  CA    . HIS   A 30  ? 0.2909 0.6296 0.3778 -0.0832 0.0171  0.0031  27  HIS   A CA    
190  C  C     . HIS   A 30  ? 0.2206 0.6292 0.4103 -0.1344 0.0347  -0.0182 27  HIS   A C     
191  O  O     . HIS   A 30  ? 0.2253 0.6281 0.4102 -0.0942 0.0202  -0.0284 27  HIS   A O     
192  C  CB    . HIS   A 30  ? 0.2747 0.6578 0.3762 -0.0423 0.0056  0.0300  27  HIS   A CB    
193  C  CG    . HIS   A 30  ? 0.2874 0.6888 0.3666 -0.0164 0.0158  0.0259  27  HIS   A CG    
194  N  ND1   . HIS   A 30  ? 0.3396 0.7087 0.4020 -0.0900 0.0496  0.0228  27  HIS   A ND1   
195  C  CD2   . HIS   A 30  ? 0.4263 0.6460 0.4732 -0.0622 0.0467  0.0202  27  HIS   A CD2   
196  C  CE1   . HIS   A 30  ? 0.3788 0.7186 0.3979 -0.0649 0.0310  0.0113  27  HIS   A CE1   
197  N  NE2   . HIS   A 30  ? 0.4533 0.6843 0.4980 -0.0567 0.0409  0.0475  27  HIS   A NE2   
198  N  N     . PHE   A 31  ? 0.2149 0.6241 0.4189 -0.1094 0.0352  -0.0298 28  PHE   A N     
199  C  CA    . PHE   A 31  ? 0.1582 0.6189 0.4064 -0.0905 0.0010  -0.0133 28  PHE   A CA    
200  C  C     . PHE   A 31  ? 0.1628 0.6816 0.4350 -0.0748 0.0053  0.0674  28  PHE   A C     
201  O  O     . PHE   A 31  ? 0.2935 0.7644 0.4115 -0.0719 -0.0189 0.1027  28  PHE   A O     
202  C  CB    . PHE   A 31  ? 0.1722 0.6559 0.4458 -0.1050 0.0245  0.0026  28  PHE   A CB    
203  C  CG    . PHE   A 31  ? 0.2393 0.6898 0.4096 -0.0166 -0.0011 0.0075  28  PHE   A CG    
204  C  CD1   . PHE   A 31  ? 0.1599 0.7171 0.4076 -0.0197 0.0124  0.0112  28  PHE   A CD1   
205  C  CD2   . PHE   A 31  ? 0.1992 0.7617 0.4338 -0.0625 -0.0025 -0.0272 28  PHE   A CD2   
206  C  CE1   . PHE   A 31  ? 0.1477 0.7883 0.4128 0.0089  0.0045  0.0077  28  PHE   A CE1   
207  C  CE2   . PHE   A 31  ? 0.2032 0.7333 0.4563 -0.0169 -0.0012 -0.0050 28  PHE   A CE2   
208  C  CZ    . PHE   A 31  ? 0.1336 0.7913 0.4542 -0.0248 0.0045  0.0102  28  PHE   A CZ    
209  N  N     . VAL   A 32  ? 0.3153 0.6490 0.5163 0.0187  -0.0690 0.0480  29  VAL   A N     
210  C  CA    . VAL   A 32  ? 0.4619 0.6867 0.6299 0.0768  -0.0354 0.1058  29  VAL   A CA    
211  C  C     . VAL   A 32  ? 0.4516 0.7814 0.7511 0.1032  -0.0604 0.0510  29  VAL   A C     
212  O  O     . VAL   A 32  ? 0.4103 0.8955 0.8920 0.0269  0.0176  0.1187  29  VAL   A O     
213  C  CB    . VAL   A 32  ? 0.5401 0.6977 0.6645 0.0862  -0.0626 0.0715  29  VAL   A CB    
214  C  CG1   . VAL   A 32  ? 0.5543 0.7114 0.6549 0.1246  -0.0776 0.0541  29  VAL   A CG1   
215  C  CG2   . VAL   A 32  ? 0.5252 0.7128 0.6798 0.0763  -0.0806 0.0769  29  VAL   A CG2   
216  N  N     . GLU   A 40  ? 0.6640 0.7052 0.5261 -0.0911 -0.0210 0.0590  37  GLU   A N     
217  C  CA    . GLU   A 40  ? 0.5450 0.6800 0.5470 0.0569  -0.0475 0.0893  37  GLU   A CA    
218  C  C     . GLU   A 40  ? 0.4414 0.5759 0.5340 0.0076  -0.0688 0.0496  37  GLU   A C     
219  O  O     . GLU   A 40  ? 0.3727 0.6218 0.5825 0.0106  -0.0872 0.0372  37  GLU   A O     
220  C  CB    . GLU   A 40  ? 0.5543 0.7258 0.6161 0.0221  -0.0063 0.0518  37  GLU   A CB    
221  C  CG    . GLU   A 40  ? 0.5999 0.7209 0.5932 0.0167  -0.0234 0.0691  37  GLU   A CG    
222  C  CD    . GLU   A 40  ? 0.5945 0.7208 0.5809 0.0154  -0.0212 0.0732  37  GLU   A CD    
223  O  OE1   . GLU   A 40  ? 0.5934 0.7206 0.5802 0.0155  -0.0221 0.0747  37  GLU   A OE1   
224  O  OE2   . GLU   A 40  ? 0.5890 0.7187 0.5809 0.0137  -0.0210 0.0730  37  GLU   A OE2   
225  N  N     . ASP   A 41  ? 0.3366 0.4635 0.5261 0.0833  -0.0810 0.0836  38  ASP   A N     
226  C  CA    . ASP   A 41  ? 0.2351 0.4776 0.5078 0.0771  -0.0939 0.0813  38  ASP   A CA    
227  C  C     . ASP   A 41  ? 0.1919 0.4227 0.4289 0.0452  -0.0498 0.0745  38  ASP   A C     
228  O  O     . ASP   A 41  ? 0.2024 0.4918 0.4337 0.0044  -0.0630 0.0934  38  ASP   A O     
229  C  CB    . ASP   A 41  ? 0.4490 0.5133 0.5717 0.0301  -0.0592 0.0339  38  ASP   A CB    
230  C  CG    . ASP   A 41  ? 0.5530 0.5576 0.5966 -0.0274 -0.0263 0.0295  38  ASP   A CG    
231  O  OD1   . ASP   A 41  ? 0.5011 0.7174 0.6646 -0.0229 -0.0325 0.0147  38  ASP   A OD1   
232  O  OD2   . ASP   A 41  ? 0.7139 0.5632 0.5686 0.0358  -0.0717 0.0124  38  ASP   A OD2   
233  N  N     . SER   A 42  ? 0.2084 0.4704 0.4102 -0.0122 -0.0329 0.0865  39  SER   A N     
234  C  CA    . SER   A 42  ? 0.2138 0.4592 0.4485 -0.0116 -0.0211 0.0835  39  SER   A CA    
235  C  C     . SER   A 42  ? 0.2122 0.4798 0.4131 -0.0653 0.0259  0.0994  39  SER   A C     
236  O  O     . SER   A 42  ? 0.2167 0.5062 0.4360 0.0242  0.0031  0.1064  39  SER   A O     
237  C  CB    . SER   A 42  ? 0.2511 0.5532 0.5124 -0.0717 -0.0379 0.0865  39  SER   A CB    
238  O  OG    . SER   A 42  ? 0.3509 0.6341 0.5107 -0.0702 0.0072  0.1099  39  SER   A OG    
239  N  N     . TYR   A 43  ? 0.2522 0.4853 0.3629 -0.0168 0.0020  0.0660  40  TYR   A N     
240  C  CA    . TYR   A 43  ? 0.2260 0.5012 0.3760 0.0505  0.0118  0.0702  40  TYR   A CA    
241  C  C     . TYR   A 43  ? 0.2583 0.5223 0.3670 0.0731  0.0089  0.0775  40  TYR   A C     
242  O  O     . TYR   A 43  ? 0.2031 0.5782 0.3848 0.1103  -0.0046 0.0698  40  TYR   A O     
243  C  CB    . TYR   A 43  ? 0.2784 0.5313 0.4468 0.0186  -0.0978 0.0440  40  TYR   A CB    
244  C  CG    . TYR   A 43  ? 0.3321 0.5812 0.5497 0.0725  -0.0807 0.0549  40  TYR   A CG    
245  C  CD1   . TYR   A 43  ? 0.3133 0.5561 0.5599 0.0395  -0.0504 0.0666  40  TYR   A CD1   
246  C  CD2   . TYR   A 43  ? 0.4174 0.5835 0.5951 0.1320  -0.1081 0.1048  40  TYR   A CD2   
247  C  CE1   . TYR   A 43  ? 0.3516 0.6565 0.5950 0.0845  -0.0434 0.1175  40  TYR   A CE1   
248  C  CE2   . TYR   A 43  ? 0.3508 0.7530 0.5590 0.1282  -0.1785 0.1218  40  TYR   A CE2   
249  C  CZ    . TYR   A 43  ? 0.4359 0.7109 0.6176 0.1049  -0.0901 0.1250  40  TYR   A CZ    
250  O  OH    . TYR   A 43  ? 0.4954 0.7260 0.6882 0.1390  -0.0553 0.1298  40  TYR   A OH    
251  N  N     . ARG   A 44  ? 0.2979 0.5928 0.4162 0.1355  0.0148  0.0491  41  ARG   A N     
252  C  CA    . ARG   A 44  ? 0.3126 0.5937 0.4049 0.1475  0.0656  0.0611  41  ARG   A CA    
253  C  C     . ARG   A 44  ? 0.2579 0.6031 0.3899 0.1744  0.0342  0.0611  41  ARG   A C     
254  O  O     . ARG   A 44  ? 0.2848 0.6480 0.4119 0.1738  -0.0005 0.0479  41  ARG   A O     
255  C  CB    . ARG   A 44  ? 0.4152 0.6268 0.5025 0.0662  0.0715  0.0766  41  ARG   A CB    
256  C  CG    . ARG   A 44  ? 0.4681 0.6904 0.5641 0.0344  0.0345  0.0548  41  ARG   A CG    
257  C  CD    . ARG   A 44  ? 0.6289 0.6636 0.6786 0.0107  0.0088  0.0622  41  ARG   A CD    
258  N  NE    . ARG   A 44  ? 0.6529 0.7388 0.7580 0.0800  -0.0183 0.0060  41  ARG   A NE    
259  C  CZ    . ARG   A 44  ? 0.7294 0.7065 0.7185 0.0933  -0.0662 0.0024  41  ARG   A CZ    
260  N  NH1   . ARG   A 44  ? 0.6979 0.6413 0.6964 0.0908  -0.0608 0.0544  41  ARG   A NH1   
261  N  NH2   . ARG   A 44  ? 0.7322 0.6932 0.7658 0.0992  -0.0669 0.0069  41  ARG   A NH2   
262  N  N     . LYS   A 45  ? 0.2692 0.5979 0.3345 0.1596  0.0403  0.0632  42  LYS   A N     
263  C  CA    . LYS   A 45  ? 0.2640 0.5889 0.4208 0.1548  0.0506  0.0626  42  LYS   A CA    
264  C  C     . LYS   A 45  ? 0.1714 0.6320 0.3575 0.1300  0.0748  0.0685  42  LYS   A C     
265  O  O     . LYS   A 45  ? 0.2861 0.6601 0.3390 0.1420  0.0495  -0.0063 42  LYS   A O     
266  C  CB    . LYS   A 45  ? 0.2726 0.6208 0.4248 0.1513  0.0845  0.0513  42  LYS   A CB    
267  C  CG    . LYS   A 45  ? 0.3863 0.6163 0.4935 0.1675  0.1046  0.0117  42  LYS   A CG    
268  C  CD    . LYS   A 45  ? 0.4313 0.6235 0.5511 0.1079  0.0921  0.0210  42  LYS   A CD    
269  C  CE    . LYS   A 45  ? 0.5864 0.5895 0.6327 0.1190  0.0831  -0.0028 42  LYS   A CE    
270  N  NZ    . LYS   A 45  ? 0.6316 0.6460 0.6607 0.0557  0.0386  -0.0404 42  LYS   A NZ    
271  N  N     . GLN   A 46  ? 0.2672 0.6291 0.3946 0.1299  0.0991  0.0398  43  GLN   A N     
272  C  CA    . GLN   A 46  ? 0.3313 0.6337 0.3659 0.1789  0.0663  0.0154  43  GLN   A CA    
273  C  C     . GLN   A 46  ? 0.3445 0.6685 0.3673 0.1568  0.1111  0.0278  43  GLN   A C     
274  O  O     . GLN   A 46  ? 0.4102 0.6803 0.4042 0.2325  0.0497  0.0415  43  GLN   A O     
275  C  CB    . GLN   A 46  ? 0.3908 0.6534 0.3336 0.1380  0.0866  0.0501  43  GLN   A CB    
276  C  CG    . GLN   A 46  ? 0.3939 0.6701 0.4016 0.1596  0.1090  0.0541  43  GLN   A CG    
277  C  CD    . GLN   A 46  ? 0.3770 0.7226 0.4149 0.1723  0.1101  0.0369  43  GLN   A CD    
278  O  OE1   . GLN   A 46  ? 0.3133 0.7954 0.4847 0.1321  0.1049  0.0657  43  GLN   A OE1   
279  N  NE2   . GLN   A 46  ? 0.5575 0.7647 0.4166 0.1724  0.1284  0.0025  43  GLN   A NE2   
280  N  N     . VAL   A 47  ? 0.2796 0.6646 0.3773 0.1927  0.0349  0.0107  44  VAL   A N     
281  C  CA    . VAL   A 47  ? 0.4668 0.6548 0.4028 0.1332  0.0446  -0.0009 44  VAL   A CA    
282  C  C     . VAL   A 47  ? 0.4391 0.6207 0.3542 0.1343  0.0730  -0.0382 44  VAL   A C     
283  O  O     . VAL   A 47  ? 0.4882 0.6115 0.4612 0.1174  0.0123  0.0096  44  VAL   A O     
284  C  CB    . VAL   A 47  ? 0.5075 0.6572 0.4095 0.1001  0.0747  0.0245  44  VAL   A CB    
285  C  CG1   . VAL   A 47  ? 0.4721 0.6540 0.4569 0.0685  0.0887  0.0550  44  VAL   A CG1   
286  C  CG2   . VAL   A 47  ? 0.5204 0.6806 0.4022 0.1243  0.0648  0.0275  44  VAL   A CG2   
287  N  N     . VAL   A 48  ? 0.5347 0.6463 0.4299 0.0912  0.0888  -0.0698 45  VAL   A N     
288  C  CA    . VAL   A 48  ? 0.5368 0.6310 0.4607 0.0510  0.0804  -0.0422 45  VAL   A CA    
289  C  C     . VAL   A 48  ? 0.5868 0.6584 0.4464 0.0166  0.0670  -0.0345 45  VAL   A C     
290  O  O     . VAL   A 48  ? 0.5757 0.6565 0.5651 0.0409  0.0419  -0.0575 45  VAL   A O     
291  C  CB    . VAL   A 48  ? 0.6126 0.6306 0.5370 0.0544  0.1478  -0.0580 45  VAL   A CB    
292  C  CG1   . VAL   A 48  ? 0.6600 0.6650 0.6060 0.0808  0.0799  -0.0596 45  VAL   A CG1   
293  C  CG2   . VAL   A 48  ? 0.6733 0.6567 0.5512 0.0483  0.1492  -0.0214 45  VAL   A CG2   
294  N  N     . ILE   A 49  ? 0.5660 0.6892 0.4376 -0.0067 0.0840  -0.0863 46  ILE   A N     
295  C  CA    . ILE   A 49  ? 0.5511 0.7124 0.4691 0.0147  0.0816  -0.0544 46  ILE   A CA    
296  C  C     . ILE   A 49  ? 0.5491 0.6874 0.4796 0.0174  0.0740  -0.0714 46  ILE   A C     
297  O  O     . ILE   A 49  ? 0.5166 0.6451 0.4899 0.0276  0.1197  -0.0470 46  ILE   A O     
298  C  CB    . ILE   A 49  ? 0.5037 0.7469 0.4315 0.0369  0.0539  -0.0525 46  ILE   A CB    
299  C  CG1   . ILE   A 49  ? 0.4714 0.7365 0.5038 0.0243  0.0438  -0.0510 46  ILE   A CG1   
300  C  CG2   . ILE   A 49  ? 0.4338 0.7473 0.4978 -0.0146 0.0552  -0.0383 46  ILE   A CG2   
301  C  CD1   . ILE   A 49  ? 0.4303 0.7944 0.4606 0.0583  0.0319  -0.0646 46  ILE   A CD1   
302  N  N     . ASP   A 50  ? 0.5569 0.7113 0.4968 -0.0113 0.0256  -0.0524 47  ASP   A N     
303  C  CA    . ASP   A 50  ? 0.4925 0.7155 0.5384 -0.0237 0.0680  -0.0159 47  ASP   A CA    
304  C  C     . ASP   A 50  ? 0.4720 0.6908 0.5925 0.0423  0.0498  -0.0476 47  ASP   A C     
305  O  O     . ASP   A 50  ? 0.3099 0.6275 0.6174 0.0411  0.1345  0.0363  47  ASP   A O     
306  C  CB    . ASP   A 50  ? 0.3579 0.7194 0.5396 -0.0197 0.0880  0.0081  47  ASP   A CB    
307  C  CG    . ASP   A 50  ? 0.3263 0.7013 0.6213 0.0130  0.0824  -0.0065 47  ASP   A CG    
308  O  OD1   . ASP   A 50  ? 0.5434 0.7225 0.5196 -0.0292 0.0004  -0.0107 47  ASP   A OD1   
309  O  OD2   . ASP   A 50  ? 0.3301 0.6814 0.6552 0.0506  0.1012  0.0120  47  ASP   A OD2   
310  N  N     . GLY   A 51  ? 0.4941 0.7558 0.6036 0.0586  0.1074  -0.0554 48  GLY   A N     
311  C  CA    . GLY   A 51  ? 0.5013 0.6434 0.6302 0.0294  0.1142  -0.0647 48  GLY   A CA    
312  C  C     . GLY   A 51  ? 0.3458 0.6596 0.6090 0.0492  0.1667  -0.0458 48  GLY   A C     
313  O  O     . GLY   A 51  ? 0.4026 0.6705 0.6659 -0.0282 0.2308  -0.0641 48  GLY   A O     
314  N  N     . GLU   A 52  ? 0.4087 0.6165 0.5519 0.0771  0.1353  -0.0090 49  GLU   A N     
315  C  CA    . GLU   A 52  ? 0.3974 0.5817 0.5923 0.1240  0.1357  -0.0027 49  GLU   A CA    
316  C  C     . GLU   A 52  ? 0.4104 0.6507 0.5612 0.1605  0.1730  0.0237  49  GLU   A C     
317  O  O     . GLU   A 52  ? 0.4025 0.7268 0.5918 0.2041  0.1092  0.0699  49  GLU   A O     
318  C  CB    . GLU   A 52  ? 0.4173 0.6264 0.6032 0.0903  0.1025  0.0104  49  GLU   A CB    
319  C  CG    . GLU   A 52  ? 0.4663 0.6742 0.6918 0.0552  0.0219  0.0246  49  GLU   A CG    
320  C  CD    . GLU   A 52  ? 0.5344 0.7943 0.6868 0.0309  0.0291  0.0281  49  GLU   A CD    
321  O  OE1   . GLU   A 52  ? 0.5825 0.9063 0.7638 0.0585  0.1057  0.0793  49  GLU   A OE1   
322  O  OE2   . GLU   A 52  ? 0.6383 0.8414 0.8812 -0.0121 -0.0119 -0.0803 49  GLU   A OE2   
323  N  N     . THR   A 53  ? 0.3895 0.6179 0.5608 0.1575  0.1367  0.0448  50  THR   A N     
324  C  CA    . THR   A 53  ? 0.4296 0.6208 0.5997 0.1753  0.1329  0.0490  50  THR   A CA    
325  C  C     . THR   A 53  ? 0.4280 0.6270 0.5472 0.2017  0.0781  0.0612  50  THR   A C     
326  O  O     . THR   A 53  ? 0.4111 0.6551 0.5940 0.1952  0.0789  0.0707  50  THR   A O     
327  C  CB    . THR   A 53  ? 0.5468 0.6466 0.5126 0.1715  0.1253  0.0274  50  THR   A CB    
328  O  OG1   . THR   A 53  ? 0.6143 0.6788 0.5545 0.1480  0.1514  -0.0056 50  THR   A OG1   
329  C  CG2   . THR   A 53  ? 0.6427 0.6635 0.5712 0.1637  0.1081  0.0581  50  THR   A CG2   
330  N  N     . CYS   A 54  ? 0.3700 0.6706 0.4641 0.1941  0.1215  0.0328  51  CYS   A N     
331  C  CA    . CYS   A 54  ? 0.3406 0.6718 0.5125 0.1921  0.0322  0.0208  51  CYS   A CA    
332  C  C     . CYS   A 54  ? 0.2544 0.6113 0.4940 0.1385  0.0480  0.0169  51  CYS   A C     
333  O  O     . CYS   A 54  ? 0.2840 0.6531 0.5079 0.1882  -0.0161 0.0260  51  CYS   A O     
334  C  CB    . CYS   A 54  ? 0.3274 0.7263 0.5541 0.1259  0.0774  0.0321  51  CYS   A CB    
335  S  SG    . CYS   A 54  ? 0.3014 0.7816 0.5465 0.1281  0.1095  0.0553  51  CYS   A SG    
336  N  N     . LEU   A 55  ? 0.1895 0.6152 0.4365 0.1448  0.0512  -0.0006 52  LEU   A N     
337  C  CA    . LEU   A 55  ? 0.2973 0.6028 0.4223 0.1615  0.0578  0.0053  52  LEU   A CA    
338  C  C     . LEU   A 55  ? 0.2532 0.6215 0.3858 0.1112  0.0435  0.0045  52  LEU   A C     
339  O  O     . LEU   A 55  ? 0.1796 0.6198 0.4049 0.1203  0.0441  -0.0141 52  LEU   A O     
340  C  CB    . LEU   A 55  ? 0.3265 0.6821 0.5139 0.1023  0.0838  -0.0132 52  LEU   A CB    
341  C  CG    . LEU   A 55  ? 0.4205 0.7116 0.5032 0.0566  0.0959  0.0271  52  LEU   A CG    
342  C  CD1   . LEU   A 55  ? 0.4111 0.7439 0.5458 0.0331  0.0536  0.0137  52  LEU   A CD1   
343  C  CD2   . LEU   A 55  ? 0.5228 0.7462 0.5859 -0.0119 0.1173  -0.0093 52  LEU   A CD2   
344  N  N     . LEU   A 56  ? 0.2567 0.6316 0.3618 0.1196  0.0304  0.0076  53  LEU   A N     
345  C  CA    . LEU   A 56  ? 0.2492 0.5467 0.3464 0.0864  0.0317  0.0054  53  LEU   A CA    
346  C  C     . LEU   A 56  ? 0.1722 0.5663 0.3248 0.0559  0.0491  0.0495  53  LEU   A C     
347  O  O     . LEU   A 56  ? 0.2601 0.5816 0.3344 0.1065  0.0603  0.0491  53  LEU   A O     
348  C  CB    . LEU   A 56  ? 0.2344 0.5614 0.3674 0.0843  0.0389  0.0067  53  LEU   A CB    
349  C  CG    . LEU   A 56  ? 0.2977 0.5612 0.4237 0.0482  0.0241  -0.0063 53  LEU   A CG    
350  C  CD1   . LEU   A 56  ? 0.2841 0.5684 0.4642 0.0527  0.0321  -0.0003 53  LEU   A CD1   
351  C  CD2   . LEU   A 56  ? 0.3148 0.5629 0.3997 0.0673  0.0516  0.0097  53  LEU   A CD2   
352  N  N     . ASP   A 57  ? 0.1478 0.5713 0.3612 0.0435  0.0291  0.0342  54  ASP   A N     
353  C  CA    . ASP   A 57  ? 0.1420 0.5571 0.3609 -0.0116 0.0380  0.0477  54  ASP   A CA    
354  C  C     . ASP   A 57  ? 0.1142 0.5286 0.3518 0.0135  0.0120  0.0718  54  ASP   A C     
355  O  O     . ASP   A 57  ? 0.0862 0.5172 0.3672 0.0305  0.0170  0.0727  54  ASP   A O     
356  C  CB    . ASP   A 57  ? 0.1041 0.5999 0.4724 0.0173  0.0084  0.0243  54  ASP   A CB    
357  C  CG    . ASP   A 57  ? 0.1831 0.6007 0.5576 -0.0330 -0.0015 0.0218  54  ASP   A CG    
358  O  OD1   . ASP   A 57  ? 0.1873 0.6290 0.5076 -0.0990 -0.0145 0.1018  54  ASP   A OD1   
359  O  OD2   . ASP   A 57  ? 0.1888 0.7595 0.6809 -0.1052 0.0170  -0.0171 54  ASP   A OD2   
360  N  N     . ILE   A 58  ? 0.1122 0.4570 0.3546 0.0280  0.0174  0.0671  55  ILE   A N     
361  C  CA    . ILE   A 58  ? 0.1391 0.3908 0.3400 0.0122  0.0294  0.0479  55  ILE   A CA    
362  C  C     . ILE   A 58  ? 0.0791 0.3822 0.3389 -0.0224 0.0165  0.0514  55  ILE   A C     
363  O  O     . ILE   A 58  ? 0.1364 0.4486 0.3646 0.0361  0.0337  0.0760  55  ILE   A O     
364  C  CB    . ILE   A 58  ? 0.1695 0.3854 0.3545 0.0123  0.0226  0.0203  55  ILE   A CB    
365  C  CG1   . ILE   A 58  ? 0.2202 0.3883 0.3737 0.0235  0.0276  0.0286  55  ILE   A CG1   
366  C  CG2   . ILE   A 58  ? 0.1231 0.4031 0.4084 -0.0020 0.0006  0.0369  55  ILE   A CG2   
367  C  CD1   . ILE   A 58  ? 0.2171 0.3809 0.4369 0.0456  0.0303  0.0057  55  ILE   A CD1   
368  N  N     . LEU   A 59  ? 0.0631 0.3924 0.3512 -0.0070 0.0019  0.0552  56  LEU   A N     
369  C  CA    . LEU   A 59  ? 0.1265 0.3559 0.3906 -0.0308 0.0213  0.0598  56  LEU   A CA    
370  C  C     . LEU   A 59  ? 0.1220 0.3550 0.3953 -0.0101 0.0156  0.0792  56  LEU   A C     
371  O  O     . LEU   A 59  ? 0.0748 0.3616 0.4080 -0.0053 -0.0079 0.0915  56  LEU   A O     
372  C  CB    . LEU   A 59  ? 0.1378 0.3940 0.4121 -0.0097 0.0148  0.0274  56  LEU   A CB    
373  C  CG    . LEU   A 59  ? 0.1169 0.3913 0.4187 -0.0072 0.0140  0.0354  56  LEU   A CG    
374  C  CD1   . LEU   A 59  ? 0.1440 0.3579 0.4561 -0.0181 -0.0019 0.0426  56  LEU   A CD1   
375  C  CD2   . LEU   A 59  ? 0.1498 0.3692 0.4358 -0.0053 0.0138  0.0208  56  LEU   A CD2   
376  N  N     . ASP   A 60  ? 0.0938 0.4221 0.4042 -0.0062 -0.0014 0.0732  57  ASP   A N     
377  C  CA    . ASP   A 60  ? 0.0867 0.4158 0.4820 -0.0553 -0.0086 0.0367  57  ASP   A CA    
378  C  C     . ASP   A 60  ? 0.1002 0.3918 0.4747 -0.0509 -0.0241 0.0436  57  ASP   A C     
379  O  O     . ASP   A 60  ? 0.4057 0.3659 0.5473 0.0007  0.1393  0.0492  57  ASP   A O     
380  C  CB    . ASP   A 60  ? 0.1214 0.4657 0.4585 0.0339  0.0065  0.0447  57  ASP   A CB    
381  C  CG    . ASP   A 60  ? 0.1189 0.4866 0.4906 0.0175  0.0118  0.0790  57  ASP   A CG    
382  O  OD1   . ASP   A 60  ? 0.0964 0.5300 0.5013 -0.0365 -0.0332 0.0933  57  ASP   A OD1   
383  O  OD2   . ASP   A 60  ? 0.1557 0.5513 0.5251 -0.0292 -0.0335 0.0923  57  ASP   A OD2   
384  N  N     . THR   A 61  ? 0.1842 0.3501 0.4285 -0.0813 -0.0365 0.0277  58  THR   A N     
385  C  CA    . THR   A 61  ? 0.1432 0.3367 0.4491 -0.0154 -0.0541 0.0474  58  THR   A CA    
386  C  C     . THR   A 61  ? 0.1521 0.3870 0.4608 -0.0007 -0.0516 0.0119  58  THR   A C     
387  O  O     . THR   A 61  ? 0.1755 0.4265 0.4425 -0.0484 -0.0305 0.0178  58  THR   A O     
388  C  CB    . THR   A 61  ? 0.1658 0.3135 0.4232 0.0023  -0.0142 0.0395  58  THR   A CB    
389  O  OG1   . THR   A 61  ? 0.1899 0.2951 0.4383 0.0251  0.0492  0.0196  58  THR   A OG1   
390  C  CG2   . THR   A 61  ? 0.1729 0.2809 0.4408 0.0198  -0.0239 0.0463  58  THR   A CG2   
391  N  N     . ALA   A 62  ? 0.1317 0.3799 0.5082 0.0204  -0.0554 0.0187  59  ALA   A N     
392  C  CA    . ALA   A 62  ? 0.1471 0.4082 0.5396 0.0435  -0.0227 0.0410  59  ALA   A CA    
393  C  C     . ALA   A 62  ? 0.1755 0.3852 0.5636 0.1231  0.0173  0.0492  59  ALA   A C     
394  O  O     . ALA   A 62  ? 0.2088 0.3928 0.5818 0.0341  -0.0224 0.0548  59  ALA   A O     
395  C  CB    . ALA   A 62  ? 0.1992 0.4222 0.5672 0.0387  0.0077  0.0641  59  ALA   A CB    
396  N  N     . GLY   A 63  ? 0.1685 0.4112 0.6528 0.1263  0.0216  0.0600  60  GLY   A N     
397  C  CA    . GLY   A 63  ? 0.2531 0.3781 0.6627 0.0900  0.0337  0.0568  60  GLY   A CA    
398  C  C     . GLY   A 63  ? 0.3186 0.3350 0.8055 0.1441  0.0296  -0.0170 60  GLY   A C     
399  O  O     . GLY   A 63  ? 0.4354 0.3934 0.7377 0.1097  0.0002  0.0557  60  GLY   A O     
400  N  N     . MET   A 70  ? 0.2129 0.4317 0.6754 -0.0260 -0.0009 0.0997  67  MET   A N     
401  C  CA    . MET   A 70  ? 0.1810 0.4194 0.7393 -0.0524 0.0600  0.0751  67  MET   A CA    
402  C  C     . MET   A 70  ? 0.2119 0.3621 0.7164 -0.0368 -0.0207 0.0554  67  MET   A C     
403  O  O     . MET   A 70  ? 0.1547 0.4051 0.7026 -0.0227 -0.0140 0.0608  67  MET   A O     
404  C  CB    . MET   A 70  ? 0.2457 0.5335 0.7381 -0.0438 0.1095  0.0963  67  MET   A CB    
405  C  CG    . MET   A 70  ? 0.2397 0.5277 0.8404 -0.0091 0.2196  0.1095  67  MET   A CG    
406  S  SD    . MET   A 70  ? 0.5129 0.5264 0.9325 -0.1272 0.2159  0.0197  67  MET   A SD    
407  C  CE    . MET   A 70  ? 0.4868 0.5242 0.8940 -0.1038 0.0959  0.0645  67  MET   A CE    
408  N  N     . ARG   A 71  ? 0.2564 0.3092 0.6775 -0.0289 -0.0090 0.0328  68  ARG   A N     
409  C  CA    . ARG   A 71  ? 0.2005 0.3010 0.6810 -0.0175 0.0043  0.0212  68  ARG   A CA    
410  C  C     . ARG   A 71  ? 0.2458 0.2751 0.5580 -0.0593 -0.0246 -0.0401 68  ARG   A C     
411  O  O     . ARG   A 71  ? 0.1723 0.2870 0.5766 -0.0537 -0.0184 -0.0133 68  ARG   A O     
412  C  CB    . ARG   A 71  ? 0.2064 0.4010 0.7228 0.0552  -0.0018 -0.0170 68  ARG   A CB    
413  C  CG    . ARG   A 71  ? 0.3356 0.4606 0.8067 0.0245  0.0128  0.0312  68  ARG   A CG    
414  C  CD    . ARG   A 71  ? 0.3972 0.5511 0.8805 0.1012  0.0506  -0.0196 68  ARG   A CD    
415  N  NE    . ARG   A 71  ? 0.5388 0.7043 0.8739 0.1050  0.0191  -0.0659 68  ARG   A NE    
416  C  CZ    . ARG   A 71  ? 0.5404 0.8133 0.8175 0.0910  0.0356  -0.0603 68  ARG   A CZ    
417  N  NH1   . ARG   A 71  ? 0.5443 0.8275 0.8385 0.0644  0.0272  -0.0549 68  ARG   A NH1   
418  N  NH2   . ARG   A 71  ? 0.6403 0.8883 0.8026 0.0585  0.0132  -0.0595 68  ARG   A NH2   
419  N  N     . ASP   A 72  ? 0.2641 0.3390 0.5943 -0.0932 -0.0683 -0.0449 69  ASP   A N     
420  C  CA    . ASP   A 72  ? 0.3084 0.3856 0.5783 -0.0458 -0.0660 -0.0503 69  ASP   A CA    
421  C  C     . ASP   A 72  ? 0.2628 0.3468 0.5691 -0.1038 -0.0623 -0.0142 69  ASP   A C     
422  O  O     . ASP   A 72  ? 0.1559 0.4178 0.5707 -0.0791 0.0037  0.0246  69  ASP   A O     
423  C  CB    . ASP   A 72  ? 0.3503 0.4758 0.6639 -0.1103 -0.1027 -0.0961 69  ASP   A CB    
424  C  CG    . ASP   A 72  ? 0.3545 0.4540 0.7149 -0.1923 -0.0694 -0.1026 69  ASP   A CG    
425  O  OD1   . ASP   A 72  ? 0.2916 0.5490 0.8132 -0.0963 -0.0984 -0.1082 69  ASP   A OD1   
426  O  OD2   . ASP   A 72  ? 0.4496 0.7495 0.7356 -0.1387 -0.1033 -0.1558 69  ASP   A OD2   
427  N  N     . GLN   A 73  ? 0.2403 0.3598 0.5707 -0.0856 -0.0405 -0.0149 70  GLN   A N     
428  C  CA    . GLN   A 73  ? 0.1600 0.4276 0.5654 -0.1119 -0.0503 0.0140  70  GLN   A CA    
429  C  C     . GLN   A 73  ? 0.1513 0.4213 0.5296 -0.0627 -0.0389 0.0094  70  GLN   A C     
430  O  O     . GLN   A 73  ? 0.0929 0.3863 0.6401 -0.1164 -0.0309 0.0337  70  GLN   A O     
431  C  CB    . GLN   A 73  ? 0.1787 0.4447 0.5797 -0.1153 -0.0397 0.0278  70  GLN   A CB    
432  C  CG    . GLN   A 73  ? 0.2817 0.4497 0.5767 -0.1073 0.0050  0.0037  70  GLN   A CG    
433  C  CD    . GLN   A 73  ? 0.2973 0.4058 0.5644 -0.1106 -0.0120 -0.0300 70  GLN   A CD    
434  O  OE1   . GLN   A 73  ? 0.2050 0.4698 0.6353 -0.0836 -0.0820 -0.0747 70  GLN   A OE1   
435  N  NE2   . GLN   A 73  ? 0.1598 0.4785 0.6088 -0.1097 -0.0076 -0.0517 70  GLN   A NE2   
436  N  N     . TYR   A 74  ? 0.1552 0.3641 0.4701 -0.0669 -0.0281 0.0206  71  TYR   A N     
437  C  CA    . TYR   A 74  ? 0.0784 0.3655 0.4663 -0.0162 -0.0301 0.0063  71  TYR   A CA    
438  C  C     . TYR   A 74  ? 0.0580 0.2805 0.4954 -0.0248 -0.0540 -0.0103 71  TYR   A C     
439  O  O     . TYR   A 74  ? 0.0998 0.2963 0.5211 -0.0262 -0.0019 -0.0028 71  TYR   A O     
440  C  CB    . TYR   A 74  ? 0.1452 0.3378 0.4758 -0.0579 -0.0721 -0.0010 71  TYR   A CB    
441  C  CG    . TYR   A 74  ? 0.1805 0.3656 0.4645 -0.0342 -0.0215 0.0200  71  TYR   A CG    
442  C  CD1   . TYR   A 74  ? 0.1534 0.3670 0.4681 -0.0663 -0.0533 0.0096  71  TYR   A CD1   
443  C  CD2   . TYR   A 74  ? 0.1655 0.3665 0.5112 -0.0741 -0.0537 0.0427  71  TYR   A CD2   
444  C  CE1   . TYR   A 74  ? 0.1718 0.3673 0.4599 -0.0584 -0.0448 -0.0020 71  TYR   A CE1   
445  C  CE2   . TYR   A 74  ? 0.1738 0.4068 0.5063 -0.0260 -0.0830 0.0068  71  TYR   A CE2   
446  C  CZ    . TYR   A 74  ? 0.1557 0.4339 0.5217 -0.0266 -0.0572 0.0061  71  TYR   A CZ    
447  O  OH    . TYR   A 74  ? 0.1769 0.4737 0.5453 -0.0115 -0.0389 -0.0331 71  TYR   A OH    
448  N  N     . MET   A 75  ? 0.1023 0.3213 0.4954 -0.0489 -0.0241 -0.0026 72  MET   A N     
449  C  CA    . MET   A 75  ? 0.1909 0.3214 0.4483 -0.0676 -0.0699 -0.0334 72  MET   A CA    
450  C  C     . MET   A 75  ? 0.2243 0.3722 0.4873 -0.0674 -0.1168 0.0435  72  MET   A C     
451  O  O     . MET   A 75  ? 0.2530 0.3668 0.5834 -0.0492 -0.1427 0.0291  72  MET   A O     
452  C  CB    . MET   A 75  ? 0.2338 0.3476 0.4379 -0.0679 -0.0565 -0.0414 72  MET   A CB    
453  C  CG    . MET   A 75  ? 0.2396 0.3486 0.3909 -0.0580 -0.0373 -0.0369 72  MET   A CG    
454  S  SD    . MET   A 75  ? 0.2212 0.4020 0.4397 -0.0280 0.0031  -0.0046 72  MET   A SD    
455  C  CE    . MET   A 75  ? 0.2291 0.4524 0.4319 0.0430  -0.0253 0.0119  72  MET   A CE    
456  N  N     . ARG   A 76  ? 0.1931 0.3620 0.5745 -0.0417 -0.0850 0.0132  73  ARG   A N     
457  C  CA    . ARG   A 76  ? 0.1996 0.4260 0.6385 -0.0304 -0.1086 0.0297  73  ARG   A CA    
458  C  C     . ARG   A 76  ? 0.1763 0.3451 0.6265 -0.0600 -0.1197 0.0457  73  ARG   A C     
459  O  O     . ARG   A 76  ? 0.2019 0.3951 0.7147 -0.0074 -0.1045 0.0503  73  ARG   A O     
460  C  CB    . ARG   A 76  ? 0.1266 0.4392 0.7749 -0.0299 -0.0765 0.0217  73  ARG   A CB    
461  C  CG    . ARG   A 76  ? 0.3742 0.5373 0.7676 -0.0384 -0.2080 0.0136  73  ARG   A CG    
462  C  CD    . ARG   A 76  ? 0.4221 0.6126 0.8476 -0.0957 -0.1576 -0.0947 73  ARG   A CD    
463  N  NE    . ARG   A 76  ? 0.5411 0.7175 0.8962 0.0536  -0.1019 -0.0383 73  ARG   A NE    
464  C  CZ    . ARG   A 76  ? 0.5835 0.6693 0.8981 0.0477  -0.0454 -0.0104 73  ARG   A CZ    
465  N  NH1   . ARG   A 76  ? 0.6352 0.7081 0.8944 0.0299  -0.0201 0.0050  73  ARG   A NH1   
466  N  NH2   . ARG   A 76  ? 0.5251 0.6548 0.8824 0.0356  -0.1092 -0.0359 73  ARG   A NH2   
467  N  N     . THR   A 77  ? 0.1250 0.4472 0.5814 -0.0618 -0.0136 0.0105  74  THR   A N     
468  C  CA    . THR   A 77  ? 0.1499 0.4254 0.5284 -0.0817 -0.0264 0.0212  74  THR   A CA    
469  C  C     . THR   A 77  ? 0.1022 0.3982 0.4975 -0.0342 0.0443  0.0084  74  THR   A C     
470  O  O     . THR   A 77  ? 0.0998 0.4044 0.4895 -0.0123 0.0120  0.0057  74  THR   A O     
471  C  CB    . THR   A 77  ? 0.1725 0.4808 0.5149 -0.1076 -0.0480 0.0265  74  THR   A CB    
472  O  OG1   . THR   A 77  ? 0.1798 0.4895 0.6285 -0.1114 -0.0001 -0.0275 74  THR   A OG1   
473  C  CG2   . THR   A 77  ? 0.1804 0.5129 0.5162 -0.1129 -0.0397 0.0379  74  THR   A CG2   
474  N  N     . GLY   A 78  ? 0.0912 0.3313 0.4227 -0.0103 0.0311  0.0168  75  GLY   A N     
475  C  CA    . GLY   A 78  ? 0.1978 0.3218 0.3810 -0.0245 0.0352  0.0273  75  GLY   A CA    
476  C  C     . GLY   A 78  ? 0.0600 0.3693 0.3964 -0.0048 -0.0070 0.0041  75  GLY   A C     
477  O  O     . GLY   A 78  ? 0.0862 0.4211 0.4185 -0.0016 -0.0217 -0.0286 75  GLY   A O     
478  N  N     . GLU   A 79  ? 0.0360 0.3918 0.3816 0.0120  0.0068  0.0188  76  GLU   A N     
479  C  CA    . GLU   A 79  ? 0.1137 0.3852 0.3959 0.0246  -0.0189 0.0255  76  GLU   A CA    
480  C  C     . GLU   A 79  ? 0.0898 0.3751 0.3922 0.0571  -0.0355 0.0647  76  GLU   A C     
481  O  O     . GLU   A 79  ? 0.1287 0.3853 0.4234 0.0390  -0.0239 0.0828  76  GLU   A O     
482  C  CB    . GLU   A 79  ? 0.1067 0.4641 0.4055 0.0299  -0.0137 0.0131  76  GLU   A CB    
483  C  CG    . GLU   A 79  ? 0.1055 0.5008 0.4777 0.0112  -0.0285 -0.0039 76  GLU   A CG    
484  C  CD    . GLU   A 79  ? 0.0981 0.6174 0.5063 0.0792  -0.0472 -0.0650 76  GLU   A CD    
485  O  OE1   . GLU   A 79  ? 0.1169 0.6086 0.5101 0.0553  -0.0342 -0.0664 76  GLU   A OE1   
486  O  OE2   . GLU   A 79  ? 0.1874 0.7544 0.6555 -0.0691 -0.0120 -0.0752 76  GLU   A OE2   
487  N  N     . GLY   A 80  ? 0.1182 0.3222 0.3649 0.0173  -0.0536 0.0374  77  GLY   A N     
488  C  CA    . GLY   A 80  ? 0.1363 0.3269 0.3781 0.0164  -0.0185 0.0285  77  GLY   A CA    
489  C  C     . GLY   A 80  ? 0.1408 0.3288 0.3142 0.0087  -0.0173 0.0334  77  GLY   A C     
490  O  O     . GLY   A 80  ? 0.0572 0.3290 0.3495 0.0195  -0.0011 0.0299  77  GLY   A O     
491  N  N     . PHE   A 81  ? 0.0947 0.2701 0.3502 0.0406  -0.0094 0.0153  78  PHE   A N     
492  C  CA    . PHE   A 81  ? 0.0840 0.2523 0.3377 0.0254  -0.0122 0.0109  78  PHE   A CA    
493  C  C     . PHE   A 81  ? 0.1281 0.2611 0.3432 -0.0028 0.0133  0.0101  78  PHE   A C     
494  O  O     . PHE   A 81  ? 0.0554 0.2857 0.3770 0.0351  -0.0127 0.0257  78  PHE   A O     
495  C  CB    . PHE   A 81  ? 0.1093 0.2617 0.3353 0.0163  0.0030  0.0188  78  PHE   A CB    
496  C  CG    . PHE   A 81  ? 0.1141 0.2818 0.3434 0.0088  -0.0101 0.0083  78  PHE   A CG    
497  C  CD1   . PHE   A 81  ? 0.1210 0.2903 0.3324 -0.0034 -0.0208 0.0112  78  PHE   A CD1   
498  C  CD2   . PHE   A 81  ? 0.0797 0.2934 0.3707 -0.0061 -0.0050 0.0171  78  PHE   A CD2   
499  C  CE1   . PHE   A 81  ? 0.1316 0.3002 0.3718 -0.0072 -0.0145 -0.0215 78  PHE   A CE1   
500  C  CE2   . PHE   A 81  ? 0.1293 0.2556 0.3618 -0.0059 -0.0333 -0.0018 78  PHE   A CE2   
501  C  CZ    . PHE   A 81  ? 0.1063 0.3262 0.3674 -0.0109 -0.0191 0.0139  78  PHE   A CZ    
502  N  N     . LEU   A 82  ? 0.0883 0.2687 0.3356 0.0013  0.0310  0.0315  79  LEU   A N     
503  C  CA    . LEU   A 82  ? 0.0673 0.2870 0.3671 0.0072  0.0244  0.0391  79  LEU   A CA    
504  C  C     . LEU   A 82  ? 0.1065 0.2921 0.3545 0.0350  -0.0048 0.0163  79  LEU   A C     
505  O  O     . LEU   A 82  ? 0.0531 0.3097 0.4051 0.0163  0.0179  0.0234  79  LEU   A O     
506  C  CB    . LEU   A 82  ? 0.1873 0.3579 0.3718 0.0344  0.0004  0.0460  79  LEU   A CB    
507  C  CG    . LEU   A 82  ? 0.3102 0.3813 0.3924 0.0399  -0.0195 0.0249  79  LEU   A CG    
508  C  CD1   . LEU   A 82  ? 0.3836 0.4031 0.3676 -0.0384 -0.0227 0.0279  79  LEU   A CD1   
509  C  CD2   . LEU   A 82  ? 0.2303 0.3275 0.3853 0.0983  -0.0153 -0.0022 79  LEU   A CD2   
510  N  N     . CYS   A 83  ? 0.0751 0.3009 0.3465 0.0294  -0.0120 0.0142  80  CYS   A N     
511  C  CA    . CYS   A 83  ? 0.0509 0.3212 0.3769 0.0139  0.0075  0.0148  80  CYS   A CA    
512  C  C     . CYS   A 83  ? 0.0756 0.3088 0.3511 -0.0129 0.0130  0.0100  80  CYS   A C     
513  O  O     . CYS   A 83  ? 0.0649 0.3302 0.3735 0.0157  -0.0016 0.0200  80  CYS   A O     
514  C  CB    . CYS   A 83  ? 0.0811 0.3407 0.3889 -0.0228 0.0180  0.0126  80  CYS   A CB    
515  S  SG    . CYS   A 83  ? 0.1260 0.4224 0.4151 -0.0305 -0.0341 0.0140  80  CYS   A SG    
516  N  N     . VAL   A 84  ? 0.0769 0.2884 0.3571 -0.0202 -0.0088 -0.0061 81  VAL   A N     
517  C  CA    . VAL   A 84  ? 0.0275 0.3179 0.3632 -0.0027 0.0081  -0.0075 81  VAL   A CA    
518  C  C     . VAL   A 84  ? 0.0516 0.3010 0.3578 -0.0060 0.0288  -0.0054 81  VAL   A C     
519  O  O     . VAL   A 84  ? 0.0547 0.3320 0.3898 0.0050  -0.0053 -0.0268 81  VAL   A O     
520  C  CB    . VAL   A 84  ? 0.0550 0.3111 0.3674 -0.0288 0.0247  -0.0147 81  VAL   A CB    
521  C  CG1   . VAL   A 84  ? 0.0538 0.3393 0.3714 -0.0417 0.0346  -0.0220 81  VAL   A CG1   
522  C  CG2   . VAL   A 84  ? 0.0735 0.3120 0.3541 0.0034  0.0263  -0.0015 81  VAL   A CG2   
523  N  N     . PHE   A 85  ? 0.0239 0.3372 0.3817 -0.0117 0.0148  -0.0025 82  PHE   A N     
524  C  CA    . PHE   A 85  ? 0.0336 0.3805 0.3530 0.0082  0.0114  -0.0072 82  PHE   A CA    
525  C  C     . PHE   A 85  ? 0.0687 0.3796 0.3811 -0.0181 0.0294  -0.0555 82  PHE   A C     
526  O  O     . PHE   A 85  ? 0.0546 0.3767 0.3866 -0.0002 -0.0008 -0.0360 82  PHE   A O     
527  C  CB    . PHE   A 85  ? 0.0386 0.4033 0.3465 -0.0028 0.0068  -0.0272 82  PHE   A CB    
528  C  CG    . PHE   A 85  ? 0.0751 0.4061 0.3307 -0.0385 0.0048  -0.0151 82  PHE   A CG    
529  C  CD1   . PHE   A 85  ? 0.1089 0.3613 0.3237 -0.0265 0.0191  -0.0236 82  PHE   A CD1   
530  C  CD2   . PHE   A 85  ? 0.1040 0.4018 0.3567 -0.0607 -0.0148 -0.0188 82  PHE   A CD2   
531  C  CE1   . PHE   A 85  ? 0.1117 0.3770 0.3379 -0.0531 0.0058  -0.0186 82  PHE   A CE1   
532  C  CE2   . PHE   A 85  ? 0.1169 0.3997 0.3588 -0.0630 0.0237  -0.0099 82  PHE   A CE2   
533  C  CZ    . PHE   A 85  ? 0.1267 0.3829 0.3591 -0.0645 -0.0066 -0.0139 82  PHE   A CZ    
534  N  N     . ALA   A 86  ? 0.0877 0.3808 0.3715 -0.0097 0.0034  -0.0477 83  ALA   A N     
535  C  CA    . ALA   A 86  ? 0.1061 0.4359 0.3522 -0.0612 0.0268  -0.0328 83  ALA   A CA    
536  C  C     . ALA   A 86  ? 0.0995 0.4656 0.3339 -0.0863 -0.0099 -0.0231 83  ALA   A C     
537  O  O     . ALA   A 86  ? 0.0941 0.5260 0.3437 -0.0708 0.0094  -0.0490 83  ALA   A O     
538  C  CB    . ALA   A 86  ? 0.0640 0.4723 0.3731 -0.0604 -0.0159 -0.0171 83  ALA   A CB    
539  N  N     . ILE   A 87  ? 0.1005 0.4957 0.3700 -0.1123 0.0222  -0.0416 84  ILE   A N     
540  C  CA    . ILE   A 87  ? 0.1340 0.5783 0.4057 -0.1339 0.0477  -0.0115 84  ILE   A CA    
541  C  C     . ILE   A 87  ? 0.2033 0.5774 0.4338 -0.0599 0.0467  -0.0163 84  ILE   A C     
542  O  O     . ILE   A 87  ? 0.1075 0.6477 0.4461 -0.1166 0.0045  -0.0165 84  ILE   A O     
543  C  CB    . ILE   A 87  ? 0.1644 0.5666 0.3871 -0.1162 0.0337  -0.0043 84  ILE   A CB    
544  C  CG1   . ILE   A 87  ? 0.2169 0.6617 0.4233 -0.1076 -0.0149 -0.0285 84  ILE   A CG1   
545  C  CG2   . ILE   A 87  ? 0.1341 0.5776 0.4345 -0.1351 0.0562  -0.0003 84  ILE   A CG2   
546  C  CD1   . ILE   A 87  ? 0.3167 0.6628 0.4517 -0.1524 0.0237  -0.0346 84  ILE   A CD1   
547  N  N     . ASN   A 88  ? 0.0635 0.6087 0.4068 -0.0505 0.0315  -0.0283 85  ASN   A N     
548  C  CA    . ASN   A 88  ? 0.0840 0.6330 0.4271 -0.0218 -0.0005 -0.0353 85  ASN   A CA    
549  C  C     . ASN   A 88  ? 0.1404 0.6327 0.4401 -0.0487 -0.0177 -0.0238 85  ASN   A C     
550  O  O     . ASN   A 88  ? 0.1063 0.6983 0.5260 -0.0420 -0.0424 -0.0090 85  ASN   A O     
551  C  CB    . ASN   A 88  ? 0.0918 0.7656 0.4258 -0.0223 -0.0085 -0.0345 85  ASN   A CB    
552  C  CG    . ASN   A 88  ? 0.1493 0.8075 0.4327 -0.0620 -0.0977 0.0407  85  ASN   A CG    
553  O  OD1   . ASN   A 88  ? 0.1104 0.7621 0.4422 -0.0109 -0.0151 0.0125  85  ASN   A OD1   
554  N  ND2   . ASN   A 88  ? 0.1688 0.8035 0.4436 0.0828  -0.0518 -0.0078 85  ASN   A ND2   
555  N  N     . ASN   A 89  ? 0.0756 0.5962 0.4329 0.0010  0.0089  -0.0331 86  ASN   A N     
556  C  CA    . ASN   A 89  ? 0.0455 0.5952 0.4211 0.0137  0.0163  -0.0249 86  ASN   A CA    
557  C  C     . ASN   A 89  ? 0.0777 0.6157 0.4140 0.0492  0.0268  0.0093  86  ASN   A C     
558  O  O     . ASN   A 89  ? 0.0636 0.5039 0.4116 0.0216  0.0272  0.0093  86  ASN   A O     
559  C  CB    . ASN   A 89  ? 0.1302 0.5475 0.4432 -0.0057 -0.0130 -0.0058 86  ASN   A CB    
560  C  CG    . ASN   A 89  ? 0.0822 0.5233 0.4505 0.0666  -0.0010 -0.0030 86  ASN   A CG    
561  O  OD1   . ASN   A 89  ? 0.1453 0.4901 0.4272 0.0574  -0.0391 -0.0098 86  ASN   A OD1   
562  N  ND2   . ASN   A 89  ? 0.1181 0.5798 0.5373 0.0273  0.0237  0.0047  86  ASN   A ND2   
563  N  N     . THR   A 90  ? 0.0484 0.5856 0.4201 0.0089  0.0234  -0.0088 87  THR   A N     
564  C  CA    . THR   A 90  ? 0.1203 0.5271 0.3985 -0.0206 0.0453  -0.0123 87  THR   A CA    
565  C  C     . THR   A 90  ? 0.1074 0.4601 0.3655 0.0223  0.0359  0.0028  87  THR   A C     
566  O  O     . THR   A 90  ? 0.0899 0.4652 0.4414 0.0143  0.0137  0.0058  87  THR   A O     
567  C  CB    . THR   A 90  ? 0.1454 0.5928 0.4461 -0.0027 0.0828  -0.0051 87  THR   A CB    
568  O  OG1   . THR   A 90  ? 0.2656 0.6788 0.5321 0.0929  0.0547  -0.0155 87  THR   A OG1   
569  C  CG2   . THR   A 90  ? 0.0816 0.6447 0.4921 -0.0145 0.0540  -0.0236 87  THR   A CG2   
570  N  N     . LYS   A 91  ? 0.0539 0.4816 0.4106 0.0558  0.0166  0.0229  88  LYS   A N     
571  C  CA    . LYS   A 91  ? 0.1106 0.4734 0.4155 0.0570  0.0390  -0.0168 88  LYS   A CA    
572  C  C     . LYS   A 91  ? 0.0951 0.4763 0.3560 0.0246  0.0313  -0.0108 88  LYS   A C     
573  O  O     . LYS   A 91  ? 0.1631 0.4558 0.3804 0.0702  -0.0288 -0.0445 88  LYS   A O     
574  C  CB    . LYS   A 91  ? 0.0550 0.5152 0.4914 0.0689  -0.0134 0.0209  88  LYS   A CB    
575  C  CG    . LYS   A 91  ? 0.1791 0.4647 0.5547 0.0792  -0.0129 0.0074  88  LYS   A CG    
576  C  CD    . LYS   A 91  ? 0.2388 0.5025 0.5909 0.1160  -0.0222 0.0351  88  LYS   A CD    
577  C  CE    . LYS   A 91  ? 0.2615 0.5393 0.6536 0.0909  -0.0031 0.0360  88  LYS   A CE    
578  N  NZ    . LYS   A 91  ? 0.2798 0.5673 0.6771 0.0733  0.0183  0.0618  88  LYS   A NZ    
579  N  N     . SER   A 92  ? 0.0696 0.4620 0.3574 0.0536  0.0182  -0.0100 89  SER   A N     
580  C  CA    . SER   A 92  ? 0.0289 0.3882 0.3901 -0.0272 0.0180  -0.0198 89  SER   A CA    
581  C  C     . SER   A 92  ? 0.1127 0.4045 0.3335 -0.0230 0.0082  -0.0069 89  SER   A C     
582  O  O     . SER   A 92  ? 0.0934 0.3490 0.3675 0.0159  0.0171  -0.0199 89  SER   A O     
583  C  CB    . SER   A 92  ? 0.0910 0.4056 0.3809 0.0239  0.0296  -0.0096 89  SER   A CB    
584  O  OG    . SER   A 92  ? 0.0397 0.4384 0.4000 0.0150  0.0181  -0.0269 89  SER   A OG    
585  N  N     . PHE   A 93  ? 0.0839 0.3778 0.3744 -0.0021 0.0132  -0.0147 90  PHE   A N     
586  C  CA    . PHE   A 93  ? 0.1174 0.3466 0.3382 -0.0175 0.0531  -0.0138 90  PHE   A CA    
587  C  C     . PHE   A 93  ? 0.1121 0.3891 0.3410 0.0216  0.0138  -0.0133 90  PHE   A C     
588  O  O     . PHE   A 93  ? 0.0960 0.3598 0.3792 0.0032  0.0008  -0.0086 90  PHE   A O     
589  C  CB    . PHE   A 93  ? 0.1113 0.3830 0.3503 -0.0458 0.0307  -0.0257 90  PHE   A CB    
590  C  CG    . PHE   A 93  ? 0.1405 0.3653 0.3546 -0.0646 0.0195  -0.0175 90  PHE   A CG    
591  C  CD1   . PHE   A 93  ? 0.1211 0.3846 0.3378 -0.0665 0.0313  0.0044  90  PHE   A CD1   
592  C  CD2   . PHE   A 93  ? 0.1247 0.4412 0.3561 -0.0658 0.0090  -0.0278 90  PHE   A CD2   
593  C  CE1   . PHE   A 93  ? 0.1151 0.3674 0.3737 -0.0723 0.0120  0.0056  90  PHE   A CE1   
594  C  CE2   . PHE   A 93  ? 0.2260 0.3774 0.3939 -0.0735 0.0726  -0.0045 90  PHE   A CE2   
595  C  CZ    . PHE   A 93  ? 0.2029 0.4027 0.3681 -0.0505 0.0195  -0.0023 90  PHE   A CZ    
596  N  N     . GLU   A 94  ? 0.1033 0.3949 0.3737 0.0234  0.0208  -0.0286 91  GLU   A N     
597  C  CA    . GLU   A 94  ? 0.1706 0.3649 0.3699 0.0043  0.0327  -0.0069 91  GLU   A CA    
598  C  C     . GLU   A 94  ? 0.1560 0.3705 0.3611 0.0054  0.0209  -0.0173 91  GLU   A C     
599  O  O     . GLU   A 94  ? 0.1655 0.4512 0.3624 0.0057  0.0148  -0.0228 91  GLU   A O     
600  C  CB    . GLU   A 94  ? 0.1582 0.3840 0.3907 0.0127  0.0143  -0.0221 91  GLU   A CB    
601  C  CG    . GLU   A 94  ? 0.2001 0.4478 0.4663 0.0034  0.0955  -0.0057 91  GLU   A CG    
602  C  CD    . GLU   A 94  ? 0.3042 0.4892 0.4873 0.0103  0.0818  0.0081  91  GLU   A CD    
603  O  OE1   . GLU   A 94  ? 0.2964 0.6828 0.6006 -0.0429 0.0658  -0.0378 91  GLU   A OE1   
604  O  OE2   . GLU   A 94  ? 0.4382 0.4749 0.6901 0.0184  0.0740  -0.0545 91  GLU   A OE2   
605  N  N     . ASP   A 95  ? 0.1122 0.3118 0.3709 0.0059  -0.0042 -0.0245 92  ASP   A N     
606  C  CA    . ASP   A 95  ? 0.1102 0.3349 0.3887 0.0060  0.0264  -0.0102 92  ASP   A CA    
607  C  C     . ASP   A 95  ? 0.1033 0.3175 0.3901 0.0026  0.0159  0.0007  92  ASP   A C     
608  O  O     . ASP   A 95  ? 0.1352 0.2872 0.3556 -0.0058 0.0097  -0.0117 92  ASP   A O     
609  C  CB    . ASP   A 95  ? 0.1135 0.3749 0.4628 0.0126  -0.0071 0.0327  92  ASP   A CB    
610  C  CG    . ASP   A 95  ? 0.2081 0.3740 0.4898 0.0490  -0.0224 0.0208  92  ASP   A CG    
611  O  OD1   . ASP   A 95  ? 0.1801 0.4633 0.5174 0.0915  -0.0006 0.0413  92  ASP   A OD1   
612  O  OD2   . ASP   A 95  ? 0.1736 0.4887 0.5581 0.0344  -0.0435 0.0942  92  ASP   A OD2   
613  N  N     . ILE   A 96  ? 0.0905 0.3137 0.3626 0.0343  0.0186  0.0060  93  ILE   A N     
614  C  CA    . ILE   A 96  ? 0.1150 0.3269 0.3562 0.0604  0.0495  -0.0140 93  ILE   A CA    
615  C  C     . ILE   A 96  ? 0.1154 0.3274 0.3408 0.0222  0.0519  -0.0043 93  ILE   A C     
616  O  O     . ILE   A 96  ? 0.1005 0.3466 0.3682 0.0151  0.0388  -0.0039 93  ILE   A O     
617  C  CB    . ILE   A 96  ? 0.1362 0.3289 0.3507 0.0725  0.0075  -0.0110 93  ILE   A CB    
618  C  CG1   . ILE   A 96  ? 0.0865 0.3835 0.3653 0.0671  0.0182  -0.0205 93  ILE   A CG1   
619  C  CG2   . ILE   A 96  ? 0.1150 0.3496 0.4017 0.0611  -0.0144 -0.0320 93  ILE   A CG2   
620  C  CD1   . ILE   A 96  ? 0.1450 0.3838 0.3354 0.0832  0.0127  -0.0169 93  ILE   A CD1   
621  N  N     . HIS   A 97  ? 0.1193 0.3048 0.3277 0.0065  0.0401  -0.0075 94  HIS   A N     
622  C  CA    . HIS   A 97  ? 0.1623 0.2959 0.3228 0.0281  0.0327  -0.0251 94  HIS   A CA    
623  C  C     . HIS   A 97  ? 0.1054 0.3370 0.3297 -0.0003 -0.0004 -0.0006 94  HIS   A C     
624  O  O     . HIS   A 97  ? 0.0788 0.3536 0.3702 0.0078  0.0151  -0.0052 94  HIS   A O     
625  C  CB    . HIS   A 97  ? 0.1357 0.3061 0.3289 0.0110  0.0231  -0.0174 94  HIS   A CB    
626  C  CG    . HIS   A 97  ? 0.1138 0.3472 0.3302 -0.0061 0.0556  -0.0288 94  HIS   A CG    
627  N  ND1   . HIS   A 97  ? 0.1034 0.3744 0.3361 -0.0401 0.0328  -0.0080 94  HIS   A ND1   
628  C  CD2   . HIS   A 97  ? 0.1197 0.3443 0.3426 0.0079  0.0154  -0.0093 94  HIS   A CD2   
629  C  CE1   . HIS   A 97  ? 0.2100 0.3655 0.3439 0.0110  0.0132  -0.0225 94  HIS   A CE1   
630  N  NE2   . HIS   A 97  ? 0.1195 0.3891 0.3664 -0.0448 -0.0062 -0.0011 94  HIS   A NE2   
631  N  N     . HIS   A 98  ? 0.1213 0.3045 0.3802 0.0160  0.0242  -0.0062 95  HIS   A N     
632  C  CA    . HIS   A 98  ? 0.1706 0.2977 0.3687 0.0116  0.0336  -0.0057 95  HIS   A CA    
633  C  C     . HIS   A 98  ? 0.1139 0.2845 0.3637 -0.0255 0.0066  -0.0202 95  HIS   A C     
634  O  O     . HIS   A 98  ? 0.1214 0.3286 0.4236 -0.0558 0.0234  -0.0412 95  HIS   A O     
635  C  CB    . HIS   A 98  ? 0.1582 0.3042 0.4141 0.0069  0.0173  0.0008  95  HIS   A CB    
636  C  CG    . HIS   A 98  ? 0.2793 0.3708 0.4404 -0.0376 0.0882  -0.0056 95  HIS   A CG    
637  N  ND1   . HIS   A 98  ? 0.3055 0.4127 0.5328 -0.0495 0.0980  -0.0577 95  HIS   A ND1   
638  C  CD2   . HIS   A 98  ? 0.2030 0.3868 0.4173 0.0104  0.0929  -0.0150 95  HIS   A CD2   
639  C  CE1   . HIS   A 98  ? 0.3526 0.4274 0.5457 -0.0654 0.1344  -0.0440 95  HIS   A CE1   
640  N  NE2   . HIS   A 98  ? 0.1963 0.3635 0.4827 0.0069  0.1443  -0.0101 95  HIS   A NE2   
641  N  N     . TYR   A 99  ? 0.1070 0.3044 0.3671 -0.0145 0.0131  -0.0276 96  TYR   A N     
642  C  CA    . TYR   A 99  ? 0.1687 0.3061 0.3507 0.0037  0.0492  0.0086  96  TYR   A CA    
643  C  C     . TYR   A 99  ? 0.1178 0.3045 0.3882 -0.0170 0.0181  -0.0200 96  TYR   A C     
644  O  O     . TYR   A 99  ? 0.1314 0.3284 0.3786 -0.0331 0.0192  0.0191  96  TYR   A O     
645  C  CB    . TYR   A 99  ? 0.1732 0.3084 0.3472 0.0139  0.0447  0.0116  96  TYR   A CB    
646  C  CG    . TYR   A 99  ? 0.1980 0.3142 0.3602 0.0298  0.0500  0.0269  96  TYR   A CG    
647  C  CD1   . TYR   A 99  ? 0.1941 0.3056 0.4264 0.0165  0.0691  0.0256  96  TYR   A CD1   
648  C  CD2   . TYR   A 99  ? 0.2049 0.3249 0.3719 -0.0192 0.0068  0.0355  96  TYR   A CD2   
649  C  CE1   . TYR   A 99  ? 0.1945 0.3161 0.4394 -0.0412 0.0339  0.0602  96  TYR   A CE1   
650  C  CE2   . TYR   A 99  ? 0.2243 0.3306 0.3851 0.0094  0.0143  0.0337  96  TYR   A CE2   
651  C  CZ    . TYR   A 99  ? 0.1797 0.3140 0.4273 0.0113  -0.0087 0.0476  96  TYR   A CZ    
652  O  OH    . TYR   A 99  ? 0.1777 0.3761 0.4738 0.0178  -0.0391 0.0588  96  TYR   A OH    
653  N  N     A ARG   A 100 ? 0.1116 0.3128 0.3823 0.0165  0.0099  -0.0009 97  ARG   A N     
654  N  N     B ARG   A 100 ? 0.0988 0.3156 0.3828 0.0039  0.0206  -0.0016 97  ARG   A N     
655  C  CA    A ARG   A 100 ? 0.1344 0.3122 0.3914 0.0369  0.0060  -0.0099 97  ARG   A CA    
656  C  CA    B ARG   A 100 ? 0.1290 0.3174 0.4023 0.0270  0.0092  -0.0115 97  ARG   A CA    
657  C  C     A ARG   A 100 ? 0.0766 0.3326 0.4097 -0.0047 0.0322  -0.0166 97  ARG   A C     
658  C  C     B ARG   A 100 ? 0.0641 0.3315 0.4104 -0.0089 0.0363  -0.0131 97  ARG   A C     
659  O  O     A ARG   A 100 ? 0.0733 0.3741 0.4056 0.0054  -0.0162 -0.0176 97  ARG   A O     
660  O  O     B ARG   A 100 ? 0.0650 0.3770 0.4130 0.0030  -0.0230 -0.0191 97  ARG   A O     
661  C  CB    A ARG   A 100 ? 0.1140 0.3278 0.4268 0.0321  -0.0039 0.0115  97  ARG   A CB    
662  C  CB    B ARG   A 100 ? 0.1116 0.3374 0.4574 0.0143  -0.0026 0.0111  97  ARG   A CB    
663  C  CG    A ARG   A 100 ? 0.1712 0.3302 0.4290 0.0368  -0.0149 0.0266  97  ARG   A CG    
664  C  CG    B ARG   A 100 ? 0.1768 0.3561 0.4795 0.0252  -0.0244 0.0280  97  ARG   A CG    
665  C  CD    A ARG   A 100 ? 0.2056 0.3428 0.4329 0.0101  -0.0106 0.0237  97  ARG   A CD    
666  C  CD    B ARG   A 100 ? 0.2296 0.3782 0.5155 -0.0176 -0.0211 0.0237  97  ARG   A CD    
667  N  NE    A ARG   A 100 ? 0.2507 0.3708 0.4039 0.0038  0.0007  0.0354  97  ARG   A NE    
668  N  NE    B ARG   A 100 ? 0.3165 0.4170 0.5443 -0.0045 -0.0569 0.0475  97  ARG   A NE    
669  C  CZ    A ARG   A 100 ? 0.2417 0.3580 0.4109 0.0091  -0.0118 0.0146  97  ARG   A CZ    
670  C  CZ    B ARG   A 100 ? 0.3284 0.4544 0.5359 -0.0162 -0.0573 0.0020  97  ARG   A CZ    
671  N  NH1   A ARG   A 100 ? 0.2132 0.3576 0.3463 -0.0154 0.0107  0.0017  97  ARG   A NH1   
672  N  NH1   B ARG   A 100 ? 0.3321 0.4316 0.5563 -0.0440 -0.0112 0.0452  97  ARG   A NH1   
673  N  NH2   A ARG   A 100 ? 0.2844 0.3796 0.4132 0.0094  -0.0085 0.0457  97  ARG   A NH2   
674  N  NH2   B ARG   A 100 ? 0.3823 0.4869 0.5709 0.0367  -0.0490 0.0231  97  ARG   A NH2   
675  N  N     . GLU   A 101 ? 0.0976 0.3443 0.3729 -0.0057 0.0330  -0.0204 98  GLU   A N     
676  C  CA    . GLU   A 101 ? 0.1909 0.3728 0.3668 -0.0224 0.0471  -0.0186 98  GLU   A CA    
677  C  C     . GLU   A 101 ? 0.1040 0.3949 0.3993 -0.0393 -0.0057 -0.0266 98  GLU   A C     
678  O  O     . GLU   A 101 ? 0.1113 0.4592 0.4117 -0.0710 -0.0040 -0.0400 98  GLU   A O     
679  C  CB    . GLU   A 101 ? 0.1630 0.4376 0.3974 -0.0331 0.0550  -0.0212 98  GLU   A CB    
680  C  CG    . GLU   A 101 ? 0.2017 0.4611 0.4288 -0.0927 0.0841  -0.0272 98  GLU   A CG    
681  C  CD    . GLU   A 101 ? 0.1737 0.4682 0.5241 -0.1320 0.1107  -0.0291 98  GLU   A CD    
682  O  OE1   . GLU   A 101 ? 0.2059 0.3901 0.3878 -0.1306 0.0667  -0.0196 98  GLU   A OE1   
683  O  OE2   . GLU   A 101 ? 0.3081 0.4962 0.5782 -0.0962 0.0640  -0.0768 98  GLU   A OE2   
684  N  N     . GLN   A 102 ? 0.1611 0.3637 0.3998 -0.0265 0.0363  -0.0039 99  GLN   A N     
685  C  CA    . GLN   A 102 ? 0.1777 0.3448 0.4375 -0.0440 0.0442  -0.0209 99  GLN   A CA    
686  C  C     . GLN   A 102 ? 0.1358 0.3295 0.4272 -0.0712 0.0295  -0.0190 99  GLN   A C     
687  O  O     . GLN   A 102 ? 0.1232 0.3530 0.4317 -0.0598 0.0010  -0.0113 99  GLN   A O     
688  C  CB    . GLN   A 102 ? 0.1916 0.3768 0.4931 -0.0193 0.0437  0.0238  99  GLN   A CB    
689  C  CG    . GLN   A 102 ? 0.2722 0.4245 0.5768 0.0257  0.0809  0.0100  99  GLN   A CG    
690  C  CD    . GLN   A 102 ? 0.4336 0.5230 0.6474 0.0891  0.0037  0.0231  99  GLN   A CD    
691  O  OE1   . GLN   A 102 ? 0.4649 0.6234 0.6568 0.1181  -0.0010 0.0158  99  GLN   A OE1   
692  N  NE2   . GLN   A 102 ? 0.5145 0.5935 0.7644 0.1736  0.0130  -0.0135 99  GLN   A NE2   
693  N  N     . ILE   A 103 ? 0.0687 0.3491 0.3931 -0.0388 0.0255  -0.0227 100 ILE   A N     
694  C  CA    . ILE   A 103 ? 0.1227 0.3672 0.4012 0.0052  0.0316  -0.0274 100 ILE   A CA    
695  C  C     . ILE   A 103 ? 0.1110 0.3936 0.3972 -0.0545 0.0131  -0.0158 100 ILE   A C     
696  O  O     . ILE   A 103 ? 0.1047 0.4796 0.4213 -0.0532 0.0144  -0.0129 100 ILE   A O     
697  C  CB    . ILE   A 103 ? 0.0566 0.3594 0.3940 0.0106  0.0016  -0.0164 100 ILE   A CB    
698  C  CG1   . ILE   A 103 ? 0.1591 0.3441 0.3582 -0.0129 0.0075  -0.0218 100 ILE   A CG1   
699  C  CG2   . ILE   A 103 ? 0.1357 0.3422 0.4331 0.0493  0.0006  -0.0345 100 ILE   A CG2   
700  C  CD1   . ILE   A 103 ? 0.0846 0.3802 0.3653 -0.0009 0.0227  -0.0379 100 ILE   A CD1   
701  N  N     . LYS   A 104 ? 0.1120 0.4278 0.3940 -0.0533 -0.0070 0.0061  101 LYS   A N     
702  C  CA    . LYS   A 104 ? 0.1493 0.4504 0.4068 -0.0060 -0.0292 -0.0087 101 LYS   A CA    
703  C  C     . LYS   A 104 ? 0.1055 0.4750 0.4171 -0.0517 -0.0154 0.0004  101 LYS   A C     
704  O  O     . LYS   A 104 ? 0.1204 0.5131 0.4855 -0.0556 -0.0648 -0.0307 101 LYS   A O     
705  C  CB    . LYS   A 104 ? 0.1637 0.4561 0.4412 -0.0262 -0.0727 0.0290  101 LYS   A CB    
706  C  CG    . LYS   A 104 ? 0.1502 0.4526 0.5420 0.0047  -0.0612 0.0053  101 LYS   A CG    
707  C  CD    . LYS   A 104 ? 0.3056 0.5556 0.5692 -0.0308 -0.0214 0.0534  101 LYS   A CD    
708  C  CE    . LYS   A 104 ? 0.4309 0.6534 0.6000 -0.0365 -0.0616 0.0218  101 LYS   A CE    
709  N  NZ    . LYS   A 104 ? 0.4983 0.7242 0.6533 -0.0708 -0.0216 -0.0056 101 LYS   A NZ    
710  N  N     . ARG   A 105 ? 0.1027 0.4596 0.4314 -0.0809 0.0032  -0.0315 102 ARG   A N     
711  C  CA    . ARG   A 105 ? 0.2100 0.4900 0.4596 -0.1357 -0.0146 -0.0351 102 ARG   A CA    
712  C  C     . ARG   A 105 ? 0.1922 0.5096 0.4761 -0.1278 -0.0222 -0.0196 102 ARG   A C     
713  O  O     . ARG   A 105 ? 0.1755 0.6321 0.5320 -0.1242 -0.0392 -0.0572 102 ARG   A O     
714  C  CB    . ARG   A 105 ? 0.2106 0.5075 0.5144 -0.1330 0.0005  -0.0523 102 ARG   A CB    
715  C  CG    . ARG   A 105 ? 0.3044 0.5561 0.5328 -0.1548 0.0063  -0.0877 102 ARG   A CG    
716  C  CD    . ARG   A 105 ? 0.3757 0.5803 0.6453 -0.1082 -0.0167 -0.0946 102 ARG   A CD    
717  N  NE    . ARG   A 105 ? 0.4914 0.6644 0.6729 -0.0995 0.0392  -0.0515 102 ARG   A NE    
718  C  CZ    . ARG   A 105 ? 0.5174 0.6876 0.6774 -0.1209 0.0187  -0.1030 102 ARG   A CZ    
719  N  NH1   . ARG   A 105 ? 0.4950 0.6442 0.6781 -0.1472 0.0409  -0.1481 102 ARG   A NH1   
720  N  NH2   . ARG   A 105 ? 0.6019 0.7211 0.6718 -0.0832 0.0253  -0.0853 102 ARG   A NH2   
721  N  N     . VAL   A 106 ? 0.1680 0.4844 0.4756 -0.1174 0.0116  -0.0501 103 VAL   A N     
722  C  CA    . VAL   A 106 ? 0.1897 0.5135 0.4795 -0.1223 0.0122  -0.0303 103 VAL   A CA    
723  C  C     . VAL   A 106 ? 0.1761 0.5076 0.5151 -0.1373 -0.0026 -0.0677 103 VAL   A C     
724  O  O     . VAL   A 106 ? 0.1742 0.6079 0.5843 -0.1618 -0.0362 -0.0380 103 VAL   A O     
725  C  CB    . VAL   A 106 ? 0.2732 0.5148 0.4930 -0.0963 -0.0068 -0.0117 103 VAL   A CB    
726  C  CG1   . VAL   A 106 ? 0.3678 0.5447 0.4878 -0.1322 0.0204  -0.0144 103 VAL   A CG1   
727  C  CG2   . VAL   A 106 ? 0.3392 0.4955 0.5095 -0.0802 -0.0710 -0.0175 103 VAL   A CG2   
728  N  N     . LYS   A 107 ? 0.1228 0.4904 0.5248 -0.0352 0.0026  -0.0252 104 LYS   A N     
729  C  CA    . LYS   A 107 ? 0.1317 0.5619 0.5627 0.0130  0.0157  -0.0503 104 LYS   A CA    
730  C  C     . LYS   A 107 ? 0.1278 0.6304 0.5873 -0.0041 0.0033  -0.0521 104 LYS   A C     
731  O  O     . LYS   A 107 ? 0.1839 0.7001 0.5846 0.0584  -0.0313 -0.0148 104 LYS   A O     
732  C  CB    . LYS   A 107 ? 0.2154 0.5539 0.5871 0.0104  0.0150  -0.0628 104 LYS   A CB    
733  C  CG    . LYS   A 107 ? 0.3573 0.5658 0.5789 -0.0719 -0.0506 -0.0862 104 LYS   A CG    
734  C  CD    . LYS   A 107 ? 0.3343 0.5261 0.6170 -0.0643 -0.0638 -0.0729 104 LYS   A CD    
735  C  CE    . LYS   A 107 ? 0.3895 0.5218 0.5196 -0.0618 -0.0338 -0.0338 104 LYS   A CE    
736  N  NZ    . LYS   A 107 ? 0.3579 0.6048 0.5111 -0.1376 -0.0362 -0.0296 104 LYS   A NZ    
737  N  N     . ASP   A 108 ? 0.1256 0.6780 0.5547 -0.0308 -0.0221 -0.0494 105 ASP   A N     
738  C  CA    . ASP   A 108 ? 0.2319 0.7656 0.6050 -0.0215 -0.0942 -0.0067 105 ASP   A CA    
739  C  C     . ASP   A 108 ? 0.1301 0.7788 0.6415 -0.0036 -0.1114 -0.0145 105 ASP   A C     
740  O  O     . ASP   A 108 ? 0.2378 0.8499 0.6334 0.1572  -0.1205 0.0204  105 ASP   A O     
741  C  CB    . ASP   A 108 ? 0.1621 0.8804 0.6520 0.0063  -0.1290 -0.0141 105 ASP   A CB    
742  C  CG    . ASP   A 108 ? 0.4184 0.9711 0.6585 0.0658  -0.0985 -0.0174 105 ASP   A CG    
743  O  OD1   . ASP   A 108 ? 0.4094 1.0160 0.6676 0.0160  0.0371  -0.0140 105 ASP   A OD1   
744  O  OD2   . ASP   A 108 ? 0.5468 1.0320 0.7351 0.0210  -0.2097 0.0410  105 ASP   A OD2   
745  N  N     . SER   A 109 ? 0.2827 0.7036 0.5962 -0.0240 -0.1804 0.0447  106 SER   A N     
746  C  CA    . SER   A 109 ? 0.3640 0.6842 0.6174 -0.0823 -0.0881 0.0105  106 SER   A CA    
747  C  C     . SER   A 109 ? 0.3572 0.7492 0.6818 -0.0843 -0.0205 0.0580  106 SER   A C     
748  O  O     . SER   A 109 ? 0.3185 0.7858 0.6334 -0.1491 -0.0390 0.0003  106 SER   A O     
749  C  CB    . SER   A 109 ? 0.4102 0.6595 0.6938 -0.0436 -0.0351 0.0193  106 SER   A CB    
750  O  OG    . SER   A 109 ? 0.3417 0.6649 0.7059 -0.0142 0.0030  -0.0075 106 SER   A OG    
751  N  N     . GLU   A 110 ? 0.4788 0.7690 0.7084 -0.1006 -0.0132 0.0745  107 GLU   A N     
752  C  CA    . GLU   A 110 ? 0.5337 0.7984 0.7596 -0.1381 0.0559  0.0360  107 GLU   A CA    
753  C  C     . GLU   A 110 ? 0.5131 0.8132 0.7142 -0.1045 0.0571  0.0523  107 GLU   A C     
754  O  O     . GLU   A 110 ? 0.6327 0.7937 0.7353 -0.1625 0.0021  0.0106  107 GLU   A O     
755  C  CB    . GLU   A 110 ? 0.7394 0.8885 0.7568 -0.1235 0.0369  0.0343  107 GLU   A CB    
756  C  CG    . GLU   A 110 ? 0.7552 0.9228 0.8847 -0.1028 0.0339  -0.0284 107 GLU   A CG    
757  C  CD    . GLU   A 110 ? 0.6681 0.9997 0.9344 -0.0960 0.0690  -0.0225 107 GLU   A CD    
758  O  OE1   . GLU   A 110 ? 0.5629 0.9799 1.0320 -0.0400 0.0410  0.0145  107 GLU   A OE1   
759  O  OE2   . GLU   A 110 ? 0.5064 1.0212 1.0739 -0.1060 0.0526  -0.0856 107 GLU   A OE2   
760  N  N     . ASP   A 111 ? 0.5096 0.7874 0.6042 0.0053  0.0023  0.0388  108 ASP   A N     
761  C  CA    . ASP   A 111 ? 0.4325 0.7107 0.5428 0.0189  -0.0592 0.0864  108 ASP   A CA    
762  C  C     . ASP   A 111 ? 0.2632 0.6529 0.4930 0.0212  -0.0661 0.0296  108 ASP   A C     
763  O  O     . ASP   A 111 ? 0.2489 0.6014 0.6597 0.0275  -0.0884 0.0627  108 ASP   A O     
764  C  CB    . ASP   A 111 ? 0.5170 0.7240 0.6491 0.0724  -0.0992 0.0759  108 ASP   A CB    
765  C  CG    . ASP   A 111 ? 0.6615 0.7883 0.7380 0.0398  -0.0640 0.0082  108 ASP   A CG    
766  O  OD1   . ASP   A 111 ? 0.7377 0.9350 0.8216 -0.0796 -0.0912 0.0339  108 ASP   A OD1   
767  O  OD2   . ASP   A 111 ? 0.6916 0.8460 0.9059 0.0558  -0.1141 0.0181  108 ASP   A OD2   
768  N  N     . VAL   A 112 ? 0.1655 0.5001 0.4253 0.0628  0.0012  0.0279  109 VAL   A N     
769  C  CA    . VAL   A 112 ? 0.1434 0.4176 0.4162 0.0435  0.0148  -0.0047 109 VAL   A CA    
770  C  C     . VAL   A 112 ? 0.1645 0.4074 0.3752 0.0415  0.0257  0.0080  109 VAL   A C     
771  O  O     . VAL   A 112 ? 0.1580 0.3796 0.3689 0.0541  0.0146  0.0297  109 VAL   A O     
772  C  CB    . VAL   A 112 ? 0.2048 0.4019 0.4359 0.0320  -0.0205 -0.0019 109 VAL   A CB    
773  C  CG1   . VAL   A 112 ? 0.1604 0.3847 0.4638 0.0159  -0.0397 0.0154  109 VAL   A CG1   
774  C  CG2   . VAL   A 112 ? 0.2442 0.4233 0.4541 0.0304  -0.0021 -0.0187 109 VAL   A CG2   
775  N  N     . PRO   A 113 ? 0.0818 0.3731 0.3785 0.0460  0.0109  0.0119  110 PRO   A N     
776  C  CA    . PRO   A 113 ? 0.1378 0.3499 0.3787 0.0529  0.0046  0.0139  110 PRO   A CA    
777  C  C     . PRO   A 113 ? 0.1440 0.3177 0.3892 0.0267  -0.0095 0.0310  110 PRO   A C     
778  O  O     . PRO   A 113 ? 0.0627 0.3235 0.3864 0.0292  0.0069  0.0179  110 PRO   A O     
779  C  CB    . PRO   A 113 ? 0.1258 0.3783 0.3719 0.0732  -0.0079 0.0204  110 PRO   A CB    
780  C  CG    . PRO   A 113 ? 0.1045 0.4178 0.3925 0.0661  -0.0031 0.0389  110 PRO   A CG    
781  C  CD    . PRO   A 113 ? 0.0643 0.4225 0.3829 0.0584  -0.0094 0.0252  110 PRO   A CD    
782  N  N     . MET   A 114 ? 0.1362 0.3198 0.3552 0.0313  -0.0149 0.0544  111 MET   A N     
783  C  CA    . MET   A 114 ? 0.1294 0.3200 0.3469 0.0370  -0.0137 0.0286  111 MET   A CA    
784  C  C     . MET   A 114 ? 0.1994 0.3125 0.3235 0.0058  0.0369  0.0369  111 MET   A C     
785  O  O     . MET   A 114 ? 0.1373 0.3186 0.3576 0.0164  0.0178  0.0289  111 MET   A O     
786  C  CB    . MET   A 114 ? 0.2649 0.3648 0.3509 0.0403  0.0002  -0.0034 111 MET   A CB    
787  C  CG    . MET   A 114 ? 0.3021 0.3715 0.3790 0.0782  -0.0064 -0.0262 111 MET   A CG    
788  S  SD    . MET   A 114 ? 0.3331 0.5228 0.4800 0.1674  0.0039  -0.0678 111 MET   A SD    
789  C  CE    . MET   A 114 ? 0.4461 0.5529 0.4530 0.1150  0.0135  -0.0907 111 MET   A CE    
790  N  N     . VAL   A 115 ? 0.1705 0.2801 0.3369 0.0395  0.0397  0.0175  112 VAL   A N     
791  C  CA    . VAL   A 115 ? 0.1706 0.2644 0.3385 0.0434  0.0087  0.0185  112 VAL   A CA    
792  C  C     . VAL   A 115 ? 0.1484 0.2850 0.3099 0.0255  -0.0011 0.0264  112 VAL   A C     
793  O  O     . VAL   A 115 ? 0.1149 0.2715 0.3640 0.0228  0.0144  0.0083  112 VAL   A O     
794  C  CB    . VAL   A 115 ? 0.1586 0.2702 0.3335 0.0366  0.0114  0.0135  112 VAL   A CB    
795  C  CG1   . VAL   A 115 ? 0.1671 0.3176 0.3481 0.0169  0.0067  0.0042  112 VAL   A CG1   
796  C  CG2   . VAL   A 115 ? 0.1814 0.2906 0.3610 0.0629  0.0144  0.0027  112 VAL   A CG2   
797  N  N     . LEU   A 116 ? 0.1555 0.2586 0.3319 0.0363  0.0225  0.0167  113 LEU   A N     
798  C  CA    . LEU   A 116 ? 0.1473 0.2903 0.3178 0.0343  -0.0104 -0.0170 113 LEU   A CA    
799  C  C     . LEU   A 116 ? 0.1285 0.3002 0.3072 -0.0152 0.0450  -0.0193 113 LEU   A C     
800  O  O     . LEU   A 116 ? 0.1972 0.3065 0.3440 -0.0129 0.0355  -0.0251 113 LEU   A O     
801  C  CB    . LEU   A 116 ? 0.1558 0.3035 0.3271 0.0404  -0.0003 -0.0180 113 LEU   A CB    
802  C  CG    . LEU   A 116 ? 0.1071 0.3495 0.3409 -0.0082 0.0051  -0.0165 113 LEU   A CG    
803  C  CD1   . LEU   A 116 ? 0.1616 0.3550 0.3782 -0.0002 0.0567  0.0089  113 LEU   A CD1   
804  C  CD2   . LEU   A 116 ? 0.1638 0.3665 0.3494 -0.0073 0.0190  -0.0079 113 LEU   A CD2   
805  N  N     . VAL   A 117 ? 0.1323 0.3211 0.3128 -0.0231 0.0256  -0.0096 114 VAL   A N     
806  C  CA    . VAL   A 117 ? 0.1413 0.3266 0.3211 -0.0102 0.0038  -0.0011 114 VAL   A CA    
807  C  C     . VAL   A 117 ? 0.1267 0.3151 0.3341 -0.0515 0.0198  -0.0147 114 VAL   A C     
808  O  O     . VAL   A 117 ? 0.0757 0.3307 0.3638 -0.0227 -0.0080 -0.0054 114 VAL   A O     
809  C  CB    . VAL   A 117 ? 0.1876 0.3264 0.3188 0.0283  0.0299  0.0067  114 VAL   A CB    
810  C  CG1   . VAL   A 117 ? 0.1299 0.3822 0.3504 0.0194  0.0235  -0.0178 114 VAL   A CG1   
811  C  CG2   . VAL   A 117 ? 0.1830 0.3345 0.3421 0.0246  0.0558  -0.0280 114 VAL   A CG2   
812  N  N     . GLY   A 118 ? 0.1259 0.3790 0.3554 -0.0852 0.0290  -0.0279 115 GLY   A N     
813  C  CA    . GLY   A 118 ? 0.1175 0.4018 0.3605 -0.0947 0.0397  -0.0134 115 GLY   A CA    
814  C  C     . GLY   A 118 ? 0.0940 0.4202 0.3719 -0.0520 0.0376  -0.0204 115 GLY   A C     
815  O  O     . GLY   A 118 ? 0.1482 0.4512 0.3744 -0.0975 0.0358  -0.0523 115 GLY   A O     
816  N  N     . ASN   A 119 ? 0.1057 0.3828 0.3500 -0.0892 -0.0012 -0.0336 116 ASN   A N     
817  C  CA    . ASN   A 119 ? 0.1427 0.4347 0.3552 -0.0737 -0.0127 -0.0188 116 ASN   A CA    
818  C  C     . ASN   A 119 ? 0.1342 0.5222 0.3343 -0.1003 0.0125  -0.0051 116 ASN   A C     
819  O  O     . ASN   A 119 ? 0.1723 0.5668 0.3463 -0.1311 0.0335  -0.0295 116 ASN   A O     
820  C  CB    . ASN   A 119 ? 0.1045 0.4420 0.3571 -0.0572 0.0285  -0.0182 116 ASN   A CB    
821  C  CG    . ASN   A 119 ? 0.1397 0.4586 0.3610 -0.0692 0.0280  -0.0206 116 ASN   A CG    
822  O  OD1   . ASN   A 119 ? 0.1316 0.4703 0.3490 -0.0957 -0.0032 -0.0473 116 ASN   A OD1   
823  N  ND2   . ASN   A 119 ? 0.0400 0.4679 0.3640 -0.0435 -0.0112 -0.0237 116 ASN   A ND2   
824  N  N     . LYS   A 120 ? 0.1408 0.5172 0.3360 -0.0642 0.0064  -0.0412 117 LYS   A N     
825  C  CA    . LYS   A 120 ? 0.1574 0.5778 0.3909 -0.1286 -0.0324 -0.0603 117 LYS   A CA    
826  C  C     . LYS   A 120 ? 0.1880 0.5909 0.4081 -0.1401 0.0325  -0.0609 117 LYS   A C     
827  O  O     . LYS   A 120 ? 0.1538 0.7510 0.4176 -0.2134 -0.0278 -0.0339 117 LYS   A O     
828  C  CB    . LYS   A 120 ? 0.1940 0.5283 0.3867 -0.1635 -0.0371 -0.0647 117 LYS   A CB    
829  C  CG    . LYS   A 120 ? 0.1538 0.5156 0.3535 -0.1089 -0.0259 -0.0122 117 LYS   A CG    
830  C  CD    . LYS   A 120 ? 0.1765 0.5305 0.3971 -0.0712 -0.0206 -0.0525 117 LYS   A CD    
831  C  CE    . LYS   A 120 ? 0.0440 0.5467 0.4341 -0.0349 -0.0159 -0.0134 117 LYS   A CE    
832  N  NZ    . LYS   A 120 ? 0.1519 0.5241 0.4722 -0.0129 0.0064  -0.0347 117 LYS   A NZ    
833  N  N     . SER   A 121 ? 0.1802 0.5833 0.4014 -0.1707 0.0046  -0.0284 118 SER   A N     
834  C  CA    . SER   A 121 ? 0.3009 0.5639 0.4248 -0.1812 0.0188  -0.0444 118 SER   A CA    
835  C  C     . SER   A 121 ? 0.2613 0.6593 0.3819 -0.1932 0.0480  -0.0243 118 SER   A C     
836  O  O     . SER   A 121 ? 0.2383 0.7180 0.4593 -0.2223 0.0122  0.0072  118 SER   A O     
837  C  CB    . SER   A 121 ? 0.3250 0.5382 0.4989 -0.1829 0.0766  -0.0608 118 SER   A CB    
838  O  OG    . SER   A 121 ? 0.3512 0.6003 0.4714 -0.1998 0.0319  -0.0745 118 SER   A OG    
839  N  N     . ASP   A 122 ? 0.2058 0.6615 0.4052 -0.2038 -0.0093 -0.0044 119 ASP   A N     
840  C  CA    . ASP   A 122 ? 0.2031 0.6955 0.4480 -0.2002 -0.0239 -0.0251 119 ASP   A CA    
841  C  C     . ASP   A 122 ? 0.2024 0.6673 0.4611 -0.1797 -0.0651 -0.0165 119 ASP   A C     
842  O  O     . ASP   A 122 ? 0.2213 0.7413 0.5667 -0.2655 -0.0419 -0.0270 119 ASP   A O     
843  C  CB    . ASP   A 122 ? 0.2932 0.7147 0.4376 -0.2392 -0.0508 -0.0191 119 ASP   A CB    
844  C  CG    . ASP   A 122 ? 0.3319 0.7222 0.3852 -0.2266 -0.0598 0.0183  119 ASP   A CG    
845  O  OD1   . ASP   A 122 ? 0.1833 0.6827 0.4689 -0.1580 -0.0138 -0.0041 119 ASP   A OD1   
846  O  OD2   . ASP   A 122 ? 0.2382 0.7926 0.4478 -0.2299 -0.0073 0.0499  119 ASP   A OD2   
847  N  N     . LEU   A 123 ? 0.2434 0.6635 0.4889 -0.2107 -0.0615 -0.0265 120 LEU   A N     
848  C  CA    . LEU   A 123 ? 0.2785 0.6946 0.4542 -0.1673 -0.0293 0.0348  120 LEU   A CA    
849  C  C     . LEU   A 123 ? 0.1966 0.7733 0.5900 -0.1866 -0.0387 0.0991  120 LEU   A C     
850  O  O     . LEU   A 123 ? 0.1618 0.7264 0.5444 -0.0915 -0.0478 0.0741  120 LEU   A O     
851  C  CB    . LEU   A 123 ? 0.2478 0.7172 0.5357 -0.1716 -0.0362 0.0103  120 LEU   A CB    
852  C  CG    . LEU   A 123 ? 0.2755 0.7403 0.5557 -0.1626 -0.0190 0.0313  120 LEU   A CG    
853  C  CD1   . LEU   A 123 ? 0.1313 0.7856 0.6051 -0.1884 -0.0357 -0.0042 120 LEU   A CD1   
854  C  CD2   . LEU   A 123 ? 0.2158 0.7487 0.5793 -0.1447 -0.0045 0.0345  120 LEU   A CD2   
855  N  N     . PRO   A 124 ? 0.2117 0.7395 0.5565 -0.1728 -0.0519 0.0342  121 PRO   A N     
856  C  CA    . PRO   A 124 ? 0.2903 0.7687 0.5577 -0.1892 -0.0162 0.0317  121 PRO   A CA    
857  C  C     . PRO   A 124 ? 0.2871 0.8050 0.5325 -0.3261 -0.0058 0.0169  121 PRO   A C     
858  O  O     . PRO   A 124 ? 0.5817 0.7893 0.5646 -0.2788 -0.0270 0.0752  121 PRO   A O     
859  C  CB    . PRO   A 124 ? 0.2231 0.6590 0.6642 -0.2569 -0.0039 -0.0005 121 PRO   A CB    
860  C  CG    . PRO   A 124 ? 0.1873 0.6971 0.5749 -0.1984 -0.0147 -0.0120 121 PRO   A CG    
861  C  CD    . PRO   A 124 ? 0.1784 0.6665 0.5451 -0.1925 -0.0324 0.0202  121 PRO   A CD    
862  N  N     . SER   A 125 ? 0.1978 0.8331 0.4977 -0.2375 -0.0066 -0.0307 122 SER   A N     
863  C  CA    . SER   A 125 ? 0.1345 0.8553 0.5329 -0.2220 0.0250  -0.0400 122 SER   A CA    
864  C  C     . SER   A 125 ? 0.1634 0.8229 0.5133 -0.1720 0.0185  -0.0054 122 SER   A C     
865  O  O     . SER   A 125 ? 0.1601 0.8204 0.5966 -0.1249 -0.0188 -0.0512 122 SER   A O     
866  C  CB    . SER   A 125 ? 0.2692 0.8452 0.6010 -0.2123 0.0380  -0.0524 122 SER   A CB    
867  O  OG    . SER   A 125 ? 0.5199 0.8776 0.5253 -0.2703 0.0394  0.0031  122 SER   A OG    
868  N  N     . ARG   A 126 ? 0.2163 0.7995 0.4896 -0.2149 0.0223  -0.0038 123 ARG   A N     
869  C  CA    . ARG   A 126 ? 0.1235 0.7507 0.5352 -0.1468 0.0374  -0.0306 123 ARG   A CA    
870  C  C     . ARG   A 126 ? 0.1365 0.7322 0.5246 -0.2196 0.0468  -0.0338 123 ARG   A C     
871  O  O     . ARG   A 126 ? 0.1308 0.7721 0.6095 -0.1852 0.0653  0.0520  123 ARG   A O     
872  C  CB    . ARG   A 126 ? 0.1793 0.7326 0.5148 -0.1587 0.0491  -0.0490 123 ARG   A CB    
873  C  CG    . ARG   A 126 ? 0.1706 0.7186 0.5301 -0.1883 0.0053  -0.0834 123 ARG   A CG    
874  C  CD    . ARG   A 126 ? 0.2483 0.7316 0.5221 -0.1821 0.0280  -0.0790 123 ARG   A CD    
875  N  NE    . ARG   A 126 ? 0.2128 0.7595 0.5410 -0.1778 0.0139  -0.1158 123 ARG   A NE    
876  C  CZ    . ARG   A 126 ? 0.2225 0.7736 0.5171 -0.2185 0.0424  -0.1158 123 ARG   A CZ    
877  N  NH1   . ARG   A 126 ? 0.2854 0.7009 0.4822 -0.2599 0.0852  -0.0981 123 ARG   A NH1   
878  N  NH2   . ARG   A 126 ? 0.2528 0.8147 0.5690 -0.1726 0.0204  -0.1784 123 ARG   A NH2   
879  N  N     . THR   A 127 ? 0.1429 0.7719 0.5188 -0.1565 0.0441  -0.1037 124 THR   A N     
880  C  CA    . THR   A 127 ? 0.1689 0.7451 0.4785 -0.1972 0.0611  -0.0531 124 THR   A CA    
881  C  C     . THR   A 127 ? 0.1884 0.7245 0.4933 -0.1469 0.0534  -0.0839 124 THR   A C     
882  O  O     . THR   A 127 ? 0.1786 0.8169 0.4931 -0.1022 0.0519  -0.0632 124 THR   A O     
883  C  CB    . THR   A 127 ? 0.1436 0.7571 0.5416 -0.1662 0.0337  -0.0763 124 THR   A CB    
884  O  OG1   . THR   A 127 ? 0.0998 0.7150 0.5595 -0.1144 0.0454  -0.0382 124 THR   A OG1   
885  C  CG2   . THR   A 127 ? 0.2362 0.7866 0.5221 -0.1374 0.0405  0.0011  124 THR   A CG2   
886  N  N     . VAL   A 128 ? 0.1802 0.6546 0.4519 -0.1822 0.0605  -0.0739 125 VAL   A N     
887  C  CA    . VAL   A 128 ? 0.2173 0.5823 0.4480 -0.1946 0.0666  -0.0321 125 VAL   A CA    
888  C  C     . VAL   A 128 ? 0.1702 0.5688 0.4608 -0.2008 0.0464  -0.0086 125 VAL   A C     
889  O  O     . VAL   A 128 ? 0.2214 0.6139 0.4487 -0.1731 0.0139  -0.0254 125 VAL   A O     
890  C  CB    . VAL   A 128 ? 0.1792 0.5666 0.4376 -0.1731 0.0381  -0.0499 125 VAL   A CB    
891  C  CG1   . VAL   A 128 ? 0.1879 0.5514 0.4335 -0.1468 0.0463  -0.0565 125 VAL   A CG1   
892  C  CG2   . VAL   A 128 ? 0.1537 0.5750 0.5102 -0.1562 0.0012  -0.0428 125 VAL   A CG2   
893  N  N     . ASP   A 129 ? 0.2045 0.5934 0.4831 -0.1836 0.0632  0.0008  126 ASP   A N     
894  C  CA    . ASP   A 129 ? 0.2993 0.5787 0.5796 -0.2546 0.0831  -0.0404 126 ASP   A CA    
895  C  C     . ASP   A 129 ? 0.3303 0.5419 0.5021 -0.2179 0.0781  -0.0693 126 ASP   A C     
896  O  O     . ASP   A 129 ? 0.3084 0.4897 0.5086 -0.2115 0.0838  -0.0655 126 ASP   A O     
897  C  CB    . ASP   A 129 ? 0.3840 0.6614 0.6302 -0.2466 0.0755  0.0285  126 ASP   A CB    
898  C  CG    . ASP   A 129 ? 0.3856 0.7491 0.8033 -0.1855 0.0477  0.0316  126 ASP   A CG    
899  O  OD1   . ASP   A 129 ? 0.5736 0.7691 0.8328 -0.2202 -0.0297 0.0548  126 ASP   A OD1   
900  O  OD2   . ASP   A 129 ? 0.5516 0.7890 0.8337 -0.1400 0.0762  0.0973  126 ASP   A OD2   
901  N  N     . THR   A 130 ? 0.3601 0.5328 0.4668 -0.2313 0.0681  -0.0505 127 THR   A N     
902  C  CA    . THR   A 130 ? 0.3610 0.5590 0.4663 -0.2068 0.0609  -0.0624 127 THR   A CA    
903  C  C     . THR   A 130 ? 0.4326 0.4837 0.4493 -0.2089 0.0854  -0.0356 127 THR   A C     
904  O  O     . THR   A 130 ? 0.4284 0.5046 0.4058 -0.2056 0.0886  -0.0752 127 THR   A O     
905  C  CB    . THR   A 130 ? 0.3705 0.5608 0.5142 -0.2107 0.0400  -0.0815 127 THR   A CB    
906  O  OG1   . THR   A 130 ? 0.4104 0.5969 0.5055 -0.2530 0.0567  -0.0575 127 THR   A OG1   
907  C  CG2   . THR   A 130 ? 0.3949 0.5925 0.5085 -0.1844 0.0396  -0.0858 127 THR   A CG2   
908  N  N     . LYS   A 131 ? 0.4057 0.4512 0.4407 -0.2235 0.0589  -0.0569 128 LYS   A N     
909  C  CA    . LYS   A 131 ? 0.3823 0.4495 0.4421 -0.1544 0.0855  -0.0330 128 LYS   A CA    
910  C  C     . LYS   A 131 ? 0.3284 0.4511 0.4162 -0.1351 0.0866  -0.0271 128 LYS   A C     
911  O  O     . LYS   A 131 ? 0.3398 0.4601 0.4319 -0.1489 0.0724  -0.0593 128 LYS   A O     
912  C  CB    . LYS   A 131 ? 0.4221 0.4085 0.5325 -0.1963 0.0891  -0.0410 128 LYS   A CB    
913  C  CG    . LYS   A 131 ? 0.4382 0.4075 0.4999 -0.1527 0.0845  -0.0436 128 LYS   A CG    
914  C  CD    . LYS   A 131 ? 0.4331 0.3994 0.4855 -0.1397 0.0800  -0.0331 128 LYS   A CD    
915  C  CE    . LYS   A 131 ? 0.4356 0.4017 0.4870 -0.1259 0.0775  -0.0344 128 LYS   A CE    
916  N  NZ    . LYS   A 131 ? 0.4340 0.4005 0.4805 -0.1200 0.0774  -0.0306 128 LYS   A NZ    
917  N  N     . GLN   A 132 ? 0.2700 0.4730 0.4277 -0.1445 0.0816  -0.0196 129 GLN   A N     
918  C  CA    . GLN   A 132 ? 0.2959 0.4433 0.4041 -0.1080 0.0736  -0.0029 129 GLN   A CA    
919  C  C     . GLN   A 132 ? 0.2669 0.4458 0.3324 -0.0997 0.0415  -0.0217 129 GLN   A C     
920  O  O     . GLN   A 132 ? 0.2284 0.4128 0.3519 -0.0891 0.0460  -0.0167 129 GLN   A O     
921  C  CB    . GLN   A 132 ? 0.2421 0.4989 0.4485 -0.1035 0.0420  -0.0153 129 GLN   A CB    
922  C  CG    . GLN   A 132 ? 0.3352 0.4770 0.4699 -0.0523 0.0758  -0.0160 129 GLN   A CG    
923  C  CD    . GLN   A 132 ? 0.2837 0.5650 0.5195 -0.0216 0.1042  -0.0035 129 GLN   A CD    
924  O  OE1   . GLN   A 132 ? 0.3829 0.7422 0.5612 -0.0102 0.0498  0.0615  129 GLN   A OE1   
925  N  NE2   . GLN   A 132 ? 0.4529 0.5868 0.5687 0.0066  0.1066  -0.0314 129 GLN   A NE2   
926  N  N     . ALA   A 133 ? 0.2191 0.4470 0.3395 -0.0967 0.0271  -0.0105 130 ALA   A N     
927  C  CA    . ALA   A 133 ? 0.2601 0.3860 0.3589 -0.1299 0.0452  -0.0159 130 ALA   A CA    
928  C  C     . ALA   A 133 ? 0.3039 0.3582 0.3333 -0.1257 0.0140  -0.0207 130 ALA   A C     
929  O  O     . ALA   A 133 ? 0.2254 0.3877 0.3833 -0.0954 0.0519  -0.0098 130 ALA   A O     
930  C  CB    . ALA   A 133 ? 0.2939 0.4078 0.3750 -0.1203 0.0213  0.0179  130 ALA   A CB    
931  N  N     . GLN   A 134 ? 0.2907 0.3608 0.3616 -0.1232 0.0605  -0.0156 131 GLN   A N     
932  C  CA    . GLN   A 134 ? 0.3789 0.3716 0.3795 -0.0860 0.0597  -0.0051 131 GLN   A CA    
933  C  C     . GLN   A 134 ? 0.3584 0.3847 0.3706 -0.0713 0.0767  -0.0175 131 GLN   A C     
934  O  O     . GLN   A 134 ? 0.3484 0.4004 0.4118 -0.0574 0.0609  -0.0462 131 GLN   A O     
935  C  CB    . GLN   A 134 ? 0.4186 0.3880 0.4667 -0.1059 0.0694  -0.0219 131 GLN   A CB    
936  C  CG    . GLN   A 134 ? 0.5479 0.4512 0.4933 -0.0803 0.0739  -0.0422 131 GLN   A CG    
937  C  CD    . GLN   A 134 ? 0.5805 0.4675 0.5765 -0.1075 0.1014  -0.0555 131 GLN   A CD    
938  O  OE1   . GLN   A 134 ? 0.6456 0.5463 0.7373 -0.1322 0.1741  -0.0447 131 GLN   A OE1   
939  N  NE2   . GLN   A 134 ? 0.6233 0.4759 0.6644 -0.0971 0.1483  -0.0572 131 GLN   A NE2   
940  N  N     . ASP   A 135 ? 0.3504 0.3779 0.3941 -0.0735 0.0780  -0.0200 132 ASP   A N     
941  C  CA    . ASP   A 135 ? 0.3492 0.3389 0.3776 -0.0547 0.0833  0.0281  132 ASP   A CA    
942  C  C     . ASP   A 135 ? 0.3200 0.3353 0.3545 -0.0338 0.0493  0.0239  132 ASP   A C     
943  O  O     . ASP   A 135 ? 0.3051 0.3436 0.3519 -0.0002 0.0652  -0.0135 132 ASP   A O     
944  C  CB    . ASP   A 135 ? 0.3652 0.4144 0.3618 -0.0541 0.0896  0.0103  132 ASP   A CB    
945  C  CG    . ASP   A 135 ? 0.4496 0.4007 0.4266 -0.0497 0.0539  0.0060  132 ASP   A CG    
946  O  OD1   . ASP   A 135 ? 0.5065 0.4341 0.4991 -0.0065 0.0516  0.0292  132 ASP   A OD1   
947  O  OD2   . ASP   A 135 ? 0.4686 0.5108 0.5408 -0.1601 0.0550  -0.0002 132 ASP   A OD2   
948  N  N     . LEU   A 136 ? 0.2583 0.2954 0.3526 -0.0416 0.0521  -0.0101 133 LEU   A N     
949  C  CA    . LEU   A 136 ? 0.2499 0.2680 0.3283 -0.0171 0.0712  0.0070  133 LEU   A CA    
950  C  C     . LEU   A 136 ? 0.2331 0.2920 0.3128 0.0094  0.0315  -0.0176 133 LEU   A C     
951  O  O     . LEU   A 136 ? 0.2210 0.2982 0.3453 -0.0044 0.0283  -0.0067 133 LEU   A O     
952  C  CB    . LEU   A 136 ? 0.2533 0.2732 0.3085 -0.0267 0.0440  -0.0015 133 LEU   A CB    
953  C  CG    . LEU   A 136 ? 0.2245 0.2984 0.3881 -0.0372 0.0139  -0.0012 133 LEU   A CG    
954  C  CD1   . LEU   A 136 ? 0.1895 0.3259 0.4018 -0.0293 -0.0087 -0.0216 133 LEU   A CD1   
955  C  CD2   . LEU   A 136 ? 0.2350 0.3100 0.3984 -0.0510 0.0241  0.0190  133 LEU   A CD2   
956  N  N     . ALA   A 137 ? 0.2152 0.3250 0.3277 0.0216  0.0519  -0.0108 134 ALA   A N     
957  C  CA    . ALA   A 137 ? 0.2380 0.3226 0.3414 0.0094  0.0878  -0.0031 134 ALA   A CA    
958  C  C     . ALA   A 137 ? 0.2860 0.3411 0.3611 0.0174  0.0761  0.0148  134 ALA   A C     
959  O  O     . ALA   A 137 ? 0.2711 0.3848 0.3709 0.0338  0.0619  0.0211  134 ALA   A O     
960  C  CB    . ALA   A 137 ? 0.1626 0.3203 0.3489 -0.0037 0.0703  -0.0033 134 ALA   A CB    
961  N  N     . ARG   A 138 ? 0.2912 0.3001 0.3619 0.0229  0.0549  0.0038  135 ARG   A N     
962  C  CA    . ARG   A 138 ? 0.3240 0.3387 0.3723 0.0527  0.0684  0.0146  135 ARG   A CA    
963  C  C     . ARG   A 138 ? 0.2849 0.3384 0.3859 0.0499  0.0575  0.0052  135 ARG   A C     
964  O  O     . ARG   A 138 ? 0.2838 0.3898 0.3957 0.0795  0.0740  0.0360  135 ARG   A O     
965  C  CB    . ARG   A 138 ? 0.3724 0.3657 0.4041 0.0319  0.0704  0.0384  135 ARG   A CB    
966  C  CG    . ARG   A 138 ? 0.5008 0.4027 0.5155 -0.0159 0.0563  -0.0124 135 ARG   A CG    
967  C  CD    . ARG   A 138 ? 0.6098 0.4171 0.5929 -0.0612 0.0714  -0.0066 135 ARG   A CD    
968  N  NE    . ARG   A 138 ? 0.6221 0.5338 0.6737 -0.0569 0.0587  0.0031  135 ARG   A NE    
969  C  CZ    . ARG   A 138 ? 0.7752 0.5999 0.6799 -0.0278 0.0270  -0.0228 135 ARG   A CZ    
970  N  NH1   . ARG   A 138 ? 0.8405 0.6366 0.7255 0.0557  0.0521  0.0171  135 ARG   A NH1   
971  N  NH2   . ARG   A 138 ? 0.7915 0.6174 0.7331 -0.0307 0.0393  -0.0575 135 ARG   A NH2   
972  N  N     A SER   A 139 ? 0.2349 0.3442 0.3785 0.0554  0.0460  0.0188  136 SER   A N     
973  N  N     B SER   A 139 ? 0.2410 0.3444 0.4018 0.0619  0.0584  0.0290  136 SER   A N     
974  C  CA    A SER   A 139 ? 0.2132 0.3634 0.3468 0.0516  0.0498  0.0273  136 SER   A CA    
975  C  CA    B SER   A 139 ? 0.2275 0.3572 0.3747 0.0561  0.0702  0.0358  136 SER   A CA    
976  C  C     A SER   A 139 ? 0.2085 0.3740 0.3548 0.0578  0.0539  0.0369  136 SER   A C     
977  C  C     B SER   A 139 ? 0.2157 0.3701 0.3642 0.0637  0.0667  0.0473  136 SER   A C     
978  O  O     A SER   A 139 ? 0.2213 0.4595 0.4064 0.0741  0.0218  0.0276  136 SER   A O     
979  O  O     B SER   A 139 ? 0.2290 0.4501 0.4135 0.0722  0.0356  0.0399  136 SER   A O     
980  C  CB    A SER   A 139 ? 0.1934 0.3611 0.3209 0.0450  0.0350  0.0298  136 SER   A CB    
981  C  CB    B SER   A 139 ? 0.2256 0.3521 0.3986 0.0606  0.0676  0.0362  136 SER   A CB    
982  O  OG    A SER   A 139 ? 0.1573 0.3945 0.3286 0.0612  0.0261  0.0074  136 SER   A OG    
983  O  OG    B SER   A 139 ? 0.2474 0.3673 0.3600 0.0639  0.0785  0.0282  136 SER   A OG    
984  N  N     . TYR   A 140 ? 0.2278 0.3466 0.3496 0.0539  0.0480  0.0243  137 TYR   A N     
985  C  CA    . TYR   A 140 ? 0.2303 0.3298 0.3780 0.0437  0.0495  0.0229  137 TYR   A CA    
986  C  C     . TYR   A 140 ? 0.2331 0.3755 0.4066 0.0595  0.0509  0.0153  137 TYR   A C     
987  O  O     . TYR   A 140 ? 0.2083 0.4063 0.4374 0.0497  0.0322  0.0040  137 TYR   A O     
988  C  CB    . TYR   A 140 ? 0.1636 0.3618 0.3938 0.0092  0.0311  0.0308  137 TYR   A CB    
989  C  CG    . TYR   A 140 ? 0.2076 0.3473 0.3825 0.0122  0.0341  0.0157  137 TYR   A CG    
990  C  CD1   . TYR   A 140 ? 0.1579 0.3274 0.3887 0.0065  -0.0011 0.0033  137 TYR   A CD1   
991  C  CD2   . TYR   A 140 ? 0.2225 0.3157 0.3995 -0.0112 0.0172  0.0278  137 TYR   A CD2   
992  C  CE1   . TYR   A 140 ? 0.2260 0.3432 0.4032 0.0276  0.0504  0.0027  137 TYR   A CE1   
993  C  CE2   . TYR   A 140 ? 0.1607 0.3342 0.4427 -0.0308 0.0163  0.0208  137 TYR   A CE2   
994  C  CZ    . TYR   A 140 ? 0.2009 0.3261 0.4539 -0.0116 0.0177  0.0167  137 TYR   A CZ    
995  O  OH    . TYR   A 140 ? 0.1676 0.3455 0.4779 -0.0193 0.0310  0.0343  137 TYR   A OH    
996  N  N     . GLY   A 141 ? 0.2338 0.3757 0.3580 0.0940  0.0399  0.0139  138 GLY   A N     
997  C  CA    . GLY   A 141 ? 0.1891 0.4070 0.3995 0.0902  0.0333  0.0112  138 GLY   A CA    
998  C  C     . GLY   A 141 ? 0.1999 0.4412 0.3867 0.0651  0.0376  0.0139  138 GLY   A C     
999  O  O     . GLY   A 141 ? 0.1701 0.4899 0.4296 0.0891  -0.0065 -0.0061 138 GLY   A O     
1000 N  N     . ILE   A 142 ? 0.2080 0.3641 0.3574 0.0316  0.0407  0.0047  139 ILE   A N     
1001 C  CA    . ILE   A 142 ? 0.1723 0.3283 0.3500 0.0309  0.0163  -0.0136 139 ILE   A CA    
1002 C  C     . ILE   A 142 ? 0.2244 0.3049 0.3266 0.0071  0.0339  -0.0069 139 ILE   A C     
1003 O  O     . ILE   A 142 ? 0.2248 0.3662 0.3757 0.0305  0.0724  0.0102  139 ILE   A O     
1004 C  CB    . ILE   A 142 ? 0.2044 0.3342 0.3721 0.0054  0.0200  -0.0036 139 ILE   A CB    
1005 C  CG1   . ILE   A 142 ? 0.1826 0.3236 0.3388 -0.0333 0.0305  0.0057  139 ILE   A CG1   
1006 C  CG2   . ILE   A 142 ? 0.2094 0.3222 0.3330 0.0123  0.0165  0.0147  139 ILE   A CG2   
1007 C  CD1   . ILE   A 142 ? 0.1633 0.3343 0.3464 -0.0167 0.0276  0.0065  139 ILE   A CD1   
1008 N  N     . PRO   A 143 ? 0.2138 0.3040 0.3260 0.0431  0.0466  0.0003  140 PRO   A N     
1009 C  CA    . PRO   A 143 ? 0.2495 0.3030 0.3351 0.0349  0.0216  0.0081  140 PRO   A CA    
1010 C  C     . PRO   A 143 ? 0.2422 0.2755 0.3326 0.0273  0.0375  -0.0088 140 PRO   A C     
1011 O  O     . PRO   A 143 ? 0.2062 0.2911 0.3709 0.0156  0.0488  0.0095  140 PRO   A O     
1012 C  CB    . PRO   A 143 ? 0.2766 0.3200 0.3455 0.0341  0.0243  -0.0182 140 PRO   A CB    
1013 C  CG    . PRO   A 143 ? 0.2423 0.3219 0.3670 0.0330  0.0554  0.0094  140 PRO   A CG    
1014 C  CD    . PRO   A 143 ? 0.2227 0.3208 0.3466 0.0500  0.0543  0.0187  140 PRO   A CD    
1015 N  N     . PHE   A 144 ? 0.2657 0.3237 0.3609 -0.0275 0.0409  0.0028  141 PHE   A N     
1016 C  CA    . PHE   A 144 ? 0.2711 0.3159 0.3432 -0.0175 0.0326  -0.0080 141 PHE   A CA    
1017 C  C     . PHE   A 144 ? 0.2136 0.3452 0.3415 -0.0377 0.0662  -0.0169 141 PHE   A C     
1018 O  O     . PHE   A 144 ? 0.2835 0.3423 0.3975 -0.0406 0.0183  -0.0161 141 PHE   A O     
1019 C  CB    . PHE   A 144 ? 0.2865 0.3384 0.3283 -0.0420 0.0292  -0.0008 141 PHE   A CB    
1020 C  CG    . PHE   A 144 ? 0.2323 0.3811 0.3758 -0.0606 0.0441  -0.0057 141 PHE   A CG    
1021 C  CD1   . PHE   A 144 ? 0.2072 0.3908 0.3962 -0.0545 0.0343  -0.0104 141 PHE   A CD1   
1022 C  CD2   . PHE   A 144 ? 0.2953 0.3493 0.4375 -0.0757 0.0393  0.0066  141 PHE   A CD2   
1023 C  CE1   . PHE   A 144 ? 0.1893 0.3693 0.3751 -0.0924 0.0342  -0.0088 141 PHE   A CE1   
1024 C  CE2   . PHE   A 144 ? 0.1975 0.3913 0.4815 -0.1283 0.0608  -0.0386 141 PHE   A CE2   
1025 C  CZ    . PHE   A 144 ? 0.2402 0.4090 0.4593 -0.1405 0.0470  -0.0248 141 PHE   A CZ    
1026 N  N     . ILE   A 145 ? 0.2926 0.3203 0.3647 -0.1062 0.0425  -0.0111 142 ILE   A N     
1027 C  CA    . ILE   A 145 ? 0.3065 0.3886 0.3639 -0.0818 0.0261  -0.0292 142 ILE   A CA    
1028 C  C     . ILE   A 145 ? 0.2648 0.3734 0.3343 -0.1060 0.0229  -0.0624 142 ILE   A C     
1029 O  O     . ILE   A 145 ? 0.2240 0.3958 0.4008 -0.1113 0.0038  -0.0601 142 ILE   A O     
1030 C  CB    . ILE   A 145 ? 0.3250 0.4650 0.3845 -0.0818 0.0422  -0.0558 142 ILE   A CB    
1031 C  CG1   . ILE   A 145 ? 0.3675 0.5118 0.4721 -0.0573 0.0229  -0.0598 142 ILE   A CG1   
1032 C  CG2   . ILE   A 145 ? 0.3296 0.4597 0.4136 -0.0984 0.0326  -0.0794 142 ILE   A CG2   
1033 C  CD1   . ILE   A 145 ? 0.3503 0.5579 0.5480 -0.0594 0.0251  -0.0454 142 ILE   A CD1   
1034 N  N     . GLU   A 146 ? 0.3232 0.4073 0.3463 -0.1654 0.0157  -0.0442 143 GLU   A N     
1035 C  CA    . GLU   A 146 ? 0.2541 0.4401 0.4066 -0.1198 0.0549  -0.0673 143 GLU   A CA    
1036 C  C     . GLU   A 146 ? 0.2844 0.4280 0.4124 -0.1002 0.0302  -0.0289 143 GLU   A C     
1037 O  O     . GLU   A 146 ? 0.3336 0.4482 0.4069 -0.1148 0.0137  -0.0603 143 GLU   A O     
1038 C  CB    . GLU   A 146 ? 0.3315 0.4917 0.4317 -0.1945 0.0647  -0.0419 143 GLU   A CB    
1039 C  CG    . GLU   A 146 ? 0.3530 0.5716 0.4498 -0.1463 0.0904  -0.0436 143 GLU   A CG    
1040 C  CD    . GLU   A 146 ? 0.3469 0.6350 0.4530 -0.1763 0.0373  -0.0694 143 GLU   A CD    
1041 O  OE1   . GLU   A 146 ? 0.3279 0.6609 0.4771 -0.2197 0.0634  -0.0860 143 GLU   A OE1   
1042 O  OE2   . GLU   A 146 ? 0.3159 0.7140 0.4593 -0.2187 0.0454  -0.0827 143 GLU   A OE2   
1043 N  N     . THR   A 147 ? 0.1933 0.4331 0.3595 -0.1000 0.0138  -0.0360 144 THR   A N     
1044 C  CA    . THR   A 147 ? 0.2399 0.4513 0.3574 -0.1211 0.0109  -0.0396 144 THR   A CA    
1045 C  C     . THR   A 147 ? 0.2435 0.4675 0.3427 -0.0787 0.0624  -0.0140 144 THR   A C     
1046 O  O     . THR   A 147 ? 0.1440 0.4950 0.3730 -0.1272 0.0059  -0.0629 144 THR   A O     
1047 C  CB    . THR   A 147 ? 0.1833 0.4135 0.3562 -0.0676 0.0259  -0.0349 144 THR   A CB    
1048 O  OG1   . THR   A 147 ? 0.1465 0.4152 0.3956 -0.0857 0.0319  -0.0413 144 THR   A OG1   
1049 C  CG2   . THR   A 147 ? 0.1811 0.4268 0.3771 -0.0466 0.0263  -0.0587 144 THR   A CG2   
1050 N  N     . SER   A 148 ? 0.2510 0.5106 0.3401 -0.0914 0.0418  -0.0360 145 SER   A N     
1051 C  CA    . SER   A 148 ? 0.2612 0.5209 0.3381 -0.1420 0.0085  -0.0271 145 SER   A CA    
1052 C  C     . SER   A 148 ? 0.1530 0.5132 0.3575 -0.1013 0.0051  -0.0262 145 SER   A C     
1053 O  O     . SER   A 148 ? 0.2220 0.4883 0.3674 -0.0988 -0.0081 -0.0341 145 SER   A O     
1054 C  CB    . SER   A 148 ? 0.3081 0.5473 0.3786 -0.1518 -0.0188 -0.0512 145 SER   A CB    
1055 O  OG    . SER   A 148 ? 0.1605 0.6237 0.4232 -0.1538 -0.0147 -0.0516 145 SER   A OG    
1056 N  N     . ALA   A 149 ? 0.2278 0.5030 0.3955 -0.1114 -0.0114 -0.0231 146 ALA   A N     
1057 C  CA    . ALA   A 149 ? 0.1938 0.5108 0.4215 -0.0751 -0.0073 0.0138  146 ALA   A CA    
1058 C  C     . ALA   A 149 ? 0.2175 0.5987 0.4159 -0.1595 0.0088  0.0126  146 ALA   A C     
1059 O  O     . ALA   A 149 ? 0.2705 0.6507 0.4191 -0.0980 0.0268  0.0059  146 ALA   A O     
1060 C  CB    . ALA   A 149 ? 0.1633 0.5166 0.4439 -0.0877 -0.0295 -0.0231 146 ALA   A CB    
1061 N  N     . LYS   A 150 ? 0.2001 0.6369 0.3977 -0.1144 0.0284  -0.0622 147 LYS   A N     
1062 C  CA    . LYS   A 150 ? 0.2141 0.6860 0.3961 -0.1872 0.0355  -0.0075 147 LYS   A CA    
1063 C  C     . LYS   A 150 ? 0.3048 0.7078 0.3613 -0.1181 -0.0256 -0.0225 147 LYS   A C     
1064 O  O     . LYS   A 150 ? 0.3983 0.7757 0.3627 -0.1381 -0.0069 -0.0622 147 LYS   A O     
1065 C  CB    . LYS   A 150 ? 0.1929 0.7295 0.3731 -0.1416 -0.0046 0.0054  147 LYS   A CB    
1066 C  CG    . LYS   A 150 ? 0.2257 0.7440 0.4208 -0.1513 -0.0485 0.0195  147 LYS   A CG    
1067 C  CD    . LYS   A 150 ? 0.2621 0.8037 0.4930 -0.1066 0.0020  0.0579  147 LYS   A CD    
1068 C  CE    . LYS   A 150 ? 0.3548 0.8184 0.5885 -0.0695 -0.0475 0.0550  147 LYS   A CE    
1069 N  NZ    . LYS   A 150 ? 0.3553 0.8493 0.6291 -0.0743 -0.0746 0.0524  147 LYS   A NZ    
1070 N  N     . THR   A 151 ? 0.4141 0.6884 0.4174 -0.0991 -0.0366 -0.0338 148 THR   A N     
1071 C  CA    . THR   A 151 ? 0.3817 0.7040 0.4087 -0.1394 -0.0630 -0.0883 148 THR   A CA    
1072 C  C     . THR   A 151 ? 0.4254 0.6842 0.4836 -0.0857 -0.0243 -0.1007 148 THR   A C     
1073 O  O     . THR   A 151 ? 0.3534 0.7068 0.5455 -0.0189 -0.0424 -0.0982 148 THR   A O     
1074 C  CB    . THR   A 151 ? 0.4830 0.6908 0.4608 -0.1572 -0.0522 -0.0779 148 THR   A CB    
1075 O  OG1   . THR   A 151 ? 0.4773 0.6157 0.4880 -0.1956 -0.0683 -0.0631 148 THR   A OG1   
1076 C  CG2   . THR   A 151 ? 0.4320 0.6466 0.5546 -0.2225 -0.0527 -0.0480 148 THR   A CG2   
1077 N  N     . ARG   A 152 ? 0.3930 0.6562 0.3699 -0.0797 0.0577  -0.1163 149 ARG   A N     
1078 C  CA    . ARG   A 152 ? 0.4039 0.6492 0.4269 -0.0661 0.0293  -0.0723 149 ARG   A CA    
1079 C  C     . ARG   A 152 ? 0.4583 0.6426 0.4968 -0.0874 0.0791  -0.0316 149 ARG   A C     
1080 O  O     . ARG   A 152 ? 0.4762 0.5809 0.5220 -0.0996 0.0165  -0.0571 149 ARG   A O     
1081 C  CB    . ARG   A 152 ? 0.4982 0.6787 0.4344 -0.0710 0.0645  -0.0798 149 ARG   A CB    
1082 C  CG    . ARG   A 152 ? 0.4977 0.7784 0.5293 -0.0428 0.0621  -0.0647 149 ARG   A CG    
1083 C  CD    . ARG   A 152 ? 0.5679 0.8634 0.6058 0.0117  0.1327  -0.0722 149 ARG   A CD    
1084 N  NE    . ARG   A 152 ? 0.5827 0.9181 0.7523 0.0157  0.0689  -0.0753 149 ARG   A NE    
1085 C  CZ    . ARG   A 152 ? 0.6127 0.8992 0.8750 0.0691  0.1278  -0.1159 149 ARG   A CZ    
1086 N  NH1   . ARG   A 152 ? 0.6191 0.8320 0.9054 0.1670  0.1744  -0.2267 149 ARG   A NH1   
1087 N  NH2   . ARG   A 152 ? 0.6135 0.9459 0.8736 0.0612  0.0769  -0.1600 149 ARG   A NH2   
1088 N  N     . GLN   A 153 ? 0.3382 0.5896 0.4544 -0.1270 -0.0437 -0.0726 150 GLN   A N     
1089 C  CA    . GLN   A 153 ? 0.3286 0.5738 0.4503 -0.1612 -0.0286 -0.0831 150 GLN   A CA    
1090 C  C     . GLN   A 153 ? 0.2829 0.5526 0.3717 -0.1363 0.0339  -0.0869 150 GLN   A C     
1091 O  O     . GLN   A 153 ? 0.2945 0.5247 0.3844 -0.1441 0.0255  -0.0500 150 GLN   A O     
1092 C  CB    . GLN   A 153 ? 0.3315 0.6193 0.5154 -0.1463 -0.0215 -0.0730 150 GLN   A CB    
1093 C  CG    . GLN   A 153 ? 0.3557 0.6443 0.6154 -0.1349 -0.0629 -0.0376 150 GLN   A CG    
1094 C  CD    . GLN   A 153 ? 0.5221 0.6792 0.7001 -0.1012 -0.0831 -0.0918 150 GLN   A CD    
1095 O  OE1   . GLN   A 153 ? 0.6095 0.8389 0.7816 -0.0989 -0.1704 -0.0437 150 GLN   A OE1   
1096 N  NE2   . GLN   A 153 ? 0.5464 0.7448 0.8305 -0.0609 -0.0201 -0.0313 150 GLN   A NE2   
1097 N  N     . ARG   A 154 ? 0.3569 0.5108 0.3897 -0.1266 0.0493  -0.0654 151 ARG   A N     
1098 C  CA    . ARG   A 154 ? 0.3610 0.4503 0.3643 -0.0927 0.0675  -0.0411 151 ARG   A CA    
1099 C  C     . ARG   A 154 ? 0.3491 0.4576 0.3246 -0.0981 0.0527  -0.0277 151 ARG   A C     
1100 O  O     . ARG   A 154 ? 0.2925 0.4159 0.3446 -0.0662 0.0375  -0.0125 151 ARG   A O     
1101 C  CB    . ARG   A 154 ? 0.3834 0.4517 0.3863 -0.1566 0.0697  -0.0246 151 ARG   A CB    
1102 C  CG    . ARG   A 154 ? 0.4392 0.4546 0.4557 -0.1766 0.0757  -0.0160 151 ARG   A CG    
1103 C  CD    . ARG   A 154 ? 0.5323 0.5052 0.4932 -0.1508 0.0505  0.0118  151 ARG   A CD    
1104 N  NE    . ARG   A 154 ? 0.5480 0.5369 0.5604 -0.1128 0.0850  0.0691  151 ARG   A NE    
1105 C  CZ    . ARG   A 154 ? 0.6200 0.5411 0.5595 -0.0626 0.0999  0.0689  151 ARG   A CZ    
1106 N  NH1   . ARG   A 154 ? 0.7156 0.5584 0.5828 -0.0896 0.1425  0.0746  151 ARG   A NH1   
1107 N  NH2   . ARG   A 154 ? 0.6369 0.4703 0.6043 -0.0489 0.0700  0.0970  151 ARG   A NH2   
1108 N  N     . VAL   A 155 ? 0.3189 0.3752 0.3622 -0.0711 0.0224  -0.0176 152 VAL   A N     
1109 C  CA    . VAL   A 155 ? 0.2572 0.3847 0.3708 -0.0735 0.0516  -0.0036 152 VAL   A CA    
1110 C  C     . VAL   A 155 ? 0.2765 0.3900 0.3642 -0.0412 0.0089  -0.0341 152 VAL   A C     
1111 O  O     . VAL   A 155 ? 0.2510 0.3730 0.3430 -0.0511 0.0163  -0.0237 152 VAL   A O     
1112 C  CB    . VAL   A 155 ? 0.2256 0.4077 0.3792 -0.0022 0.0287  -0.0250 152 VAL   A CB    
1113 C  CG1   . VAL   A 155 ? 0.2015 0.3993 0.4075 0.0114  0.0439  0.0096  152 VAL   A CG1   
1114 C  CG2   . VAL   A 155 ? 0.2200 0.4279 0.3961 -0.0331 -0.0053 0.0029  152 VAL   A CG2   
1115 N  N     . GLU   A 156 ? 0.3019 0.3803 0.3599 -0.0660 -0.0114 -0.0442 153 GLU   A N     
1116 C  CA    . GLU   A 156 ? 0.3133 0.4170 0.4244 -0.0195 -0.0047 -0.0296 153 GLU   A CA    
1117 C  C     . GLU   A 156 ? 0.3026 0.3818 0.3968 -0.0187 0.0377  -0.0376 153 GLU   A C     
1118 O  O     . GLU   A 156 ? 0.2701 0.3979 0.3945 -0.0063 0.0451  -0.0377 153 GLU   A O     
1119 C  CB    . GLU   A 156 ? 0.3852 0.4469 0.4724 0.0104  -0.0020 -0.0651 153 GLU   A CB    
1120 C  CG    . GLU   A 156 ? 0.4234 0.5624 0.5369 0.0177  0.0353  -0.0705 153 GLU   A CG    
1121 C  CD    . GLU   A 156 ? 0.5909 0.6118 0.5414 0.0538  0.0463  -0.1027 153 GLU   A CD    
1122 O  OE1   . GLU   A 156 ? 0.6850 0.7559 0.5053 -0.0092 0.0739  -0.0880 153 GLU   A OE1   
1123 O  OE2   . GLU   A 156 ? 0.6514 0.6935 0.6570 0.1585  0.0404  -0.0912 153 GLU   A OE2   
1124 N  N     . ASP   A 157 ? 0.2881 0.3665 0.3850 -0.0089 0.0363  -0.0398 154 ASP   A N     
1125 C  CA    . ASP   A 157 ? 0.3447 0.3768 0.4033 0.0104  0.0181  -0.0191 154 ASP   A CA    
1126 C  C     . ASP   A 157 ? 0.3439 0.3492 0.3515 -0.0008 0.0178  0.0175  154 ASP   A C     
1127 O  O     . ASP   A 157 ? 0.2830 0.3762 0.3842 0.0216  0.0279  0.0199  154 ASP   A O     
1128 C  CB    . ASP   A 157 ? 0.4344 0.4298 0.4489 -0.0657 0.0167  -0.0219 154 ASP   A CB    
1129 C  CG    . ASP   A 157 ? 0.5208 0.4429 0.5198 -0.0477 -0.0060 -0.0519 154 ASP   A CG    
1130 O  OD1   . ASP   A 157 ? 0.6154 0.4777 0.5548 -0.0659 0.0701  -0.0340 154 ASP   A OD1   
1131 O  OD2   . ASP   A 157 ? 0.5929 0.5433 0.5785 -0.1484 -0.0245 -0.0366 154 ASP   A OD2   
1132 N  N     . ALA   A 158 ? 0.2168 0.3627 0.3516 -0.0291 0.0172  -0.0113 155 ALA   A N     
1133 C  CA    . ALA   A 158 ? 0.2949 0.3439 0.3490 -0.0027 0.0421  -0.0072 155 ALA   A CA    
1134 C  C     . ALA   A 158 ? 0.2816 0.3379 0.2925 0.0248  0.0242  0.0007  155 ALA   A C     
1135 O  O     . ALA   A 158 ? 0.2273 0.3627 0.3295 0.0306  0.0107  -0.0101 155 ALA   A O     
1136 C  CB    . ALA   A 158 ? 0.2558 0.3875 0.3561 0.0031  0.0594  -0.0148 155 ALA   A CB    
1137 N  N     . PHE   A 159 ? 0.2020 0.3183 0.3099 0.0192  0.0316  0.0064  156 PHE   A N     
1138 C  CA    . PHE   A 159 ? 0.1806 0.3126 0.3332 0.0340  0.0190  0.0293  156 PHE   A CA    
1139 C  C     . PHE   A 159 ? 0.2536 0.3086 0.3017 0.0704  -0.0005 0.0245  156 PHE   A C     
1140 O  O     . PHE   A 159 ? 0.2049 0.3663 0.3542 0.0438  0.0338  0.0000  156 PHE   A O     
1141 C  CB    . PHE   A 159 ? 0.2065 0.2957 0.3290 0.0226  0.0108  0.0138  156 PHE   A CB    
1142 C  CG    . PHE   A 159 ? 0.2055 0.3024 0.3388 0.0280  -0.0025 0.0257  156 PHE   A CG    
1143 C  CD1   . PHE   A 159 ? 0.2197 0.2946 0.3152 0.0302  0.0074  0.0057  156 PHE   A CD1   
1144 C  CD2   . PHE   A 159 ? 0.1904 0.3262 0.3310 -0.0040 0.0197  0.0007  156 PHE   A CD2   
1145 C  CE1   . PHE   A 159 ? 0.2251 0.3170 0.3331 0.0423  -0.0027 0.0139  156 PHE   A CE1   
1146 C  CE2   . PHE   A 159 ? 0.1991 0.3426 0.3369 0.0102  0.0032  0.0235  156 PHE   A CE2   
1147 C  CZ    . PHE   A 159 ? 0.2202 0.3328 0.3312 0.0460  -0.0045 0.0134  156 PHE   A CZ    
1148 N  N     . TYR   A 160 ? 0.2156 0.3238 0.3421 0.0368  0.0161  0.0103  157 TYR   A N     
1149 C  CA    . TYR   A 160 ? 0.2585 0.3175 0.3654 0.0489  0.0308  0.0253  157 TYR   A CA    
1150 C  C     . TYR   A 160 ? 0.2297 0.3612 0.3583 0.0447  0.0144  0.0120  157 TYR   A C     
1151 O  O     . TYR   A 160 ? 0.2052 0.4138 0.3819 0.0559  0.0405  0.0071  157 TYR   A O     
1152 C  CB    . TYR   A 160 ? 0.3804 0.3727 0.3979 0.0735  0.0751  -0.0266 157 TYR   A CB    
1153 C  CG    . TYR   A 160 ? 0.3914 0.4404 0.3961 0.0544  0.0646  -0.0243 157 TYR   A CG    
1154 C  CD1   . TYR   A 160 ? 0.3298 0.4983 0.3978 0.0812  0.1207  0.0239  157 TYR   A CD1   
1155 C  CD2   . TYR   A 160 ? 0.5091 0.5131 0.4156 0.0051  0.1282  -0.0778 157 TYR   A CD2   
1156 C  CE1   . TYR   A 160 ? 0.5611 0.5744 0.3756 0.0450  0.0904  0.0052  157 TYR   A CE1   
1157 C  CE2   . TYR   A 160 ? 0.5820 0.5632 0.4137 0.0027  0.1072  -0.0479 157 TYR   A CE2   
1158 C  CZ    . TYR   A 160 ? 0.6476 0.5746 0.4003 0.0347  0.0664  -0.0189 157 TYR   A CZ    
1159 O  OH    . TYR   A 160 ? 0.7338 0.6735 0.4089 -0.0018 0.1105  -0.0969 157 TYR   A OH    
1160 N  N     . THR   A 161 ? 0.2797 0.3786 0.3544 0.0227  0.0529  -0.0001 158 THR   A N     
1161 C  CA    . THR   A 161 ? 0.2448 0.2967 0.3614 0.0185  0.0379  0.0028  158 THR   A CA    
1162 C  C     . THR   A 161 ? 0.1924 0.2713 0.3405 0.0418  0.0318  0.0161  158 THR   A C     
1163 O  O     . THR   A 161 ? 0.2172 0.3521 0.3603 0.0569  0.0176  0.0190  158 THR   A O     
1164 C  CB    . THR   A 161 ? 0.2446 0.3161 0.3612 -0.0013 0.0419  -0.0060 158 THR   A CB    
1165 O  OG1   . THR   A 161 ? 0.3712 0.3250 0.3950 -0.0070 0.0284  -0.0186 158 THR   A OG1   
1166 C  CG2   . THR   A 161 ? 0.2927 0.3691 0.3717 -0.0356 -0.0120 0.0179  158 THR   A CG2   
1167 N  N     . LEU   A 162 ? 0.2203 0.2823 0.3147 0.0543  0.0143  0.0079  159 LEU   A N     
1168 C  CA    . LEU   A 162 ? 0.1682 0.2626 0.3320 0.0841  0.0284  -0.0049 159 LEU   A CA    
1169 C  C     . LEU   A 162 ? 0.1778 0.2946 0.3305 0.0922  0.0279  -0.0058 159 LEU   A C     
1170 O  O     . LEU   A 162 ? 0.1150 0.3586 0.3510 0.0717  0.0314  0.0214  159 LEU   A O     
1171 C  CB    . LEU   A 162 ? 0.1595 0.2621 0.3361 0.0721  -0.0084 -0.0122 159 LEU   A CB    
1172 C  CG    . LEU   A 162 ? 0.1170 0.2739 0.3491 0.0547  0.0204  -0.0181 159 LEU   A CG    
1173 C  CD1   . LEU   A 162 ? 0.1791 0.2898 0.3595 0.0472  0.0043  0.0057  159 LEU   A CD1   
1174 C  CD2   . LEU   A 162 ? 0.1600 0.2858 0.3432 0.0536  -0.0150 -0.0089 159 LEU   A CD2   
1175 N  N     . VAL   A 163 ? 0.1484 0.3458 0.3393 0.0785  0.0323  -0.0028 160 VAL   A N     
1176 C  CA    . VAL   A 163 ? 0.1518 0.3537 0.3718 0.0975  0.0348  0.0137  160 VAL   A CA    
1177 C  C     . VAL   A 163 ? 0.1484 0.3404 0.3857 0.0866  0.0281  0.0189  160 VAL   A C     
1178 O  O     . VAL   A 163 ? 0.1595 0.4129 0.3992 0.0915  0.0083  0.0169  160 VAL   A O     
1179 C  CB    . VAL   A 163 ? 0.1622 0.3702 0.3774 0.0712  0.0658  -0.0013 160 VAL   A CB    
1180 C  CG1   . VAL   A 163 ? 0.1767 0.4233 0.4068 0.0955  0.0737  -0.0115 160 VAL   A CG1   
1181 C  CG2   . VAL   A 163 ? 0.2529 0.3923 0.3766 0.1034  0.0714  0.0111  160 VAL   A CG2   
1182 N  N     . ARG   A 164 ? 0.1719 0.3236 0.3882 0.0956  0.0201  0.0157  161 ARG   A N     
1183 C  CA    . ARG   A 164 ? 0.1571 0.3277 0.4035 0.0897  0.0485  0.0333  161 ARG   A CA    
1184 C  C     . ARG   A 164 ? 0.2542 0.2902 0.4197 0.1178  0.0214  0.0282  161 ARG   A C     
1185 O  O     . ARG   A 164 ? 0.2772 0.3791 0.4394 0.1102  0.0009  0.0708  161 ARG   A O     
1186 C  CB    . ARG   A 164 ? 0.2922 0.3432 0.4420 0.0367  0.0450  0.0400  161 ARG   A CB    
1187 C  CG    . ARG   A 164 ? 0.3515 0.3803 0.4414 0.0555  0.0636  0.0349  161 ARG   A CG    
1188 C  CD    . ARG   A 164 ? 0.4409 0.3713 0.5481 0.0481  0.0387  -0.0184 161 ARG   A CD    
1189 N  NE    . ARG   A 164 ? 0.5145 0.5055 0.5007 0.0459  0.0403  -0.0197 161 ARG   A NE    
1190 C  CZ    . ARG   A 164 ? 0.5750 0.6125 0.5444 0.0193  -0.0112 -0.0430 161 ARG   A CZ    
1191 N  NH1   . ARG   A 164 ? 0.5442 0.6061 0.6393 -0.0056 -0.0048 -0.0070 161 ARG   A NH1   
1192 N  NH2   . ARG   A 164 ? 0.6773 0.6879 0.6050 -0.0151 0.0004  -0.1193 161 ARG   A NH2   
1193 N  N     . GLU   A 165 ? 0.2101 0.2947 0.4004 0.1040  0.0140  0.0233  162 GLU   A N     
1194 C  CA    . GLU   A 165 ? 0.2282 0.3177 0.4151 0.0926  0.0153  0.0065  162 GLU   A CA    
1195 C  C     . GLU   A 165 ? 0.2315 0.3621 0.3788 0.0697  0.0178  0.0229  162 GLU   A C     
1196 O  O     . GLU   A 165 ? 0.1443 0.4036 0.4063 0.0739  0.0183  0.0465  162 GLU   A O     
1197 C  CB    . GLU   A 165 ? 0.1693 0.3093 0.3881 0.0507  0.0171  0.0341  162 GLU   A CB    
1198 C  CG    . GLU   A 165 ? 0.2038 0.3594 0.3928 0.0181  0.0695  0.0274  162 GLU   A CG    
1199 C  CD    . GLU   A 165 ? 0.2633 0.3899 0.4355 0.0443  0.0505  0.0582  162 GLU   A CD    
1200 O  OE1   . GLU   A 165 ? 0.3970 0.4080 0.4526 0.0620  -0.0007 0.0258  162 GLU   A OE1   
1201 O  OE2   . GLU   A 165 ? 0.3864 0.4180 0.5127 0.0737  0.0986  0.0270  162 GLU   A OE2   
1202 N  N     . ILE   A 166 ? 0.0942 0.3787 0.4023 0.0902  0.0145  0.0317  163 ILE   A N     
1203 C  CA    . ILE   A 166 ? 0.1093 0.3725 0.3893 0.0750  0.0167  0.0007  163 ILE   A CA    
1204 C  C     . ILE   A 166 ? 0.1980 0.3849 0.4713 0.1335  -0.0280 0.0134  163 ILE   A C     
1205 O  O     . ILE   A 166 ? 0.1309 0.4607 0.4936 0.1178  -0.0028 -0.0257 163 ILE   A O     
1206 C  CB    . ILE   A 166 ? 0.0886 0.4104 0.4132 0.0710  0.0034  0.0325  163 ILE   A CB    
1207 C  CG1   . ILE   A 166 ? 0.0863 0.3492 0.4014 0.0450  0.0121  0.0156  163 ILE   A CG1   
1208 C  CG2   . ILE   A 166 ? 0.1854 0.4123 0.4343 0.0091  0.0130  0.0424  163 ILE   A CG2   
1209 C  CD1   . ILE   A 166 ? 0.1906 0.3374 0.4001 0.0347  0.0074  0.0061  163 ILE   A CD1   
1210 N  N     . ARG   A 167 ? 0.0679 0.4080 0.5078 0.1084  0.0229  0.0054  164 ARG   A N     
1211 C  CA    . ARG   A 167 ? 0.1125 0.4551 0.5393 0.1579  -0.0067 -0.0174 164 ARG   A CA    
1212 C  C     . ARG   A 167 ? 0.1781 0.4759 0.5728 0.1631  -0.0518 0.0179  164 ARG   A C     
1213 O  O     . ARG   A 167 ? 0.1843 0.5906 0.6133 0.2109  -0.0567 -0.0032 164 ARG   A O     
1214 C  CB    . ARG   A 167 ? 0.2268 0.4797 0.5388 0.1429  -0.0019 -0.0310 164 ARG   A CB    
1215 C  CG    . ARG   A 167 ? 0.2116 0.5044 0.5582 0.2098  -0.0624 -0.0009 164 ARG   A CG    
1216 C  CD    . ARG   A 167 ? 0.3857 0.5862 0.5547 0.1147  -0.0233 -0.0228 164 ARG   A CD    
1217 N  NE    . ARG   A 167 ? 0.1986 0.6323 0.5585 0.1416  0.0034  -0.0388 164 ARG   A NE    
1218 C  CZ    . ARG   A 167 ? 0.2781 0.6577 0.5590 0.1567  0.0302  -0.0528 164 ARG   A CZ    
1219 N  NH1   . ARG   A 167 ? 0.3108 0.6811 0.5911 0.1367  0.0689  -0.0398 164 ARG   A NH1   
1220 N  NH2   . ARG   A 167 ? 0.4571 0.6833 0.5863 0.0806  0.0085  -0.0228 164 ARG   A NH2   
1221 N  N     . GLN   A 168 ? 0.2539 0.4534 0.5382 0.1537  -0.0463 0.0564  165 GLN   A N     
1222 C  CA    . GLN   A 168 ? 0.2794 0.4816 0.5030 0.1456  -0.0987 0.0326  165 GLN   A CA    
1223 C  C     . GLN   A 168 ? 0.2253 0.4889 0.5408 0.1472  -0.1160 0.0177  165 GLN   A C     
1224 O  O     . GLN   A 168 ? 0.2506 0.5599 0.5547 0.2220  -0.1146 0.0218  165 GLN   A O     
1225 C  CB    . GLN   A 168 ? 0.3269 0.4807 0.5515 0.0902  -0.0778 0.0210  165 GLN   A CB    
1226 C  CG    . GLN   A 168 ? 0.3550 0.4603 0.5133 0.0930  -0.0901 0.0258  165 GLN   A CG    
1227 C  CD    . GLN   A 168 ? 0.3569 0.4561 0.5056 0.0946  -0.0898 0.0290  165 GLN   A CD    
1228 O  OE1   . GLN   A 168 ? 0.3565 0.4545 0.5039 0.0945  -0.0890 0.0281  165 GLN   A OE1   
1229 N  NE2   . GLN   A 168 ? 0.3558 0.4574 0.5054 0.0939  -0.0897 0.0293  165 GLN   A NE2   
1230 N  N     . TYR   A 169 ? 0.2491 0.4963 0.5058 0.1611  -0.0446 -0.0063 166 TYR   A N     
1231 C  CA    . TYR   A 169 ? 0.1178 0.5597 0.5150 0.1604  -0.0778 -0.0301 166 TYR   A CA    
1232 C  C     . TYR   A 169 ? 0.1587 0.6879 0.5468 0.0623  -0.0614 -0.0202 166 TYR   A C     
1233 O  O     . TYR   A 169 ? 0.1974 0.7625 0.5527 0.1599  -0.0623 -0.1096 166 TYR   A O     
1234 C  CB    . TYR   A 169 ? 0.1326 0.5796 0.5229 0.1723  -0.1116 -0.0174 166 TYR   A CB    
1235 C  CG    . TYR   A 169 ? 0.2082 0.6214 0.5743 0.1251  -0.1113 -0.0417 166 TYR   A CG    
1236 C  CD1   . TYR   A 169 ? 0.3205 0.6688 0.5792 0.0592  -0.0902 -0.0527 166 TYR   A CD1   
1237 C  CD2   . TYR   A 169 ? 0.3487 0.6487 0.6049 0.0687  -0.0661 -0.0510 166 TYR   A CD2   
1238 C  CE1   . TYR   A 169 ? 0.4575 0.6830 0.6340 0.0223  -0.0996 -0.0756 166 TYR   A CE1   
1239 C  CE2   . TYR   A 169 ? 0.5063 0.6329 0.6574 0.0316  -0.0609 -0.0538 166 TYR   A CE2   
1240 C  CZ    . TYR   A 169 ? 0.5502 0.6341 0.6327 -0.0025 -0.1060 -0.0917 166 TYR   A CZ    
1241 O  OH    . TYR   A 169 ? 0.5832 0.6868 0.6496 -0.0331 -0.2031 -0.0999 166 TYR   A OH    
1242 N  N     . ARG   A 170 ? 0.1421 0.7181 0.5856 0.1858  -0.0187 -0.0514 167 ARG   A N     
1243 C  CA    . ARG   A 170 ? 0.1783 0.6760 0.6316 0.0885  -0.0588 -0.0419 167 ARG   A CA    
1244 C  C     . ARG   A 170 ? 0.1302 0.8362 0.7368 0.1568  -0.1020 -0.0139 167 ARG   A C     
1245 O  O     . ARG   A 170 ? 0.1678 0.7497 0.7104 0.0833  -0.0903 -0.1787 167 ARG   A O     
1246 C  CB    . ARG   A 170 ? 0.1817 0.6451 0.6309 0.1204  -0.1012 0.0031  167 ARG   A CB    
1247 C  CG    . ARG   A 170 ? 0.2815 0.6141 0.6538 0.1233  -0.0418 -0.0218 167 ARG   A CG    
1248 C  CD    . ARG   A 170 ? 0.2523 0.5999 0.6587 0.1426  -0.0939 0.0401  167 ARG   A CD    
1249 N  NE    . ARG   A 170 ? 0.2607 0.5899 0.7289 0.1511  -0.0285 0.0485  167 ARG   A NE    
1250 C  CZ    . ARG   A 170 ? 0.3824 0.6073 0.7426 0.2016  -0.0173 0.0665  167 ARG   A CZ    
1251 N  NH1   . ARG   A 170 ? 0.5351 0.6271 0.7134 0.1344  -0.0176 0.0376  167 ARG   A NH1   
1252 N  NH2   . ARG   A 170 ? 0.5087 0.6069 0.7969 0.2129  -0.0344 0.0691  167 ARG   A NH2   
1253 N  N     . LEU   A 171 ? 0.2536 0.7227 0.7723 0.2130  -0.1096 -0.0796 168 LEU   A N     
1254 C  CA    . LEU   A 171 ? 0.3279 0.8445 0.7850 0.3257  -0.1697 -0.0974 168 LEU   A CA    
1255 C  C     . LEU   A 171 ? 0.3711 0.9173 0.7803 0.3151  -0.0788 -0.0831 168 LEU   A C     
1256 O  O     . LEU   A 171 ? 0.5253 0.9761 0.6614 0.3543  -0.0744 -0.0634 168 LEU   A O     
1257 C  CB    . LEU   A 171 ? 0.5024 0.7324 0.8544 0.3956  -0.1338 -0.0918 168 LEU   A CB    
1258 C  CG    . LEU   A 171 ? 0.5755 0.7613 0.8442 0.3379  -0.1800 -0.0337 168 LEU   A CG    
1259 C  CD1   . LEU   A 171 ? 0.7999 0.7625 0.8813 0.2207  -0.1677 -0.0158 168 LEU   A CD1   
1260 C  CD2   . LEU   A 171 ? 0.5109 0.7794 0.8597 0.3693  -0.1284 -0.0962 168 LEU   A CD2   
1261 N  N     . LYS   A 172 ? 0.3711 0.9267 0.7372 0.3355  -0.1303 -0.0753 169 LYS   A N     
1262 C  CA    . LYS   A 172 ? 0.4714 1.0228 0.7404 0.2687  -0.0835 -0.0337 169 LYS   A CA    
1263 C  C     . LYS   A 172 ? 0.7074 1.1138 0.7426 0.1563  -0.1704 -0.0546 169 LYS   A C     
1264 O  O     . LYS   A 172 ? 0.8930 1.1487 0.6977 0.0967  -0.0756 0.0042  169 LYS   A O     
1265 C  CB    . LYS   A 172 ? 0.4440 1.0172 0.7430 0.2617  -0.0944 0.0087  169 LYS   A CB    
1266 C  CG    . LYS   A 172 ? 0.5286 0.9826 0.7503 0.2427  -0.0376 -0.0022 169 LYS   A CG    
1267 C  CD    . LYS   A 172 ? 0.4553 1.1138 0.7426 0.1775  -0.0593 0.0296  169 LYS   A CD    
1268 C  CE    . LYS   A 172 ? 0.5737 1.1113 0.7234 0.1094  -0.0113 0.0353  169 LYS   A CE    
1269 N  NZ    . LYS   A 172 ? 0.3709 1.1621 0.7608 0.1453  0.0380  -0.0026 169 LYS   A NZ    
1270 O  OXT   . LYS   A 172 ? 0.7250 1.2363 0.9102 0.0378  -0.1726 0.0028  169 LYS   A OXT   
1271 P  PG    . GNP   B .   ? 0.1971 0.3830 0.4905 0.0802  -0.0082 0.0481  201 GNP   A PG    
1272 O  O1G   . GNP   B .   ? 0.2609 0.4230 0.4367 0.0042  0.0039  0.0376  201 GNP   A O1G   
1273 O  O2G   . GNP   B .   ? 0.2619 0.3409 0.5646 0.0945  -0.0390 0.0384  201 GNP   A O2G   
1274 O  O3G   . GNP   B .   ? 0.2510 0.3534 0.4755 0.0629  0.0271  -0.0006 201 GNP   A O3G   
1275 N  N3B   . GNP   B .   ? 0.1556 0.3789 0.5070 0.0340  -0.0228 0.0657  201 GNP   A N3B   
1276 P  PB    . GNP   B .   ? 0.1100 0.3910 0.4342 0.0121  -0.0220 0.0220  201 GNP   A PB    
1277 O  O1B   . GNP   B .   ? 0.0216 0.4087 0.4347 0.0276  -0.0248 0.0160  201 GNP   A O1B   
1278 O  O2B   . GNP   B .   ? 0.1120 0.3786 0.4541 0.0081  -0.0018 0.0468  201 GNP   A O2B   
1279 O  O3A   . GNP   B .   ? 0.1097 0.4122 0.4144 0.0213  -0.0032 -0.0044 201 GNP   A O3A   
1280 P  PA    . GNP   B .   ? 0.0957 0.4599 0.4410 -0.0060 -0.0279 0.0024  201 GNP   A PA    
1281 O  O1A   . GNP   B .   ? 0.1057 0.4716 0.5383 0.0220  -0.0382 0.0396  201 GNP   A O1A   
1282 O  O2A   . GNP   B .   ? 0.1261 0.4678 0.4081 0.0031  0.0074  -0.0069 201 GNP   A O2A   
1283 O  "O5'" . GNP   B .   ? 0.1042 0.5032 0.4288 -0.0322 -0.0499 0.0023  201 GNP   A "O5'" 
1284 C  "C5'" . GNP   B .   ? 0.1474 0.5517 0.4673 -0.0057 -0.0127 -0.0430 201 GNP   A "C5'" 
1285 C  "C4'" . GNP   B .   ? 0.0824 0.5831 0.4967 0.0320  -0.0209 -0.0379 201 GNP   A "C4'" 
1286 O  "O4'" . GNP   B .   ? 0.0174 0.5995 0.4863 -0.0216 -0.0377 -0.0202 201 GNP   A "O4'" 
1287 C  "C3'" . GNP   B .   ? 0.0504 0.6603 0.4961 0.0031  -0.0631 -0.0030 201 GNP   A "C3'" 
1288 O  "O3'" . GNP   B .   ? 0.0956 0.7800 0.5294 0.0372  -0.1263 -0.0113 201 GNP   A "O3'" 
1289 C  "C2'" . GNP   B .   ? 0.1835 0.6529 0.4519 0.0039  -0.0181 -0.0141 201 GNP   A "C2'" 
1290 O  "O2'" . GNP   B .   ? 0.1972 0.7419 0.4467 -0.0197 -0.0189 -0.0045 201 GNP   A "O2'" 
1291 C  "C1'" . GNP   B .   ? 0.0996 0.6120 0.4433 -0.0306 -0.1081 -0.0144 201 GNP   A "C1'" 
1292 N  N9    . GNP   B .   ? 0.0666 0.5910 0.4170 -0.0470 -0.0459 -0.0151 201 GNP   A N9    
1293 C  C8    . GNP   B .   ? 0.0426 0.5108 0.4358 -0.0526 -0.0030 -0.0165 201 GNP   A C8    
1294 N  N7    . GNP   B .   ? 0.0869 0.4962 0.4156 -0.0618 -0.0119 -0.0097 201 GNP   A N7    
1295 C  C5    . GNP   B .   ? 0.0961 0.5579 0.3885 -0.0872 -0.0111 -0.0144 201 GNP   A C5    
1296 C  C6    . GNP   B .   ? 0.0978 0.5532 0.4103 -0.0654 0.0429  -0.0086 201 GNP   A C6    
1297 O  O6    . GNP   B .   ? 0.1330 0.5370 0.4346 -0.1126 -0.0086 0.0143  201 GNP   A O6    
1298 N  N1    . GNP   B .   ? 0.1425 0.6329 0.4301 -0.0971 -0.0415 0.0038  201 GNP   A N1    
1299 C  C2    . GNP   B .   ? 0.0324 0.6939 0.4920 -0.1069 0.0231  0.0483  201 GNP   A C2    
1300 N  N2    . GNP   B .   ? 0.0760 0.7147 0.5808 -0.1879 -0.0365 0.0057  201 GNP   A N2    
1301 N  N3    . GNP   B .   ? 0.1446 0.6694 0.4389 -0.1170 -0.0075 0.0204  201 GNP   A N3    
1302 C  C4    . GNP   B .   ? 0.1070 0.5913 0.3879 -0.0452 0.0145  -0.0074 201 GNP   A C4    
1303 MG MG    . MG    C .   ? 0.0754 0.3613 0.4379 0.0253  -0.0209 0.0507  202 MG    A MG    
1304 CO CO    . CO    D .   ? 0.6437 1.2013 0.8880 -0.1938 -0.3300 0.3476  203 CO    A CO    
1305 CO CO    . CO    E .   ? 0.1614 0.4089 0.4551 -0.0473 0.0387  -0.0272 204 CO    A CO    
1306 C  CBK   . A1ILF F .   ? 0.4929 0.6750 0.5776 -0.0652 -0.0767 0.1581  205 A1ILF A CBK   
1307 C  CBL   . A1ILF F .   ? 0.4700 0.7207 0.5802 -0.0670 -0.0837 0.1626  205 A1ILF A CBL   
1308 C  CBM   . A1ILF F .   ? 0.4863 0.6881 0.5990 -0.0638 -0.1491 0.1643  205 A1ILF A CBM   
1309 N  NBV   . A1ILF F .   ? 0.3983 0.7821 0.6670 -0.0471 -0.1564 0.1447  205 A1ILF A NBV   
1310 C  CBN   . A1ILF F .   ? 0.4178 0.6977 0.6019 -0.0324 -0.1561 0.1674  205 A1ILF A CBN   
1311 C  CBO   . A1ILF F .   ? 0.4117 0.6879 0.6153 -0.0699 -0.1105 0.1781  205 A1ILF A CBO   
1312 C  CBJ   . A1ILF F .   ? 0.3994 0.6332 0.5708 -0.0893 -0.1348 0.1438  205 A1ILF A CBJ   
1313 N  NAQ   . A1ILF F .   ? 0.2761 0.5643 0.5422 -0.1565 -0.1018 0.1164  205 A1ILF A NAQ   
1314 C  CAB   . A1ILF F .   ? 0.3250 0.4807 0.5475 -0.2137 -0.0556 0.1187  205 A1ILF A CAB   
1315 O  OAA   . A1ILF F .   ? 0.4040 0.4547 0.6486 -0.1891 -0.0869 0.1163  205 A1ILF A OAA   
1316 C  CAR   . A1ILF F .   ? 0.2580 0.5199 0.5164 -0.0763 -0.1257 0.0768  205 A1ILF A CAR   
1317 C  CAS   . A1ILF F .   ? 0.2100 0.5719 0.5268 -0.1357 -0.0562 0.0419  205 A1ILF A CAS   
1318 C  CAT   . A1ILF F .   ? 0.2071 0.4907 0.4766 -0.1635 -0.0567 0.0309  205 A1ILF A CAT   
1319 C  CAU   . A1ILF F .   ? 0.1894 0.5316 0.4688 -0.1345 -0.0228 0.0371  205 A1ILF A CAU   
1320 C  CAV   . A1ILF F .   ? 0.1907 0.5540 0.4797 -0.1268 -0.0327 0.0302  205 A1ILF A CAV   
1321 N  NAW   . A1ILF F .   ? 0.1266 0.5095 0.4879 -0.1095 -0.0240 0.0738  205 A1ILF A NAW   
1322 C  CAX   . A1ILF F .   ? 0.1263 0.4740 0.5398 -0.0476 -0.0600 0.0727  205 A1ILF A CAX   
1323 C  CAY   . A1ILF F .   ? 0.1495 0.5216 0.5154 -0.0364 -0.0482 0.0655  205 A1ILF A CAY   
1324 O  OBD   . A1ILF F .   ? 0.1231 0.6228 0.5321 -0.0579 -0.0428 0.0674  205 A1ILF A OBD   
1325 C  CAZ   . A1ILF F .   ? 0.0978 0.4844 0.5406 0.0186  -0.0592 0.0549  205 A1ILF A CAZ   
1326 C  CBA   . A1ILF F .   ? 0.0411 0.4944 0.5475 -0.0160 -0.0274 0.0721  205 A1ILF A CBA   
1327 C  CBB   . A1ILF F .   ? 0.1044 0.5055 0.5177 -0.0323 -0.0748 0.0543  205 A1ILF A CBB   
1328 CL CLBC  . A1ILF F .   ? 0.1462 0.4703 0.5379 -0.0451 -0.0232 0.0606  205 A1ILF A CLBC  
1329 C  CBI   . A1ILF F .   ? 0.1640 0.4880 0.5273 -0.0358 -0.0815 0.0632  205 A1ILF A CBI   
1330 S  SBH   . A1ILF F .   ? 0.1334 0.4958 0.5175 -0.0820 -0.0037 0.0653  205 A1ILF A SBH   
1331 C  CBG   . A1ILF F .   ? 0.2323 0.4914 0.5304 -0.1097 -0.0696 0.0722  205 A1ILF A CBG   
1332 N  NBF   . A1ILF F .   ? 0.1323 0.5059 0.5636 -0.0839 -0.0045 0.0778  205 A1ILF A NBF   
1333 S  SAH   . A1ILF F .   ? 0.2422 0.5256 0.5739 -0.1411 -0.0599 0.0529  205 A1ILF A SAH   
1334 O  OAI   . A1ILF F .   ? 0.2021 0.5874 0.5770 -0.0926 -0.0963 0.0102  205 A1ILF A OAI   
1335 O  OBE   . A1ILF F .   ? 0.3164 0.5296 0.5981 -0.1685 -0.1144 0.0415  205 A1ILF A OBE   
1336 C  CAG   . A1ILF F .   ? 0.1841 0.5445 0.5111 -0.2044 -0.0901 0.0532  205 A1ILF A CAG   
1337 C  CAF   . A1ILF F .   ? 0.2372 0.5108 0.4843 -0.0980 -0.0508 0.1244  205 A1ILF A CAF   
1338 N  NAE   . A1ILF F .   ? 0.2376 0.5307 0.5226 -0.1329 -0.1114 0.0985  205 A1ILF A NAE   
1339 C  CAJ   . A1ILF F .   ? 0.2773 0.5234 0.5366 -0.1800 -0.0446 0.1017  205 A1ILF A CAJ   
1340 C  CAC   . A1ILF F .   ? 0.2893 0.5362 0.5294 -0.1874 -0.1011 0.1106  205 A1ILF A CAC   
1341 C  CAD   . A1ILF F .   ? 0.2842 0.5114 0.4963 -0.1751 -0.1050 0.0986  205 A1ILF A CAD   
1342 N  NAK   . A1ILF F .   ? 0.2975 0.4676 0.5453 -0.1203 -0.1037 0.1016  205 A1ILF A NAK   
1343 C  CAP   . A1ILF F .   ? 0.3141 0.4490 0.5666 -0.1207 -0.1281 0.0880  205 A1ILF A CAP   
1344 C  CAO   . A1ILF F .   ? 0.2665 0.4265 0.5812 -0.0916 -0.1074 0.1024  205 A1ILF A CAO   
1345 C  CAL   . A1ILF F .   ? 0.3270 0.4392 0.5418 -0.1045 -0.0711 0.0936  205 A1ILF A CAL   
1346 C  CAM   . A1ILF F .   ? 0.3040 0.4299 0.5567 -0.0823 -0.0785 0.1029  205 A1ILF A CAM   
1347 C  CAN   . A1ILF F .   ? 0.3389 0.4320 0.5679 -0.0700 -0.0550 0.1058  205 A1ILF A CAN   
1348 N  NBP   . A1ILF F .   ? 0.2544 0.4316 0.6455 -0.0403 -0.0546 0.1052  205 A1ILF A NBP   
1349 C  CBQ   . A1ILF F .   ? 0.2885 0.4345 0.5745 -0.0393 -0.0743 0.1148  205 A1ILF A CBQ   
1350 C  CBR   . A1ILF F .   ? 0.2411 0.4593 0.5937 -0.0305 -0.0501 0.0975  205 A1ILF A CBR   
1351 C  CBS   . A1ILF F .   ? 0.1793 0.4839 0.5827 -0.0524 -0.0786 0.0728  205 A1ILF A CBS   
1352 N  NBW   . A1ILF F .   ? 0.2340 0.5849 0.5746 -0.0630 -0.0983 0.0446  205 A1ILF A NBW   
1353 C  CBT   . A1ILF F .   ? 0.2755 0.4755 0.6119 -0.0459 -0.0887 0.0761  205 A1ILF A CBT   
1354 C  CBU   . A1ILF F .   ? 0.2496 0.4714 0.5912 -0.0480 -0.0796 0.1157  205 A1ILF A CBU   
1355 O  O     . HOH   G .   ? 0.5020 0.5369 0.8608 -0.0669 0.0958  -0.2002 301 HOH   A O     
1356 O  O     . HOH   G .   ? 0.2112 0.8573 0.8520 0.0014  -0.1042 0.1888  302 HOH   A O     
1357 O  O     . HOH   G .   ? 0.0866 0.4780 0.5710 -0.0140 -0.0081 0.0108  303 HOH   A O     
1358 O  O     . HOH   G .   ? 0.6569 0.5146 0.6202 -0.0275 0.0869  0.0345  304 HOH   A O     
1359 O  O     . HOH   G .   ? 0.3589 0.5559 0.4747 -0.0916 0.0699  -0.0870 305 HOH   A O     
1360 O  O     . HOH   G .   ? 0.2008 0.3426 0.4057 0.0574  0.0228  0.0270  306 HOH   A O     
1361 O  O     . HOH   G .   ? 0.5476 0.3493 0.6465 0.0512  0.2034  0.0134  307 HOH   A O     
1362 O  O     . HOH   G .   ? 0.1860 0.6043 0.4796 0.0910  0.0089  0.0370  308 HOH   A O     
1363 O  O     . HOH   G .   ? 0.1045 0.4864 0.4647 -0.0129 -0.0310 0.0245  309 HOH   A O     
1364 O  O     . HOH   G .   ? 0.2678 0.7659 0.7026 -0.0058 -0.2273 0.2242  310 HOH   A O     
1365 O  O     . HOH   G .   ? 0.2495 0.4819 0.5930 0.0158  -0.0758 0.0302  311 HOH   A O     
1366 O  O     . HOH   G .   ? 0.3658 0.5505 0.4698 -0.1682 0.1140  -0.0282 312 HOH   A O     
1367 O  O     . HOH   G .   ? 0.8777 0.6004 0.5511 0.2873  -0.0516 0.0794  313 HOH   A O     
1368 O  O     . HOH   G .   ? 0.3124 0.5090 0.6473 0.1153  -0.0996 -0.0099 314 HOH   A O     
1369 O  O     . HOH   G .   ? 0.3322 0.9086 0.5945 0.1219  -0.1249 0.1690  315 HOH   A O     
1370 O  O     . HOH   G .   ? 0.6940 0.5010 0.4162 -0.0971 0.0766  -0.0019 316 HOH   A O     
1371 O  O     . HOH   G .   ? 0.2608 0.6132 0.6434 0.1214  -0.0056 0.0353  317 HOH   A O     
1372 O  O     . HOH   G .   ? 0.5440 0.8137 0.5230 0.1709  0.0870  0.1268  318 HOH   A O     
1373 O  O     . HOH   G .   ? 0.2328 0.5936 0.4151 -0.0080 -0.0034 -0.0064 319 HOH   A O     
1374 O  O     . HOH   G .   ? 1.0731 0.7929 0.6535 -0.3962 0.1888  0.0827  320 HOH   A O     
1375 O  O     . HOH   G .   ? 0.5593 0.5853 0.6184 0.2915  0.1194  0.1118  321 HOH   A O     
1376 O  O     . HOH   G .   ? 0.7148 0.8266 0.4114 0.1589  0.0718  0.0939  322 HOH   A O     
1377 O  O     . HOH   G .   ? 0.1427 0.4769 0.4779 0.1094  -0.0663 0.0957  323 HOH   A O     
1378 O  O     . HOH   G .   ? 0.0841 0.3120 0.4386 0.0040  -0.0041 0.0050  324 HOH   A O     
1379 O  O     . HOH   G .   ? 0.0952 0.3777 0.4152 -0.0002 0.0524  -0.0556 325 HOH   A O     
1380 O  O     . HOH   G .   ? 0.5887 0.7516 0.7283 -0.2388 -0.0625 -0.1196 326 HOH   A O     
1381 O  O     . HOH   G .   ? 0.1343 0.6208 0.5643 -0.0120 -0.0176 0.0137  327 HOH   A O     
1382 O  O     . HOH   G .   ? 0.0776 0.6891 0.5110 0.0162  -0.0352 -0.0111 328 HOH   A O     
1383 O  O     . HOH   G .   ? 0.2668 0.6290 0.7919 -0.2252 -0.0261 -0.0100 329 HOH   A O     
1384 O  O     . HOH   G .   ? 0.1827 0.4321 0.5883 0.0407  0.0074  -0.0363 330 HOH   A O     
1385 O  O     . HOH   G .   ? 0.3124 0.6297 0.8495 -0.0647 -0.1503 -0.2127 331 HOH   A O     
1386 O  O     . HOH   G .   ? 0.3675 0.4089 0.5121 -0.0344 0.1006  0.0841  332 HOH   A O     
1387 O  O     . HOH   G .   ? 0.4834 0.3517 0.5355 0.0888  0.0908  0.0080  333 HOH   A O     
1388 O  O     . HOH   G .   ? 0.1965 0.8377 0.5214 -0.2127 0.0513  -0.1269 334 HOH   A O     
1389 O  O     . HOH   G .   ? 0.4333 0.9618 0.7088 -0.0474 0.2062  0.1460  335 HOH   A O     
1390 O  O     . HOH   G .   ? 0.3668 0.6082 0.8428 0.1023  0.0460  -0.1039 336 HOH   A O     
1391 O  O     . HOH   G .   ? 0.2022 0.5620 0.4268 0.0000  -0.0010 -0.0601 337 HOH   A O     
1392 O  O     . HOH   G .   ? 0.4068 0.4559 0.6157 0.1328  0.0787  0.0034  338 HOH   A O     
1393 O  O     . HOH   G .   ? 0.2148 0.7106 0.6781 -0.0556 0.1023  0.0427  339 HOH   A O     
1394 O  O     . HOH   G .   ? 0.2339 0.4433 0.5142 0.0227  0.0159  0.0927  340 HOH   A O     
1395 O  O     . HOH   G .   ? 0.1526 0.3602 0.5522 0.0978  0.0374  0.0748  341 HOH   A O     
1396 O  O     . HOH   G .   ? 0.1541 0.8016 0.5330 0.0244  0.0031  -0.0093 342 HOH   A O     
1397 O  O     . HOH   G .   ? 0.3741 0.4193 0.4428 -0.0804 0.0437  -0.0668 343 HOH   A O     
1398 O  O     . HOH   G .   ? 0.2222 0.4153 0.5103 0.0891  0.0521  0.0161  344 HOH   A O     
1399 O  O     . HOH   G .   ? 0.7498 0.4133 0.7919 -0.2092 -0.2580 -0.0199 345 HOH   A O     
1400 O  O     . HOH   G .   ? 0.3077 0.5973 0.7503 -0.2446 0.0206  -0.0299 346 HOH   A O     
1401 O  O     . HOH   G .   ? 0.1201 0.3545 0.5584 0.0334  -0.0389 -0.0646 347 HOH   A O     
1402 O  O     . HOH   G .   ? 0.2524 0.8764 0.7082 0.0469  0.0470  -0.0948 348 HOH   A O     
1403 O  O     . HOH   G .   ? 0.2251 0.7294 0.9609 0.0599  0.0278  -0.0436 349 HOH   A O     
1404 O  O     . HOH   G .   ? 0.5374 0.3931 0.6403 -0.0105 0.0539  0.0367  350 HOH   A O     
1405 O  O     . HOH   G .   ? 0.1461 0.7350 0.5158 -0.0191 -0.0043 0.0680  351 HOH   A O     
1406 O  O     . HOH   G .   ? 0.1497 0.7853 0.7404 -0.0163 -0.0188 0.0706  352 HOH   A O     
1407 O  O     . HOH   G .   ? 0.5223 0.7504 0.7007 0.0440  -0.2369 0.1249  353 HOH   A O     
1408 O  O     . HOH   G .   ? 0.1808 0.8846 0.5616 0.0452  -0.0065 -0.0539 354 HOH   A O     
1409 O  O     . HOH   G .   ? 0.2751 0.7474 0.6956 0.2037  -0.0067 -0.0754 355 HOH   A O     
1410 O  O     . HOH   G .   ? 0.3985 0.6709 0.8210 0.1001  -0.2248 0.0541  356 HOH   A O     
1411 O  O     . HOH   G .   ? 0.3566 0.7865 0.5544 0.0255  0.0228  -0.0467 357 HOH   A O     
1412 O  O     . HOH   G .   ? 0.2322 0.4238 0.7469 0.0716  -0.1356 -0.0308 358 HOH   A O     
# 
