data_9GGX
# 
_entry.id   9GGX 
# 
_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   9GGX         pdb_00009ggx 10.2210/pdb9ggx/pdb 
WWPDB D_1292140440 ?            ?                   
# 
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                        9GGX 
_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.db_name 
_pdbx_database_related.details 
_pdbx_database_related.db_id 
_pdbx_database_related.content_type 
PDB . 9GGY unspecified 
PDB . 9GH2 unspecified 
PDB . 9GGZ unspecified 
PDB . 9GH0 unspecified 
PDB . 9GH1 unspecified 
PDB . 9GGW unspecified 
PDB . 9GGU unspecified 
PDB . 9GGT unspecified 
PDB . 9GGV unspecified 
PDB . 9G0Y unspecified 
PDB . 9G4B unspecified 
# 
_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    1   ?       ?     ? ? 
5 non-polymer syn 
;(3E,15S)-17-(cis-4-aminocyclohexyl)-7-chloro-10,15,20-trihydroxy-2,2-dioxo-2-lambda-6,5-dithia-3,12,17-triazatetracyclo[17.3.1.04,12.06,11]tricosa-1(22),3,6(11),7,9,19(23),20-heptaen-18-one
;
567.077   1   ?       ?     ? ? 
6 water       nat water 18.015    118 ?       ?     ? ? 
# 
_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 
;(3E,15S)-17-(cis-4-aminocyclohexyl)-7-chloro-10,15,20-trihydroxy-2,2-dioxo-2-lambda-6,5-dithia-3,12,17-triazatetracyclo[17.3.1.04,12.06,11]tricosa-1(22),3,6(11),7,9,19(23),20-heptaen-18-one
;
A1IMB 
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 
A1IMB non-polymer         . 
;(3E,15S)-17-(cis-4-aminocyclohexyl)-7-chloro-10,15,20-trihydroxy-2,2-dioxo-2-lambda-6,5-dithia-3,12,17-triazatetracyclo[17.3.1.04,12.06,11]tricosa-1(22),3,6(11),7,9,19(23),20-heptaen-18-one
;
? 'C24 H27 Cl N4 O6 S2' 567.077 
ALA   'L-peptide linking' y ALANINE ? 'C3 H7 N O2'          89.093  
ARG   'L-peptide linking' y ARGININE ? 'C6 H15 N4 O2 1'      175.209 
ASN   'L-peptide linking' y ASPARAGINE ? 'C4 H8 N2 O3'         132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'          133.103 
CO    non-polymer         . 'COBALT (II) ION' ? 'Co 2'                58.933  
CYS   'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S'        121.158 
GLN   'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3'        146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'          147.129 
GLY   'peptide linking'   y GLYCINE ? 'C2 H5 N O2'          75.067  
GNP   non-polymer         . 'PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER' ? 'C10 H17 N6 O13 P3'   522.196 
HIS   'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1'      156.162 
HOH   non-polymer         . WATER ? 'H2 O'                18.015  
ILE   'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2'         131.173 
LEU   'L-peptide linking' y LEUCINE ? 'C6 H13 N O2'         131.173 
LYS   'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1'      147.195 
MET   'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S'       149.211 
MG    non-polymer         . 'MAGNESIUM ION' ? 'Mg 2'                24.305  
PHE   'L-peptide linking' y PHENYLALANINE ? 'C9 H11 N O2'         165.189 
PRO   'L-peptide linking' y PROLINE ? 'C5 H9 N O2'          115.130 
SER   'L-peptide linking' y SERINE ? 'C3 H7 N O3'          105.093 
THR   'L-peptide linking' y THREONINE ? 'C4 H9 N O3'          119.119 
TYR   'L-peptide linking' y TYROSINE ? 'C9 H11 N O3'         181.189 
VAL   'L-peptide linking' y VALINE ? 'C5 H11 N O2'         117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   GLY 1   -2  ?   ?   ?   A . n 
A 1 2   GLY 2   -1  ?   ?   ?   A . n 
A 1 3   SER 3   0   ?   ?   ?   A . n 
A 1 4   MET 4   1   1   MET MET A . n 
A 1 5   THR 5   2   2   THR THR A . n 
A 1 6   GLU 6   3   3   GLU GLU A . n 
A 1 7   TYR 7   4   4   TYR TYR A . n 
A 1 8   LYS 8   5   5   LYS LYS A . n 
A 1 9   LEU 9   6   6   LEU LEU A . n 
A 1 10  VAL 10  7   7   VAL VAL A . n 
A 1 11  VAL 11  8   8   VAL VAL A . n 
A 1 12  VAL 12  9   9   VAL VAL A . n 
A 1 13  GLY 13  10  10  GLY GLY A . n 
A 1 14  ALA 14  11  11  ALA ALA A . n 
A 1 15  GLY 15  12  12  GLY GLY A . n 
A 1 16  GLY 16  13  13  GLY GLY A . n 
A 1 17  VAL 17  14  14  VAL VAL A . n 
A 1 18  GLY 18  15  15  GLY GLY A . n 
A 1 19  LYS 19  16  16  LYS LYS A . n 
A 1 20  SER 20  17  17  SER SER A . n 
A 1 21  ALA 21  18  18  ALA ALA A . n 
A 1 22  LEU 22  19  19  LEU LEU A . n 
A 1 23  THR 23  20  20  THR THR A . n 
A 1 24  ILE 24  21  21  ILE ILE A . n 
A 1 25  GLN 25  22  22  GLN GLN A . n 
A 1 26  LEU 26  23  23  LEU LEU A . n 
A 1 27  ILE 27  24  24  ILE ILE A . n 
A 1 28  GLN 28  25  25  GLN GLN A . n 
A 1 29  ASN 29  26  26  ASN ASN A . n 
A 1 30  HIS 30  27  27  HIS HIS A . n 
A 1 31  PHE 31  28  28  PHE PHE A . n 
A 1 32  VAL 32  29  29  VAL VAL A . n 
A 1 33  ASP 33  30  30  ASP ASP A . n 
A 1 34  GLU 34  31  31  GLU GLU A . n 
A 1 35  TYR 35  32  32  TYR TYR A . n 
A 1 36  ASP 36  33  33  ASP ASP A . n 
A 1 37  PRO 37  34  34  PRO PRO A . n 
A 1 38  THR 38  35  35  THR THR A . n 
A 1 39  ILE 39  36  36  ILE ILE A . n 
A 1 40  GLU 40  37  37  GLU GLU A . n 
A 1 41  ASP 41  38  38  ASP ASP A . n 
A 1 42  SER 42  39  39  SER SER A . n 
A 1 43  TYR 43  40  40  TYR TYR A . n 
A 1 44  ARG 44  41  41  ARG ARG A . n 
A 1 45  LYS 45  42  42  LYS LYS A . n 
A 1 46  GLN 46  43  43  GLN GLN A . n 
A 1 47  VAL 47  44  44  VAL VAL A . n 
A 1 48  VAL 48  45  45  VAL VAL A . n 
A 1 49  ILE 49  46  46  ILE ILE A . n 
A 1 50  ASP 50  47  47  ASP ASP A . n 
A 1 51  GLY 51  48  48  GLY GLY A . n 
A 1 52  GLU 52  49  49  GLU GLU A . n 
A 1 53  THR 53  50  50  THR THR A . n 
A 1 54  CYS 54  51  51  CYS CYS A . n 
A 1 55  LEU 55  52  52  LEU LEU A . n 
A 1 56  LEU 56  53  53  LEU LEU A . n 
A 1 57  ASP 57  54  54  ASP ASP A . n 
A 1 58  ILE 58  55  55  ILE ILE A . n 
A 1 59  LEU 59  56  56  LEU LEU A . n 
A 1 60  ASP 60  57  57  ASP ASP A . n 
A 1 61  THR 61  58  58  THR THR A . n 
A 1 62  ALA 62  59  59  ALA ALA A . n 
A 1 63  GLY 63  60  60  GLY GLY A . n 
A 1 64  GLN 64  61  61  GLN GLN A . n 
A 1 65  GLU 65  62  62  GLU GLU A . n 
A 1 66  GLU 66  63  63  GLU GLU A . n 
A 1 67  TYR 67  64  64  TYR TYR A . n 
A 1 68  SER 68  65  65  SER SER A . n 
A 1 69  ALA 69  66  66  ALA ALA A . n 
A 1 70  MET 70  67  67  MET MET A . n 
A 1 71  ARG 71  68  68  ARG ARG A . n 
A 1 72  ASP 72  69  69  ASP ASP A . n 
A 1 73  GLN 73  70  70  GLN GLN A . n 
A 1 74  TYR 74  71  71  TYR TYR A . n 
A 1 75  MET 75  72  72  MET MET A . n 
A 1 76  ARG 76  73  73  ARG ARG A . n 
A 1 77  THR 77  74  74  THR THR A . n 
A 1 78  GLY 78  75  75  GLY GLY A . n 
A 1 79  GLU 79  76  76  GLU GLU A . n 
A 1 80  GLY 80  77  77  GLY GLY A . n 
A 1 81  PHE 81  78  78  PHE PHE A . n 
A 1 82  LEU 82  79  79  LEU LEU A . n 
A 1 83  CYS 83  80  80  CYS CYS A . n 
A 1 84  VAL 84  81  81  VAL VAL A . n 
A 1 85  PHE 85  82  82  PHE PHE A . n 
A 1 86  ALA 86  83  83  ALA ALA A . n 
A 1 87  ILE 87  84  84  ILE ILE A . n 
A 1 88  ASN 88  85  85  ASN ASN A . n 
A 1 89  ASN 89  86  86  ASN ASN A . n 
A 1 90  THR 90  87  87  THR THR A . n 
A 1 91  LYS 91  88  88  LYS LYS A . n 
A 1 92  SER 92  89  89  SER SER A . n 
A 1 93  PHE 93  90  90  PHE PHE A . n 
A 1 94  GLU 94  91  91  GLU GLU A . n 
A 1 95  ASP 95  92  92  ASP ASP A . n 
A 1 96  ILE 96  93  93  ILE ILE A . n 
A 1 97  HIS 97  94  94  HIS HIS A . n 
A 1 98  HIS 98  95  95  HIS HIS A . n 
A 1 99  TYR 99  96  96  TYR TYR A . n 
A 1 100 ARG 100 97  97  ARG ARG A . n 
A 1 101 GLU 101 98  98  GLU GLU A . n 
A 1 102 GLN 102 99  99  GLN GLN A . n 
A 1 103 ILE 103 100 100 ILE ILE A . n 
A 1 104 LYS 104 101 101 LYS LYS A . n 
A 1 105 ARG 105 102 102 ARG ARG A . n 
A 1 106 VAL 106 103 103 VAL VAL A . n 
A 1 107 LYS 107 104 104 LYS LYS A . n 
A 1 108 ASP 108 105 105 ASP ASP A . n 
A 1 109 SER 109 106 106 SER SER A . n 
A 1 110 GLU 110 107 107 GLU GLU A . n 
A 1 111 ASP 111 108 108 ASP ASP A . n 
A 1 112 VAL 112 109 109 VAL VAL A . n 
A 1 113 PRO 113 110 110 PRO PRO A . n 
A 1 114 MET 114 111 111 MET MET A . n 
A 1 115 VAL 115 112 112 VAL VAL A . n 
A 1 116 LEU 116 113 113 LEU LEU A . n 
A 1 117 VAL 117 114 114 VAL VAL A . n 
A 1 118 GLY 118 115 115 GLY GLY A . n 
A 1 119 ASN 119 116 116 ASN ASN A . n 
A 1 120 LYS 120 117 117 LYS LYS A . n 
A 1 121 SER 121 118 118 SER SER A . n 
A 1 122 ASP 122 119 119 ASP ASP A . n 
A 1 123 LEU 123 120 120 LEU LEU A . n 
A 1 124 PRO 124 121 121 PRO PRO A . n 
A 1 125 SER 125 122 122 SER SER A . n 
A 1 126 ARG 126 123 123 ARG ARG A . n 
A 1 127 THR 127 124 124 THR THR A . n 
A 1 128 VAL 128 125 125 VAL VAL A . n 
A 1 129 ASP 129 126 126 ASP ASP A . n 
A 1 130 THR 130 127 127 THR THR A . n 
A 1 131 LYS 131 128 128 LYS LYS A . n 
A 1 132 GLN 132 129 129 GLN GLN A . n 
A 1 133 ALA 133 130 130 ALA ALA A . n 
A 1 134 GLN 134 131 131 GLN GLN A . n 
A 1 135 ASP 135 132 132 ASP ASP A . n 
A 1 136 LEU 136 133 133 LEU LEU A . n 
A 1 137 ALA 137 134 134 ALA ALA A . n 
A 1 138 ARG 138 135 135 ARG ARG A . n 
A 1 139 SER 139 136 136 SER SER A . n 
A 1 140 TYR 140 137 137 TYR TYR A . n 
A 1 141 GLY 141 138 138 GLY GLY A . n 
A 1 142 ILE 142 139 139 ILE ILE A . n 
A 1 143 PRO 143 140 140 PRO PRO A . n 
A 1 144 PHE 144 141 141 PHE PHE A . n 
A 1 145 ILE 145 142 142 ILE ILE A . n 
A 1 146 GLU 146 143 143 GLU GLU A . n 
A 1 147 THR 147 144 144 THR THR A . n 
A 1 148 SER 148 145 145 SER SER A . n 
A 1 149 ALA 149 146 146 ALA ALA A . n 
A 1 150 LYS 150 147 147 LYS LYS A . n 
A 1 151 THR 151 148 148 THR THR A . n 
A 1 152 ARG 152 149 149 ARG ARG A . n 
A 1 153 GLN 153 150 150 GLN GLN A . n 
A 1 154 ARG 154 151 151 ARG ARG A . n 
A 1 155 VAL 155 152 152 VAL VAL A . n 
A 1 156 GLU 156 153 153 GLU GLU A . n 
A 1 157 ASP 157 154 154 ASP ASP A . n 
A 1 158 ALA 158 155 155 ALA ALA A . n 
A 1 159 PHE 159 156 156 PHE PHE A . n 
A 1 160 TYR 160 157 157 TYR TYR A . n 
A 1 161 THR 161 158 158 THR THR A . n 
A 1 162 LEU 162 159 159 LEU LEU A . n 
A 1 163 VAL 163 160 160 VAL VAL A . n 
A 1 164 ARG 164 161 161 ARG ARG A . n 
A 1 165 GLU 165 162 162 GLU GLU A . n 
A 1 166 ILE 166 163 163 ILE ILE A . n 
A 1 167 ARG 167 164 164 ARG ARG A . n 
A 1 168 GLN 168 165 165 GLN GLN A . n 
A 1 169 TYR 169 166 166 TYR TYR A . n 
A 1 170 ARG 170 167 167 ARG ARG A . n 
A 1 171 LEU 171 168 168 LEU LEU A . n 
A 1 172 LYS 172 169 169 LYS LYS A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1IMB 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1IMB 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
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 2    CO    CO  A . 
E 5 A1IMB 1   204 1    A1IMB DRG A . 
F 6 HOH   1   301 223  HOH   HOH A . 
F 6 HOH   2   302 124  HOH   HOH A . 
F 6 HOH   3   303 149  HOH   HOH A . 
F 6 HOH   4   304 9    HOH   HOH A . 
F 6 HOH   5   305 123  HOH   HOH A . 
F 6 HOH   6   306 243  HOH   HOH A . 
F 6 HOH   7   307 231  HOH   HOH A . 
F 6 HOH   8   308 212  HOH   HOH A . 
F 6 HOH   9   309 125  HOH   HOH A . 
F 6 HOH   10  310 195  HOH   HOH A . 
F 6 HOH   11  311 203  HOH   HOH A . 
F 6 HOH   12  312 159  HOH   HOH A . 
F 6 HOH   13  313 75   HOH   HOH A . 
F 6 HOH   14  314 135  HOH   HOH A . 
F 6 HOH   15  315 63   HOH   HOH A . 
F 6 HOH   16  316 153  HOH   HOH A . 
F 6 HOH   17  317 137  HOH   HOH A . 
F 6 HOH   18  318 144  HOH   HOH A . 
F 6 HOH   19  319 120  HOH   HOH A . 
F 6 HOH   20  320 240  HOH   HOH A . 
F 6 HOH   21  321 227  HOH   HOH A . 
F 6 HOH   22  322 128  HOH   HOH A . 
F 6 HOH   23  323 230  HOH   HOH A . 
F 6 HOH   24  324 138  HOH   HOH A . 
F 6 HOH   25  325 181  HOH   HOH A . 
F 6 HOH   26  326 145  HOH   HOH A . 
F 6 HOH   27  327 143  HOH   HOH A . 
F 6 HOH   28  328 200  HOH   HOH A . 
F 6 HOH   29  329 189  HOH   HOH A . 
F 6 HOH   30  330 208  HOH   HOH A . 
F 6 HOH   31  331 151  HOH   HOH A . 
F 6 HOH   32  332 2    HOH   HOH A . 
F 6 HOH   33  333 193  HOH   HOH A . 
F 6 HOH   34  334 78   HOH   HOH A . 
F 6 HOH   35  335 1    HOH   HOH A . 
F 6 HOH   36  336 155  HOH   HOH A . 
F 6 HOH   37  337 5    HOH   HOH A . 
F 6 HOH   38  338 101  HOH   HOH A . 
F 6 HOH   39  339 248  HOH   HOH A . 
F 6 HOH   40  340 64   HOH   HOH A . 
F 6 HOH   41  341 108  HOH   HOH A . 
F 6 HOH   42  342 127  HOH   HOH A . 
F 6 HOH   43  343 170  HOH   HOH A . 
F 6 HOH   44  344 175  HOH   HOH A . 
F 6 HOH   45  345 152  HOH   HOH A . 
F 6 HOH   46  346 156  HOH   HOH A . 
F 6 HOH   47  347 112  HOH   HOH A . 
F 6 HOH   48  348 218  HOH   HOH A . 
F 6 HOH   49  349 148  HOH   HOH A . 
F 6 HOH   50  350 180  HOH   HOH A . 
F 6 HOH   51  351 210  HOH   HOH A . 
F 6 HOH   52  352 53   HOH   HOH A . 
F 6 HOH   53  353 122  HOH   HOH A . 
F 6 HOH   54  354 196  HOH   HOH A . 
F 6 HOH   55  355 109  HOH   HOH A . 
F 6 HOH   56  356 245  HOH   HOH A . 
F 6 HOH   57  357 238  HOH   HOH A . 
F 6 HOH   58  358 251  HOH   HOH A . 
F 6 HOH   59  359 56   HOH   HOH A . 
F 6 HOH   60  360 244  HOH   HOH A . 
F 6 HOH   61  361 136  HOH   HOH A . 
F 6 HOH   62  362 161  HOH   HOH A . 
F 6 HOH   63  363 163  HOH   HOH A . 
F 6 HOH   64  364 177  HOH   HOH A . 
F 6 HOH   65  365 79   HOH   HOH A . 
F 6 HOH   66  366 45   HOH   HOH A . 
F 6 HOH   67  367 235  HOH   HOH A . 
F 6 HOH   68  368 57   HOH   HOH A . 
F 6 HOH   69  369 13   HOH   HOH A . 
F 6 HOH   70  370 224  HOH   HOH A . 
F 6 HOH   71  371 265  HOH   HOH A . 
F 6 HOH   72  372 30   HOH   HOH A . 
F 6 HOH   73  373 154  HOH   HOH A . 
F 6 HOH   74  374 169  HOH   HOH A . 
F 6 HOH   75  375 173  HOH   HOH A . 
F 6 HOH   76  376 126  HOH   HOH A . 
F 6 HOH   77  377 142  HOH   HOH A . 
F 6 HOH   78  378 234  HOH   HOH A . 
F 6 HOH   79  379 61   HOH   HOH A . 
F 6 HOH   80  380 204  HOH   HOH A . 
F 6 HOH   81  381 158  HOH   HOH A . 
F 6 HOH   82  382 140  HOH   HOH A . 
F 6 HOH   83  383 146  HOH   HOH A . 
F 6 HOH   84  384 131  HOH   HOH A . 
F 6 HOH   85  385 166  HOH   HOH A . 
F 6 HOH   86  386 150  HOH   HOH A . 
F 6 HOH   87  387 80   HOH   HOH A . 
F 6 HOH   88  388 171  HOH   HOH A . 
F 6 HOH   89  389 129  HOH   HOH A . 
F 6 HOH   90  390 139  HOH   HOH A . 
F 6 HOH   91  391 130  HOH   HOH A . 
F 6 HOH   92  392 191  HOH   HOH A . 
F 6 HOH   93  393 215  HOH   HOH A . 
F 6 HOH   94  394 81   HOH   HOH A . 
F 6 HOH   95  395 252  HOH   HOH A . 
F 6 HOH   96  396 247  HOH   HOH A . 
F 6 HOH   97  397 147  HOH   HOH A . 
F 6 HOH   98  398 133  HOH   HOH A . 
F 6 HOH   99  399 259  HOH   HOH A . 
F 6 HOH   100 400 141  HOH   HOH A . 
F 6 HOH   101 401 162  HOH   HOH A . 
F 6 HOH   102 402 160  HOH   HOH A . 
F 6 HOH   103 403 157  HOH   HOH A . 
F 6 HOH   104 404 257  HOH   HOH A . 
F 6 HOH   105 405 255  HOH   HOH A . 
F 6 HOH   106 406 176  HOH   HOH A . 
F 6 HOH   107 407 167  HOH   HOH A . 
F 6 HOH   108 408 164  HOH   HOH A . 
F 6 HOH   109 409 264  HOH   HOH A . 
F 6 HOH   110 410 187  HOH   HOH A . 
F 6 HOH   111 411 236  HOH   HOH A . 
F 6 HOH   112 412 233  HOH   HOH A . 
F 6 HOH   113 413 260  HOH   HOH A . 
F 6 HOH   114 414 222  HOH   HOH A . 
F 6 HOH   115 415 250  HOH   HOH A . 
F 6 HOH   116 416 226  HOH   HOH A . 
F 6 HOH   117 417 229  HOH   HOH A . 
F 6 HOH   118 418 261  HOH   HOH A . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 0 A GLU 31  ? CG  ? A GLU 34  CG  
2  1 Y 0 A GLU 31  ? CD  ? A GLU 34  CD  
3  1 Y 0 A GLU 31  ? OE1 ? A GLU 34  OE1 
4  1 Y 0 A GLU 31  ? OE2 ? A GLU 34  OE2 
5  1 Y 0 A GLU 63  ? CG  ? A GLU 66  CG  
6  1 Y 0 A GLU 63  ? CD  ? A GLU 66  CD  
7  1 Y 0 A GLU 63  ? OE1 ? A GLU 66  OE1 
8  1 Y 0 A GLU 63  ? OE2 ? A GLU 66  OE2 
9  1 Y 0 A GLU 107 ? CG  ? A GLU 110 CG  
10 1 Y 0 A GLU 107 ? CD  ? A GLU 110 CD  
11 1 Y 0 A GLU 107 ? OE1 ? A GLU 110 OE1 
12 1 Y 0 A GLU 107 ? OE2 ? A GLU 110 OE2 
13 1 Y 0 A GLN 165 ? CD  ? A GLN 168 CD  
14 1 Y 0 A GLN 165 ? OE1 ? A GLN 168 OE1 
15 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                   109.770 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9GGX 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     71.541 
_cell.length_a_esd                 ? 
_cell.length_b                     34.241 
_cell.length_b_esd                 ? 
_cell.length_c                     69.776 
_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                         9GGX 
_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                   9GGX 
_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             2.05 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          40.03 
_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               0.190 
_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 EIGER X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2021-02-18 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.9795 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'DIAMOND BEAMLINE I04' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9795 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   I04 
_diffrn_source.pdbx_synchrotron_site       Diamond 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9GGX 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.290 
_reflns.d_resolution_low                               29.460 
_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                                     38563 
_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                           96.800 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                3.300 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          8.100 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           2 
_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                                0.068 
_reflns.pdbx_Rpim_I_all                                0.037 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       126902 
_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                              0.057 
_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 
1.290 1.330  ? ? ? ? ? ? 2387 ? ? ? ? ? ? ? ? ? ? ? 2.700 ? ? ? 0.636 0.364 ? 1 1 0.944 ? ? 81.100 ? 0.517 ? ? ? ? ? ? ? ? ? 
5.790 29.460 ? ? ? ? ? ? 464  ? ? ? ? ? ? ? ? ? ? ? 3.300 ? ? ? 0.042 0.022 ? 2 1 0.996 ? ? 95.600 ? 0.035 ? ? ? ? ? ? ? ? ? 
# 
_refine.aniso_B[1][1]                            -1.0400 
_refine.aniso_B[1][2]                            0.0000 
_refine.aniso_B[1][3]                            0.0200 
_refine.aniso_B[2][2]                            1.1600 
_refine.aniso_B[2][3]                            0.0000 
_refine.aniso_B[3][3]                            -0.1000 
_refine.B_iso_max                                52.680 
_refine.B_iso_mean                               22.5280 
_refine.B_iso_min                                14.940 
_refine.correlation_coeff_Fo_to_Fc               0.9720 
_refine.correlation_coeff_Fo_to_Fc_free          0.9620 
_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                                 9GGX 
_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                            1.3000 
_refine.ls_d_res_low                             29.4600 
_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                     36660 
_refine.ls_number_reflns_R_free                  1900 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    96.9000 
_refine.ls_percent_reflns_R_free                 4.9000 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1839 
_refine.ls_R_factor_R_free                       0.2235 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1819 
_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                       0.0630 
_refine.pdbx_overall_ESU_R_Free                  0.0610 
_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                             3.6770 
_refine.overall_SU_ML                            0.0640 
_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                       1.3000 
_refine_hist.d_res_low                        29.4600 
_refine_hist.number_atoms_solvent             118 
_refine_hist.number_atoms_total               1551 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       169 
_refine_hist.pdbx_B_iso_mean_ligand           22.85 
_refine_hist.pdbx_B_iso_mean_solvent          32.16 
_refine_hist.pdbx_number_atoms_protein        1362 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         71 
_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' ? 0.020  0.013  1443 ? r_bond_refined_d       ? ? 
'X-RAY DIFFRACTION' ? 0.035  0.018  1313 ? r_bond_other_d         ? ? 
'X-RAY DIFFRACTION' ? 2.022  1.706  1963 ? r_angle_refined_deg    ? ? 
'X-RAY DIFFRACTION' ? 2.393  1.622  3037 ? r_angle_other_deg      ? ? 
'X-RAY DIFFRACTION' ? 4.482  5.000  168  ? r_dihedral_angle_1_deg ? ? 
'X-RAY DIFFRACTION' ? 33.865 21.646 79   ? r_dihedral_angle_2_deg ? ? 
'X-RAY DIFFRACTION' ? 12.440 15.000 247  ? r_dihedral_angle_3_deg ? ? 
'X-RAY DIFFRACTION' ? 13.720 15.000 12   ? r_dihedral_angle_4_deg ? ? 
'X-RAY DIFFRACTION' ? 0.136  0.200  192  ? r_chiral_restr         ? ? 
'X-RAY DIFFRACTION' ? 0.010  0.020  1586 ? r_gen_planes_refined   ? ? 
'X-RAY DIFFRACTION' ? 0.011  0.020  303  ? r_gen_planes_other     ? ? 
'X-RAY DIFFRACTION' ? 2.128  2.198  675  ? r_mcbond_it            ? ? 
'X-RAY DIFFRACTION' ? 2.129  2.194  674  ? r_mcbond_other         ? ? 
'X-RAY DIFFRACTION' ? 2.486  3.297  842  ? r_mcangle_it           ? ? 
'X-RAY DIFFRACTION' ? 2.853  3.000  2756 ? r_rigid_bond_restr     ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.3000 
_refine_ls_shell.d_res_low                        1.3300 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             116 
_refine_ls_shell.number_reflns_R_work             2376 
_refine_ls_shell.percent_reflns_obs               85.8100 
_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                  0.3640 
_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   ? 
_refine_ls_shell.pdbx_phase_error                 ? 
_refine_ls_shell.pdbx_fsc_work                    ? 
_refine_ls_shell.pdbx_fsc_free                    ? 
_refine_ls_shell.R_factor_R_free                  0.3270 
# 
_struct.entry_id                     9GGX 
_struct.title                        'Human KRas4A (GMPPNP) in complex with compound 19' 
_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        9GGX 
_struct_keywords.text            'RAS, GTPase, inhibitor, CELL CYCLE' 
_struct_keywords.pdbx_keywords   'CELL CYCLE' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 5 ? 
F N N 6 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    RASK_HUMAN 
_struct_ref.pdbx_db_accession          P01116 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MTEYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLC
VFAINNTKSFEDIHHYREQIKRVKDSEDVPMVLVGNKCDLPSRTVDTKQAQDLARSYGIPFIETSAKTRQRVEDAFYTLV
REIRQYRLK
;
_struct_ref.pdbx_align_begin           1 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9GGX 
_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 9GGX GLY A 1   ? UNP P01116 ?   ?   'expression tag'      -2  1 
1 9GGX GLY A 2   ? UNP P01116 ?   ?   'expression tag'      -1  2 
1 9GGX SER A 3   ? UNP P01116 ?   ?   'expression tag'      0   3 
1 9GGX 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)' 1700 ? 
1 MORE         -23  ? 
1 'SSA (A^2)'  8510 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 GLY A 18  ? ASN A 29  ? GLY A 15  ASN A 26  1 ? 12 
HELX_P HELX_P2 AA2 MET A 70  ? GLY A 78  ? MET A 67  GLY A 75  1 ? 9  
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 ? ? ? ? ? ? ? 2.030 ? ? 
metalc2  metalc ? ? A HIS 97  NE2 ? ? ? 1_555 D CO  . CO ? ? A HIS 94  A CO  203 1_555 ? ? ? ? ? ? ? 2.246 ? ? 
metalc3  metalc ? ? A HIS 98  NE2 ? ? ? 1_555 D CO  . CO ? ? A HIS 95  A CO  203 2_655 ? ? ? ? ? ? ? 2.056 ? ? 
metalc4  metalc ? ? A GLU 101 OE1 ? ? ? 1_555 D CO  . CO ? ? A GLU 98  A CO  203 1_555 ? ? ? ? ? ? ? 2.065 ? ? 
metalc5  metalc ? ? B GNP .   O1G ? ? ? 1_555 C MG  . MG ? ? A GNP 201 A MG  202 1_555 ? ? ? ? ? ? ? 2.165 ? ? 
metalc6  metalc ? ? B GNP .   O2B ? ? ? 1_555 C MG  . MG ? ? A GNP 201 A MG  202 1_555 ? ? ? ? ? ? ? 2.153 ? ? 
metalc7  metalc ? ? C MG  .   MG  ? ? ? 1_555 F HOH . O  ? ? A MG  202 A HOH 302 1_555 ? ? ? ? ? ? ? 2.199 ? ? 
metalc8  metalc ? ? C MG  .   MG  ? ? ? 1_555 F HOH . O  ? ? A MG  202 A HOH 338 1_555 ? ? ? ? ? ? ? 2.068 ? ? 
metalc9  metalc ? ? C MG  .   MG  ? ? ? 1_555 F HOH . O  ? ? A MG  202 A HOH 359 1_555 ? ? ? ? ? ? ? 2.265 ? ? 
metalc10 metalc ? ? D CO  .   CO  ? ? ? 1_555 F HOH . O  ? ? A CO  203 A HOH 303 1_555 ? ? ? ? ? ? ? 2.238 ? ? 
metalc11 metalc ? ? D CO  .   CO  ? ? ? 1_555 F HOH . O  ? ? A CO  203 A HOH 313 2_655 ? ? ? ? ? ? ? 2.203 ? ? 
metalc12 metalc ? ? D CO  .   CO  ? ? ? 1_555 F HOH . O  ? ? A CO  203 A HOH 369 1_555 ? ? ? ? ? ? ? 2.265 ? ? 
# 
_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_555 173.0 ? 
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 90.5  ? 
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 92.3  ? 
4  OG  ? A SER 20  ? A SER 17  ? 1_555 MG ? C MG . ? A MG 202 ? 1_555 O   ? F HOH .   ? A HOH 302 ? 1_555 83.9  ? 
5  O1G ? B GNP .   ? A GNP 201 ? 1_555 MG ? C MG . ? A MG 202 ? 1_555 O   ? F HOH .   ? A HOH 302 ? 1_555 89.5  ? 
6  O2B ? B GNP .   ? A GNP 201 ? 1_555 MG ? C MG . ? A MG 202 ? 1_555 O   ? F HOH .   ? A HOH 302 ? 1_555 95.1  ? 
7  OG  ? A SER 20  ? A SER 17  ? 1_555 MG ? C MG . ? A MG 202 ? 1_555 O   ? F HOH .   ? A HOH 338 ? 1_555 83.5  ? 
8  O1G ? B GNP .   ? A GNP 201 ? 1_555 MG ? C MG . ? A MG 202 ? 1_555 O   ? F HOH .   ? A HOH 338 ? 1_555 102.9 ? 
9  O2B ? B GNP .   ? A GNP 201 ? 1_555 MG ? C MG . ? A MG 202 ? 1_555 O   ? F HOH .   ? A HOH 338 ? 1_555 91.3  ? 
10 O   ? F HOH .   ? A HOH 302 ? 1_555 MG ? C MG . ? A MG 202 ? 1_555 O   ? F HOH .   ? A HOH 338 ? 1_555 165.9 ? 
11 OG  ? A SER 20  ? A SER 17  ? 1_555 MG ? C MG . ? A MG 202 ? 1_555 O   ? F HOH .   ? A HOH 359 ? 1_555 85.8  ? 
12 O1G ? B GNP .   ? A GNP 201 ? 1_555 MG ? C MG . ? A MG 202 ? 1_555 O   ? F HOH .   ? A HOH 359 ? 1_555 91.6  ? 
13 O2B ? B GNP .   ? A GNP 201 ? 1_555 MG ? C MG . ? A MG 202 ? 1_555 O   ? F HOH .   ? A HOH 359 ? 1_555 175.8 ? 
14 O   ? F HOH .   ? A HOH 302 ? 1_555 MG ? C MG . ? A MG 202 ? 1_555 O   ? F HOH .   ? A HOH 359 ? 1_555 86.6  ? 
15 O   ? F HOH .   ? A HOH 338 ? 1_555 MG ? C MG . ? A MG 202 ? 1_555 O   ? F HOH .   ? A HOH 359 ? 1_555 86.3  ? 
16 NE2 ? A HIS 97  ? A HIS 94  ? 1_555 CO ? D CO . ? A CO 203 ? 1_555 NE2 ? A HIS 98  ? A HIS 95  ? 1_555 67.3  ? 
17 NE2 ? A HIS 97  ? A HIS 94  ? 1_555 CO ? D CO . ? A CO 203 ? 1_555 OE1 ? A GLU 101 ? A GLU 98  ? 1_555 90.2  ? 
18 NE2 ? A HIS 98  ? A HIS 95  ? 1_555 CO ? D CO . ? A CO 203 ? 1_555 OE1 ? A GLU 101 ? A GLU 98  ? 1_555 119.6 ? 
19 NE2 ? A HIS 97  ? A HIS 94  ? 1_555 CO ? D CO . ? A CO 203 ? 1_555 O   ? F HOH .   ? A HOH 303 ? 1_555 176.0 ? 
20 NE2 ? A HIS 98  ? A HIS 95  ? 1_555 CO ? D CO . ? A CO 203 ? 1_555 O   ? F HOH .   ? A HOH 303 ? 1_555 115.7 ? 
21 OE1 ? A GLU 101 ? A GLU 98  ? 1_555 CO ? D CO . ? A CO 203 ? 1_555 O   ? F HOH .   ? A HOH 303 ? 1_555 86.1  ? 
22 NE2 ? A HIS 97  ? A HIS 94  ? 1_555 CO ? D CO . ? A CO 203 ? 1_555 O   ? F HOH .   ? A HOH 313 ? 2_655 90.8  ? 
23 NE2 ? A HIS 98  ? A HIS 95  ? 1_555 CO ? D CO . ? A CO 203 ? 1_555 O   ? F HOH .   ? A HOH 313 ? 2_655 145.8 ? 
24 OE1 ? A GLU 101 ? A GLU 98  ? 1_555 CO ? D CO . ? A CO 203 ? 1_555 O   ? F HOH .   ? A HOH 313 ? 2_655 84.8  ? 
25 O   ? F HOH .   ? A HOH 303 ? 1_555 CO ? D CO . ? A CO 203 ? 1_555 O   ? F HOH .   ? A HOH 313 ? 2_655 87.6  ? 
26 NE2 ? A HIS 97  ? A HIS 94  ? 1_555 CO ? D CO . ? A CO 203 ? 1_555 O   ? F HOH .   ? A HOH 369 ? 1_555 96.8  ? 
27 NE2 ? A HIS 98  ? A HIS 95  ? 1_555 CO ? D CO . ? A CO 203 ? 1_555 O   ? F HOH .   ? A HOH 369 ? 1_555 47.9  ? 
28 OE1 ? A GLU 101 ? A GLU 98  ? 1_555 CO ? D CO . ? A CO 203 ? 1_555 O   ? F HOH .   ? A HOH 369 ? 1_555 83.7  ? 
29 O   ? F HOH .   ? A HOH 303 ? 1_555 CO ? D CO . ? A CO 203 ? 1_555 O   ? F HOH .   ? A HOH 369 ? 1_555 84.0  ? 
30 O   ? F HOH .   ? A HOH 313 ? 2_655 CO ? D CO . ? A CO 203 ? 1_555 O   ? F HOH .   ? A HOH 369 ? 1_555 166.2 ? 
# 
_struct_sheet.id               AA1 
_struct_sheet.type             ? 
_struct_sheet.number_strands   6 
_struct_sheet.details          ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA1 4 5 ? parallel      
AA1 5 6 ? parallel      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 ASP A 41  ? ILE A 49  ? ASP A 38  ILE A 46  
AA1 2 GLU A 52  ? ASP A 60  ? GLU A 49  ASP A 57  
AA1 3 THR A 5   ? GLY A 13  ? THR A 2   GLY A 10  
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 55  ? O LEU A 52  N THR A 5   ? N THR A 2   
AA1 3 4 N VAL A 10  ? N VAL A 7   O LEU A 82  ? O LEU A 79  
AA1 4 5 N PHE A 85  ? N PHE A 82  O ASN A 119 ? O ASN A 116 
AA1 5 6 N LEU A 116 ? N LEU A 113 O ILE A 145 ? O ILE A 142 
# 
_pdbx_entry_details.entry_id                   9GGX 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_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            OE2 
_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                1.176 
_pdbx_validate_rmsd_bond.bond_target_value         1.252 
_pdbx_validate_rmsd_bond.bond_deviation            -0.076 
_pdbx_validate_rmsd_bond.bond_standard_deviation   0.011 
_pdbx_validate_rmsd_bond.linker_flag               N 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A GLY -2 ? A GLY 1 
2 1 Y 1 A GLY -1 ? A GLY 2 
3 1 Y 1 A SER 0  ? A SER 3 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
A1IMB OAT    O  N N 1   
A1IMB CAS    C  N N 2   
A1IMB CAM    C  Y N 3   
A1IMB CAN    C  Y N 4   
A1IMB CAL    C  Y N 5   
A1IMB OAR    O  N N 6   
A1IMB CAK    C  Y N 7   
A1IMB CAJ    C  Y N 8   
A1IMB CAI    C  Y N 9   
A1IMB SAH    S  N N 10  
A1IMB OAP    O  N N 11  
A1IMB OAQ    O  N N 12  
A1IMB NAG    N  N N 13  
A1IMB CAF    C  N N 14  
A1IMB SAO    S  N N 15  
A1IMB CAC    C  Y N 16  
A1IMB CAB    C  Y N 17  
A1IMB CLAA   CL N N 18  
A1IMB CBJ    C  Y N 19  
A1IMB CBK    C  Y N 20  
A1IMB CBG    C  Y N 21  
A1IMB OBH    O  N N 22  
A1IMB CAD    C  Y N 23  
A1IMB NAE    N  N N 24  
A1IMB CAU    C  N N 25  
A1IMB CAV    C  N N 26  
A1IMB CAW    C  N S 27  
A1IMB OBF    O  N N 28  
A1IMB CAX    C  N N 29  
A1IMB NAY    N  N N 30  
A1IMB CAZ    C  N N 31  
A1IMB CBA    C  N N 32  
A1IMB CBB    C  N N 33  
A1IMB CBC    C  N N 34  
A1IMB NBI    N  N N 35  
A1IMB CBD    C  N N 36  
A1IMB CBE    C  N N 37  
A1IMB H1     H  N N 38  
A1IMB H2     H  N N 39  
A1IMB H3     H  N N 40  
A1IMB H4     H  N N 41  
A1IMB H6     H  N N 42  
A1IMB H7     H  N N 43  
A1IMB H8     H  N N 44  
A1IMB H9     H  N N 45  
A1IMB H10    H  N N 46  
A1IMB H11    H  N N 47  
A1IMB H12    H  N N 48  
A1IMB H13    H  N N 49  
A1IMB H14    H  N N 50  
A1IMB H15    H  N N 51  
A1IMB H16    H  N N 52  
A1IMB H17    H  N N 53  
A1IMB H18    H  N N 54  
A1IMB H19    H  N N 55  
A1IMB H20    H  N N 56  
A1IMB H21    H  N N 57  
A1IMB H22    H  N N 58  
A1IMB H23    H  N N 59  
A1IMB H24    H  N N 60  
A1IMB H26    H  N N 61  
A1IMB H27    H  N N 62  
A1IMB H28    H  N N 63  
A1IMB H29    H  N N 64  
ALA   N      N  N N 65  
ALA   CA     C  N S 66  
ALA   C      C  N N 67  
ALA   O      O  N N 68  
ALA   CB     C  N N 69  
ALA   OXT    O  N N 70  
ALA   H      H  N N 71  
ALA   H2     H  N N 72  
ALA   HA     H  N N 73  
ALA   HB1    H  N N 74  
ALA   HB2    H  N N 75  
ALA   HB3    H  N N 76  
ALA   HXT    H  N N 77  
ARG   N      N  N N 78  
ARG   CA     C  N S 79  
ARG   C      C  N N 80  
ARG   O      O  N N 81  
ARG   CB     C  N N 82  
ARG   CG     C  N N 83  
ARG   CD     C  N N 84  
ARG   NE     N  N N 85  
ARG   CZ     C  N N 86  
ARG   NH1    N  N N 87  
ARG   NH2    N  N N 88  
ARG   OXT    O  N N 89  
ARG   H      H  N N 90  
ARG   H2     H  N N 91  
ARG   HA     H  N N 92  
ARG   HB2    H  N N 93  
ARG   HB3    H  N N 94  
ARG   HG2    H  N N 95  
ARG   HG3    H  N N 96  
ARG   HD2    H  N N 97  
ARG   HD3    H  N N 98  
ARG   HE     H  N N 99  
ARG   HH11   H  N N 100 
ARG   HH12   H  N N 101 
ARG   HH21   H  N N 102 
ARG   HH22   H  N N 103 
ARG   HXT    H  N N 104 
ASN   N      N  N N 105 
ASN   CA     C  N S 106 
ASN   C      C  N N 107 
ASN   O      O  N N 108 
ASN   CB     C  N N 109 
ASN   CG     C  N N 110 
ASN   OD1    O  N N 111 
ASN   ND2    N  N N 112 
ASN   OXT    O  N N 113 
ASN   H      H  N N 114 
ASN   H2     H  N N 115 
ASN   HA     H  N N 116 
ASN   HB2    H  N N 117 
ASN   HB3    H  N N 118 
ASN   HD21   H  N N 119 
ASN   HD22   H  N N 120 
ASN   HXT    H  N N 121 
ASP   N      N  N N 122 
ASP   CA     C  N S 123 
ASP   C      C  N N 124 
ASP   O      O  N N 125 
ASP   CB     C  N N 126 
ASP   CG     C  N N 127 
ASP   OD1    O  N N 128 
ASP   OD2    O  N N 129 
ASP   OXT    O  N N 130 
ASP   H      H  N N 131 
ASP   H2     H  N N 132 
ASP   HA     H  N N 133 
ASP   HB2    H  N N 134 
ASP   HB3    H  N N 135 
ASP   HD2    H  N N 136 
ASP   HXT    H  N N 137 
CO    CO     CO N N 138 
CYS   N      N  N N 139 
CYS   CA     C  N R 140 
CYS   C      C  N N 141 
CYS   O      O  N N 142 
CYS   CB     C  N N 143 
CYS   SG     S  N N 144 
CYS   OXT    O  N N 145 
CYS   H      H  N N 146 
CYS   H2     H  N N 147 
CYS   HA     H  N N 148 
CYS   HB2    H  N N 149 
CYS   HB3    H  N N 150 
CYS   HG     H  N N 151 
CYS   HXT    H  N N 152 
GLN   N      N  N N 153 
GLN   CA     C  N S 154 
GLN   C      C  N N 155 
GLN   O      O  N N 156 
GLN   CB     C  N N 157 
GLN   CG     C  N N 158 
GLN   CD     C  N N 159 
GLN   OE1    O  N N 160 
GLN   NE2    N  N N 161 
GLN   OXT    O  N N 162 
GLN   H      H  N N 163 
GLN   H2     H  N N 164 
GLN   HA     H  N N 165 
GLN   HB2    H  N N 166 
GLN   HB3    H  N N 167 
GLN   HG2    H  N N 168 
GLN   HG3    H  N N 169 
GLN   HE21   H  N N 170 
GLN   HE22   H  N N 171 
GLN   HXT    H  N N 172 
GLU   N      N  N N 173 
GLU   CA     C  N S 174 
GLU   C      C  N N 175 
GLU   O      O  N N 176 
GLU   CB     C  N N 177 
GLU   CG     C  N N 178 
GLU   CD     C  N N 179 
GLU   OE1    O  N N 180 
GLU   OE2    O  N N 181 
GLU   OXT    O  N N 182 
GLU   H      H  N N 183 
GLU   H2     H  N N 184 
GLU   HA     H  N N 185 
GLU   HB2    H  N N 186 
GLU   HB3    H  N N 187 
GLU   HG2    H  N N 188 
GLU   HG3    H  N N 189 
GLU   HE2    H  N N 190 
GLU   HXT    H  N N 191 
GLY   N      N  N N 192 
GLY   CA     C  N N 193 
GLY   C      C  N N 194 
GLY   O      O  N N 195 
GLY   OXT    O  N N 196 
GLY   H      H  N N 197 
GLY   H2     H  N N 198 
GLY   HA2    H  N N 199 
GLY   HA3    H  N N 200 
GLY   HXT    H  N N 201 
GNP   PG     P  N N 202 
GNP   O1G    O  N N 203 
GNP   O2G    O  N N 204 
GNP   O3G    O  N N 205 
GNP   N3B    N  N N 206 
GNP   PB     P  N R 207 
GNP   O1B    O  N N 208 
GNP   O2B    O  N N 209 
GNP   O3A    O  N N 210 
GNP   PA     P  N S 211 
GNP   O1A    O  N N 212 
GNP   O2A    O  N N 213 
GNP   "O5'"  O  N N 214 
GNP   "C5'"  C  N N 215 
GNP   "C4'"  C  N R 216 
GNP   "O4'"  O  N N 217 
GNP   "C3'"  C  N S 218 
GNP   "O3'"  O  N N 219 
GNP   "C2'"  C  N R 220 
GNP   "O2'"  O  N N 221 
GNP   "C1'"  C  N R 222 
GNP   N9     N  Y N 223 
GNP   C8     C  Y N 224 
GNP   N7     N  Y N 225 
GNP   C5     C  Y N 226 
GNP   C6     C  Y N 227 
GNP   O6     O  N N 228 
GNP   N1     N  Y N 229 
GNP   C2     C  Y N 230 
GNP   N2     N  N N 231 
GNP   N3     N  Y N 232 
GNP   C4     C  Y N 233 
GNP   HOG2   H  N N 234 
GNP   HOG3   H  N N 235 
GNP   HNB3   H  N N 236 
GNP   HOB2   H  N N 237 
GNP   HOA2   H  N N 238 
GNP   "H5'2" H  N N 239 
GNP   "H5'1" H  N N 240 
GNP   "H4'"  H  N N 241 
GNP   "H3'"  H  N N 242 
GNP   "HO3'" H  N N 243 
GNP   "H2'"  H  N N 244 
GNP   "HO2'" H  N N 245 
GNP   "H1'"  H  N N 246 
GNP   H8     H  N N 247 
GNP   HN1    H  N N 248 
GNP   HN21   H  N N 249 
GNP   HN22   H  N N 250 
HIS   N      N  N N 251 
HIS   CA     C  N S 252 
HIS   C      C  N N 253 
HIS   O      O  N N 254 
HIS   CB     C  N N 255 
HIS   CG     C  Y N 256 
HIS   ND1    N  Y N 257 
HIS   CD2    C  Y N 258 
HIS   CE1    C  Y N 259 
HIS   NE2    N  Y N 260 
HIS   OXT    O  N N 261 
HIS   H      H  N N 262 
HIS   H2     H  N N 263 
HIS   HA     H  N N 264 
HIS   HB2    H  N N 265 
HIS   HB3    H  N N 266 
HIS   HD1    H  N N 267 
HIS   HD2    H  N N 268 
HIS   HE1    H  N N 269 
HIS   HE2    H  N N 270 
HIS   HXT    H  N N 271 
HOH   O      O  N N 272 
HOH   H1     H  N N 273 
HOH   H2     H  N N 274 
ILE   N      N  N N 275 
ILE   CA     C  N S 276 
ILE   C      C  N N 277 
ILE   O      O  N N 278 
ILE   CB     C  N S 279 
ILE   CG1    C  N N 280 
ILE   CG2    C  N N 281 
ILE   CD1    C  N N 282 
ILE   OXT    O  N N 283 
ILE   H      H  N N 284 
ILE   H2     H  N N 285 
ILE   HA     H  N N 286 
ILE   HB     H  N N 287 
ILE   HG12   H  N N 288 
ILE   HG13   H  N N 289 
ILE   HG21   H  N N 290 
ILE   HG22   H  N N 291 
ILE   HG23   H  N N 292 
ILE   HD11   H  N N 293 
ILE   HD12   H  N N 294 
ILE   HD13   H  N N 295 
ILE   HXT    H  N N 296 
LEU   N      N  N N 297 
LEU   CA     C  N S 298 
LEU   C      C  N N 299 
LEU   O      O  N N 300 
LEU   CB     C  N N 301 
LEU   CG     C  N N 302 
LEU   CD1    C  N N 303 
LEU   CD2    C  N N 304 
LEU   OXT    O  N N 305 
LEU   H      H  N N 306 
LEU   H2     H  N N 307 
LEU   HA     H  N N 308 
LEU   HB2    H  N N 309 
LEU   HB3    H  N N 310 
LEU   HG     H  N N 311 
LEU   HD11   H  N N 312 
LEU   HD12   H  N N 313 
LEU   HD13   H  N N 314 
LEU   HD21   H  N N 315 
LEU   HD22   H  N N 316 
LEU   HD23   H  N N 317 
LEU   HXT    H  N N 318 
LYS   N      N  N N 319 
LYS   CA     C  N S 320 
LYS   C      C  N N 321 
LYS   O      O  N N 322 
LYS   CB     C  N N 323 
LYS   CG     C  N N 324 
LYS   CD     C  N N 325 
LYS   CE     C  N N 326 
LYS   NZ     N  N N 327 
LYS   OXT    O  N N 328 
LYS   H      H  N N 329 
LYS   H2     H  N N 330 
LYS   HA     H  N N 331 
LYS   HB2    H  N N 332 
LYS   HB3    H  N N 333 
LYS   HG2    H  N N 334 
LYS   HG3    H  N N 335 
LYS   HD2    H  N N 336 
LYS   HD3    H  N N 337 
LYS   HE2    H  N N 338 
LYS   HE3    H  N N 339 
LYS   HZ1    H  N N 340 
LYS   HZ2    H  N N 341 
LYS   HZ3    H  N N 342 
LYS   HXT    H  N N 343 
MET   N      N  N N 344 
MET   CA     C  N S 345 
MET   C      C  N N 346 
MET   O      O  N N 347 
MET   CB     C  N N 348 
MET   CG     C  N N 349 
MET   SD     S  N N 350 
MET   CE     C  N N 351 
MET   OXT    O  N N 352 
MET   H      H  N N 353 
MET   H2     H  N N 354 
MET   HA     H  N N 355 
MET   HB2    H  N N 356 
MET   HB3    H  N N 357 
MET   HG2    H  N N 358 
MET   HG3    H  N N 359 
MET   HE1    H  N N 360 
MET   HE2    H  N N 361 
MET   HE3    H  N N 362 
MET   HXT    H  N N 363 
MG    MG     MG N N 364 
PHE   N      N  N N 365 
PHE   CA     C  N S 366 
PHE   C      C  N N 367 
PHE   O      O  N N 368 
PHE   CB     C  N N 369 
PHE   CG     C  Y N 370 
PHE   CD1    C  Y N 371 
PHE   CD2    C  Y N 372 
PHE   CE1    C  Y N 373 
PHE   CE2    C  Y N 374 
PHE   CZ     C  Y N 375 
PHE   OXT    O  N N 376 
PHE   H      H  N N 377 
PHE   H2     H  N N 378 
PHE   HA     H  N N 379 
PHE   HB2    H  N N 380 
PHE   HB3    H  N N 381 
PHE   HD1    H  N N 382 
PHE   HD2    H  N N 383 
PHE   HE1    H  N N 384 
PHE   HE2    H  N N 385 
PHE   HZ     H  N N 386 
PHE   HXT    H  N N 387 
PRO   N      N  N N 388 
PRO   CA     C  N S 389 
PRO   C      C  N N 390 
PRO   O      O  N N 391 
PRO   CB     C  N N 392 
PRO   CG     C  N N 393 
PRO   CD     C  N N 394 
PRO   OXT    O  N N 395 
PRO   H      H  N N 396 
PRO   HA     H  N N 397 
PRO   HB2    H  N N 398 
PRO   HB3    H  N N 399 
PRO   HG2    H  N N 400 
PRO   HG3    H  N N 401 
PRO   HD2    H  N N 402 
PRO   HD3    H  N N 403 
PRO   HXT    H  N N 404 
SER   N      N  N N 405 
SER   CA     C  N S 406 
SER   C      C  N N 407 
SER   O      O  N N 408 
SER   CB     C  N N 409 
SER   OG     O  N N 410 
SER   OXT    O  N N 411 
SER   H      H  N N 412 
SER   H2     H  N N 413 
SER   HA     H  N N 414 
SER   HB2    H  N N 415 
SER   HB3    H  N N 416 
SER   HG     H  N N 417 
SER   HXT    H  N N 418 
THR   N      N  N N 419 
THR   CA     C  N S 420 
THR   C      C  N N 421 
THR   O      O  N N 422 
THR   CB     C  N R 423 
THR   OG1    O  N N 424 
THR   CG2    C  N N 425 
THR   OXT    O  N N 426 
THR   H      H  N N 427 
THR   H2     H  N N 428 
THR   HA     H  N N 429 
THR   HB     H  N N 430 
THR   HG1    H  N N 431 
THR   HG21   H  N N 432 
THR   HG22   H  N N 433 
THR   HG23   H  N N 434 
THR   HXT    H  N N 435 
TYR   N      N  N N 436 
TYR   CA     C  N S 437 
TYR   C      C  N N 438 
TYR   O      O  N N 439 
TYR   CB     C  N N 440 
TYR   CG     C  Y N 441 
TYR   CD1    C  Y N 442 
TYR   CD2    C  Y N 443 
TYR   CE1    C  Y N 444 
TYR   CE2    C  Y N 445 
TYR   CZ     C  Y N 446 
TYR   OH     O  N N 447 
TYR   OXT    O  N N 448 
TYR   H      H  N N 449 
TYR   H2     H  N N 450 
TYR   HA     H  N N 451 
TYR   HB2    H  N N 452 
TYR   HB3    H  N N 453 
TYR   HD1    H  N N 454 
TYR   HD2    H  N N 455 
TYR   HE1    H  N N 456 
TYR   HE2    H  N N 457 
TYR   HH     H  N N 458 
TYR   HXT    H  N N 459 
VAL   N      N  N N 460 
VAL   CA     C  N S 461 
VAL   C      C  N N 462 
VAL   O      O  N N 463 
VAL   CB     C  N N 464 
VAL   CG1    C  N N 465 
VAL   CG2    C  N N 466 
VAL   OXT    O  N N 467 
VAL   H      H  N N 468 
VAL   H2     H  N N 469 
VAL   HA     H  N N 470 
VAL   HB     H  N N 471 
VAL   HG11   H  N N 472 
VAL   HG12   H  N N 473 
VAL   HG13   H  N N 474 
VAL   HG21   H  N N 475 
VAL   HG22   H  N N 476 
VAL   HG23   H  N N 477 
VAL   HXT    H  N N 478 
# 
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 
A1IMB CLAA  CAB    sing N N 1   
A1IMB OAQ   SAH    doub N N 2   
A1IMB SAO   CAC    sing N N 3   
A1IMB SAO   CAF    sing N N 4   
A1IMB CAB   CAC    sing Y N 5   
A1IMB CAB   CBJ    doub Y N 6   
A1IMB SAH   OAP    doub N N 7   
A1IMB SAH   CAI    sing N N 8   
A1IMB SAH   NAG    sing N N 9   
A1IMB CAC   CAD    doub Y N 10  
A1IMB CAJ   CAI    doub Y N 11  
A1IMB CAJ   CAK    sing Y N 12  
A1IMB CBJ   CBK    sing Y N 13  
A1IMB CAF   NAG    doub N N 14  
A1IMB CAF   NAE    sing N N 15  
A1IMB CAI   CAN    sing Y N 16  
A1IMB CAK   CAL    doub Y N 17  
A1IMB CAD   NAE    sing N N 18  
A1IMB CAD   CBG    sing Y N 19  
A1IMB NAE   CAU    sing N N 20  
A1IMB CBK   CBG    doub Y N 21  
A1IMB CAN   CAM    doub Y N 22  
A1IMB CAL   OAR    sing N N 23  
A1IMB CAL   CAM    sing Y N 24  
A1IMB CBG   OBH    sing N N 25  
A1IMB CAM   CAS    sing N N 26  
A1IMB CAU   CAV    sing N N 27  
A1IMB CAV   CAW    sing N N 28  
A1IMB CAS   OAT    doub N N 29  
A1IMB CAS   NAY    sing N N 30  
A1IMB CAW   CAX    sing N N 31  
A1IMB CAW   OBF    sing N N 32  
A1IMB CAX   NAY    sing N N 33  
A1IMB NAY   CAZ    sing N N 34  
A1IMB CAZ   CBE    sing N N 35  
A1IMB CAZ   CBA    sing N N 36  
A1IMB CBE   CBD    sing N N 37  
A1IMB CBA   CBB    sing N N 38  
A1IMB CBD   CBC    sing N N 39  
A1IMB CBB   CBC    sing N N 40  
A1IMB CBC   NBI    sing N N 41  
A1IMB CAN   H1     sing N N 42  
A1IMB OAR   H2     sing N N 43  
A1IMB CAK   H3     sing N N 44  
A1IMB CAJ   H4     sing N N 45  
A1IMB CBJ   H6     sing N N 46  
A1IMB CBK   H7     sing N N 47  
A1IMB OBH   H8     sing N N 48  
A1IMB CAU   H9     sing N N 49  
A1IMB CAU   H10    sing N N 50  
A1IMB CAV   H11    sing N N 51  
A1IMB CAV   H12    sing N N 52  
A1IMB CAW   H13    sing N N 53  
A1IMB OBF   H14    sing N N 54  
A1IMB CAX   H15    sing N N 55  
A1IMB CAX   H16    sing N N 56  
A1IMB CAZ   H17    sing N N 57  
A1IMB CBA   H18    sing N N 58  
A1IMB CBA   H19    sing N N 59  
A1IMB CBB   H20    sing N N 60  
A1IMB CBB   H21    sing N N 61  
A1IMB CBC   H22    sing N N 62  
A1IMB NBI   H23    sing N N 63  
A1IMB NBI   H24    sing N N 64  
A1IMB CBD   H26    sing N N 65  
A1IMB CBD   H27    sing N N 66  
A1IMB CBE   H28    sing N N 67  
A1IMB CBE   H29    sing N N 68  
ALA   N     CA     sing N N 69  
ALA   N     H      sing N N 70  
ALA   N     H2     sing N N 71  
ALA   CA    C      sing N N 72  
ALA   CA    CB     sing N N 73  
ALA   CA    HA     sing N N 74  
ALA   C     O      doub N N 75  
ALA   C     OXT    sing N N 76  
ALA   CB    HB1    sing N N 77  
ALA   CB    HB2    sing N N 78  
ALA   CB    HB3    sing N N 79  
ALA   OXT   HXT    sing N N 80  
ARG   N     CA     sing N N 81  
ARG   N     H      sing N N 82  
ARG   N     H2     sing N N 83  
ARG   CA    C      sing N N 84  
ARG   CA    CB     sing N N 85  
ARG   CA    HA     sing N N 86  
ARG   C     O      doub N N 87  
ARG   C     OXT    sing N N 88  
ARG   CB    CG     sing N N 89  
ARG   CB    HB2    sing N N 90  
ARG   CB    HB3    sing N N 91  
ARG   CG    CD     sing N N 92  
ARG   CG    HG2    sing N N 93  
ARG   CG    HG3    sing N N 94  
ARG   CD    NE     sing N N 95  
ARG   CD    HD2    sing N N 96  
ARG   CD    HD3    sing N N 97  
ARG   NE    CZ     sing N N 98  
ARG   NE    HE     sing N N 99  
ARG   CZ    NH1    sing N N 100 
ARG   CZ    NH2    doub N N 101 
ARG   NH1   HH11   sing N N 102 
ARG   NH1   HH12   sing N N 103 
ARG   NH2   HH21   sing N N 104 
ARG   NH2   HH22   sing N N 105 
ARG   OXT   HXT    sing N N 106 
ASN   N     CA     sing N N 107 
ASN   N     H      sing N N 108 
ASN   N     H2     sing N N 109 
ASN   CA    C      sing N N 110 
ASN   CA    CB     sing N N 111 
ASN   CA    HA     sing N N 112 
ASN   C     O      doub N N 113 
ASN   C     OXT    sing N N 114 
ASN   CB    CG     sing N N 115 
ASN   CB    HB2    sing N N 116 
ASN   CB    HB3    sing N N 117 
ASN   CG    OD1    doub N N 118 
ASN   CG    ND2    sing N N 119 
ASN   ND2   HD21   sing N N 120 
ASN   ND2   HD22   sing N N 121 
ASN   OXT   HXT    sing N N 122 
ASP   N     CA     sing N N 123 
ASP   N     H      sing N N 124 
ASP   N     H2     sing N N 125 
ASP   CA    C      sing N N 126 
ASP   CA    CB     sing N N 127 
ASP   CA    HA     sing N N 128 
ASP   C     O      doub N N 129 
ASP   C     OXT    sing N N 130 
ASP   CB    CG     sing N N 131 
ASP   CB    HB2    sing N N 132 
ASP   CB    HB3    sing N N 133 
ASP   CG    OD1    doub N N 134 
ASP   CG    OD2    sing N N 135 
ASP   OD2   HD2    sing N N 136 
ASP   OXT   HXT    sing N N 137 
CYS   N     CA     sing N N 138 
CYS   N     H      sing N N 139 
CYS   N     H2     sing N N 140 
CYS   CA    C      sing N N 141 
CYS   CA    CB     sing N N 142 
CYS   CA    HA     sing N N 143 
CYS   C     O      doub N N 144 
CYS   C     OXT    sing N N 145 
CYS   CB    SG     sing N N 146 
CYS   CB    HB2    sing N N 147 
CYS   CB    HB3    sing N N 148 
CYS   SG    HG     sing N N 149 
CYS   OXT   HXT    sing N N 150 
GLN   N     CA     sing N N 151 
GLN   N     H      sing N N 152 
GLN   N     H2     sing N N 153 
GLN   CA    C      sing N N 154 
GLN   CA    CB     sing N N 155 
GLN   CA    HA     sing N N 156 
GLN   C     O      doub N N 157 
GLN   C     OXT    sing N N 158 
GLN   CB    CG     sing N N 159 
GLN   CB    HB2    sing N N 160 
GLN   CB    HB3    sing N N 161 
GLN   CG    CD     sing N N 162 
GLN   CG    HG2    sing N N 163 
GLN   CG    HG3    sing N N 164 
GLN   CD    OE1    doub N N 165 
GLN   CD    NE2    sing N N 166 
GLN   NE2   HE21   sing N N 167 
GLN   NE2   HE22   sing N N 168 
GLN   OXT   HXT    sing N N 169 
GLU   N     CA     sing N N 170 
GLU   N     H      sing N N 171 
GLU   N     H2     sing N N 172 
GLU   CA    C      sing N N 173 
GLU   CA    CB     sing N N 174 
GLU   CA    HA     sing N N 175 
GLU   C     O      doub N N 176 
GLU   C     OXT    sing N N 177 
GLU   CB    CG     sing N N 178 
GLU   CB    HB2    sing N N 179 
GLU   CB    HB3    sing N N 180 
GLU   CG    CD     sing N N 181 
GLU   CG    HG2    sing N N 182 
GLU   CG    HG3    sing N N 183 
GLU   CD    OE1    doub N N 184 
GLU   CD    OE2    sing N N 185 
GLU   OE2   HE2    sing N N 186 
GLU   OXT   HXT    sing N N 187 
GLY   N     CA     sing N N 188 
GLY   N     H      sing N N 189 
GLY   N     H2     sing N N 190 
GLY   CA    C      sing N N 191 
GLY   CA    HA2    sing N N 192 
GLY   CA    HA3    sing N N 193 
GLY   C     O      doub N N 194 
GLY   C     OXT    sing N N 195 
GLY   OXT   HXT    sing N N 196 
GNP   PG    O1G    doub N N 197 
GNP   PG    O2G    sing N N 198 
GNP   PG    O3G    sing N N 199 
GNP   PG    N3B    sing N N 200 
GNP   O2G   HOG2   sing N N 201 
GNP   O3G   HOG3   sing N N 202 
GNP   N3B   PB     sing N N 203 
GNP   N3B   HNB3   sing N N 204 
GNP   PB    O1B    doub N N 205 
GNP   PB    O2B    sing N N 206 
GNP   PB    O3A    sing N N 207 
GNP   O2B   HOB2   sing N N 208 
GNP   O3A   PA     sing N N 209 
GNP   PA    O1A    doub N N 210 
GNP   PA    O2A    sing N N 211 
GNP   PA    "O5'"  sing N N 212 
GNP   O2A   HOA2   sing N N 213 
GNP   "O5'" "C5'"  sing N N 214 
GNP   "C5'" "C4'"  sing N N 215 
GNP   "C5'" "H5'2" sing N N 216 
GNP   "C5'" "H5'1" sing N N 217 
GNP   "C4'" "O4'"  sing N N 218 
GNP   "C4'" "C3'"  sing N N 219 
GNP   "C4'" "H4'"  sing N N 220 
GNP   "O4'" "C1'"  sing N N 221 
GNP   "C3'" "O3'"  sing N N 222 
GNP   "C3'" "C2'"  sing N N 223 
GNP   "C3'" "H3'"  sing N N 224 
GNP   "O3'" "HO3'" sing N N 225 
GNP   "C2'" "O2'"  sing N N 226 
GNP   "C2'" "C1'"  sing N N 227 
GNP   "C2'" "H2'"  sing N N 228 
GNP   "O2'" "HO2'" sing N N 229 
GNP   "C1'" N9     sing N N 230 
GNP   "C1'" "H1'"  sing N N 231 
GNP   N9    C8     sing Y N 232 
GNP   N9    C4     sing Y N 233 
GNP   C8    N7     doub Y N 234 
GNP   C8    H8     sing N N 235 
GNP   N7    C5     sing Y N 236 
GNP   C5    C6     sing Y N 237 
GNP   C5    C4     doub Y N 238 
GNP   C6    O6     doub N N 239 
GNP   C6    N1     sing Y N 240 
GNP   N1    C2     sing Y N 241 
GNP   N1    HN1    sing N N 242 
GNP   C2    N2     sing N N 243 
GNP   C2    N3     doub Y N 244 
GNP   N2    HN21   sing N N 245 
GNP   N2    HN22   sing N N 246 
GNP   N3    C4     sing Y N 247 
HIS   N     CA     sing N N 248 
HIS   N     H      sing N N 249 
HIS   N     H2     sing N N 250 
HIS   CA    C      sing N N 251 
HIS   CA    CB     sing N N 252 
HIS   CA    HA     sing N N 253 
HIS   C     O      doub N N 254 
HIS   C     OXT    sing N N 255 
HIS   CB    CG     sing N N 256 
HIS   CB    HB2    sing N N 257 
HIS   CB    HB3    sing N N 258 
HIS   CG    ND1    sing Y N 259 
HIS   CG    CD2    doub Y N 260 
HIS   ND1   CE1    doub Y N 261 
HIS   ND1   HD1    sing N N 262 
HIS   CD2   NE2    sing Y N 263 
HIS   CD2   HD2    sing N N 264 
HIS   CE1   NE2    sing Y N 265 
HIS   CE1   HE1    sing N N 266 
HIS   NE2   HE2    sing N N 267 
HIS   OXT   HXT    sing N N 268 
HOH   O     H1     sing N N 269 
HOH   O     H2     sing N N 270 
ILE   N     CA     sing N N 271 
ILE   N     H      sing N N 272 
ILE   N     H2     sing N N 273 
ILE   CA    C      sing N N 274 
ILE   CA    CB     sing N N 275 
ILE   CA    HA     sing N N 276 
ILE   C     O      doub N N 277 
ILE   C     OXT    sing N N 278 
ILE   CB    CG1    sing N N 279 
ILE   CB    CG2    sing N N 280 
ILE   CB    HB     sing N N 281 
ILE   CG1   CD1    sing N N 282 
ILE   CG1   HG12   sing N N 283 
ILE   CG1   HG13   sing N N 284 
ILE   CG2   HG21   sing N N 285 
ILE   CG2   HG22   sing N N 286 
ILE   CG2   HG23   sing N N 287 
ILE   CD1   HD11   sing N N 288 
ILE   CD1   HD12   sing N N 289 
ILE   CD1   HD13   sing N N 290 
ILE   OXT   HXT    sing N N 291 
LEU   N     CA     sing N N 292 
LEU   N     H      sing N N 293 
LEU   N     H2     sing N N 294 
LEU   CA    C      sing N N 295 
LEU   CA    CB     sing N N 296 
LEU   CA    HA     sing N N 297 
LEU   C     O      doub N N 298 
LEU   C     OXT    sing N N 299 
LEU   CB    CG     sing N N 300 
LEU   CB    HB2    sing N N 301 
LEU   CB    HB3    sing N N 302 
LEU   CG    CD1    sing N N 303 
LEU   CG    CD2    sing N N 304 
LEU   CG    HG     sing N N 305 
LEU   CD1   HD11   sing N N 306 
LEU   CD1   HD12   sing N N 307 
LEU   CD1   HD13   sing N N 308 
LEU   CD2   HD21   sing N N 309 
LEU   CD2   HD22   sing N N 310 
LEU   CD2   HD23   sing N N 311 
LEU   OXT   HXT    sing N N 312 
LYS   N     CA     sing N N 313 
LYS   N     H      sing N N 314 
LYS   N     H2     sing N N 315 
LYS   CA    C      sing N N 316 
LYS   CA    CB     sing N N 317 
LYS   CA    HA     sing N N 318 
LYS   C     O      doub N N 319 
LYS   C     OXT    sing N N 320 
LYS   CB    CG     sing N N 321 
LYS   CB    HB2    sing N N 322 
LYS   CB    HB3    sing N N 323 
LYS   CG    CD     sing N N 324 
LYS   CG    HG2    sing N N 325 
LYS   CG    HG3    sing N N 326 
LYS   CD    CE     sing N N 327 
LYS   CD    HD2    sing N N 328 
LYS   CD    HD3    sing N N 329 
LYS   CE    NZ     sing N N 330 
LYS   CE    HE2    sing N N 331 
LYS   CE    HE3    sing N N 332 
LYS   NZ    HZ1    sing N N 333 
LYS   NZ    HZ2    sing N N 334 
LYS   NZ    HZ3    sing N N 335 
LYS   OXT   HXT    sing N N 336 
MET   N     CA     sing N N 337 
MET   N     H      sing N N 338 
MET   N     H2     sing N N 339 
MET   CA    C      sing N N 340 
MET   CA    CB     sing N N 341 
MET   CA    HA     sing N N 342 
MET   C     O      doub N N 343 
MET   C     OXT    sing N N 344 
MET   CB    CG     sing N N 345 
MET   CB    HB2    sing N N 346 
MET   CB    HB3    sing N N 347 
MET   CG    SD     sing N N 348 
MET   CG    HG2    sing N N 349 
MET   CG    HG3    sing N N 350 
MET   SD    CE     sing N N 351 
MET   CE    HE1    sing N N 352 
MET   CE    HE2    sing N N 353 
MET   CE    HE3    sing N N 354 
MET   OXT   HXT    sing N N 355 
PHE   N     CA     sing N N 356 
PHE   N     H      sing N N 357 
PHE   N     H2     sing N N 358 
PHE   CA    C      sing N N 359 
PHE   CA    CB     sing N N 360 
PHE   CA    HA     sing N N 361 
PHE   C     O      doub N N 362 
PHE   C     OXT    sing N N 363 
PHE   CB    CG     sing N N 364 
PHE   CB    HB2    sing N N 365 
PHE   CB    HB3    sing N N 366 
PHE   CG    CD1    doub Y N 367 
PHE   CG    CD2    sing Y N 368 
PHE   CD1   CE1    sing Y N 369 
PHE   CD1   HD1    sing N N 370 
PHE   CD2   CE2    doub Y N 371 
PHE   CD2   HD2    sing N N 372 
PHE   CE1   CZ     doub Y N 373 
PHE   CE1   HE1    sing N N 374 
PHE   CE2   CZ     sing Y N 375 
PHE   CE2   HE2    sing N N 376 
PHE   CZ    HZ     sing N N 377 
PHE   OXT   HXT    sing N N 378 
PRO   N     CA     sing N N 379 
PRO   N     CD     sing N N 380 
PRO   N     H      sing N N 381 
PRO   CA    C      sing N N 382 
PRO   CA    CB     sing N N 383 
PRO   CA    HA     sing N N 384 
PRO   C     O      doub N N 385 
PRO   C     OXT    sing N N 386 
PRO   CB    CG     sing N N 387 
PRO   CB    HB2    sing N N 388 
PRO   CB    HB3    sing N N 389 
PRO   CG    CD     sing N N 390 
PRO   CG    HG2    sing N N 391 
PRO   CG    HG3    sing N N 392 
PRO   CD    HD2    sing N N 393 
PRO   CD    HD3    sing N N 394 
PRO   OXT   HXT    sing N N 395 
SER   N     CA     sing N N 396 
SER   N     H      sing N N 397 
SER   N     H2     sing N N 398 
SER   CA    C      sing N N 399 
SER   CA    CB     sing N N 400 
SER   CA    HA     sing N N 401 
SER   C     O      doub N N 402 
SER   C     OXT    sing N N 403 
SER   CB    OG     sing N N 404 
SER   CB    HB2    sing N N 405 
SER   CB    HB3    sing N N 406 
SER   OG    HG     sing N N 407 
SER   OXT   HXT    sing N N 408 
THR   N     CA     sing N N 409 
THR   N     H      sing N N 410 
THR   N     H2     sing N N 411 
THR   CA    C      sing N N 412 
THR   CA    CB     sing N N 413 
THR   CA    HA     sing N N 414 
THR   C     O      doub N N 415 
THR   C     OXT    sing N N 416 
THR   CB    OG1    sing N N 417 
THR   CB    CG2    sing N N 418 
THR   CB    HB     sing N N 419 
THR   OG1   HG1    sing N N 420 
THR   CG2   HG21   sing N N 421 
THR   CG2   HG22   sing N N 422 
THR   CG2   HG23   sing N N 423 
THR   OXT   HXT    sing N N 424 
TYR   N     CA     sing N N 425 
TYR   N     H      sing N N 426 
TYR   N     H2     sing N N 427 
TYR   CA    C      sing N N 428 
TYR   CA    CB     sing N N 429 
TYR   CA    HA     sing N N 430 
TYR   C     O      doub N N 431 
TYR   C     OXT    sing N N 432 
TYR   CB    CG     sing N N 433 
TYR   CB    HB2    sing N N 434 
TYR   CB    HB3    sing N N 435 
TYR   CG    CD1    doub Y N 436 
TYR   CG    CD2    sing Y N 437 
TYR   CD1   CE1    sing Y N 438 
TYR   CD1   HD1    sing N N 439 
TYR   CD2   CE2    doub Y N 440 
TYR   CD2   HD2    sing N N 441 
TYR   CE1   CZ     doub Y N 442 
TYR   CE1   HE1    sing N N 443 
TYR   CE2   CZ     sing Y N 444 
TYR   CE2   HE2    sing N N 445 
TYR   CZ    OH     sing N N 446 
TYR   OH    HH     sing N N 447 
TYR   OXT   HXT    sing N N 448 
VAL   N     CA     sing N N 449 
VAL   N     H      sing N N 450 
VAL   N     H2     sing N N 451 
VAL   CA    C      sing N N 452 
VAL   CA    CB     sing N N 453 
VAL   CA    HA     sing N N 454 
VAL   C     O      doub N N 455 
VAL   C     OXT    sing N N 456 
VAL   CB    CG1    sing N N 457 
VAL   CB    CG2    sing N N 458 
VAL   CB    HB     sing N N 459 
VAL   CG1   HG11   sing N N 460 
VAL   CG1   HG12   sing N N 461 
VAL   CG1   HG13   sing N N 462 
VAL   CG2   HG21   sing N N 463 
VAL   CG2   HG22   sing N N 464 
VAL   CG2   HG23   sing N N 465 
VAL   OXT   HXT    sing N N 466 
# 
_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                    9GGX 
_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]   0.013978 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.005025 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.029205 
_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]   0.015230 
_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   ? 6.934  2.123   24.120 1.00 38.16 ? 1   MET   A N     1 
ATOM   2    C  CA    . MET   A 1 4   ? 8.190  2.915   24.098 1.00 36.12 ? 1   MET   A CA    1 
ATOM   3    C  C     . MET   A 1 4   ? 9.053  2.430   22.929 1.00 31.39 ? 1   MET   A C     1 
ATOM   4    O  O     . MET   A 1 4   ? 9.138  1.255   22.733 1.00 34.91 ? 1   MET   A O     1 
ATOM   5    C  CB    . MET   A 1 4   ? 9.003  2.703   25.373 1.00 38.04 ? 1   MET   A CB    1 
ATOM   6    C  CG    . MET   A 1 4   ? 10.236 3.556   25.464 1.00 31.99 ? 1   MET   A CG    1 
ATOM   7    S  SD    . MET   A 1 4   ? 11.202 2.976   26.843 1.00 35.57 ? 1   MET   A SD    1 
ATOM   8    C  CE    . MET   A 1 4   ? 10.086 3.366   28.191 1.00 35.99 ? 1   MET   A CE    1 
ATOM   9    N  N     . THR   A 1 5   ? 9.651  3.365   22.226 1.00 29.45 ? 2   THR   A N     1 
ATOM   10   C  CA    . THR   A 1 5   ? 10.438 2.947   21.045 1.00 28.44 ? 2   THR   A CA    1 
ATOM   11   C  C     . THR   A 1 5   ? 11.664 2.153   21.466 1.00 25.83 ? 2   THR   A C     1 
ATOM   12   O  O     . THR   A 1 5   ? 12.424 2.635   22.276 1.00 28.22 ? 2   THR   A O     1 
ATOM   13   C  CB    . THR   A 1 5   ? 10.750 4.151   20.165 1.00 34.14 ? 2   THR   A CB    1 
ATOM   14   O  OG1   . THR   A 1 5   ? 9.506  4.709   19.786 1.00 32.93 ? 2   THR   A OG1   1 
ATOM   15   C  CG2   . THR   A 1 5   ? 11.490 3.761   18.913 1.00 35.67 ? 2   THR   A CG2   1 
ATOM   16   N  N     . GLU   A 1 6   ? 11.843 1.017   20.799 1.00 25.94 ? 3   GLU   A N     1 
ATOM   17   C  CA    . GLU   A 1 6   ? 12.960 0.087   21.004 1.00 22.64 ? 3   GLU   A CA    1 
ATOM   18   C  C     . GLU   A 1 6   ? 13.809 0.036   19.717 1.00 23.24 ? 3   GLU   A C     1 
ATOM   19   O  O     . GLU   A 1 6   ? 13.242 0.013   18.652 1.00 28.42 ? 3   GLU   A O     1 
ATOM   20   C  CB    . GLU   A 1 6   ? 12.316 -1.271  21.181 1.00 29.11 ? 3   GLU   A CB    1 
ATOM   21   C  CG    . GLU   A 1 6   ? 13.185 -2.304  21.811 1.00 32.67 ? 3   GLU   A CG    1 
ATOM   22   C  CD    . GLU   A 1 6   ? 12.308 -3.233  22.639 1.00 34.34 ? 3   GLU   A CD    1 
ATOM   23   O  OE1   . GLU   A 1 6   ? 11.308 -2.777  23.108 1.00 42.25 ? 3   GLU   A OE1   1 
ATOM   24   O  OE2   . GLU   A 1 6   ? 12.636 -4.374  22.778 1.00 40.31 ? 3   GLU   A OE2   1 
ATOM   25   N  N     . TYR   A 1 7   ? 15.117 0.058   19.875 1.00 20.84 ? 4   TYR   A N     1 
ATOM   26   C  CA    . TYR   A 1 7   ? 16.080 -0.055  18.742 1.00 19.95 ? 4   TYR   A CA    1 
ATOM   27   C  C     . TYR   A 1 7   ? 17.006 -1.218  19.053 1.00 19.89 ? 4   TYR   A C     1 
ATOM   28   O  O     . TYR   A 1 7   ? 17.656 -1.268  20.089 1.00 20.73 ? 4   TYR   A O     1 
ATOM   29   C  CB    . TYR   A 1 7   ? 16.909 1.212   18.646 1.00 20.15 ? 4   TYR   A CB    1 
ATOM   30   C  CG    . TYR   A 1 7   ? 16.134 2.457   18.343 1.00 20.19 ? 4   TYR   A CG    1 
ATOM   31   C  CD1   . TYR   A 1 7   ? 15.549 2.643   17.116 1.00 24.67 ? 4   TYR   A CD1   1 
ATOM   32   C  CD2   . TYR   A 1 7   ? 15.949 3.440   19.302 1.00 20.58 ? 4   TYR   A CD2   1 
ATOM   33   C  CE1   . TYR   A 1 7   ? 14.818 3.769   16.831 1.00 26.60 ? 4   TYR   A CE1   1 
ATOM   34   C  CE2   . TYR   A 1 7   ? 15.222 4.576   19.028 1.00 23.02 ? 4   TYR   A CE2   1 
ATOM   35   C  CZ    . TYR   A 1 7   ? 14.656 4.744   17.782 1.00 22.67 ? 4   TYR   A CZ    1 
ATOM   36   O  OH    . TYR   A 1 7   ? 13.951 5.831   17.444 1.00 26.23 ? 4   TYR   A OH    1 
ATOM   37   N  N     . LYS   A 1 8   ? 17.052 -2.152  18.126 1.00 18.74 ? 5   LYS   A N     1 
ATOM   38   C  CA    . LYS   A 1 8   ? 17.973 -3.312  18.171 1.00 19.24 ? 5   LYS   A CA    1 
ATOM   39   C  C     . LYS   A 1 8   ? 19.294 -2.912  17.489 1.00 17.00 ? 5   LYS   A C     1 
ATOM   40   O  O     . LYS   A 1 8   ? 19.300 -2.706  16.278 1.00 18.32 ? 5   LYS   A O     1 
ATOM   41   C  CB    . LYS   A 1 8   ? 17.296 -4.526  17.530 1.00 21.43 ? 5   LYS   A CB    1 
ATOM   42   C  CG    . LYS   A 1 8   ? 16.064 -5.002  18.299 1.00 26.70 ? 5   LYS   A CG    1 
ATOM   43   C  CD    . LYS   A 1 8   ? 15.402 -6.296  17.899 1.00 32.99 ? 5   LYS   A CD    1 
ATOM   44   C  CE    . LYS   A 1 8   ? 14.191 -6.599  18.769 1.00 38.05 ? 5   LYS   A CE    1 
ATOM   45   N  NZ    . LYS   A 1 8   ? 14.451 -6.364  20.208 1.00 41.25 ? 5   LYS   A NZ    1 
ATOM   46   N  N     . LEU   A 1 9   ? 20.353 -2.752  18.277 1.00 16.29 ? 6   LEU   A N     1 
ATOM   47   C  CA    . LEU   A 1 9   ? 21.653 -2.342  17.772 1.00 15.25 ? 6   LEU   A CA    1 
ATOM   48   C  C     . LEU   A 1 9   ? 22.577 -3.551  17.842 1.00 17.12 ? 6   LEU   A C     1 
ATOM   49   O  O     . LEU   A 1 9   ? 22.499 -4.362  18.765 1.00 16.63 ? 6   LEU   A O     1 
ATOM   50   C  CB    . LEU   A 1 9   ? 22.255 -1.234  18.650 1.00 17.72 ? 6   LEU   A CB    1 
ATOM   51   C  CG    . LEU   A 1 9   ? 21.394 -0.003  18.949 1.00 22.20 ? 6   LEU   A CG    1 
ATOM   52   C  CD1   . LEU   A 1 9   ? 22.231 1.090   19.599 1.00 22.23 ? 6   LEU   A CD1   1 
ATOM   53   C  CD2   . LEU   A 1 9   ? 20.755 0.541   17.684 1.00 22.74 ? 6   LEU   A CD2   1 
ATOM   54   N  N     . VAL   A 1 10  ? 23.481 -3.645  16.864 1.00 16.53 ? 7   VAL   A N     1 
ATOM   55   C  CA    . VAL   A 1 10  ? 24.433 -4.755  16.825 1.00 15.99 ? 7   VAL   A CA    1 
ATOM   56   C  C     . VAL   A 1 10  ? 25.844 -4.196  16.667 1.00 16.17 ? 7   VAL   A C     1 
ATOM   57   O  O     . VAL   A 1 10  ? 26.059 -3.368  15.779 1.00 18.46 ? 7   VAL   A O     1 
ATOM   58   C  CB    . VAL   A 1 10  ? 24.137 -5.734  15.676 1.00 17.95 ? 7   VAL   A CB    1 
ATOM   59   C  CG1   . VAL   A 1 10  ? 25.017 -6.969  15.784 1.00 19.21 ? 7   VAL   A CG1   1 
ATOM   60   C  CG2   . VAL   A 1 10  ? 22.680 -6.162  15.668 1.00 20.07 ? 7   VAL   A CG2   1 
ATOM   61   N  N     . VAL   A 1 11  ? 26.774 -4.657  17.525 1.00 14.94 ? 8   VAL   A N     1 
ATOM   62   C  CA    . VAL   A 1 11  ? 28.160 -4.217  17.412 1.00 16.39 ? 8   VAL   A CA    1 
ATOM   63   C  C     . VAL   A 1 11  ? 28.933 -5.357  16.757 1.00 16.98 ? 8   VAL   A C     1 
ATOM   64   O  O     . VAL   A 1 11  ? 28.966 -6.477  17.294 1.00 17.21 ? 8   VAL   A O     1 
ATOM   65   C  CB    . VAL   A 1 11  ? 28.764 -3.865  18.788 1.00 16.02 ? 8   VAL   A CB    1 
ATOM   66   C  CG1   . VAL   A 1 11  ? 30.166 -3.293  18.684 1.00 17.53 ? 8   VAL   A CG1   1 
ATOM   67   C  CG2   . VAL   A 1 11  ? 27.889 -2.907  19.594 1.00 17.47 ? 8   VAL   A CG2   1 
ATOM   68   N  N     . VAL   A 1 12  ? 29.520 -5.085  15.577 1.00 16.24 ? 9   VAL   A N     1 
ATOM   69   C  CA    . VAL   A 1 12  ? 30.194 -6.132  14.802 1.00 17.74 ? 9   VAL   A CA    1 
ATOM   70   C  C     . VAL   A 1 12  ? 31.601 -5.664  14.453 1.00 17.07 ? 9   VAL   A C     1 
ATOM   71   O  O     . VAL   A 1 12  ? 31.882 -4.467  14.442 1.00 16.44 ? 9   VAL   A O     1 
ATOM   72   C  CB    . VAL   A 1 12  ? 29.459 -6.485  13.490 1.00 18.29 ? 9   VAL   A CB    1 
ATOM   73   C  CG1   . VAL   A 1 12  ? 28.039 -6.922  13.771 1.00 19.38 ? 9   VAL   A CG1   1 
ATOM   74   C  CG2   . VAL   A 1 12  ? 29.460 -5.324  12.498 1.00 20.20 ? 9   VAL   A CG2   1 
ATOM   75   N  N     . GLY   A 1 13  ? 32.454 -6.634  14.129 1.00 16.42 ? 10  GLY   A N     1 
ATOM   76   C  CA    . GLY   A 1 13  ? 33.821 -6.327  13.722 1.00 17.61 ? 10  GLY   A CA    1 
ATOM   77   C  C     . GLY   A 1 13  ? 34.729 -7.522  13.938 1.00 17.98 ? 10  GLY   A C     1 
ATOM   78   O  O     . GLY   A 1 13  ? 34.318 -8.536  14.491 1.00 18.58 ? 10  GLY   A O     1 
ATOM   79   N  N     . ALA   A 1 14  ? 35.972 -7.366  13.482 1.00 17.62 ? 11  ALA   A N     1 
ATOM   80   C  CA    . ALA   A 1 14  ? 36.982 -8.417  13.646 1.00 18.56 ? 11  ALA   A CA    1 
ATOM   81   C  C     . ALA   A 1 14  ? 37.339 -8.627  15.125 1.00 19.96 ? 11  ALA   A C     1 
ATOM   82   O  O     . ALA   A 1 14  ? 37.182 -7.714  15.912 1.00 19.66 ? 11  ALA   A O     1 
ATOM   83   C  CB    . ALA   A 1 14  ? 38.240 -8.027  12.911 1.00 19.23 ? 11  ALA   A CB    1 
ATOM   84   N  N     . GLY   A 1 15  ? 37.963 -9.747  15.391 1.00 20.56 ? 12  GLY   A N     1 
ATOM   85   C  CA    . GLY   A 1 15  ? 38.390 -10.081 16.753 1.00 21.42 ? 12  GLY   A CA    1 
ATOM   86   C  C     . GLY   A 1 15  ? 39.290 -9.030  17.347 1.00 21.38 ? 12  GLY   A C     1 
ATOM   87   O  O     . GLY   A 1 15  ? 40.161 -8.537  16.674 1.00 21.27 ? 12  GLY   A O     1 
ATOM   88   N  N     . GLY   A 1 16  ? 39.047 -8.674  18.621 1.00 20.51 ? 13  GLY   A N     1 
ATOM   89   C  CA    . GLY   A 1 16  ? 39.927 -7.787  19.393 1.00 23.90 ? 13  GLY   A CA    1 
ATOM   90   C  C     . GLY   A 1 16  ? 39.876 -6.327  19.060 1.00 21.08 ? 13  GLY   A C     1 
ATOM   91   O  O     . GLY   A 1 16  ? 40.689 -5.636  19.510 1.00 23.66 ? 13  GLY   A O     1 
ATOM   92   N  N     . VAL   A 1 17  ? 38.908 -5.876  18.280 1.00 20.35 ? 14  VAL   A N     1 
ATOM   93   C  CA    . VAL   A 1 17  ? 38.873 -4.466  17.933 1.00 18.46 ? 14  VAL   A CA    1 
ATOM   94   C  C     . VAL   A 1 17  ? 38.325 -3.591  19.054 1.00 19.14 ? 14  VAL   A C     1 
ATOM   95   O  O     . VAL   A 1 17  ? 38.473 -2.357  18.962 1.00 18.74 ? 14  VAL   A O     1 
ATOM   96   C  CB    . VAL   A 1 17  ? 38.100 -4.199  16.622 1.00 18.35 ? 14  VAL   A CB    1 
ATOM   97   C  CG1   . VAL   A 1 17  ? 38.803 -4.836  15.424 1.00 18.21 ? 14  VAL   A CG1   1 
ATOM   98   C  CG2   . VAL   A 1 17  ? 36.628 -4.596  16.688 1.00 18.51 ? 14  VAL   A CG2   1 
ATOM   99   N  N     . GLY   A 1 18  ? 37.606 -4.217  20.009 1.00 18.52 ? 15  GLY   A N     1 
ATOM   100  C  CA    . GLY   A 1 18  ? 37.048 -3.452  21.116 1.00 16.88 ? 15  GLY   A CA    1 
ATOM   101  C  C     . GLY   A 1 18  ? 35.517 -3.345  21.113 1.00 18.59 ? 15  GLY   A C     1 
ATOM   102  O  O     . GLY   A 1 18  ? 34.959 -2.395  21.682 1.00 17.82 ? 15  GLY   A O     1 
ATOM   103  N  N     . LYS   A 1 19  ? 34.825 -4.303  20.464 1.00 16.67 ? 16  LYS   A N     1 
ATOM   104  C  CA    . LYS   A 1 19  ? 33.360 -4.332  20.423 1.00 16.30 ? 16  LYS   A CA    1 
ATOM   105  C  C     . LYS   A 1 19  ? 32.800 -4.382  21.848 1.00 18.01 ? 16  LYS   A C     1 
ATOM   106  O  O     . LYS   A 1 19  ? 31.967 -3.565  22.202 1.00 17.79 ? 16  LYS   A O     1 
ATOM   107  C  CB    . LYS   A 1 19  ? 32.897 -5.566  19.636 1.00 16.49 ? 16  LYS   A CB    1 
ATOM   108  C  CG    . LYS   A 1 19  ? 33.371 -5.623  18.177 1.00 18.17 ? 16  LYS   A CG    1 
ATOM   109  C  CD    . LYS   A 1 19  ? 33.001 -6.898  17.448 1.00 18.52 ? 16  LYS   A CD    1 
ATOM   110  C  CE    . LYS   A 1 19  ? 33.589 -8.160  18.049 1.00 18.69 ? 16  LYS   A CE    1 
ATOM   111  N  NZ    . LYS   A 1 19  ? 35.074 -8.128  17.904 1.00 19.63 ? 16  LYS   A NZ    1 
ATOM   112  N  N     . SER   A 1 20  ? 33.361 -5.288  22.679 1.00 17.49 ? 17  SER   A N     1 
ATOM   113  C  CA    . SER   A 1 20  ? 32.879 -5.476  24.041 1.00 17.82 ? 17  SER   A CA    1 
ATOM   114  C  C     . SER   A 1 20  ? 33.217 -4.250  24.883 1.00 19.12 ? 17  SER   A C     1 
ATOM   115  O  O     . SER   A 1 20  ? 32.362 -3.784  25.639 1.00 18.95 ? 17  SER   A O     1 
ATOM   116  C  CB    . SER   A 1 20  ? 33.435 -6.750  24.633 1.00 17.92 ? 17  SER   A CB    1 
ATOM   117  O  OG    . SER   A 1 20  ? 32.969 -7.919  23.954 1.00 19.10 ? 17  SER   A OG    1 
ATOM   118  N  N     . ALA   A 1 21  ? 34.439 -3.723  24.734 1.00 17.20 ? 18  ALA   A N     1 
ATOM   119  C  CA    . ALA   A 1 21  ? 34.848 -2.542  25.494 1.00 17.75 ? 18  ALA   A CA    1 
ATOM   120  C  C     . ALA   A 1 21  ? 33.997 -1.310  25.187 1.00 18.32 ? 18  ALA   A C     1 
ATOM   121  O  O     . ALA   A 1 21  ? 33.607 -0.591  26.100 1.00 17.82 ? 18  ALA   A O     1 
ATOM   122  C  CB    . ALA   A 1 21  ? 36.319 -2.273  25.316 1.00 19.09 ? 18  ALA   A CB    1 
ATOM   123  N  N     . LEU   A 1 22  ? 33.584 -1.112  23.927 1.00 17.12 ? 19  LEU   A N     1 
ATOM   124  C  CA    . LEU   A 1 22  ? 32.696 -0.019  23.575 1.00 18.50 ? 19  LEU   A CA    1 
ATOM   125  C  C     . LEU   A 1 22  ? 31.332 -0.225  24.222 1.00 18.13 ? 19  LEU   A C     1 
ATOM   126  O  O     . LEU   A 1 22  ? 30.810 0.692   24.819 1.00 17.60 ? 19  LEU   A O     1 
ATOM   127  C  CB    . LEU   A 1 22  ? 32.593 0.043   22.045 1.00 18.62 ? 19  LEU   A CB    1 
ATOM   128  C  CG    . LEU   A 1 22  ? 33.799 0.665   21.357 1.00 18.44 ? 19  LEU   A CG    1 
ATOM   129  C  CD1   . LEU   A 1 22  ? 33.614 0.516   19.867 1.00 21.23 ? 19  LEU   A CD1   1 
ATOM   130  C  CD2   . LEU   A 1 22  ? 33.923 2.135   21.703 1.00 19.81 ? 19  LEU   A CD2   1 
ATOM   131  N  N     . THR   A 1 23  ? 30.818 -1.423  24.126 1.00 17.57 ? 20  THR   A N     1 
ATOM   132  C  CA    . THR   A 1 23  ? 29.476 -1.752  24.696 1.00 18.03 ? 20  THR   A CA    1 
ATOM   133  C  C     . THR   A 1 23  ? 29.465 -1.602  26.238 1.00 19.06 ? 20  THR   A C     1 
ATOM   134  O  O     . THR   A 1 23  ? 28.634 -0.912  26.735 1.00 19.36 ? 20  THR   A O     1 
ATOM   135  C  CB    . THR   A 1 23  ? 29.063 -3.170  24.308 1.00 17.51 ? 20  THR   A CB    1 
ATOM   136  O  OG1   . THR   A 1 23  ? 29.140 -3.305  22.878 1.00 18.16 ? 20  THR   A OG1   1 
ATOM   137  C  CG2   . THR   A 1 23  ? 27.656 -3.497  24.763 1.00 19.29 ? 20  THR   A CG2   1 
ATOM   138  N  N     . ILE   A 1 24  ? 30.458 -2.166  26.864 1.00 18.78 ? 21  ILE   A N     1 
ATOM   139  C  CA    . ILE   A 1 24  ? 30.554 -2.073  28.363 1.00 19.37 ? 21  ILE   A CA    1 
ATOM   140  C  C     . ILE   A 1 24  ? 30.765 -0.614  28.777 1.00 19.02 ? 21  ILE   A C     1 
ATOM   141  O  O     . ILE   A 1 24  ? 30.253 -0.204  29.856 1.00 19.77 ? 21  ILE   A O     1 
ATOM   142  C  CB    . ILE   A 1 24  ? 31.592 -3.055  28.892 1.00 21.03 ? 21  ILE   A CB    1 
ATOM   143  C  CG1   . ILE   A 1 24  ? 31.181 -4.513  28.705 1.00 24.16 ? 21  ILE   A CG1   1 
ATOM   144  C  CG2   . ILE   A 1 24  ? 31.842 -2.808  30.378 1.00 21.43 ? 21  ILE   A CG2   1 
ATOM   145  C  CD1   . ILE   A 1 24  ? 29.723 -4.770  28.864 1.00 25.33 ? 21  ILE   A CD1   1 
ATOM   146  N  N     . GLN   A 1 25  ? 31.497 0.189   28.009 1.00 18.25 ? 22  GLN   A N     1 
ATOM   147  C  CA    . GLN   A 1 25  ? 31.642 1.624   28.329 1.00 18.01 ? 22  GLN   A CA    1 
ATOM   148  C  C     . GLN   A 1 25  ? 30.285 2.321   28.285 1.00 19.98 ? 22  GLN   A C     1 
ATOM   149  O  O     . GLN   A 1 25  ? 30.003 3.098   29.177 1.00 21.62 ? 22  GLN   A O     1 
ATOM   150  C  CB    . GLN   A 1 25  ? 32.647 2.315   27.400 1.00 20.00 ? 22  GLN   A CB    1 
ATOM   151  C  CG    . GLN   A 1 25  ? 34.041 2.267   27.955 1.00 21.21 ? 22  GLN   A CG    1 
ATOM   152  C  CD    . GLN   A 1 25  ? 34.327 3.143   29.161 1.00 21.07 ? 22  GLN   A CD    1 
ATOM   153  O  OE1   . GLN   A 1 25  ? 33.425 3.671   29.815 1.00 24.28 ? 22  GLN   A OE1   1 
ATOM   154  N  NE2   . GLN   A 1 25  ? 35.588 3.262   29.485 1.00 23.43 ? 22  GLN   A NE2   1 
ATOM   155  N  N     . LEU   A 1 26  ? 29.454 2.084   27.292 1.00 20.43 ? 23  LEU   A N     1 
ATOM   156  C  CA    . LEU   A 1 26  ? 28.131 2.659   27.211 1.00 20.17 ? 23  LEU   A CA    1 
ATOM   157  C  C     . LEU   A 1 26  ? 27.266 2.187   28.383 1.00 20.25 ? 23  LEU   A C     1 
ATOM   158  O  O     . LEU   A 1 26  ? 26.539 2.994   28.964 1.00 21.97 ? 23  LEU   A O     1 
ATOM   159  C  CB    . LEU   A 1 26  ? 27.453 2.273   25.890 1.00 20.43 ? 23  LEU   A CB    1 
ATOM   160  C  CG    . LEU   A 1 26  ? 26.183 3.076   25.652 1.00 21.13 ? 23  LEU   A CG    1 
ATOM   161  C  CD1   . LEU   A 1 26  ? 26.495 4.490   25.162 1.00 21.65 ? 23  LEU   A CD1   1 
ATOM   162  C  CD2   . LEU   A 1 26  ? 25.277 2.353   24.685 1.00 22.66 ? 23  LEU   A CD2   1 
ATOM   163  N  N     . ILE   A 1 27  ? 27.367 0.890   28.729 1.00 19.63 ? 24  ILE   A N     1 
ATOM   164  C  CA    . ILE   A 1 27  ? 26.450 0.277   29.693 1.00 20.33 ? 24  ILE   A CA    1 
ATOM   165  C  C     . ILE   A 1 27  ? 26.887 0.590   31.126 1.00 20.66 ? 24  ILE   A C     1 
ATOM   166  O  O     . ILE   A 1 27  ? 26.029 0.975   31.933 1.00 23.91 ? 24  ILE   A O     1 
ATOM   167  C  CB    . ILE   A 1 27  ? 26.299 -1.235  29.448 1.00 20.48 ? 24  ILE   A CB    1 
ATOM   168  C  CG1   . ILE   A 1 27  ? 25.662 -1.522  28.085 1.00 21.96 ? 24  ILE   A CG1   1 
ATOM   169  C  CG2   . ILE   A 1 27  ? 25.518 -1.889  30.585 1.00 22.08 ? 24  ILE   A CG2   1 
ATOM   170  C  CD1   . ILE   A 1 27  ? 24.322 -0.813  27.837 1.00 21.61 ? 24  ILE   A CD1   1 
ATOM   171  N  N     . GLN   A 1 28  ? 28.180 0.435   31.421 1.00 19.01 ? 25  GLN   A N     1 
ATOM   172  C  CA    . GLN   A 1 28  ? 28.680 0.501   32.798 1.00 20.56 ? 25  GLN   A CA    1 
ATOM   173  C  C     . GLN   A 1 28  ? 29.533 1.742   33.038 1.00 23.07 ? 25  GLN   A C     1 
ATOM   174  O  O     . GLN   A 1 28  ? 29.854 2.038   34.198 1.00 23.02 ? 25  GLN   A O     1 
ATOM   175  C  CB    . GLN   A 1 28  ? 29.545 -0.714  33.114 1.00 20.76 ? 25  GLN   A CB    1 
ATOM   176  C  CG    . GLN   A 1 28  ? 28.819 -2.030  33.003 1.00 23.63 ? 25  GLN   A CG    1 
ATOM   177  C  CD    . GLN   A 1 28  ? 29.760 -3.135  33.398 1.00 24.65 ? 25  GLN   A CD    1 
ATOM   178  O  OE1   . GLN   A 1 28  ? 30.872 -2.892  33.847 1.00 28.56 ? 25  GLN   A OE1   1 
ATOM   179  N  NE2   . GLN   A 1 28  ? 29.349 -4.364  33.165 1.00 30.24 ? 25  GLN   A NE2   1 
ATOM   180  N  N     . ASN   A 1 29  ? 29.953 2.427   31.957 1.00 22.08 ? 26  ASN   A N     1 
ATOM   181  C  CA    . ASN   A 1 29  ? 30.869 3.558   32.080 1.00 20.32 ? 26  ASN   A CA    1 
ATOM   182  C  C     . ASN   A 1 29  ? 32.220 3.108   32.631 1.00 21.11 ? 26  ASN   A C     1 
ATOM   183  O  O     . ASN   A 1 29  ? 32.939 3.873   33.266 1.00 24.03 ? 26  ASN   A O     1 
ATOM   184  C  CB    . ASN   A 1 29  ? 30.276 4.645   32.973 1.00 23.92 ? 26  ASN   A CB    1 
ATOM   185  C  CG    . ASN   A 1 29  ? 29.433 5.608   32.183 1.00 29.50 ? 26  ASN   A CG    1 
ATOM   186  O  OD1   . ASN   A 1 29  ? 29.832 6.752   31.970 1.00 38.26 ? 26  ASN   A OD1   1 
ATOM   187  N  ND2   . ASN   A 1 29  ? 28.300 5.128   31.704 1.00 42.54 ? 26  ASN   A ND2   1 
ATOM   188  N  N     . HIS   A 1 30  ? 32.554 1.834   32.408 1.00 20.69 ? 27  HIS   A N     1 
ATOM   189  C  CA    . HIS   A 1 30  ? 33.749 1.217   32.942 1.00 21.19 ? 27  HIS   A CA    1 
ATOM   190  C  C     . HIS   A 1 30  ? 34.491 0.515   31.813 1.00 22.90 ? 27  HIS   A C     1 
ATOM   191  O  O     . HIS   A 1 30  ? 33.842 0.016   30.890 1.00 22.21 ? 27  HIS   A O     1 
ATOM   192  C  CB    . HIS   A 1 30  ? 33.336 0.208   34.019 1.00 23.12 ? 27  HIS   A CB    1 
ATOM   193  C  CG    . HIS   A 1 30  ? 34.502 -0.337  34.742 1.00 24.64 ? 27  HIS   A CG    1 
ATOM   194  N  ND1   . HIS   A 1 30  ? 35.214 0.445   35.617 1.00 26.89 ? 27  HIS   A ND1   1 
ATOM   195  C  CD2   . HIS   A 1 30  ? 35.069 -1.562  34.741 1.00 28.78 ? 27  HIS   A CD2   1 
ATOM   196  C  CE1   . HIS   A 1 30  ? 36.201 -0.262  36.111 1.00 29.91 ? 27  HIS   A CE1   1 
ATOM   197  N  NE2   . HIS   A 1 30  ? 36.134 -1.498  35.608 1.00 31.29 ? 27  HIS   A NE2   1 
ATOM   198  N  N     . PHE   A 1 31  ? 35.828 0.512   31.873 1.00 22.76 ? 28  PHE   A N     1 
ATOM   199  C  CA    . PHE   A 1 31  ? 36.662 -0.126  30.848 1.00 23.77 ? 28  PHE   A CA    1 
ATOM   200  C  C     . PHE   A 1 31  ? 36.946 -1.584  31.221 1.00 24.85 ? 28  PHE   A C     1 
ATOM   201  O  O     . PHE   A 1 31  ? 37.422 -1.844  32.327 1.00 29.47 ? 28  PHE   A O     1 
ATOM   202  C  CB    . PHE   A 1 31  ? 37.957 0.675   30.653 1.00 25.38 ? 28  PHE   A CB    1 
ATOM   203  C  CG    . PHE   A 1 31  ? 38.872 0.176   29.560 1.00 24.02 ? 28  PHE   A CG    1 
ATOM   204  C  CD1   . PHE   A 1 31  ? 38.403 -0.039  28.270 1.00 22.89 ? 28  PHE   A CD1   1 
ATOM   205  C  CD2   . PHE   A 1 31  ? 40.201 -0.106  29.835 1.00 25.16 ? 28  PHE   A CD2   1 
ATOM   206  C  CE1   . PHE   A 1 31  ? 39.250 -0.509  27.281 1.00 26.22 ? 28  PHE   A CE1   1 
ATOM   207  C  CE2   . PHE   A 1 31  ? 41.046 -0.576  28.836 1.00 26.53 ? 28  PHE   A CE2   1 
ATOM   208  C  CZ    . PHE   A 1 31  ? 40.566 -0.779  27.561 1.00 25.29 ? 28  PHE   A CZ    1 
ATOM   209  N  N     . VAL   A 1 32  ? 36.651 -2.527  30.299 1.00 24.75 ? 29  VAL   A N     1 
ATOM   210  C  CA    . VAL   A 1 32  ? 36.790 -3.972  30.478 1.00 26.90 ? 29  VAL   A CA    1 
ATOM   211  C  C     . VAL   A 1 32  ? 38.188 -4.388  30.947 1.00 28.24 ? 29  VAL   A C     1 
ATOM   212  O  O     . VAL   A 1 32  ? 39.194 -3.799  30.568 1.00 33.93 ? 29  VAL   A O     1 
ATOM   213  C  CB    . VAL   A 1 32  ? 36.428 -4.766  29.201 1.00 28.98 ? 29  VAL   A CB    1 
ATOM   214  C  CG1   . VAL   A 1 32  ? 34.950 -4.673  28.857 1.00 28.63 ? 29  VAL   A CG1   1 
ATOM   215  C  CG2   . VAL   A 1 32  ? 37.283 -4.385  28.001 1.00 30.04 ? 29  VAL   A CG2   1 
ATOM   216  N  N     . ASP   A 1 33  ? 38.208 -5.458  31.740 1.00 31.58 ? 30  ASP   A N     1 
ATOM   217  C  CA    . ASP   A 1 33  ? 39.470 -6.029  32.250 1.00 31.39 ? 30  ASP   A CA    1 
ATOM   218  C  C     . ASP   A 1 33  ? 39.850 -7.201  31.383 1.00 31.23 ? 30  ASP   A C     1 
ATOM   219  O  O     . ASP   A 1 33  ? 39.008 -7.971  31.014 1.00 36.58 ? 30  ASP   A O     1 
ATOM   220  C  CB    . ASP   A 1 33  ? 39.303 -6.579  33.664 1.00 31.08 ? 30  ASP   A CB    1 
ATOM   221  C  CG    . ASP   A 1 33  ? 38.982 -5.455  34.612 1.00 32.47 ? 30  ASP   A CG    1 
ATOM   222  O  OD1   . ASP   A 1 33  ? 39.814 -4.569  34.733 1.00 34.62 ? 30  ASP   A OD1   1 
ATOM   223  O  OD2   . ASP   A 1 33  ? 37.861 -5.488  35.170 1.00 38.61 ? 30  ASP   A OD2   1 
ATOM   224  N  N     . GLU   A 1 34  ? 41.143 -7.372  31.164 1.00 35.43 ? 31  GLU   A N     1 
ATOM   225  C  CA    . GLU   A 1 34  ? 41.555 -8.513  30.311 1.00 39.08 ? 31  GLU   A CA    1 
ATOM   226  C  C     . GLU   A 1 34  ? 41.395 -9.793  31.124 1.00 35.47 ? 31  GLU   A C     1 
ATOM   227  O  O     . GLU   A 1 34  ? 41.264 -10.831 30.568 1.00 37.99 ? 31  GLU   A O     1 
ATOM   228  C  CB    . GLU   A 1 34  ? 42.977 -8.310  29.779 1.00 45.55 ? 31  GLU   A CB    1 
ATOM   229  C  CG    . GLU   A 1 34  ? 43.140 -7.042  28.961 0.00 27.00 ? 31  GLU   A CG    1 
ATOM   230  C  CD    . GLU   A 1 34  ? 44.552 -6.790  28.463 0.00 27.00 ? 31  GLU   A CD    1 
ATOM   231  O  OE1   . GLU   A 1 34  ? 45.444 -7.598  28.787 0.00 27.00 ? 31  GLU   A OE1   1 
ATOM   232  O  OE2   . GLU   A 1 34  ? 44.756 -5.786  27.752 0.00 27.00 ? 31  GLU   A OE2   1 
ATOM   233  N  N     . TYR   A 1 35  ? 41.301 -9.700  32.447 1.00 36.73 ? 32  TYR   A N     1 
ATOM   234  C  CA    . TYR   A 1 35  ? 41.262 -10.969 33.203 1.00 33.65 ? 32  TYR   A CA    1 
ATOM   235  C  C     . TYR   A 1 35  ? 39.857 -11.563 33.266 1.00 33.46 ? 32  TYR   A C     1 
ATOM   236  O  O     . TYR   A 1 35  ? 39.676 -12.711 33.671 1.00 38.68 ? 32  TYR   A O     1 
ATOM   237  C  CB    . TYR   A 1 35  ? 41.945 -10.782 34.552 1.00 36.67 ? 32  TYR   A CB    1 
ATOM   238  C  CG    . TYR   A 1 35  ? 41.492 -9.571  35.311 1.00 32.37 ? 32  TYR   A CG    1 
ATOM   239  C  CD1   . TYR   A 1 35  ? 40.252 -9.542  35.907 1.00 33.02 ? 32  TYR   A CD1   1 
ATOM   240  C  CD2   . TYR   A 1 35  ? 42.330 -8.492  35.464 1.00 32.72 ? 32  TYR   A CD2   1 
ATOM   241  C  CE1   . TYR   A 1 35  ? 39.869 -8.470  36.688 1.00 33.33 ? 32  TYR   A CE1   1 
ATOM   242  C  CE2   . TYR   A 1 35  ? 41.955 -7.406  36.222 1.00 33.01 ? 32  TYR   A CE2   1 
ATOM   243  C  CZ    . TYR   A 1 35  ? 40.728 -7.407  36.851 1.00 33.49 ? 32  TYR   A CZ    1 
ATOM   244  O  OH    . TYR   A 1 35  ? 40.352 -6.336  37.587 1.00 33.34 ? 32  TYR   A OH    1 
ATOM   245  N  N     . ASP   A 1 36  ? 38.874 -10.785 32.811 1.00 34.75 ? 33  ASP   A N     1 
ATOM   246  C  CA    . ASP   A 1 36  ? 37.491 -11.282 32.643 1.00 34.39 ? 33  ASP   A CA    1 
ATOM   247  C  C     . ASP   A 1 36  ? 37.002 -10.945 31.220 1.00 35.18 ? 33  ASP   A C     1 
ATOM   248  O  O     . ASP   A 1 36  ? 36.414 -9.883  31.041 1.00 34.19 ? 33  ASP   A O     1 
ATOM   249  C  CB    . ASP   A 1 36  ? 36.556 -10.764 33.744 1.00 39.84 ? 33  ASP   A CB    1 
ATOM   250  C  CG    . ASP   A 1 36  ? 36.698 -11.406 35.129 1.00 36.54 ? 33  ASP   A CG    1 
ATOM   251  O  OD1   . ASP   A 1 36  ? 36.531 -12.607 35.233 1.00 38.73 ? 33  ASP   A OD1   1 
ATOM   252  O  OD2   . ASP   A 1 36  ? 36.894 -10.672 36.094 1.00 44.68 ? 33  ASP   A OD2   1 
ATOM   253  N  N     . PRO   A 1 37  ? 37.286 -11.788 30.201 1.00 34.30 ? 34  PRO   A N     1 
ATOM   254  C  CA    . PRO   A 1 37  ? 36.819 -11.531 28.833 1.00 33.35 ? 34  PRO   A CA    1 
ATOM   255  C  C     . PRO   A 1 37  ? 35.294 -11.597 28.705 1.00 31.95 ? 34  PRO   A C     1 
ATOM   256  O  O     . PRO   A 1 37  ? 34.670 -12.459 29.206 1.00 35.40 ? 34  PRO   A O     1 
ATOM   257  C  CB    . PRO   A 1 37  ? 37.559 -12.513 27.922 1.00 34.83 ? 34  PRO   A CB    1 
ATOM   258  C  CG    . PRO   A 1 37  ? 38.225 -13.510 28.846 1.00 38.53 ? 34  PRO   A CG    1 
ATOM   259  C  CD    . PRO   A 1 37  ? 38.133 -12.975 30.266 1.00 34.44 ? 34  PRO   A CD    1 
ATOM   260  N  N     . THR   A 1 38  ? 34.735 -10.633 27.995 1.00 32.67 ? 35  THR   A N     1 
ATOM   261  C  CA    . THR   A 1 38  ? 33.276 -10.474 27.868 1.00 26.53 ? 35  THR   A CA    1 
ATOM   262  C  C     . THR   A 1 38  ? 32.735 -11.582 26.976 1.00 27.70 ? 35  THR   A C     1 
ATOM   263  O  O     . THR   A 1 38  ? 33.344 -11.839 25.955 1.00 31.61 ? 35  THR   A O     1 
ATOM   264  C  CB    . THR   A 1 38  ? 33.035 -9.096  27.252 1.00 26.04 ? 35  THR   A CB    1 
ATOM   265  O  OG1   . THR   A 1 38  ? 33.808 -8.122  27.949 1.00 27.64 ? 35  THR   A OG1   1 
ATOM   266  C  CG2   . THR   A 1 38  ? 31.583 -8.699  27.244 1.00 30.28 ? 35  THR   A CG2   1 
ATOM   267  N  N     . ILE   A 1 39  ? 31.660 -12.223 27.320 1.00 27.76 ? 36  ILE   A N     1 
ATOM   268  C  CA    . ILE   A 1 39  ? 31.014 -13.249 26.457 1.00 29.04 ? 36  ILE   A CA    1 
ATOM   269  C  C     . ILE   A 1 39  ? 29.937 -12.532 25.626 1.00 26.18 ? 36  ILE   A C     1 
ATOM   270  O  O     . ILE   A 1 39  ? 29.457 -11.511 26.041 1.00 27.98 ? 36  ILE   A O     1 
ATOM   271  C  CB    . ILE   A 1 39  ? 30.421 -14.394 27.280 1.00 34.77 ? 36  ILE   A CB    1 
ATOM   272  C  CG1   . ILE   A 1 39  ? 31.353 -14.791 28.411 1.00 38.37 ? 36  ILE   A CG1   1 
ATOM   273  C  CG2   . ILE   A 1 39  ? 30.120 -15.590 26.409 1.00 36.95 ? 36  ILE   A CG2   1 
ATOM   274  C  CD1   . ILE   A 1 39  ? 30.733 -15.677 29.423 1.00 43.62 ? 36  ILE   A CD1   1 
ATOM   275  N  N     . GLU   A 1 40  ? 29.614 -13.072 24.467 1.00 24.83 ? 37  GLU   A N     1 
ATOM   276  C  CA    . GLU   A 1 40  ? 28.589 -12.469 23.609 1.00 22.00 ? 37  GLU   A CA    1 
ATOM   277  C  C     . GLU   A 1 40  ? 27.305 -12.398 24.426 1.00 20.36 ? 37  GLU   A C     1 
ATOM   278  O  O     . GLU   A 1 40  ? 26.902 -13.393 24.982 1.00 23.48 ? 37  GLU   A O     1 
ATOM   279  C  CB    . GLU   A 1 40  ? 28.410 -13.367 22.391 1.00 23.04 ? 37  GLU   A CB    1 
ATOM   280  C  CG    . GLU   A 1 40  ? 27.379 -12.875 21.396 1.00 22.84 ? 37  GLU   A CG    1 
ATOM   281  C  CD    . GLU   A 1 40  ? 27.352 -13.600 20.066 1.00 24.99 ? 37  GLU   A CD    1 
ATOM   282  O  OE1   . GLU   A 1 40  ? 28.263 -13.414 19.298 1.00 26.41 ? 37  GLU   A OE1   1 
ATOM   283  O  OE2   . GLU   A 1 40  ? 26.423 -14.292 19.802 1.00 25.02 ? 37  GLU   A OE2   1 
ATOM   284  N  N     . ASP   A 1 41  ? 26.691 -11.233 24.410 1.00 19.51 ? 38  ASP   A N     1 
ATOM   285  C  CA    . ASP   A 1 41  ? 25.439 -11.027 25.158 1.00 19.76 ? 38  ASP   A CA    1 
ATOM   286  C  C     . ASP   A 1 41  ? 24.805 -9.732  24.662 1.00 19.29 ? 38  ASP   A C     1 
ATOM   287  O  O     . ASP   A 1 41  ? 25.422 -8.986  23.915 1.00 18.82 ? 38  ASP   A O     1 
ATOM   288  C  CB    . ASP   A 1 41  ? 25.724 -10.923 26.664 1.00 20.51 ? 38  ASP   A CB    1 
ATOM   289  C  CG    . ASP   A 1 41  ? 24.578 -11.334 27.572 1.00 24.35 ? 38  ASP   A CG    1 
ATOM   290  O  OD1   . ASP   A 1 41  ? 23.498 -11.561 27.076 1.00 21.79 ? 38  ASP   A OD1   1 
ATOM   291  O  OD2   . ASP   A 1 41  ? 24.809 -11.426 28.761 1.00 27.57 ? 38  ASP   A OD2   1 
ATOM   292  N  N     . SER   A 1 42  ? 23.580 -9.518  25.092 1.00 18.09 ? 39  SER   A N     1 
ATOM   293  C  CA    . SER   A 1 42  ? 22.860 -8.279  24.823 1.00 18.40 ? 39  SER   A CA    1 
ATOM   294  C  C     . SER   A 1 42  ? 22.644 -7.523  26.134 1.00 17.66 ? 39  SER   A C     1 
ATOM   295  O  O     . SER   A 1 42  ? 22.720 -8.086  27.237 1.00 19.93 ? 39  SER   A O     1 
ATOM   296  C  CB    . SER   A 1 42  ? 21.549 -8.568  24.162 1.00 19.59 ? 39  SER   A CB    1 
ATOM   297  O  OG    . SER   A 1 42  ? 20.742 -9.326  25.073 1.00 21.08 ? 39  SER   A OG    1 
ATOM   298  N  N     . TYR   A 1 43  ? 22.406 -6.224  25.979 1.00 17.05 ? 40  TYR   A N     1 
ATOM   299  C  CA    . TYR   A 1 43  ? 22.278 -5.274  27.073 1.00 18.19 ? 40  TYR   A CA    1 
ATOM   300  C  C     . TYR   A 1 43  ? 21.158 -4.294  26.745 1.00 21.64 ? 40  TYR   A C     1 
ATOM   301  O  O     . TYR   A 1 43  ? 20.999 -3.903  25.594 1.00 19.84 ? 40  TYR   A O     1 
ATOM   302  C  CB    . TYR   A 1 43  ? 23.586 -4.512  27.240 1.00 20.05 ? 40  TYR   A CB    1 
ATOM   303  C  CG    . TYR   A 1 43  ? 24.781 -5.409  27.389 1.00 19.70 ? 40  TYR   A CG    1 
ATOM   304  C  CD1   . TYR   A 1 43  ? 25.452 -5.894  26.274 1.00 20.45 ? 40  TYR   A CD1   1 
ATOM   305  C  CD2   . TYR   A 1 43  ? 25.259 -5.734  28.644 1.00 22.52 ? 40  TYR   A CD2   1 
ATOM   306  C  CE1   . TYR   A 1 43  ? 26.562 -6.718  26.417 1.00 19.24 ? 40  TYR   A CE1   1 
ATOM   307  C  CE2   . TYR   A 1 43  ? 26.360 -6.562  28.796 1.00 21.19 ? 40  TYR   A CE2   1 
ATOM   308  C  CZ    . TYR   A 1 43  ? 27.017 -7.055  27.682 1.00 20.62 ? 40  TYR   A CZ    1 
ATOM   309  O  OH    . TYR   A 1 43  ? 28.095 -7.875  27.866 1.00 21.90 ? 40  TYR   A OH    1 
ATOM   310  N  N     . ARG   A 1 44  ? 20.411 -3.897  27.779 1.00 21.75 ? 41  ARG   A N     1 
ATOM   311  C  CA    . ARG   A 1 44  ? 19.328 -2.930  27.642 1.00 20.85 ? 41  ARG   A CA    1 
ATOM   312  C  C     . ARG   A 1 44  ? 19.663 -1.638  28.374 1.00 21.57 ? 41  ARG   A C     1 
ATOM   313  O  O     . ARG   A 1 44  ? 20.236 -1.654  29.458 1.00 23.12 ? 41  ARG   A O     1 
ATOM   314  C  CB    . ARG   A 1 44  ? 17.991 -3.528  28.090 1.00 24.49 ? 41  ARG   A CB    1 
ATOM   315  C  CG    . ARG   A 1 44  ? 17.307 -4.310  26.975 1.00 32.18 ? 41  ARG   A CG    1 
ATOM   316  C  CD    . ARG   A 1 44  ? 16.691 -5.661  27.311 1.00 38.78 ? 41  ARG   A CD    1 
ATOM   317  N  NE    . ARG   A 1 44  ? 17.658 -6.550  27.946 1.00 39.77 ? 41  ARG   A NE    1 
ATOM   318  C  CZ    . ARG   A 1 44  ? 18.526 -7.361  27.343 1.00 34.72 ? 41  ARG   A CZ    1 
ATOM   319  N  NH1   . ARG   A 1 44  ? 18.606 -7.457  26.021 1.00 30.75 ? 41  ARG   A NH1   1 
ATOM   320  N  NH2   . ARG   A 1 44  ? 19.337 -8.082  28.091 1.00 38.57 ? 41  ARG   A NH2   1 
ATOM   321  N  N     . LYS   A 1 45  ? 19.316 -0.514  27.751 1.00 19.14 ? 42  LYS   A N     1 
ATOM   322  C  CA    . LYS   A 1 45  ? 19.590 0.792   28.347 1.00 20.36 ? 42  LYS   A CA    1 
ATOM   323  C  C     . LYS   A 1 45  ? 18.563 1.776   27.776 1.00 22.28 ? 42  LYS   A C     1 
ATOM   324  O  O     . LYS   A 1 45  ? 18.424 1.926   26.563 1.00 21.75 ? 42  LYS   A O     1 
ATOM   325  C  CB    . LYS   A 1 45  ? 21.033 1.244   28.084 1.00 22.29 ? 42  LYS   A CB    1 
ATOM   326  C  CG    . LYS   A 1 45  ? 21.392 2.644   28.576 1.00 26.05 ? 42  LYS   A CG    1 
ATOM   327  C  CD    . LYS   A 1 45  ? 22.828 2.983   28.205 1.00 26.82 ? 42  LYS   A CD    1 
ATOM   328  C  CE    . LYS   A 1 45  ? 23.317 4.353   28.608 1.00 30.41 ? 42  LYS   A CE    1 
ATOM   329  N  NZ    . LYS   A 1 45  ? 23.678 4.359   30.046 1.00 35.12 ? 42  LYS   A NZ    1 
ATOM   330  N  N     . GLN   A 1 46  ? 17.790 2.422   28.662 1.00 20.62 ? 43  GLN   A N     1 
ATOM   331  C  CA    . GLN   A 1 46  ? 16.811 3.406   28.234 1.00 20.30 ? 43  GLN   A CA    1 
ATOM   332  C  C     . GLN   A 1 46  ? 17.468 4.770   28.298 1.00 22.06 ? 43  GLN   A C     1 
ATOM   333  O  O     . GLN   A 1 46  ? 18.135 5.091   29.285 1.00 23.64 ? 43  GLN   A O     1 
ATOM   334  C  CB    . GLN   A 1 46  ? 15.607 3.378   29.181 1.00 21.28 ? 43  GLN   A CB    1 
ATOM   335  C  CG    . GLN   A 1 46  ? 14.575 4.448   28.851 1.00 23.74 ? 43  GLN   A CG    1 
ATOM   336  C  CD    . GLN   A 1 46  ? 13.345 4.395   29.722 1.00 23.83 ? 43  GLN   A CD    1 
ATOM   337  O  OE1   . GLN   A 1 46  ? 12.775 3.329   29.966 1.00 26.38 ? 43  GLN   A OE1   1 
ATOM   338  N  NE2   . GLN   A 1 46  ? 12.879 5.579   30.108 1.00 26.99 ? 43  GLN   A NE2   1 
ATOM   339  N  N     . VAL   A 1 47  ? 17.337 5.521   27.184 1.00 22.17 ? 44  VAL   A N     1 
ATOM   340  C  CA    . VAL   A 1 47  ? 17.970 6.815   26.963 1.00 24.58 ? 44  VAL   A CA    1 
ATOM   341  C  C     . VAL   A 1 47  ? 16.954 7.742   26.297 1.00 22.08 ? 44  VAL   A C     1 
ATOM   342  O  O     . VAL   A 1 47  ? 15.952 7.277   25.754 1.00 26.76 ? 44  VAL   A O     1 
ATOM   343  C  CB    . VAL   A 1 47  ? 19.231 6.664   26.080 1.00 27.12 ? 44  VAL   A CB    1 
ATOM   344  C  CG1   . VAL   A 1 47  ? 20.287 5.759   26.700 1.00 30.04 ? 44  VAL   A CG1   1 
ATOM   345  C  CG2   . VAL   A 1 47  ? 18.881 6.158   24.683 1.00 28.76 ? 44  VAL   A CG2   1 
ATOM   346  N  N     . VAL   A 1 48  ? 17.246 9.016   26.395 1.00 23.60 ? 45  VAL   A N     1 
ATOM   347  C  CA    . VAL   A 1 48  ? 16.434 10.057  25.726 1.00 24.25 ? 45  VAL   A CA    1 
ATOM   348  C  C     . VAL   A 1 48  ? 17.393 10.690  24.716 1.00 24.40 ? 45  VAL   A C     1 
ATOM   349  O  O     . VAL   A 1 48  ? 18.456 11.115  25.101 1.00 24.97 ? 45  VAL   A O     1 
ATOM   350  C  CB    . VAL   A 1 48  ? 15.867 11.126  26.668 1.00 26.19 ? 45  VAL   A CB    1 
ATOM   351  C  CG1   . VAL   A 1 48  ? 15.014 12.097  25.882 1.00 25.75 ? 45  VAL   A CG1   1 
ATOM   352  C  CG2   . VAL   A 1 48  ? 15.040 10.487  27.775 1.00 26.26 ? 45  VAL   A CG2   1 
ATOM   353  N  N     . ILE   A 1 49  ? 16.997 10.632  23.450 1.00 23.94 ? 46  ILE   A N     1 
ATOM   354  C  CA    . ILE   A 1 49  ? 17.797 11.198  22.320 1.00 25.06 ? 46  ILE   A CA    1 
ATOM   355  C  C     . ILE   A 1 49  ? 16.900 12.202  21.589 1.00 23.35 ? 46  ILE   A C     1 
ATOM   356  O  O     . ILE   A 1 49  ? 15.845 11.850  21.159 1.00 23.45 ? 46  ILE   A O     1 
ATOM   357  C  CB    . ILE   A 1 49  ? 18.382 10.059  21.450 1.00 25.20 ? 46  ILE   A CB    1 
ATOM   358  C  CG1   . ILE   A 1 49  ? 19.357 9.161   22.212 1.00 26.75 ? 46  ILE   A CG1   1 
ATOM   359  C  CG2   . ILE   A 1 49  ? 19.068 10.641  20.229 1.00 26.60 ? 46  ILE   A CG2   1 
ATOM   360  C  CD1   . ILE   A 1 49  ? 19.721 7.864   21.526 1.00 27.33 ? 46  ILE   A CD1   1 
ATOM   361  N  N     . ASP   A 1 50  ? 17.333 13.457  21.567 1.00 24.55 ? 47  ASP   A N     1 
ATOM   362  C  CA    . ASP   A 1 50  ? 16.579 14.568  20.943 1.00 22.83 ? 47  ASP   A CA    1 
ATOM   363  C  C     . ASP   A 1 50  ? 15.142 14.613  21.462 1.00 24.14 ? 47  ASP   A C     1 
ATOM   364  O  O     . ASP   A 1 50  ? 14.217 14.734  20.692 1.00 23.91 ? 47  ASP   A O     1 
ATOM   365  C  CB    . ASP   A 1 50  ? 16.658 14.463  19.411 1.00 25.53 ? 47  ASP   A CB    1 
ATOM   366  C  CG    . ASP   A 1 50  ? 18.084 14.340  18.893 1.00 25.11 ? 47  ASP   A CG    1 
ATOM   367  O  OD1   . ASP   A 1 50  ? 18.966 14.863  19.497 1.00 27.76 ? 47  ASP   A OD1   1 
ATOM   368  O  OD2   . ASP   A 1 50  ? 18.271 13.689  17.871 1.00 25.65 ? 47  ASP   A OD2   1 
ATOM   369  N  N     . GLY   A 1 51  ? 14.991 14.448  22.776 1.00 23.85 ? 48  GLY   A N     1 
ATOM   370  C  CA    . GLY   A 1 51  ? 13.691 14.586  23.424 1.00 25.11 ? 48  GLY   A CA    1 
ATOM   371  C  C     . GLY   A 1 51  ? 12.737 13.407  23.203 1.00 24.93 ? 48  GLY   A C     1 
ATOM   372  O  O     . GLY   A 1 51  ? 11.577 13.465  23.628 1.00 28.15 ? 48  GLY   A O     1 
ATOM   373  N  N     . GLU   A 1 52  ? 13.206 12.341  22.544 1.00 26.25 ? 49  GLU   A N     1 
ATOM   374  C  CA    . GLU   A 1 52  ? 12.387 11.144  22.375 1.00 25.53 ? 49  GLU   A CA    1 
ATOM   375  C  C     . GLU   A 1 52  ? 12.976 10.012  23.222 1.00 24.78 ? 49  GLU   A C     1 
ATOM   376  O  O     . GLU   A 1 52  ? 14.164 9.710   23.124 1.00 24.14 ? 49  GLU   A O     1 
ATOM   377  C  CB    . GLU   A 1 52  ? 12.320 10.739  20.897 1.00 25.08 ? 49  GLU   A CB    1 
ATOM   378  C  CG    . GLU   A 1 52  ? 11.530 11.707  20.009 1.00 25.99 ? 49  GLU   A CG    1 
ATOM   379  C  CD    . GLU   A 1 52  ? 10.022 11.768  20.205 1.00 28.54 ? 49  GLU   A CD    1 
ATOM   380  O  OE1   . GLU   A 1 52  ? 9.492  10.988  20.995 1.00 29.96 ? 49  GLU   A OE1   1 
ATOM   381  O  OE2   . GLU   A 1 52  ? 9.364  12.593  19.538 1.00 27.81 ? 49  GLU   A OE2   1 
ATOM   382  N  N     . THR   A 1 53  ? 12.129 9.375   24.038 1.00 24.30 ? 50  THR   A N     1 
ATOM   383  C  CA    . THR   A 1 53  ? 12.583 8.302   24.908 1.00 24.68 ? 50  THR   A CA    1 
ATOM   384  C  C     . THR   A 1 53  ? 12.673 7.007   24.113 1.00 23.98 ? 50  THR   A C     1 
ATOM   385  O  O     . THR   A 1 53  ? 11.781 6.716   23.319 1.00 28.18 ? 50  THR   A O     1 
ATOM   386  C  CB    . THR   A 1 53  ? 11.608 8.082   26.073 1.00 25.16 ? 50  THR   A CB    1 
ATOM   387  O  OG1   . THR   A 1 53  ? 11.423 9.343   26.709 1.00 29.07 ? 50  THR   A OG1   1 
ATOM   388  C  CG2   . THR   A 1 53  ? 12.092 7.043   27.066 1.00 27.01 ? 50  THR   A CG2   1 
ATOM   389  N  N     . CYS   A 1 54  ? 13.716 6.210   24.379 1.00 24.11 ? 51  CYS   A N     1 
ATOM   390  C  CA    . CYS   A 1 54  ? 13.778 4.929   23.702 1.00 24.86 ? 51  CYS   A CA    1 
ATOM   391  C  C     . CYS   A 1 54  ? 14.551 3.909   24.530 1.00 23.64 ? 51  CYS   A C     1 
ATOM   392  O  O     . CYS   A 1 54  ? 15.323 4.244   25.440 1.00 23.17 ? 51  CYS   A O     1 
ATOM   393  C  CB    . CYS   A 1 54  ? 14.373 5.084   22.306 1.00 26.42 ? 51  CYS   A CB    1 
ATOM   394  S  SG    . CYS   A 1 54  ? 16.109 5.570   22.374 1.00 26.31 ? 51  CYS   A SG    1 
ATOM   395  N  N     . LEU   A 1 55  ? 14.316 2.655   24.166 1.00 21.68 ? 52  LEU   A N     1 
ATOM   396  C  CA    . LEU   A 1 55  ? 15.024 1.545   24.785 1.00 22.45 ? 52  LEU   A CA    1 
ATOM   397  C  C     . LEU   A 1 55  ? 16.022 0.968   23.782 1.00 21.05 ? 52  LEU   A C     1 
ATOM   398  O  O     . LEU   A 1 55  ? 15.618 0.531   22.704 1.00 22.06 ? 52  LEU   A O     1 
ATOM   399  C  CB    . LEU   A 1 55  ? 14.022 0.478   25.210 1.00 23.39 ? 52  LEU   A CB    1 
ATOM   400  C  CG    . LEU   A 1 55  ? 14.631 -0.725  25.933 1.00 26.00 ? 52  LEU   A CG    1 
ATOM   401  C  CD1   . LEU   A 1 55  ? 15.194 -0.324  27.285 1.00 24.97 ? 52  LEU   A CD1   1 
ATOM   402  C  CD2   . LEU   A 1 55  ? 13.611 -1.853  26.061 1.00 27.55 ? 52  LEU   A CD2   1 
ATOM   403  N  N     . LEU   A 1 56  ? 17.282 0.940   24.196 1.00 18.37 ? 53  LEU   A N     1 
ATOM   404  C  CA    . LEU   A 1 56  ? 18.334 0.389   23.279 1.00 18.38 ? 53  LEU   A CA    1 
ATOM   405  C  C     . LEU   A 1 56  ? 18.534 -1.062  23.654 1.00 20.22 ? 53  LEU   A C     1 
ATOM   406  O  O     . LEU   A 1 56  ? 18.673 -1.320  24.876 1.00 22.35 ? 53  LEU   A O     1 
ATOM   407  C  CB    . LEU   A 1 56  ? 19.645 1.122   23.502 1.00 18.93 ? 53  LEU   A CB    1 
ATOM   408  C  CG    . LEU   A 1 56  ? 19.609 2.614   23.262 1.00 21.07 ? 53  LEU   A CG    1 
ATOM   409  C  CD1   . LEU   A 1 56  ? 20.991 3.206   23.333 1.00 23.75 ? 53  LEU   A CD1   1 
ATOM   410  C  CD2   . LEU   A 1 56  ? 18.880 2.977   21.971 1.00 20.88 ? 53  LEU   A CD2   1 
ATOM   411  N  N     . ASP   A 1 57  ? 18.427 -1.986  22.715 1.00 18.97 ? 54  ASP   A N     1 
ATOM   412  C  CA    . ASP   A 1 57  ? 18.719 -3.397  22.992 1.00 19.47 ? 54  ASP   A CA    1 
ATOM   413  C  C     . ASP   A 1 57  ? 19.968 -3.684  22.150 1.00 18.55 ? 54  ASP   A C     1 
ATOM   414  O  O     . ASP   A 1 57  ? 19.798 -3.807  20.926 1.00 18.32 ? 54  ASP   A O     1 
ATOM   415  C  CB    . ASP   A 1 57  ? 17.518 -4.249  22.635 1.00 21.14 ? 54  ASP   A CB    1 
ATOM   416  C  CG    . ASP   A 1 57  ? 17.679 -5.719  22.921 1.00 21.65 ? 54  ASP   A CG    1 
ATOM   417  O  OD1   . ASP   A 1 57  ? 18.753 -6.103  23.426 1.00 21.55 ? 54  ASP   A OD1   1 
ATOM   418  O  OD2   . ASP   A 1 57  ? 16.730 -6.477  22.638 1.00 27.26 ? 54  ASP   A OD2   1 
ATOM   419  N  N     . ILE   A 1 58  ? 21.109 -3.826  22.772 1.00 16.46 ? 55  ILE   A N     1 
ATOM   420  C  CA    . ILE   A 1 58  ? 22.424 -3.887  22.074 1.00 17.71 ? 55  ILE   A CA    1 
ATOM   421  C  C     . ILE   A 1 58  ? 23.023 -5.273  22.165 1.00 19.03 ? 55  ILE   A C     1 
ATOM   422  O  O     . ILE   A 1 58  ? 23.253 -5.781  23.210 1.00 18.09 ? 55  ILE   A O     1 
ATOM   423  C  CB    . ILE   A 1 58  ? 23.367 -2.845  22.685 1.00 18.94 ? 55  ILE   A CB    1 
ATOM   424  C  CG1   . ILE   A 1 58  ? 22.748 -1.452  22.697 1.00 19.09 ? 55  ILE   A CG1   1 
ATOM   425  C  CG2   . ILE   A 1 58  ? 24.717 -2.859  21.971 1.00 19.37 ? 55  ILE   A CG2   1 
ATOM   426  C  CD1   . ILE   A 1 58  ? 23.503 -0.468  23.509 1.00 19.91 ? 55  ILE   A CD1   1 
ATOM   427  N  N     . LEU   A 1 59  ? 23.387 -5.838  21.025 1.00 16.59 ? 56  LEU   A N     1 
ATOM   428  C  CA    . LEU   A 1 59  ? 24.004 -7.143  21.000 1.00 16.58 ? 56  LEU   A CA    1 
ATOM   429  C  C     . LEU   A 1 59  ? 25.466 -6.941  20.654 1.00 17.42 ? 56  LEU   A C     1 
ATOM   430  O  O     . LEU   A 1 59  ? 25.813 -6.358  19.619 1.00 17.62 ? 56  LEU   A O     1 
ATOM   431  C  CB    . LEU   A 1 59  ? 23.366 -8.034  19.934 1.00 16.81 ? 56  LEU   A CB    1 
ATOM   432  C  CG    . LEU   A 1 59  ? 24.049 -9.399  19.729 1.00 18.21 ? 56  LEU   A CG    1 
ATOM   433  C  CD1   . LEU   A 1 59  ? 23.916 -10.289 20.955 1.00 19.40 ? 56  LEU   A CD1   1 
ATOM   434  C  CD2   . LEU   A 1 59  ? 23.458 -10.104 18.518 1.00 19.42 ? 56  LEU   A CD2   1 
ATOM   435  N  N     . ASP   A 1 60  ? 26.326 -7.353  21.586 1.00 16.55 ? 57  ASP   A N     1 
ATOM   436  C  CA    . ASP   A 1 60  ? 27.768 -7.314  21.437 1.00 17.14 ? 57  ASP   A CA    1 
ATOM   437  C  C     . ASP   A 1 60  ? 28.199 -8.651  20.863 1.00 18.55 ? 57  ASP   A C     1 
ATOM   438  O  O     . ASP   A 1 60  ? 28.209 -9.628  21.599 1.00 19.88 ? 57  ASP   A O     1 
ATOM   439  C  CB    . ASP   A 1 60  ? 28.385 -7.124  22.821 1.00 17.64 ? 57  ASP   A CB    1 
ATOM   440  C  CG    . ASP   A 1 60  ? 29.885 -7.232  22.857 1.00 19.15 ? 57  ASP   A CG    1 
ATOM   441  O  OD1   . ASP   A 1 60  ? 30.488 -6.899  21.833 1.00 18.52 ? 57  ASP   A OD1   1 
ATOM   442  O  OD2   . ASP   A 1 60  ? 30.424 -7.639  23.935 1.00 18.85 ? 57  ASP   A OD2   1 
ATOM   443  N  N     . THR   A 1 61  ? 28.572 -8.687  19.581 1.00 17.31 ? 58  THR   A N     1 
ATOM   444  C  CA    . THR   A 1 61  ? 28.818 -9.960  18.907 1.00 17.89 ? 58  THR   A CA    1 
ATOM   445  C  C     . THR   A 1 61  ? 30.279 -10.392 18.996 1.00 18.56 ? 58  THR   A C     1 
ATOM   446  O  O     . THR   A 1 61  ? 31.179 -9.574  19.143 1.00 20.36 ? 58  THR   A O     1 
ATOM   447  C  CB    . THR   A 1 61  ? 28.360 -9.938  17.439 1.00 18.11 ? 58  THR   A CB    1 
ATOM   448  O  OG1   . THR   A 1 61  ? 29.178 -9.066  16.665 1.00 19.10 ? 58  THR   A OG1   1 
ATOM   449  C  CG2   . THR   A 1 61  ? 26.924 -9.507  17.320 1.00 20.47 ? 58  THR   A CG2   1 
ATOM   450  N  N     . ALA   A 1 62  ? 30.478 -11.689 18.853 1.00 20.12 ? 59  ALA   A N     1 
ATOM   451  C  CA    . ALA   A 1 62  ? 31.834 -12.269 18.798 1.00 20.91 ? 59  ALA   A CA    1 
ATOM   452  C  C     . ALA   A 1 62  ? 32.537 -11.778 17.523 1.00 21.77 ? 59  ALA   A C     1 
ATOM   453  O  O     . ALA   A 1 62  ? 31.881 -11.562 16.530 1.00 23.58 ? 59  ALA   A O     1 
ATOM   454  C  CB    . ALA   A 1 62  ? 31.701 -13.758 18.707 1.00 21.14 ? 59  ALA   A CB    1 
ATOM   455  N  N     . GLY   A 1 63  ? 33.854 -11.768 17.552 1.00 22.07 ? 60  GLY   A N     1 
ATOM   456  C  CA    . GLY   A 1 63  ? 34.644 -11.458 16.340 1.00 22.27 ? 60  GLY   A CA    1 
ATOM   457  C  C     . GLY   A 1 63  ? 34.161 -12.250 15.134 1.00 22.58 ? 60  GLY   A C     1 
ATOM   458  O  O     . GLY   A 1 63  ? 33.901 -13.428 15.204 1.00 20.97 ? 60  GLY   A O     1 
ATOM   459  N  N     . GLN   A 1 64  ? 34.133 -11.572 13.987 1.00 22.87 ? 61  GLN   A N     1 
ATOM   460  C  CA    . GLN   A 1 64  ? 33.608 -12.128 12.711 1.00 22.01 ? 61  GLN   A CA    1 
ATOM   461  C  C     . GLN   A 1 64  ? 34.346 -13.412 12.284 1.00 23.91 ? 61  GLN   A C     1 
ATOM   462  O  O     . GLN   A 1 64  ? 33.724 -14.188 11.671 1.00 25.33 ? 61  GLN   A O     1 
ATOM   463  C  CB    . GLN   A 1 64  ? 33.608 -11.026 11.653 1.00 22.43 ? 61  GLN   A CB    1 
ATOM   464  C  CG    . GLN   A 1 64  ? 32.486 -10.006 11.795 1.00 21.42 ? 61  GLN   A CG    1 
ATOM   465  C  CD    . GLN   A 1 64  ? 31.100 -10.555 11.586 1.00 23.19 ? 61  GLN   A CD    1 
ATOM   466  O  OE1   . GLN   A 1 64  ? 30.800 -11.229 10.608 1.00 25.03 ? 61  GLN   A OE1   1 
ATOM   467  N  NE2   . GLN   A 1 64  ? 30.207 -10.253 12.525 1.00 25.47 ? 61  GLN   A NE2   1 
ATOM   468  N  N     . GLU   A 1 65  ? 35.596 -13.585 12.698 1.00 24.17 ? 62  GLU   A N     1 
ATOM   469  C  CA    . GLU   A 1 65  ? 36.407 -14.781 12.328 1.00 27.26 ? 62  GLU   A CA    1 
ATOM   470  C  C     . GLU   A 1 65  ? 36.268 -15.876 13.389 1.00 29.95 ? 62  GLU   A C     1 
ATOM   471  O  O     . GLU   A 1 65  ? 36.725 -16.984 13.173 1.00 33.03 ? 62  GLU   A O     1 
ATOM   472  C  CB    . GLU   A 1 65  ? 37.867 -14.400 12.124 1.00 28.79 ? 62  GLU   A CB    1 
ATOM   473  C  CG    . GLU   A 1 65  ? 38.555 -13.865 13.358 1.00 33.88 ? 62  GLU   A CG    1 
ATOM   474  C  CD    . GLU   A 1 65  ? 38.295 -12.386 13.617 1.00 35.53 ? 62  GLU   A CD    1 
ATOM   475  O  OE1   . GLU   A 1 65  ? 37.165 -12.051 13.800 1.00 40.20 ? 62  GLU   A OE1   1 
ATOM   476  O  OE2   . GLU   A 1 65  ? 39.236 -11.598 13.592 1.00 38.00 ? 62  GLU   A OE2   1 
ATOM   477  N  N     . GLU   A 1 66  ? 35.654 -15.511 14.518 1.00 30.50 ? 63  GLU   A N     1 
ATOM   478  C  CA    . GLU   A 1 66  ? 35.449 -16.508 15.579 1.00 29.97 ? 63  GLU   A CA    1 
ATOM   479  C  C     . GLU   A 1 66  ? 34.316 -17.421 15.130 1.00 32.16 ? 63  GLU   A C     1 
ATOM   480  O  O     . GLU   A 1 66  ? 33.483 -17.083 14.221 1.00 30.57 ? 63  GLU   A O     1 
ATOM   481  C  CB    . GLU   A 1 66  ? 35.164 -15.845 16.934 1.00 32.41 ? 63  GLU   A CB    1 
ATOM   482  C  CG    . GLU   A 1 66  ? 35.395 -16.733 18.158 0.00 27.00 ? 63  GLU   A CG    1 
ATOM   483  C  CD    . GLU   A 1 66  ? 34.833 -16.249 19.490 0.00 27.00 ? 63  GLU   A CD    1 
ATOM   484  O  OE1   . GLU   A 1 66  ? 34.640 -15.026 19.644 0.00 27.00 ? 63  GLU   A OE1   1 
ATOM   485  O  OE2   . GLU   A 1 66  ? 34.592 -17.097 20.374 0.00 27.00 ? 63  GLU   A OE2   1 
ATOM   486  N  N     . TYR   A 1 67  ? 34.300 -18.586 15.738 1.00 36.13 ? 64  TYR   A N     1 
ATOM   487  C  CA    . TYR   A 1 67  ? 33.194 -19.438 15.315 1.00 33.26 ? 64  TYR   A CA    1 
ATOM   488  C  C     . TYR   A 1 67  ? 31.777 -18.874 15.781 1.00 32.01 ? 64  TYR   A C     1 
ATOM   489  O  O     . TYR   A 1 67  ? 31.733 -18.557 16.979 1.00 27.87 ? 64  TYR   A O     1 
ATOM   490  C  CB    . TYR   A 1 67  ? 33.142 -20.895 15.833 1.00 32.84 ? 64  TYR   A CB    1 
ATOM   491  C  CG    . TYR   A 1 67  ? 31.832 -21.587 15.486 1.00 30.40 ? 64  TYR   A CG    1 
ATOM   492  C  CD1   . TYR   A 1 67  ? 31.531 -21.893 14.167 1.00 37.37 ? 64  TYR   A CD1   1 
ATOM   493  C  CD2   . TYR   A 1 67  ? 30.795 -21.845 16.422 1.00 36.69 ? 64  TYR   A CD2   1 
ATOM   494  C  CE1   . TYR   A 1 67  ? 30.324 -22.448 13.776 1.00 35.41 ? 64  TYR   A CE1   1 
ATOM   495  C  CE2   . TYR   A 1 67  ? 29.582 -22.399 16.047 1.00 32.94 ? 64  TYR   A CE2   1 
ATOM   496  C  CZ    . TYR   A 1 67  ? 29.345 -22.702 14.719 1.00 31.94 ? 64  TYR   A CZ    1 
ATOM   497  O  OH    . TYR   A 1 67  ? 28.153 -23.249 14.341 1.00 32.24 ? 64  TYR   A OH    1 
ATOM   498  N  N     . SER   A 1 68  ? 30.675 -18.763 14.961 1.00 28.26 ? 65  SER   A N     1 
ATOM   499  C  CA    . SER   A 1 68  ? 29.270 -18.424 15.420 1.00 26.81 ? 65  SER   A CA    1 
ATOM   500  C  C     . SER   A 1 68  ? 28.139 -18.961 14.511 1.00 27.06 ? 65  SER   A C     1 
ATOM   501  O  O     . SER   A 1 68  ? 28.343 -18.850 13.340 1.00 31.37 ? 65  SER   A O     1 
ATOM   502  C  CB    . SER   A 1 68  ? 29.065 -16.962 15.600 1.00 27.81 ? 65  SER   A CB    1 
ATOM   503  O  OG    . SER   A 1 68  ? 27.732 -16.703 16.054 1.00 29.30 ? 65  SER   A OG    1 
ATOM   504  N  N     . ALA   A 1 69  ? 26.955 -19.391 15.043 1.00 26.65 ? 66  ALA   A N     1 
ATOM   505  C  CA    . ALA   A 1 69  ? 25.802 -19.922 14.286 1.00 25.27 ? 66  ALA   A CA    1 
ATOM   506  C  C     . ALA   A 1 69  ? 24.659 -18.911 14.243 1.00 24.64 ? 66  ALA   A C     1 
ATOM   507  O  O     . ALA   A 1 69  ? 23.642 -19.242 13.724 1.00 25.98 ? 66  ALA   A O     1 
ATOM   508  C  CB    . ALA   A 1 69  ? 25.296 -21.180 14.940 1.00 27.46 ? 66  ALA   A CB    1 
ATOM   509  N  N     . MET   A 1 70  ? 24.846 -17.745 14.857 1.00 26.85 ? 67  MET   A N     1 
ATOM   510  C  CA    . MET   A 1 70  ? 23.751 -16.752 15.006 1.00 25.27 ? 67  MET   A CA    1 
ATOM   511  C  C     . MET   A 1 70  ? 23.905 -15.530 14.101 1.00 22.51 ? 67  MET   A C     1 
ATOM   512  O  O     . MET   A 1 70  ? 23.051 -14.715 14.176 1.00 21.88 ? 67  MET   A O     1 
ATOM   513  C  CB    . MET   A 1 70  ? 23.727 -16.224 16.440 1.00 26.13 ? 67  MET   A CB    1 
ATOM   514  C  CG    . MET   A 1 70  ? 23.928 -17.309 17.464 1.00 30.49 ? 67  MET   A CG    1 
ATOM   515  S  SD    . MET   A 1 70  ? 22.637 -18.505 17.324 1.00 28.89 ? 67  MET   A SD    1 
ATOM   516  C  CE    . MET   A 1 70  ? 21.143 -17.533 17.436 1.00 29.77 ? 67  MET   A CE    1 
ATOM   517  N  N     . ARG   A 1 71  ? 24.905 -15.508 13.209 1.00 21.31 ? 68  ARG   A N     1 
ATOM   518  C  CA    . ARG   A 1 71  ? 25.136 -14.308 12.370 1.00 20.08 ? 68  ARG   A CA    1 
ATOM   519  C  C     . ARG   A 1 71  ? 23.941 -13.966 11.482 1.00 19.47 ? 68  ARG   A C     1 
ATOM   520  O  O     . ARG   A 1 71  ? 23.605 -12.843 11.428 1.00 19.77 ? 68  ARG   A O     1 
ATOM   521  C  CB    . ARG   A 1 71  ? 26.403 -14.434 11.508 1.00 23.12 ? 68  ARG   A CB    1 
ATOM   522  C  CG    . ARG   A 1 71  ? 27.675 -14.438 12.330 1.00 25.28 ? 68  ARG   A CG    1 
ATOM   523  C  CD    . ARG   A 1 71  ? 28.931 -13.876 11.721 1.00 24.40 ? 68  ARG   A CD    1 
ATOM   524  N  NE    . ARG   A 1 71  ? 29.995 -13.913 12.679 1.00 26.17 ? 68  ARG   A NE    1 
ATOM   525  C  CZ    . ARG   A 1 71  ? 30.735 -14.947 12.961 1.00 22.58 ? 68  ARG   A CZ    1 
ATOM   526  N  NH1   . ARG   A 1 71  ? 30.593 -16.056 12.274 1.00 27.47 ? 68  ARG   A NH1   1 
ATOM   527  N  NH2   . ARG   A 1 71  ? 31.665 -14.869 13.881 1.00 27.05 ? 68  ARG   A NH2   1 
ATOM   528  N  N     . ASP   A 1 72  ? 23.371 -14.930 10.778 1.00 20.81 ? 69  ASP   A N     1 
ATOM   529  C  CA    . ASP   A 1 72  ? 22.266 -14.547 9.914  1.00 21.09 ? 69  ASP   A CA    1 
ATOM   530  C  C     . ASP   A 1 72  ? 21.113 -13.974 10.733 1.00 20.15 ? 69  ASP   A C     1 
ATOM   531  O  O     . ASP   A 1 72  ? 20.521 -12.982 10.310 1.00 20.40 ? 69  ASP   A O     1 
ATOM   532  C  CB    . ASP   A 1 72  ? 21.796 -15.691 9.015  1.00 24.71 ? 69  ASP   A CB    1 
ATOM   533  C  CG    . ASP   A 1 72  ? 22.794 -16.153 7.968  1.00 26.10 ? 69  ASP   A CG    1 
ATOM   534  O  OD1   . ASP   A 1 72  ? 23.825 -15.474 7.758  1.00 27.01 ? 69  ASP   A OD1   1 
ATOM   535  O  OD2   . ASP   A 1 72  ? 22.520 -17.234 7.364  1.00 32.81 ? 69  ASP   A OD2   1 
ATOM   536  N  N     . GLN   A 1 73  ? 20.825 -14.594 11.870 1.00 19.13 ? 70  GLN   A N     1 
ATOM   537  C  CA    . GLN   A 1 73  ? 19.692 -14.123 12.708 1.00 20.26 ? 70  GLN   A CA    1 
ATOM   538  C  C     . GLN   A 1 73  ? 19.949 -12.730 13.283 1.00 19.49 ? 70  GLN   A C     1 
ATOM   539  O  O     . GLN   A 1 73  ? 19.090 -11.933 13.207 1.00 19.90 ? 70  GLN   A O     1 
ATOM   540  C  CB    . GLN   A 1 73  ? 19.405 -15.137 13.807 1.00 19.73 ? 70  GLN   A CB    1 
ATOM   541  C  CG    . GLN   A 1 73  ? 18.188 -14.735 14.633 1.00 19.11 ? 70  GLN   A CG    1 
ATOM   542  C  CD    . GLN   A 1 73  ? 16.930 -14.647 13.812 1.00 20.36 ? 70  GLN   A CD    1 
ATOM   543  O  OE1   . GLN   A 1 73  ? 16.419 -15.634 13.359 1.00 26.48 ? 70  GLN   A OE1   1 
ATOM   544  N  NE2   . GLN   A 1 73  ? 16.401 -13.469 13.672 1.00 20.65 ? 70  GLN   A NE2   1 
ATOM   545  N  N     . TYR   A 1 74  ? 21.142 -12.467 13.771 1.00 17.57 ? 71  TYR   A N     1 
ATOM   546  C  CA    . TYR   A 1 74  ? 21.368 -11.125 14.334 1.00 17.02 ? 71  TYR   A CA    1 
ATOM   547  C  C     . TYR   A 1 74  ? 21.311 -10.040 13.260 1.00 18.60 ? 71  TYR   A C     1 
ATOM   548  O  O     . TYR   A 1 74  ? 21.007 -8.960  13.518 1.00 18.48 ? 71  TYR   A O     1 
ATOM   549  C  CB    . TYR   A 1 74  ? 22.456 -11.114 15.401 1.00 17.83 ? 71  TYR   A CB    1 
ATOM   550  C  CG    . TYR   A 1 74  ? 23.889 -11.187 14.941 1.00 18.66 ? 71  TYR   A CG    1 
ATOM   551  C  CD1   . TYR   A 1 74  ? 24.398 -10.247 14.069 1.00 18.75 ? 71  TYR   A CD1   1 
ATOM   552  C  CD2   . TYR   A 1 74  ? 24.735 -12.151 15.436 1.00 19.15 ? 71  TYR   A CD2   1 
ATOM   553  C  CE1   . TYR   A 1 74  ? 25.726 -10.285 13.693 1.00 21.29 ? 71  TYR   A CE1   1 
ATOM   554  C  CE2   . TYR   A 1 74  ? 26.070 -12.189 15.088 1.00 20.56 ? 71  TYR   A CE2   1 
ATOM   555  C  CZ    . TYR   A 1 74  ? 26.555 -11.246 14.210 1.00 20.50 ? 71  TYR   A CZ    1 
ATOM   556  O  OH    . TYR   A 1 74  ? 27.860 -11.324 13.857 1.00 23.68 ? 71  TYR   A OH    1 
ATOM   557  N  N     . MET   A 1 75  ? 21.774 -10.393 12.050 1.00 17.61 ? 72  MET   A N     1 
ATOM   558  C  CA    . MET   A 1 75  ? 21.730 -9.421  10.929 1.00 17.80 ? 72  MET   A CA    1 
ATOM   559  C  C     . MET   A 1 75  ? 20.280 -9.196  10.511 1.00 19.60 ? 72  MET   A C     1 
ATOM   560  O  O     . MET   A 1 75  ? 19.957 -8.093  10.222 1.00 21.04 ? 72  MET   A O     1 
ATOM   561  C  CB    . MET   A 1 75  ? 22.629 -9.886  9.771  1.00 18.40 ? 72  MET   A CB    1 
ATOM   562  C  CG    . MET   A 1 75  ? 24.049 -9.904  10.185 1.00 17.50 ? 72  MET   A CG    1 
ATOM   563  S  SD    . MET   A 1 75  ? 25.235 -10.391 8.905  1.00 20.06 ? 72  MET   A SD    1 
ATOM   564  C  CE    . MET   A 1 75  ? 26.804 -10.206 9.725  1.00 20.17 ? 72  MET   A CE    1 
ATOM   565  N  N     . ARG   A 1 76  ? 19.455 -10.231 10.553 1.00 19.96 ? 73  ARG   A N     1 
ATOM   566  C  CA    . ARG   A 1 76  ? 18.022 -10.054 10.234 1.00 22.32 ? 73  ARG   A CA    1 
ATOM   567  C  C     . ARG   A 1 76  ? 17.336 -9.211  11.326 1.00 21.79 ? 73  ARG   A C     1 
ATOM   568  O  O     . ARG   A 1 76  ? 16.597 -8.337  10.979 1.00 22.97 ? 73  ARG   A O     1 
ATOM   569  C  CB    . ARG   A 1 76  ? 17.301 -11.395 10.198 1.00 24.78 ? 73  ARG   A CB    1 
ATOM   570  C  CG    . ARG   A 1 76  ? 17.292 -12.154 8.893  1.00 30.58 ? 73  ARG   A CG    1 
ATOM   571  C  CD    . ARG   A 1 76  ? 16.088 -13.069 8.946  1.00 33.98 ? 73  ARG   A CD    1 
ATOM   572  N  NE    . ARG   A 1 76  ? 16.263 -14.142 9.898  1.00 32.06 ? 73  ARG   A NE    1 
ATOM   573  C  CZ    . ARG   A 1 76  ? 17.064 -15.167 9.698  1.00 36.04 ? 73  ARG   A CZ    1 
ATOM   574  N  NH1   . ARG   A 1 76  ? 17.166 -16.117 10.609 1.00 33.49 ? 73  ARG   A NH1   1 
ATOM   575  N  NH2   . ARG   A 1 76  ? 17.759 -15.239 8.569  1.00 43.52 ? 73  ARG   A NH2   1 
ATOM   576  N  N     . THR   A 1 77  ? 17.651 -9.483  12.602 1.00 21.09 ? 74  THR   A N     1 
ATOM   577  C  CA    . THR   A 1 77  ? 16.975 -8.772  13.675 1.00 21.07 ? 74  THR   A CA    1 
ATOM   578  C  C     . THR   A 1 77  ? 17.516 -7.359  13.865 1.00 18.64 ? 74  THR   A C     1 
ATOM   579  O  O     . THR   A 1 77  ? 16.800 -6.443  14.280 1.00 19.49 ? 74  THR   A O     1 
ATOM   580  C  CB    . THR   A 1 77  ? 17.081 -9.574  14.969 1.00 21.46 ? 74  THR   A CB    1 
ATOM   581  O  OG1   . THR   A 1 77  ? 16.383 -10.794 14.716 1.00 24.27 ? 74  THR   A OG1   1 
ATOM   582  C  CG2   . THR   A 1 77  ? 16.479 -8.845  16.148 1.00 23.06 ? 74  THR   A CG2   1 
ATOM   583  N  N     . GLY   A 1 78  ? 18.820 -7.174  13.620 1.00 17.20 ? 75  GLY   A N     1 
ATOM   584  C  CA    . GLY   A 1 78  ? 19.472 -5.898  13.865 1.00 17.99 ? 75  GLY   A CA    1 
ATOM   585  C  C     . GLY   A 1 78  ? 18.875 -4.766  13.032 1.00 18.41 ? 75  GLY   A C     1 
ATOM   586  O  O     . GLY   A 1 78  ? 18.727 -4.870  11.816 1.00 19.15 ? 75  GLY   A O     1 
ATOM   587  N  N     . GLU   A 1 79  ? 18.621 -3.650  13.682 1.00 17.43 ? 76  GLU   A N     1 
ATOM   588  C  CA    . GLU   A 1 79  ? 18.084 -2.485  12.973 1.00 18.20 ? 76  GLU   A CA    1 
ATOM   589  C  C     . GLU   A 1 79  ? 19.224 -1.544  12.595 1.00 17.62 ? 76  GLU   A C     1 
ATOM   590  O  O     . GLU   A 1 79  ? 19.016 -0.773  11.702 1.00 20.38 ? 76  GLU   A O     1 
ATOM   591  C  CB    . GLU   A 1 79  ? 17.004 -1.792  13.800 1.00 19.44 ? 76  GLU   A CB    1 
ATOM   592  C  CG    . GLU   A 1 79  ? 15.820 -2.703  13.971 1.00 21.52 ? 76  GLU   A CG    1 
ATOM   593  C  CD    . GLU   A 1 79  ? 14.838 -2.385  15.099 1.00 25.18 ? 76  GLU   A CD    1 
ATOM   594  O  OE1   . GLU   A 1 79  ? 15.203 -1.758  16.087 1.00 23.94 ? 76  GLU   A OE1   1 
ATOM   595  O  OE2   . GLU   A 1 79  ? 13.753 -2.819  14.964 1.00 33.38 ? 76  GLU   A OE2   1 
ATOM   596  N  N     . GLY   A 1 80  ? 20.317 -1.553  13.344 1.00 15.92 ? 77  GLY   A N     1 
ATOM   597  C  CA    . GLY   A 1 80  ? 21.466 -0.687  13.015 1.00 16.43 ? 77  GLY   A CA    1 
ATOM   598  C  C     . GLY   A 1 80  ? 22.731 -1.371  13.433 1.00 18.41 ? 77  GLY   A C     1 
ATOM   599  O  O     . GLY   A 1 80  ? 22.692 -2.160  14.376 1.00 17.05 ? 77  GLY   A O     1 
ATOM   600  N  N     . PHE   A 1 81  ? 23.811 -1.185  12.676 1.00 17.54 ? 78  PHE   A N     1 
ATOM   601  C  CA    . PHE   A 1 81  ? 25.079 -1.880  12.950 1.00 16.32 ? 78  PHE   A CA    1 
ATOM   602  C  C     . PHE   A 1 81  ? 26.233 -0.919  13.187 1.00 18.61 ? 78  PHE   A C     1 
ATOM   603  O  O     . PHE   A 1 81  ? 26.453 0.009   12.424 1.00 17.64 ? 78  PHE   A O     1 
ATOM   604  C  CB    . PHE   A 1 81  ? 25.392 -2.832  11.786 1.00 17.31 ? 78  PHE   A CB    1 
ATOM   605  C  CG    . PHE   A 1 81  ? 24.335 -3.873  11.606 1.00 16.35 ? 78  PHE   A CG    1 
ATOM   606  C  CD1   . PHE   A 1 81  ? 23.160 -3.575  10.952 1.00 18.59 ? 78  PHE   A CD1   1 
ATOM   607  C  CD2   . PHE   A 1 81  ? 24.499 -5.129  12.124 1.00 17.81 ? 78  PHE   A CD2   1 
ATOM   608  C  CE1   . PHE   A 1 81  ? 22.137 -4.486  10.883 1.00 18.28 ? 78  PHE   A CE1   1 
ATOM   609  C  CE2   . PHE   A 1 81  ? 23.480 -6.044  12.031 1.00 19.08 ? 78  PHE   A CE2   1 
ATOM   610  C  CZ    . PHE   A 1 81  ? 22.322 -5.735  11.386 1.00 19.41 ? 78  PHE   A CZ    1 
ATOM   611  N  N     . LEU   A 1 82  ? 26.926 -1.151  14.283 1.00 16.94 ? 79  LEU   A N     1 
ATOM   612  C  CA    . LEU   A 1 82  ? 28.142 -0.413  14.604 1.00 16.71 ? 79  LEU   A CA    1 
ATOM   613  C  C     . LEU   A 1 82  ? 29.282 -1.261  14.034 1.00 17.38 ? 79  LEU   A C     1 
ATOM   614  O  O     . LEU   A 1 82  ? 29.509 -2.321  14.544 1.00 17.37 ? 79  LEU   A O     1 
ATOM   615  C  CB    . LEU   A 1 82  ? 28.238 -0.286  16.133 1.00 21.29 ? 79  LEU   A CB    1 
ATOM   616  C  CG    . LEU   A 1 82  ? 28.762 1.048   16.619 1.00 23.98 ? 79  LEU   A CG    1 
ATOM   617  C  CD1   . LEU   A 1 82  ? 27.895 2.210   16.212 1.00 21.39 ? 79  LEU   A CD1   1 
ATOM   618  C  CD2   . LEU   A 1 82  ? 29.009 1.004   18.112 1.00 21.17 ? 79  LEU   A CD2   1 
ATOM   619  N  N     . CYS   A 1 83  ? 29.855 -0.805  12.891 1.00 17.85 ? 80  CYS   A N     1 
ATOM   620  C  CA    . CYS   A 1 83  ? 30.896 -1.579  12.175 1.00 17.96 ? 80  CYS   A CA    1 
ATOM   621  C  C     . CYS   A 1 83  ? 32.221 -1.081  12.686 1.00 17.70 ? 80  CYS   A C     1 
ATOM   622  O  O     . CYS   A 1 83  ? 32.617 -0.011  12.363 1.00 17.92 ? 80  CYS   A O     1 
ATOM   623  C  CB    . CYS   A 1 83  ? 30.757 -1.348  10.676 1.00 18.99 ? 80  CYS   A CB    1 
ATOM   624  S  SG    . CYS   A 1 83  ? 29.240 -2.116  10.086 1.00 21.78 ? 80  CYS   A SG    1 
ATOM   625  N  N     . VAL   A 1 84  ? 32.782 -1.874  13.585 1.00 17.11 ? 81  VAL   A N     1 
ATOM   626  C  CA    . VAL   A 1 84  ? 33.994 -1.456  14.310 1.00 16.17 ? 81  VAL   A CA    1 
ATOM   627  C  C     . VAL   A 1 84  ? 35.289 -2.077  13.768 1.00 17.97 ? 81  VAL   A C     1 
ATOM   628  O  O     . VAL   A 1 84  ? 35.397 -3.244  13.683 1.00 18.69 ? 81  VAL   A O     1 
ATOM   629  C  CB    . VAL   A 1 84  ? 33.835 -1.813  15.816 1.00 15.98 ? 81  VAL   A CB    1 
ATOM   630  C  CG1   . VAL   A 1 84  ? 34.958 -1.245  16.629 1.00 16.09 ? 81  VAL   A CG1   1 
ATOM   631  C  CG2   . VAL   A 1 84  ? 32.473 -1.435  16.411 1.00 16.09 ? 81  VAL   A CG2   1 
ATOM   632  N  N     . PHE   A 1 85  ? 36.229 -1.201  13.508 1.00 17.96 ? 82  PHE   A N     1 
ATOM   633  C  CA    . PHE   A 1 85  ? 37.601 -1.675  13.258 1.00 18.44 ? 82  PHE   A CA    1 
ATOM   634  C  C     . PHE   A 1 85  ? 38.520 -1.025  14.289 1.00 20.09 ? 82  PHE   A C     1 
ATOM   635  O  O     . PHE   A 1 85  ? 38.093 -0.093  14.987 1.00 18.54 ? 82  PHE   A O     1 
ATOM   636  C  CB    . PHE   A 1 85  ? 38.059 -1.327  11.818 1.00 17.53 ? 82  PHE   A CB    1 
ATOM   637  C  CG    . PHE   A 1 85  ? 38.248 0.141   11.556 1.00 17.00 ? 82  PHE   A CG    1 
ATOM   638  C  CD1   . PHE   A 1 85  ? 37.188 0.926   11.187 1.00 18.15 ? 82  PHE   A CD1   1 
ATOM   639  C  CD2   . PHE   A 1 85  ? 39.479 0.748   11.668 1.00 18.15 ? 82  PHE   A CD2   1 
ATOM   640  C  CE1   . PHE   A 1 85  ? 37.330 2.271   10.945 1.00 17.78 ? 82  PHE   A CE1   1 
ATOM   641  C  CE2   . PHE   A 1 85  ? 39.629 2.095   11.393 1.00 19.79 ? 82  PHE   A CE2   1 
ATOM   642  C  CZ    . PHE   A 1 85  ? 38.563 2.852   11.013 1.00 19.51 ? 82  PHE   A CZ    1 
ATOM   643  N  N     . ALA   A 1 86  ? 39.736 -1.506  14.374 1.00 19.08 ? 83  ALA   A N     1 
ATOM   644  C  CA    . ALA   A 1 86  ? 40.688 -0.863  15.269 1.00 20.28 ? 83  ALA   A CA    1 
ATOM   645  C  C     . ALA   A 1 86  ? 41.737 -0.163  14.411 1.00 19.08 ? 83  ALA   A C     1 
ATOM   646  O  O     . ALA   A 1 86  ? 42.172 -0.745  13.416 1.00 20.34 ? 83  ALA   A O     1 
ATOM   647  C  CB    . ALA   A 1 86  ? 41.313 -1.914  16.155 1.00 21.00 ? 83  ALA   A CB    1 
ATOM   648  N  N     . ILE   A 1 87  ? 42.114 1.060   14.808 1.00 19.63 ? 84  ILE   A N     1 
ATOM   649  C  CA    . ILE   A 1 87  ? 43.021 1.908   14.042 1.00 20.79 ? 84  ILE   A CA    1 
ATOM   650  C  C     . ILE   A 1 87  ? 44.430 1.309   13.941 1.00 19.83 ? 84  ILE   A C     1 
ATOM   651  O  O     . ILE   A 1 87  ? 45.201 1.778   13.117 1.00 20.60 ? 84  ILE   A O     1 
ATOM   652  C  CB    . ILE   A 1 87  ? 43.017 3.377   14.519 1.00 21.39 ? 84  ILE   A CB    1 
ATOM   653  C  CG1   . ILE   A 1 87  ? 43.633 3.543   15.918 1.00 23.93 ? 84  ILE   A CG1   1 
ATOM   654  C  CG2   . ILE   A 1 87  ? 41.618 3.997   14.389 1.00 22.95 ? 84  ILE   A CG2   1 
ATOM   655  C  CD1   . ILE   A 1 87  ? 44.243 4.915   16.146 1.00 27.28 ? 84  ILE   A CD1   1 
ATOM   656  N  N     . ASN   A 1 88  ? 44.737 0.229   14.665 1.00 21.38 ? 85  ASN   A N     1 
ATOM   657  C  CA    . ASN   A 1 88  ? 46.036 -0.422  14.641 1.00 23.96 ? 85  ASN   A CA    1 
ATOM   658  C  C     . ASN   A 1 88  ? 45.953 -1.730  13.865 1.00 22.92 ? 85  ASN   A C     1 
ATOM   659  O  O     . ASN   A 1 88  ? 46.872 -2.540  13.941 1.00 23.98 ? 85  ASN   A O     1 
ATOM   660  C  CB    . ASN   A 1 88  ? 46.575 -0.684  16.066 1.00 23.80 ? 85  ASN   A CB    1 
ATOM   661  C  CG    . ASN   A 1 88  ? 45.775 -1.707  16.858 1.00 25.17 ? 85  ASN   A CG    1 
ATOM   662  O  OD1   . ASN   A 1 88  ? 44.598 -1.955  16.584 1.00 27.33 ? 85  ASN   A OD1   1 
ATOM   663  N  ND2   . ASN   A 1 88  ? 46.386 -2.323  17.864 1.00 23.49 ? 85  ASN   A ND2   1 
ATOM   664  N  N     . ASN   A 1 89  ? 44.849 -1.940  13.157 1.00 21.04 ? 86  ASN   A N     1 
ATOM   665  C  CA    . ASN   A 1 89  ? 44.613 -3.250  12.511 1.00 21.40 ? 86  ASN   A CA    1 
ATOM   666  C  C     . ASN   A 1 89  ? 43.998 -3.034  11.126 1.00 22.37 ? 86  ASN   A C     1 
ATOM   667  O  O     . ASN   A 1 89  ? 42.831 -2.917  10.972 1.00 20.66 ? 86  ASN   A O     1 
ATOM   668  C  CB    . ASN   A 1 89  ? 43.749 -4.149  13.392 1.00 22.32 ? 86  ASN   A CB    1 
ATOM   669  C  CG    . ASN   A 1 89  ? 43.512 -5.529  12.854 1.00 24.32 ? 86  ASN   A CG    1 
ATOM   670  O  OD1   . ASN   A 1 89  ? 43.749 -5.795  11.683 1.00 23.77 ? 86  ASN   A OD1   1 
ATOM   671  N  ND2   . ASN   A 1 89  ? 43.016 -6.421  13.683 1.00 28.07 ? 86  ASN   A ND2   1 
ATOM   672  N  N     . THR   A 1 90  ? 44.874 -3.038  10.106 1.00 22.15 ? 87  THR   A N     1 
ATOM   673  C  CA    . THR   A 1 90  ? 44.408 -2.750  8.717  1.00 21.40 ? 87  THR   A CA    1 
ATOM   674  C  C     . THR   A 1 90  ? 43.446 -3.819  8.241  1.00 20.09 ? 87  THR   A C     1 
ATOM   675  O  O     . THR   A 1 90  ? 42.546 -3.494  7.588  1.00 20.86 ? 87  THR   A O     1 
ATOM   676  C  CB    . THR   A 1 90  ? 45.575 -2.561  7.735  1.00 21.94 ? 87  THR   A CB    1 
ATOM   677  O  OG1   . THR   A 1 90  ? 46.278 -3.789  7.737  1.00 25.82 ? 87  THR   A OG1   1 
ATOM   678  C  CG2   . THR   A 1 90  ? 46.449 -1.404  8.116  1.00 22.58 ? 87  THR   A CG2   1 
ATOM   679  N  N     . LYS   A 1 91  ? 43.677 -5.058  8.604  1.00 19.76 ? 88  LYS   A N     1 
ATOM   680  C  CA    . LYS   A 1 91  ? 42.760 -6.116  8.162  1.00 21.76 ? 88  LYS   A CA    1 
ATOM   681  C  C     . LYS   A 1 91  ? 41.360 -5.888  8.757  1.00 20.16 ? 88  LYS   A C     1 
ATOM   682  O  O     . LYS   A 1 91  ? 40.401 -6.161  8.113  1.00 18.50 ? 88  LYS   A O     1 
ATOM   683  C  CB    . LYS   A 1 91  ? 43.321 -7.473  8.552  1.00 23.11 ? 88  LYS   A CB    1 
ATOM   684  C  CG    . LYS   A 1 91  ? 42.460 -8.618  8.104  1.00 27.04 ? 88  LYS   A CG    1 
ATOM   685  C  CD    . LYS   A 1 91  ? 43.039 -9.948  8.391  1.00 30.55 ? 88  LYS   A CD    1 
ATOM   686  C  CE    . LYS   A 1 91  ? 42.079 -11.088 8.161  1.00 37.90 ? 88  LYS   A CE    1 
ATOM   687  N  NZ    . LYS   A 1 91  ? 41.464 -11.021 6.823  1.00 39.83 ? 88  LYS   A NZ    1 
ATOM   688  N  N     . SER   A 1 92  ? 41.303 -5.397  10.012 1.00 18.53 ? 89  SER   A N     1 
ATOM   689  C  CA    . SER   A 1 92  ? 40.006 -5.187  10.632 1.00 18.47 ? 89  SER   A CA    1 
ATOM   690  C  C     . SER   A 1 92  ? 39.236 -4.107  9.867  1.00 18.79 ? 89  SER   A C     1 
ATOM   691  O  O     . SER   A 1 92  ? 38.015 -4.195  9.716  1.00 19.62 ? 89  SER   A O     1 
ATOM   692  C  CB    . SER   A 1 92  ? 40.202 -4.893  12.106 1.00 18.68 ? 89  SER   A CB    1 
ATOM   693  O  OG    . SER   A 1 92  ? 40.551 -3.543  12.349 1.00 17.07 ? 89  SER   A OG    1 
ATOM   694  N  N     . PHE   A 1 93  ? 39.971 -3.125  9.326  1.00 17.91 ? 90  PHE   A N     1 
ATOM   695  C  CA    . PHE   A 1 93  ? 39.385 -2.062  8.526  1.00 17.98 ? 90  PHE   A CA    1 
ATOM   696  C  C     . PHE   A 1 93  ? 39.013 -2.563  7.137  1.00 18.41 ? 90  PHE   A C     1 
ATOM   697  O  O     . PHE   A 1 93  ? 37.911 -2.310  6.659  1.00 18.29 ? 90  PHE   A O     1 
ATOM   698  C  CB    . PHE   A 1 93  ? 40.392 -0.916  8.373  1.00 19.41 ? 90  PHE   A CB    1 
ATOM   699  C  CG    . PHE   A 1 93  ? 39.970 0.159   7.400  1.00 18.51 ? 90  PHE   A CG    1 
ATOM   700  C  CD1   . PHE   A 1 93  ? 38.962 1.051   7.714  1.00 18.52 ? 90  PHE   A CD1   1 
ATOM   701  C  CD2   . PHE   A 1 93  ? 40.598 0.277   6.165  1.00 18.56 ? 90  PHE   A CD2   1 
ATOM   702  C  CE1   . PHE   A 1 93  ? 38.591 2.047   6.829  1.00 20.69 ? 90  PHE   A CE1   1 
ATOM   703  C  CE2   . PHE   A 1 93  ? 40.231 1.288   5.287  1.00 21.38 ? 90  PHE   A CE2   1 
ATOM   704  C  CZ    . PHE   A 1 93  ? 39.224 2.171   5.614  1.00 19.77 ? 90  PHE   A CZ    1 
ATOM   705  N  N     . GLU   A 1 94  ? 39.913 -3.327  6.513  1.00 18.68 ? 91  GLU   A N     1 
ATOM   706  C  CA    . GLU   A 1 94  ? 39.606 -3.814  5.168  1.00 19.09 ? 91  GLU   A CA    1 
ATOM   707  C  C     . GLU   A 1 94  ? 38.410 -4.749  5.215  1.00 19.26 ? 91  GLU   A C     1 
ATOM   708  O  O     . GLU   A 1 94  ? 37.600 -4.727  4.274  1.00 19.03 ? 91  GLU   A O     1 
ATOM   709  C  CB    . GLU   A 1 94  ? 40.819 -4.503  4.545  1.00 19.85 ? 91  GLU   A CB    1 
ATOM   710  C  CG    . GLU   A 1 94  ? 41.919 -3.498  4.243  1.00 22.53 ? 91  GLU   A CG    1 
ATOM   711  C  CD    . GLU   A 1 94  ? 41.595 -2.401  3.229  1.00 28.01 ? 91  GLU   A CD    1 
ATOM   712  O  OE1   . GLU   A 1 94  ? 40.723 -2.631  2.354  1.00 28.91 ? 91  GLU   A OE1   1 
ATOM   713  O  OE2   . GLU   A 1 94  ? 42.199 -1.287  3.325  1.00 38.24 ? 91  GLU   A OE2   1 
ATOM   714  N  N     . ASP   A 1 95  ? 38.309 -5.552  6.290  1.00 18.46 ? 92  ASP   A N     1 
ATOM   715  C  CA    . ASP   A 1 95  ? 37.230 -6.526  6.367  1.00 18.34 ? 92  ASP   A CA    1 
ATOM   716  C  C     . ASP   A 1 95  ? 35.842 -5.917  6.605  1.00 18.58 ? 92  ASP   A C     1 
ATOM   717  O  O     . ASP   A 1 95  ? 34.852 -6.627  6.437  1.00 18.84 ? 92  ASP   A O     1 
ATOM   718  C  CB    . ASP   A 1 95  ? 37.505 -7.651  7.359  1.00 21.80 ? 92  ASP   A CB    1 
ATOM   719  C  CG    . ASP   A 1 95  ? 38.593 -8.611  6.889  1.00 22.32 ? 92  ASP   A CG    1 
ATOM   720  O  OD1   . ASP   A 1 95  ? 38.951 -8.593  5.707  1.00 23.99 ? 92  ASP   A OD1   1 
ATOM   721  O  OD2   . ASP   A 1 95  ? 39.040 -9.374  7.730  1.00 25.89 ? 92  ASP   A OD2   1 
ATOM   722  N  N     . ILE   A 1 96  ? 35.771 -4.627  6.969  1.00 18.94 ? 93  ILE   A N     1 
ATOM   723  C  CA    . ILE   A 1 96  ? 34.493 -3.922  7.024  1.00 19.37 ? 93  ILE   A CA    1 
ATOM   724  C  C     . ILE   A 1 96  ? 33.738 -4.155  5.715  1.00 17.22 ? 93  ILE   A C     1 
ATOM   725  O  O     . ILE   A 1 96  ? 32.536 -4.283  5.737  1.00 17.56 ? 93  ILE   A O     1 
ATOM   726  C  CB    . ILE   A 1 96  ? 34.643 -2.405  7.290  1.00 21.12 ? 93  ILE   A CB    1 
ATOM   727  C  CG1   . ILE   A 1 96  ? 35.357 -2.120  8.615  1.00 21.30 ? 93  ILE   A CG1   1 
ATOM   728  C  CG2   . ILE   A 1 96  ? 33.285 -1.707  7.225  1.00 21.90 ? 93  ILE   A CG2   1 
ATOM   729  C  CD1   . ILE   A 1 96  ? 34.578 -2.564  9.844  1.00 23.33 ? 93  ILE   A CD1   1 
ATOM   730  N  N     . HIS   A 1 97  ? 34.448 -4.164  4.565  1.00 18.00 ? 94  HIS   A N     1 
ATOM   731  C  CA    . HIS   A 1 97  ? 33.794 -4.439  3.297  1.00 18.25 ? 94  HIS   A CA    1 
ATOM   732  C  C     . HIS   A 1 97  ? 32.941 -5.705  3.371  1.00 17.74 ? 94  HIS   A C     1 
ATOM   733  O  O     . HIS   A 1 97  ? 31.792 -5.715  2.930  1.00 17.58 ? 94  HIS   A O     1 
ATOM   734  C  CB    . HIS   A 1 97  ? 34.864 -4.626  2.201  1.00 17.88 ? 94  HIS   A CB    1 
ATOM   735  C  CG    . HIS   A 1 97  ? 34.312 -5.242  0.949  1.00 19.54 ? 94  HIS   A CG    1 
ATOM   736  N  ND1   . HIS   A 1 97  ? 33.857 -4.499  -0.123 1.00 19.50 ? 94  HIS   A ND1   1 
ATOM   737  C  CD2   . HIS   A 1 97  ? 34.084 -6.527  0.613  1.00 18.80 ? 94  HIS   A CD2   1 
ATOM   738  C  CE1   . HIS   A 1 97  ? 33.429 -5.316  -1.077 1.00 20.21 ? 94  HIS   A CE1   1 
ATOM   739  N  NE2   . HIS   A 1 97  ? 33.532 -6.571  -0.655 1.00 20.04 ? 94  HIS   A NE2   1 
ATOM   740  N  N     . HIS   A 1 98  ? 33.528 -6.777  3.942  1.00 17.99 ? 95  HIS   A N     1 
ATOM   741  C  CA    . HIS   A 1 98  ? 32.898 -8.073  3.969  1.00 19.73 ? 95  HIS   A CA    1 
ATOM   742  C  C     . HIS   A 1 98  ? 31.700 -8.052  4.913  1.00 19.23 ? 95  HIS   A C     1 
ATOM   743  O  O     . HIS   A 1 98  ? 30.659 -8.569  4.572  1.00 18.69 ? 95  HIS   A O     1 
ATOM   744  C  CB    . HIS   A 1 98  ? 33.922 -9.137  4.376  1.00 20.93 ? 95  HIS   A CB    1 
ATOM   745  C  CG    . HIS   A 1 98  ? 35.083 -9.273  3.440  1.00 23.55 ? 95  HIS   A CG    1 
ATOM   746  N  ND1   . HIS   A 1 98  ? 35.259 -10.404 2.647  1.00 28.90 ? 95  HIS   A ND1   1 
ATOM   747  C  CD2   . HIS   A 1 98  ? 36.149 -8.476  3.203  1.00 23.06 ? 95  HIS   A CD2   1 
ATOM   748  C  CE1   . HIS   A 1 98  ? 36.373 -10.281 1.950  1.00 26.50 ? 95  HIS   A CE1   1 
ATOM   749  N  NE2   . HIS   A 1 98  ? 36.932 -9.106  2.267  1.00 23.70 ? 95  HIS   A NE2   1 
ATOM   750  N  N     . TYR   A 1 99  ? 31.831 -7.414  6.074  1.00 19.76 ? 96  TYR   A N     1 
ATOM   751  C  CA    . TYR   A 1 99  ? 30.740 -7.437  7.027  1.00 18.65 ? 96  TYR   A CA    1 
ATOM   752  C  C     . TYR   A 1 99  ? 29.557 -6.647  6.488  1.00 18.99 ? 96  TYR   A C     1 
ATOM   753  O  O     . TYR   A 1 99  ? 28.429 -7.119  6.610  1.00 18.81 ? 96  TYR   A O     1 
ATOM   754  C  CB    . TYR   A 1 99  ? 31.200 -6.908  8.376  1.00 20.20 ? 96  TYR   A CB    1 
ATOM   755  C  CG    . TYR   A 1 99  ? 32.530 -7.444  8.852  1.00 22.19 ? 96  TYR   A CG    1 
ATOM   756  C  CD1   . TYR   A 1 99  ? 33.002 -8.704  8.487  1.00 20.59 ? 96  TYR   A CD1   1 
ATOM   757  C  CD2   . TYR   A 1 99  ? 33.346 -6.651  9.643  1.00 20.61 ? 96  TYR   A CD2   1 
ATOM   758  C  CE1   . TYR   A 1 99  ? 34.227 -9.180  8.947  1.00 22.63 ? 96  TYR   A CE1   1 
ATOM   759  C  CE2   . TYR   A 1 99  ? 34.567 -7.108  10.107 1.00 20.88 ? 96  TYR   A CE2   1 
ATOM   760  C  CZ    . TYR   A 1 99  ? 34.989 -8.376  9.778  1.00 21.54 ? 96  TYR   A CZ    1 
ATOM   761  O  OH    . TYR   A 1 99  ? 36.219 -8.792  10.213 1.00 26.20 ? 96  TYR   A OH    1 
ATOM   762  N  N     . ARG   A 1 100 ? 29.819 -5.444  5.992  1.00 18.16 ? 97  ARG   A N     1 
ATOM   763  C  CA    . ARG   A 1 100 ? 28.779 -4.598  5.372  1.00 19.12 ? 97  ARG   A CA    1 
ATOM   764  C  C     . ARG   A 1 100 ? 28.080 -5.371  4.254  1.00 18.74 ? 97  ARG   A C     1 
ATOM   765  O  O     . ARG   A 1 100 ? 26.887 -5.388  4.196  1.00 18.80 ? 97  ARG   A O     1 
ATOM   766  C  CB    . ARG   A 1 100 ? 29.402 -3.301  4.863  1.00 21.33 ? 97  ARG   A CB    1 
ATOM   767  C  CG    . ARG   A 1 100 ? 28.452 -2.447  4.050  1.00 23.55 ? 97  ARG   A CG    1 
ATOM   768  C  CD    . ARG   A 1 100 ? 29.015 -1.096  3.688  1.00 26.76 ? 97  ARG   A CD    1 
ATOM   769  N  NE    . ARG   A 1 100 ? 28.261 -0.373  2.696  1.00 29.93 ? 97  ARG   A NE    1 
ATOM   770  C  CZ    . ARG   A 1 100 ? 28.439 -0.475  1.381  1.00 35.67 ? 97  ARG   A CZ    1 
ATOM   771  N  NH1   . ARG   A 1 100 ? 29.333 -1.298  0.870  1.00 33.42 ? 97  ARG   A NH1   1 
ATOM   772  N  NH2   . ARG   A 1 100 ? 27.716 0.241   0.539  1.00 44.42 ? 97  ARG   A NH2   1 
ATOM   773  N  N     . GLU   A 1 101 ? 28.852 -6.017  3.385  1.00 18.70 ? 98  GLU   A N     1 
ATOM   774  C  CA    . GLU   A 1 101 ? 28.211 -6.773  2.285  1.00 20.91 ? 98  GLU   A CA    1 
ATOM   775  C  C     . GLU   A 1 101 ? 27.334 -7.903  2.830  1.00 20.99 ? 98  GLU   A C     1 
ATOM   776  O  O     . GLU   A 1 101 ? 26.303 -8.088  2.361  1.00 21.66 ? 98  GLU   A O     1 
ATOM   777  C  CB    . GLU   A 1 101 ? 29.301 -7.254  1.313  1.00 21.56 ? 98  GLU   A CB    1 
ATOM   778  C  CG    . GLU   A 1 101 ? 28.796 -8.178  0.232  1.00 26.08 ? 98  GLU   A CG    1 
ATOM   779  C  CD    . GLU   A 1 101 ? 29.913 -8.769  -0.633 1.00 27.70 ? 98  GLU   A CD    1 
ATOM   780  O  OE1   . GLU   A 1 101 ? 30.897 -8.113  -0.795 1.00 28.32 ? 98  GLU   A OE1   1 
ATOM   781  O  OE2   . GLU   A 1 101 ? 29.812 -9.915  -0.966 1.00 32.37 ? 98  GLU   A OE2   1 
ATOM   782  N  N     . GLN   A 1 102 ? 27.789 -8.586  3.868  1.00 19.92 ? 99  GLN   A N     1 
ATOM   783  C  CA    . GLN   A 1 102 ? 26.975 -9.697  4.415  1.00 21.62 ? 99  GLN   A CA    1 
ATOM   784  C  C     . GLN   A 1 102 ? 25.688 -9.161  5.076  1.00 19.60 ? 99  GLN   A C     1 
ATOM   785  O  O     . GLN   A 1 102 ? 24.676 -9.757  4.875  1.00 20.97 ? 99  GLN   A O     1 
ATOM   786  C  CB    . GLN   A 1 102 ? 27.875 -10.535 5.305  1.00 22.70 ? 99  GLN   A CB    1 
ATOM   787  C  CG    . GLN   A 1 102 ? 27.196 -11.769 5.847  1.00 25.44 ? 99  GLN   A CG    1 
ATOM   788  C  CD    . GLN   A 1 102 ? 26.746 -12.752 4.805  1.00 27.82 ? 99  GLN   A CD    1 
ATOM   789  O  OE1   . GLN   A 1 102 ? 27.203 -12.713 3.661  1.00 29.87 ? 99  GLN   A OE1   1 
ATOM   790  N  NE2   . GLN   A 1 102 ? 25.884 -13.666 5.193  1.00 31.49 ? 99  GLN   A NE2   1 
ATOM   791  N  N     . ILE   A 1 103 ? 25.770 -8.024  5.765  1.00 18.19 ? 100 ILE   A N     1 
ATOM   792  C  CA    . ILE   A 1 103 ? 24.579 -7.495  6.400  1.00 18.43 ? 100 ILE   A CA    1 
ATOM   793  C  C     . ILE   A 1 103 ? 23.571 -7.108  5.321  1.00 20.66 ? 100 ILE   A C     1 
ATOM   794  O  O     . ILE   A 1 103 ? 22.386 -7.372  5.463  1.00 21.39 ? 100 ILE   A O     1 
ATOM   795  C  CB    . ILE   A 1 103 ? 24.940 -6.283  7.271  1.00 19.04 ? 100 ILE   A CB    1 
ATOM   796  C  CG1   . ILE   A 1 103 ? 25.814 -6.704  8.452  1.00 18.78 ? 100 ILE   A CG1   1 
ATOM   797  C  CG2   . ILE   A 1 103 ? 23.703 -5.538  7.758  1.00 20.56 ? 100 ILE   A CG2   1 
ATOM   798  C  CD1   . ILE   A 1 103 ? 26.575 -5.542  9.045  1.00 19.46 ? 100 ILE   A CD1   1 
ATOM   799  N  N     . LYS   A 1 104 ? 24.051 -6.434  4.277  1.00 20.24 ? 101 LYS   A N     1 
ATOM   800  C  CA    . LYS   A 1 104 ? 23.138 -5.988  3.219  1.00 21.04 ? 101 LYS   A CA    1 
ATOM   801  C  C     . LYS   A 1 104 ? 22.511 -7.197  2.525  1.00 20.65 ? 101 LYS   A C     1 
ATOM   802  O  O     . LYS   A 1 104 ? 21.336 -7.170  2.185  1.00 23.24 ? 101 LYS   A O     1 
ATOM   803  C  CB    . LYS   A 1 104 ? 23.884 -5.077  2.236  1.00 21.63 ? 101 LYS   A CB    1 
ATOM   804  C  CG    . LYS   A 1 104 ? 24.196 -3.694  2.785  1.00 23.44 ? 101 LYS   A CG    1 
ATOM   805  C  CD    . LYS   A 1 104 ? 24.675 -2.628  1.820  1.00 31.39 ? 101 LYS   A CD    1 
ATOM   806  C  CE    . LYS   A 1 104 ? 25.377 -3.136  0.580  1.00 34.71 ? 101 LYS   A CE    1 
ATOM   807  N  NZ    . LYS   A 1 104 ? 25.422 -2.066  -0.445 1.00 37.38 ? 101 LYS   A NZ    1 
ATOM   808  N  N     . ARG   A 1 105 ? 23.292 -8.272  2.356  1.00 22.20 ? 102 ARG   A N     1 
ATOM   809  C  CA    . ARG   A 1 105 ? 22.828 -9.493  1.721  1.00 24.31 ? 102 ARG   A CA    1 
ATOM   810  C  C     . ARG   A 1 105 ? 21.724 -10.146 2.550  1.00 21.93 ? 102 ARG   A C     1 
ATOM   811  O  O     . ARG   A 1 105 ? 20.650 -10.398 2.023  1.00 24.53 ? 102 ARG   A O     1 
ATOM   812  C  CB    . ARG   A 1 105 ? 23.970 -10.478 1.484  1.00 26.14 ? 102 ARG   A CB    1 
ATOM   813  C  CG    . ARG   A 1 105 ? 23.521 -11.836 0.966  1.00 32.49 ? 102 ARG   A CG    1 
ATOM   814  C  CD    . ARG   A 1 105 ? 24.676 -12.732 0.566  1.00 38.03 ? 102 ARG   A CD    1 
ATOM   815  N  NE    . ARG   A 1 105 ? 25.530 -12.049 -0.399 1.00 39.31 ? 102 ARG   A NE    1 
ATOM   816  C  CZ    . ARG   A 1 105 ? 26.774 -11.627 -0.169 1.00 36.74 ? 102 ARG   A CZ    1 
ATOM   817  N  NH1   . ARG   A 1 105 ? 27.438 -11.009 -1.130 1.00 34.90 ? 102 ARG   A NH1   1 
ATOM   818  N  NH2   . ARG   A 1 105 ? 27.350 -11.819 1.007  1.00 38.58 ? 102 ARG   A NH2   1 
ATOM   819  N  N     . VAL   A 1 106 ? 21.991 -10.411 3.842  1.00 21.86 ? 103 VAL   A N     1 
ATOM   820  C  CA    . VAL   A 1 106 ? 21.014 -11.011 4.728  1.00 25.03 ? 103 VAL   A CA    1 
ATOM   821  C  C     . VAL   A 1 106 ? 19.735 -10.187 4.776  1.00 23.59 ? 103 VAL   A C     1 
ATOM   822  O  O     . VAL   A 1 106 ? 18.644 -10.752 4.814  1.00 26.41 ? 103 VAL   A O     1 
ATOM   823  C  CB    . VAL   A 1 106 ? 21.600 -11.176 6.140  1.00 23.89 ? 103 VAL   A CB    1 
ATOM   824  C  CG1   . VAL   A 1 106 ? 20.501 -11.528 7.149  1.00 25.43 ? 103 VAL   A CG1   1 
ATOM   825  C  CG2   . VAL   A 1 106 ? 22.716 -12.209 6.090  1.00 22.85 ? 103 VAL   A CG2   1 
ATOM   826  N  N     . LYS   A 1 107 ? 19.854 -8.857  4.821  1.00 22.79 ? 104 LYS   A N     1 
ATOM   827  C  CA    . LYS   A 1 107 ? 18.682 -8.021  5.054  1.00 28.57 ? 104 LYS   A CA    1 
ATOM   828  C  C     . LYS   A 1 107 ? 18.008 -7.691  3.719  1.00 27.71 ? 104 LYS   A C     1 
ATOM   829  O  O     . LYS   A 1 107 ? 16.920 -7.124  3.721  1.00 30.04 ? 104 LYS   A O     1 
ATOM   830  C  CB    . LYS   A 1 107 ? 19.043 -6.786  5.894  1.00 24.77 ? 104 LYS   A CB    1 
ATOM   831  C  CG    . LYS   A 1 107 ? 19.614 -7.098  7.275  1.00 24.73 ? 104 LYS   A CG    1 
ATOM   832  C  CD    . LYS   A 1 107 ? 19.821 -5.875  8.137  1.00 24.74 ? 104 LYS   A CD    1 
ATOM   833  C  CE    . LYS   A 1 107 ? 18.527 -5.240  8.588  1.00 23.83 ? 104 LYS   A CE    1 
ATOM   834  N  NZ    . LYS   A 1 107 ? 17.798 -6.179  9.480  1.00 23.72 ? 104 LYS   A NZ    1 
ATOM   835  N  N     . ASP   A 1 108 ? 18.631 -8.123  2.604  1.00 27.89 ? 105 ASP   A N     1 
ATOM   836  C  CA    . ASP   A 1 108 ? 18.163 -7.877  1.245  1.00 29.35 ? 105 ASP   A CA    1 
ATOM   837  C  C     . ASP   A 1 108 ? 17.896 -6.384  1.054  1.00 30.68 ? 105 ASP   A C     1 
ATOM   838  O  O     . ASP   A 1 108 ? 16.856 -5.993  0.524  1.00 35.36 ? 105 ASP   A O     1 
ATOM   839  C  CB    . ASP   A 1 108 ? 16.925 -8.722  0.905  1.00 31.43 ? 105 ASP   A CB    1 
ATOM   840  C  CG    . ASP   A 1 108 ? 16.614 -8.788  -0.587 1.00 34.49 ? 105 ASP   A CG    1 
ATOM   841  O  OD1   . ASP   A 1 108 ? 17.558 -8.644  -1.387 1.00 34.74 ? 105 ASP   A OD1   1 
ATOM   842  O  OD2   . ASP   A 1 108 ? 15.420 -8.971  -0.939 1.00 40.55 ? 105 ASP   A OD2   1 
ATOM   843  N  N     . SER   A 1 109 ? 18.850 -5.541  1.457  1.00 28.42 ? 106 SER   A N     1 
ATOM   844  C  CA    . SER   A 1 109 ? 18.641 -4.102  1.440  1.00 29.84 ? 106 SER   A CA    1 
ATOM   845  C  C     . SER   A 1 109 ? 19.959 -3.388  1.156  1.00 29.70 ? 106 SER   A C     1 
ATOM   846  O  O     . SER   A 1 109 ? 20.993 -3.755  1.710  1.00 32.58 ? 106 SER   A O     1 
ATOM   847  C  CB    . SER   A 1 109 ? 18.042 -3.655  2.758  1.00 31.69 ? 106 SER   A CB    1 
ATOM   848  O  OG    . SER   A 1 109 ? 17.759 -2.265  2.736  1.00 38.02 ? 106 SER   A OG    1 
ATOM   849  N  N     . GLU   A 1 110 ? 19.907 -2.349  0.317  1.00 32.74 ? 107 GLU   A N     1 
ATOM   850  C  CA    . GLU   A 1 110 ? 21.108 -1.587  0.016  1.00 35.39 ? 107 GLU   A CA    1 
ATOM   851  C  C     . GLU   A 1 110 ? 21.291 -0.482  1.055  1.00 34.58 ? 107 GLU   A C     1 
ATOM   852  O  O     . GLU   A 1 110 ? 22.380 0.078   1.202  1.00 36.23 ? 107 GLU   A O     1 
ATOM   853  C  CB    . GLU   A 1 110 ? 21.076 -1.082  -1.427 1.00 39.40 ? 107 GLU   A CB    1 
ATOM   854  C  CG    . GLU   A 1 110 ? 21.320 -2.188  -2.438 0.00 27.00 ? 107 GLU   A CG    1 
ATOM   855  C  CD    . GLU   A 1 110 ? 21.421 -1.752  -3.889 0.00 27.00 ? 107 GLU   A CD    1 
ATOM   856  O  OE1   . GLU   A 1 110 ? 21.158 -0.566  -4.176 0.00 27.00 ? 107 GLU   A OE1   1 
ATOM   857  O  OE2   . GLU   A 1 110 ? 21.764 -2.603  -4.733 0.00 27.00 ? 107 GLU   A OE2   1 
ATOM   858  N  N     . ASP   A 1 111 ? 20.208 -0.203  1.789  1.00 30.76 ? 108 ASP   A N     1 
ATOM   859  C  CA    . ASP   A 1 111 ? 20.174 0.829   2.808  1.00 30.86 ? 108 ASP   A CA    1 
ATOM   860  C  C     . ASP   A 1 111 ? 19.902 0.140   4.135  1.00 27.89 ? 108 ASP   A C     1 
ATOM   861  O  O     . ASP   A 1 111 ? 18.784 -0.303  4.384  1.00 35.48 ? 108 ASP   A O     1 
ATOM   862  C  CB    . ASP   A 1 111 ? 19.030 1.819   2.557  1.00 36.32 ? 108 ASP   A CB    1 
ATOM   863  C  CG    . ASP   A 1 111 ? 19.355 2.878   1.516  1.00 45.35 ? 108 ASP   A CG    1 
ATOM   864  O  OD1   . ASP   A 1 111 ? 20.065 3.849   1.862  1.00 51.43 ? 108 ASP   A OD1   1 
ATOM   865  O  OD2   . ASP   A 1 111 ? 18.904 2.720   0.360  1.00 52.11 ? 108 ASP   A OD2   1 
ATOM   866  N  N     . VAL   A 1 112 ? 20.958 -0.002  4.943  1.00 23.80 ? 109 VAL   A N     1 
ATOM   867  C  CA    . VAL   A 1 112 ? 20.845 -0.509  6.299  1.00 20.21 ? 109 VAL   A CA    1 
ATOM   868  C  C     . VAL   A 1 112 ? 21.552 0.510   7.184  1.00 20.88 ? 109 VAL   A C     1 
ATOM   869  O  O     . VAL   A 1 112 ? 22.707 0.851   6.902  1.00 19.11 ? 109 VAL   A O     1 
ATOM   870  C  CB    . VAL   A 1 112 ? 21.536 -1.877  6.460  1.00 21.57 ? 109 VAL   A CB    1 
ATOM   871  C  CG1   . VAL   A 1 112 ? 21.435 -2.379  7.897  1.00 21.32 ? 109 VAL   A CG1   1 
ATOM   872  C  CG2   . VAL   A 1 112 ? 20.983 -2.913  5.500  1.00 22.89 ? 109 VAL   A CG2   1 
ATOM   873  N  N     . PRO   A 1 113 ? 20.934 0.978   8.299  1.00 18.36 ? 110 PRO   A N     1 
ATOM   874  C  CA    . PRO   A 1 113 ? 21.572 1.921   9.209  1.00 17.53 ? 110 PRO   A CA    1 
ATOM   875  C  C     . PRO   A 1 113 ? 22.868 1.351   9.758  1.00 18.08 ? 110 PRO   A C     1 
ATOM   876  O  O     . PRO   A 1 113 ? 22.863 0.250   10.303 1.00 18.43 ? 110 PRO   A O     1 
ATOM   877  C  CB    . PRO   A 1 113 ? 20.546 2.126   10.327 1.00 17.29 ? 110 PRO   A CB    1 
ATOM   878  C  CG    . PRO   A 1 113 ? 19.247 1.917   9.568  1.00 18.39 ? 110 PRO   A CG    1 
ATOM   879  C  CD    . PRO   A 1 113 ? 19.521 0.733   8.679  1.00 18.30 ? 110 PRO   A CD    1 
ATOM   880  N  N     . MET   A 1 114 ? 23.954 2.104   9.571  1.00 16.77 ? 111 MET   A N     1 
ATOM   881  C  CA    . MET   A 1 114 ? 25.299 1.690   9.960  1.00 17.96 ? 111 MET   A CA    1 
ATOM   882  C  C     . MET   A 1 114 ? 26.108 2.924   10.321 1.00 17.31 ? 111 MET   A C     1 
ATOM   883  O  O     . MET   A 1 114 ? 25.904 3.993   9.748  1.00 18.31 ? 111 MET   A O     1 
ATOM   884  C  CB    . MET   A 1 114 ? 26.017 0.958   8.806  1.00 21.19 ? 111 MET   A CB    1 
ATOM   885  C  CG    . MET   A 1 114 ? 25.403 -0.378  8.378  1.00 21.32 ? 111 MET   A CG    1 
ATOM   886  S  SD    . MET   A 1 114 ? 26.582 -1.366  7.393  1.00 26.54 ? 111 MET   A SD    1 
ATOM   887  C  CE    . MET   A 1 114 ? 25.474 -2.518  6.597  1.00 27.73 ? 111 MET   A CE    1 
ATOM   888  N  N     . VAL   A 1 115 ? 27.083 2.735   11.229 1.00 17.78 ? 112 VAL   A N     1 
ATOM   889  C  CA    . VAL   A 1 115 ? 28.093 3.725   11.552 1.00 17.49 ? 112 VAL   A CA    1 
ATOM   890  C  C     . VAL   A 1 115 ? 29.437 3.002   11.525 1.00 18.31 ? 112 VAL   A C     1 
ATOM   891  O  O     . VAL   A 1 115 ? 29.579 1.897   12.068 1.00 17.24 ? 112 VAL   A O     1 
ATOM   892  C  CB    . VAL   A 1 115 ? 27.842 4.392   12.926 1.00 17.93 ? 112 VAL   A CB    1 
ATOM   893  C  CG1   . VAL   A 1 115 ? 29.054 5.248   13.323 1.00 19.52 ? 112 VAL   A CG1   1 
ATOM   894  C  CG2   . VAL   A 1 115 ? 26.542 5.181   12.982 1.00 20.65 ? 112 VAL   A CG2   1 
ATOM   895  N  N     . LEU   A 1 116 ? 30.397 3.595   10.832 1.00 16.70 ? 113 LEU   A N     1 
ATOM   896  C  CA    . LEU   A 1 116 ? 31.768 3.079   10.845 1.00 17.40 ? 113 LEU   A CA    1 
ATOM   897  C  C     . LEU   A 1 116 ? 32.504 3.637   12.060 1.00 17.74 ? 113 LEU   A C     1 
ATOM   898  O  O     . LEU   A 1 116 ? 32.498 4.840   12.239 1.00 18.54 ? 113 LEU   A O     1 
ATOM   899  C  CB    . LEU   A 1 116 ? 32.443 3.517   9.539  1.00 17.60 ? 113 LEU   A CB    1 
ATOM   900  C  CG    . LEU   A 1 116 ? 33.880 3.050   9.381  1.00 17.64 ? 113 LEU   A CG    1 
ATOM   901  C  CD1   . LEU   A 1 116 ? 33.940 1.543   9.211  1.00 18.54 ? 113 LEU   A CD1   1 
ATOM   902  C  CD2   . LEU   A 1 116 ? 34.590 3.755   8.234  1.00 18.95 ? 113 LEU   A CD2   1 
ATOM   903  N  N     . VAL   A 1 117 ? 33.084 2.762   12.882 1.00 16.01 ? 114 VAL   A N     1 
ATOM   904  C  CA    . VAL   A 1 117 ? 33.784 3.193   14.081 1.00 16.75 ? 114 VAL   A CA    1 
ATOM   905  C  C     . VAL   A 1 117 ? 35.229 2.693   14.035 1.00 16.70 ? 114 VAL   A C     1 
ATOM   906  O  O     . VAL   A 1 117 ? 35.448 1.492   13.871 1.00 18.05 ? 114 VAL   A O     1 
ATOM   907  C  CB    . VAL   A 1 117 ? 33.071 2.628   15.334 1.00 18.35 ? 114 VAL   A CB    1 
ATOM   908  C  CG1   . VAL   A 1 117 ? 33.853 2.978   16.605 1.00 19.34 ? 114 VAL   A CG1   1 
ATOM   909  C  CG2   . VAL   A 1 117 ? 31.604 3.045   15.445 1.00 17.28 ? 114 VAL   A CG2   1 
ATOM   910  N  N     . GLY   A 1 118 ? 36.180 3.630   14.126 1.00 18.93 ? 115 GLY   A N     1 
ATOM   911  C  CA    . GLY   A 1 118 ? 37.585 3.278   14.290 1.00 17.23 ? 115 GLY   A CA    1 
ATOM   912  C  C     . GLY   A 1 118 ? 37.943 3.383   15.776 1.00 18.97 ? 115 GLY   A C     1 
ATOM   913  O  O     . GLY   A 1 118 ? 37.989 4.490   16.296 1.00 20.93 ? 115 GLY   A O     1 
ATOM   914  N  N     . ASN   A 1 119 ? 38.069 2.224   16.416 1.00 17.45 ? 116 ASN   A N     1 
ATOM   915  C  CA    . ASN   A 1 119 ? 38.312 2.189   17.850 1.00 19.44 ? 116 ASN   A CA    1 
ATOM   916  C  C     . ASN   A 1 119 ? 39.819 2.124   18.127 1.00 19.54 ? 116 ASN   A C     1 
ATOM   917  O  O     . ASN   A 1 119 ? 40.640 1.913   17.234 1.00 20.42 ? 116 ASN   A O     1 
ATOM   918  C  CB    . ASN   A 1 119 ? 37.556 1.021   18.492 1.00 18.21 ? 116 ASN   A CB    1 
ATOM   919  C  CG    . ASN   A 1 119 ? 37.625 1.059   20.013 1.00 18.16 ? 116 ASN   A CG    1 
ATOM   920  O  OD1   . ASN   A 1 119 ? 37.414 2.111   20.599 1.00 18.75 ? 116 ASN   A OD1   1 
ATOM   921  N  ND2   . ASN   A 1 119 ? 37.908 -0.069  20.608 1.00 18.81 ? 116 ASN   A ND2   1 
ATOM   922  N  N     . LYS   A 1 120 ? 40.173 2.307   19.405 1.00 20.43 ? 117 LYS   A N     1 
ATOM   923  C  CA    . LYS   A 1 120 ? 41.548 2.319   19.906 1.00 21.41 ? 117 LYS   A CA    1 
ATOM   924  C  C     . LYS   A 1 120 ? 42.315 3.556   19.431 1.00 23.43 ? 117 LYS   A C     1 
ATOM   925  O  O     . LYS   A 1 120 ? 43.537 3.471   19.256 1.00 23.17 ? 117 LYS   A O     1 
ATOM   926  C  CB    . LYS   A 1 120 ? 42.301 1.033   19.580 1.00 21.83 ? 117 LYS   A CB    1 
ATOM   927  C  CG    . LYS   A 1 120 ? 41.583 -0.258  19.910 1.00 22.32 ? 117 LYS   A CG    1 
ATOM   928  C  CD    . LYS   A 1 120 ? 42.499 -1.382  20.155 1.00 22.33 ? 117 LYS   A CD    1 
ATOM   929  C  CE    . LYS   A 1 120 ? 41.758 -2.673  20.416 1.00 23.80 ? 117 LYS   A CE    1 
ATOM   930  N  NZ    . LYS   A 1 120 ? 42.679 -3.791  20.676 1.00 27.41 ? 117 LYS   A NZ    1 
ATOM   931  N  N     . SER   A 1 121 ? 41.639 4.708   19.413 1.00 22.22 ? 118 SER   A N     1 
ATOM   932  C  CA    . SER   A 1 121 ? 42.194 5.963   18.923 1.00 24.68 ? 118 SER   A CA    1 
ATOM   933  C  C     . SER   A 1 121 ? 43.272 6.475   19.868 1.00 26.48 ? 118 SER   A C     1 
ATOM   934  O  O     . SER   A 1 121 ? 44.013 7.395   19.511 1.00 27.42 ? 118 SER   A O     1 
ATOM   935  C  CB    . SER   A 1 121 ? 41.156 7.028   18.672 1.00 25.63 ? 118 SER   A CB    1 
ATOM   936  O  OG    . SER   A 1 121 ? 40.586 7.525   19.887 1.00 26.98 ? 118 SER   A OG    1 
ATOM   937  N  N     . ASP   A 1 122 ? 43.354 5.855   21.041 1.00 23.59 ? 119 ASP   A N     1 
ATOM   938  C  CA    . ASP   A 1 122 ? 44.369 6.208   22.016 1.00 25.03 ? 119 ASP   A CA    1 
ATOM   939  C  C     . ASP   A 1 122 ? 45.735 5.644   21.633 1.00 24.26 ? 119 ASP   A C     1 
ATOM   940  O  O     . ASP   A 1 122 ? 46.736 6.085   22.197 1.00 28.82 ? 119 ASP   A O     1 
ATOM   941  C  CB    . ASP   A 1 122 ? 43.965 5.719   23.409 1.00 25.59 ? 119 ASP   A CB    1 
ATOM   942  C  CG    . ASP   A 1 122 ? 43.708 4.229   23.449 1.00 22.39 ? 119 ASP   A CG    1 
ATOM   943  O  OD1   . ASP   A 1 122 ? 42.620 3.798   22.937 1.00 25.19 ? 119 ASP   A OD1   1 
ATOM   944  O  OD2   . ASP   A 1 122 ? 44.604 3.493   23.900 1.00 24.73 ? 119 ASP   A OD2   1 
ATOM   945  N  N     . LEU   A 1 123 ? 45.793 4.632   20.759 1.00 24.54 ? 120 LEU   A N     1 
ATOM   946  C  CA    . LEU   A 1 123 ? 47.027 3.910   20.495 1.00 23.55 ? 120 LEU   A CA    1 
ATOM   947  C  C     . LEU   A 1 123 ? 47.886 4.663   19.498 1.00 25.95 ? 120 LEU   A C     1 
ATOM   948  O  O     . LEU   A 1 123 ? 47.386 5.018   18.430 1.00 27.23 ? 120 LEU   A O     1 
ATOM   949  C  CB    . LEU   A 1 123 ? 46.758 2.506   19.954 1.00 25.71 ? 120 LEU   A CB    1 
ATOM   950  C  CG    . LEU   A 1 123 ? 46.245 1.470   20.944 1.00 24.83 ? 120 LEU   A CG    1 
ATOM   951  C  CD1   . LEU   A 1 123 ? 46.101 0.127   20.275 1.00 24.59 ? 120 LEU   A CD1   1 
ATOM   952  C  CD2   . LEU   A 1 123 ? 47.201 1.293   22.104 1.00 24.16 ? 120 LEU   A CD2   1 
ATOM   953  N  N     . PRO   A 1 124 ? 49.208 4.840   19.776 1.00 22.29 ? 121 PRO   A N     1 
ATOM   954  C  CA    . PRO   A 1 124 ? 50.096 5.510   18.807 1.00 24.43 ? 121 PRO   A CA    1 
ATOM   955  C  C     . PRO   A 1 124 ? 50.394 4.651   17.583 1.00 24.82 ? 121 PRO   A C     1 
ATOM   956  O  O     . PRO   A 1 124 ? 50.829 5.148   16.548 1.00 27.85 ? 121 PRO   A O     1 
ATOM   957  C  CB    . PRO   A 1 124 ? 51.379 5.792   19.619 1.00 25.47 ? 121 PRO   A CB    1 
ATOM   958  C  CG    . PRO   A 1 124 ? 51.342 4.827   20.815 1.00 26.19 ? 121 PRO   A CG    1 
ATOM   959  C  CD    . PRO   A 1 124 ? 49.885 4.431   21.015 1.00 24.19 ? 121 PRO   A CD    1 
ATOM   960  N  N     . SER   A 1 125 ? 50.188 3.342   17.705 1.00 22.73 ? 122 SER   A N     1 
ATOM   961  C  CA    . SER   A 1 125 ? 50.582 2.357   16.706 1.00 23.26 ? 122 SER   A CA    1 
ATOM   962  C  C     . SER   A 1 125 ? 49.521 2.228   15.602 1.00 23.24 ? 122 SER   A C     1 
ATOM   963  O  O     . SER   A 1 125 ? 49.100 1.122   15.254 1.00 25.39 ? 122 SER   A O     1 
ATOM   964  C  CB    . SER   A 1 125 ? 50.884 1.055   17.388 1.00 25.75 ? 122 SER   A CB    1 
ATOM   965  O  OG    . SER   A 1 125 ? 49.823 0.688   18.274 1.00 26.49 ? 122 SER   A OG    1 
ATOM   966  N  N     . ARG   A 1 126 ? 49.151 3.386   15.064 1.00 23.16 ? 123 ARG   A N     1 
ATOM   967  C  CA    . ARG   A 1 126 ? 48.084 3.529   14.078 1.00 22.73 ? 123 ARG   A CA    1 
ATOM   968  C  C     . ARG   A 1 126 ? 48.563 3.063   12.703 1.00 25.03 ? 123 ARG   A C     1 
ATOM   969  O  O     . ARG   A 1 126 ? 49.594 3.551   12.197 1.00 26.41 ? 123 ARG   A O     1 
ATOM   970  C  CB    . ARG   A 1 126 ? 47.672 4.995   13.983 1.00 23.92 ? 123 ARG   A CB    1 
ATOM   971  C  CG    . ARG   A 1 126 ? 46.709 5.305   12.840 1.00 24.99 ? 123 ARG   A CG    1 
ATOM   972  C  CD    . ARG   A 1 126 ? 46.338 6.761   12.706 1.00 24.35 ? 123 ARG   A CD    1 
ATOM   973  N  NE    . ARG   A 1 126 ? 45.475 7.358   13.725 1.00 29.78 ? 123 ARG   A NE    1 
ATOM   974  C  CZ    . ARG   A 1 126 ? 44.140 7.327   13.726 1.00 29.15 ? 123 ARG   A CZ    1 
ATOM   975  N  NH1   . ARG   A 1 126 ? 43.468 6.727   12.753 1.00 27.22 ? 123 ARG   A NH1   1 
ATOM   976  N  NH2   . ARG   A 1 126 ? 43.486 7.904   14.716 1.00 32.39 ? 123 ARG   A NH2   1 
ATOM   977  N  N     . THR   A 1 127 ? 47.765 2.171   12.082 1.00 21.81 ? 124 THR   A N     1 
ATOM   978  C  CA    . THR   A 1 127 ? 48.044 1.711   10.726 1.00 21.00 ? 124 THR   A CA    1 
ATOM   979  C  C     . THR   A 1 127 ? 46.940 2.095   9.732  1.00 24.64 ? 124 THR   A C     1 
ATOM   980  O  O     . THR   A 1 127 ? 47.130 1.873   8.535  1.00 27.62 ? 124 THR   A O     1 
ATOM   981  C  CB    . THR   A 1 127 ? 48.308 0.201   10.700 1.00 23.67 ? 124 THR   A CB    1 
ATOM   982  O  OG1   . THR   A 1 127 ? 47.138 -0.408  11.254 1.00 24.39 ? 124 THR   A OG1   1 
ATOM   983  C  CG2   . THR   A 1 127 ? 49.522 -0.197  11.522 1.00 24.80 ? 124 THR   A CG2   1 
ATOM   984  N  N     . VAL   A 1 128 ? 45.816 2.629   10.200 1.00 22.82 ? 125 VAL   A N     1 
ATOM   985  C  CA    . VAL   A 1 128 ? 44.671 3.079   9.367  1.00 22.73 ? 125 VAL   A CA    1 
ATOM   986  C  C     . VAL   A 1 128 ? 44.526 4.568   9.566  1.00 22.40 ? 125 VAL   A C     1 
ATOM   987  O  O     . VAL   A 1 128 ? 44.246 5.000   10.686 1.00 28.58 ? 125 VAL   A O     1 
ATOM   988  C  CB    . VAL   A 1 128 ? 43.366 2.361   9.734  1.00 21.38 ? 125 VAL   A CB    1 
ATOM   989  C  CG1   . VAL   A 1 128 ? 42.204 2.813   8.882  1.00 23.04 ? 125 VAL   A CG1   1 
ATOM   990  C  CG2   . VAL   A 1 128 ? 43.539 0.868   9.703  1.00 24.34 ? 125 VAL   A CG2   1 
ATOM   991  N  N     . ASP   A 1 129 ? 44.727 5.344   8.518  1.00 24.92 ? 126 ASP   A N     1 
ATOM   992  C  CA    . ASP   A 1 129 ? 44.636 6.808   8.649  1.00 25.65 ? 126 ASP   A CA    1 
ATOM   993  C  C     . ASP   A 1 129 ? 43.177 7.247   8.662  1.00 24.27 ? 126 ASP   A C     1 
ATOM   994  O  O     . ASP   A 1 129 ? 42.358 6.622   8.051  1.00 25.00 ? 126 ASP   A O     1 
ATOM   995  C  CB    . ASP   A 1 129 ? 45.583 7.483   7.659  1.00 30.93 ? 126 ASP   A CB    1 
ATOM   996  C  CG    . ASP   A 1 129 ? 45.228 7.049   6.267  1.00 33.11 ? 126 ASP   A CG    1 
ATOM   997  O  OD1   . ASP   A 1 129 ? 45.411 5.862   5.967  1.00 37.30 ? 126 ASP   A OD1   1 
ATOM   998  O  OD2   . ASP   A 1 129 ? 44.606 7.854   5.631  1.00 38.43 ? 126 ASP   A OD2   1 
ATOM   999  N  N     . THR   A 1 130 ? 42.915 8.293   9.429  1.00 24.94 ? 127 THR   A N     1 
ATOM   1000 C  CA    . THR   A 1 130 ? 41.555 8.823   9.618  1.00 25.20 ? 127 THR   A CA    1 
ATOM   1001 C  C     . THR   A 1 130 ? 40.919 9.168   8.261  1.00 23.46 ? 127 THR   A C     1 
ATOM   1002 O  O     . THR   A 1 130 ? 39.801 8.883   8.074  1.00 23.30 ? 127 THR   A O     1 
ATOM   1003 C  CB    . THR   A 1 130 ? 41.604 10.071  10.503 1.00 26.96 ? 127 THR   A CB    1 
ATOM   1004 O  OG1   . THR   A 1 130 ? 42.155 9.730   11.775 1.00 26.67 ? 127 THR   A OG1   1 
ATOM   1005 C  CG2   . THR   A 1 130 ? 40.276 10.771  10.594 1.00 27.10 ? 127 THR   A CG2   1 
ATOM   1006 N  N     . LYS   A 1 131 ? 41.671 9.824   7.373  1.00 24.29 ? 128 LYS   A N     1 
ATOM   1007 C  CA    . LYS   A 1 131 ? 41.153 10.276  6.093  1.00 25.21 ? 128 LYS   A CA    1 
ATOM   1008 C  C     . LYS   A 1 131 ? 40.687 9.087   5.250  1.00 23.72 ? 128 LYS   A C     1 
ATOM   1009 O  O     . LYS   A 1 131 ? 39.620 9.155   4.635  1.00 22.68 ? 128 LYS   A O     1 
ATOM   1010 C  CB    . LYS   A 1 131 ? 42.231 11.074  5.348  1.00 27.88 ? 128 LYS   A CB    1 
ATOM   1011 C  CG    . LYS   A 1 131 ? 41.794 11.570  3.976  1.00 34.16 ? 128 LYS   A CG    1 
ATOM   1012 C  CD    . LYS   A 1 131 ? 42.553 12.786  3.473  1.00 37.67 ? 128 LYS   A CD    1 
ATOM   1013 C  CE    . LYS   A 1 131 ? 42.592 12.819  1.956  1.00 42.39 ? 128 LYS   A CE    1 
ATOM   1014 N  NZ    . LYS   A 1 131 ? 41.247 12.606  1.359  1.00 44.74 ? 128 LYS   A NZ    1 
ATOM   1015 N  N     . GLN   A 1 132 ? 41.484 8.003   5.257  1.00 22.21 ? 129 GLN   A N     1 
ATOM   1016 C  CA    . GLN   A 1 132 ? 41.131 6.801   4.519  1.00 23.47 ? 129 GLN   A CA    1 
ATOM   1017 C  C     . GLN   A 1 132 ? 39.759 6.294   4.963  1.00 22.19 ? 129 GLN   A C     1 
ATOM   1018 O  O     . GLN   A 1 132 ? 38.893 5.985   4.132  1.00 19.76 ? 129 GLN   A O     1 
ATOM   1019 C  CB    . GLN   A 1 132 ? 42.172 5.712   4.739  1.00 25.11 ? 129 GLN   A CB    1 
ATOM   1020 C  CG    . GLN   A 1 132 ? 41.853 4.438   3.996  1.00 26.58 ? 129 GLN   A CG    1 
ATOM   1021 C  CD    . GLN   A 1 132 ? 42.970 3.432   4.097  1.00 29.01 ? 129 GLN   A CD    1 
ATOM   1022 O  OE1   . GLN   A 1 132 ? 42.971 2.429   3.392  1.00 37.90 ? 129 GLN   A OE1   1 
ATOM   1023 N  NE2   . GLN   A 1 132 ? 43.897 3.674   5.005  1.00 32.69 ? 129 GLN   A NE2   1 
ATOM   1024 N  N     . ALA   A 1 133 ? 39.577 6.170   6.279  1.00 20.72 ? 130 ALA   A N     1 
ATOM   1025 C  CA    . ALA   A 1 133 ? 38.323 5.640   6.799  1.00 21.12 ? 130 ALA   A CA    1 
ATOM   1026 C  C     . ALA   A 1 133 ? 37.181 6.621   6.560  1.00 18.97 ? 130 ALA   A C     1 
ATOM   1027 O  O     . ALA   A 1 133 ? 36.046 6.217   6.263  1.00 19.67 ? 130 ALA   A O     1 
ATOM   1028 C  CB    . ALA   A 1 133 ? 38.504 5.302   8.274  1.00 21.53 ? 130 ALA   A CB    1 
ATOM   1029 N  N     . GLN   A 1 134 ? 37.470 7.935   6.622  1.00 19.97 ? 131 GLN   A N     1 
ATOM   1030 C  CA    . GLN   A 1 134 ? 36.461 8.933   6.334  1.00 22.28 ? 131 GLN   A CA    1 
ATOM   1031 C  C     . GLN   A 1 134 ? 35.954 8.810   4.886  1.00 19.57 ? 131 GLN   A C     1 
ATOM   1032 O  O     . GLN   A 1 134 ? 34.760 8.886   4.629  1.00 20.04 ? 131 GLN   A O     1 
ATOM   1033 C  CB    . GLN   A 1 134 ? 37.012 10.327  6.614  1.00 24.45 ? 131 GLN   A CB    1 
ATOM   1034 C  CG    . GLN   A 1 134 ? 35.941 11.389  6.406  1.00 27.87 ? 131 GLN   A CG    1 
ATOM   1035 C  CD    . GLN   A 1 134 ? 34.732 11.184  7.301  1.00 33.19 ? 131 GLN   A CD    1 
ATOM   1036 O  OE1   . GLN   A 1 134 ? 34.802 11.465  8.501  1.00 36.55 ? 131 GLN   A OE1   1 
ATOM   1037 N  NE2   . GLN   A 1 134 ? 33.636 10.692  6.734  1.00 30.85 ? 131 GLN   A NE2   1 
ATOM   1038 N  N     . ASP   A 1 135 ? 36.881 8.637   3.949  1.00 20.50 ? 132 ASP   A N     1 
ATOM   1039 C  CA    . ASP   A 1 135 ? 36.513 8.571   2.540  1.00 20.33 ? 132 ASP   A CA    1 
ATOM   1040 C  C     . ASP   A 1 135 ? 35.719 7.295   2.284  1.00 18.50 ? 132 ASP   A C     1 
ATOM   1041 O  O     . ASP   A 1 135 ? 34.773 7.301   1.492  1.00 18.97 ? 132 ASP   A O     1 
ATOM   1042 C  CB    . ASP   A 1 135 ? 37.770 8.651   1.669  1.00 20.14 ? 132 ASP   A CB    1 
ATOM   1043 C  CG    . ASP   A 1 135 ? 38.334 10.070  1.600  1.00 22.53 ? 132 ASP   A CG    1 
ATOM   1044 O  OD1   . ASP   A 1 135 ? 37.541 11.011  1.678  1.00 26.71 ? 132 ASP   A OD1   1 
ATOM   1045 O  OD2   . ASP   A 1 135 ? 39.565 10.208  1.551  1.00 24.07 ? 132 ASP   A OD2   1 
ATOM   1046 N  N     . LEU   A 1 136 ? 36.119 6.202   2.966  1.00 18.32 ? 133 LEU   A N     1 
ATOM   1047 C  CA    . LEU   A 1 136 ? 35.389 4.966   2.782  1.00 19.18 ? 133 LEU   A CA    1 
ATOM   1048 C  C     . LEU   A 1 136 ? 33.949 5.142   3.276  1.00 17.97 ? 133 LEU   A C     1 
ATOM   1049 O  O     . LEU   A 1 136 ? 32.984 4.761   2.598  1.00 17.95 ? 133 LEU   A O     1 
ATOM   1050 C  CB    . LEU   A 1 136 ? 36.091 3.813   3.520  1.00 18.80 ? 133 LEU   A CB    1 
ATOM   1051 C  CG    . LEU   A 1 136 ? 35.370 2.484   3.315  1.00 19.97 ? 133 LEU   A CG    1 
ATOM   1052 C  CD1   . LEU   A 1 136 ? 35.491 1.999   1.883  1.00 21.30 ? 133 LEU   A CD1   1 
ATOM   1053 C  CD2   . LEU   A 1 136 ? 35.834 1.416   4.311  1.00 22.66 ? 133 LEU   A CD2   1 
ATOM   1054 N  N     . ALA   A 1 137 ? 33.793 5.716   4.494  1.00 17.75 ? 134 ALA   A N     1 
ATOM   1055 C  CA    . ALA   A 1 137 ? 32.461 5.942   5.013  1.00 17.67 ? 134 ALA   A CA    1 
ATOM   1056 C  C     . ALA   A 1 137 ? 31.634 6.813   4.063  1.00 18.03 ? 134 ALA   A C     1 
ATOM   1057 O  O     . ALA   A 1 137 ? 30.429 6.590   3.914  1.00 18.86 ? 134 ALA   A O     1 
ATOM   1058 C  CB    . ALA   A 1 137 ? 32.543 6.583   6.387  1.00 18.47 ? 134 ALA   A CB    1 
ATOM   1059 N  N     . ARG   A 1 138 ? 32.232 7.855   3.492  1.00 18.87 ? 135 ARG   A N     1 
ATOM   1060 C  CA    . ARG   A 1 138 ? 31.503 8.708   2.501  1.00 19.75 ? 135 ARG   A CA    1 
ATOM   1061 C  C     . ARG   A 1 138 ? 31.016 7.875   1.299  1.00 20.21 ? 135 ARG   A C     1 
ATOM   1062 O  O     . ARG   A 1 138 ? 29.942 8.083   0.859  1.00 20.80 ? 135 ARG   A O     1 
ATOM   1063 C  CB    . ARG   A 1 138 ? 32.426 9.793   1.942  1.00 24.22 ? 135 ARG   A CB    1 
ATOM   1064 C  CG    . ARG   A 1 138 ? 32.767 10.927  2.881  1.00 29.51 ? 135 ARG   A CG    1 
ATOM   1065 C  CD    . ARG   A 1 138 ? 33.600 11.992  2.202  1.00 37.74 ? 135 ARG   A CD    1 
ATOM   1066 N  NE    . ARG   A 1 138 ? 34.336 12.571  3.282  1.00 42.26 ? 135 ARG   A NE    1 
ATOM   1067 C  CZ    . ARG   A 1 138 ? 34.922 13.739  3.286  1.00 46.70 ? 135 ARG   A CZ    1 
ATOM   1068 N  NH1   . ARG   A 1 138 ? 35.498 14.174  4.394  1.00 50.42 ? 135 ARG   A NH1   1 
ATOM   1069 N  NH2   . ARG   A 1 138 ? 34.873 14.496  2.208  1.00 52.68 ? 135 ARG   A NH2   1 
ATOM   1070 N  N     . SER   A 1 139 ? 31.847 6.928   0.854  1.00 18.67 ? 136 SER   A N     1 
ATOM   1071 C  CA    . SER   A 1 139 ? 31.503 6.035   -0.284 1.00 20.07 ? 136 SER   A CA    1 
ATOM   1072 C  C     . SER   A 1 139 ? 30.268 5.185   0.060  1.00 19.93 ? 136 SER   A C     1 
ATOM   1073 O  O     . SER   A 1 139 ? 29.366 5.050   -0.737 1.00 19.27 ? 136 SER   A O     1 
ATOM   1074 C  CB    . SER   A 1 139 ? 32.713 5.212   -0.631 1.00 21.80 ? 136 SER   A CB    1 
ATOM   1075 O  OG    . SER   A 1 139 ? 32.457 4.423   -1.762 1.00 26.14 ? 136 SER   A OG    1 
ATOM   1076 N  N     . TYR   A 1 140 ? 30.237 4.722   1.322  1.00 19.41 ? 137 TYR   A N     1 
ATOM   1077 C  CA    . TYR   A 1 140 ? 29.154 3.885   1.902  1.00 20.24 ? 137 TYR   A CA    1 
ATOM   1078 C  C     . TYR   A 1 140 ? 27.935 4.733   2.297  1.00 20.60 ? 137 TYR   A C     1 
ATOM   1079 O  O     . TYR   A 1 140 ? 26.877 4.170   2.434  1.00 22.68 ? 137 TYR   A O     1 
ATOM   1080 C  CB    . TYR   A 1 140 ? 29.664 3.171   3.158  1.00 19.40 ? 137 TYR   A CB    1 
ATOM   1081 C  CG    . TYR   A 1 140 ? 30.682 2.079   2.966  1.00 19.95 ? 137 TYR   A CG    1 
ATOM   1082 C  CD1   . TYR   A 1 140 ? 30.984 1.527   1.720  1.00 20.25 ? 137 TYR   A CD1   1 
ATOM   1083 C  CD2   . TYR   A 1 140 ? 31.365 1.590   4.059  1.00 21.38 ? 137 TYR   A CD2   1 
ATOM   1084 C  CE1   . TYR   A 1 140 ? 31.922 0.517   1.616  1.00 22.09 ? 137 TYR   A CE1   1 
ATOM   1085 C  CE2   . TYR   A 1 140 ? 32.297 0.586   3.967  1.00 21.02 ? 137 TYR   A CE2   1 
ATOM   1086 C  CZ    . TYR   A 1 140 ? 32.580 0.038   2.734  1.00 21.64 ? 137 TYR   A CZ    1 
ATOM   1087 O  OH    . TYR   A 1 140 ? 33.490 -0.941  2.725  1.00 21.08 ? 137 TYR   A OH    1 
ATOM   1088 N  N     . GLY   A 1 141 ? 28.111 6.036   2.395  1.00 20.32 ? 138 GLY   A N     1 
ATOM   1089 C  CA    . GLY   A 1 141 ? 27.033 6.934   2.784  1.00 20.03 ? 138 GLY   A CA    1 
ATOM   1090 C  C     . GLY   A 1 141 ? 26.647 6.760   4.244  1.00 20.52 ? 138 GLY   A C     1 
ATOM   1091 O  O     . GLY   A 1 141 ? 25.456 6.862   4.567  1.00 22.45 ? 138 GLY   A O     1 
ATOM   1092 N  N     . ILE   A 1 142 ? 27.660 6.583   5.109  1.00 16.72 ? 139 ILE   A N     1 
ATOM   1093 C  CA    . ILE   A 1 142 ? 27.414 6.407   6.537  1.00 17.49 ? 139 ILE   A CA    1 
ATOM   1094 C  C     . ILE   A 1 142 ? 28.316 7.310   7.350  1.00 19.21 ? 139 ILE   A C     1 
ATOM   1095 O  O     . ILE   A 1 142 ? 29.415 7.658   6.899  1.00 19.60 ? 139 ILE   A O     1 
ATOM   1096 C  CB    . ILE   A 1 142 ? 27.614 4.934   6.959  1.00 17.03 ? 139 ILE   A CB    1 
ATOM   1097 C  CG1   . ILE   A 1 142 ? 29.075 4.480   6.886  1.00 17.51 ? 139 ILE   A CG1   1 
ATOM   1098 C  CG2   . ILE   A 1 142 ? 26.683 4.017   6.164  1.00 17.74 ? 139 ILE   A CG2   1 
ATOM   1099 C  CD1   . ILE   A 1 142 ? 29.240 3.005   7.199  1.00 17.34 ? 139 ILE   A CD1   1 
ATOM   1100 N  N     . PRO   A 1 143 ? 27.943 7.651   8.613  1.00 17.98 ? 140 PRO   A N     1 
ATOM   1101 C  CA    . PRO   A 1 143 ? 28.859 8.352   9.513  1.00 18.80 ? 140 PRO   A CA    1 
ATOM   1102 C  C     . PRO   A 1 143 ? 30.110 7.554   9.895  1.00 18.95 ? 140 PRO   A C     1 
ATOM   1103 O  O     . PRO   A 1 143 ? 30.105 6.317   9.937  1.00 18.74 ? 140 PRO   A O     1 
ATOM   1104 C  CB    . PRO   A 1 143 ? 27.978 8.665   10.750 1.00 18.88 ? 140 PRO   A CB    1 
ATOM   1105 C  CG    . PRO   A 1 143 ? 26.564 8.521   10.251 1.00 17.59 ? 140 PRO   A CG    1 
ATOM   1106 C  CD    . PRO   A 1 143 ? 26.634 7.384   9.241  1.00 17.83 ? 140 PRO   A CD    1 
ATOM   1107 N  N     . PHE   A 1 144 ? 31.177 8.276   10.139 1.00 19.95 ? 141 PHE   A N     1 
ATOM   1108 C  CA    . PHE   A 1 144 ? 32.427 7.679   10.634 1.00 18.75 ? 141 PHE   A CA    1 
ATOM   1109 C  C     . PHE   A 1 144 ? 32.804 8.398   11.927 1.00 19.82 ? 141 PHE   A C     1 
ATOM   1110 O  O     . PHE   A 1 144 ? 32.779 9.603   11.942 1.00 19.55 ? 141 PHE   A O     1 
ATOM   1111 C  CB    . PHE   A 1 144 ? 33.562 7.828   9.614  1.00 19.46 ? 141 PHE   A CB    1 
ATOM   1112 C  CG    . PHE   A 1 144 ? 34.928 7.531   10.160 1.00 21.10 ? 141 PHE   A CG    1 
ATOM   1113 C  CD1   . PHE   A 1 144 ? 35.203 6.324   10.765 1.00 21.07 ? 141 PHE   A CD1   1 
ATOM   1114 C  CD2   . PHE   A 1 144 ? 35.952 8.441   10.057 1.00 20.60 ? 141 PHE   A CD2   1 
ATOM   1115 C  CE1   . PHE   A 1 144 ? 36.450 6.048   11.286 1.00 20.19 ? 141 PHE   A CE1   1 
ATOM   1116 C  CE2   . PHE   A 1 144 ? 37.203 8.157   10.563 1.00 22.96 ? 141 PHE   A CE2   1 
ATOM   1117 C  CZ    . PHE   A 1 144 ? 37.455 6.958   11.173 1.00 22.27 ? 141 PHE   A CZ    1 
ATOM   1118 N  N     . ILE   A 1 145 ? 33.102 7.622   12.966 1.00 20.50 ? 142 ILE   A N     1 
ATOM   1119 C  CA    . ILE   A 1 145 ? 33.509 8.202   14.280 1.00 22.91 ? 142 ILE   A CA    1 
ATOM   1120 C  C     . ILE   A 1 145 ? 34.718 7.441   14.811 1.00 21.07 ? 142 ILE   A C     1 
ATOM   1121 O  O     . ILE   A 1 145 ? 34.721 6.265   14.730 1.00 20.79 ? 142 ILE   A O     1 
ATOM   1122 C  CB    . ILE   A 1 145 ? 32.319 8.163   15.280 1.00 21.95 ? 142 ILE   A CB    1 
ATOM   1123 C  CG1   . ILE   A 1 145 ? 31.056 8.798   14.699 1.00 24.26 ? 142 ILE   A CG1   1 
ATOM   1124 C  CG2   . ILE   A 1 145 ? 32.689 8.824   16.598 1.00 24.38 ? 142 ILE   A CG2   1 
ATOM   1125 C  CD1   . ILE   A 1 145 ? 29.760 8.367   15.346 1.00 30.17 ? 142 ILE   A CD1   1 
ATOM   1126 N  N     . GLU   A 1 146 ? 35.722 8.153   15.283 1.00 22.06 ? 143 GLU   A N     1 
ATOM   1127 C  CA    . GLU   A 1 146 ? 36.869 7.485   15.912 1.00 22.84 ? 143 GLU   A CA    1 
ATOM   1128 C  C     . GLU   A 1 146 ? 36.549 7.475   17.414 1.00 22.55 ? 143 GLU   A C     1 
ATOM   1129 O  O     . GLU   A 1 146 ? 36.162 8.494   17.903 1.00 23.09 ? 143 GLU   A O     1 
ATOM   1130 C  CB    . GLU   A 1 146 ? 38.207 8.184   15.663 1.00 24.53 ? 143 GLU   A CB    1 
ATOM   1131 C  CG    . GLU   A 1 146 ? 38.759 7.916   14.254 1.00 25.78 ? 143 GLU   A CG    1 
ATOM   1132 C  CD    . GLU   A 1 146 ? 40.252 8.079   14.060 1.00 26.01 ? 143 GLU   A CD    1 
ATOM   1133 O  OE1   . GLU   A 1 146 ? 40.962 8.549   14.924 1.00 26.66 ? 143 GLU   A OE1   1 
ATOM   1134 O  OE2   . GLU   A 1 146 ? 40.702 7.720   12.940 1.00 26.76 ? 143 GLU   A OE2   1 
ATOM   1135 N  N     . THR   A 1 147 ? 36.821 6.351   18.032 1.00 19.31 ? 144 THR   A N     1 
ATOM   1136 C  CA    . THR   A 1 147 ? 36.502 6.196   19.460 1.00 20.01 ? 144 THR   A CA    1 
ATOM   1137 C  C     . THR   A 1 147 ? 37.691 5.598   20.194 1.00 22.16 ? 144 THR   A C     1 
ATOM   1138 O  O     . THR   A 1 147 ? 38.572 5.041   19.654 1.00 20.77 ? 144 THR   A O     1 
ATOM   1139 C  CB    . THR   A 1 147 ? 35.351 5.200   19.596 1.00 18.84 ? 144 THR   A CB    1 
ATOM   1140 O  OG1   . THR   A 1 147 ? 35.705 3.914   19.111 1.00 18.01 ? 144 THR   A OG1   1 
ATOM   1141 C  CG2   . THR   A 1 147 ? 34.031 5.680   19.057 1.00 20.22 ? 144 THR   A CG2   1 
ATOM   1142 N  N     . SER   A 1 148 ? 37.652 5.767   21.515 1.00 22.15 ? 145 SER   A N     1 
ATOM   1143 C  CA    . SER   A 1 148 ? 38.561 5.026   22.403 1.00 21.41 ? 145 SER   A CA    1 
ATOM   1144 C  C     . SER   A 1 148 ? 37.687 4.475   23.541 1.00 20.79 ? 145 SER   A C     1 
ATOM   1145 O  O     . SER   A 1 148 ? 37.198 5.269   24.318 1.00 23.32 ? 145 SER   A O     1 
ATOM   1146 C  CB    . SER   A 1 148 ? 39.640 5.854   23.001 1.00 24.22 ? 145 SER   A CB    1 
ATOM   1147 O  OG    . SER   A 1 148 ? 40.385 5.076   23.920 1.00 25.10 ? 145 SER   A OG    1 
ATOM   1148 N  N     . ALA   A 1 149 ? 37.499 3.187   23.576 1.00 20.86 ? 146 ALA   A N     1 
ATOM   1149 C  CA    . ALA   A 1 149 ? 36.821 2.558   24.705 1.00 20.80 ? 146 ALA   A CA    1 
ATOM   1150 C  C     . ALA   A 1 149 ? 37.637 2.778   25.982 1.00 21.68 ? 146 ALA   A C     1 
ATOM   1151 O  O     . ALA   A 1 149 ? 37.046 2.935   27.052 1.00 23.37 ? 146 ALA   A O     1 
ATOM   1152 C  CB    . ALA   A 1 149 ? 36.624 1.089   24.427 1.00 21.48 ? 146 ALA   A CB    1 
ATOM   1153 N  N     . LYS   A 1 150 ? 38.966 2.839   25.852 1.00 22.10 ? 147 LYS   A N     1 
ATOM   1154 C  CA    . LYS   A 1 150 ? 39.868 3.023   26.990 1.00 24.70 ? 147 LYS   A CA    1 
ATOM   1155 C  C     . LYS   A 1 150 ? 39.658 4.401   27.620 1.00 23.44 ? 147 LYS   A C     1 
ATOM   1156 O  O     . LYS   A 1 150 ? 39.546 4.530   28.864 1.00 28.07 ? 147 LYS   A O     1 
ATOM   1157 C  CB    . LYS   A 1 150 ? 41.333 2.790   26.576 1.00 25.36 ? 147 LYS   A CB    1 
ATOM   1158 C  CG    . LYS   A 1 150 ? 42.338 2.834   27.735 1.00 30.18 ? 147 LYS   A CG    1 
ATOM   1159 C  CD    . LYS   A 1 150 ? 43.789 2.667   27.349 1.00 31.45 ? 147 LYS   A CD    1 
ATOM   1160 C  CE    . LYS   A 1 150 ? 44.682 3.043   28.519 1.00 33.31 ? 147 LYS   A CE    1 
ATOM   1161 N  NZ    . LYS   A 1 150 ? 46.125 3.012   28.175 1.00 34.18 ? 147 LYS   A NZ    1 
ATOM   1162 N  N     . THR   A 1 151 ? 39.585 5.458   26.811 1.00 26.07 ? 148 THR   A N     1 
ATOM   1163 C  CA    . THR   A 1 151 ? 39.474 6.800   27.370 1.00 24.86 ? 148 THR   A CA    1 
ATOM   1164 C  C     . THR   A 1 151 ? 38.032 7.285   27.419 1.00 25.41 ? 148 THR   A C     1 
ATOM   1165 O  O     . THR   A 1 151 ? 37.776 8.375   27.921 1.00 29.82 ? 148 THR   A O     1 
ATOM   1166 C  CB    . THR   A 1 151 ? 40.293 7.846   26.602 1.00 29.23 ? 148 THR   A CB    1 
ATOM   1167 O  OG1   . THR   A 1 151 ? 39.560 8.217   25.425 1.00 32.96 ? 148 THR   A OG1   1 
ATOM   1168 C  CG2   . THR   A 1 151 ? 41.680 7.352   26.258 1.00 30.47 ? 148 THR   A CG2   1 
ATOM   1169 N  N     . ARG   A 1 152 ? 37.109 6.515   26.858 1.00 23.90 ? 149 ARG   A N     1 
ATOM   1170 C  CA    . ARG   A 1 152 ? 35.669 6.822   26.699 1.00 25.74 ? 149 ARG   A CA    1 
ATOM   1171 C  C     . ARG   A 1 152 ? 35.405 7.892   25.617 1.00 29.33 ? 149 ARG   A C     1 
ATOM   1172 O  O     . ARG   A 1 152 ? 34.269 8.234   25.390 1.00 29.36 ? 149 ARG   A O     1 
ATOM   1173 C  CB    . ARG   A 1 152 ? 34.935 6.978   28.047 1.00 28.13 ? 149 ARG   A CB    1 
ATOM   1174 C  CG    . ARG   A 1 152 ? 33.430 6.869   27.968 1.00 31.04 ? 149 ARG   A CG    1 
ATOM   1175 C  CD    . ARG   A 1 152 ? 32.783 6.790   29.354 1.00 33.58 ? 149 ARG   A CD    1 
ATOM   1176 N  NE    . ARG   A 1 152 ? 31.511 6.147   29.159 1.00 33.27 ? 149 ARG   A NE    1 
ATOM   1177 C  CZ    . ARG   A 1 152 ? 30.432 6.784   28.737 1.00 34.73 ? 149 ARG   A CZ    1 
ATOM   1178 N  NH1   . ARG   A 1 152 ? 30.492 8.068   28.450 1.00 34.79 ? 149 ARG   A NH1   1 
ATOM   1179 N  NH2   . ARG   A 1 152 ? 29.297 6.153   28.555 1.00 40.43 ? 149 ARG   A NH2   1 
ATOM   1180 N  N     . GLN   A 1 153 ? 36.418 8.242   24.823 1.00 22.90 ? 150 GLN   A N     1 
ATOM   1181 C  CA    . GLN   A 1 153 ? 36.207 9.260   23.806 1.00 26.03 ? 150 GLN   A CA    1 
ATOM   1182 C  C     . GLN   A 1 153 ? 35.201 8.788   22.745 1.00 21.94 ? 150 GLN   A C     1 
ATOM   1183 O  O     . GLN   A 1 153 ? 35.416 7.764   22.108 1.00 21.34 ? 150 GLN   A O     1 
ATOM   1184 C  CB    . GLN   A 1 153 ? 37.524 9.558   23.090 1.00 27.51 ? 150 GLN   A CB    1 
ATOM   1185 C  CG    . GLN   A 1 153 ? 37.426 10.704  22.093 1.00 33.69 ? 150 GLN   A CG    1 
ATOM   1186 C  CD    . GLN   A 1 153 ? 37.428 12.023  22.823 1.00 38.27 ? 150 GLN   A CD    1 
ATOM   1187 O  OE1   . GLN   A 1 153 ? 37.742 12.079  24.008 1.00 48.24 ? 150 GLN   A OE1   1 
ATOM   1188 N  NE2   . GLN   A 1 153 ? 37.091 13.094  22.119 1.00 50.56 ? 150 GLN   A NE2   1 
ATOM   1189 N  N     . ARG   A 1 154 ? 34.164 9.580   22.530 1.00 22.40 ? 151 ARG   A N     1 
ATOM   1190 C  CA    . ARG   A 1 154 ? 33.139 9.430   21.455 1.00 22.54 ? 151 ARG   A CA    1 
ATOM   1191 C  C     . ARG   A 1 154 ? 32.349 8.122   21.534 1.00 22.42 ? 151 ARG   A C     1 
ATOM   1192 O  O     . ARG   A 1 154 ? 31.662 7.788   20.627 1.00 20.94 ? 151 ARG   A O     1 
ATOM   1193 C  CB    . ARG   A 1 154 ? 33.811 9.679   20.087 1.00 22.38 ? 151 ARG   A CB    1 
ATOM   1194 C  CG    . ARG   A 1 154 ? 34.135 11.146  19.863 1.00 26.32 ? 151 ARG   A CG    1 
ATOM   1195 C  CD    . ARG   A 1 154 ? 34.576 11.577  18.473 1.00 29.50 ? 151 ARG   A CD    1 
ATOM   1196 N  NE    . ARG   A 1 154 ? 35.915 11.038  18.448 1.00 44.83 ? 151 ARG   A NE    1 
ATOM   1197 C  CZ    . ARG   A 1 154 ? 37.053 11.706  18.346 1.00 38.27 ? 151 ARG   A CZ    1 
ATOM   1198 N  NH1   . ARG   A 1 154 ? 37.074 13.017  18.244 1.00 41.97 ? 151 ARG   A NH1   1 
ATOM   1199 N  NH2   . ARG   A 1 154 ? 38.180 11.042  18.353 1.00 44.22 ? 151 ARG   A NH2   1 
ATOM   1200 N  N     . VAL   A 1 155 ? 32.347 7.452   22.682 1.00 21.16 ? 152 VAL   A N     1 
ATOM   1201 C  CA    . VAL   A 1 155 ? 31.627 6.188   22.765 1.00 22.37 ? 152 VAL   A CA    1 
ATOM   1202 C  C     . VAL   A 1 155 ? 30.118 6.439   22.692 1.00 20.92 ? 152 VAL   A C     1 
ATOM   1203 O  O     . VAL   A 1 155 ? 29.386 5.816   21.907 1.00 19.84 ? 152 VAL   A O     1 
ATOM   1204 C  CB    . VAL   A 1 155 ? 32.020 5.400   24.026 1.00 21.43 ? 152 VAL   A CB    1 
ATOM   1205 C  CG1   . VAL   A 1 155 ? 31.099 4.207   24.224 1.00 22.19 ? 152 VAL   A CG1   1 
ATOM   1206 C  CG2   . VAL   A 1 155 ? 33.463 4.948   23.960 1.00 21.91 ? 152 VAL   A CG2   1 
ATOM   1207 N  N     . GLU   A 1 156 ? 29.635 7.376   23.498 1.00 20.62 ? 153 GLU   A N     1 
ATOM   1208 C  CA    . GLU   A 1 156 ? 28.220 7.685   23.457 1.00 20.56 ? 153 GLU   A CA    1 
ATOM   1209 C  C     . GLU   A 1 156 ? 27.847 8.163   22.051 1.00 20.45 ? 153 GLU   A C     1 
ATOM   1210 O  O     . GLU   A 1 156 ? 26.813 7.788   21.500 1.00 19.83 ? 153 GLU   A O     1 
ATOM   1211 C  CB    . GLU   A 1 156 ? 27.948 8.716   24.552 1.00 23.42 ? 153 GLU   A CB    1 
ATOM   1212 C  CG    . GLU   A 1 156 ? 26.489 8.966   24.806 1.00 31.61 ? 153 GLU   A CG    1 
ATOM   1213 C  CD    . GLU   A 1 156 ? 26.266 9.672   26.138 1.00 33.26 ? 153 GLU   A CD    1 
ATOM   1214 O  OE1   . GLU   A 1 156 ? 27.138 9.573   27.027 1.00 38.94 ? 153 GLU   A OE1   1 
ATOM   1215 O  OE2   . GLU   A 1 156 ? 25.229 10.311  26.278 1.00 41.79 ? 153 GLU   A OE2   1 
ATOM   1216 N  N     . ASP   A 1 157 ? 28.717 9.003   21.475 1.00 22.63 ? 154 ASP   A N     1 
ATOM   1217 C  CA    . ASP   A 1 157 ? 28.447 9.613   20.181 1.00 23.90 ? 154 ASP   A CA    1 
ATOM   1218 C  C     . ASP   A 1 157 ? 28.252 8.523   19.144 1.00 21.40 ? 154 ASP   A C     1 
ATOM   1219 O  O     . ASP   A 1 157 ? 27.378 8.665   18.292 1.00 21.02 ? 154 ASP   A O     1 
ATOM   1220 C  CB    . ASP   A 1 157 ? 29.578 10.566  19.773 1.00 23.23 ? 154 ASP   A CB    1 
ATOM   1221 C  CG    . ASP   A 1 157 ? 29.613 11.922  20.455 1.00 26.63 ? 154 ASP   A CG    1 
ATOM   1222 O  OD1   . ASP   A 1 157 ? 28.617 12.297  21.105 1.00 28.87 ? 154 ASP   A OD1   1 
ATOM   1223 O  OD2   . ASP   A 1 157 ? 30.658 12.604  20.297 1.00 29.64 ? 154 ASP   A OD2   1 
ATOM   1224 N  N     . ALA   A 1 158 ? 29.044 7.448   19.249 1.00 19.10 ? 155 ALA   A N     1 
ATOM   1225 C  CA    . ALA   A 1 158 ? 29.016 6.362   18.265 1.00 18.83 ? 155 ALA   A CA    1 
ATOM   1226 C  C     . ALA   A 1 158 ? 27.651 5.682   18.330 1.00 20.02 ? 155 ALA   A C     1 
ATOM   1227 O  O     . ALA   A 1 158 ? 26.926 5.554   17.343 1.00 18.72 ? 155 ALA   A O     1 
ATOM   1228 C  CB    . ALA   A 1 158 ? 30.130 5.384   18.499 1.00 20.22 ? 155 ALA   A CB    1 
ATOM   1229 N  N     . PHE   A 1 159 ? 27.241 5.280   19.542 1.00 20.51 ? 156 PHE   A N     1 
ATOM   1230 C  CA    . PHE   A 1 159 ? 25.965 4.604   19.680 1.00 19.59 ? 156 PHE   A CA    1 
ATOM   1231 C  C     . PHE   A 1 159 ? 24.774 5.513   19.360 1.00 19.07 ? 156 PHE   A C     1 
ATOM   1232 O  O     . PHE   A 1 159 ? 23.827 5.081   18.731 1.00 17.95 ? 156 PHE   A O     1 
ATOM   1233 C  CB    . PHE   A 1 159 ? 25.777 4.021   21.082 1.00 18.01 ? 156 PHE   A CB    1 
ATOM   1234 C  CG    . PHE   A 1 159 ? 26.593 2.775   21.291 1.00 18.30 ? 156 PHE   A CG    1 
ATOM   1235 C  CD1   . PHE   A 1 159 ? 26.090 1.520   20.967 1.00 19.17 ? 156 PHE   A CD1   1 
ATOM   1236 C  CD2   . PHE   A 1 159 ? 27.872 2.846   21.826 1.00 17.65 ? 156 PHE   A CD2   1 
ATOM   1237 C  CE1   . PHE   A 1 159 ? 26.879 0.383   21.145 1.00 19.12 ? 156 PHE   A CE1   1 
ATOM   1238 C  CE2   . PHE   A 1 159 ? 28.640 1.704   22.037 1.00 18.09 ? 156 PHE   A CE2   1 
ATOM   1239 C  CZ    . PHE   A 1 159 ? 28.126 0.463   21.710 1.00 17.98 ? 156 PHE   A CZ    1 
ATOM   1240 N  N     . TYR   A 1 160 ? 24.803 6.773   19.832 1.00 19.02 ? 157 TYR   A N     1 
ATOM   1241 C  CA    . TYR   A 1 160 ? 23.656 7.638   19.625 1.00 19.37 ? 157 TYR   A CA    1 
ATOM   1242 C  C     . TYR   A 1 160 ? 23.550 8.095   18.167 1.00 19.23 ? 157 TYR   A C     1 
ATOM   1243 O  O     . TYR   A 1 160 ? 22.452 8.255   17.653 1.00 20.01 ? 157 TYR   A O     1 
ATOM   1244 C  CB    . TYR   A 1 160 ? 23.708 8.841   20.576 1.00 24.48 ? 157 TYR   A CB    1 
ATOM   1245 C  CG    . TYR   A 1 160 ? 23.520 8.485   22.040 1.00 26.08 ? 157 TYR   A CG    1 
ATOM   1246 C  CD1   . TYR   A 1 160 ? 23.204 7.193   22.443 1.00 23.61 ? 157 TYR   A CD1   1 
ATOM   1247 C  CD2   . TYR   A 1 160 ? 23.643 9.457   23.022 1.00 31.35 ? 157 TYR   A CD2   1 
ATOM   1248 C  CE1   . TYR   A 1 160 ? 23.033 6.869   23.784 1.00 28.41 ? 157 TYR   A CE1   1 
ATOM   1249 C  CE2   . TYR   A 1 160 ? 23.450 9.150   24.362 1.00 35.08 ? 157 TYR   A CE2   1 
ATOM   1250 C  CZ    . TYR   A 1 160 ? 23.167 7.851   24.746 1.00 30.88 ? 157 TYR   A CZ    1 
ATOM   1251 O  OH    . TYR   A 1 160 ? 22.983 7.504   26.063 1.00 40.27 ? 157 TYR   A OH    1 
ATOM   1252 N  N     . THR   A 1 161 ? 24.690 8.188   17.484 1.00 18.64 ? 158 THR   A N     1 
ATOM   1253 C  CA    . THR   A 1 161 ? 24.657 8.465   16.061 1.00 18.82 ? 158 THR   A CA    1 
ATOM   1254 C  C     . THR   A 1 161 ? 23.959 7.313   15.340 1.00 17.78 ? 158 THR   A C     1 
ATOM   1255 O  O     . THR   A 1 161 ? 23.146 7.515   14.446 1.00 18.85 ? 158 THR   A O     1 
ATOM   1256 C  CB    . THR   A 1 161 ? 26.077 8.692   15.520 1.00 17.98 ? 158 THR   A CB    1 
ATOM   1257 O  OG1   . THR   A 1 161 ? 26.599 9.913   16.059 1.00 19.81 ? 158 THR   A OG1   1 
ATOM   1258 C  CG2   . THR   A 1 161 ? 26.090 8.801   14.001 1.00 21.11 ? 158 THR   A CG2   1 
ATOM   1259 N  N     . LEU   A 1 162 ? 24.261 6.073   15.753 1.00 18.39 ? 159 LEU   A N     1 
ATOM   1260 C  CA    . LEU   A 1 162 ? 23.589 4.941   15.136 1.00 18.31 ? 159 LEU   A CA    1 
ATOM   1261 C  C     . LEU   A 1 162 ? 22.080 4.976   15.366 1.00 16.95 ? 159 LEU   A C     1 
ATOM   1262 O  O     . LEU   A 1 162 ? 21.284 4.727   14.466 1.00 17.37 ? 159 LEU   A O     1 
ATOM   1263 C  CB    . LEU   A 1 162 ? 24.173 3.616   15.643 1.00 16.94 ? 159 LEU   A CB    1 
ATOM   1264 C  CG    . LEU   A 1 162 ? 23.586 2.347   15.015 1.00 16.55 ? 159 LEU   A CG    1 
ATOM   1265 C  CD1   . LEU   A 1 162 ? 23.782 2.309   13.494 1.00 15.86 ? 159 LEU   A CD1   1 
ATOM   1266 C  CD2   . LEU   A 1 162 ? 24.219 1.122   15.674 1.00 16.04 ? 159 LEU   A CD2   1 
ATOM   1267 N  N     . VAL   A 1 163 ? 21.650 5.295   16.607 1.00 18.14 ? 160 VAL   A N     1 
ATOM   1268 C  CA    . VAL   A 1 163 ? 20.211 5.465   16.812 1.00 19.82 ? 160 VAL   A CA    1 
ATOM   1269 C  C     . VAL   A 1 163 ? 19.604 6.488   15.836 1.00 18.68 ? 160 VAL   A C     1 
ATOM   1270 O  O     . VAL   A 1 163 ? 18.541 6.225   15.263 1.00 19.94 ? 160 VAL   A O     1 
ATOM   1271 C  CB    . VAL   A 1 163 ? 19.873 5.807   18.279 1.00 19.29 ? 160 VAL   A CB    1 
ATOM   1272 C  CG1   . VAL   A 1 163 ? 18.388 6.106   18.409 1.00 19.52 ? 160 VAL   A CG1   1 
ATOM   1273 C  CG2   . VAL   A 1 163 ? 20.252 4.654   19.194 1.00 20.44 ? 160 VAL   A CG2   1 
ATOM   1274 N  N     . ARG   A 1 164 ? 20.304 7.622   15.647 1.00 20.99 ? 161 ARG   A N     1 
ATOM   1275 C  CA    . ARG   A 1 164 ? 19.798 8.668   14.754 1.00 20.41 ? 161 ARG   A CA    1 
ATOM   1276 C  C     . ARG   A 1 164 ? 19.700 8.182   13.314 1.00 20.75 ? 161 ARG   A C     1 
ATOM   1277 O  O     . ARG   A 1 164 ? 18.772 8.544   12.595 1.00 21.57 ? 161 ARG   A O     1 
ATOM   1278 C  CB    . ARG   A 1 164 ? 20.570 9.979   14.873 1.00 20.71 ? 161 ARG   A CB    1 
ATOM   1279 C  CG    . ARG   A 1 164 ? 20.317 10.659  16.205 1.00 23.06 ? 161 ARG   A CG    1 
ATOM   1280 C  CD    . ARG   A 1 164 ? 20.977 12.017  16.249 1.00 25.95 ? 161 ARG   A CD    1 
ATOM   1281 N  NE    . ARG   A 1 164 ? 20.837 12.667  17.546 1.00 28.20 ? 161 ARG   A NE    1 
ATOM   1282 C  CZ    . ARG   A 1 164 ? 21.745 12.610  18.506 1.00 27.62 ? 161 ARG   A CZ    1 
ATOM   1283 N  NH1   . ARG   A 1 164 ? 22.848 11.898  18.346 1.00 29.28 ? 161 ARG   A NH1   1 
ATOM   1284 N  NH2   . ARG   A 1 164 ? 21.536 13.281  19.627 1.00 33.39 ? 161 ARG   A NH2   1 
ATOM   1285 N  N     . GLU   A 1 165 ? 20.644 7.318   12.913 1.00 19.07 ? 162 GLU   A N     1 
ATOM   1286 C  CA    . GLU   A 1 165 ? 20.619 6.762   11.570 1.00 20.20 ? 162 GLU   A CA    1 
ATOM   1287 C  C     . GLU   A 1 165 ? 19.404 5.844   11.436 1.00 19.59 ? 162 GLU   A C     1 
ATOM   1288 O  O     . GLU   A 1 165 ? 18.766 5.811   10.377 1.00 20.21 ? 162 GLU   A O     1 
ATOM   1289 C  CB    . GLU   A 1 165 ? 21.903 5.978   11.281 1.00 19.14 ? 162 GLU   A CB    1 
ATOM   1290 C  CG    . GLU   A 1 165 ? 23.132 6.858   11.112 1.00 18.84 ? 162 GLU   A CG    1 
ATOM   1291 C  CD    . GLU   A 1 165 ? 23.055 7.838   9.954  1.00 19.61 ? 162 GLU   A CD    1 
ATOM   1292 O  OE1   . GLU   A 1 165 ? 23.055 7.379   8.837  1.00 22.59 ? 162 GLU   A OE1   1 
ATOM   1293 O  OE2   . GLU   A 1 165 ? 23.070 9.072   10.204 1.00 23.17 ? 162 GLU   A OE2   1 
ATOM   1294 N  N     . ILE   A 1 166 ? 19.082 5.109   12.496 1.00 19.28 ? 163 ILE   A N     1 
ATOM   1295 C  CA    . ILE   A 1 166 ? 17.883 4.229   12.445 1.00 20.68 ? 163 ILE   A CA    1 
ATOM   1296 C  C     . ILE   A 1 166 ? 16.639 5.130   12.383 1.00 21.40 ? 163 ILE   A C     1 
ATOM   1297 O  O     . ILE   A 1 166 ? 15.783 4.879   11.594 1.00 21.89 ? 163 ILE   A O     1 
ATOM   1298 C  CB    . ILE   A 1 166 ? 17.819 3.243   13.624 1.00 19.62 ? 163 ILE   A CB    1 
ATOM   1299 C  CG1   . ILE   A 1 166 ? 18.960 2.219   13.596 1.00 21.38 ? 163 ILE   A CG1   1 
ATOM   1300 C  CG2   . ILE   A 1 166 ? 16.467 2.558   13.608 1.00 21.57 ? 163 ILE   A CG2   1 
ATOM   1301 C  CD1   . ILE   A 1 166 ? 19.220 1.514   14.903 1.00 21.55 ? 163 ILE   A CD1   1 
ATOM   1302 N  N     . ARG   A 1 167 ? 16.606 6.190   13.193 1.00 23.03 ? 164 ARG   A N     1 
ATOM   1303 C  CA    . ARG   A 1 167 ? 15.462 7.134   13.168 1.00 24.84 ? 164 ARG   A CA    1 
ATOM   1304 C  C     . ARG   A 1 167 ? 15.257 7.688   11.761 1.00 24.76 ? 164 ARG   A C     1 
ATOM   1305 O  O     . ARG   A 1 167 ? 14.164 7.678   11.309 1.00 26.23 ? 164 ARG   A O     1 
ATOM   1306 C  CB    . ARG   A 1 167 ? 15.662 8.254   14.184 1.00 26.57 ? 164 ARG   A CB    1 
ATOM   1307 C  CG    . ARG   A 1 167 ? 15.590 7.769   15.615 1.00 27.72 ? 164 ARG   A CG    1 
ATOM   1308 C  CD    . ARG   A 1 167 ? 15.699 8.922   16.579 1.00 29.56 ? 164 ARG   A CD    1 
ATOM   1309 N  NE    . ARG   A 1 167 ? 15.191 8.475   17.868 1.00 28.67 ? 164 ARG   A NE    1 
ATOM   1310 C  CZ    . ARG   A 1 167 ? 15.310 9.173   18.972 1.00 30.21 ? 164 ARG   A CZ    1 
ATOM   1311 N  NH1   . ARG   A 1 167 ? 15.952 10.315  18.983 1.00 29.83 ? 164 ARG   A NH1   1 
ATOM   1312 N  NH2   . ARG   A 1 167 ? 14.817 8.673   20.098 1.00 31.64 ? 164 ARG   A NH2   1 
ATOM   1313 N  N     . GLN   A 1 168 ? 16.334 8.145   11.139 1.00 24.29 ? 165 GLN   A N     1 
ATOM   1314 C  CA    . GLN   A 1 168 ? 16.255 8.688   9.753  1.00 25.47 ? 165 GLN   A CA    1 
ATOM   1315 C  C     . GLN   A 1 168 ? 15.789 7.599   8.792  1.00 25.90 ? 165 GLN   A C     1 
ATOM   1316 O  O     . GLN   A 1 168 ? 14.948 7.884   7.987  1.00 27.43 ? 165 GLN   A O     1 
ATOM   1317 C  CB    . GLN   A 1 168 ? 17.636 9.157   9.325  1.00 25.39 ? 165 GLN   A CB    1 
ATOM   1318 C  CG    . GLN   A 1 168 ? 17.965 10.542  9.822  1.00 28.30 ? 165 GLN   A CG    1 
ATOM   1319 C  CD    . GLN   A 1 168 ? 19.380 10.946  9.487  0.00 27.00 ? 165 GLN   A CD    1 
ATOM   1320 O  OE1   . GLN   A 1 168 ? 20.147 10.177  8.913  0.00 27.00 ? 165 GLN   A OE1   1 
ATOM   1321 N  NE2   . GLN   A 1 168 ? 19.737 12.168  9.848  0.00 27.00 ? 165 GLN   A NE2   1 
ATOM   1322 N  N     . TYR   A 1 169 ? 16.279 6.388   8.948  1.00 21.81 ? 166 TYR   A N     1 
ATOM   1323 C  CA    . TYR   A 1 169 ? 15.816 5.284   8.082  1.00 25.99 ? 166 TYR   A CA    1 
ATOM   1324 C  C     . TYR   A 1 169 ? 14.313 5.027   8.261  1.00 26.25 ? 166 TYR   A C     1 
ATOM   1325 O  O     . TYR   A 1 169 ? 13.621 4.737   7.297  1.00 28.77 ? 166 TYR   A O     1 
ATOM   1326 C  CB    . TYR   A 1 169 ? 16.616 4.022   8.387  1.00 25.54 ? 166 TYR   A CB    1 
ATOM   1327 C  CG    . TYR   A 1 169 ? 16.185 2.803   7.628  1.00 28.07 ? 166 TYR   A CG    1 
ATOM   1328 C  CD1   . TYR   A 1 169 ? 16.630 2.592   6.338  1.00 29.46 ? 166 TYR   A CD1   1 
ATOM   1329 C  CD2   . TYR   A 1 169 ? 15.317 1.876   8.168  1.00 30.37 ? 166 TYR   A CD2   1 
ATOM   1330 C  CE1   . TYR   A 1 169 ? 16.231 1.486   5.620  1.00 31.91 ? 166 TYR   A CE1   1 
ATOM   1331 C  CE2   . TYR   A 1 169 ? 14.896 0.775   7.461  1.00 33.67 ? 166 TYR   A CE2   1 
ATOM   1332 C  CZ    . TYR   A 1 169 ? 15.359 0.580   6.173  1.00 34.69 ? 166 TYR   A CZ    1 
ATOM   1333 O  OH    . TYR   A 1 169 ? 14.947 -0.522  5.498  1.00 38.51 ? 166 TYR   A OH    1 
ATOM   1334 N  N     . ARG   A 1 170 ? 13.835 5.104   9.516  1.00 26.56 ? 167 ARG   A N     1 
ATOM   1335 C  CA    . ARG   A 1 170 ? 12.405 4.799   9.752  1.00 27.89 ? 167 ARG   A CA    1 
ATOM   1336 C  C     . ARG   A 1 170 ? 11.526 5.847   9.070  1.00 28.78 ? 167 ARG   A C     1 
ATOM   1337 O  O     . ARG   A 1 170 ? 10.385 5.546   8.854  1.00 34.72 ? 167 ARG   A O     1 
ATOM   1338 C  CB    . ARG   A 1 170 ? 12.141 4.658   11.255 1.00 29.00 ? 167 ARG   A CB    1 
ATOM   1339 C  CG    . ARG   A 1 170 ? 12.463 3.267   11.777 1.00 31.64 ? 167 ARG   A CG    1 
ATOM   1340 C  CD    . ARG   A 1 170 ? 12.460 3.216   13.287 1.00 30.86 ? 167 ARG   A CD    1 
ATOM   1341 N  NE    . ARG   A 1 170 ? 12.793 1.912   13.826 1.00 31.63 ? 167 ARG   A NE    1 
ATOM   1342 C  CZ    . ARG   A 1 170 ? 12.645 1.599   15.097 1.00 31.81 ? 167 ARG   A CZ    1 
ATOM   1343 N  NH1   . ARG   A 1 170 ? 12.156 2.496   15.924 1.00 39.86 ? 167 ARG   A NH1   1 
ATOM   1344 N  NH2   . ARG   A 1 170 ? 12.971 0.409   15.542 1.00 35.50 ? 167 ARG   A NH2   1 
ATOM   1345 N  N     . LEU   A 1 171 ? 12.072 7.023   8.785  1.00 31.00 ? 168 LEU   A N     1 
ATOM   1346 C  CA    . LEU   A 1 171 ? 11.321 8.145   8.168  1.00 34.99 ? 168 LEU   A CA    1 
ATOM   1347 C  C     . LEU   A 1 171 ? 11.168 7.975   6.651  1.00 36.48 ? 168 LEU   A C     1 
ATOM   1348 O  O     . LEU   A 1 171 ? 10.348 8.677   6.080  1.00 40.66 ? 168 LEU   A O     1 
ATOM   1349 C  CB    . LEU   A 1 171 ? 12.087 9.434   8.461  1.00 42.55 ? 168 LEU   A CB    1 
ATOM   1350 C  CG    . LEU   A 1 171 ? 12.074 9.934   9.900  1.00 42.60 ? 168 LEU   A CG    1 
ATOM   1351 C  CD1   . LEU   A 1 171 ? 12.996 11.122  10.044 1.00 43.93 ? 168 LEU   A CD1   1 
ATOM   1352 C  CD2   . LEU   A 1 171 ? 10.687 10.326  10.293 1.00 45.16 ? 168 LEU   A CD2   1 
ATOM   1353 N  N     . LYS   A 1 172 ? 11.878 7.017   6.070  1.00 35.21 ? 169 LYS   A N     1 
ATOM   1354 C  CA    . LYS   A 1 172 ? 11.966 6.871   4.592  1.00 35.51 ? 169 LYS   A CA    1 
ATOM   1355 C  C     . LYS   A 1 172 ? 10.664 6.355   3.996  1.00 42.57 ? 169 LYS   A C     1 
ATOM   1356 O  O     . LYS   A 1 172 ? 10.254 6.882   2.965  1.00 45.47 ? 169 LYS   A O     1 
ATOM   1357 C  CB    . LYS   A 1 172 ? 13.200 6.034   4.264  1.00 38.21 ? 169 LYS   A CB    1 
ATOM   1358 C  CG    . LYS   A 1 172 ? 14.474 6.771   4.620  1.00 35.81 ? 169 LYS   A CG    1 
ATOM   1359 C  CD    . LYS   A 1 172 ? 15.679 6.521   3.775  1.00 37.86 ? 169 LYS   A CD    1 
ATOM   1360 C  CE    . LYS   A 1 172 ? 16.924 7.033   4.456  1.00 43.00 ? 169 LYS   A CE    1 
ATOM   1361 N  NZ    . LYS   A 1 172 ? 16.939 8.505   4.540  1.00 48.62 ? 169 LYS   A NZ    1 
ATOM   1362 O  OXT   . LYS   A 1 172 ? 10.094 5.442   4.569  1.00 49.07 ? 169 LYS   A OXT   1 
HETATM 1363 P  PG    . GNP   B 2 .   ? 36.269 -10.294 20.644 1.00 21.29 ? 201 GNP   A PG    1 
HETATM 1364 O  O1G   . GNP   B 2 .   ? 34.834 -10.300 21.058 1.00 22.27 ? 201 GNP   A O1G   1 
HETATM 1365 O  O2G   . GNP   B 2 .   ? 36.907 -11.460 21.032 1.00 24.03 ? 201 GNP   A O2G   1 
HETATM 1366 O  O3G   . GNP   B 2 .   ? 36.173 -10.311 19.091 1.00 24.44 ? 201 GNP   A O3G   1 
HETATM 1367 N  N3B   . GNP   B 2 .   ? 36.969 -8.973  21.124 1.00 18.95 ? 201 GNP   A N3B   1 
HETATM 1368 P  PB    . GNP   B 2 .   ? 36.395 -7.508  21.174 1.00 19.55 ? 201 GNP   A PB    1 
HETATM 1369 O  O1B   . GNP   B 2 .   ? 36.379 -6.744  19.878 1.00 18.66 ? 201 GNP   A O1B   1 
HETATM 1370 O  O2B   . GNP   B 2 .   ? 35.147 -7.353  22.014 1.00 19.85 ? 201 GNP   A O2B   1 
HETATM 1371 O  O3A   . GNP   B 2 .   ? 37.488 -6.732  21.953 1.00 21.94 ? 201 GNP   A O3A   1 
HETATM 1372 P  PA    . GNP   B 2 .   ? 37.531 -6.375  23.583 1.00 21.04 ? 201 GNP   A PA    1 
HETATM 1373 O  O1A   . GNP   B 2 .   ? 37.387 -7.642  24.309 1.00 21.64 ? 201 GNP   A O1A   1 
HETATM 1374 O  O2A   . GNP   B 2 .   ? 36.693 -5.216  23.832 1.00 21.32 ? 201 GNP   A O2A   1 
HETATM 1375 O  "O5'" . GNP   B 2 .   ? 38.997 -5.888  23.760 1.00 24.03 ? 201 GNP   A "O5'" 1 
HETATM 1376 C  "C5'" . GNP   B 2 .   ? 40.072 -6.678  23.248 1.00 24.06 ? 201 GNP   A "C5'" 1 
HETATM 1377 C  "C4'" . GNP   B 2 .   ? 41.363 -6.044  23.671 1.00 25.44 ? 201 GNP   A "C4'" 1 
HETATM 1378 O  "O4'" . GNP   B 2 .   ? 41.382 -4.676  23.227 1.00 23.43 ? 201 GNP   A "O4'" 1 
HETATM 1379 C  "C3'" . GNP   B 2 .   ? 41.528 -5.967  25.192 1.00 25.07 ? 201 GNP   A "C3'" 1 
HETATM 1380 O  "O3'" . GNP   B 2 .   ? 42.889 -6.145  25.510 1.00 30.11 ? 201 GNP   A "O3'" 1 
HETATM 1381 C  "C2'" . GNP   B 2 .   ? 41.053 -4.553  25.496 1.00 25.41 ? 201 GNP   A "C2'" 1 
HETATM 1382 O  "O2'" . GNP   B 2 .   ? 41.635 -4.062  26.678 1.00 30.55 ? 201 GNP   A "O2'" 1 
HETATM 1383 C  "C1'" . GNP   B 2 .   ? 41.594 -3.791  24.292 1.00 24.36 ? 201 GNP   A "C1'" 1 
HETATM 1384 N  N9    . GNP   B 2 .   ? 40.898 -2.558  23.969 1.00 23.43 ? 201 GNP   A N9    1 
HETATM 1385 C  C8    . GNP   B 2 .   ? 39.584 -2.424  23.643 1.00 23.18 ? 201 GNP   A C8    1 
HETATM 1386 N  N7    . GNP   B 2 .   ? 39.242 -1.202  23.375 1.00 22.91 ? 201 GNP   A N7    1 
HETATM 1387 C  C5    . GNP   B 2 .   ? 40.411 -0.480  23.465 1.00 26.41 ? 201 GNP   A C5    1 
HETATM 1388 C  C6    . GNP   B 2 .   ? 40.660 0.890   23.222 1.00 25.88 ? 201 GNP   A C6    1 
HETATM 1389 O  O6    . GNP   B 2 .   ? 39.890 1.766   22.854 1.00 23.12 ? 201 GNP   A O6    1 
HETATM 1390 N  N1    . GNP   B 2 .   ? 41.998 1.208   23.449 1.00 26.40 ? 201 GNP   A N1    1 
HETATM 1391 C  C2    . GNP   B 2 .   ? 42.947 0.315   23.833 1.00 24.37 ? 201 GNP   A C2    1 
HETATM 1392 N  N2    . GNP   B 2 .   ? 44.173 0.810   23.969 1.00 29.35 ? 201 GNP   A N2    1 
HETATM 1393 N  N3    . GNP   B 2 .   ? 42.730 -0.980  24.007 1.00 24.74 ? 201 GNP   A N3    1 
HETATM 1394 C  C4    . GNP   B 2 .   ? 41.433 -1.312  23.843 1.00 25.38 ? 201 GNP   A C4    1 
HETATM 1395 MG MG    . MG    C 3 .   ? 33.982 -9.061  22.616 1.00 16.95 ? 202 MG    A MG    1 
HETATM 1396 CO CO    . CO    D 4 .   ? 32.808 -8.543  -1.450 1.00 24.14 ? 203 CO    A CO    1 
HETATM 1397 O  OAT   . A1IMB E 5 .   ? 22.429 -16.600 22.917 1.00 25.02 ? 204 A1IMB A OAT   1 
HETATM 1398 C  CAS   . A1IMB E 5 .   ? 22.209 -15.435 22.709 1.00 24.05 ? 204 A1IMB A CAS   1 
HETATM 1399 C  CAM   . A1IMB E 5 .   ? 22.195 -14.932 21.403 1.00 22.94 ? 204 A1IMB A CAM   1 
HETATM 1400 C  CAN   . A1IMB E 5 .   ? 21.001 -14.766 20.702 1.00 20.54 ? 204 A1IMB A CAN   1 
HETATM 1401 C  CAL   . A1IMB E 5 .   ? 23.374 -14.589 20.736 1.00 21.10 ? 204 A1IMB A CAL   1 
HETATM 1402 O  OAR   . A1IMB E 5 .   ? 24.526 -14.707 21.383 1.00 19.82 ? 204 A1IMB A OAR   1 
HETATM 1403 C  CAK   . A1IMB E 5 .   ? 23.339 -14.046 19.464 1.00 19.31 ? 204 A1IMB A CAK   1 
HETATM 1404 C  CAJ   . A1IMB E 5 .   ? 22.163 -13.886 18.790 1.00 20.47 ? 204 A1IMB A CAJ   1 
HETATM 1405 C  CAI   . A1IMB E 5 .   ? 21.005 -14.297 19.388 1.00 22.39 ? 204 A1IMB A CAI   1 
HETATM 1406 S  SAH   . A1IMB E 5 .   ? 19.446 -14.027 18.549 1.00 23.93 ? 204 A1IMB A SAH   1 
HETATM 1407 O  OAP   . A1IMB E 5 .   ? 18.749 -15.287 18.652 1.00 25.86 ? 204 A1IMB A OAP   1 
HETATM 1408 O  OAQ   . A1IMB E 5 .   ? 19.702 -13.573 17.194 1.00 27.70 ? 204 A1IMB A OAQ   1 
HETATM 1409 N  NAG   . A1IMB E 5 .   ? 18.836 -12.925 19.461 1.00 21.55 ? 204 A1IMB A NAG   1 
HETATM 1410 C  CAF   . A1IMB E 5 .   ? 19.077 -11.650 19.306 1.00 21.81 ? 204 A1IMB A CAF   1 
HETATM 1411 S  SAO   . A1IMB E 5 .   ? 19.401 -10.793 17.910 1.00 20.58 ? 204 A1IMB A SAO   1 
HETATM 1412 C  CAC   . A1IMB E 5 .   ? 19.549 -9.368  18.741 1.00 21.51 ? 204 A1IMB A CAC   1 
HETATM 1413 C  CAB   . A1IMB E 5 .   ? 19.803 -8.189  18.249 1.00 19.41 ? 204 A1IMB A CAB   1 
HETATM 1414 CL CLAA  . A1IMB E 5 .   ? 20.115 -8.058  16.557 1.00 21.10 ? 204 A1IMB A CLAA  1 
HETATM 1415 C  CBJ   . A1IMB E 5 .   ? 19.892 -7.077  19.057 1.00 22.71 ? 204 A1IMB A CBJ   1 
HETATM 1416 C  CBK   . A1IMB E 5 .   ? 19.637 -7.214  20.393 1.00 19.10 ? 204 A1IMB A CBK   1 
HETATM 1417 C  CBG   . A1IMB E 5 .   ? 19.359 -8.462  20.867 1.00 20.24 ? 204 A1IMB A CBG   1 
HETATM 1418 O  OBH   . A1IMB E 5 .   ? 19.108 -8.592  22.183 1.00 20.20 ? 204 A1IMB A OBH   1 
HETATM 1419 C  CAD   . A1IMB E 5 .   ? 19.302 -9.533  20.080 1.00 20.88 ? 204 A1IMB A CAD   1 
HETATM 1420 N  NAE   . A1IMB E 5 .   ? 19.024 -10.817 20.336 1.00 21.19 ? 204 A1IMB A NAE   1 
HETATM 1421 C  CAU   . A1IMB E 5 .   ? 18.839 -11.272 21.712 1.00 22.78 ? 204 A1IMB A CAU   1 
HETATM 1422 C  CAV   . A1IMB E 5 .   ? 20.298 -11.653 22.162 1.00 21.46 ? 204 A1IMB A CAV   1 
HETATM 1423 C  CAW   . A1IMB E 5 .   ? 20.434 -12.644 23.341 1.00 20.77 ? 204 A1IMB A CAW   1 
HETATM 1424 O  OBF   . A1IMB E 5 .   ? 20.085 -11.960 24.489 1.00 20.62 ? 204 A1IMB A OBF   1 
HETATM 1425 C  CAX   . A1IMB E 5 .   ? 21.840 -13.173 23.473 1.00 21.05 ? 204 A1IMB A CAX   1 
HETATM 1426 N  NAY   . A1IMB E 5 .   ? 22.007 -14.615 23.738 1.00 21.03 ? 204 A1IMB A NAY   1 
HETATM 1427 C  CAZ   . A1IMB E 5 .   ? 22.082 -15.147 25.112 1.00 22.82 ? 204 A1IMB A CAZ   1 
HETATM 1428 C  CBA   . A1IMB E 5 .   ? 21.032 -14.560 25.994 1.00 23.35 ? 204 A1IMB A CBA   1 
HETATM 1429 C  CBB   . A1IMB E 5 .   ? 21.033 -15.286 27.370 1.00 25.29 ? 204 A1IMB A CBB   1 
HETATM 1430 C  CBC   . A1IMB E 5 .   ? 22.338 -15.099 28.059 1.00 22.58 ? 204 A1IMB A CBC   1 
HETATM 1431 N  NBI   . A1IMB E 5 .   ? 22.506 -13.743 28.512 1.00 25.27 ? 204 A1IMB A NBI   1 
HETATM 1432 C  CBD   . A1IMB E 5 .   ? 23.472 -15.555 27.187 1.00 25.22 ? 204 A1IMB A CBD   1 
HETATM 1433 C  CBE   . A1IMB E 5 .   ? 23.418 -14.893 25.783 1.00 22.73 ? 204 A1IMB A CBE   1 
HETATM 1434 O  O     . HOH   F 6 .   ? 28.281 14.542  22.176 1.00 37.67 ? 301 HOH   A O     1 
HETATM 1435 O  O     . HOH   F 6 .   ? 32.280 -8.610  21.298 1.00 21.52 ? 302 HOH   A O     1 
HETATM 1436 O  O     . HOH   F 6 .   ? 31.943 -10.452 -2.235 1.00 27.17 ? 303 HOH   A O     1 
HETATM 1437 O  O     . HOH   F 6 .   ? 31.727 1.980   -1.644 1.00 24.14 ? 304 HOH   A O     1 
HETATM 1438 O  O     . HOH   F 6 .   ? 31.223 -9.358  15.131 1.00 20.47 ? 305 HOH   A O     1 
HETATM 1439 O  O     . HOH   F 6 .   ? 40.585 -5.092  28.798 1.00 40.33 ? 306 HOH   A O     1 
HETATM 1440 O  O     . HOH   F 6 .   ? 16.859 14.973  24.487 1.00 37.93 ? 307 HOH   A O     1 
HETATM 1441 O  O     . HOH   F 6 .   ? 7.605  9.420   20.150 1.00 37.64 ? 308 HOH   A O     1 
HETATM 1442 O  O     . HOH   F 6 .   ? 22.597 -7.791  29.814 1.00 25.38 ? 309 HOH   A O     1 
HETATM 1443 O  O     . HOH   F 6 .   ? 14.224 -6.189  14.570 1.00 35.97 ? 310 HOH   A O     1 
HETATM 1444 O  O     . HOH   F 6 .   ? 43.375 -4.087  17.451 1.00 33.96 ? 311 HOH   A O     1 
HETATM 1445 O  O     . HOH   F 6 .   ? 26.319 11.622  22.140 1.00 35.93 ? 312 HOH   A O     1 
HETATM 1446 O  O     . HOH   F 6 .   ? 39.377 -7.586  3.327  1.00 23.87 ? 313 HOH   A O     1 
HETATM 1447 O  O     . HOH   F 6 .   ? 38.662 -2.196  34.610 1.00 29.88 ? 314 HOH   A O     1 
HETATM 1448 O  O     . HOH   F 6 .   ? 28.830 -8.948  25.586 1.00 23.68 ? 315 HOH   A O     1 
HETATM 1449 O  O     . HOH   F 6 .   ? 41.762 8.827   1.981  1.00 25.63 ? 316 HOH   A O     1 
HETATM 1450 O  O     . HOH   F 6 .   ? 29.624 -12.639 15.323 1.00 26.11 ? 317 HOH   A O     1 
HETATM 1451 O  O     . HOH   F 6 .   ? 16.640 -0.548  10.510 1.00 34.68 ? 318 HOH   A O     1 
HETATM 1452 O  O     . HOH   F 6 .   ? 16.611 11.938  16.726 1.00 27.13 ? 319 HOH   A O     1 
HETATM 1453 O  O     . HOH   F 6 .   ? 36.360 -8.248  27.151 1.00 31.14 ? 320 HOH   A O     1 
HETATM 1454 O  O     . HOH   F 6 .   ? 9.289  10.105  23.514 1.00 30.82 ? 321 HOH   A O     1 
HETATM 1455 O  O     . HOH   F 6 .   ? 27.177 -16.052 24.717 1.00 31.81 ? 322 HOH   A O     1 
HETATM 1456 O  O     . HOH   F 6 .   ? 40.855 10.047  23.941 1.00 42.51 ? 323 HOH   A O     1 
HETATM 1457 O  O     . HOH   F 6 .   ? 28.192 -14.128 16.699 1.00 32.37 ? 324 HOH   A O     1 
HETATM 1458 O  O     . HOH   F 6 .   ? 29.738 -11.522 8.148  1.00 30.46 ? 325 HOH   A O     1 
HETATM 1459 O  O     . HOH   F 6 .   ? 47.670 -3.041  11.008 1.00 25.74 ? 326 HOH   A O     1 
HETATM 1460 O  O     . HOH   F 6 .   ? 16.390 -18.251 14.016 1.00 30.08 ? 327 HOH   A O     1 
HETATM 1461 O  O     . HOH   F 6 .   ? 42.032 -6.173  16.184 1.00 38.43 ? 328 HOH   A O     1 
HETATM 1462 O  O     . HOH   F 6 .   ? 23.571 10.850  12.172 1.00 30.18 ? 329 HOH   A O     1 
HETATM 1463 O  O     . HOH   F 6 .   ? 27.295 -16.658 18.835 1.00 32.21 ? 330 HOH   A O     1 
HETATM 1464 O  O     . HOH   F 6 .   ? 46.810 3.933   25.396 1.00 34.27 ? 331 HOH   A O     1 
HETATM 1465 O  O     . HOH   F 6 .   ? 34.702 -1.166  28.503 1.00 21.05 ? 332 HOH   A O     1 
HETATM 1466 O  O     . HOH   F 6 .   ? 49.526 -3.085  13.820 1.00 43.02 ? 333 HOH   A O     1 
HETATM 1467 O  O     . HOH   F 6 .   ? 30.217 9.927   5.645  1.00 27.66 ? 334 HOH   A O     1 
HETATM 1468 O  O     . HOH   F 6 .   ? 23.856 4.835   8.178  1.00 19.66 ? 335 HOH   A O     1 
HETATM 1469 O  O     . HOH   F 6 .   ? 26.412 2.418   -0.431 1.00 44.86 ? 336 HOH   A O     1 
HETATM 1470 O  O     . HOH   F 6 .   ? 36.617 -5.038  11.892 1.00 19.51 ? 337 HOH   A O     1 
HETATM 1471 O  O     . HOH   F 6 .   ? 35.238 -9.410  24.222 1.00 20.34 ? 338 HOH   A O     1 
HETATM 1472 O  O     . HOH   F 6 .   ? 22.251 -1.104  31.214 1.00 36.06 ? 339 HOH   A O     1 
HETATM 1473 O  O     . HOH   F 6 .   ? 31.649 9.002   25.413 1.00 30.66 ? 340 HOH   A O     1 
HETATM 1474 O  O     . HOH   F 6 .   ? 20.536 5.583   30.495 1.00 32.32 ? 341 HOH   A O     1 
HETATM 1475 O  O     . HOH   F 6 .   ? 20.551 -10.525 27.912 1.00 26.45 ? 342 HOH   A O     1 
HETATM 1476 O  O     . HOH   F 6 .   ? 30.674 -3.639  1.318  1.00 26.46 ? 343 HOH   A O     1 
HETATM 1477 O  O     . HOH   F 6 .   ? 39.481 -11.099 4.748  1.00 32.46 ? 344 HOH   A O     1 
HETATM 1478 O  O     . HOH   F 6 .   ? 49.178 -1.985  18.169 1.00 25.30 ? 345 HOH   A O     1 
HETATM 1479 O  O     . HOH   F 6 .   ? 24.237 4.167   3.233  1.00 34.93 ? 346 HOH   A O     1 
HETATM 1480 O  O     . HOH   F 6 .   ? 40.405 10.640  16.771 1.00 36.26 ? 347 HOH   A O     1 
HETATM 1481 O  O     . HOH   F 6 .   ? 50.881 0.865   20.833 1.00 28.05 ? 348 HOH   A O     1 
HETATM 1482 O  O     . HOH   F 6 .   ? 34.352 -1.688  0.192  1.00 21.51 ? 349 HOH   A O     1 
HETATM 1483 O  O     . HOH   F 6 .   ? 19.443 6.024   7.686  1.00 35.12 ? 350 HOH   A O     1 
HETATM 1484 O  O     . HOH   F 6 .   ? 12.738 6.836   19.863 1.00 33.66 ? 351 HOH   A O     1 
HETATM 1485 O  O     . HOH   F 6 .   ? 44.425 -3.039  22.712 1.00 26.39 ? 352 HOH   A O     1 
HETATM 1486 O  O     . HOH   F 6 .   ? 24.249 1.435   4.635  1.00 35.89 ? 353 HOH   A O     1 
HETATM 1487 O  O     . HOH   F 6 .   ? 41.493 -9.868  14.593 1.00 44.66 ? 354 HOH   A O     1 
HETATM 1488 O  O     . HOH   F 6 .   ? 28.176 10.223  1.355  1.00 30.81 ? 355 HOH   A O     1 
HETATM 1489 O  O     . HOH   F 6 .   ? 14.556 7.833   30.381 1.00 35.63 ? 356 HOH   A O     1 
HETATM 1490 O  O     . HOH   F 6 .   ? 10.842 12.004  25.930 1.00 33.94 ? 357 HOH   A O     1 
HETATM 1491 O  O     . HOH   F 6 .   ? 10.865 2.428   31.842 1.00 27.37 ? 358 HOH   A O     1 
HETATM 1492 O  O     . HOH   F 6 .   ? 32.743 -10.787 23.400 1.00 23.51 ? 359 HOH   A O     1 
HETATM 1493 O  O     . HOH   F 6 .   ? 22.325 -10.748 29.950 1.00 32.57 ? 360 HOH   A O     1 
HETATM 1494 O  O     . HOH   F 6 .   ? 19.141 9.507   28.453 1.00 39.82 ? 361 HOH   A O     1 
HETATM 1495 O  O     . HOH   F 6 .   ? 14.173 -0.062  12.318 1.00 33.15 ? 362 HOH   A O     1 
HETATM 1496 O  O     . HOH   F 6 .   ? 41.674 -5.025  1.140  1.00 29.17 ? 363 HOH   A O     1 
HETATM 1497 O  O     . HOH   F 6 .   ? 24.004 8.534   6.362  1.00 37.32 ? 364 HOH   A O     1 
HETATM 1498 O  O     . HOH   F 6 .   ? 16.196 -7.965  7.927  1.00 31.29 ? 365 HOH   A O     1 
HETATM 1499 O  O     . HOH   F 6 .   ? 12.910 -2.807  17.709 1.00 32.50 ? 366 HOH   A O     1 
HETATM 1500 O  O     . HOH   F 6 .   ? 10.626 15.860  24.922 1.00 27.44 ? 367 HOH   A O     1 
HETATM 1501 O  O     . HOH   F 6 .   ? 30.554 10.397  23.213 1.00 25.79 ? 368 HOH   A O     1 
HETATM 1502 O  O     . HOH   F 6 .   ? 32.949 -9.688  0.499  1.00 27.73 ? 369 HOH   A O     1 
HETATM 1503 O  O     . HOH   F 6 .   ? 22.681 13.442  22.292 1.00 40.91 ? 370 HOH   A O     1 
HETATM 1504 O  O     . HOH   F 6 .   ? 18.691 15.090  15.353 1.00 35.48 ? 371 HOH   A O     1 
HETATM 1505 O  O     . HOH   F 6 .   ? 40.911 5.436   11.145 1.00 28.63 ? 372 HOH   A O     1 
HETATM 1506 O  O     . HOH   F 6 .   ? 26.723 6.235   -1.050 1.00 36.68 ? 373 HOH   A O     1 
HETATM 1507 O  O     . HOH   F 6 .   ? 25.665 -7.121  -0.316 1.00 33.51 ? 374 HOH   A O     1 
HETATM 1508 O  O     . HOH   F 6 .   ? 44.258 8.447   2.787  1.00 37.25 ? 375 HOH   A O     1 
HETATM 1509 O  O     . HOH   F 6 .   ? 21.046 -5.423  30.197 1.00 26.22 ? 376 HOH   A O     1 
HETATM 1510 O  O     . HOH   F 6 .   ? 24.261 -17.725 10.673 1.00 25.67 ? 377 HOH   A O     1 
HETATM 1511 O  O     . HOH   F 6 .   ? 38.722 -10.227 24.702 1.00 36.38 ? 378 HOH   A O     1 
HETATM 1512 O  O     . HOH   F 6 .   ? 33.677 12.096  23.984 1.00 32.79 ? 379 HOH   A O     1 
HETATM 1513 O  O     . HOH   F 6 .   ? 27.042 -20.252 17.864 1.00 32.37 ? 380 HOH   A O     1 
HETATM 1514 O  O     . HOH   F 6 .   ? 35.572 11.094  14.981 1.00 31.95 ? 381 HOH   A O     1 
HETATM 1515 O  O     . HOH   F 6 .   ? 19.456 -17.999 10.582 1.00 32.85 ? 382 HOH   A O     1 
HETATM 1516 O  O     . HOH   F 6 .   ? 38.621 -0.566  2.001  1.00 24.71 ? 383 HOH   A O     1 
HETATM 1517 O  O     . HOH   F 6 .   ? 36.725 -11.907 23.985 1.00 31.88 ? 384 HOH   A O     1 
HETATM 1518 O  O     . HOH   F 6 .   ? 31.249 11.078  9.083  1.00 35.27 ? 385 HOH   A O     1 
HETATM 1519 O  O     . HOH   F 6 .   ? 17.347 -2.144  -1.235 1.00 40.21 ? 386 HOH   A O     1 
HETATM 1520 O  O     . HOH   F 6 .   ? 44.314 11.039  8.115  1.00 37.86 ? 387 HOH   A O     1 
HETATM 1521 O  O     . HOH   F 6 .   ? 30.759 -10.404 2.198  1.00 30.59 ? 388 HOH   A O     1 
HETATM 1522 O  O     . HOH   F 6 .   ? 35.594 -6.895  32.224 1.00 39.31 ? 389 HOH   A O     1 
HETATM 1523 O  O     . HOH   F 6 .   ? 21.603 -17.503 12.186 1.00 22.96 ? 390 HOH   A O     1 
HETATM 1524 O  O     . HOH   F 6 .   ? 39.628 -9.943  22.215 1.00 30.62 ? 391 HOH   A O     1 
HETATM 1525 O  O     . HOH   F 6 .   ? 11.921 7.634   13.359 1.00 35.08 ? 392 HOH   A O     1 
HETATM 1526 O  O     . HOH   F 6 .   ? 17.846 17.509  20.512 1.00 29.72 ? 393 HOH   A O     1 
HETATM 1527 O  O     . HOH   F 6 .   ? 45.404 9.684   10.516 1.00 31.21 ? 394 HOH   A O     1 
HETATM 1528 O  O     . HOH   F 6 .   ? 30.529 -11.357 30.022 1.00 36.32 ? 395 HOH   A O     1 
HETATM 1529 O  O     . HOH   F 6 .   ? 10.056 5.956   31.224 1.00 39.51 ? 396 HOH   A O     1 
HETATM 1530 O  O     . HOH   F 6 .   ? 36.935 -1.775  3.794  1.00 29.64 ? 397 HOH   A O     1 
HETATM 1531 O  O     . HOH   F 6 .   ? 35.532 5.068   32.030 1.00 35.74 ? 398 HOH   A O     1 
HETATM 1532 O  O     . HOH   F 6 .   ? 23.082 15.746  20.732 1.00 35.50 ? 399 HOH   A O     1 
HETATM 1533 O  O     . HOH   F 6 .   ? 21.912 -21.440 12.352 1.00 38.54 ? 400 HOH   A O     1 
HETATM 1534 O  O     . HOH   F 6 .   ? 33.539 -13.080 21.855 1.00 39.13 ? 401 HOH   A O     1 
HETATM 1535 O  O     . HOH   F 6 .   ? 17.527 11.502  14.025 1.00 34.36 ? 402 HOH   A O     1 
HETATM 1536 O  O     . HOH   F 6 .   ? 22.976 4.522   5.639  1.00 30.27 ? 403 HOH   A O     1 
HETATM 1537 O  O     . HOH   F 6 .   ? 31.741 -11.557 6.250  1.00 33.95 ? 404 HOH   A O     1 
HETATM 1538 O  O     . HOH   F 6 .   ? 49.629 -2.788  8.845  1.00 35.91 ? 405 HOH   A O     1 
HETATM 1539 O  O     . HOH   F 6 .   ? 20.434 4.105   6.231  1.00 35.10 ? 406 HOH   A O     1 
HETATM 1540 O  O     . HOH   F 6 .   ? 14.084 13.009  16.855 1.00 38.00 ? 407 HOH   A O     1 
HETATM 1541 O  O     . HOH   F 6 .   ? 42.394 -7.675  3.990  1.00 33.57 ? 408 HOH   A O     1 
HETATM 1542 O  O     . HOH   F 6 .   ? 22.582 -3.715  32.040 1.00 41.99 ? 409 HOH   A O     1 
HETATM 1543 O  O     . HOH   F 6 .   ? 17.247 14.967  11.795 1.00 34.06 ? 410 HOH   A O     1 
HETATM 1544 O  O     . HOH   F 6 .   ? 12.893 17.310  25.184 1.00 34.63 ? 411 HOH   A O     1 
HETATM 1545 O  O     . HOH   F 6 .   ? 49.413 3.803   24.718 1.00 38.63 ? 412 HOH   A O     1 
HETATM 1546 O  O     . HOH   F 6 .   ? 25.874 15.550  19.991 1.00 36.29 ? 413 HOH   A O     1 
HETATM 1547 O  O     . HOH   F 6 .   ? 42.173 -9.511  22.154 1.00 34.80 ? 414 HOH   A O     1 
HETATM 1548 O  O     . HOH   F 6 .   ? 24.614 -7.425  31.655 1.00 33.33 ? 415 HOH   A O     1 
HETATM 1549 O  O     . HOH   F 6 .   ? 18.816 18.132  23.086 1.00 30.48 ? 416 HOH   A O     1 
HETATM 1550 O  O     . HOH   F 6 .   ? 50.329 1.558   23.522 1.00 28.71 ? 417 HOH   A O     1 
HETATM 1551 O  O     . HOH   F 6 .   ? 16.963 19.351  24.584 1.00 37.44 ? 418 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   ? 0.4560 0.6580 0.3356 -0.0010 0.0898  -0.0250 1   MET   A N     
2    C  CA    . MET   A 4   ? 0.4608 0.6018 0.3095 0.0161  0.0824  -0.0187 1   MET   A CA    
3    C  C     . MET   A 4   ? 0.3752 0.4544 0.3630 0.0572  0.0744  -0.0179 1   MET   A C     
4    O  O     . MET   A 4   ? 0.3844 0.4901 0.4516 0.0533  0.0987  -0.0091 1   MET   A O     
5    C  CB    . MET   A 4   ? 0.5161 0.6412 0.2877 -0.0427 0.0696  -0.0578 1   MET   A CB    
6    C  CG    . MET   A 4   ? 0.4211 0.5690 0.2252 0.0344  0.1328  -0.1182 1   MET   A CG    
7    S  SD    . MET   A 4   ? 0.4765 0.5174 0.3575 0.0760  0.1104  -0.0162 1   MET   A SD    
8    C  CE    . MET   A 4   ? 0.4015 0.5026 0.4633 0.1102  0.1312  -0.0290 1   MET   A CE    
9    N  N     . THR   A 5   ? 0.3073 0.4513 0.3601 0.0723  0.1032  -0.0608 2   THR   A N     
10   C  CA    . THR   A 5   ? 0.3282 0.4254 0.3268 0.0775  0.0811  -0.0520 2   THR   A CA    
11   C  C     . THR   A 5   ? 0.3184 0.3378 0.3251 0.0337  0.0755  -0.0302 2   THR   A C     
12   O  O     . THR   A 5   ? 0.3866 0.4478 0.2377 0.0587  0.0660  -0.0325 2   THR   A O     
13   C  CB    . THR   A 5   ? 0.3923 0.4899 0.4148 0.0769  0.0570  0.0376  2   THR   A CB    
14   O  OG1   . THR   A 5   ? 0.3602 0.5757 0.3153 0.0386  0.0450  0.0439  2   THR   A OG1   
15   C  CG2   . THR   A 5   ? 0.4638 0.5219 0.3695 0.0718  0.0543  0.0620  2   THR   A CG2   
16   N  N     . GLU   A 6   ? 0.3160 0.3520 0.3174 0.0130  0.0414  -0.0533 3   GLU   A N     
17   C  CA    . GLU   A 6   ? 0.3059 0.3617 0.1924 0.0294  0.0782  -0.0600 3   GLU   A CA    
18   C  C     . GLU   A 6   ? 0.3035 0.3775 0.2017 0.0296  0.0817  -0.0181 3   GLU   A C     
19   O  O     . GLU   A 6   ? 0.2893 0.4988 0.2916 0.0355  0.0288  -0.0615 3   GLU   A O     
20   C  CB    . GLU   A 6   ? 0.3868 0.4189 0.3004 -0.0135 0.1129  -0.0356 3   GLU   A CB    
21   C  CG    . GLU   A 6   ? 0.3814 0.5100 0.3499 0.0080  0.1068  -0.0113 3   GLU   A CG    
22   C  CD    . GLU   A 6   ? 0.4245 0.4028 0.4774 0.0020  0.0563  0.0408  3   GLU   A CD    
23   O  OE1   . GLU   A 6   ? 0.4518 0.5428 0.6107 0.0668  -0.0058 -0.1251 3   GLU   A OE1   
24   O  OE2   . GLU   A 6   ? 0.6520 0.3675 0.5120 -0.0190 0.0485  -0.0101 3   GLU   A OE2   
25   N  N     . TYR   A 7   ? 0.3006 0.3403 0.1507 0.0479  0.0856  -0.0191 4   TYR   A N     
26   C  CA    . TYR   A 7   ? 0.2956 0.3349 0.1274 0.0367  0.0791  -0.0090 4   TYR   A CA    
27   C  C     . TYR   A 7   ? 0.2670 0.3148 0.1740 0.0054  0.0454  0.0067  4   TYR   A C     
28   O  O     . TYR   A 7   ? 0.3110 0.3394 0.1372 0.0559  0.0659  -0.0045 4   TYR   A O     
29   C  CB    . TYR   A 7   ? 0.3170 0.2962 0.1522 0.0453  0.0964  -0.0086 4   TYR   A CB    
30   C  CG    . TYR   A 7   ? 0.2783 0.2835 0.2051 0.0419  0.0775  -0.0085 4   TYR   A CG    
31   C  CD1   . TYR   A 7   ? 0.3820 0.3499 0.2054 0.0536  0.0643  -0.0162 4   TYR   A CD1   
32   C  CD2   . TYR   A 7   ? 0.3424 0.2805 0.1588 0.0302  0.0735  0.0040  4   TYR   A CD2   
33   C  CE1   . TYR   A 7   ? 0.4480 0.3548 0.2076 0.0662  0.0181  -0.0113 4   TYR   A CE1   
34   C  CE2   . TYR   A 7   ? 0.3570 0.3082 0.2094 0.0402  0.0531  -0.0116 4   TYR   A CE2   
35   C  CZ    . TYR   A 7   ? 0.3658 0.2479 0.2473 0.0224  0.0334  0.0199  4   TYR   A CZ    
36   O  OH    . TYR   A 7   ? 0.4336 0.2956 0.2673 0.0705  0.0229  0.0253  4   TYR   A OH    
37   N  N     . LYS   A 8   ? 0.2800 0.2908 0.1411 0.0029  0.0244  0.0189  5   LYS   A N     
38   C  CA    . LYS   A 8   ? 0.2513 0.2867 0.1929 -0.0143 0.0450  0.0434  5   LYS   A CA    
39   C  C     . LYS   A 8   ? 0.2380 0.2329 0.1747 0.0041  0.0438  0.0106  5   LYS   A C     
40   O  O     . LYS   A 8   ? 0.2571 0.2670 0.1718 -0.0008 0.0450  -0.0288 5   LYS   A O     
41   C  CB    . LYS   A 8   ? 0.2856 0.3053 0.2230 -0.0260 0.0462  0.0098  5   LYS   A CB    
42   C  CG    . LYS   A 8   ? 0.2814 0.3839 0.3490 -0.0299 0.0781  0.0244  5   LYS   A CG    
43   C  CD    . LYS   A 8   ? 0.4624 0.4109 0.3799 -0.0534 0.0789  0.0193  5   LYS   A CD    
44   C  CE    . LYS   A 8   ? 0.5177 0.4979 0.4298 -0.1396 0.1047  0.0932  5   LYS   A CE    
45   N  NZ    . LYS   A 8   ? 0.5879 0.4872 0.4923 -0.0879 0.0345  0.0285  5   LYS   A NZ    
46   N  N     . LEU   A 9   ? 0.2137 0.2639 0.1411 0.0147  0.0710  -0.0261 6   LEU   A N     
47   C  CA    . LEU   A 9   ? 0.2170 0.2687 0.0935 0.0065  0.0432  0.0222  6   LEU   A CA    
48   C  C     . LEU   A 9   ? 0.2655 0.2615 0.1232 0.0185  0.0351  0.0157  6   LEU   A C     
49   O  O     . LEU   A 9   ? 0.2509 0.2522 0.1287 0.0109  0.0711  -0.0017 6   LEU   A O     
50   C  CB    . LEU   A 9   ? 0.2615 0.2470 0.1646 -0.0218 0.0449  0.0287  6   LEU   A CB    
51   C  CG    . LEU   A 9   ? 0.3285 0.2805 0.2345 0.0228  0.0456  0.0303  6   LEU   A CG    
52   C  CD1   . LEU   A 9   ? 0.3439 0.2858 0.2147 0.0226  0.0223  0.0551  6   LEU   A CD1   
53   C  CD2   . LEU   A 9   ? 0.3637 0.2302 0.2697 0.0086  0.0255  0.0353  6   LEU   A CD2   
54   N  N     . VAL   A 10  ? 0.2511 0.2422 0.1346 0.0080  0.0385  0.0045  7   VAL   A N     
55   C  CA    . VAL   A 10  ? 0.2258 0.2289 0.1529 -0.0159 0.0250  0.0378  7   VAL   A CA    
56   C  C     . VAL   A 10  ? 0.2112 0.2271 0.1758 -0.0097 0.0261  0.0051  7   VAL   A C     
57   O  O     . VAL   A 10  ? 0.2225 0.3049 0.1739 0.0054  0.0550  0.0338  7   VAL   A O     
58   C  CB    . VAL   A 10  ? 0.2862 0.2419 0.1539 -0.0183 0.0404  0.0178  7   VAL   A CB    
59   C  CG1   . VAL   A 10  ? 0.2816 0.2600 0.1879 -0.0030 0.0212  -0.0073 7   VAL   A CG1   
60   C  CG2   . VAL   A 10  ? 0.2828 0.2642 0.2153 0.0065  0.0171  0.0007  7   VAL   A CG2   
61   N  N     . VAL   A 11  ? 0.2080 0.2370 0.1225 0.0111  0.0263  -0.0238 8   VAL   A N     
62   C  CA    . VAL   A 11  ? 0.2287 0.2519 0.1418 0.0030  0.0150  -0.0032 8   VAL   A CA    
63   C  C     . VAL   A 11  ? 0.2437 0.2706 0.1307 0.0149  0.0233  -0.0022 8   VAL   A C     
64   O  O     . VAL   A 11  ? 0.2594 0.2816 0.1126 0.0310  0.0423  0.0060  8   VAL   A O     
65   C  CB    . VAL   A 11  ? 0.2348 0.2394 0.1343 0.0287  0.0220  -0.0145 8   VAL   A CB    
66   C  CG1   . VAL   A 11  ? 0.2292 0.3392 0.0975 0.0306  0.0405  -0.0362 8   VAL   A CG1   
67   C  CG2   . VAL   A 11  ? 0.2294 0.2676 0.1667 0.0178  0.0469  -0.0354 8   VAL   A CG2   
68   N  N     . VAL   A 12  ? 0.2428 0.2450 0.1292 0.0323  0.0367  -0.0099 9   VAL   A N     
69   C  CA    . VAL   A 12  ? 0.2512 0.2161 0.2064 0.0206  0.0061  -0.0409 9   VAL   A CA    
70   C  C     . VAL   A 12  ? 0.2637 0.2433 0.1412 0.0262  0.0256  -0.0150 9   VAL   A C     
71   O  O     . VAL   A 12  ? 0.2246 0.2790 0.1208 -0.0016 0.0802  -0.0109 9   VAL   A O     
72   C  CB    . VAL   A 12  ? 0.2701 0.2753 0.1495 0.0257  0.0263  -0.0149 9   VAL   A CB    
73   C  CG1   . VAL   A 12  ? 0.2452 0.3011 0.1898 0.0210  -0.0130 0.0028  9   VAL   A CG1   
74   C  CG2   . VAL   A 12  ? 0.2918 0.2844 0.1912 0.0317  0.0110  0.0030  9   VAL   A CG2   
75   N  N     . GLY   A 13  ? 0.2159 0.2280 0.1796 -0.0008 0.0391  0.0007  10  GLY   A N     
76   C  CA    . GLY   A 13  ? 0.2346 0.2834 0.1507 -0.0011 0.0772  -0.0113 10  GLY   A CA    
77   C  C     . GLY   A 13  ? 0.2198 0.2879 0.1752 0.0002  0.0486  -0.0378 10  GLY   A C     
78   O  O     . GLY   A 13  ? 0.2424 0.3016 0.1619 0.0310  0.0523  0.0071  10  GLY   A O     
79   N  N     . ALA   A 14  ? 0.2170 0.3030 0.1492 0.0089  0.0364  0.0228  11  ALA   A N     
80   C  CA    . ALA   A 14  ? 0.2379 0.2895 0.1778 0.0237  0.0518  -0.0005 11  ALA   A CA    
81   C  C     . ALA   A 14  ? 0.2656 0.2978 0.1948 -0.0068 0.0117  -0.0143 11  ALA   A C     
82   O  O     . ALA   A 14  ? 0.2811 0.2508 0.2148 0.0099  0.0149  -0.0036 11  ALA   A O     
83   C  CB    . ALA   A 14  ? 0.2546 0.3567 0.1191 0.0610  0.0895  -0.0216 11  ALA   A CB    
84   N  N     . GLY   A 15  ? 0.2721 0.3646 0.1444 0.0405  0.0649  -0.0211 12  GLY   A N     
85   C  CA    . GLY   A 15  ? 0.3103 0.3303 0.1732 0.0324  0.0396  0.0216  12  GLY   A CA    
86   C  C     . GLY   A 15  ? 0.2975 0.3289 0.1859 0.0110  0.0660  0.0098  12  GLY   A C     
87   O  O     . GLY   A 15  ? 0.2819 0.3419 0.1843 0.0096  0.0441  0.0330  12  GLY   A O     
88   N  N     . GLY   A 16  ? 0.2680 0.3484 0.1629 0.0172  0.0739  0.0318  13  GLY   A N     
89   C  CA    . GLY   A 16  ? 0.2620 0.3990 0.2469 0.0095  0.0529  -0.0145 13  GLY   A CA    
90   C  C     . GLY   A 16  ? 0.2143 0.3858 0.2006 0.0237  0.0569  -0.0275 13  GLY   A C     
91   O  O     . GLY   A 16  ? 0.2659 0.4725 0.1606 -0.0038 0.0158  0.0198  13  GLY   A O     
92   N  N     . VAL   A 17  ? 0.2407 0.3653 0.1672 0.0034  0.0561  -0.0205 14  VAL   A N     
93   C  CA    . VAL   A 17  ? 0.2188 0.3514 0.1312 0.0129  0.0679  -0.0117 14  VAL   A CA    
94   C  C     . VAL   A 17  ? 0.2514 0.3442 0.1315 0.0015  0.0648  -0.0093 14  VAL   A C     
95   O  O     . VAL   A 17  ? 0.2536 0.3680 0.0904 -0.0132 0.0552  0.0015  14  VAL   A O     
96   C  CB    . VAL   A 17  ? 0.2561 0.3192 0.1216 0.0191  0.0575  -0.0147 14  VAL   A CB    
97   C  CG1   . VAL   A 17  ? 0.2394 0.3165 0.1357 -0.0163 0.0724  -0.0246 14  VAL   A CG1   
98   C  CG2   . VAL   A 17  ? 0.2507 0.3050 0.1473 0.0053  0.0423  -0.0039 14  VAL   A CG2   
99   N  N     . GLY   A 18  ? 0.2485 0.3333 0.1216 -0.0275 0.0525  -0.0189 15  GLY   A N     
100  C  CA    . GLY   A 18  ? 0.2394 0.2972 0.1045 -0.0098 0.0306  -0.0053 15  GLY   A CA    
101  C  C     . GLY   A 18  ? 0.2475 0.2967 0.1619 -0.0288 0.0399  0.0204  15  GLY   A C     
102  O  O     . GLY   A 18  ? 0.2487 0.3084 0.1198 -0.0346 0.0569  -0.0046 15  GLY   A O     
103  N  N     . LYS   A 19  ? 0.2382 0.2680 0.1270 -0.0087 0.0531  0.0027  16  LYS   A N     
104  C  CA    . LYS   A 19  ? 0.2378 0.2625 0.1187 -0.0091 0.0635  0.0229  16  LYS   A CA    
105  C  C     . LYS   A 19  ? 0.2419 0.3175 0.1248 0.0089  0.0700  0.0160  16  LYS   A C     
106  O  O     . LYS   A 19  ? 0.2632 0.3021 0.1104 0.0073  0.0547  0.0224  16  LYS   A O     
107  C  CB    . LYS   A 19  ? 0.2312 0.2896 0.1055 -0.0297 0.0671  0.0187  16  LYS   A CB    
108  C  CG    . LYS   A 19  ? 0.2632 0.3329 0.0943 -0.0115 0.0598  0.0300  16  LYS   A CG    
109  C  CD    . LYS   A 19  ? 0.2288 0.3122 0.1625 0.0039  0.0865  -0.0057 16  LYS   A CD    
110  C  CE    . LYS   A 19  ? 0.2774 0.2703 0.1623 -0.0282 0.0769  0.0000  16  LYS   A CE    
111  N  NZ    . LYS   A 19  ? 0.2662 0.3075 0.1720 0.0129  0.0279  0.0054  16  LYS   A NZ    
112  N  N     . SER   A 20  ? 0.2153 0.3168 0.1322 0.0074  0.0700  0.0149  17  SER   A N     
113  C  CA    . SER   A 20  ? 0.2236 0.2968 0.1564 -0.0085 0.1057  0.0013  17  SER   A CA    
114  C  C     . SER   A 20  ? 0.2288 0.2770 0.2207 0.0061  0.0347  0.0060  17  SER   A C     
115  O  O     . SER   A 20  ? 0.2639 0.3053 0.1508 0.0108  0.0456  0.0052  17  SER   A O     
116  C  CB    . SER   A 20  ? 0.2521 0.3057 0.1228 -0.0104 0.0906  0.0085  17  SER   A CB    
117  O  OG    . SER   A 20  ? 0.2875 0.2895 0.1487 0.0023  0.0686  -0.0089 17  SER   A OG    
118  N  N     . ALA   A 21  ? 0.2683 0.3056 0.0793 -0.0390 0.0437  0.0132  18  ALA   A N     
119  C  CA    . ALA   A 21  ? 0.2533 0.3179 0.1030 -0.0246 0.0525  -0.0103 18  ALA   A CA    
120  C  C     . ALA   A 21  ? 0.2830 0.3246 0.0883 0.0022  0.0340  -0.0303 18  ALA   A C     
121  O  O     . ALA   A 21  ? 0.2861 0.3082 0.0827 -0.0177 0.0562  -0.0278 18  ALA   A O     
122  C  CB    . ALA   A 21  ? 0.2677 0.3444 0.1132 -0.0366 0.0264  -0.0061 18  ALA   A CB    
123  N  N     . LEU   A 22  ? 0.2663 0.3129 0.0711 -0.0047 0.0664  -0.0111 19  LEU   A N     
124  C  CA    . LEU   A 22  ? 0.2843 0.2952 0.1232 -0.0362 0.0355  -0.0009 19  LEU   A CA    
125  C  C     . LEU   A 22  ? 0.2717 0.3028 0.1142 0.0020  0.0313  -0.0029 19  LEU   A C     
126  O  O     . LEU   A 22  ? 0.2817 0.2917 0.0952 -0.0212 0.0626  0.0316  19  LEU   A O     
127  C  CB    . LEU   A 22  ? 0.2903 0.2890 0.1281 -0.0411 0.0129  0.0221  19  LEU   A CB    
128  C  CG    . LEU   A 22  ? 0.2731 0.2889 0.1385 -0.0199 0.0487  -0.0152 19  LEU   A CG    
129  C  CD1   . LEU   A 22  ? 0.3149 0.3475 0.1439 0.0168  0.0224  -0.0188 19  LEU   A CD1   
130  C  CD2   . LEU   A 22  ? 0.2935 0.2981 0.1612 -0.0136 0.0759  -0.0028 19  LEU   A CD2   
131  N  N     . THR   A 23  ? 0.2606 0.3046 0.1022 -0.0213 0.0433  0.0148  20  THR   A N     
132  C  CA    . THR   A 23  ? 0.2407 0.2981 0.1462 -0.0177 0.0398  -0.0148 20  THR   A CA    
133  C  C     . THR   A 23  ? 0.2872 0.2874 0.1495 0.0168  0.0215  -0.0312 20  THR   A C     
134  O  O     . THR   A 23  ? 0.3224 0.2665 0.1464 -0.0021 0.0851  -0.0058 20  THR   A O     
135  C  CB    . THR   A 23  ? 0.2599 0.2801 0.1253 -0.0212 0.0776  -0.0116 20  THR   A CB    
136  O  OG1   . THR   A 23  ? 0.2873 0.2876 0.1151 -0.0107 0.0354  0.0028  20  THR   A OG1   
137  C  CG2   . THR   A 23  ? 0.2631 0.2653 0.2043 -0.0157 0.0900  -0.0008 20  THR   A CG2   
138  N  N     . ILE   A 24  ? 0.2600 0.3120 0.1414 -0.0141 0.0500  0.0096  21  ILE   A N     
139  C  CA    . ILE   A 24  ? 0.2561 0.3439 0.1359 -0.0211 0.0352  -0.0081 21  ILE   A CA    
140  C  C     . ILE   A 24  ? 0.2707 0.3073 0.1445 0.0020  0.0499  0.0180  21  ILE   A C     
141  O  O     . ILE   A 24  ? 0.3005 0.3010 0.1496 -0.0165 0.0797  -0.0125 21  ILE   A O     
142  C  CB    . ILE   A 24  ? 0.3105 0.3381 0.1501 -0.0215 0.0337  0.0140  21  ILE   A CB    
143  C  CG1   . ILE   A 24  ? 0.3722 0.3757 0.1700 -0.0970 0.0237  0.0164  21  ILE   A CG1   
144  C  CG2   . ILE   A 24  ? 0.3194 0.3437 0.1509 -0.0047 0.0258  0.0443  21  ILE   A CG2   
145  C  CD1   . ILE   A 24  ? 0.3780 0.3729 0.2114 -0.0697 0.0403  0.0078  21  ILE   A CD1   
146  N  N     . GLN   A 25  ? 0.2754 0.2880 0.1298 -0.0095 0.0590  -0.0070 22  GLN   A N     
147  C  CA    . GLN   A 25  ? 0.2920 0.2935 0.0988 -0.0268 0.0485  0.0178  22  GLN   A CA    
148  C  C     . GLN   A 25  ? 0.3361 0.2453 0.1777 -0.0004 0.0497  -0.0204 22  GLN   A C     
149  O  O     . GLN   A 25  ? 0.3648 0.3113 0.1451 -0.0092 0.0949  -0.0284 22  GLN   A O     
150  C  CB    . GLN   A 25  ? 0.3341 0.3307 0.0951 -0.0401 0.0774  0.0178  22  GLN   A CB    
151  C  CG    . GLN   A 25  ? 0.3506 0.3217 0.1333 -0.0065 0.0407  -0.0281 22  GLN   A CG    
152  C  CD    . GLN   A 25  ? 0.3346 0.3613 0.1047 -0.0249 0.0570  -0.0309 22  GLN   A CD    
153  O  OE1   . GLN   A 25  ? 0.3347 0.3960 0.1919 -0.0175 0.0877  -0.0340 22  GLN   A OE1   
154  N  NE2   . GLN   A 25  ? 0.3654 0.3709 0.1536 -0.0715 0.0269  -0.0038 22  GLN   A NE2   
155  N  N     . LEU   A 26  ? 0.3339 0.3168 0.1255 -0.0185 0.0696  -0.0025 23  LEU   A N     
156  C  CA    . LEU   A 26  ? 0.3469 0.2778 0.1416 0.0038  0.0443  0.0193  23  LEU   A CA    
157  C  C     . LEU   A 26  ? 0.3099 0.3011 0.1581 -0.0194 0.0606  -0.0206 23  LEU   A C     
158  O  O     . LEU   A 26  ? 0.3437 0.3313 0.1598 0.0208  0.0546  -0.0164 23  LEU   A O     
159  C  CB    . LEU   A 26  ? 0.3430 0.2646 0.1685 -0.0090 0.0350  0.0000  23  LEU   A CB    
160  C  CG    . LEU   A 26  ? 0.3409 0.2928 0.1689 -0.0027 0.0701  -0.0146 23  LEU   A CG    
161  C  CD1   . LEU   A 26  ? 0.3634 0.2929 0.1663 0.0277  0.0962  -0.0162 23  LEU   A CD1   
162  C  CD2   . LEU   A 26  ? 0.4055 0.3222 0.1333 -0.0533 0.0943  -0.0121 23  LEU   A CD2   
163  N  N     . ILE   A 27  ? 0.2761 0.3117 0.1580 -0.0066 0.1042  -0.0226 24  ILE   A N     
164  C  CA    . ILE   A 27  ? 0.2658 0.3679 0.1388 -0.0127 0.0690  0.0193  24  ILE   A CA    
165  C  C     . ILE   A 27  ? 0.2711 0.3194 0.1945 -0.0167 0.0580  -0.0415 24  ILE   A C     
166  O  O     . ILE   A 27  ? 0.3264 0.4222 0.1597 0.0177  0.0856  -0.0370 24  ILE   A O     
167  C  CB    . ILE   A 27  ? 0.2422 0.3593 0.1766 -0.0067 0.0809  0.0316  24  ILE   A CB    
168  C  CG1   . ILE   A 27  ? 0.3341 0.2926 0.2074 -0.0039 0.0331  0.0225  24  ILE   A CG1   
169  C  CG2   . ILE   A 27  ? 0.2680 0.3419 0.2287 -0.0141 0.0905  0.0499  24  ILE   A CG2   
170  C  CD1   . ILE   A 27  ? 0.3434 0.2870 0.1905 0.0073  0.0502  0.0079  24  ILE   A CD1   
171  N  N     . GLN   A 28  ? 0.2789 0.3214 0.1218 -0.0282 0.0625  -0.0134 25  GLN   A N     
172  C  CA    . GLN   A 28  ? 0.2830 0.3545 0.1437 -0.0308 0.0461  -0.0264 25  GLN   A CA    
173  C  C     . GLN   A 28  ? 0.3550 0.3613 0.1599 -0.0506 0.0388  -0.0323 25  GLN   A C     
174  O  O     . GLN   A 28  ? 0.3578 0.3768 0.1399 -0.0483 0.0662  -0.0448 25  GLN   A O     
175  C  CB    . GLN   A 28  ? 0.2643 0.4083 0.1160 -0.0169 0.0499  -0.0001 25  GLN   A CB    
176  C  CG    . GLN   A 28  ? 0.3329 0.3872 0.1774 -0.0096 0.0379  -0.0555 25  GLN   A CG    
177  C  CD    . GLN   A 28  ? 0.3557 0.3764 0.2041 -0.0389 0.0234  0.0116  25  GLN   A CD    
178  O  OE1   . GLN   A 28  ? 0.3655 0.4670 0.2526 -0.0085 -0.0108 0.0681  25  GLN   A OE1   
179  N  NE2   . GLN   A 28  ? 0.4897 0.3616 0.2974 -0.0391 0.0723  0.0143  25  GLN   A NE2   
180  N  N     . ASN   A 29  ? 0.3644 0.3131 0.1611 -0.0343 0.0854  -0.0619 26  ASN   A N     
181  C  CA    . ASN   A 29  ? 0.3965 0.2786 0.0967 -0.0196 0.0666  -0.0134 26  ASN   A CA    
182  C  C     . ASN   A 29  ? 0.3671 0.3273 0.1075 -0.0690 0.0997  0.0002  26  ASN   A C     
183  O  O     . ASN   A 29  ? 0.3897 0.3296 0.1936 -0.0689 0.0941  -0.0223 26  ASN   A O     
184  C  CB    . ASN   A 29  ? 0.3852 0.4095 0.1139 0.0327  0.0664  -0.0618 26  ASN   A CB    
185  C  CG    . ASN   A 29  ? 0.4975 0.3211 0.3021 0.0420  0.0311  -0.0491 26  ASN   A CG    
186  O  OD1   . ASN   A 29  ? 0.6615 0.4523 0.3397 -0.0910 0.0422  0.0113  26  ASN   A OD1   
187  N  ND2   . ASN   A 29  ? 0.5020 0.5199 0.5941 -0.0542 0.0126  -0.0134 26  ASN   A ND2   
188  N  N     . HIS   A 30  ? 0.3439 0.3215 0.1205 -0.0444 0.0624  0.0199  27  HIS   A N     
189  C  CA    . HIS   A 30  ? 0.3427 0.3177 0.1445 -0.0546 0.0740  0.0165  27  HIS   A CA    
190  C  C     . HIS   A 30  ? 0.3197 0.3528 0.1975 -0.0292 0.0502  -0.0254 27  HIS   A C     
191  O  O     . HIS   A 30  ? 0.3085 0.3568 0.1785 -0.0252 0.0652  -0.0678 27  HIS   A O     
192  C  CB    . HIS   A 30  ? 0.3368 0.3098 0.2319 -0.0365 0.0871  0.0555  27  HIS   A CB    
193  C  CG    . HIS   A 30  ? 0.2822 0.3765 0.2774 -0.0398 0.1071  0.0500  27  HIS   A CG    
194  N  ND1   . HIS   A 30  ? 0.2885 0.4764 0.2565 -0.0686 0.0674  0.0781  27  HIS   A ND1   
195  C  CD2   . HIS   A 30  ? 0.3981 0.3520 0.3433 -0.0489 0.0870  0.0654  27  HIS   A CD2   
196  C  CE1   . HIS   A 30  ? 0.3725 0.4300 0.3338 -0.0180 0.0750  0.0661  27  HIS   A CE1   
197  N  NE2   . HIS   A 30  ? 0.3710 0.4337 0.3842 -0.0562 0.0942  0.0329  27  HIS   A NE2   
198  N  N     . PHE   A 31  ? 0.3286 0.4105 0.1256 -0.0185 0.0373  -0.0231 28  PHE   A N     
199  C  CA    . PHE   A 31  ? 0.3444 0.3940 0.1648 -0.0273 0.0592  -0.0464 28  PHE   A CA    
200  C  C     . PHE   A 31  ? 0.3633 0.4214 0.1593 -0.0018 0.0408  0.0052  28  PHE   A C     
201  O  O     . PHE   A 31  ? 0.4624 0.4583 0.1990 0.0525  -0.0282 -0.0066 28  PHE   A O     
202  C  CB    . PHE   A 31  ? 0.3405 0.4480 0.1756 -0.0409 0.0678  0.0010  28  PHE   A CB    
203  C  CG    . PHE   A 31  ? 0.2951 0.4532 0.1643 -0.0100 0.0116  -0.0121 28  PHE   A CG    
204  C  CD1   . PHE   A 31  ? 0.2687 0.4167 0.1841 -0.0464 0.0150  -0.0326 28  PHE   A CD1   
205  C  CD2   . PHE   A 31  ? 0.2829 0.4970 0.1762 0.0264  0.0639  0.0343  28  PHE   A CD2   
206  C  CE1   . PHE   A 31  ? 0.3329 0.4607 0.2027 -0.0155 0.0291  -0.0381 28  PHE   A CE1   
207  C  CE2   . PHE   A 31  ? 0.2167 0.5614 0.2297 0.0149  0.0574  -0.0084 28  PHE   A CE2   
208  C  CZ    . PHE   A 31  ? 0.3162 0.4378 0.2067 0.0089  0.0763  -0.0313 28  PHE   A CZ    
209  N  N     . VAL   A 32  ? 0.3089 0.4008 0.2308 -0.0085 0.0263  -0.0226 29  VAL   A N     
210  C  CA    . VAL   A 32  ? 0.3367 0.4109 0.2743 0.0055  0.0494  -0.0117 29  VAL   A CA    
211  C  C     . VAL   A 32  ? 0.3876 0.4159 0.2694 -0.0099 -0.0040 0.0100  29  VAL   A C     
212  O  O     . VAL   A 32  ? 0.3741 0.5396 0.3753 -0.0324 -0.0281 0.0251  29  VAL   A O     
213  C  CB    . VAL   A 32  ? 0.3736 0.3818 0.3453 0.0189  -0.0012 -0.0434 29  VAL   A CB    
214  C  CG1   . VAL   A 32  ? 0.3700 0.4402 0.2776 0.0167  0.0241  -0.0645 29  VAL   A CG1   
215  C  CG2   . VAL   A 32  ? 0.4005 0.3849 0.3559 0.0435  0.0259  -0.0444 29  VAL   A CG2   
216  N  N     . ASP   A 33  ? 0.3950 0.4810 0.3237 0.0714  0.0042  0.0586  30  ASP   A N     
217  C  CA    . ASP   A 33  ? 0.4546 0.4862 0.2518 0.0653  -0.0161 0.0939  30  ASP   A CA    
218  C  C     . ASP   A 33  ? 0.3729 0.5131 0.3005 0.0522  -0.0083 0.0499  30  ASP   A C     
219  O  O     . ASP   A 33  ? 0.4368 0.5910 0.3620 0.0195  -0.0239 -0.0267 30  ASP   A O     
220  C  CB    . ASP   A 33  ? 0.4471 0.4973 0.2361 0.0911  0.0667  0.0665  30  ASP   A CB    
221  C  CG    . ASP   A 33  ? 0.3813 0.5047 0.3476 -0.0061 0.0229  -0.0141 30  ASP   A CG    
222  O  OD1   . ASP   A 33  ? 0.5093 0.4322 0.3736 -0.0610 -0.0002 0.0911  30  ASP   A OD1   
223  O  OD2   . ASP   A 33  ? 0.4023 0.6999 0.3644 0.0438  0.0674  0.1092  30  ASP   A OD2   
224  N  N     . GLU   A 34  ? 0.3756 0.6111 0.3593 0.0588  -0.0252 0.0219  31  GLU   A N     
225  C  CA    . GLU   A 34  ? 0.4285 0.5786 0.4775 0.0717  0.0290  0.0096  31  GLU   A CA    
226  C  C     . GLU   A 34  ? 0.5131 0.5250 0.3095 0.0736  0.0375  -0.0563 31  GLU   A C     
227  O  O     . GLU   A 34  ? 0.5125 0.5483 0.3823 0.0732  -0.0626 -0.0723 31  GLU   A O     
228  C  CB    . GLU   A 34  ? 0.4431 0.6735 0.6139 0.0496  0.0566  -0.0228 31  GLU   A CB    
229  C  CG    . GLU   A 34  ? 0.3419 0.3419 0.3419 0.0000  0.0000  0.0000  31  GLU   A CG    
230  C  CD    . GLU   A 34  ? 0.3419 0.3419 0.3419 0.0000  0.0000  0.0000  31  GLU   A CD    
231  O  OE1   . GLU   A 34  ? 0.3419 0.3419 0.3419 0.0000  0.0000  0.0000  31  GLU   A OE1   
232  O  OE2   . GLU   A 34  ? 0.3419 0.3419 0.3419 0.0000  0.0000  0.0000  31  GLU   A OE2   
233  N  N     . TYR   A 35  ? 0.5723 0.5204 0.3025 0.0991  -0.0058 -0.0240 32  TYR   A N     
234  C  CA    . TYR   A 35  ? 0.5294 0.4518 0.2974 0.0762  -0.0156 -0.0797 32  TYR   A CA    
235  C  C     . TYR   A 35  ? 0.5415 0.3809 0.3490 0.0625  -0.0530 -0.0202 32  TYR   A C     
236  O  O     . TYR   A 35  ? 0.6157 0.4053 0.4485 0.0334  0.0033  0.0247  32  TYR   A O     
237  C  CB    . TYR   A 35  ? 0.5629 0.4896 0.3406 0.0460  -0.0688 -0.1009 32  TYR   A CB    
238  C  CG    . TYR   A 35  ? 0.5508 0.4159 0.2630 0.0442  -0.0658 -0.0239 32  TYR   A CG    
239  C  CD1   . TYR   A 35  ? 0.5011 0.4015 0.3517 0.0339  -0.0876 -0.0472 32  TYR   A CD1   
240  C  CD2   . TYR   A 35  ? 0.5274 0.4272 0.2884 0.0366  -0.1325 0.0270  32  TYR   A CD2   
241  C  CE1   . TYR   A 35  ? 0.5746 0.3766 0.3149 0.0545  -0.0483 -0.0062 32  TYR   A CE1   
242  C  CE2   . TYR   A 35  ? 0.4799 0.3728 0.4014 0.0377  -0.1082 0.0254  32  TYR   A CE2   
243  C  CZ    . TYR   A 35  ? 0.5474 0.3642 0.3608 0.0738  -0.0632 0.0132  32  TYR   A CZ    
244  O  OH    . TYR   A 35  ? 0.6148 0.3737 0.2782 0.0723  -0.0621 0.0121  32  TYR   A OH    
245  N  N     . ASP   A 36  ? 0.4726 0.4929 0.3547 0.0739  0.0152  0.0475  33  ASP   A N     
246  C  CA    . ASP   A 36  ? 0.5006 0.5246 0.2813 0.0645  0.0142  0.0403  33  ASP   A CA    
247  C  C     . ASP   A 36  ? 0.5501 0.4432 0.3430 0.1301  -0.0498 0.0286  33  ASP   A C     
248  O  O     . ASP   A 36  ? 0.4712 0.3920 0.4357 0.0974  -0.0170 0.0013  33  ASP   A O     
249  C  CB    . ASP   A 36  ? 0.6253 0.5312 0.3572 0.0727  0.0770  -0.0141 33  ASP   A CB    
250  C  CG    . ASP   A 36  ? 0.6073 0.3888 0.3920 0.0644  0.0334  -0.0194 33  ASP   A CG    
251  O  OD1   . ASP   A 36  ? 0.6328 0.4148 0.4238 0.0188  0.0396  0.0452  33  ASP   A OD1   
252  O  OD2   . ASP   A 36  ? 0.6555 0.5622 0.4800 -0.0645 -0.0421 -0.0755 33  ASP   A OD2   
253  N  N     . PRO   A 37  ? 0.4664 0.4838 0.3530 0.1073  -0.0630 0.0058  34  PRO   A N     
254  C  CA    . PRO   A 37  ? 0.4587 0.4799 0.3286 0.1068  -0.0172 0.0237  34  PRO   A CA    
255  C  C     . PRO   A 37  ? 0.4607 0.3563 0.3968 -0.0271 -0.0190 0.0696  34  PRO   A C     
256  O  O     . PRO   A 37  ? 0.5004 0.4224 0.4220 -0.0661 -0.0193 0.1280  34  PRO   A O     
257  C  CB    . PRO   A 37  ? 0.4724 0.4842 0.3667 0.0799  -0.0015 -0.0176 34  PRO   A CB    
258  C  CG    . PRO   A 37  ? 0.5549 0.5402 0.3688 0.0872  0.0008  0.0074  34  PRO   A CG    
259  C  CD    . PRO   A 37  ? 0.5093 0.4574 0.3417 0.1143  -0.0189 0.0474  34  PRO   A CD    
260  N  N     . THR   A 38  ? 0.4360 0.4150 0.3900 0.0691  0.0144  0.0493  35  THR   A N     
261  C  CA    . THR   A 38  ? 0.4129 0.3443 0.2507 0.0346  0.0383  0.0182  35  THR   A CA    
262  C  C     . THR   A 38  ? 0.3834 0.4105 0.2583 0.0252  0.0443  -0.0052 35  THR   A C     
263  O  O     . THR   A 38  ? 0.4882 0.4816 0.2312 0.0102  0.0582  -0.0474 35  THR   A O     
264  C  CB    . THR   A 38  ? 0.4440 0.3571 0.1883 -0.0024 -0.0261 0.0260  35  THR   A CB    
265  O  OG1   . THR   A 38  ? 0.4034 0.4002 0.2464 0.0050  -0.0467 0.0268  35  THR   A OG1   
266  C  CG2   . THR   A 38  ? 0.4227 0.3955 0.3323 -0.0277 -0.0272 0.0408  35  THR   A CG2   
267  N  N     . ILE   A 39  ? 0.3431 0.4408 0.2707 0.0076  -0.0606 0.0197  36  ILE   A N     
268  C  CA    . ILE   A 39  ? 0.3734 0.3857 0.3440 0.0206  -0.0709 -0.0066 36  ILE   A CA    
269  C  C     . ILE   A 39  ? 0.3787 0.2996 0.3163 0.0091  -0.0662 -0.0045 36  ILE   A C     
270  O  O     . ILE   A 39  ? 0.4023 0.3457 0.3151 0.0289  -0.0389 -0.0004 36  ILE   A O     
271  C  CB    . ILE   A 39  ? 0.5418 0.3884 0.3907 0.0232  -0.0521 0.0245  36  ILE   A CB    
272  C  CG1   . ILE   A 39  ? 0.5478 0.4721 0.4379 -0.0020 -0.0885 0.0136  36  ILE   A CG1   
273  C  CG2   . ILE   A 39  ? 0.5530 0.4258 0.4251 0.0077  -0.0496 0.0089  36  ILE   A CG2   
274  C  CD1   . ILE   A 39  ? 0.5907 0.4660 0.6007 -0.0177 -0.0137 0.0233  36  ILE   A CD1   
275  N  N     . GLU   A 40  ? 0.2887 0.3722 0.2824 0.0030  -0.0106 -0.0351 37  GLU   A N     
276  C  CA    . GLU   A 40  ? 0.2717 0.2628 0.3013 0.0383  0.0413  -0.0255 37  GLU   A CA    
277  C  C     . GLU   A 40  ? 0.2713 0.2614 0.2407 -0.0024 0.0230  -0.0284 37  GLU   A C     
278  O  O     . GLU   A 40  ? 0.3599 0.3025 0.2298 0.0202  0.0669  0.0177  37  GLU   A O     
279  C  CB    . GLU   A 40  ? 0.3216 0.2237 0.3299 0.0217  0.0164  -0.0420 37  GLU   A CB    
280  C  CG    . GLU   A 40  ? 0.3260 0.2213 0.3204 0.0192  0.0286  -0.0243 37  GLU   A CG    
281  C  CD    . GLU   A 40  ? 0.3300 0.2979 0.3215 0.0109  0.0470  -0.0612 37  GLU   A CD    
282  O  OE1   . GLU   A 40  ? 0.3932 0.3213 0.2888 -0.0347 0.0461  -0.0238 37  GLU   A OE1   
283  O  OE2   . GLU   A 40  ? 0.3433 0.3383 0.2690 -0.0106 0.1205  -0.0259 37  GLU   A OE2   
284  N  N     . ASP   A 41  ? 0.2610 0.2869 0.1934 0.0297  0.0518  0.0168  38  ASP   A N     
285  C  CA    . ASP   A 41  ? 0.2797 0.2884 0.1823 0.0183  0.0635  -0.0095 38  ASP   A CA    
286  C  C     . ASP   A 41  ? 0.2640 0.2770 0.1919 -0.0040 0.0371  0.0163  38  ASP   A C     
287  O  O     . ASP   A 41  ? 0.2852 0.2613 0.1685 -0.0035 0.0374  0.0000  38  ASP   A O     
288  C  CB    . ASP   A 41  ? 0.3594 0.2175 0.2021 0.0096  0.0050  0.0162  38  ASP   A CB    
289  C  CG    . ASP   A 41  ? 0.3652 0.3201 0.2396 -0.0336 0.0025  0.0587  38  ASP   A CG    
290  O  OD1   . ASP   A 41  ? 0.3629 0.2836 0.1812 -0.0144 0.0519  0.0464  38  ASP   A OD1   
291  O  OD2   . ASP   A 41  ? 0.4712 0.3466 0.2298 -0.0389 -0.0152 0.0263  38  ASP   A OD2   
292  N  N     . SER   A 42  ? 0.2658 0.2664 0.1551 -0.0091 0.0442  0.0444  39  SER   A N     
293  C  CA    . SER   A 42  ? 0.2691 0.2676 0.1624 0.0084  0.0756  0.0106  39  SER   A CA    
294  C  C     . SER   A 42  ? 0.2758 0.2498 0.1451 0.0101  0.0310  0.0103  39  SER   A C     
295  O  O     . SER   A 42  ? 0.3454 0.2667 0.1449 0.0030  0.0410  0.0296  39  SER   A O     
296  C  CB    . SER   A 42  ? 0.3244 0.2877 0.1320 -0.0318 0.0357  0.0302  39  SER   A CB    
297  O  OG    . SER   A 42  ? 0.2931 0.3157 0.1921 -0.0068 0.1004  0.0125  39  SER   A OG    
298  N  N     . TYR   A 43  ? 0.2871 0.2466 0.1138 0.0048  0.0562  -0.0154 40  TYR   A N     
299  C  CA    . TYR   A 43  ? 0.3268 0.2887 0.0753 0.0197  0.0534  -0.0171 40  TYR   A CA    
300  C  C     . TYR   A 43  ? 0.3787 0.2915 0.1518 0.0377  0.0433  0.0160  40  TYR   A C     
301  O  O     . TYR   A 43  ? 0.3430 0.2634 0.1474 0.0503  0.0751  0.0298  40  TYR   A O     
302  C  CB    . TYR   A 43  ? 0.3373 0.3003 0.1241 0.0306  0.0138  -0.0257 40  TYR   A CB    
303  C  CG    . TYR   A 43  ? 0.3097 0.3029 0.1359 0.0245  0.0377  -0.0145 40  TYR   A CG    
304  C  CD1   . TYR   A 43  ? 0.2957 0.3310 0.1501 -0.0035 0.0576  -0.0227 40  TYR   A CD1   
305  C  CD2   . TYR   A 43  ? 0.3115 0.3668 0.1772 0.0075  0.0307  0.0565  40  TYR   A CD2   
306  C  CE1   . TYR   A 43  ? 0.3160 0.2795 0.1355 -0.0005 0.0553  0.0152  40  TYR   A CE1   
307  C  CE2   . TYR   A 43  ? 0.3124 0.3516 0.1411 0.0248  0.0688  0.0284  40  TYR   A CE2   
308  C  CZ    . TYR   A 43  ? 0.2570 0.3669 0.1593 0.0301  0.0448  0.0075  40  TYR   A CZ    
309  O  OH    . TYR   A 43  ? 0.3041 0.3356 0.1922 0.0429  0.0445  0.0182  40  TYR   A OH    
310  N  N     . ARG   A 44  ? 0.3669 0.2942 0.1652 0.0294  0.0593  0.0210  41  ARG   A N     
311  C  CA    . ARG   A 44  ? 0.3426 0.3176 0.1321 0.0147  0.0664  0.0315  41  ARG   A CA    
312  C  C     . ARG   A 44  ? 0.3093 0.3086 0.2016 0.0058  0.0463  0.0263  41  ARG   A C     
313  O  O     . ARG   A 44  ? 0.3913 0.3340 0.1531 0.0284  0.0487  0.0236  41  ARG   A O     
314  C  CB    . ARG   A 44  ? 0.3263 0.3322 0.2718 0.0173  0.0856  0.0439  41  ARG   A CB    
315  C  CG    . ARG   A 44  ? 0.3854 0.4799 0.3572 -0.0663 0.0409  0.0408  41  ARG   A CG    
316  C  CD    . ARG   A 44  ? 0.5539 0.4337 0.4858 -0.0547 -0.0247 0.0088  41  ARG   A CD    
317  N  NE    . ARG   A 44  ? 0.5335 0.5568 0.4204 0.0308  0.0048  -0.0225 41  ARG   A NE    
318  C  CZ    . ARG   A 44  ? 0.5515 0.5216 0.2460 0.0024  0.0064  -0.0091 41  ARG   A CZ    
319  N  NH1   . ARG   A 44  ? 0.4713 0.4591 0.2380 0.0094  0.0964  0.0679  41  ARG   A NH1   
320  N  NH2   . ARG   A 44  ? 0.5898 0.5628 0.3127 0.0608  0.0298  0.0346  41  ARG   A NH2   
321  N  N     . LYS   A 45  ? 0.3239 0.2792 0.1241 0.0012  0.1113  0.0110  42  LYS   A N     
322  C  CA    . LYS   A 45  ? 0.3434 0.3064 0.1238 0.0242  0.0662  -0.0275 42  LYS   A CA    
323  C  C     . LYS   A 45  ? 0.3676 0.3282 0.1506 0.0457  0.1039  0.0189  42  LYS   A C     
324  O  O     . LYS   A 45  ? 0.3636 0.3079 0.1548 0.0422  0.0649  0.0095  42  LYS   A O     
325  C  CB    . LYS   A 45  ? 0.3401 0.2860 0.2208 0.0472  0.0410  -0.0548 42  LYS   A CB    
326  C  CG    . LYS   A 45  ? 0.3651 0.2978 0.3269 0.0100  0.0275  -0.0283 42  LYS   A CG    
327  C  CD    . LYS   A 45  ? 0.3654 0.3405 0.3130 0.0045  0.0519  0.0227  42  LYS   A CD    
328  C  CE    . LYS   A 45  ? 0.4369 0.3913 0.3272 0.0116  0.0127  -0.0351 42  LYS   A CE    
329  N  NZ    . LYS   A 45  ? 0.5209 0.4820 0.3312 -0.0047 -0.0066 -0.0502 42  LYS   A NZ    
330  N  N     . GLN   A 46  ? 0.3452 0.3300 0.1081 0.0533  0.0882  0.0317  43  GLN   A N     
331  C  CA    . GLN   A 46  ? 0.3503 0.3291 0.0919 0.0611  0.1009  -0.0003 43  GLN   A CA    
332  C  C     . GLN   A 46  ? 0.3325 0.3618 0.1438 0.0190  0.0856  0.0063  43  GLN   A C     
333  O  O     . GLN   A 46  ? 0.3894 0.3226 0.1861 0.0118  0.0509  -0.0109 43  GLN   A O     
334  C  CB    . GLN   A 46  ? 0.3296 0.3219 0.1570 0.0247  0.1160  0.0228  43  GLN   A CB    
335  C  CG    . GLN   A 46  ? 0.3283 0.3595 0.2141 0.0309  0.1036  0.0425  43  GLN   A CG    
336  C  CD    . GLN   A 46  ? 0.3413 0.3526 0.2113 0.0312  0.1164  0.0211  43  GLN   A CD    
337  O  OE1   . GLN   A 46  ? 0.3637 0.4294 0.2091 -0.0105 0.1190  0.0383  43  GLN   A OE1   
338  N  NE2   . GLN   A 46  ? 0.3924 0.3941 0.2389 0.1082  0.0878  0.0383  43  GLN   A NE2   
339  N  N     . VAL   A 47  ? 0.3821 0.3308 0.1295 0.0243  0.0295  -0.0225 44  VAL   A N     
340  C  CA    . VAL   A 47  ? 0.4103 0.3901 0.1335 -0.0036 0.0750  -0.0486 44  VAL   A CA    
341  C  C     . VAL   A 47  ? 0.3677 0.3138 0.1573 -0.0089 0.1125  -0.0378 44  VAL   A C     
342  O  O     . VAL   A 47  ? 0.4332 0.3095 0.2737 0.0077  0.0070  0.0101  44  VAL   A O     
343  C  CB    . VAL   A 47  ? 0.4124 0.3899 0.2280 0.0187  0.1031  -0.0035 44  VAL   A CB    
344  C  CG1   . VAL   A 47  ? 0.4872 0.4498 0.2043 0.0240  0.0480  0.0108  44  VAL   A CG1   
345  C  CG2   . VAL   A 47  ? 0.4915 0.3678 0.2332 -0.0026 0.0810  0.0048  44  VAL   A CG2   
346  N  N     . VAL   A 48  ? 0.4196 0.3331 0.1440 -0.0224 0.0718  0.0035  45  VAL   A N     
347  C  CA    . VAL   A 48  ? 0.3830 0.2755 0.2629 -0.0291 0.0403  -0.0174 45  VAL   A CA    
348  C  C     . VAL   A 48  ? 0.3768 0.3379 0.2123 -0.0441 0.0112  -0.0103 45  VAL   A C     
349  O  O     . VAL   A 48  ? 0.3824 0.3576 0.2085 -0.0511 0.0204  0.0112  45  VAL   A O     
350  C  CB    . VAL   A 48  ? 0.4389 0.3052 0.2508 0.0215  0.0944  0.0251  45  VAL   A CB    
351  C  CG1   . VAL   A 48  ? 0.3764 0.3676 0.2344 0.0296  0.0390  -0.0325 45  VAL   A CG1   
352  C  CG2   . VAL   A 48  ? 0.4408 0.3765 0.1805 0.0258  0.0940  0.0220  45  VAL   A CG2   
353  N  N     . ILE   A 49  ? 0.4364 0.2828 0.1903 -0.0166 0.0262  0.0147  46  ILE   A N     
354  C  CA    . ILE   A 49  ? 0.3959 0.3538 0.2023 -0.0085 0.0644  -0.0189 46  ILE   A CA    
355  C  C     . ILE   A 49  ? 0.3505 0.3528 0.1836 -0.0172 0.0530  -0.0099 46  ILE   A C     
356  O  O     . ILE   A 49  ? 0.3117 0.3419 0.2373 -0.0056 0.0770  0.0358  46  ILE   A O     
357  C  CB    . ILE   A 49  ? 0.4788 0.2916 0.1867 -0.0075 0.0739  0.0385  46  ILE   A CB    
358  C  CG1   . ILE   A 49  ? 0.4935 0.3474 0.1752 0.0378  0.0397  -0.0164 46  ILE   A CG1   
359  C  CG2   . ILE   A 49  ? 0.4656 0.3196 0.2252 -0.0280 0.1143  0.0344  46  ILE   A CG2   
360  C  CD1   . ILE   A 49  ? 0.5238 0.3331 0.1813 0.0368  0.0721  0.0227  46  ILE   A CD1   
361  N  N     . ASP   A 50  ? 0.3420 0.3750 0.2156 0.0178  -0.0279 0.0075  47  ASP   A N     
362  C  CA    . ASP   A 50  ? 0.3794 0.2722 0.2157 -0.0056 0.0398  0.0142  47  ASP   A CA    
363  C  C     . ASP   A 50  ? 0.3743 0.3137 0.2290 0.0266  0.0063  0.0330  47  ASP   A C     
364  O  O     . ASP   A 50  ? 0.3596 0.3509 0.1979 -0.0187 0.0549  0.0592  47  ASP   A O     
365  C  CB    . ASP   A 50  ? 0.4021 0.3485 0.2192 -0.0356 0.0608  0.0401  47  ASP   A CB    
366  C  CG    . ASP   A 50  ? 0.3542 0.3100 0.2899 -0.0520 0.0146  0.0006  47  ASP   A CG    
367  O  OD1   . ASP   A 50  ? 0.3810 0.4447 0.2289 -0.0804 0.0064  0.0237  47  ASP   A OD1   
368  O  OD2   . ASP   A 50  ? 0.3762 0.3335 0.2646 0.0057  0.0319  0.0143  47  ASP   A OD2   
369  N  N     . GLY   A 51  ? 0.3332 0.3477 0.2252 0.0031  0.0626  0.0082  48  GLY   A N     
370  C  CA    . GLY   A 51  ? 0.3265 0.3157 0.3117 0.0208  0.0541  -0.0141 48  GLY   A CA    
371  C  C     . GLY   A 51  ? 0.2737 0.3646 0.3089 0.0274  0.0027  0.0129  48  GLY   A C     
372  O  O     . GLY   A 51  ? 0.3163 0.4320 0.3212 0.0282  0.0554  -0.0067 48  GLY   A O     
373  N  N     . GLU   A 52  ? 0.3928 0.3425 0.2618 0.0000  0.0254  0.0172  49  GLU   A N     
374  C  CA    . GLU   A 52  ? 0.3828 0.3454 0.2418 0.0187  0.0122  0.0353  49  GLU   A CA    
375  C  C     . GLU   A 52  ? 0.3500 0.3053 0.2859 0.0190  0.0197  0.0173  49  GLU   A C     
376  O  O     . GLU   A 52  ? 0.3579 0.2995 0.2596 0.0205  0.0087  0.0216  49  GLU   A O     
377  C  CB    . GLU   A 52  ? 0.3654 0.3201 0.2672 0.0633  0.0461  -0.0201 49  GLU   A CB    
378  C  CG    . GLU   A 52  ? 0.3350 0.3604 0.2919 0.0297  0.0433  0.0230  49  GLU   A CG    
379  C  CD    . GLU   A 52  ? 0.3349 0.3897 0.3596 0.0127  0.0133  0.0624  49  GLU   A CD    
380  O  OE1   . GLU   A 52  ? 0.4273 0.3987 0.3122 -0.0415 0.0019  0.0575  49  GLU   A OE1   
381  O  OE2   . GLU   A 52  ? 0.3315 0.3434 0.3817 0.0171  0.0523  0.0870  49  GLU   A OE2   
382  N  N     . THR   A 53  ? 0.3610 0.3228 0.2393 0.0341  0.0361  -0.0008 50  THR   A N     
383  C  CA    . THR   A 53  ? 0.3798 0.3443 0.2134 0.0511  0.0410  -0.0023 50  THR   A CA    
384  C  C     . THR   A 53  ? 0.3418 0.3582 0.2111 0.0246  0.0174  -0.0140 50  THR   A C     
385  O  O     . THR   A 53  ? 0.3958 0.3819 0.2927 -0.0179 -0.0216 -0.0213 50  THR   A O     
386  C  CB    . THR   A 53  ? 0.3297 0.3273 0.2988 0.0133  0.0519  0.0322  50  THR   A CB    
387  O  OG1   . THR   A 53  ? 0.4670 0.3456 0.2920 0.0253  0.0409  0.0072  50  THR   A OG1   
388  C  CG2   . THR   A 53  ? 0.3825 0.3619 0.2818 0.0519  0.0658  0.0306  50  THR   A CG2   
389  N  N     . CYS   A 54  ? 0.4325 0.3323 0.1511 0.0664  0.0667  0.0155  51  CYS   A N     
390  C  CA    . CYS   A 54  ? 0.3922 0.3311 0.2212 0.0544  0.0676  0.0026  51  CYS   A CA    
391  C  C     . CYS   A 54  ? 0.3539 0.3168 0.2275 -0.0009 0.0531  0.0096  51  CYS   A C     
392  O  O     . CYS   A 54  ? 0.3508 0.3077 0.2216 0.0433  0.0470  -0.0014 51  CYS   A O     
393  C  CB    . CYS   A 54  ? 0.4075 0.3536 0.2425 0.0923  0.0867  0.0127  51  CYS   A CB    
394  S  SG    . CYS   A 54  ? 0.4360 0.3678 0.1958 0.0335  0.0967  0.0021  51  CYS   A SG    
395  N  N     . LEU   A 55  ? 0.3383 0.3100 0.1753 0.0413  0.0818  -0.0208 52  LEU   A N     
396  C  CA    . LEU   A 55  ? 0.3021 0.3510 0.1998 0.0388  0.0826  -0.0031 52  LEU   A CA    
397  C  C     . LEU   A 55  ? 0.3128 0.2724 0.2144 0.0334  0.0818  -0.0078 52  LEU   A C     
398  O  O     . LEU   A 55  ? 0.2874 0.3474 0.2032 0.0327  0.0900  -0.0093 52  LEU   A O     
399  C  CB    . LEU   A 55  ? 0.2971 0.3715 0.2200 0.0140  0.0795  -0.0005 52  LEU   A CB    
400  C  CG    . LEU   A 55  ? 0.3706 0.3771 0.2401 0.0015  0.0643  0.0226  52  LEU   A CG    
401  C  CD1   . LEU   A 55  ? 0.4243 0.2640 0.2602 -0.0007 0.0751  0.0003  52  LEU   A CD1   
402  C  CD2   . LEU   A 55  ? 0.4295 0.3624 0.2548 -0.0122 -0.0018 0.0429  52  LEU   A CD2   
403  N  N     . LEU   A 56  ? 0.3151 0.2718 0.1109 0.0469  0.1108  0.0097  53  LEU   A N     
404  C  CA    . LEU   A 56  ? 0.2942 0.2897 0.1144 0.0345  0.0963  -0.0194 53  LEU   A CA    
405  C  C     . LEU   A 56  ? 0.3038 0.3134 0.1509 0.0180  0.0252  0.0296  53  LEU   A C     
406  O  O     . LEU   A 56  ? 0.4137 0.2789 0.1563 0.0843  0.0439  0.0039  53  LEU   A O     
407  C  CB    . LEU   A 56  ? 0.2788 0.2940 0.1465 0.0635  0.0814  -0.0316 53  LEU   A CB    
408  C  CG    . LEU   A 56  ? 0.3513 0.2780 0.1709 0.0354  0.0806  -0.0518 53  LEU   A CG    
409  C  CD1   . LEU   A 56  ? 0.3686 0.2992 0.2345 0.0307  0.0787  -0.0496 53  LEU   A CD1   
410  C  CD2   . LEU   A 56  ? 0.3850 0.2401 0.1681 0.0043  0.0988  -0.0005 53  LEU   A CD2   
411  N  N     . ASP   A 57  ? 0.2630 0.3053 0.1522 0.0087  0.0905  0.0100  54  ASP   A N     
412  C  CA    . ASP   A 57  ? 0.2600 0.3367 0.1430 0.0504  0.0618  0.0174  54  ASP   A CA    
413  C  C     . ASP   A 57  ? 0.2519 0.2800 0.1726 0.0244  0.0666  0.0102  54  ASP   A C     
414  O  O     . ASP   A 57  ? 0.2480 0.2958 0.1520 0.0246  0.0878  0.0254  54  ASP   A O     
415  C  CB    . ASP   A 57  ? 0.3166 0.3388 0.1478 0.0341  0.1007  -0.0018 54  ASP   A CB    
416  C  CG    . ASP   A 57  ? 0.3389 0.3099 0.1737 -0.0100 0.1093  -0.0289 54  ASP   A CG    
417  O  OD1   . ASP   A 57  ? 0.3520 0.3004 0.1661 0.0047  0.0564  0.0031  54  ASP   A OD1   
418  O  OD2   . ASP   A 57  ? 0.3382 0.3545 0.3428 0.0049  0.0333  -0.0253 54  ASP   A OD2   
419  N  N     . ILE   A 58  ? 0.2337 0.2497 0.1418 0.0028  0.0807  -0.0013 55  ILE   A N     
420  C  CA    . ILE   A 58  ? 0.2363 0.3206 0.1159 0.0016  0.0769  0.0242  55  ILE   A CA    
421  C  C     . ILE   A 58  ? 0.2730 0.3294 0.1206 0.0271  0.0544  0.0126  55  ILE   A C     
422  O  O     . ILE   A 58  ? 0.2540 0.3080 0.1252 0.0356  0.0559  0.0129  55  ILE   A O     
423  C  CB    . ILE   A 58  ? 0.2658 0.3234 0.1302 0.0058  0.0585  0.0367  55  ILE   A CB    
424  C  CG1   . ILE   A 58  ? 0.2717 0.3104 0.1430 -0.0112 0.1032  0.0084  55  ILE   A CG1   
425  C  CG2   . ILE   A 58  ? 0.2364 0.3649 0.1344 0.0033  0.0402  0.0275  55  ILE   A CG2   
426  C  CD1   . ILE   A 58  ? 0.2726 0.3044 0.1795 0.0158  0.0847  0.0024  55  ILE   A CD1   
427  N  N     . LEU   A 59  ? 0.2751 0.2464 0.1089 0.0003  0.0494  0.0130  56  LEU   A N     
428  C  CA    . LEU   A 59  ? 0.2494 0.2378 0.1426 -0.0191 0.0255  0.0442  56  LEU   A CA    
429  C  C     . LEU   A 59  ? 0.2514 0.2332 0.1772 -0.0058 0.0427  0.0257  56  LEU   A C     
430  O  O     . LEU   A 59  ? 0.2751 0.2684 0.1258 0.0179  0.0310  0.0322  56  LEU   A O     
431  C  CB    . LEU   A 59  ? 0.2550 0.2470 0.1366 -0.0233 0.0333  0.0344  56  LEU   A CB    
432  C  CG    . LEU   A 59  ? 0.2629 0.2506 0.1784 -0.0217 0.0207  0.0368  56  LEU   A CG    
433  C  CD1   . LEU   A 59  ? 0.2727 0.2831 0.1814 -0.0259 0.0346  0.0417  56  LEU   A CD1   
434  C  CD2   . LEU   A 59  ? 0.2835 0.2535 0.2007 -0.0265 0.0374  -0.0018 56  LEU   A CD2   
435  N  N     . ASP   A 60  ? 0.2360 0.2352 0.1574 0.0298  0.0744  0.0112  57  ASP   A N     
436  C  CA    . ASP   A 60  ? 0.2541 0.2470 0.1500 -0.0042 0.0324  0.0219  57  ASP   A CA    
437  C  C     . ASP   A 60  ? 0.2755 0.2456 0.1836 0.0054  0.0500  0.0242  57  ASP   A C     
438  O  O     . ASP   A 60  ? 0.2995 0.2742 0.1815 0.0044  0.0356  0.0365  57  ASP   A O     
439  C  CB    . ASP   A 60  ? 0.2747 0.2524 0.1428 0.0129  0.0187  0.0324  57  ASP   A CB    
440  C  CG    . ASP   A 60  ? 0.2754 0.2675 0.1846 0.0126  0.0461  0.0224  57  ASP   A CG    
441  O  OD1   . ASP   A 60  ? 0.2621 0.2679 0.1733 0.0092  0.0485  0.0214  57  ASP   A OD1   
442  O  OD2   . ASP   A 60  ? 0.2520 0.2903 0.1737 0.0103  0.0548  0.0093  57  ASP   A OD2   
443  N  N     . THR   A 61  ? 0.2710 0.2220 0.1645 0.0116  0.0252  0.0319  58  THR   A N     
444  C  CA    . THR   A 61  ? 0.2636 0.2274 0.1886 -0.0173 0.0209  0.0105  58  THR   A CA    
445  C  C     . THR   A 61  ? 0.2845 0.2881 0.1326 0.0186  0.0583  -0.0192 58  THR   A C     
446  O  O     . THR   A 61  ? 0.3005 0.2916 0.1814 0.0185  0.0603  -0.0163 58  THR   A O     
447  C  CB    . THR   A 61  ? 0.2757 0.2331 0.1790 0.0020  0.0082  0.0083  58  THR   A CB    
448  O  OG1   . THR   A 61  ? 0.2864 0.2837 0.1554 0.0078  0.0690  -0.0151 58  THR   A OG1   
449  C  CG2   . THR   A 61  ? 0.2868 0.3211 0.1698 0.0303  0.0023  -0.0143 58  THR   A CG2   
450  N  N     . ALA   A 62  ? 0.2775 0.2828 0.2042 0.0019  0.0628  -0.0224 59  ALA   A N     
451  C  CA    . ALA   A 62  ? 0.2920 0.3025 0.1997 0.0270  0.0551  0.0124  59  ALA   A CA    
452  C  C     . ALA   A 62  ? 0.2946 0.3273 0.2051 0.0286  0.0592  -0.0079 59  ALA   A C     
453  O  O     . ALA   A 62  ? 0.2841 0.3722 0.2394 -0.0182 0.0353  0.0063  59  ALA   A O     
454  C  CB    . ALA   A 62  ? 0.2458 0.3023 0.2549 0.0218  0.0590  0.0452  59  ALA   A CB    
455  N  N     . GLY   A 63  ? 0.3098 0.3133 0.2153 0.0313  0.0297  0.0138  60  GLY   A N     
456  C  CA    . GLY   A 63  ? 0.3133 0.3027 0.2299 0.0221  0.0288  0.0734  60  GLY   A CA    
457  C  C     . GLY   A 63  ? 0.2996 0.2874 0.2709 0.0162  0.0373  0.0448  60  GLY   A C     
458  O  O     . GLY   A 63  ? 0.3306 0.2731 0.1930 0.0206  0.0596  0.0131  60  GLY   A O     
459  N  N     . GLN   A 64  ? 0.3377 0.2856 0.2454 0.0198  0.0779  0.0231  61  GLN   A N     
460  C  CA    . GLN   A 64  ? 0.3489 0.2605 0.2268 0.0110  0.0583  0.0412  61  GLN   A CA    
461  C  C     . GLN   A 64  ? 0.3325 0.2976 0.2784 0.0185  0.0720  0.0218  61  GLN   A C     
462  O  O     . GLN   A 64  ? 0.3128 0.3514 0.2980 0.0032  0.0904  -0.0242 61  GLN   A O     
463  C  CB    . GLN   A 64  ? 0.3637 0.2520 0.2364 -0.0019 0.0485  0.0416  61  GLN   A CB    
464  C  CG    . GLN   A 64  ? 0.3600 0.2919 0.1618 0.0172  0.0536  0.0152  61  GLN   A CG    
465  C  CD    . GLN   A 64  ? 0.3323 0.3084 0.2402 0.0327  0.0431  -0.0215 61  GLN   A CD    
466  O  OE1   . GLN   A 64  ? 0.4161 0.3053 0.2296 0.0107  0.0478  -0.0176 61  GLN   A OE1   
467  N  NE2   . GLN   A 64  ? 0.3631 0.3533 0.2511 0.0718  0.0565  -0.0196 61  GLN   A NE2   
468  N  N     . GLU   A 65  ? 0.3316 0.3578 0.2290 0.0414  0.1097  -0.0154 62  GLU   A N     
469  C  CA    . GLU   A 65  ? 0.3223 0.3671 0.3463 0.0733  0.0857  -0.0093 62  GLU   A CA    
470  C  C     . GLU   A 65  ? 0.4534 0.3311 0.3531 0.0792  0.0284  -0.0137 62  GLU   A C     
471  O  O     . GLU   A 65  ? 0.4043 0.3663 0.4843 0.0640  0.0973  -0.0423 62  GLU   A O     
472  C  CB    . GLU   A 65  ? 0.3190 0.4215 0.3532 0.0896  0.0854  -0.0364 62  GLU   A CB    
473  C  CG    . GLU   A 65  ? 0.4109 0.4052 0.4710 0.0455  0.0480  -0.1081 62  GLU   A CG    
474  C  CD    . GLU   A 65  ? 0.4619 0.3857 0.5023 0.0194  -0.0308 -0.0979 62  GLU   A CD    
475  O  OE1   . GLU   A 65  ? 0.4780 0.5013 0.5480 0.0036  0.0404  -0.0829 62  GLU   A OE1   
476  O  OE2   . GLU   A 65  ? 0.4994 0.4939 0.4506 -0.0419 0.0185  -0.0497 62  GLU   A OE2   
477  N  N     . GLU   A 66  ? 0.3999 0.3709 0.3880 0.0522  0.0807  0.0222  63  GLU   A N     
478  C  CA    . GLU   A 66  ? 0.4621 0.3340 0.3427 0.0796  0.0215  -0.0034 63  GLU   A CA    
479  C  C     . GLU   A 66  ? 0.3968 0.3866 0.4383 0.0748  0.0568  0.0272  63  GLU   A C     
480  O  O     . GLU   A 66  ? 0.4350 0.3643 0.3621 -0.0096 0.0851  0.0469  63  GLU   A O     
481  C  CB    . GLU   A 66  ? 0.5378 0.3641 0.3294 0.0972  0.0483  0.0345  63  GLU   A CB    
482  C  CG    . GLU   A 66  ? 0.3419 0.3419 0.3419 0.0000  0.0000  0.0000  63  GLU   A CG    
483  C  CD    . GLU   A 66  ? 0.3419 0.3419 0.3419 0.0000  0.0000  0.0000  63  GLU   A CD    
484  O  OE1   . GLU   A 66  ? 0.3419 0.3419 0.3419 0.0000  0.0000  0.0000  63  GLU   A OE1   
485  O  OE2   . GLU   A 66  ? 0.3419 0.3419 0.3419 0.0000  0.0000  0.0000  63  GLU   A OE2   
486  N  N     . TYR   A 67  ? 0.4656 0.3761 0.5308 0.0024  0.0246  0.0264  64  TYR   A N     
487  C  CA    . TYR   A 67  ? 0.4121 0.4274 0.4241 0.0382  0.0180  0.0369  64  TYR   A CA    
488  C  C     . TYR   A 67  ? 0.4174 0.4824 0.3163 0.0418  0.0199  -0.0213 64  TYR   A C     
489  O  O     . TYR   A 67  ? 0.4204 0.3320 0.3063 -0.0025 0.0119  0.0017  64  TYR   A O     
490  C  CB    . TYR   A 67  ? 0.4507 0.3885 0.4085 0.0049  0.0175  -0.0207 64  TYR   A CB    
491  C  CG    . TYR   A 67  ? 0.4328 0.3880 0.3340 -0.0209 0.1115  0.0062  64  TYR   A CG    
492  C  CD1   . TYR   A 67  ? 0.4658 0.5422 0.4117 -0.0376 0.0346  -0.0418 64  TYR   A CD1   
493  C  CD2   . TYR   A 67  ? 0.4542 0.4757 0.4641 -0.0763 0.1581  0.0845  64  TYR   A CD2   
494  C  CE1   . TYR   A 67  ? 0.5011 0.4305 0.4136 -0.1122 0.1259  -0.0369 64  TYR   A CE1   
495  C  CE2   . TYR   A 67  ? 0.4966 0.4084 0.3463 -0.0489 0.1079  0.0155  64  TYR   A CE2   
496  C  CZ    . TYR   A 67  ? 0.4196 0.4252 0.3686 -0.0470 0.0591  0.0338  64  TYR   A CZ    
497  O  OH    . TYR   A 67  ? 0.4280 0.4368 0.3602 -0.0251 0.0559  -0.0510 64  TYR   A OH    
498  N  N     . SER   A 68  ? 0.2737 0.4051 0.3949 -0.0434 0.0714  0.0281  65  SER   A N     
499  C  CA    . SER   A 68  ? 0.3009 0.2874 0.4304 -0.0329 0.0661  -0.0058 65  SER   A CA    
500  C  C     . SER   A 68  ? 0.3593 0.3767 0.2921 -0.0417 0.0845  -0.0219 65  SER   A C     
501  O  O     . SER   A 68  ? 0.5653 0.3565 0.2701 0.0008  0.0508  0.0551  65  SER   A O     
502  C  CB    . SER   A 68  ? 0.3521 0.2826 0.4220 -0.0299 0.1191  -0.0182 65  SER   A CB    
503  O  OG    . SER   A 68  ? 0.3315 0.3648 0.4167 -0.0002 0.0717  -0.0081 65  SER   A OG    
504  N  N     . ALA   A 69  ? 0.3267 0.3261 0.3596 -0.0127 0.0809  -0.0056 66  ALA   A N     
505  C  CA    . ALA   A 69  ? 0.4041 0.2642 0.2917 -0.0094 0.0444  0.0048  66  ALA   A CA    
506  C  C     . ALA   A 69  ? 0.3857 0.2800 0.2701 -0.0140 0.0313  -0.0218 66  ALA   A C     
507  O  O     . ALA   A 69  ? 0.4153 0.2920 0.2795 -0.0031 0.0044  -0.0537 66  ALA   A O     
508  C  CB    . ALA   A 69  ? 0.4232 0.2945 0.3255 -0.0510 0.0141  0.0005  66  ALA   A CB    
509  N  N     . MET   A 70  ? 0.4592 0.2506 0.3102 -0.0112 -0.0254 -0.0192 67  MET   A N     
510  C  CA    . MET   A 70  ? 0.4130 0.2877 0.2592 -0.0174 0.0289  0.0131  67  MET   A CA    
511  C  C     . MET   A 70  ? 0.3490 0.2652 0.2410 0.0006  0.0461  0.0078  67  MET   A C     
512  O  O     . MET   A 70  ? 0.3387 0.2938 0.1987 0.0117  0.0411  -0.0524 67  MET   A O     
513  C  CB    . MET   A 70  ? 0.4611 0.2793 0.2521 -0.0238 0.0119  0.0135  67  MET   A CB    
514  C  CG    . MET   A 70  ? 0.5251 0.3245 0.3086 -0.0141 0.0618  0.0613  67  MET   A CG    
515  S  SD    . MET   A 70  ? 0.5046 0.3103 0.2826 0.0002  0.0800  0.0349  67  MET   A SD    
516  C  CE    . MET   A 70  ? 0.4131 0.4567 0.2610 -0.0452 0.0586  0.1105  67  MET   A CE    
517  N  N     . ARG   A 71  ? 0.3069 0.2648 0.2377 0.0168  0.0296  -0.0263 68  ARG   A N     
518  C  CA    . ARG   A 71  ? 0.2889 0.2457 0.2282 0.0143  0.0393  -0.0324 68  ARG   A CA    
519  C  C     . ARG   A 71  ? 0.2878 0.2674 0.1844 -0.0086 0.0474  0.0041  68  ARG   A C     
520  O  O     . ARG   A 71  ? 0.2806 0.2773 0.1930 0.0045  0.0208  -0.0453 68  ARG   A O     
521  C  CB    . ARG   A 71  ? 0.2916 0.3547 0.2321 0.0790  0.0529  -0.0280 68  ARG   A CB    
522  C  CG    . ARG   A 71  ? 0.2734 0.3350 0.3521 0.0581  0.0704  -0.0256 68  ARG   A CG    
523  C  CD    . ARG   A 71  ? 0.3341 0.2885 0.3044 0.0168  0.0992  -0.0002 68  ARG   A CD    
524  N  NE    . ARG   A 71  ? 0.3666 0.3047 0.3231 -0.0051 0.1238  0.0082  68  ARG   A NE    
525  C  CZ    . ARG   A 71  ? 0.3119 0.2891 0.2567 -0.0423 0.0753  -0.0031 68  ARG   A CZ    
526  N  NH1   . ARG   A 71  ? 0.4432 0.3046 0.2957 0.0105  0.0730  -0.0536 68  ARG   A NH1   
527  N  NH2   . ARG   A 71  ? 0.3534 0.3166 0.3577 -0.0286 0.0214  0.0151  68  ARG   A NH2   
528  N  N     . ASP   A 72  ? 0.2708 0.2928 0.2268 -0.0189 0.0488  -0.0115 69  ASP   A N     
529  C  CA    . ASP   A 72  ? 0.2616 0.2738 0.2658 -0.0222 0.0439  -0.0197 69  ASP   A CA    
530  C  C     . ASP   A 72  ? 0.2658 0.2727 0.2270 -0.0239 0.0417  -0.0032 69  ASP   A C     
531  O  O     . ASP   A 72  ? 0.2890 0.2820 0.2038 0.0030  0.0626  -0.0522 69  ASP   A O     
532  C  CB    . ASP   A 72  ? 0.3291 0.2947 0.3151 -0.0198 0.0255  -0.0581 69  ASP   A CB    
533  C  CG    . ASP   A 72  ? 0.3205 0.3519 0.3193 -0.0232 0.0255  -0.0696 69  ASP   A CG    
534  O  OD1   . ASP   A 72  ? 0.3581 0.3413 0.3267 -0.0382 0.0354  -0.0667 69  ASP   A OD1   
535  O  OD2   . ASP   A 72  ? 0.4456 0.3838 0.4170 -0.0383 0.0127  -0.1074 69  ASP   A OD2   
536  N  N     . GLN   A 73  ? 0.2825 0.2244 0.2199 0.0007  0.0416  -0.0071 70  GLN   A N     
537  C  CA    . GLN   A 73  ? 0.2683 0.2625 0.2386 -0.0141 0.0338  -0.0071 70  GLN   A CA    
538  C  C     . GLN   A 73  ? 0.2962 0.2526 0.1918 -0.0228 0.0297  0.0373  70  GLN   A C     
539  O  O     . GLN   A 73  ? 0.2970 0.2475 0.2113 -0.0091 0.0062  0.0192  70  GLN   A O     
540  C  CB    . GLN   A 73  ? 0.2625 0.2424 0.2447 -0.0244 0.0151  -0.0011 70  GLN   A CB    
541  C  CG    . GLN   A 73  ? 0.2978 0.2404 0.1879 -0.0381 0.0329  -0.0053 70  GLN   A CG    
542  C  CD    . GLN   A 73  ? 0.2659 0.2974 0.2099 -0.0175 0.0596  -0.0110 70  GLN   A CD    
543  O  OE1   . GLN   A 73  ? 0.3420 0.3283 0.3355 -0.0199 0.0059  -0.0542 70  GLN   A OE1   
544  N  NE2   . GLN   A 73  ? 0.2777 0.2795 0.2271 -0.0164 0.0796  -0.0151 70  GLN   A NE2   
545  N  N     . TYR   A 74  ? 0.2560 0.2498 0.1615 -0.0180 0.0883  -0.0105 71  TYR   A N     
546  C  CA    . TYR   A 74  ? 0.1889 0.2179 0.2399 -0.0124 0.0318  0.0229  71  TYR   A CA    
547  C  C     . TYR   A 74  ? 0.2285 0.2737 0.2045 0.0176  0.0731  0.0381  71  TYR   A C     
548  O  O     . TYR   A 74  ? 0.2170 0.2766 0.2084 0.0016  0.0654  -0.0015 71  TYR   A O     
549  C  CB    . TYR   A 74  ? 0.2331 0.2244 0.2199 0.0147  0.0225  -0.0017 71  TYR   A CB    
550  C  CG    . TYR   A 74  ? 0.2464 0.2912 0.1713 -0.0074 0.0427  -0.0127 71  TYR   A CG    
551  C  CD1   . TYR   A 74  ? 0.2423 0.2791 0.1907 0.0071  0.0493  -0.0075 71  TYR   A CD1   
552  C  CD2   . TYR   A 74  ? 0.2600 0.3400 0.1273 0.0175  0.0594  -0.0211 71  TYR   A CD2   
553  C  CE1   . TYR   A 74  ? 0.2571 0.3202 0.2315 -0.0106 0.0746  -0.0147 71  TYR   A CE1   
554  C  CE2   . TYR   A 74  ? 0.2690 0.3358 0.1763 0.0446  0.0417  -0.0748 71  TYR   A CE2   
555  C  CZ    . TYR   A 74  ? 0.2300 0.3294 0.2192 0.0050  0.0460  -0.0881 71  TYR   A CZ    
556  O  OH    . TYR   A 74  ? 0.2442 0.4059 0.2493 0.0219  0.0587  -0.0448 71  TYR   A OH    
557  N  N     . MET   A 75  ? 0.2190 0.2574 0.1926 -0.0021 0.0492  0.0320  72  MET   A N     
558  C  CA    . MET   A 75  ? 0.2611 0.2341 0.1811 0.0018  0.0350  0.0278  72  MET   A CA    
559  C  C     . MET   A 75  ? 0.2756 0.2967 0.1722 0.0133  0.0175  0.0067  72  MET   A C     
560  O  O     . MET   A 75  ? 0.2752 0.3130 0.2110 0.0099  0.0033  0.0270  72  MET   A O     
561  C  CB    . MET   A 75  ? 0.2874 0.2170 0.1947 0.0008  0.0259  -0.0069 72  MET   A CB    
562  C  CG    . MET   A 75  ? 0.3034 0.2114 0.1500 0.0050  0.0586  -0.0092 72  MET   A CG    
563  S  SD    . MET   A 75  ? 0.3013 0.3032 0.1577 -0.0005 0.0538  -0.0133 72  MET   A SD    
564  C  CE    . MET   A 75  ? 0.2683 0.2514 0.2465 0.0039  0.0602  0.0383  72  MET   A CE    
565  N  N     . ARG   A 76  ? 0.2648 0.3272 0.1663 -0.0047 0.0277  0.0360  73  ARG   A N     
566  C  CA    . ARG   A 76  ? 0.2940 0.3234 0.2305 -0.0032 -0.0043 0.0351  73  ARG   A CA    
567  C  C     . ARG   A 76  ? 0.2530 0.3430 0.2317 -0.0057 0.0009  0.0378  73  ARG   A C     
568  O  O     . ARG   A 76  ? 0.3024 0.2952 0.2752 -0.0005 0.0411  0.0268  73  ARG   A O     
569  C  CB    . ARG   A 76  ? 0.3740 0.3212 0.2461 -0.0083 -0.0208 0.0625  73  ARG   A CB    
570  C  CG    . ARG   A 76  ? 0.4487 0.4072 0.3058 -0.0349 0.0147  -0.0034 73  ARG   A CG    
571  C  CD    . ARG   A 76  ? 0.4605 0.4314 0.3990 -0.0511 0.0147  -0.0089 73  ARG   A CD    
572  N  NE    . ARG   A 76  ? 0.4565 0.3740 0.3875 -0.0378 -0.0348 -0.0637 73  ARG   A NE    
573  C  CZ    . ARG   A 76  ? 0.5295 0.4066 0.4331 -0.0043 0.0311  -0.0203 73  ARG   A CZ    
574  N  NH1   . ARG   A 76  ? 0.5051 0.4251 0.3421 -0.0350 0.0479  -0.0375 73  ARG   A NH1   
575  N  NH2   . ARG   A 76  ? 0.5786 0.5636 0.5113 -0.0572 0.1078  -0.0467 73  ARG   A NH2   
576  N  N     . THR   A 77  ? 0.2840 0.2855 0.2318 0.0321  -0.0112 0.0096  74  THR   A N     
577  C  CA    . THR   A 77  ? 0.2298 0.3147 0.2558 0.0011  0.0407  0.0278  74  THR   A CA    
578  C  C     . THR   A 77  ? 0.2132 0.2767 0.2183 0.0379  0.0419  0.0343  74  THR   A C     
579  O  O     . THR   A 77  ? 0.2325 0.2779 0.2299 0.0316  0.0528  0.0129  74  THR   A O     
580  C  CB    . THR   A 77  ? 0.2970 0.2732 0.2451 0.0028  0.0497  0.0129  74  THR   A CB    
581  O  OG1   . THR   A 77  ? 0.3218 0.3228 0.2776 -0.0387 0.1050  -0.0452 74  THR   A OG1   
582  C  CG2   . THR   A 77  ? 0.3256 0.3083 0.2422 0.0019  0.0607  -0.0011 74  THR   A CG2   
583  N  N     . GLY   A 78  ? 0.2174 0.2463 0.1895 0.0169  0.0766  0.0099  75  GLY   A N     
584  C  CA    . GLY   A 78  ? 0.2499 0.2495 0.1842 0.0194  0.0929  -0.0059 75  GLY   A CA    
585  C  C     . GLY   A 78  ? 0.2389 0.2606 0.2000 0.0152  0.0492  0.0003  75  GLY   A C     
586  O  O     . GLY   A 78  ? 0.2745 0.2611 0.1920 0.0048  0.0352  -0.0045 75  GLY   A O     
587  N  N     . GLU   A 79  ? 0.2207 0.2650 0.1763 0.0004  0.0605  0.0071  76  GLU   A N     
588  C  CA    . GLU   A 79  ? 0.2457 0.3012 0.1442 0.0116  0.0413  0.0127  76  GLU   A CA    
589  C  C     . GLU   A 79  ? 0.2027 0.2906 0.1760 0.0362  0.0289  0.0408  76  GLU   A C     
590  O  O     . GLU   A 79  ? 0.2686 0.3412 0.1645 0.0197  -0.0023 0.0514  76  GLU   A O     
591  C  CB    . GLU   A 79  ? 0.2342 0.3270 0.1772 0.0251  0.0540  0.0211  76  GLU   A CB    
592  C  CG    . GLU   A 79  ? 0.2280 0.3555 0.2340 0.0143  0.0254  0.0065  76  GLU   A CG    
593  C  CD    . GLU   A 79  ? 0.2704 0.4009 0.2851 0.0522  0.0330  -0.0753 76  GLU   A CD    
594  O  OE1   . GLU   A 79  ? 0.2785 0.3987 0.2320 0.0311  0.0419  -0.0366 76  GLU   A OE1   
595  O  OE2   . GLU   A 79  ? 0.3303 0.5764 0.3615 -0.0137 0.0532  -0.0777 76  GLU   A OE2   
596  N  N     . GLY   A 80  ? 0.2304 0.2729 0.1013 -0.0139 0.0471  0.0333  77  GLY   A N     
597  C  CA    . GLY   A 80  ? 0.2289 0.3047 0.0906 -0.0101 0.0647  0.0104  77  GLY   A CA    
598  C  C     . GLY   A 80  ? 0.2811 0.2529 0.1652 0.0032  0.0159  0.0008  77  GLY   A C     
599  O  O     . GLY   A 80  ? 0.2431 0.2343 0.1701 0.0046  0.0608  -0.0036 77  GLY   A O     
600  N  N     . PHE   A 81  ? 0.2792 0.2187 0.1684 0.0118  0.0252  -0.0059 78  PHE   A N     
601  C  CA    . PHE   A 81  ? 0.3091 0.2167 0.0941 0.0192  0.0344  0.0273  78  PHE   A CA    
602  C  C     . PHE   A 81  ? 0.2564 0.2415 0.2093 0.0410  0.0093  0.0204  78  PHE   A C     
603  O  O     . PHE   A 81  ? 0.2590 0.2631 0.1480 -0.0016 0.0327  -0.0096 78  PHE   A O     
604  C  CB    . PHE   A 81  ? 0.2710 0.2588 0.1278 0.0362  0.0583  -0.0015 78  PHE   A CB    
605  C  CG    . PHE   A 81  ? 0.2482 0.2698 0.1029 0.0300  0.0804  -0.0227 78  PHE   A CG    
606  C  CD1   . PHE   A 81  ? 0.2895 0.2723 0.1444 0.0399  0.0433  -0.0315 78  PHE   A CD1   
607  C  CD2   . PHE   A 81  ? 0.2814 0.2505 0.1444 0.0219  0.0390  -0.0139 78  PHE   A CD2   
608  C  CE1   . PHE   A 81  ? 0.2522 0.3156 0.1265 0.0354  0.0235  -0.0389 78  PHE   A CE1   
609  C  CE2   . PHE   A 81  ? 0.2893 0.2750 0.1606 0.0054  0.0503  -0.0515 78  PHE   A CE2   
610  C  CZ    . PHE   A 81  ? 0.2862 0.2946 0.1565 -0.0043 0.0677  -0.0246 78  PHE   A CZ    
611  N  N     . LEU   A 82  ? 0.2152 0.2745 0.1538 0.0306  0.0640  0.0094  79  LEU   A N     
612  C  CA    . LEU   A 82  ? 0.3008 0.2122 0.1218 0.0296  -0.0067 -0.0045 79  LEU   A CA    
613  C  C     . LEU   A 82  ? 0.2878 0.2536 0.1187 0.0241  0.0315  0.0211  79  LEU   A C     
614  O  O     . LEU   A 82  ? 0.2199 0.2446 0.1954 0.0176  0.0860  0.0258  79  LEU   A O     
615  C  CB    . LEU   A 82  ? 0.3619 0.3315 0.1155 0.0168  -0.0249 0.0234  79  LEU   A CB    
616  C  CG    . LEU   A 82  ? 0.3972 0.3591 0.1549 0.0058  -0.0197 0.0047  79  LEU   A CG    
617  C  CD1   . LEU   A 82  ? 0.3207 0.3377 0.1542 0.0150  0.0256  -0.0516 79  LEU   A CD1   
618  C  CD2   . LEU   A 82  ? 0.4040 0.2718 0.1285 -0.0337 0.0362  0.0344  79  LEU   A CD2   
619  N  N     . CYS   A 83  ? 0.2600 0.2930 0.1251 0.0133  0.0354  0.0245  80  CYS   A N     
620  C  CA    . CYS   A 83  ? 0.2964 0.2579 0.1280 0.0255  0.0376  0.0172  80  CYS   A CA    
621  C  C     . CYS   A 83  ? 0.2951 0.2659 0.1114 0.0183  0.0519  -0.0379 80  CYS   A C     
622  O  O     . CYS   A 83  ? 0.2663 0.3001 0.1144 -0.0060 0.0228  -0.0020 80  CYS   A O     
623  C  CB    . CYS   A 83  ? 0.3066 0.2870 0.1278 0.0220  0.0049  0.0237  80  CYS   A CB    
624  S  SG    . CYS   A 83  ? 0.2911 0.3724 0.1640 0.0007  0.0106  -0.0003 80  CYS   A SG    
625  N  N     . VAL   A 84  ? 0.2073 0.2789 0.1639 -0.0059 0.0820  -0.0150 81  VAL   A N     
626  C  CA    . VAL   A 84  ? 0.2284 0.2750 0.1110 -0.0141 0.0826  0.0252  81  VAL   A CA    
627  C  C     . VAL   A 84  ? 0.2252 0.3230 0.1346 0.0216  0.0522  0.0313  81  VAL   A C     
628  O  O     . VAL   A 84  ? 0.2178 0.3396 0.1527 0.0003  0.0700  0.0004  81  VAL   A O     
629  C  CB    . VAL   A 84  ? 0.2159 0.2794 0.1117 0.0027  0.0668  0.0213  81  VAL   A CB    
630  C  CG1   . VAL   A 84  ? 0.2212 0.2899 0.1000 -0.0278 0.0800  0.0347  81  VAL   A CG1   
631  C  CG2   . VAL   A 84  ? 0.2118 0.2349 0.1643 0.0000  0.0570  -0.0169 81  VAL   A CG2   
632  N  N     . PHE   A 85  ? 0.2721 0.3234 0.0867 0.0002  0.0445  -0.0117 82  PHE   A N     
633  C  CA    . PHE   A 85  ? 0.2476 0.3146 0.1382 -0.0103 0.0759  0.0022  82  PHE   A CA    
634  C  C     . PHE   A 85  ? 0.2939 0.3159 0.1533 0.0216  0.0389  -0.0048 82  PHE   A C     
635  O  O     . PHE   A 85  ? 0.2191 0.3305 0.1548 0.0023  0.0288  -0.0310 82  PHE   A O     
636  C  CB    . PHE   A 85  ? 0.2415 0.3120 0.1125 0.0214  0.0571  -0.0090 82  PHE   A CB    
637  C  CG    . PHE   A 85  ? 0.2452 0.3169 0.0835 -0.0065 0.0353  -0.0210 82  PHE   A CG    
638  C  CD1   . PHE   A 85  ? 0.2323 0.3373 0.1198 -0.0082 0.0572  -0.0057 82  PHE   A CD1   
639  C  CD2   . PHE   A 85  ? 0.2369 0.3517 0.1008 0.0083  0.0165  -0.0036 82  PHE   A CD2   
640  C  CE1   . PHE   A 85  ? 0.2351 0.3430 0.0972 0.0101  0.0320  -0.0039 82  PHE   A CE1   
641  C  CE2   . PHE   A 85  ? 0.2549 0.3673 0.1297 -0.0340 0.0496  0.0054  82  PHE   A CE2   
642  C  CZ    . PHE   A 85  ? 0.2850 0.3674 0.0888 -0.0167 0.0291  -0.0051 82  PHE   A CZ    
643  N  N     . ALA   A 86  ? 0.2823 0.3493 0.0934 0.0026  0.0573  0.0042  83  ALA   A N     
644  C  CA    . ALA   A 86  ? 0.2555 0.3885 0.1264 -0.0198 0.0623  0.0033  83  ALA   A CA    
645  C  C     . ALA   A 86  ? 0.2245 0.3750 0.1251 -0.0278 0.0277  0.0035  83  ALA   A C     
646  O  O     . ALA   A 86  ? 0.2668 0.3712 0.1349 -0.0178 0.0353  -0.0074 83  ALA   A O     
647  C  CB    . ALA   A 86  ? 0.2283 0.4368 0.1326 0.0082  0.0580  0.0112  83  ALA   A CB    
648  N  N     . ILE   A 87  ? 0.2514 0.3616 0.1328 -0.0290 0.0605  0.0318  84  ILE   A N     
649  C  CA    . ILE   A 87  ? 0.2834 0.3306 0.1759 -0.0390 0.0320  0.0670  84  ILE   A CA    
650  C  C     . ILE   A 87  ? 0.2594 0.3231 0.1708 -0.0562 0.0355  0.0171  84  ILE   A C     
651  O  O     . ILE   A 87  ? 0.2630 0.3562 0.1634 -0.0514 0.0562  -0.0086 84  ILE   A O     
652  C  CB    . ILE   A 87  ? 0.3081 0.3406 0.1641 -0.0886 0.0509  0.0514  84  ILE   A CB    
653  C  CG1   . ILE   A 87  ? 0.4076 0.3949 0.1067 -0.0854 0.0854  0.0360  84  ILE   A CG1   
654  C  CG2   . ILE   A 87  ? 0.3375 0.4073 0.1269 -0.0602 0.0508  0.0656  84  ILE   A CG2   
655  C  CD1   . ILE   A 87  ? 0.4380 0.4301 0.1685 -0.0826 0.0495  -0.0076 84  ILE   A CD1   
656  N  N     . ASN   A 88  ? 0.2803 0.3717 0.1602 -0.0011 0.0042  0.0071  85  ASN   A N     
657  C  CA    . ASN   A 88  ? 0.2858 0.4175 0.2070 -0.0176 -0.0187 0.0175  85  ASN   A CA    
658  C  C     . ASN   A 88  ? 0.2687 0.4421 0.1601 0.0218  0.0439  0.0174  85  ASN   A C     
659  O  O     . ASN   A 88  ? 0.2453 0.5104 0.1552 0.0111  0.0402  0.0230  85  ASN   A O     
660  C  CB    . ASN   A 88  ? 0.2487 0.4449 0.2104 -0.0059 -0.0252 0.0087  85  ASN   A CB    
661  C  CG    . ASN   A 88  ? 0.2931 0.5013 0.1618 0.0156  0.0308  0.0303  85  ASN   A CG    
662  O  OD1   . ASN   A 88  ? 0.2900 0.5620 0.1861 -0.0018 0.0333  0.0822  85  ASN   A OD1   
663  N  ND2   . ASN   A 88  ? 0.2620 0.4655 0.1647 0.0406  0.0359  0.0081  85  ASN   A ND2   
664  N  N     . ASN   A 89  ? 0.2583 0.4095 0.1314 0.0285  0.0612  0.0089  86  ASN   A N     
665  C  CA    . ASN   A 89  ? 0.2303 0.4084 0.1743 0.0372  0.0746  0.0109  86  ASN   A CA    
666  C  C     . ASN   A 89  ? 0.2383 0.4370 0.1743 0.0329  0.0768  0.0228  86  ASN   A C     
667  O  O     . ASN   A 89  ? 0.2283 0.3964 0.1602 -0.0030 0.0633  -0.0051 86  ASN   A O     
668  C  CB    . ASN   A 89  ? 0.2713 0.4090 0.1678 0.0147  0.0538  0.0274  86  ASN   A CB    
669  C  CG    . ASN   A 89  ? 0.3360 0.3678 0.2201 0.0499  0.0604  0.0470  86  ASN   A CG    
670  O  OD1   . ASN   A 89  ? 0.3220 0.3689 0.2119 0.0406  0.0169  0.0276  86  ASN   A OD1   
671  N  ND2   . ASN   A 89  ? 0.3144 0.4335 0.3185 -0.0347 0.0370  0.0814  86  ASN   A ND2   
672  N  N     . THR   A 90  ? 0.2011 0.4645 0.1759 0.0345  0.0629  0.0268  87  THR   A N     
673  C  CA    . THR   A 90  ? 0.2595 0.3914 0.1620 0.0199  0.0555  0.0164  87  THR   A CA    
674  C  C     . THR   A 90  ? 0.2006 0.3499 0.2127 0.0573  0.0889  0.0065  87  THR   A C     
675  O  O     . THR   A 90  ? 0.2497 0.3893 0.1534 0.0423  0.0659  0.0066  87  THR   A O     
676  C  CB    . THR   A 90  ? 0.2636 0.3762 0.1935 0.0012  0.0725  -0.0037 87  THR   A CB    
677  O  OG1   . THR   A 90  ? 0.3135 0.4510 0.2163 0.0560  0.0369  -0.0191 87  THR   A OG1   
678  C  CG2   . THR   A 90  ? 0.2753 0.4328 0.1498 -0.0333 0.0547  -0.0255 87  THR   A CG2   
679  N  N     . LYS   A 91  ? 0.2339 0.3742 0.1426 0.0557  0.0393  -0.0018 88  LYS   A N     
680  C  CA    . LYS   A 91  ? 0.2480 0.3668 0.2119 0.0356  0.0623  0.0207  88  LYS   A CA    
681  C  C     . LYS   A 91  ? 0.2629 0.3481 0.1548 0.0315  0.0666  0.0064  88  LYS   A C     
682  O  O     . LYS   A 91  ? 0.2694 0.2544 0.1788 0.0374  0.0793  -0.0170 88  LYS   A O     
683  C  CB    . LYS   A 91  ? 0.2660 0.3979 0.2139 0.0554  0.0666  0.0266  88  LYS   A CB    
684  C  CG    . LYS   A 91  ? 0.2889 0.4045 0.3339 0.0446  0.0859  0.0311  88  LYS   A CG    
685  C  CD    . LYS   A 91  ? 0.3018 0.4615 0.3975 0.0946  0.0285  0.0203  88  LYS   A CD    
686  C  CE    . LYS   A 91  ? 0.4714 0.4839 0.4844 0.0261  0.0186  0.0078  88  LYS   A CE    
687  N  NZ    . LYS   A 91  ? 0.4433 0.5323 0.5375 0.0506  -0.0289 -0.0567 88  LYS   A NZ    
688  N  N     . SER   A 92  ? 0.2399 0.3238 0.1401 0.0365  0.0355  0.0173  89  SER   A N     
689  C  CA    . SER   A 92  ? 0.2386 0.3084 0.1548 0.0181  0.0475  0.0054  89  SER   A CA    
690  C  C     . SER   A 92  ? 0.2960 0.2880 0.1297 0.0088  0.0378  -0.0068 89  SER   A C     
691  O  O     . SER   A 92  ? 0.3055 0.3200 0.1198 0.0249  0.0484  0.0049  89  SER   A O     
692  C  CB    . SER   A 92  ? 0.2780 0.3012 0.1305 -0.0013 0.0379  0.0621  89  SER   A CB    
693  O  OG    . SER   A 92  ? 0.2242 0.3103 0.1140 0.0134  0.0756  0.0024  89  SER   A OG    
694  N  N     . PHE   A 93  ? 0.2377 0.2913 0.1514 0.0410  0.0664  -0.0051 90  PHE   A N     
695  C  CA    . PHE   A 93  ? 0.2502 0.2845 0.1484 0.0306  0.0338  -0.0138 90  PHE   A CA    
696  C  C     . PHE   A 93  ? 0.2859 0.2698 0.1436 0.0285  0.0413  -0.0050 90  PHE   A C     
697  O  O     . PHE   A 93  ? 0.2646 0.3115 0.1188 -0.0003 0.0519  0.0228  90  PHE   A O     
698  C  CB    . PHE   A 93  ? 0.2927 0.2963 0.1483 0.0236  0.0487  -0.0028 90  PHE   A CB    
699  C  CG    . PHE   A 93  ? 0.2762 0.3124 0.1145 0.0066  0.0408  -0.0070 90  PHE   A CG    
700  C  CD1   . PHE   A 93  ? 0.2702 0.2736 0.1598 -0.0062 0.0396  -0.0042 90  PHE   A CD1   
701  C  CD2   . PHE   A 93  ? 0.2588 0.2939 0.1522 0.0386  0.0825  -0.0144 90  PHE   A CD2   
702  C  CE1   . PHE   A 93  ? 0.2737 0.3126 0.1996 0.0168  0.0611  0.0264  90  PHE   A CE1   
703  C  CE2   . PHE   A 93  ? 0.2947 0.3623 0.1551 0.0258  0.0354  0.0223  90  PHE   A CE2   
704  C  CZ    . PHE   A 93  ? 0.2853 0.3006 0.1651 0.0034  0.0304  0.0419  90  PHE   A CZ    
705  N  N     . GLU   A 94  ? 0.2641 0.2928 0.1528 0.0335  0.0244  -0.0139 91  GLU   A N     
706  C  CA    . GLU   A 94  ? 0.2665 0.3193 0.1394 0.0276  0.0155  0.0006  91  GLU   A CA    
707  C  C     . GLU   A 94  ? 0.2902 0.3046 0.1369 0.0273  0.0446  -0.0100 91  GLU   A C     
708  O  O     . GLU   A 94  ? 0.2904 0.3186 0.1138 0.0084  0.0724  -0.0235 91  GLU   A O     
709  C  CB    . GLU   A 94  ? 0.2655 0.3328 0.1558 0.0082  0.0455  -0.0354 91  GLU   A CB    
710  C  CG    . GLU   A 94  ? 0.2930 0.3259 0.2370 0.0089  0.0684  -0.0365 91  GLU   A CG    
711  C  CD    . GLU   A 94  ? 0.3747 0.3871 0.3022 0.0111  0.0396  -0.0010 91  GLU   A CD    
712  O  OE1   . GLU   A 94  ? 0.3247 0.4386 0.3352 0.0136  0.0655  0.0146  91  GLU   A OE1   
713  O  OE2   . GLU   A 94  ? 0.5881 0.4746 0.3900 -0.0741 0.1019  -0.0181 91  GLU   A OE2   
714  N  N     . ASP   A 95  ? 0.2867 0.2615 0.1531 0.0290  0.0284  -0.0053 92  ASP   A N     
715  C  CA    . ASP   A 95  ? 0.2624 0.2603 0.1741 0.0385  0.0432  0.0139  92  ASP   A CA    
716  C  C     . ASP   A 95  ? 0.2399 0.3059 0.1602 0.0241  0.0495  0.0575  92  ASP   A C     
717  O  O     . ASP   A 95  ? 0.2510 0.3317 0.1329 0.0158  0.0643  0.0493  92  ASP   A O     
718  C  CB    . ASP   A 95  ? 0.3088 0.3035 0.2159 0.0301  0.0548  0.0642  92  ASP   A CB    
719  C  CG    . ASP   A 95  ? 0.3462 0.2712 0.2303 0.0374  0.0266  0.0115  92  ASP   A CG    
720  O  OD1   . ASP   A 95  ? 0.3410 0.3268 0.2435 0.0592  0.0290  0.0205  92  ASP   A OD1   
721  O  OD2   . ASP   A 95  ? 0.3081 0.3610 0.3147 0.0353  0.0234  0.0798  92  ASP   A OD2   
722  N  N     . ILE   A 96  ? 0.2730 0.3413 0.1051 0.0194  0.0562  0.0305  93  ILE   A N     
723  C  CA    . ILE   A 96  ? 0.2659 0.3346 0.1353 0.0176  0.0329  0.0712  93  ILE   A CA    
724  C  C     . ILE   A 96  ? 0.2445 0.2788 0.1307 0.0120  0.0580  0.0403  93  ILE   A C     
725  O  O     . ILE   A 96  ? 0.2790 0.2492 0.1387 0.0196  0.0620  0.0028  93  ILE   A O     
726  C  CB    . ILE   A 96  ? 0.2775 0.3630 0.1617 0.0152  0.0473  -0.0046 93  ILE   A CB    
727  C  CG1   . ILE   A 96  ? 0.2695 0.3749 0.1648 0.0470  0.0519  0.0065  93  ILE   A CG1   
728  C  CG2   . ILE   A 96  ? 0.3133 0.3691 0.1494 0.0402  0.0386  -0.0485 93  ILE   A CG2   
729  C  CD1   . ILE   A 96  ? 0.2197 0.4619 0.2047 0.0470  0.0525  0.0429  93  ILE   A CD1   
730  N  N     . HIS   A 97  ? 0.2377 0.2844 0.1614 0.0178  0.0830  0.0075  94  HIS   A N     
731  C  CA    . HIS   A 97  ? 0.2585 0.2899 0.1448 0.0195  0.0819  0.0318  94  HIS   A CA    
732  C  C     . HIS   A 97  ? 0.2479 0.2912 0.1349 0.0277  0.0591  0.0182  94  HIS   A C     
733  O  O     . HIS   A 97  ? 0.2447 0.2902 0.1329 -0.0020 0.0885  0.0163  94  HIS   A O     
734  C  CB    . HIS   A 97  ? 0.2549 0.2761 0.1483 0.0072  0.0836  0.0070  94  HIS   A CB    
735  C  CG    . HIS   A 97  ? 0.2645 0.3041 0.1738 0.0222  0.0598  -0.0113 94  HIS   A CG    
736  N  ND1   . HIS   A 97  ? 0.2181 0.3782 0.1444 -0.0075 0.0683  -0.0088 94  HIS   A ND1   
737  C  CD2   . HIS   A 97  ? 0.2812 0.2929 0.1399 0.0136  0.0699  0.0343  94  HIS   A CD2   
738  C  CE1   . HIS   A 97  ? 0.2696 0.3475 0.1507 -0.0060 0.0204  0.0154  94  HIS   A CE1   
739  N  NE2   . HIS   A 97  ? 0.2261 0.3664 0.1688 0.0147  0.0703  -0.0109 94  HIS   A NE2   
740  N  N     . HIS   A 98  ? 0.2493 0.2914 0.1427 0.0471  0.0708  0.0165  95  HIS   A N     
741  C  CA    . HIS   A 98  ? 0.2535 0.3358 0.1601 0.0098  0.0476  0.0215  95  HIS   A CA    
742  C  C     . HIS   A 98  ? 0.2239 0.2895 0.2171 0.0193  0.0391  0.0231  95  HIS   A C     
743  O  O     . HIS   A 98  ? 0.2328 0.3050 0.1720 0.0110  0.0478  0.0040  95  HIS   A O     
744  C  CB    . HIS   A 98  ? 0.2784 0.3118 0.2049 0.0025  0.0878  0.0549  95  HIS   A CB    
745  C  CG    . HIS   A 98  ? 0.2691 0.3372 0.2885 0.0200  0.1074  -0.0235 95  HIS   A CG    
746  N  ND1   . HIS   A 98  ? 0.3712 0.3433 0.3833 -0.0242 0.1755  -0.0429 95  HIS   A ND1   
747  C  CD2   . HIS   A 98  ? 0.3138 0.3641 0.1982 -0.0007 0.1040  -0.0189 95  HIS   A CD2   
748  C  CE1   . HIS   A 98  ? 0.3423 0.3585 0.3059 0.0029  0.1545  -0.0476 95  HIS   A CE1   
749  N  NE2   . HIS   A 98  ? 0.3301 0.2893 0.2808 0.0367  0.1440  0.0178  95  HIS   A NE2   
750  N  N     . TYR   A 99  ? 0.2414 0.3102 0.1992 -0.0134 0.0599  0.0409  96  TYR   A N     
751  C  CA    . TYR   A 99  ? 0.2726 0.2645 0.1714 -0.0260 0.0663  0.0419  96  TYR   A CA    
752  C  C     . TYR   A 99  ? 0.2545 0.3018 0.1651 -0.0303 0.0396  -0.0258 96  TYR   A C     
753  O  O     . TYR   A 99  ? 0.2445 0.3322 0.1379 -0.0368 0.0256  -0.0013 96  TYR   A O     
754  C  CB    . TYR   A 99  ? 0.2721 0.3238 0.1716 -0.0236 0.0760  0.0268  96  TYR   A CB    
755  C  CG    . TYR   A 99  ? 0.3111 0.3186 0.2132 -0.0171 0.0484  0.0346  96  TYR   A CG    
756  C  CD1   . TYR   A 99  ? 0.3355 0.3016 0.1451 -0.0390 0.0546  0.0380  96  TYR   A CD1   
757  C  CD2   . TYR   A 99  ? 0.3394 0.3239 0.1196 -0.0122 0.0793  -0.0010 96  TYR   A CD2   
758  C  CE1   . TYR   A 99  ? 0.3436 0.3135 0.2026 -0.0162 0.0771  0.0607  96  TYR   A CE1   
759  C  CE2   . TYR   A 99  ? 0.3281 0.3213 0.1439 0.0092  0.0971  0.0505  96  TYR   A CE2   
760  C  CZ    . TYR   A 99  ? 0.3697 0.3272 0.1214 0.0164  0.0394  0.0791  96  TYR   A CZ    
761  O  OH    . TYR   A 99  ? 0.3628 0.4408 0.1917 0.0019  0.0280  0.0775  96  TYR   A OH    
762  N  N     . ARG   A 100 ? 0.2183 0.3177 0.1540 -0.0050 0.0767  0.0124  97  ARG   A N     
763  C  CA    . ARG   A 100 ? 0.2208 0.3155 0.1902 0.0089  0.0509  -0.0118 97  ARG   A CA    
764  C  C     . ARG   A 100 ? 0.2337 0.2976 0.1808 0.0146  0.0310  -0.0007 97  ARG   A C     
765  O  O     . ARG   A 100 ? 0.2502 0.3102 0.1539 0.0101  0.0255  -0.0047 97  ARG   A O     
766  C  CB    . ARG   A 100 ? 0.2641 0.3208 0.2252 -0.0043 0.0320  0.0017  97  ARG   A CB    
767  C  CG    . ARG   A 100 ? 0.2730 0.3532 0.2684 -0.0297 0.0155  0.0248  97  ARG   A CG    
768  C  CD    . ARG   A 100 ? 0.2842 0.3507 0.3818 -0.0542 -0.0325 0.0263  97  ARG   A CD    
769  N  NE    . ARG   A 100 ? 0.3306 0.3645 0.4420 -0.0078 -0.0545 0.0239  97  ARG   A NE    
770  C  CZ    . ARG   A 100 ? 0.4103 0.4738 0.4708 0.0484  -0.0201 0.0234  97  ARG   A CZ    
771  N  NH1   . ARG   A 100 ? 0.4667 0.4082 0.3947 0.0046  0.0301  -0.0007 97  ARG   A NH1   
772  N  NH2   . ARG   A 100 ? 0.5567 0.5448 0.5862 0.0823  -0.0433 0.1064  97  ARG   A NH2   
773  N  N     . GLU   A 101 ? 0.2654 0.2976 0.1472 0.0003  0.0645  0.0239  98  GLU   A N     
774  C  CA    . GLU   A 101 ? 0.2648 0.3301 0.1995 -0.0125 0.0699  -0.0258 98  GLU   A CA    
775  C  C     . GLU   A 101 ? 0.2557 0.3113 0.2302 0.0010  0.0354  -0.0038 98  GLU   A C     
776  O  O     . GLU   A 101 ? 0.2988 0.3250 0.1991 0.0034  0.0369  -0.0404 98  GLU   A O     
777  C  CB    . GLU   A 101 ? 0.2826 0.3507 0.1859 -0.0031 0.0938  0.0212  98  GLU   A CB    
778  C  CG    . GLU   A 101 ? 0.2952 0.4170 0.2786 -0.0267 0.1279  -0.0579 98  GLU   A CG    
779  C  CD    . GLU   A 101 ? 0.3435 0.4208 0.2882 -0.0726 0.1802  -0.0911 98  GLU   A CD    
780  O  OE1   . GLU   A 101 ? 0.3360 0.4148 0.3249 -0.0891 0.0851  -0.0379 98  GLU   A OE1   
781  O  OE2   . GLU   A 101 ? 0.4217 0.4168 0.3914 -0.0324 0.0661  -0.0960 98  GLU   A OE2   
782  N  N     . GLN   A 102 ? 0.2585 0.3170 0.1813 0.0233  0.0670  -0.0145 99  GLN   A N     
783  C  CA    . GLN   A 102 ? 0.2772 0.3190 0.2250 0.0007  0.0466  -0.0475 99  GLN   A CA    
784  C  C     . GLN   A 102 ? 0.2560 0.3107 0.1779 0.0173  0.0205  -0.0080 99  GLN   A C     
785  O  O     . GLN   A 102 ? 0.2833 0.3505 0.1627 0.0106  0.0191  0.0126  99  GLN   A O     
786  C  CB    . GLN   A 102 ? 0.3067 0.3344 0.2214 0.0086  0.0451  -0.0488 99  GLN   A CB    
787  C  CG    . GLN   A 102 ? 0.3766 0.3435 0.2464 -0.0014 -0.0058 0.0000  99  GLN   A CG    
788  C  CD    . GLN   A 102 ? 0.4597 0.3366 0.2605 -0.0224 0.0580  -0.0299 99  GLN   A CD    
789  O  OE1   . GLN   A 102 ? 0.4911 0.4136 0.2302 -0.0131 0.0446  0.0060  99  GLN   A OE1   
790  N  NE2   . GLN   A 102 ? 0.4254 0.3768 0.3942 -0.0268 0.0240  0.0115  99  GLN   A NE2   
791  N  N     . ILE   A 103 ? 0.2484 0.3163 0.1261 0.0120  0.0653  0.0179  100 ILE   A N     
792  C  CA    . ILE   A 103 ? 0.2616 0.2858 0.1528 0.0029  0.0794  -0.0062 100 ILE   A CA    
793  C  C     . ILE   A 103 ? 0.2974 0.2941 0.1933 0.0260  0.0454  -0.0355 100 ILE   A C     
794  O  O     . ILE   A 103 ? 0.3038 0.3161 0.1926 0.0150  0.0089  -0.0251 100 ILE   A O     
795  C  CB    . ILE   A 103 ? 0.2406 0.2991 0.1837 -0.0003 0.0825  -0.0186 100 ILE   A CB    
796  C  CG1   . ILE   A 103 ? 0.2321 0.3082 0.1731 0.0186  0.1000  0.0066  100 ILE   A CG1   
797  C  CG2   . ILE   A 103 ? 0.2521 0.3546 0.1744 0.0366  0.0580  -0.0244 100 ILE   A CG2   
798  C  CD1   . ILE   A 103 ? 0.2929 0.3042 0.1423 0.0019  0.1021  0.0111  100 ILE   A CD1   
799  N  N     . LYS   A 104 ? 0.2270 0.3336 0.2082 0.0019  0.0611  -0.0089 101 LYS   A N     
800  C  CA    . LYS   A 104 ? 0.2705 0.2967 0.2322 0.0336  0.0509  -0.0004 101 LYS   A CA    
801  C  C     . LYS   A 104 ? 0.2657 0.3275 0.1914 -0.0169 0.0409  0.0417  101 LYS   A C     
802  O  O     . LYS   A 104 ? 0.3016 0.3171 0.2641 0.0056  -0.0108 -0.0102 101 LYS   A O     
803  C  CB    . LYS   A 104 ? 0.2972 0.3287 0.1958 -0.0001 0.0189  0.0048  101 LYS   A CB    
804  C  CG    . LYS   A 104 ? 0.3067 0.2858 0.2980 0.0269  -0.0460 0.0267  101 LYS   A CG    
805  C  CD    . LYS   A 104 ? 0.4006 0.3816 0.4102 -0.0159 0.0231  0.0637  101 LYS   A CD    
806  C  CE    . LYS   A 104 ? 0.4401 0.4432 0.4355 -0.0313 0.0675  0.0543  101 LYS   A CE    
807  N  NZ    . LYS   A 104 ? 0.5978 0.3911 0.4313 -0.0821 0.0237  0.0109  101 LYS   A NZ    
808  N  N     . ARG   A 105 ? 0.3122 0.3455 0.1856 0.0036  0.0332  0.0184  102 ARG   A N     
809  C  CA    . ARG   A 105 ? 0.3119 0.3748 0.2369 -0.0309 -0.0011 0.0143  102 ARG   A CA    
810  C  C     . ARG   A 105 ? 0.3278 0.3215 0.1839 -0.0304 -0.0096 -0.0087 102 ARG   A C     
811  O  O     . ARG   A 105 ? 0.3349 0.3824 0.2146 -0.0293 0.0029  -0.0449 102 ARG   A O     
812  C  CB    . ARG   A 105 ? 0.3371 0.3826 0.2734 -0.0092 -0.0120 0.0233  102 ARG   A CB    
813  C  CG    . ARG   A 105 ? 0.4051 0.4164 0.4130 -0.0456 0.0120  0.0027  102 ARG   A CG    
814  C  CD    . ARG   A 105 ? 0.4180 0.5299 0.4968 -0.0185 0.0648  0.0156  102 ARG   A CD    
815  N  NE    . ARG   A 105 ? 0.4754 0.5181 0.4997 -0.0291 0.0415  0.0523  102 ARG   A NE    
816  C  CZ    . ARG   A 105 ? 0.4800 0.4981 0.4176 -0.0186 0.0152  -0.0176 102 ARG   A CZ    
817  N  NH1   . ARG   A 105 ? 0.4553 0.5635 0.3069 -0.0342 -0.0119 -0.0550 102 ARG   A NH1   
818  N  NH2   . ARG   A 105 ? 0.5246 0.6119 0.3293 0.0927  0.1230  0.0204  102 ARG   A NH2   
819  N  N     . VAL   A 106 ? 0.3076 0.3386 0.1843 -0.0148 -0.0134 -0.0241 103 VAL   A N     
820  C  CA    . VAL   A 106 ? 0.3494 0.3551 0.2465 -0.0543 -0.0257 0.0302  103 VAL   A CA    
821  C  C     . VAL   A 106 ? 0.3162 0.3744 0.2054 -0.0527 -0.0148 -0.0104 103 VAL   A C     
822  O  O     . VAL   A 106 ? 0.3005 0.4214 0.2813 -0.0505 0.0132  -0.0159 103 VAL   A O     
823  C  CB    . VAL   A 106 ? 0.3469 0.3359 0.2247 -0.0672 -0.0244 -0.0035 103 VAL   A CB    
824  C  CG1   . VAL   A 106 ? 0.3655 0.3598 0.2410 -0.0671 0.0036  -0.0311 103 VAL   A CG1   
825  C  CG2   . VAL   A 106 ? 0.3289 0.3559 0.1834 -0.0476 -0.0033 0.0154  103 VAL   A CG2   
826  N  N     . LYS   A 107 ? 0.3200 0.3761 0.1696 -0.0180 0.0427  -0.0221 104 LYS   A N     
827  C  CA    . LYS   A 107 ? 0.3300 0.4493 0.3062 0.0079  -0.0022 -0.0405 104 LYS   A CA    
828  C  C     . LYS   A 107 ? 0.3353 0.4202 0.2973 0.0500  0.0201  -0.0168 104 LYS   A C     
829  O  O     . LYS   A 107 ? 0.3574 0.5074 0.2765 0.0617  -0.0115 -0.0400 104 LYS   A O     
830  C  CB    . LYS   A 107 ? 0.3004 0.4388 0.2019 -0.0198 0.0399  0.0025  104 LYS   A CB    
831  C  CG    . LYS   A 107 ? 0.3305 0.4024 0.2067 -0.0232 0.0167  0.0062  104 LYS   A CG    
832  C  CD    . LYS   A 107 ? 0.3317 0.3550 0.2533 -0.0262 -0.0173 0.0354  104 LYS   A CD    
833  C  CE    . LYS   A 107 ? 0.3304 0.3327 0.2423 -0.0245 -0.0122 0.0253  104 LYS   A CE    
834  N  NZ    . LYS   A 107 ? 0.3311 0.3562 0.2137 -0.0046 0.0109  0.0229  104 LYS   A NZ    
835  N  N     . ASP   A 108 ? 0.3183 0.4921 0.2491 -0.0025 0.0184  0.0097  105 ASP   A N     
836  C  CA    . ASP   A 108 ? 0.3866 0.4508 0.2776 0.0200  -0.0343 -0.0082 105 ASP   A CA    
837  C  C     . ASP   A 108 ? 0.3436 0.4524 0.3695 0.0371  -0.0556 -0.0272 105 ASP   A C     
838  O  O     . ASP   A 108 ? 0.3395 0.5350 0.4690 0.0599  -0.0875 -0.0537 105 ASP   A O     
839  C  CB    . ASP   A 108 ? 0.4376 0.4631 0.2935 -0.0180 -0.0279 0.0274  105 ASP   A CB    
840  C  CG    . ASP   A 108 ? 0.4196 0.5712 0.3194 -0.0245 -0.0405 -0.0021 105 ASP   A CG    
841  O  OD1   . ASP   A 108 ? 0.4997 0.5210 0.2992 -0.0294 0.0128  -0.0385 105 ASP   A OD1   
842  O  OD2   . ASP   A 108 ? 0.4578 0.6798 0.4029 -0.0559 -0.0885 -0.0004 105 ASP   A OD2   
843  N  N     . SER   A 109 ? 0.3686 0.4128 0.2983 0.0512  -0.0523 -0.0436 106 SER   A N     
844  C  CA    . SER   A 109 ? 0.3717 0.4193 0.3424 0.0603  -0.0230 -0.0592 106 SER   A CA    
845  C  C     . SER   A 109 ? 0.3861 0.3753 0.3669 0.0812  0.0015  0.0120  106 SER   A C     
846  O  O     . SER   A 109 ? 0.3771 0.3954 0.4651 0.0799  -0.0085 0.0391  106 SER   A O     
847  C  CB    . SER   A 109 ? 0.4220 0.4202 0.3615 0.0247  0.0360  -0.0472 106 SER   A CB    
848  O  OG    . SER   A 109 ? 0.4765 0.4338 0.5341 0.0284  0.0613  -0.0403 106 SER   A OG    
849  N  N     . GLU   A 110 ? 0.4451 0.4216 0.3770 0.0701  -0.0370 0.0451  107 GLU   A N     
850  C  CA    . GLU   A 110 ? 0.4816 0.4567 0.4061 0.0324  -0.0308 0.0391  107 GLU   A CA    
851  C  C     . GLU   A 110 ? 0.4015 0.4670 0.4454 0.0511  -0.0024 0.0124  107 GLU   A C     
852  O  O     . GLU   A 110 ? 0.4574 0.5197 0.3993 -0.0110 0.0044  0.0745  107 GLU   A O     
853  C  CB    . GLU   A 110 ? 0.5366 0.5492 0.4109 0.0845  -0.0238 0.0543  107 GLU   A CB    
854  C  CG    . GLU   A 110 ? 0.3419 0.3419 0.3419 0.0000  0.0000  0.0000  107 GLU   A CG    
855  C  CD    . GLU   A 110 ? 0.3419 0.3419 0.3419 0.0000  0.0000  0.0000  107 GLU   A CD    
856  O  OE1   . GLU   A 110 ? 0.3419 0.3419 0.3419 0.0000  0.0000  0.0000  107 GLU   A OE1   
857  O  OE2   . GLU   A 110 ? 0.3419 0.3419 0.3419 0.0000  0.0000  0.0000  107 GLU   A OE2   
858  N  N     . ASP   A 111 ? 0.4609 0.3926 0.3152 0.0366  -0.0011 0.0100  108 ASP   A N     
859  C  CA    . ASP   A 111 ? 0.5070 0.4522 0.2131 0.0075  -0.0416 0.0186  108 ASP   A CA    
860  C  C     . ASP   A 111 ? 0.3502 0.4661 0.2431 0.0378  0.0351  0.0132  108 ASP   A C     
861  O  O     . ASP   A 111 ? 0.3589 0.5056 0.4835 -0.0199 -0.0290 0.0569  108 ASP   A O     
862  C  CB    . ASP   A 111 ? 0.6205 0.5272 0.2321 0.0822  -0.0077 0.0336  108 ASP   A CB    
863  C  CG    . ASP   A 111 ? 0.7281 0.5728 0.4221 -0.0482 -0.0100 0.0960  108 ASP   A CG    
864  O  OD1   . ASP   A 111 ? 0.7371 0.7269 0.4901 -0.0527 -0.0464 -0.0532 108 ASP   A OD1   
865  O  OD2   . ASP   A 111 ? 0.8168 0.7875 0.3756 0.0402  0.0371  -0.0012 108 ASP   A OD2   
866  N  N     . VAL   A 112 ? 0.3799 0.3797 0.1446 0.0184  0.0383  0.0204  109 VAL   A N     
867  C  CA    . VAL   A 112 ? 0.2964 0.3434 0.1279 0.0031  0.0962  -0.0004 109 VAL   A CA    
868  C  C     . VAL   A 112 ? 0.2322 0.3475 0.2133 0.0276  0.0475  -0.0039 109 VAL   A C     
869  O  O     . VAL   A 112 ? 0.2573 0.2927 0.1758 -0.0051 0.0425  -0.0042 109 VAL   A O     
870  C  CB    . VAL   A 112 ? 0.3152 0.3463 0.1581 0.0054  0.0383  0.0081  109 VAL   A CB    
871  C  CG1   . VAL   A 112 ? 0.3347 0.3016 0.1735 0.0122  0.0256  0.0292  109 VAL   A CG1   
872  C  CG2   . VAL   A 112 ? 0.3265 0.3355 0.2078 0.0298  0.0795  -0.0497 109 VAL   A CG2   
873  N  N     . PRO   A 113 ? 0.2327 0.2844 0.1802 0.0238  0.0533  0.0248  110 PRO   A N     
874  C  CA    . PRO   A 113 ? 0.2307 0.2647 0.1705 -0.0154 0.0708  0.0530  110 PRO   A CA    
875  C  C     . PRO   A 113 ? 0.2616 0.2751 0.1501 0.0117  0.0513  -0.0355 110 PRO   A C     
876  O  O     . PRO   A 113 ? 0.2867 0.2789 0.1344 0.0118  0.0610  -0.0108 110 PRO   A O     
877  C  CB    . PRO   A 113 ? 0.2317 0.2552 0.1700 0.0365  0.0562  0.0140  110 PRO   A CB    
878  C  CG    . PRO   A 113 ? 0.2135 0.2358 0.2492 0.0370  0.0374  0.0426  110 PRO   A CG    
879  C  CD    . PRO   A 113 ? 0.2126 0.2599 0.2225 0.0371  0.0132  0.0303  110 PRO   A CD    
880  N  N     . MET   A 114 ? 0.2846 0.2083 0.1442 0.0195  0.0328  0.0329  111 MET   A N     
881  C  CA    . MET   A 114 ? 0.2470 0.3058 0.1296 0.0073  0.0780  0.0148  111 MET   A CA    
882  C  C     . MET   A 114 ? 0.2275 0.3116 0.1183 0.0351  0.0858  -0.0221 111 MET   A C     
883  O  O     . MET   A 114 ? 0.2505 0.2924 0.1526 0.0051  0.0596  -0.0122 111 MET   A O     
884  C  CB    . MET   A 114 ? 0.3307 0.3198 0.1543 -0.0130 0.1167  -0.0092 111 MET   A CB    
885  C  CG    . MET   A 114 ? 0.3339 0.3254 0.1505 0.0057  0.1121  0.0096  111 MET   A CG    
886  S  SD    . MET   A 114 ? 0.3936 0.4245 0.1903 0.0838  0.0821  -0.0524 111 MET   A SD    
887  C  CE    . MET   A 114 ? 0.4250 0.4728 0.1557 0.0586  0.0476  -0.0481 111 MET   A CE    
888  N  N     . VAL   A 115 ? 0.2503 0.2779 0.1471 0.0222  0.0592  0.0049  112 VAL   A N     
889  C  CA    . VAL   A 115 ? 0.3130 0.2626 0.0889 0.0000  0.0426  0.0200  112 VAL   A CA    
890  C  C     . VAL   A 115 ? 0.2817 0.2454 0.1684 -0.0165 0.0050  0.0090  112 VAL   A C     
891  O  O     . VAL   A 115 ? 0.2514 0.2528 0.1508 0.0159  0.0661  0.0044  112 VAL   A O     
892  C  CB    . VAL   A 115 ? 0.3232 0.2479 0.1102 0.0003  0.0572  0.0022  112 VAL   A CB    
893  C  CG1   . VAL   A 115 ? 0.3233 0.2788 0.1393 0.0066  0.0444  -0.0269 112 VAL   A CG1   
894  C  CG2   . VAL   A 115 ? 0.3289 0.2867 0.1688 0.0036  0.0541  -0.0036 112 VAL   A CG2   
895  N  N     . LEU   A 116 ? 0.2897 0.2286 0.1161 0.0039  0.0225  0.0063  113 LEU   A N     
896  C  CA    . LEU   A 116 ? 0.2445 0.2491 0.1673 -0.0483 0.0371  0.0382  113 LEU   A CA    
897  C  C     . LEU   A 116 ? 0.2290 0.2797 0.1651 -0.0049 0.0458  0.0125  113 LEU   A C     
898  O  O     . LEU   A 116 ? 0.2728 0.3145 0.1168 -0.0359 0.0553  -0.0086 113 LEU   A O     
899  C  CB    . LEU   A 116 ? 0.2798 0.2879 0.1008 -0.0213 0.0150  0.0193  113 LEU   A CB    
900  C  CG    . LEU   A 116 ? 0.2546 0.2924 0.1230 -0.0435 0.0214  0.0393  113 LEU   A CG    
901  C  CD1   . LEU   A 116 ? 0.2420 0.2939 0.1682 -0.0324 0.0639  0.0738  113 LEU   A CD1   
902  C  CD2   . LEU   A 116 ? 0.2651 0.3089 0.1457 -0.0407 0.0482  0.0498  113 LEU   A CD2   
903  N  N     . VAL   A 117 ? 0.2199 0.2566 0.1317 -0.0227 0.0531  -0.0098 114 VAL   A N     
904  C  CA    . VAL   A 117 ? 0.2210 0.2683 0.1469 -0.0565 0.0475  0.0103  114 VAL   A CA    
905  C  C     . VAL   A 117 ? 0.2418 0.3113 0.0812 -0.0074 0.0526  0.0278  114 VAL   A C     
906  O  O     . VAL   A 117 ? 0.2317 0.3302 0.1236 0.0049  0.0574  0.0219  114 VAL   A O     
907  C  CB    . VAL   A 117 ? 0.2629 0.2895 0.1447 -0.0295 0.0723  0.0094  114 VAL   A CB    
908  C  CG1   . VAL   A 117 ? 0.2700 0.3278 0.1371 0.0008  0.0621  -0.0012 114 VAL   A CG1   
909  C  CG2   . VAL   A 117 ? 0.2677 0.2656 0.1232 -0.0286 0.0532  -0.0285 114 VAL   A CG2   
910  N  N     . GLY   A 118 ? 0.2848 0.3169 0.1174 -0.0153 0.0331  0.0295  115 GLY   A N     
911  C  CA    . GLY   A 118 ? 0.2418 0.3059 0.1067 -0.0662 0.0559  -0.0067 115 GLY   A CA    
912  C  C     . GLY   A 118 ? 0.2776 0.3351 0.1081 -0.0492 0.0342  0.0179  115 GLY   A C     
913  O  O     . GLY   A 118 ? 0.2902 0.3932 0.1116 -0.0664 0.0490  -0.0147 115 GLY   A O     
914  N  N     . ASN   A 119 ? 0.2352 0.3006 0.1272 -0.0166 0.0243  -0.0218 116 ASN   A N     
915  C  CA    . ASN   A 119 ? 0.2777 0.3402 0.1207 -0.0481 0.0200  -0.0268 116 ASN   A CA    
916  C  C     . ASN   A 119 ? 0.2757 0.3525 0.1142 -0.0431 0.0302  -0.0317 116 ASN   A C     
917  O  O     . ASN   A 119 ? 0.2440 0.3999 0.1318 -0.0486 0.0549  0.0093  116 ASN   A O     
918  C  CB    . ASN   A 119 ? 0.2765 0.3210 0.0943 -0.0436 0.0577  -0.0550 116 ASN   A CB    
919  C  CG    . ASN   A 119 ? 0.2410 0.3519 0.0972 -0.0439 0.0535  -0.0336 116 ASN   A CG    
920  O  OD1   . ASN   A 119 ? 0.2537 0.3362 0.1223 -0.0668 0.0715  -0.0170 116 ASN   A OD1   
921  N  ND2   . ASN   A 119 ? 0.2130 0.3675 0.1340 -0.0238 0.0640  -0.0226 116 ASN   A ND2   
922  N  N     . LYS   A 120 ? 0.2918 0.3760 0.1083 -0.0499 0.0319  -0.0258 117 LYS   A N     
923  C  CA    . LYS   A 120 ? 0.2962 0.4147 0.1024 -0.0388 0.0156  -0.0201 117 LYS   A CA    
924  C  C     . LYS   A 120 ? 0.3003 0.4424 0.1472 -0.0326 0.0283  -0.0064 117 LYS   A C     
925  O  O     . LYS   A 120 ? 0.2880 0.4228 0.1697 -0.0607 0.0269  -0.0364 117 LYS   A O     
926  C  CB    . LYS   A 120 ? 0.2915 0.4296 0.1079 -0.0474 0.0436  -0.0164 117 LYS   A CB    
927  C  CG    . LYS   A 120 ? 0.3062 0.4215 0.1200 -0.0524 0.0167  -0.0377 117 LYS   A CG    
928  C  CD    . LYS   A 120 ? 0.2995 0.4386 0.1102 -0.0416 0.0348  -0.0519 117 LYS   A CD    
929  C  CE    . LYS   A 120 ? 0.3199 0.4167 0.1675 -0.0242 0.0362  -0.0225 117 LYS   A CE    
930  N  NZ    . LYS   A 120 ? 0.2729 0.5045 0.2640 0.0033  0.0718  -0.0108 117 LYS   A NZ    
931  N  N     . SER   A 121 ? 0.2995 0.4240 0.1206 -0.0463 0.0259  0.0348  118 SER   A N     
932  C  CA    . SER   A 121 ? 0.3065 0.4444 0.1867 -0.0825 0.0761  -0.0083 118 SER   A CA    
933  C  C     . SER   A 121 ? 0.3359 0.4355 0.2345 -0.0914 0.0138  0.0457  118 SER   A C     
934  O  O     . SER   A 121 ? 0.4234 0.4251 0.1931 -0.1302 0.0075  -0.0010 118 SER   A O     
935  C  CB    . SER   A 121 ? 0.3357 0.4548 0.1830 -0.0669 0.0480  -0.0148 118 SER   A CB    
936  O  OG    . SER   A 121 ? 0.3397 0.4685 0.2166 -0.0712 0.0725  -0.0137 118 SER   A OG    
937  N  N     . ASP   A 122 ? 0.2899 0.4305 0.1759 -0.0790 0.0305  -0.0049 119 ASP   A N     
938  C  CA    . ASP   A 122 ? 0.2951 0.4485 0.2072 -0.0851 0.0176  0.0261  119 ASP   A CA    
939  C  C     . ASP   A 122 ? 0.2886 0.4173 0.2157 -0.1220 0.0417  0.0362  119 ASP   A C     
940  O  O     . ASP   A 122 ? 0.2825 0.5516 0.2607 -0.1097 0.0343  -0.0238 119 ASP   A O     
941  C  CB    . ASP   A 122 ? 0.2888 0.4878 0.1956 -0.1007 0.0308  0.0009  119 ASP   A CB    
942  C  CG    . ASP   A 122 ? 0.2477 0.4648 0.1382 -0.0355 0.0718  0.0243  119 ASP   A CG    
943  O  OD1   . ASP   A 122 ? 0.3192 0.4762 0.1613 -0.0908 0.0348  0.0121  119 ASP   A OD1   
944  O  OD2   . ASP   A 122 ? 0.3206 0.3882 0.2308 -0.0419 -0.0091 -0.0173 119 ASP   A OD2   
945  N  N     . LEU   A 123 ? 0.3250 0.4254 0.1820 -0.0435 -0.0149 0.0248  120 LEU   A N     
946  C  CA    . LEU   A 123 ? 0.2945 0.3997 0.2007 -0.0520 -0.0203 0.0623  120 LEU   A CA    
947  C  C     . LEU   A 123 ? 0.2849 0.4409 0.2601 -0.0790 0.0067  0.0431  120 LEU   A C     
948  O  O     . LEU   A 123 ? 0.2726 0.4544 0.3073 -0.0096 -0.0038 0.0533  120 LEU   A O     
949  C  CB    . LEU   A 123 ? 0.3206 0.4164 0.2397 -0.0350 0.0476  0.0224  120 LEU   A CB    
950  C  CG    . LEU   A 123 ? 0.3029 0.3964 0.2440 -0.0642 0.0416  0.0143  120 LEU   A CG    
951  C  CD1   . LEU   A 123 ? 0.3293 0.3945 0.2105 -0.0510 -0.0008 0.0099  120 LEU   A CD1   
952  C  CD2   . LEU   A 123 ? 0.3171 0.3935 0.2074 -0.0499 0.0627  0.0541  120 LEU   A CD2   
953  N  N     . PRO   A 124 ? 0.2804 0.3761 0.1901 -0.0732 0.0234  0.0189  121 PRO   A N     
954  C  CA    . PRO   A 124 ? 0.2727 0.3658 0.2894 -0.0593 0.0677  0.0349  121 PRO   A CA    
955  C  C     . PRO   A 124 ? 0.3203 0.3710 0.2514 -0.0413 0.0543  0.0521  121 PRO   A C     
956  O  O     . PRO   A 124 ? 0.4127 0.3797 0.2658 -0.0928 0.0527  0.0573  121 PRO   A O     
957  C  CB    . PRO   A 124 ? 0.3006 0.3441 0.3229 -0.0570 0.0393  0.0159  121 PRO   A CB    
958  C  CG    . PRO   A 124 ? 0.2989 0.4497 0.2463 -0.0382 0.0003  -0.0010 121 PRO   A CG    
959  C  CD    . PRO   A 124 ? 0.3062 0.4027 0.2099 -0.0456 0.0001  -0.0081 121 PRO   A CD    
960  N  N     . SER   A 125 ? 0.3012 0.3813 0.1811 -0.0642 0.0586  0.0197  122 SER   A N     
961  C  CA    . SER   A 125 ? 0.2550 0.3875 0.2410 -0.0532 0.0639  -0.0089 122 SER   A CA    
962  C  C     . SER   A 125 ? 0.2470 0.4197 0.2163 -0.0715 0.0777  0.0135  122 SER   A C     
963  O  O     . SER   A 125 ? 0.2893 0.4360 0.2391 -0.0506 0.0272  -0.0112 122 SER   A O     
964  C  CB    . SER   A 125 ? 0.3451 0.4075 0.2257 -0.0686 0.0583  0.0110  122 SER   A CB    
965  O  OG    . SER   A 125 ? 0.3905 0.4020 0.2137 -0.0353 0.1006  -0.0126 122 SER   A OG    
966  N  N     . ARG   A 126 ? 0.2350 0.4326 0.2122 -0.0922 0.0311  0.0513  123 ARG   A N     
967  C  CA    . ARG   A 126 ? 0.2481 0.4394 0.1760 -0.0570 0.0416  -0.0078 123 ARG   A CA    
968  C  C     . ARG   A 126 ? 0.3037 0.4800 0.1670 -0.0911 0.0751  -0.0028 123 ARG   A C     
969  O  O     . ARG   A 126 ? 0.2651 0.5000 0.2384 -0.0932 0.0409  0.0140  123 ARG   A O     
970  C  CB    . ARG   A 126 ? 0.2493 0.4143 0.2450 -0.0567 0.0194  -0.0011 123 ARG   A CB    
971  C  CG    . ARG   A 126 ? 0.2878 0.4760 0.1857 -0.0663 0.0440  0.0096  123 ARG   A CG    
972  C  CD    . ARG   A 126 ? 0.2602 0.4732 0.1917 -0.0565 0.0627  -0.0166 123 ARG   A CD    
973  N  NE    . ARG   A 126 ? 0.3311 0.5504 0.2498 -0.0341 0.0327  -0.1395 123 ARG   A NE    
974  C  CZ    . ARG   A 126 ? 0.3249 0.5195 0.2629 -0.0282 0.0568  -0.0661 123 ARG   A CZ    
975  N  NH1   . ARG   A 126 ? 0.3284 0.4930 0.2127 -0.0994 0.0670  0.0137  123 ARG   A NH1   
976  N  NH2   . ARG   A 126 ? 0.3834 0.5293 0.3178 0.0031  0.0351  -0.1310 123 ARG   A NH2   
977  N  N     . THR   A 127 ? 0.2811 0.4170 0.1303 -0.0428 0.0973  0.0281  124 THR   A N     
978  C  CA    . THR   A 127 ? 0.2361 0.4066 0.1551 -0.0380 0.1119  0.0040  124 THR   A CA    
979  C  C     . THR   A 127 ? 0.2501 0.4968 0.1893 -0.0324 0.0720  -0.0276 124 THR   A C     
980  O  O     . THR   A 127 ? 0.3075 0.5598 0.1820 -0.0161 0.0553  -0.0468 124 THR   A O     
981  C  CB    . THR   A 127 ? 0.2778 0.4279 0.1933 -0.0114 0.0662  0.0036  124 THR   A CB    
982  O  OG1   . THR   A 127 ? 0.2673 0.4486 0.2105 -0.0188 0.0590  0.0144  124 THR   A OG1   
983  C  CG2   . THR   A 127 ? 0.2517 0.4476 0.2429 -0.0161 0.0748  0.0186  124 THR   A CG2   
984  N  N     . VAL   A 128 ? 0.2532 0.4297 0.1840 -0.0251 0.0531  -0.0151 125 VAL   A N     
985  C  CA    . VAL   A 128 ? 0.2604 0.4179 0.1850 -0.0495 0.0523  0.0027  125 VAL   A CA    
986  C  C     . VAL   A 128 ? 0.2849 0.4129 0.1531 -0.0853 0.0850  -0.0034 125 VAL   A C     
987  O  O     . VAL   A 128 ? 0.4517 0.4708 0.1633 -0.0530 0.0819  -0.0298 125 VAL   A O     
988  C  CB    . VAL   A 128 ? 0.2514 0.4168 0.1440 -0.0406 0.0731  -0.0554 125 VAL   A CB    
989  C  CG1   . VAL   A 128 ? 0.2709 0.4073 0.1972 -0.0186 0.0712  -0.0752 125 VAL   A CG1   
990  C  CG2   . VAL   A 128 ? 0.3061 0.4402 0.1783 -0.0136 0.0812  -0.0167 125 VAL   A CG2   
991  N  N     . ASP   A 129 ? 0.3645 0.3675 0.2147 -0.0489 0.0213  0.0357  126 ASP   A N     
992  C  CA    . ASP   A 129 ? 0.3766 0.3746 0.2233 -0.0283 0.0217  0.0146  126 ASP   A CA    
993  C  C     . ASP   A 129 ? 0.3741 0.3028 0.2452 -0.0689 0.0413  0.0217  126 ASP   A C     
994  O  O     . ASP   A 129 ? 0.3387 0.3961 0.2148 -0.0457 0.0580  -0.0259 126 ASP   A O     
995  C  CB    . ASP   A 129 ? 0.4834 0.4251 0.2664 -0.0169 0.0923  0.0269  126 ASP   A CB    
996  C  CG    . ASP   A 129 ? 0.5397 0.4319 0.2863 0.0108  0.0487  0.0162  126 ASP   A CG    
997  O  OD1   . ASP   A 129 ? 0.5392 0.4769 0.4012 0.0317  -0.0289 -0.0157 126 ASP   A OD1   
998  O  OD2   . ASP   A 129 ? 0.4556 0.5249 0.4796 0.0108  0.0759  0.0778  126 ASP   A OD2   
999  N  N     . THR   A 130 ? 0.3895 0.3254 0.2328 -0.0462 -0.0109 -0.0017 127 THR   A N     
1000 C  CA    . THR   A 130 ? 0.3701 0.3576 0.2295 -0.0743 0.0036  0.0249  127 THR   A CA    
1001 C  C     . THR   A 130 ? 0.3427 0.3543 0.1941 -0.0646 0.0466  0.0198  127 THR   A C     
1002 O  O     . THR   A 130 ? 0.3626 0.3695 0.1531 -0.0576 0.0575  -0.0167 127 THR   A O     
1003 C  CB    . THR   A 130 ? 0.3948 0.4095 0.2200 -0.0663 0.0375  -0.0058 127 THR   A CB    
1004 O  OG1   . THR   A 130 ? 0.3600 0.4207 0.2326 -0.0411 0.0518  0.0224  127 THR   A OG1   
1005 C  CG2   . THR   A 130 ? 0.4162 0.4498 0.1635 -0.0414 -0.0314 -0.0650 127 THR   A CG2   
1006 N  N     . LYS   A 131 ? 0.3323 0.3477 0.2426 -0.0770 0.0221  0.0457  128 LYS   A N     
1007 C  CA    . LYS   A 131 ? 0.3557 0.3595 0.2426 -0.0674 0.0225  0.0665  128 LYS   A CA    
1008 C  C     . LYS   A 131 ? 0.3414 0.3261 0.2334 -0.0605 0.0431  0.0810  128 LYS   A C     
1009 O  O     . LYS   A 131 ? 0.3604 0.3714 0.1299 -0.0605 0.0863  0.0164  128 LYS   A O     
1010 C  CB    . LYS   A 131 ? 0.3794 0.4239 0.2559 -0.0964 0.0581  0.0342  128 LYS   A CB    
1011 C  CG    . LYS   A 131 ? 0.4908 0.4464 0.3605 -0.0558 -0.0127 0.0899  128 LYS   A CG    
1012 C  CD    . LYS   A 131 ? 0.4583 0.5456 0.4272 -0.0672 0.0736  0.1275  128 LYS   A CD    
1013 C  CE    . LYS   A 131 ? 0.5529 0.6255 0.4321 -0.0728 0.0412  0.1123  128 LYS   A CE    
1014 N  NZ    . LYS   A 131 ? 0.6075 0.5523 0.5400 -0.0554 -0.0321 0.0846  128 LYS   A NZ    
1015 N  N     . GLN   A 132 ? 0.2927 0.3761 0.1748 -0.0632 0.0897  0.0255  129 GLN   A N     
1016 C  CA    . GLN   A 132 ? 0.3261 0.3646 0.2007 -0.0460 0.0351  0.0365  129 GLN   A CA    
1017 C  C     . GLN   A 132 ? 0.3341 0.3261 0.1826 -0.0493 0.0466  0.0375  129 GLN   A C     
1018 O  O     . GLN   A 132 ? 0.2622 0.3093 0.1790 -0.0165 0.0732  0.0063  129 GLN   A O     
1019 C  CB    . GLN   A 132 ? 0.3675 0.3707 0.2156 -0.0299 0.0543  0.0268  129 GLN   A CB    
1020 C  CG    . GLN   A 132 ? 0.4175 0.3498 0.2424 -0.0113 0.0795  0.0396  129 GLN   A CG    
1021 C  CD    . GLN   A 132 ? 0.3853 0.4186 0.2980 0.0172  0.1261  -0.0226 129 GLN   A CD    
1022 O  OE1   . GLN   A 132 ? 0.5055 0.4278 0.5066 0.0638  0.1059  -0.0994 129 GLN   A OE1   
1023 N  NE2   . GLN   A 132 ? 0.3394 0.5006 0.4018 0.0377  0.0743  0.0399  129 GLN   A NE2   
1024 N  N     . ALA   A 133 ? 0.3036 0.3121 0.1714 -0.0424 0.0329  0.0141  130 ALA   A N     
1025 C  CA    . ALA   A 133 ? 0.3310 0.3337 0.1377 -0.0516 0.0420  0.0176  130 ALA   A CA    
1026 C  C     . ALA   A 133 ? 0.3240 0.3591 0.0376 -0.0630 0.0801  0.0146  130 ALA   A C     
1027 O  O     . ALA   A 133 ? 0.2961 0.3339 0.1172 -0.0108 0.0608  -0.0046 130 ALA   A O     
1028 C  CB    . ALA   A 133 ? 0.3358 0.3408 0.1413 -0.0254 0.0103  0.0163  130 ALA   A CB    
1029 N  N     . GLN   A 134 ? 0.2968 0.3542 0.1077 -0.0501 0.0611  -0.0165 131 GLN   A N     
1030 C  CA    . GLN   A 134 ? 0.3351 0.3901 0.1212 -0.0128 0.0788  -0.0239 131 GLN   A CA    
1031 C  C     . GLN   A 134 ? 0.2982 0.3096 0.1354 -0.0101 0.0662  0.0116  131 GLN   A C     
1032 O  O     . GLN   A 134 ? 0.3013 0.3603 0.0998 -0.0163 0.0757  -0.0404 131 GLN   A O     
1033 C  CB    . GLN   A 134 ? 0.3979 0.3826 0.1485 -0.0134 0.0917  -0.0196 131 GLN   A CB    
1034 C  CG    . GLN   A 134 ? 0.4134 0.4063 0.2393 0.0026  0.0591  -0.0344 131 GLN   A CG    
1035 C  CD    . GLN   A 134 ? 0.4738 0.4621 0.3248 -0.0085 0.1142  -0.0132 131 GLN   A CD    
1036 O  OE1   . GLN   A 134 ? 0.5676 0.5050 0.3158 0.0414  0.0730  -0.0212 131 GLN   A OE1   
1037 N  NE2   . GLN   A 134 ? 0.4653 0.3716 0.3351 0.0335  0.1563  -0.0327 131 GLN   A NE2   
1038 N  N     . ASP   A 135 ? 0.3316 0.2999 0.1473 -0.0069 0.0917  -0.0096 132 ASP   A N     
1039 C  CA    . ASP   A 135 ? 0.2915 0.3172 0.1637 -0.0101 0.0532  -0.0026 132 ASP   A CA    
1040 C  C     . ASP   A 135 ? 0.2598 0.3206 0.1222 0.0016  0.0901  -0.0026 132 ASP   A C     
1041 O  O     . ASP   A 135 ? 0.2581 0.3176 0.1448 -0.0012 0.0725  -0.0118 132 ASP   A O     
1042 C  CB    . ASP   A 135 ? 0.3178 0.2986 0.1486 -0.0233 0.0781  -0.0039 132 ASP   A CB    
1043 C  CG    . ASP   A 135 ? 0.3495 0.3255 0.1810 -0.0386 0.0265  0.0312  132 ASP   A CG    
1044 O  OD1   . ASP   A 135 ? 0.4300 0.3262 0.2584 -0.0159 0.0672  0.0641  132 ASP   A OD1   
1045 O  OD2   . ASP   A 135 ? 0.3498 0.3570 0.2075 -0.0734 0.0787  0.0056  132 ASP   A OD2   
1046 N  N     . LEU   A 136 ? 0.2827 0.3306 0.0826 0.0182  0.0678  -0.0054 133 LEU   A N     
1047 C  CA    . LEU   A 136 ? 0.2863 0.3384 0.1038 0.0032  0.0654  0.0052  133 LEU   A CA    
1048 C  C     . LEU   A 136 ? 0.2779 0.2930 0.1116 0.0019  0.0588  0.0007  133 LEU   A C     
1049 O  O     . LEU   A 136 ? 0.2715 0.2836 0.1268 0.0077  0.0745  -0.0091 133 LEU   A O     
1050 C  CB    . LEU   A 136 ? 0.2474 0.3141 0.1528 0.0135  0.0903  -0.0103 133 LEU   A CB    
1051 C  CG    . LEU   A 136 ? 0.3059 0.2953 0.1575 0.0163  0.0590  -0.0183 133 LEU   A CG    
1052 C  CD1   . LEU   A 136 ? 0.3543 0.2773 0.1777 0.0068  0.0208  -0.0507 133 LEU   A CD1   
1053 C  CD2   . LEU   A 136 ? 0.3352 0.2709 0.2548 0.0249  0.0264  -0.0081 133 LEU   A CD2   
1054 N  N     . ALA   A 137 ? 0.2925 0.2710 0.1109 0.0089  0.0377  0.0033  134 ALA   A N     
1055 C  CA    . ALA   A 137 ? 0.2828 0.2596 0.1289 0.0082  0.0518  -0.0050 134 ALA   A CA    
1056 C  C     . ALA   A 137 ? 0.2607 0.2779 0.1462 0.0336  0.0598  -0.0262 134 ALA   A C     
1057 O  O     . ALA   A 137 ? 0.2871 0.3178 0.1114 -0.0022 0.0630  -0.0110 134 ALA   A O     
1058 C  CB    . ALA   A 137 ? 0.2943 0.2798 0.1274 0.0230  0.0276  -0.0064 134 ALA   A CB    
1059 N  N     . ARG   A 138 ? 0.2831 0.2870 0.1467 0.0286  0.0619  -0.0085 135 ARG   A N     
1060 C  CA    . ARG   A 138 ? 0.2690 0.3162 0.1648 0.0392  0.0681  0.0002  135 ARG   A CA    
1061 C  C     . ARG   A 138 ? 0.3022 0.2976 0.1680 0.0391  0.0583  0.0015  135 ARG   A C     
1062 O  O     . ARG   A 138 ? 0.2954 0.3308 0.1639 0.0601  0.0805  0.0038  135 ARG   A O     
1063 C  CB    . ARG   A 138 ? 0.3473 0.3444 0.2285 -0.0251 0.0302  0.0149  135 ARG   A CB    
1064 C  CG    . ARG   A 138 ? 0.4254 0.3754 0.3202 -0.0020 -0.0265 -0.0022 135 ARG   A CG    
1065 C  CD    . ARG   A 138 ? 0.5972 0.4173 0.4193 -0.0649 0.0222  0.0192  135 ARG   A CD    
1066 N  NE    . ARG   A 138 ? 0.6894 0.4660 0.4503 -0.0475 -0.0556 0.0593  135 ARG   A NE    
1067 C  CZ    . ARG   A 138 ? 0.6918 0.5677 0.5147 -0.1220 -0.0100 0.0478  135 ARG   A CZ    
1068 N  NH1   . ARG   A 138 ? 0.6895 0.6622 0.5640 -0.0204 -0.1090 0.0477  135 ARG   A NH1   
1069 N  NH2   . ARG   A 138 ? 0.7643 0.6871 0.5500 -0.0213 -0.0078 0.0925  135 ARG   A NH2   
1070 N  N     . SER   A 139 ? 0.2480 0.3118 0.1493 0.0129  0.0649  0.0205  136 SER   A N     
1071 C  CA    . SER   A 139 ? 0.2894 0.3199 0.1531 0.0131  0.0423  0.0136  136 SER   A CA    
1072 C  C     . SER   A 139 ? 0.2713 0.3221 0.1636 0.0284  0.0565  0.0022  136 SER   A C     
1073 O  O     . SER   A 139 ? 0.2474 0.3323 0.1524 0.0065  0.0827  0.0140  136 SER   A O     
1074 C  CB    . SER   A 139 ? 0.2715 0.4252 0.1313 0.0174  0.0781  -0.0282 136 SER   A CB    
1075 O  OG    . SER   A 139 ? 0.4001 0.3867 0.2062 -0.0306 0.0286  0.0007  136 SER   A OG    
1076 N  N     . TYR   A 140 ? 0.2943 0.2815 0.1615 0.0155  0.0081  -0.0061 137 TYR   A N     
1077 C  CA    . TYR   A 140 ? 0.3016 0.2968 0.1706 0.0291  0.0249  -0.0051 137 TYR   A CA    
1078 C  C     . TYR   A 140 ? 0.3019 0.3192 0.1615 0.0274  0.0156  -0.0054 137 TYR   A C     
1079 O  O     . TYR   A 140 ? 0.3136 0.3435 0.2046 0.0182  0.0456  -0.0390 137 TYR   A O     
1080 C  CB    . TYR   A 140 ? 0.3268 0.2529 0.1573 0.0336  0.0589  0.0040  137 TYR   A CB    
1081 C  CG    . TYR   A 140 ? 0.3095 0.3119 0.1366 0.0501  0.0808  0.0255  137 TYR   A CG    
1082 C  CD1   . TYR   A 140 ? 0.3404 0.2897 0.1393 0.0248  0.0697  0.0145  137 TYR   A CD1   
1083 C  CD2   . TYR   A 140 ? 0.3182 0.3302 0.1639 0.0057  0.0526  0.0513  137 TYR   A CD2   
1084 C  CE1   . TYR   A 140 ? 0.3744 0.3389 0.1258 0.0679  0.0390  0.0009  137 TYR   A CE1   
1085 C  CE2   . TYR   A 140 ? 0.3226 0.3163 0.1597 -0.0229 0.0469  0.0446  137 TYR   A CE2   
1086 C  CZ    . TYR   A 140 ? 0.3278 0.3173 0.1769 0.0267  0.0332  0.0423  137 TYR   A CZ    
1087 O  OH    . TYR   A 140 ? 0.3526 0.2732 0.1749 0.0037  0.0443  0.0403  137 TYR   A OH    
1088 N  N     . GLY   A 141 ? 0.3080 0.3240 0.1401 0.0450  0.0426  0.0039  138 GLY   A N     
1089 C  CA    . GLY   A 141 ? 0.2655 0.3393 0.1563 0.0273  0.0207  -0.0046 138 GLY   A CA    
1090 C  C     . GLY   A 141 ? 0.2897 0.3058 0.1839 0.0285  0.0349  0.0292  138 GLY   A C     
1091 O  O     . GLY   A 141 ? 0.2954 0.3900 0.1675 0.0260  0.0293  0.0296  138 GLY   A O     
1092 N  N     . ILE   A 142 ? 0.2493 0.2736 0.1122 0.0120  0.1032  0.0002  139 ILE   A N     
1093 C  CA    . ILE   A 142 ? 0.2775 0.2701 0.1166 -0.0064 0.1125  -0.0066 139 ILE   A CA    
1094 C  C     . ILE   A 142 ? 0.3065 0.2684 0.1548 0.0036  0.0634  -0.0094 139 ILE   A C     
1095 O  O     . ILE   A 142 ? 0.3023 0.2973 0.1451 -0.0023 0.0670  0.0048  139 ILE   A O     
1096 C  CB    . ILE   A 142 ? 0.2776 0.2716 0.0976 -0.0065 0.0790  0.0079  139 ILE   A CB    
1097 C  CG1   . ILE   A 142 ? 0.2579 0.2867 0.1206 -0.0181 0.0119  0.0222  139 ILE   A CG1   
1098 C  CG2   . ILE   A 142 ? 0.2687 0.2988 0.1066 -0.0072 0.0847  -0.0079 139 ILE   A CG2   
1099 C  CD1   . ILE   A 142 ? 0.2375 0.2974 0.1239 -0.0232 0.0088  0.0290  139 ILE   A CD1   
1100 N  N     . PRO   A 143 ? 0.2722 0.2510 0.1597 0.0041  0.0782  -0.0081 140 PRO   A N     
1101 C  CA    . PRO   A 143 ? 0.2855 0.2535 0.1750 -0.0127 0.0788  0.0141  140 PRO   A CA    
1102 C  C     . PRO   A 143 ? 0.3154 0.2867 0.1178 0.0039  0.0794  0.0119  140 PRO   A C     
1103 O  O     . PRO   A 143 ? 0.2942 0.2929 0.1249 -0.0076 0.0541  0.0255  140 PRO   A O     
1104 C  CB    . PRO   A 143 ? 0.3207 0.2745 0.1220 0.0039  0.0590  0.0031  140 PRO   A CB    
1105 C  CG    . PRO   A 143 ? 0.3019 0.2478 0.1186 0.0040  0.0827  0.0144  140 PRO   A CG    
1106 C  CD    . PRO   A 143 ? 0.2533 0.2180 0.2060 0.0087  0.0649  -0.0125 140 PRO   A CD    
1107 N  N     . PHE   A 144 ? 0.3337 0.2723 0.1519 0.0054  0.0840  -0.0144 141 PHE   A N     
1108 C  CA    . PHE   A 144 ? 0.3053 0.2515 0.1555 -0.0274 0.1019  -0.0098 141 PHE   A CA    
1109 C  C     . PHE   A 144 ? 0.2821 0.2776 0.1932 -0.0058 0.0492  -0.0075 141 PHE   A C     
1110 O  O     . PHE   A 144 ? 0.2987 0.3017 0.1424 -0.0208 0.0917  -0.0285 141 PHE   A O     
1111 C  CB    . PHE   A 144 ? 0.3275 0.2917 0.1201 -0.0183 0.1017  -0.0087 141 PHE   A CB    
1112 C  CG    . PHE   A 144 ? 0.3312 0.3015 0.1691 -0.0130 0.0637  -0.0304 141 PHE   A CG    
1113 C  CD1   . PHE   A 144 ? 0.3473 0.3243 0.1288 0.0391  0.0456  -0.0490 141 PHE   A CD1   
1114 C  CD2   . PHE   A 144 ? 0.3474 0.2901 0.1450 -0.0095 0.0325  0.0042  141 PHE   A CD2   
1115 C  CE1   . PHE   A 144 ? 0.3340 0.2808 0.1521 0.0097  0.0422  -0.0196 141 PHE   A CE1   
1116 C  CE2   . PHE   A 144 ? 0.2877 0.3280 0.2566 -0.0374 0.0541  -0.0072 141 PHE   A CE2   
1117 C  CZ    . PHE   A 144 ? 0.3408 0.3232 0.1820 -0.0106 0.0211  -0.0447 141 PHE   A CZ    
1118 N  N     . ILE   A 145 ? 0.3262 0.2887 0.1640 -0.0354 0.0866  0.0033  142 ILE   A N     
1119 C  CA    . ILE   A 145 ? 0.3443 0.3211 0.2048 -0.0344 0.0789  -0.0494 142 ILE   A CA    
1120 C  C     . ILE   A 145 ? 0.3341 0.3013 0.1650 -0.0442 0.0977  -0.0417 142 ILE   A C     
1121 O  O     . ILE   A 145 ? 0.3070 0.3233 0.1594 -0.0672 0.0354  -0.0384 142 ILE   A O     
1122 C  CB    . ILE   A 145 ? 0.3252 0.3360 0.1725 -0.0778 0.0567  -0.0524 142 ILE   A CB    
1123 C  CG1   . ILE   A 145 ? 0.3716 0.3425 0.2076 -0.0459 0.0790  -0.0350 142 ILE   A CG1   
1124 C  CG2   . ILE   A 145 ? 0.4093 0.3508 0.1660 -0.1035 0.0082  -0.0269 142 ILE   A CG2   
1125 C  CD1   . ILE   A 145 ? 0.3935 0.5210 0.2316 -0.0665 0.1035  -0.0255 142 ILE   A CD1   
1126 N  N     . GLU   A 146 ? 0.3383 0.3276 0.1721 -0.0555 0.0909  -0.0310 143 GLU   A N     
1127 C  CA    . GLU   A 146 ? 0.3128 0.3742 0.1807 -0.0370 0.0975  -0.0506 143 GLU   A CA    
1128 C  C     . GLU   A 146 ? 0.2993 0.3825 0.1750 0.0260  0.0392  -0.0112 143 GLU   A C     
1129 O  O     . GLU   A 146 ? 0.3607 0.3546 0.1620 -0.0463 0.0898  0.0039  143 GLU   A O     
1130 C  CB    . GLU   A 146 ? 0.3460 0.4159 0.1701 -0.0691 0.0628  0.0048  143 GLU   A CB    
1131 C  CG    . GLU   A 146 ? 0.3545 0.4602 0.1648 -0.0886 0.0594  -0.0073 143 GLU   A CG    
1132 C  CD    . GLU   A 146 ? 0.3394 0.4531 0.1957 -0.0508 0.0667  -0.0489 143 GLU   A CD    
1133 O  OE1   . GLU   A 146 ? 0.3579 0.4600 0.1950 -0.1041 0.0546  -0.0243 143 GLU   A OE1   
1134 O  OE2   . GLU   A 146 ? 0.3877 0.4488 0.1801 -0.0652 0.0808  -0.0249 143 GLU   A OE2   
1135 N  N     . THR   A 147 ? 0.2805 0.3498 0.1031 -0.0650 0.0630  -0.0257 144 THR   A N     
1136 C  CA    . THR   A 147 ? 0.3297 0.3195 0.1109 -0.0485 0.0699  -0.0178 144 THR   A CA    
1137 C  C     . THR   A 147 ? 0.3202 0.4082 0.1134 -0.0187 0.0543  -0.0687 144 THR   A C     
1138 O  O     . THR   A 147 ? 0.2822 0.3804 0.1265 -0.0341 0.0325  -0.0296 144 THR   A O     
1139 C  CB    . THR   A 147 ? 0.3195 0.2851 0.1109 -0.0345 0.0850  -0.0058 144 THR   A CB    
1140 O  OG1   . THR   A 147 ? 0.2790 0.2840 0.1212 -0.0064 0.0441  -0.0161 144 THR   A OG1   
1141 C  CG2   . THR   A 147 ? 0.2981 0.3338 0.1361 -0.0284 0.0981  -0.0451 144 THR   A CG2   
1142 N  N     . SER   A 148 ? 0.3161 0.4222 0.1030 -0.0648 0.0519  -0.0200 145 SER   A N     
1143 C  CA    . SER   A 148 ? 0.2656 0.3923 0.1555 -0.0460 0.0718  -0.0225 145 SER   A CA    
1144 C  C     . SER   A 148 ? 0.2452 0.3496 0.1951 -0.0367 0.0695  -0.0024 145 SER   A C     
1145 O  O     . SER   A 148 ? 0.3191 0.4140 0.1526 -0.0518 0.0477  -0.0415 145 SER   A O     
1146 C  CB    . SER   A 148 ? 0.2638 0.4600 0.1965 -0.0446 0.0408  -0.0087 145 SER   A CB    
1147 O  OG    . SER   A 148 ? 0.3342 0.4533 0.1660 -0.0604 0.0322  -0.0004 145 SER   A OG    
1148 N  N     . ALA   A 149 ? 0.2885 0.3740 0.1301 -0.0819 0.0810  -0.0459 146 ALA   A N     
1149 C  CA    . ALA   A 149 ? 0.3091 0.3453 0.1360 -0.0445 0.0636  0.0009  146 ALA   A CA    
1150 C  C     . ALA   A 149 ? 0.2861 0.3939 0.1436 -0.0339 0.0678  -0.0206 146 ALA   A C     
1151 O  O     . ALA   A 149 ? 0.3281 0.4291 0.1307 -0.0410 0.0820  -0.0322 146 ALA   A O     
1152 C  CB    . ALA   A 149 ? 0.2903 0.3471 0.1785 -0.0364 0.0981  -0.0220 146 ALA   A CB    
1153 N  N     . LYS   A 150 ? 0.2822 0.3911 0.1662 -0.0272 0.0288  -0.0624 147 LYS   A N     
1154 C  CA    . LYS   A 150 ? 0.2971 0.4385 0.2028 -0.0105 -0.0097 -0.0163 147 LYS   A CA    
1155 C  C     . LYS   A 150 ? 0.2846 0.4485 0.1574 -0.0074 0.0103  -0.0444 147 LYS   A C     
1156 O  O     . LYS   A 150 ? 0.4142 0.5000 0.1523 -0.0566 -0.0007 -0.0308 147 LYS   A O     
1157 C  CB    . LYS   A 150 ? 0.2975 0.5041 0.1619 -0.0530 -0.0038 -0.0245 147 LYS   A CB    
1158 C  CG    . LYS   A 150 ? 0.3294 0.5888 0.2283 -0.0070 -0.0450 0.0060  147 LYS   A CG    
1159 C  CD    . LYS   A 150 ? 0.3265 0.5936 0.2747 -0.0368 -0.0321 0.0253  147 LYS   A CD    
1160 C  CE    . LYS   A 150 ? 0.3734 0.5980 0.2942 -0.0591 -0.0266 -0.0027 147 LYS   A CE    
1161 N  NZ    . LYS   A 150 ? 0.3868 0.5430 0.3687 -0.0345 -0.0159 -0.0087 147 LYS   A NZ    
1162 N  N     . THR   A 151 ? 0.3608 0.4277 0.2019 -0.0079 0.0087  -0.0727 148 THR   A N     
1163 C  CA    . THR   A 151 ? 0.4126 0.4071 0.1247 -0.0494 -0.0217 -0.0451 148 THR   A CA    
1164 C  C     . THR   A 151 ? 0.4171 0.3815 0.1668 -0.0247 0.0374  -0.0467 148 THR   A C     
1165 O  O     . THR   A 151 ? 0.4774 0.3964 0.2590 -0.0363 -0.0019 -0.0772 148 THR   A O     
1166 C  CB    . THR   A 151 ? 0.4052 0.4733 0.2321 -0.0709 0.0044  -0.0396 148 THR   A CB    
1167 O  OG1   . THR   A 151 ? 0.5379 0.4571 0.2573 -0.0733 -0.0656 -0.0569 148 THR   A OG1   
1168 C  CG2   . THR   A 151 ? 0.3861 0.4465 0.3249 -0.0555 -0.0318 -0.0156 148 THR   A CG2   
1169 N  N     . ARG   A 152 ? 0.4032 0.3742 0.1306 -0.0525 0.0819  -0.0526 149 ARG   A N     
1170 C  CA    . ARG   A 152 ? 0.3999 0.3869 0.1909 -0.0044 0.0794  -0.0631 149 ARG   A CA    
1171 C  C     . ARG   A 152 ? 0.3880 0.3976 0.3289 -0.0284 0.1110  0.0031  149 ARG   A C     
1172 O  O     . ARG   A 152 ? 0.4409 0.4268 0.2479 -0.0361 0.0247  -0.0812 149 ARG   A O     
1173 C  CB    . ARG   A 152 ? 0.4351 0.4186 0.2149 0.0053  0.1145  -0.0292 149 ARG   A CB    
1174 C  CG    . ARG   A 152 ? 0.4453 0.4674 0.2665 -0.0085 0.0960  -0.0380 149 ARG   A CG    
1175 C  CD    . ARG   A 152 ? 0.4474 0.5268 0.3015 0.0172  0.1386  -0.0587 149 ARG   A CD    
1176 N  NE    . ARG   A 152 ? 0.5079 0.4915 0.2644 -0.0282 0.0581  -0.0241 149 ARG   A NE    
1177 C  CZ    . ARG   A 152 ? 0.5283 0.3822 0.4088 -0.0491 0.0303  0.0320  149 ARG   A CZ    
1178 N  NH1   . ARG   A 152 ? 0.6134 0.3225 0.3857 -0.0385 0.0962  -0.0758 149 ARG   A NH1   
1179 N  NH2   . ARG   A 152 ? 0.5973 0.4805 0.4582 -0.1195 0.0294  -0.0474 149 ARG   A NH2   
1180 N  N     . GLN   A 153 ? 0.3172 0.3506 0.2020 -0.0627 0.0169  -0.0379 150 GLN   A N     
1181 C  CA    . GLN   A 153 ? 0.3514 0.3798 0.2577 -0.0726 -0.0089 -0.0031 150 GLN   A CA    
1182 C  C     . GLN   A 153 ? 0.3502 0.2735 0.2099 -0.0825 0.0355  -0.0261 150 GLN   A C     
1183 O  O     . GLN   A 153 ? 0.3356 0.3106 0.1645 -0.0395 0.0424  -0.0347 150 GLN   A O     
1184 C  CB    . GLN   A 153 ? 0.3994 0.3878 0.2578 -0.1035 0.0099  0.0178  150 GLN   A CB    
1185 C  CG    . GLN   A 153 ? 0.4474 0.4164 0.4163 -0.0565 0.0159  0.0882  150 GLN   A CG    
1186 C  CD    . GLN   A 153 ? 0.5924 0.4923 0.3691 -0.0190 0.0169  0.0417  150 GLN   A CD    
1187 O  OE1   . GLN   A 153 ? 0.7349 0.6798 0.4180 -0.1067 -0.0634 0.0126  150 GLN   A OE1   
1188 N  NE2   . GLN   A 153 ? 0.7461 0.5346 0.6401 0.0257  -0.0776 0.1097  150 GLN   A NE2   
1189 N  N     . ARG   A 154 ? 0.3584 0.3194 0.1732 -0.0714 0.0201  -0.0270 151 ARG   A N     
1190 C  CA    . ARG   A 154 ? 0.3678 0.3514 0.1370 -0.0512 0.0343  -0.0461 151 ARG   A CA    
1191 C  C     . ARG   A 154 ? 0.3330 0.3578 0.1608 -0.0459 0.0205  -0.0030 151 ARG   A C     
1192 O  O     . ARG   A 154 ? 0.3297 0.3268 0.1390 -0.0264 0.0356  -0.0107 151 ARG   A O     
1193 C  CB    . ARG   A 154 ? 0.3655 0.3633 0.1215 -0.0443 0.0307  -0.0435 151 ARG   A CB    
1194 C  CG    . ARG   A 154 ? 0.4662 0.3771 0.1566 -0.0632 0.0140  -0.0319 151 ARG   A CG    
1195 C  CD    . ARG   A 154 ? 0.5349 0.4248 0.1609 -0.0546 0.0217  -0.0116 151 ARG   A CD    
1196 N  NE    . ARG   A 154 ? 0.5358 0.5927 0.5748 -0.0484 0.0153  -0.0058 151 ARG   A NE    
1197 C  CZ    . ARG   A 154 ? 0.5216 0.4240 0.5085 -0.0154 0.0589  -0.0153 151 ARG   A CZ    
1198 N  NH1   . ARG   A 154 ? 0.6202 0.4447 0.5296 0.0560  0.0322  0.0515  151 ARG   A NH1   
1199 N  NH2   . ARG   A 154 ? 0.5133 0.5327 0.6339 -0.0049 -0.0415 -0.0434 151 ARG   A NH2   
1200 N  N     . VAL   A 155 ? 0.3734 0.3090 0.1213 -0.0411 0.0424  -0.0529 152 VAL   A N     
1201 C  CA    . VAL   A 155 ? 0.3614 0.3372 0.1511 -0.0334 0.0258  -0.0198 152 VAL   A CA    
1202 C  C     . VAL   A 155 ? 0.3397 0.2708 0.1843 -0.0431 0.0433  0.0042  152 VAL   A C     
1203 O  O     . VAL   A 155 ? 0.2879 0.3258 0.1400 -0.0430 0.0726  -0.0089 152 VAL   A O     
1204 C  CB    . VAL   A 155 ? 0.3518 0.3135 0.1487 -0.0132 0.0135  -0.0397 152 VAL   A CB    
1205 C  CG1   . VAL   A 155 ? 0.2921 0.3697 0.1812 -0.0259 0.0277  0.0142  152 VAL   A CG1   
1206 C  CG2   . VAL   A 155 ? 0.3151 0.3233 0.1939 -0.0536 0.0016  0.0233  152 VAL   A CG2   
1207 N  N     . GLU   A 156 ? 0.3524 0.2706 0.1603 -0.0407 0.0186  -0.0109 153 GLU   A N     
1208 C  CA    . GLU   A 156 ? 0.3444 0.2511 0.1856 -0.0299 0.0253  -0.0310 153 GLU   A CA    
1209 C  C     . GLU   A 156 ? 0.3281 0.2567 0.1922 -0.0052 0.0359  -0.0376 153 GLU   A C     
1210 O  O     . GLU   A 156 ? 0.3056 0.3051 0.1425 -0.0198 0.0819  -0.0292 153 GLU   A O     
1211 C  CB    . GLU   A 156 ? 0.4003 0.3004 0.1891 -0.0122 0.0670  -0.0401 153 GLU   A CB    
1212 C  CG    . GLU   A 156 ? 0.4263 0.3896 0.3851 -0.0154 0.0416  -0.0879 153 GLU   A CG    
1213 C  CD    . GLU   A 156 ? 0.4204 0.4737 0.3695 0.0038  0.0709  -0.0815 153 GLU   A CD    
1214 O  OE1   . GLU   A 156 ? 0.5699 0.5276 0.3820 -0.0312 0.0080  -0.0796 153 GLU   A OE1   
1215 O  OE2   . GLU   A 156 ? 0.4962 0.5244 0.5672 0.0803  0.0531  -0.0282 153 GLU   A OE2   
1216 N  N     . ASP   A 157 ? 0.3774 0.2919 0.1904 -0.0241 0.0276  -0.0081 154 ASP   A N     
1217 C  CA    . ASP   A 157 ? 0.3982 0.3065 0.2031 -0.0258 0.0339  0.0062  154 ASP   A CA    
1218 C  C     . ASP   A 157 ? 0.3512 0.2907 0.1712 -0.0332 0.0726  0.0233  154 ASP   A C     
1219 O  O     . ASP   A 157 ? 0.3129 0.2856 0.2000 -0.0312 0.0889  0.0088  154 ASP   A O     
1220 C  CB    . ASP   A 157 ? 0.3741 0.2878 0.2203 -0.0161 0.0216  -0.0222 154 ASP   A CB    
1221 C  CG    . ASP   A 157 ? 0.4192 0.2976 0.2950 -0.0097 -0.0051 -0.0352 154 ASP   A CG    
1222 O  OD1   . ASP   A 157 ? 0.4163 0.3526 0.3280 -0.0080 0.0042  0.0010  154 ASP   A OD1   
1223 O  OD2   . ASP   A 157 ? 0.4803 0.3589 0.2868 -0.0483 0.0002  -0.0199 154 ASP   A OD2   
1224 N  N     . ALA   A 158 ? 0.3229 0.2900 0.1126 -0.0401 0.0298  -0.0136 155 ALA   A N     
1225 C  CA    . ALA   A 158 ? 0.3556 0.2746 0.0850 -0.0031 0.0512  0.0058  155 ALA   A CA    
1226 C  C     . ALA   A 158 ? 0.3595 0.2728 0.1283 -0.0031 0.0669  0.0122  155 ALA   A C     
1227 O  O     . ALA   A 158 ? 0.3005 0.2803 0.1302 -0.0052 0.0863  0.0076  155 ALA   A O     
1228 C  CB    . ALA   A 158 ? 0.2952 0.3302 0.1429 -0.0035 0.1166  -0.0260 155 ALA   A CB    
1229 N  N     . PHE   A 159 ? 0.3561 0.3010 0.1221 0.0079  0.0803  0.0029  156 PHE   A N     
1230 C  CA    . PHE   A 159 ? 0.3385 0.3046 0.1011 0.0016  0.0468  0.0178  156 PHE   A CA    
1231 C  C     . PHE   A 159 ? 0.3164 0.2677 0.1402 -0.0204 0.0756  0.0425  156 PHE   A C     
1232 O  O     . PHE   A 159 ? 0.3016 0.2692 0.1110 0.0058  0.0879  -0.0127 156 PHE   A O     
1233 C  CB    . PHE   A 159 ? 0.3307 0.2865 0.0670 -0.0094 0.0430  -0.0196 156 PHE   A CB    
1234 C  CG    . PHE   A 159 ? 0.3147 0.2850 0.0954 -0.0188 0.0934  0.0236  156 PHE   A CG    
1235 C  CD1   . PHE   A 159 ? 0.3252 0.2801 0.1230 0.0069  0.0643  -0.0148 156 PHE   A CD1   
1236 C  CD2   . PHE   A 159 ? 0.3179 0.2492 0.1034 -0.0301 0.0961  -0.0273 156 PHE   A CD2   
1237 C  CE1   . PHE   A 159 ? 0.3469 0.2522 0.1274 -0.0073 0.0811  0.0015  156 PHE   A CE1   
1238 C  CE2   . PHE   A 159 ? 0.2983 0.2944 0.0946 -0.0219 0.0598  0.0107  156 PHE   A CE2   
1239 C  CZ    . PHE   A 159 ? 0.3275 0.2383 0.1171 0.0066  0.0955  0.0150  156 PHE   A CZ    
1240 N  N     . TYR   A 160 ? 0.3173 0.2939 0.1116 -0.0047 0.0982  -0.0070 157 TYR   A N     
1241 C  CA    . TYR   A 160 ? 0.3300 0.2438 0.1621 -0.0176 0.0691  0.0271  157 TYR   A CA    
1242 C  C     . TYR   A 160 ? 0.3219 0.2332 0.1755 0.0000  0.0552  0.0271  157 TYR   A C     
1243 O  O     . TYR   A 160 ? 0.3373 0.2862 0.1366 0.0211  0.0752  0.0075  157 TYR   A O     
1244 C  CB    . TYR   A 160 ? 0.3842 0.3062 0.2395 0.0040  0.0812  -0.0356 157 TYR   A CB    
1245 C  CG    . TYR   A 160 ? 0.4101 0.3327 0.2477 -0.0006 0.0843  -0.0201 157 TYR   A CG    
1246 C  CD1   . TYR   A 160 ? 0.3748 0.3842 0.1378 -0.0419 0.0682  -0.0291 157 TYR   A CD1   
1247 C  CD2   . TYR   A 160 ? 0.5288 0.3940 0.2683 -0.0502 0.1289  -0.0425 157 TYR   A CD2   
1248 C  CE1   . TYR   A 160 ? 0.4138 0.4569 0.2084 -0.0636 0.1144  0.0746  157 TYR   A CE1   
1249 C  CE2   . TYR   A 160 ? 0.5560 0.5173 0.2594 -0.0804 0.1049  -0.0264 157 TYR   A CE2   
1250 C  CZ    . TYR   A 160 ? 0.5670 0.5652 0.0411 -0.0556 0.0948  0.0794  157 TYR   A CZ    
1251 O  OH    . TYR   A 160 ? 0.6846 0.7628 0.0826 -0.1886 0.2045  0.0446  157 TYR   A OH    
1252 N  N     . THR   A 161 ? 0.3169 0.2533 0.1378 -0.0009 0.0513  -0.0151 158 THR   A N     
1253 C  CA    . THR   A 161 ? 0.3189 0.2497 0.1462 0.0137  0.0616  -0.0108 158 THR   A CA    
1254 C  C     . THR   A 161 ? 0.2632 0.2543 0.1577 0.0123  0.0882  0.0039  158 THR   A C     
1255 O  O     . THR   A 161 ? 0.2863 0.2717 0.1580 0.0040  0.0797  0.0072  158 THR   A O     
1256 C  CB    . THR   A 161 ? 0.3022 0.2500 0.1308 0.0154  0.0663  -0.0164 158 THR   A CB    
1257 O  OG1   . THR   A 161 ? 0.3298 0.2745 0.1483 -0.0076 0.0600  -0.0042 158 THR   A OG1   
1258 C  CG2   . THR   A 161 ? 0.3890 0.2793 0.1337 0.0200  0.0633  0.0034  158 THR   A CG2   
1259 N  N     . LEU   A 162 ? 0.3063 0.2790 0.1133 0.0191  0.0509  0.0198  159 LEU   A N     
1260 C  CA    . LEU   A 162 ? 0.2897 0.2977 0.1079 0.0059  0.0516  0.0191  159 LEU   A CA    
1261 C  C     . LEU   A 162 ? 0.2818 0.2039 0.1584 0.0231  0.0591  0.0059  159 LEU   A C     
1262 O  O     . LEU   A 162 ? 0.2980 0.2077 0.1543 0.0112  0.0757  -0.0012 159 LEU   A O     
1263 C  CB    . LEU   A 162 ? 0.2204 0.2936 0.1295 -0.0003 0.0409  0.0128  159 LEU   A CB    
1264 C  CG    . LEU   A 162 ? 0.2237 0.2662 0.1389 0.0119  0.0842  -0.0038 159 LEU   A CG    
1265 C  CD1   . LEU   A 162 ? 0.2421 0.2256 0.1347 -0.0107 0.0645  0.0049  159 LEU   A CD1   
1266 C  CD2   . LEU   A 162 ? 0.2282 0.2384 0.1424 0.0105  0.0767  -0.0422 159 LEU   A CD2   
1267 N  N     . VAL   A 163 ? 0.3012 0.2637 0.1240 0.0288  0.0425  0.0093  160 VAL   A N     
1268 C  CA    . VAL   A 163 ? 0.3205 0.2817 0.1508 0.0439  0.0706  -0.0023 160 VAL   A CA    
1269 C  C     . VAL   A 163 ? 0.3094 0.2672 0.1330 0.0615  0.0872  -0.0331 160 VAL   A C     
1270 O  O     . VAL   A 163 ? 0.3084 0.2987 0.1503 0.0218  0.1050  -0.0212 160 VAL   A O     
1271 C  CB    . VAL   A 163 ? 0.3332 0.2496 0.1499 0.0333  0.0823  0.0124  160 VAL   A CB    
1272 C  CG1   . VAL   A 163 ? 0.3408 0.2486 0.1520 0.0335  0.0863  0.0077  160 VAL   A CG1   
1273 C  CG2   . VAL   A 163 ? 0.3532 0.2423 0.1810 0.0551  0.1068  0.0080  160 VAL   A CG2   
1274 N  N     . ARG   A 164 ? 0.3557 0.2568 0.1849 0.0515  0.0319  -0.0004 161 ARG   A N     
1275 C  CA    . ARG   A 164 ? 0.3210 0.2725 0.1819 0.0743  0.0713  0.0146  161 ARG   A CA    
1276 C  C     . ARG   A 164 ? 0.3303 0.2409 0.2172 0.0372  0.0671  0.0027  161 ARG   A C     
1277 O  O     . ARG   A 164 ? 0.3241 0.2712 0.2241 0.0349  0.0677  0.0314  161 ARG   A O     
1278 C  CB    . ARG   A 164 ? 0.3399 0.2888 0.1580 0.0491  0.0420  0.0292  161 ARG   A CB    
1279 C  CG    . ARG   A 164 ? 0.3862 0.3356 0.1544 0.0345  0.0911  0.0246  161 ARG   A CG    
1280 C  CD    . ARG   A 164 ? 0.4125 0.3407 0.2325 0.0226  0.0466  0.0387  161 ARG   A CD    
1281 N  NE    . ARG   A 164 ? 0.4400 0.4165 0.2149 0.0090  0.0062  0.0394  161 ARG   A NE    
1282 C  CZ    . ARG   A 164 ? 0.3976 0.3182 0.3333 0.0024  -0.0250 0.0625  161 ARG   A CZ    
1283 N  NH1   . ARG   A 164 ? 0.4198 0.3192 0.3735 0.0165  -0.0081 0.0290  161 ARG   A NH1   
1284 N  NH2   . ARG   A 164 ? 0.5504 0.4678 0.2504 -0.1036 -0.0043 0.0792  161 ARG   A NH2   
1285 N  N     . GLU   A 165 ? 0.3255 0.2338 0.1652 0.0377  0.0499  0.0259  162 GLU   A N     
1286 C  CA    . GLU   A 165 ? 0.3097 0.2864 0.1713 0.0355  -0.0055 -0.0032 162 GLU   A CA    
1287 C  C     . GLU   A 165 ? 0.3139 0.2633 0.1668 0.0231  0.0336  0.0005  162 GLU   A C     
1288 O  O     . GLU   A 165 ? 0.2910 0.3037 0.1730 0.0280  0.0355  -0.0102 162 GLU   A O     
1289 C  CB    . GLU   A 165 ? 0.2954 0.2778 0.1537 0.0230  0.0171  0.0177  162 GLU   A CB    
1290 C  CG    . GLU   A 165 ? 0.3153 0.2341 0.1661 0.0270  0.0418  0.0041  162 GLU   A CG    
1291 C  CD    . GLU   A 165 ? 0.2878 0.2577 0.1994 0.0056  0.0480  0.0329  162 GLU   A CD    
1292 O  OE1   . GLU   A 165 ? 0.3788 0.2832 0.1963 0.0468  0.0176  0.0091  162 GLU   A OE1   
1293 O  OE2   . GLU   A 165 ? 0.3508 0.2789 0.2505 -0.0050 0.0381  0.0078  162 GLU   A OE2   
1294 N  N     . ILE   A 166 ? 0.3156 0.2760 0.1408 0.0455  0.0275  -0.0160 163 ILE   A N     
1295 C  CA    . ILE   A 166 ? 0.3451 0.2943 0.1461 0.0228  0.0299  0.0058  163 ILE   A CA    
1296 C  C     . ILE   A 166 ? 0.2990 0.2620 0.2519 0.0008  0.0532  -0.0120 163 ILE   A C     
1297 O  O     . ILE   A 166 ? 0.2852 0.3231 0.2234 0.0185  0.0915  -0.0250 163 ILE   A O     
1298 C  CB    . ILE   A 166 ? 0.3204 0.3014 0.1233 0.0233  0.0408  0.0008  163 ILE   A CB    
1299 C  CG1   . ILE   A 166 ? 0.2810 0.3559 0.1753 0.0277  0.0771  0.0257  163 ILE   A CG1   
1300 C  CG2   . ILE   A 166 ? 0.2861 0.3599 0.1735 0.0174  0.0669  0.0030  163 ILE   A CG2   
1301 C  CD1   . ILE   A 166 ? 0.3204 0.2988 0.1993 0.0513  0.0604  -0.0017 163 ILE   A CD1   
1302 N  N     . ARG   A 167 ? 0.2951 0.3602 0.2195 0.0384  0.0341  -0.0459 164 ARG   A N     
1303 C  CA    . ARG   A 167 ? 0.3302 0.3130 0.3006 0.0496  0.0290  -0.0202 164 ARG   A CA    
1304 C  C     . ARG   A 167 ? 0.2948 0.3598 0.2860 0.0143  0.0225  -0.0432 164 ARG   A C     
1305 O  O     . ARG   A 167 ? 0.2924 0.4193 0.2849 0.0548  0.0307  -0.0865 164 ARG   A O     
1306 C  CB    . ARG   A 167 ? 0.3631 0.3206 0.3258 0.0061  0.0263  -0.0170 164 ARG   A CB    
1307 C  CG    . ARG   A 167 ? 0.3823 0.3152 0.3557 0.0334  0.0618  0.0239  164 ARG   A CG    
1308 C  CD    . ARG   A 167 ? 0.5043 0.3650 0.2538 0.0110  0.0497  0.0408  164 ARG   A CD    
1309 N  NE    . ARG   A 167 ? 0.4831 0.3404 0.2655 0.0088  0.0940  0.0107  164 ARG   A NE    
1310 C  CZ    . ARG   A 167 ? 0.5408 0.4175 0.1896 -0.0391 0.0922  0.0396  164 ARG   A CZ    
1311 N  NH1   . ARG   A 167 ? 0.5641 0.3947 0.1744 -0.0256 0.1542  0.0082  164 ARG   A NH1   
1312 N  NH2   . ARG   A 167 ? 0.5469 0.4898 0.1655 0.0028  0.1168  0.0468  164 ARG   A NH2   
1313 N  N     . GLN   A 168 ? 0.3157 0.3200 0.2873 0.0404  0.0298  0.0080  165 GLN   A N     
1314 C  CA    . GLN   A 168 ? 0.3203 0.3901 0.2573 0.0586  0.0180  -0.0067 165 GLN   A CA    
1315 C  C     . GLN   A 168 ? 0.2936 0.3818 0.3085 0.0531  -0.0125 0.0112  165 GLN   A C     
1316 O  O     . GLN   A 168 ? 0.3807 0.4011 0.2604 0.1022  -0.0233 0.0040  165 GLN   A O     
1317 C  CB    . GLN   A 168 ? 0.3786 0.3633 0.2226 -0.0062 0.0178  0.0329  165 GLN   A CB    
1318 C  CG    . GLN   A 168 ? 0.4090 0.3450 0.3213 0.0192  0.0002  0.0407  165 GLN   A CG    
1319 C  CD    . GLN   A 168 ? 0.3419 0.3419 0.3419 0.0000  0.0000  0.0000  165 GLN   A CD    
1320 O  OE1   . GLN   A 168 ? 0.3419 0.3419 0.3419 0.0000  0.0000  0.0000  165 GLN   A OE1   
1321 N  NE2   . GLN   A 168 ? 0.3419 0.3419 0.3419 0.0000  0.0000  0.0000  165 GLN   A NE2   
1322 N  N     . TYR   A 169 ? 0.2623 0.3800 0.1863 0.0767  0.0632  -0.0007 166 TYR   A N     
1323 C  CA    . TYR   A 169 ? 0.2873 0.4245 0.2754 0.0487  0.0121  -0.0215 166 TYR   A CA    
1324 C  C     . TYR   A 169 ? 0.3014 0.4518 0.2442 0.0228  0.0312  -0.0170 166 TYR   A C     
1325 O  O     . TYR   A 169 ? 0.3520 0.4426 0.2983 0.0475  -0.0326 -0.0076 166 TYR   A O     
1326 C  CB    . TYR   A 169 ? 0.2905 0.4249 0.2550 0.0517  0.0061  0.0021  166 TYR   A CB    
1327 C  CG    . TYR   A 169 ? 0.3514 0.4436 0.2712 0.0392  0.0547  -0.0184 166 TYR   A CG    
1328 C  CD1   . TYR   A 169 ? 0.3777 0.4470 0.2946 0.0453  0.0680  -0.0522 166 TYR   A CD1   
1329 C  CD2   . TYR   A 169 ? 0.4285 0.3477 0.3777 0.0056  -0.0237 -0.0096 166 TYR   A CD2   
1330 C  CE1   . TYR   A 169 ? 0.4994 0.4156 0.2972 0.0176  0.0146  -0.0233 166 TYR   A CE1   
1331 C  CE2   . TYR   A 169 ? 0.5346 0.3859 0.3584 0.0036  -0.0251 -0.0330 166 TYR   A CE2   
1332 C  CZ    . TYR   A 169 ? 0.4770 0.4132 0.4276 -0.0024 0.0482  -0.0641 166 TYR   A CZ    
1333 O  OH    . TYR   A 169 ? 0.5594 0.4551 0.4486 -0.0207 -0.0353 -0.0644 166 TYR   A OH    
1334 N  N     . ARG   A 170 ? 0.3074 0.4547 0.2468 0.0495  0.0454  0.0158  167 ARG   A N     
1335 C  CA    . ARG   A 170 ? 0.3263 0.4668 0.2665 0.0247  0.0271  0.0381  167 ARG   A CA    
1336 C  C     . ARG   A 170 ? 0.3130 0.4592 0.3213 0.0487  -0.0083 -0.0199 167 ARG   A C     
1337 O  O     . ARG   A 170 ? 0.3408 0.5762 0.4019 0.0420  -0.0250 -0.0344 167 ARG   A O     
1338 C  CB    . ARG   A 170 ? 0.3640 0.4788 0.2588 0.0111  0.0069  0.0315  167 ARG   A CB    
1339 C  CG    . ARG   A 170 ? 0.4074 0.4540 0.3404 0.0368  0.0402  -0.0079 167 ARG   A CG    
1340 C  CD    . ARG   A 170 ? 0.4112 0.4246 0.3365 0.0453  -0.0270 0.0142  167 ARG   A CD    
1341 N  NE    . ARG   A 170 ? 0.4229 0.4341 0.3446 0.0542  0.0082  0.0402  167 ARG   A NE    
1342 C  CZ    . ARG   A 170 ? 0.4971 0.3560 0.3553 0.0922  -0.0001 0.0333  167 ARG   A CZ    
1343 N  NH1   . ARG   A 170 ? 0.5597 0.5455 0.4092 0.0957  0.1096  -0.0359 167 ARG   A NH1   
1344 N  NH2   . ARG   A 170 ? 0.5044 0.3827 0.4616 0.0813  -0.0884 0.0913  167 ARG   A NH2   
1345 N  N     . LEU   A 171 ? 0.3542 0.4491 0.3744 0.1189  0.0525  0.0274  168 LEU   A N     
1346 C  CA    . LEU   A 171 ? 0.3802 0.5263 0.4226 0.1655  -0.0053 0.0230  168 LEU   A CA    
1347 C  C     . LEU   A 171 ? 0.4573 0.5316 0.3971 0.1826  0.0557  0.0785  168 LEU   A C     
1348 O  O     . LEU   A 171 ? 0.4786 0.6208 0.4454 0.1604  -0.0363 0.0788  168 LEU   A O     
1349 C  CB    . LEU   A 171 ? 0.5121 0.5573 0.5470 0.1261  0.0188  0.0002  168 LEU   A CB    
1350 C  CG    . LEU   A 171 ? 0.5554 0.4811 0.5821 0.1300  -0.0362 -0.0423 168 LEU   A CG    
1351 C  CD1   . LEU   A 171 ? 0.6242 0.4783 0.5667 0.0930  0.0076  0.0332  168 LEU   A CD1   
1352 C  CD2   . LEU   A 171 ? 0.5561 0.6257 0.5341 0.0976  0.0185  -0.0478 168 LEU   A CD2   
1353 N  N     . LYS   A 172 ? 0.4015 0.5898 0.3463 0.1588  0.0107  0.0038  169 LYS   A N     
1354 C  CA    . LYS   A 172 ? 0.4552 0.5711 0.3227 0.0977  -0.0199 0.0807  169 LYS   A CA    
1355 C  C     . LYS   A 172 ? 0.5495 0.5902 0.4776 -0.0031 -0.0698 0.0795  169 LYS   A C     
1356 O  O     . LYS   A 172 ? 0.6803 0.6019 0.4452 0.0214  -0.0271 0.1007  169 LYS   A O     
1357 C  CB    . LYS   A 172 ? 0.4259 0.6179 0.4081 0.0668  -0.0015 0.0082  169 LYS   A CB    
1358 C  CG    . LYS   A 172 ? 0.4259 0.5884 0.3461 0.0260  0.0768  0.0435  169 LYS   A CG    
1359 C  CD    . LYS   A 172 ? 0.4579 0.6036 0.3770 0.0716  0.0891  0.0223  169 LYS   A CD    
1360 C  CE    . LYS   A 172 ? 0.5921 0.5619 0.4796 0.0052  0.0448  -0.0284 169 LYS   A CE    
1361 N  NZ    . LYS   A 172 ? 0.7763 0.5720 0.4989 0.0271  0.0638  0.0363  169 LYS   A NZ    
1362 O  OXT   . LYS   A 172 ? 0.6046 0.6935 0.5661 -0.0631 0.0202  0.0804  169 LYS   A OXT   
1363 P  PG    . GNP   B .   ? 0.3161 0.2956 0.1970 0.0582  0.0529  -0.0092 201 GNP   A PG    
1364 O  O1G   . GNP   B .   ? 0.3165 0.2975 0.2319 -0.0119 0.0150  -0.0025 201 GNP   A O1G   
1365 O  O2G   . GNP   B .   ? 0.3618 0.3322 0.2190 0.0916  0.0748  -0.0259 201 GNP   A O2G   
1366 O  O3G   . GNP   B .   ? 0.4017 0.3412 0.1857 0.0046  0.0467  0.0088  201 GNP   A O3G   
1367 N  N3B   . GNP   B .   ? 0.2505 0.3260 0.1435 0.0057  0.0708  0.0281  201 GNP   A N3B   
1368 P  PB    . GNP   B .   ? 0.2533 0.3182 0.1714 0.0205  0.0385  -0.0033 201 GNP   A PB    
1369 O  O1B   . GNP   B .   ? 0.2514 0.3196 0.1379 0.0215  0.0447  0.0295  201 GNP   A O1B   
1370 O  O2B   . GNP   B .   ? 0.2373 0.3317 0.1850 0.0074  0.0594  0.0155  201 GNP   A O2B   
1371 O  O3A   . GNP   B .   ? 0.2826 0.4083 0.1426 0.0083  0.0924  -0.0105 201 GNP   A O3A   
1372 P  PA    . GNP   B .   ? 0.2850 0.3374 0.1769 0.0089  0.0194  -0.0078 201 GNP   A PA    
1373 O  O1A   . GNP   B .   ? 0.2604 0.3160 0.2457 0.0100  -0.0154 -0.0155 201 GNP   A O1A   
1374 O  O2A   . GNP   B .   ? 0.3586 0.3190 0.1323 -0.0055 -0.0015 -0.0190 201 GNP   A O2A   
1375 O  "O5'" . GNP   B .   ? 0.3136 0.4588 0.1404 0.0040  0.0138  -0.0495 201 GNP   A "O5'" 
1376 C  "C5'" . GNP   B .   ? 0.3150 0.4194 0.1797 0.0145  0.0184  -0.0323 201 GNP   A "C5'" 
1377 C  "C4'" . GNP   B .   ? 0.3138 0.4445 0.2083 0.0138  0.0240  -0.0314 201 GNP   A "C4'" 
1378 O  "O4'" . GNP   B .   ? 0.2545 0.4097 0.2260 0.0118  0.0141  -0.0510 201 GNP   A "O4'" 
1379 C  "C3'" . GNP   B .   ? 0.2707 0.4629 0.2188 -0.0385 -0.0137 -0.0147 201 GNP   A "C3'" 
1380 O  "O3'" . GNP   B .   ? 0.3094 0.5324 0.3021 0.0184  -0.0497 0.0220  201 GNP   A "O3'" 
1381 C  "C2'" . GNP   B .   ? 0.2842 0.4258 0.2553 -0.0455 -0.0450 0.0063  201 GNP   A "C2'" 
1382 O  "O2'" . GNP   B .   ? 0.4103 0.5591 0.1913 -0.0737 -0.0209 0.0078  201 GNP   A "O2'" 
1383 C  "C1'" . GNP   B .   ? 0.2112 0.4714 0.2427 -0.0209 0.0031  -0.0411 201 GNP   A "C1'" 
1384 N  N9    . GNP   B .   ? 0.2658 0.4308 0.1937 -0.0364 0.0064  -0.0148 201 GNP   A N9    
1385 C  C8    . GNP   B .   ? 0.2326 0.3974 0.2508 -0.0257 0.0467  -0.0031 201 GNP   A C8    
1386 N  N7    . GNP   B .   ? 0.2598 0.3938 0.2169 -0.0504 0.0286  -0.0404 201 GNP   A N7    
1387 C  C5    . GNP   B .   ? 0.2492 0.4576 0.2967 -0.0772 0.0183  0.0053  201 GNP   A C5    
1388 C  C6    . GNP   B .   ? 0.2379 0.4284 0.3166 -0.0343 -0.0015 -0.0223 201 GNP   A C6    
1389 O  O6    . GNP   B .   ? 0.2748 0.4155 0.1881 -0.0657 0.0399  -0.0045 201 GNP   A O6    
1390 N  N1    . GNP   B .   ? 0.2514 0.4893 0.2620 -0.0339 0.0007  0.0077  201 GNP   A N1    
1391 C  C2    . GNP   B .   ? 0.2774 0.4590 0.1894 -0.0485 -0.0100 0.0149  201 GNP   A C2    
1392 N  N2    . GNP   B .   ? 0.2885 0.6001 0.2266 -0.0925 0.0054  0.0377  201 GNP   A N2    
1393 N  N3    . GNP   B .   ? 0.2559 0.4560 0.2279 -0.0247 0.0215  0.0167  201 GNP   A N3    
1394 C  C4    . GNP   B .   ? 0.2786 0.4478 0.2377 -0.0617 0.0250  -0.0281 201 GNP   A C4    
1395 MG MG    . MG    C .   ? 0.2545 0.2825 0.1067 0.0277  0.0442  0.0239  202 MG    A MG    
1396 CO CO    . CO    D .   ? 0.3377 0.3367 0.2427 -0.0209 0.0980  -0.0189 203 CO    A CO    
1397 O  OAT   . A1IMB E .   ? 0.3583 0.2871 0.3053 0.0141  0.0315  0.0205  204 A1IMB A OAT   
1398 C  CAS   . A1IMB E .   ? 0.3590 0.3036 0.2509 0.0509  -0.0014 0.0190  204 A1IMB A CAS   
1399 C  CAM   . A1IMB E .   ? 0.3371 0.2643 0.2703 0.0203  0.0350  0.0238  204 A1IMB A CAM   
1400 C  CAN   . A1IMB E .   ? 0.2978 0.2403 0.2423 0.0122  0.0541  -0.0249 204 A1IMB A CAN   
1401 C  CAL   . A1IMB E .   ? 0.3273 0.2363 0.2377 -0.0037 0.0050  0.0102  204 A1IMB A CAL   
1402 O  OAR   . A1IMB E .   ? 0.2886 0.2458 0.2184 -0.0026 0.0323  -0.0093 204 A1IMB A OAR   
1403 C  CAK   . A1IMB E .   ? 0.2927 0.2262 0.2148 0.0165  0.0280  -0.0102 204 A1IMB A CAK   
1404 C  CAJ   . A1IMB E .   ? 0.3394 0.2359 0.2022 0.0302  -0.0169 0.0032  204 A1IMB A CAJ   
1405 C  CAI   . A1IMB E .   ? 0.3356 0.2629 0.2519 0.0078  -0.0004 -0.0165 204 A1IMB A CAI   
1406 S  SAH   . A1IMB E .   ? 0.3617 0.2674 0.2800 -0.0063 0.0087  -0.0083 204 A1IMB A SAH   
1407 O  OAP   . A1IMB E .   ? 0.4119 0.2497 0.3208 -0.0178 -0.0782 -0.0282 204 A1IMB A OAP   
1408 O  OAQ   . A1IMB E .   ? 0.4045 0.3907 0.2574 0.0040  0.0338  0.0055  204 A1IMB A OAQ   
1409 N  NAG   . A1IMB E .   ? 0.3045 0.2622 0.2519 0.0162  0.0232  0.0084  204 A1IMB A NAG   
1410 C  CAF   . A1IMB E .   ? 0.2969 0.2823 0.2492 -0.0359 0.0170  0.0286  204 A1IMB A CAF   
1411 S  SAO   . A1IMB E .   ? 0.2734 0.2995 0.2088 -0.0163 0.0522  0.0097  204 A1IMB A SAO   
1412 C  CAC   . A1IMB E .   ? 0.2812 0.2661 0.2700 0.0012  0.0576  0.0197  204 A1IMB A CAC   
1413 C  CAB   . A1IMB E .   ? 0.2458 0.3173 0.1744 0.0261  0.0839  0.0698  204 A1IMB A CAB   
1414 CL CLAA  . A1IMB E .   ? 0.3112 0.3165 0.1738 -0.0154 0.0582  0.0123  204 A1IMB A CLAA  
1415 C  CBJ   . A1IMB E .   ? 0.2877 0.3415 0.2335 0.0273  0.0498  0.0455  204 A1IMB A CBJ   
1416 C  CBK   . A1IMB E .   ? 0.2480 0.2713 0.2064 0.0178  0.0510  -0.0294 204 A1IMB A CBK   
1417 C  CBG   . A1IMB E .   ? 0.2779 0.3166 0.1744 0.0041  0.0951  0.0223  204 A1IMB A CBG   
1418 O  OBH   . A1IMB E .   ? 0.2999 0.3052 0.1623 0.0181  0.0306  0.0267  204 A1IMB A OBH   
1419 C  CAD   . A1IMB E .   ? 0.2547 0.2813 0.2570 0.0144  0.0282  0.0086  204 A1IMB A CAD   
1420 N  NAE   . A1IMB E .   ? 0.2638 0.3242 0.2170 -0.0114 0.0419  0.0438  204 A1IMB A NAE   
1421 C  CAU   . A1IMB E .   ? 0.3015 0.3308 0.2331 -0.0093 0.0701  0.0364  204 A1IMB A CAU   
1422 C  CAV   . A1IMB E .   ? 0.3172 0.2646 0.2335 -0.0245 0.0552  0.0474  204 A1IMB A CAV   
1423 C  CAW   . A1IMB E .   ? 0.3268 0.2618 0.2006 -0.0076 0.0397  0.0175  204 A1IMB A CAW   
1424 O  OBF   . A1IMB E .   ? 0.3238 0.2614 0.1982 0.0011  0.0583  0.0324  204 A1IMB A OBF   
1425 C  CAX   . A1IMB E .   ? 0.3177 0.2586 0.2233 -0.0418 -0.0009 0.0449  204 A1IMB A CAX   
1426 N  NAY   . A1IMB E .   ? 0.3099 0.2559 0.2331 -0.0294 0.0230  0.0439  204 A1IMB A NAY   
1427 C  CAZ   . A1IMB E .   ? 0.3272 0.2836 0.2560 0.0355  0.0281  0.0647  204 A1IMB A CAZ   
1428 C  CBA   . A1IMB E .   ? 0.3749 0.2776 0.2343 0.0310  0.0319  0.0252  204 A1IMB A CBA   
1429 C  CBB   . A1IMB E .   ? 0.4050 0.3180 0.2376 0.0288  0.0578  0.0381  204 A1IMB A CBB   
1430 C  CBC   . A1IMB E .   ? 0.4435 0.2350 0.1793 0.0204  0.0278  0.0845  204 A1IMB A CBC   
1431 N  NBI   . A1IMB E .   ? 0.4660 0.2677 0.2263 -0.0375 0.0274  0.0665  204 A1IMB A NBI   
1432 C  CBD   . A1IMB E .   ? 0.4313 0.2864 0.2404 0.0270  0.0297  0.0503  204 A1IMB A CBD   
1433 C  CBE   . A1IMB E .   ? 0.3738 0.2804 0.2091 0.0126  0.0163  0.0246  204 A1IMB A CBE   
1434 O  O     . HOH   F .   ? 0.4954 0.4401 0.4956 -0.0371 0.0177  0.0060  301 HOH   A O     
1435 O  O     . HOH   F .   ? 0.2748 0.3765 0.1664 -0.0003 0.0917  -0.0007 302 HOH   A O     
1436 O  O     . HOH   F .   ? 0.3699 0.3357 0.3268 0.0168  0.0858  -0.0822 303 HOH   A O     
1437 O  O     . HOH   F .   ? 0.4771 0.3021 0.1377 -0.0015 0.0301  0.0080  304 HOH   A O     
1438 O  O     . HOH   F .   ? 0.2650 0.2733 0.2394 0.0180  0.0703  -0.0563 305 HOH   A O     
1439 O  O     . HOH   F .   ? 0.5331 0.6414 0.3578 0.0159  0.0386  0.0659  306 HOH   A O     
1440 O  O     . HOH   F .   ? 0.5272 0.3839 0.5297 -0.0880 0.0765  0.0259  307 HOH   A O     
1441 O  O     . HOH   F .   ? 0.5045 0.4266 0.4990 -0.0690 -0.0104 0.0914  308 HOH   A O     
1442 O  O     . HOH   F .   ? 0.4631 0.3041 0.1970 -0.0099 0.0566  0.0162  309 HOH   A O     
1443 O  O     . HOH   F .   ? 0.2975 0.5558 0.5134 0.0268  -0.0020 -0.0018 310 HOH   A O     
1444 O  O     . HOH   F .   ? 0.4184 0.5983 0.2736 0.0966  0.0248  0.0244  311 HOH   A O     
1445 O  O     . HOH   F .   ? 0.4730 0.3970 0.4948 -0.0115 0.0123  0.0084  312 HOH   A O     
1446 O  O     . HOH   F .   ? 0.3225 0.2338 0.3504 0.0031  0.0878  -0.0173 313 HOH   A O     
1447 O  O     . HOH   F .   ? 0.3874 0.4097 0.3378 0.0661  0.0619  -0.0372 314 HOH   A O     
1448 O  O     . HOH   F .   ? 0.3800 0.3191 0.2003 0.0147  0.0814  0.0550  315 HOH   A O     
1449 O  O     . HOH   F .   ? 0.3862 0.4007 0.1865 -0.0612 0.0781  -0.0213 316 HOH   A O     
1450 O  O     . HOH   F .   ? 0.3300 0.4320 0.2297 0.0430  0.0103  -0.1011 317 HOH   A O     
1451 O  O     . HOH   F .   ? 0.3870 0.5285 0.4022 -0.0555 -0.0561 0.2322  318 HOH   A O     
1452 O  O     . HOH   F .   ? 0.3643 0.3796 0.2868 0.0306  0.0415  -0.0024 319 HOH   A O     
1453 O  O     . HOH   F .   ? 0.4660 0.4550 0.2619 0.0088  -0.0167 -0.0246 320 HOH   A O     
1454 O  O     . HOH   F .   ? 0.3456 0.5754 0.2498 0.0090  0.0274  -0.0173 321 HOH   A O     
1455 O  O     . HOH   F .   ? 0.4760 0.3214 0.4110 0.0270  -0.0145 0.0280  322 HOH   A O     
1456 O  O     . HOH   F .   ? 0.6102 0.5515 0.4534 -0.1217 0.0908  0.0241  323 HOH   A O     
1457 O  O     . HOH   F .   ? 0.4043 0.4636 0.3620 0.0146  0.0381  -0.0716 324 HOH   A O     
1458 O  O     . HOH   F .   ? 0.3972 0.4231 0.3367 0.0498  0.0630  -0.0420 325 HOH   A O     
1459 O  O     . HOH   F .   ? 0.2716 0.4305 0.2756 0.0160  0.0313  -0.0164 326 HOH   A O     
1460 O  O     . HOH   F .   ? 0.4034 0.3999 0.3396 0.0067  0.0258  0.0173  327 HOH   A O     
1461 O  O     . HOH   F .   ? 0.4503 0.7175 0.2924 -0.0222 0.0687  0.0176  328 HOH   A O     
1462 O  O     . HOH   F .   ? 0.4612 0.3874 0.2980 -0.0089 -0.0266 -0.0994 329 HOH   A O     
1463 O  O     . HOH   F .   ? 0.5456 0.3414 0.3366 0.0065  0.0188  -0.0184 330 HOH   A O     
1464 O  O     . HOH   F .   ? 0.4129 0.6391 0.2499 -0.0977 -0.0174 -0.0065 331 HOH   A O     
1465 O  O     . HOH   F .   ? 0.3185 0.3604 0.1208 -0.0021 0.0457  -0.0065 332 HOH   A O     
1466 O  O     . HOH   F .   ? 0.4047 0.6318 0.5980 0.0569  0.1078  0.0743  333 HOH   A O     
1467 O  O     . HOH   F .   ? 0.4287 0.2940 0.3280 -0.0044 0.1424  -0.0205 334 HOH   A O     
1468 O  O     . HOH   F .   ? 0.3244 0.2629 0.1598 -0.0082 0.0680  0.0469  335 HOH   A O     
1469 O  O     . HOH   F .   ? 0.7135 0.5373 0.4537 -0.0355 0.0830  -0.0237 336 HOH   A O     
1470 O  O     . HOH   F .   ? 0.2434 0.3237 0.1742 0.0194  0.0621  -0.0145 337 HOH   A O     
1471 O  O     . HOH   F .   ? 0.2628 0.3468 0.1629 0.0263  0.0283  0.0252  338 HOH   A O     
1472 O  O     . HOH   F .   ? 0.4227 0.5662 0.3809 0.0749  -0.0165 -0.0294 339 HOH   A O     
1473 O  O     . HOH   F .   ? 0.6025 0.3544 0.2077 -0.0788 0.0062  0.0014  340 HOH   A O     
1474 O  O     . HOH   F .   ? 0.4595 0.5232 0.2453 0.0033  0.0562  -0.0110 341 HOH   A O     
1475 O  O     . HOH   F .   ? 0.4144 0.3961 0.1943 -0.0081 0.0508  0.0722  342 HOH   A O     
1476 O  O     . HOH   F .   ? 0.3093 0.4327 0.2633 -0.0160 0.0595  0.0702  343 HOH   A O     
1477 O  O     . HOH   F .   ? 0.5001 0.4005 0.3326 -0.0140 0.0878  -0.0631 344 HOH   A O     
1478 O  O     . HOH   F .   ? 0.3245 0.3698 0.2667 -0.0110 -0.0119 -0.0131 345 HOH   A O     
1479 O  O     . HOH   F .   ? 0.4651 0.5531 0.3089 -0.0002 0.0890  -0.0645 346 HOH   A O     
1480 O  O     . HOH   F .   ? 0.4821 0.5618 0.3337 -0.0031 0.0162  -0.1250 347 HOH   A O     
1481 O  O     . HOH   F .   ? 0.5332 0.2889 0.2435 -0.0298 -0.0109 -0.0126 348 HOH   A O     
1482 O  O     . HOH   F .   ? 0.3262 0.3128 0.1782 0.0001  0.0403  -0.0062 349 HOH   A O     
1483 O  O     . HOH   F .   ? 0.5021 0.5641 0.2679 0.0553  0.0564  0.0512  350 HOH   A O     
1484 O  O     . HOH   F .   ? 0.5066 0.4113 0.3609 0.0689  0.0126  -0.0309 351 HOH   A O     
1485 O  O     . HOH   F .   ? 0.3200 0.4473 0.2352 0.0122  0.0153  -0.0181 352 HOH   A O     
1486 O  O     . HOH   F .   ? 0.5112 0.5753 0.2769 -0.0755 0.1280  0.1251  353 HOH   A O     
1487 O  O     . HOH   F .   ? 0.5314 0.8235 0.3421 0.2048  0.1816  -0.1324 354 HOH   A O     
1488 O  O     . HOH   F .   ? 0.4475 0.3797 0.3433 0.0932  0.0675  -0.0257 355 HOH   A O     
1489 O  O     . HOH   F .   ? 0.5370 0.4606 0.3561 -0.0338 0.0729  -0.0110 356 HOH   A O     
1490 O  O     . HOH   F .   ? 0.5140 0.4096 0.3657 -0.0211 0.0657  0.0686  357 HOH   A O     
1491 O  O     . HOH   F .   ? 0.3374 0.4203 0.2821 0.0300  0.0793  0.0039  358 HOH   A O     
1492 O  O     . HOH   F .   ? 0.3367 0.3318 0.2248 0.0136  0.0657  0.0809  359 HOH   A O     
1493 O  O     . HOH   F .   ? 0.4670 0.3908 0.3796 -0.0080 0.1076  0.0694  360 HOH   A O     
1494 O  O     . HOH   F .   ? 0.6357 0.5158 0.3612 -0.0545 -0.0897 -0.0194 361 HOH   A O     
1495 O  O     . HOH   F .   ? 0.4062 0.4115 0.4417 0.0635  -0.0110 0.0193  362 HOH   A O     
1496 O  O     . HOH   F .   ? 0.3693 0.4719 0.2669 0.0377  0.0103  -0.0264 363 HOH   A O     
1497 O  O     . HOH   F .   ? 0.5599 0.4724 0.3854 0.0896  0.0976  0.0096  364 HOH   A O     
1498 O  O     . HOH   F .   ? 0.3622 0.4465 0.3798 0.0104  -0.0294 -0.0550 365 HOH   A O     
1499 O  O     . HOH   F .   ? 0.3688 0.5349 0.3310 0.0314  0.1164  0.0344  366 HOH   A O     
1500 O  O     . HOH   F .   ? 0.3826 0.3681 0.2918 0.0274  0.0538  0.0307  367 HOH   A O     
1501 O  O     . HOH   F .   ? 0.3958 0.3896 0.1945 -0.0575 0.0838  -0.0509 368 HOH   A O     
1502 O  O     . HOH   F .   ? 0.3869 0.4062 0.2604 -0.0572 0.0909  0.0611  369 HOH   A O     
1503 O  O     . HOH   F .   ? 0.6148 0.5206 0.4189 -0.0583 -0.0305 0.1377  370 HOH   A O     
1504 O  O     . HOH   F .   ? 0.4074 0.5803 0.3602 -0.0549 -0.0181 0.0437  371 HOH   A O     
1505 O  O     . HOH   F .   ? 0.3917 0.3961 0.3000 -0.0261 0.0195  0.0400  372 HOH   A O     
1506 O  O     . HOH   F .   ? 0.3871 0.5995 0.4071 0.0764  0.1075  0.0177  373 HOH   A O     
1507 O  O     . HOH   F .   ? 0.4212 0.5843 0.2676 -0.0130 0.0113  0.0134  374 HOH   A O     
1508 O  O     . HOH   F .   ? 0.4616 0.5490 0.4048 -0.0576 -0.0033 0.0296  375 HOH   A O     
1509 O  O     . HOH   F .   ? 0.4054 0.4178 0.1730 0.1029  0.0774  0.0213  376 HOH   A O     
1510 O  O     . HOH   F .   ? 0.4270 0.3147 0.2336 0.0090  0.0718  -0.0250 377 HOH   A O     
1511 O  O     . HOH   F .   ? 0.5686 0.5198 0.2937 0.0183  0.0294  0.0562  378 HOH   A O     
1512 O  O     . HOH   F .   ? 0.5215 0.3683 0.3560 -0.0075 -0.0473 -0.1181 379 HOH   A O     
1513 O  O     . HOH   F .   ? 0.4571 0.4269 0.3460 -0.0406 0.0754  -0.0056 380 HOH   A O     
1514 O  O     . HOH   F .   ? 0.4918 0.3714 0.3506 -0.1194 0.0288  0.0740  381 HOH   A O     
1515 O  O     . HOH   F .   ? 0.4157 0.4953 0.3369 -0.0532 0.0204  -0.0117 382 HOH   A O     
1516 O  O     . HOH   F .   ? 0.3114 0.3343 0.2930 0.0068  0.0095  -0.0318 383 HOH   A O     
1517 O  O     . HOH   F .   ? 0.4286 0.4389 0.3437 0.1554  0.0150  0.0067  384 HOH   A O     
1518 O  O     . HOH   F .   ? 0.4526 0.3465 0.5407 -0.0312 -0.0693 -0.0060 385 HOH   A O     
1519 O  O     . HOH   F .   ? 0.5738 0.4276 0.5261 -0.0121 0.0472  0.0599  386 HOH   A O     
1520 O  O     . HOH   F .   ? 0.4652 0.5106 0.4628 -0.1054 0.0245  0.0591  387 HOH   A O     
1521 O  O     . HOH   F .   ? 0.3946 0.4778 0.2897 -0.0320 0.1073  0.0104  388 HOH   A O     
1522 O  O     . HOH   F .   ? 0.4969 0.5420 0.4545 -0.0610 0.0122  0.1073  389 HOH   A O     
1523 O  O     . HOH   F .   ? 0.3823 0.2599 0.2302 0.0054  0.0356  -0.0089 390 HOH   A O     
1524 O  O     . HOH   F .   ? 0.3738 0.4162 0.3733 0.0325  -0.0243 0.0458  391 HOH   A O     
1525 O  O     . HOH   F .   ? 0.3790 0.4518 0.5018 0.0463  0.0920  -0.0466 392 HOH   A O     
1526 O  O     . HOH   F .   ? 0.4219 0.4204 0.2868 -0.0647 -0.0080 0.0344  393 HOH   A O     
1527 O  O     . HOH   F .   ? 0.4132 0.4833 0.2894 -0.0951 -0.0141 -0.0315 394 HOH   A O     
1528 O  O     . HOH   F .   ? 0.5264 0.5246 0.3290 -0.0450 0.1079  0.0678  395 HOH   A O     
1529 O  O     . HOH   F .   ? 0.5012 0.5465 0.4533 -0.0038 0.1823  -0.0161 396 HOH   A O     
1530 O  O     . HOH   F .   ? 0.4027 0.3478 0.3758 0.0356  -0.0039 -0.0193 397 HOH   A O     
1531 O  O     . HOH   F .   ? 0.5691 0.4955 0.2932 -0.1001 0.0376  -0.0315 398 HOH   A O     
1532 O  O     . HOH   F .   ? 0.5374 0.4695 0.3419 -0.0626 -0.0346 0.0285  399 HOH   A O     
1533 O  O     . HOH   F .   ? 0.6461 0.4158 0.4021 -0.0156 0.0250  0.0043  400 HOH   A O     
1534 O  O     . HOH   F .   ? 0.5435 0.3549 0.5881 0.0667  -0.0577 -0.0113 401 HOH   A O     
1535 O  O     . HOH   F .   ? 0.4893 0.4621 0.3542 0.0035  -0.0587 0.0833  402 HOH   A O     
1536 O  O     . HOH   F .   ? 0.3804 0.5553 0.2142 0.0322  0.0263  -0.0262 403 HOH   A O     
1537 O  O     . HOH   F .   ? 0.5379 0.4038 0.3480 -0.0493 0.0482  0.0691  404 HOH   A O     
1538 O  O     . HOH   F .   ? 0.3707 0.5798 0.4139 0.0333  0.0967  -0.0710 405 HOH   A O     
1539 O  O     . HOH   F .   ? 0.4260 0.5435 0.3640 -0.0298 0.0582  0.0248  406 HOH   A O     
1540 O  O     . HOH   F .   ? 0.4198 0.4817 0.5423 -0.0196 -0.0250 0.0207  407 HOH   A O     
1541 O  O     . HOH   F .   ? 0.4020 0.4565 0.4169 0.0386  0.1857  -0.0884 408 HOH   A O     
1542 O  O     . HOH   F .   ? 0.6260 0.3662 0.6033 0.0230  0.1500  -0.0574 409 HOH   A O     
1543 O  O     . HOH   F .   ? 0.5628 0.3994 0.3319 -0.0288 0.0285  0.0272  410 HOH   A O     
1544 O  O     . HOH   F .   ? 0.3998 0.5100 0.4060 -0.0436 -0.0073 0.0852  411 HOH   A O     
1545 O  O     . HOH   F .   ? 0.5764 0.5771 0.3142 -0.0704 -0.0187 -0.0478 412 HOH   A O     
1546 O  O     . HOH   F .   ? 0.5580 0.4797 0.3411 0.0481  0.0642  -0.0502 413 HOH   A O     
1547 O  O     . HOH   F .   ? 0.4559 0.4806 0.3856 0.0507  0.0720  0.0222  414 HOH   A O     
1548 O  O     . HOH   F .   ? 0.4576 0.5446 0.2639 0.0351  -0.0024 0.0252  415 HOH   A O     
1549 O  O     . HOH   F .   ? 0.3831 0.4249 0.3498 -0.0783 0.0102  0.0748  416 HOH   A O     
1550 O  O     . HOH   F .   ? 0.3512 0.4761 0.2632 -0.0374 0.0418  0.0086  417 HOH   A O     
1551 O  O     . HOH   F .   ? 0.4810 0.5584 0.3829 -0.0265 -0.0019 -0.1621 418 HOH   A O     
# 
