data_9GGZ
# 
_entry.id   9GGZ 
# 
_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   9GGZ         pdb_00009ggz 10.2210/pdb9ggz/pdb 
WWPDB D_1292140423 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-04-16 
_pdbx_audit_revision_history.part_number         ? 
# 
_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_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9GGZ 
_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 . 9GH0 unspecified 
PDB . 9GH1 unspecified 
PDB . 9GGW unspecified 
PDB . 9GGX 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            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_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  0000-0003-0401-2693 
primary 'Pellicano, F.'      2  ?                   
primary 'Schuttelkopf, A.W.' 3  0000-0002-9424-8730 
primary 'Beyer, K.S.'        4  0000-0002-3047-304X 
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 0000-0002-6673-9508 
primary 'Davies, K.'         11 ?                   
primary 'Drysdale, M.J.'     12 ?                   
primary 'Engelman, J.'       13 ?                   
primary 'Estevan-Barber, A.' 14 ?                   
primary 'Gohlke, A.'         15 0000-0002-5447-5453 
primary 'Gray, C.H.'         16 ?                   
primary 'Guthy, D.A.'        17 ?                   
primary 'Hong, M.'           18 ?                   
primary 'Hopkins, A.'        19 0009-0003-0675-2385 
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 0000-0002-3391-1228 
primary 'Pasquali, C.C.'     28 0009-0008-1322-2549 
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 0000-0003-1876-8774 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'GTPase KRas' 19607.078 1  3.6.5.2 C118S ? ? 
2 non-polymer syn 'PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER' 522.196   1  ?       ?     ? ? 
3 non-polymer syn 'MAGNESIUM ION' 24.305    1  ?       ?     ? ? 
4 non-polymer syn 'COBALT (II) ION' 58.933    2  ?       ?     ? ? 
5 non-polymer syn 
;(3Z)-18-(4-aminocyclohexyl)-7-chloro-10-hydroxy-2,2-dioxo-21-[[(3S)-pyrrolidin-3-yl]amino]-2-lambda-6,5-dithia-3,12,18,22-tetrazatetracyclo[18.3.1.04,12.06,11]tetracosa-1(23),3,6,8,10,20(24),21-heptaen-19-one
;
634.213   1  ?       ?     ? ? 
6 water       nat water 18.015    77 ?       ?     ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'K-Ras 2,Ki-Ras,c-K-ras,c-Ki-ras' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;GGSMTEYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEG
FLCVFAINNTKSFEDIHHYREQIKRVKDSEDVPMVLVGNKSDLPSRTVDTKQAQDLARSYGIPFIETSAKTRQRVEDAFY
TLVREIRQYRLK
;
_entity_poly.pdbx_seq_one_letter_code_can   
;GGSMTEYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEG
FLCVFAINNTKSFEDIHHYREQIKRVKDSEDVPMVLVGNKSDLPSRTVDTKQAQDLARSYGIPFIETSAKTRQRVEDAFY
TLVREIRQYRLK
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER' GNP   
3 'MAGNESIUM ION' MG    
4 'COBALT (II) ION' CO    
5 
;(3Z)-18-(4-aminocyclohexyl)-7-chloro-10-hydroxy-2,2-dioxo-21-[[(3S)-pyrrolidin-3-yl]amino]-2-lambda-6,5-dithia-3,12,18,22-tetrazatetracyclo[18.3.1.04,12.06,11]tetracosa-1(23),3,6,8,10,20(24),21-heptaen-19-one
;
A1IK8 
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 
A1IK8 non-polymer         . 
;(3Z)-18-(4-aminocyclohexyl)-7-chloro-10-hydroxy-2,2-dioxo-21-[[(3S)-pyrrolidin-3-yl]amino]-2-lambda-6,5-dithia-3,12,18,22-tetrazatetracyclo[18.3.1.04,12.06,11]tetracosa-1(23),3,6,8,10,20(24),21-heptaen-19-one
;
? 'C28 H36 Cl N7 O4 S2' 634.213 
ALA   'L-peptide linking' y ALANINE ? 'C3 H7 N O2'          89.093  
ARG   'L-peptide linking' y ARGININE ? 'C6 H15 N4 O2 1'      175.209 
ASN   'L-peptide linking' y ASPARAGINE ? 'C4 H8 N2 O3'         132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'          133.103 
CO    non-polymer         . 'COBALT (II) ION' ? 'Co 2'                58.933  
CYS   'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S'        121.158 
GLN   'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3'        146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'          147.129 
GLY   'peptide linking'   y GLYCINE ? 'C2 H5 N O2'          75.067  
GNP   non-polymer         . 'PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER' ? 'C10 H17 N6 O13 P3'   522.196 
HIS   'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1'      156.162 
HOH   non-polymer         . WATER ? 'H2 O'                18.015  
ILE   'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2'         131.173 
LEU   'L-peptide linking' y LEUCINE ? 'C6 H13 N O2'         131.173 
LYS   'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1'      147.195 
MET   'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S'       149.211 
MG    non-polymer         . 'MAGNESIUM ION' ? 'Mg 2'                24.305  
PHE   'L-peptide linking' y PHENYLALANINE ? 'C9 H11 N O2'         165.189 
PRO   'L-peptide linking' y PROLINE ? 'C5 H9 N O2'          115.130 
SER   'L-peptide linking' y SERINE ? 'C3 H7 N O3'          105.093 
THR   'L-peptide linking' y THREONINE ? 'C4 H9 N O3'          119.119 
TYR   'L-peptide linking' y TYROSINE ? 'C9 H11 N O3'         181.189 
VAL   'L-peptide linking' y VALINE ? 'C5 H11 N O2'         117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   GLY 1   -2  ?   ?   ?   A . n 
A 1 2   GLY 2   -1  ?   ?   ?   A . n 
A 1 3   SER 3   0   ?   ?   ?   A . n 
A 1 4   MET 4   1   1   MET MET A . n 
A 1 5   THR 5   2   2   THR THR A . n 
A 1 6   GLU 6   3   3   GLU GLU A . n 
A 1 7   TYR 7   4   4   TYR TYR A . n 
A 1 8   LYS 8   5   5   LYS LYS A . n 
A 1 9   LEU 9   6   6   LEU LEU A . n 
A 1 10  VAL 10  7   7   VAL VAL A . n 
A 1 11  VAL 11  8   8   VAL VAL A . n 
A 1 12  VAL 12  9   9   VAL VAL A . n 
A 1 13  GLY 13  10  10  GLY GLY A . n 
A 1 14  ALA 14  11  11  ALA ALA A . n 
A 1 15  GLY 15  12  12  GLY GLY A . n 
A 1 16  GLY 16  13  13  GLY GLY A . n 
A 1 17  VAL 17  14  14  VAL VAL A . n 
A 1 18  GLY 18  15  15  GLY GLY A . n 
A 1 19  LYS 19  16  16  LYS LYS A . n 
A 1 20  SER 20  17  17  SER SER A . n 
A 1 21  ALA 21  18  18  ALA ALA A . n 
A 1 22  LEU 22  19  19  LEU LEU A . n 
A 1 23  THR 23  20  20  THR THR A . n 
A 1 24  ILE 24  21  21  ILE ILE A . n 
A 1 25  GLN 25  22  22  GLN GLN A . n 
A 1 26  LEU 26  23  23  LEU LEU A . n 
A 1 27  ILE 27  24  24  ILE ILE A . n 
A 1 28  GLN 28  25  25  GLN GLN A . n 
A 1 29  ASN 29  26  26  ASN ASN A . n 
A 1 30  HIS 30  27  27  HIS HIS A . n 
A 1 31  PHE 31  28  28  PHE PHE A . n 
A 1 32  VAL 32  29  29  VAL VAL A . n 
A 1 33  ASP 33  30  30  ASP ASP A . n 
A 1 34  GLU 34  31  ?   ?   ?   A . n 
A 1 35  TYR 35  32  ?   ?   ?   A . n 
A 1 36  ASP 36  33  ?   ?   ?   A . n 
A 1 37  PRO 37  34  ?   ?   ?   A . n 
A 1 38  THR 38  35  ?   ?   ?   A . n 
A 1 39  ILE 39  36  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  ?   ?   ?   A . n 
A 1 65  GLU 65  62  ?   ?   ?   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        A1IK8 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1IK8 
_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 1    CO    CO  A . 
E 4 CO    1  204 2    CO    CO  A . 
F 5 A1IK8 1  205 1    A1IK8 DRG A . 
G 6 HOH   1  301 1    HOH   HOH A . 
G 6 HOH   2  302 130  HOH   HOH A . 
G 6 HOH   3  303 198  HOH   HOH A . 
G 6 HOH   4  304 173  HOH   HOH A . 
G 6 HOH   5  305 133  HOH   HOH A . 
G 6 HOH   6  306 227  HOH   HOH A . 
G 6 HOH   7  307 137  HOH   HOH A . 
G 6 HOH   8  308 228  HOH   HOH A . 
G 6 HOH   9  309 120  HOH   HOH A . 
G 6 HOH   10 310 64   HOH   HOH A . 
G 6 HOH   11 311 209  HOH   HOH A . 
G 6 HOH   12 312 9    HOH   HOH A . 
G 6 HOH   13 313 78   HOH   HOH A . 
G 6 HOH   14 314 28   HOH   HOH A . 
G 6 HOH   15 315 125  HOH   HOH A . 
G 6 HOH   16 316 50   HOH   HOH A . 
G 6 HOH   17 317 13   HOH   HOH A . 
G 6 HOH   18 318 163  HOH   HOH A . 
G 6 HOH   19 319 4    HOH   HOH A . 
G 6 HOH   20 320 112  HOH   HOH A . 
G 6 HOH   21 321 211  HOH   HOH A . 
G 6 HOH   22 322 2    HOH   HOH A . 
G 6 HOH   23 323 165  HOH   HOH A . 
G 6 HOH   24 324 182  HOH   HOH A . 
G 6 HOH   25 325 102  HOH   HOH A . 
G 6 HOH   26 326 5    HOH   HOH A . 
G 6 HOH   27 327 42   HOH   HOH A . 
G 6 HOH   28 328 131  HOH   HOH A . 
G 6 HOH   29 329 187  HOH   HOH A . 
G 6 HOH   30 330 61   HOH   HOH A . 
G 6 HOH   31 331 26   HOH   HOH A . 
G 6 HOH   32 332 169  HOH   HOH A . 
G 6 HOH   33 333 226  HOH   HOH A . 
G 6 HOH   34 334 3    HOH   HOH A . 
G 6 HOH   35 335 179  HOH   HOH A . 
G 6 HOH   36 336 87   HOH   HOH A . 
G 6 HOH   37 337 126  HOH   HOH A . 
G 6 HOH   38 338 122  HOH   HOH A . 
G 6 HOH   39 339 144  HOH   HOH A . 
G 6 HOH   40 340 22   HOH   HOH A . 
G 6 HOH   41 341 135  HOH   HOH A . 
G 6 HOH   42 342 177  HOH   HOH A . 
G 6 HOH   43 343 138  HOH   HOH A . 
G 6 HOH   44 344 53   HOH   HOH A . 
G 6 HOH   45 345 224  HOH   HOH A . 
G 6 HOH   46 346 206  HOH   HOH A . 
G 6 HOH   47 347 175  HOH   HOH A . 
G 6 HOH   48 348 151  HOH   HOH A . 
G 6 HOH   49 349 109  HOH   HOH A . 
G 6 HOH   50 350 146  HOH   HOH A . 
G 6 HOH   51 351 100  HOH   HOH A . 
G 6 HOH   52 352 128  HOH   HOH A . 
G 6 HOH   53 353 30   HOH   HOH A . 
G 6 HOH   54 354 229  HOH   HOH A . 
G 6 HOH   55 355 210  HOH   HOH A . 
G 6 HOH   56 356 80   HOH   HOH A . 
G 6 HOH   57 357 136  HOH   HOH A . 
G 6 HOH   58 358 214  HOH   HOH A . 
G 6 HOH   59 359 45   HOH   HOH A . 
G 6 HOH   60 360 81   HOH   HOH A . 
G 6 HOH   61 361 160  HOH   HOH A . 
G 6 HOH   62 362 57   HOH   HOH A . 
G 6 HOH   63 363 225  HOH   HOH A . 
G 6 HOH   64 364 132  HOH   HOH A . 
G 6 HOH   65 365 142  HOH   HOH A . 
G 6 HOH   66 366 134  HOH   HOH A . 
G 6 HOH   67 367 157  HOH   HOH A . 
G 6 HOH   68 368 143  HOH   HOH A . 
G 6 HOH   69 369 127  HOH   HOH A . 
G 6 HOH   70 370 145  HOH   HOH A . 
G 6 HOH   71 371 217  HOH   HOH A . 
G 6 HOH   72 372 121  HOH   HOH A . 
G 6 HOH   73 373 201  HOH   HOH A . 
G 6 HOH   74 374 220  HOH   HOH A . 
G 6 HOH   75 375 215  HOH   HOH A . 
G 6 HOH   76 376 216  HOH   HOH A . 
G 6 HOH   77 377 221  HOH   HOH A . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement        ? ? ? ? ? ? ? ? ? ? ? REFMAC      ? ? ? 5.8.0258 1 
? 'data scaling'    ? ? ? ? ? ? ? ? ? ? ? Aimless     ? ? ? 0.7.4    2 
? 'data extraction' ? ? ? ? ? ? ? ? ? ? ? PDB_EXTRACT ? ? ? 3.22     3 
? 'data reduction'  ? ? ? ? ? ? ? ? ? ? ? XDS         ? ? ? .        4 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   108.630 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9GGZ 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     72.254 
_cell.length_a_esd                 ? 
_cell.length_b                     34.866 
_cell.length_b_esd                 ? 
_cell.length_c                     69.575 
_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                         9GGZ 
_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                   9GGZ 
_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             2.12 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          41.92 
_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               0.080 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              7.5 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '24% PEG 3350, 100 mM MgCl2, 10 mM CoCl2, 100 mM HEPES' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            292 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2020-12-11 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.9795 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'DIAMOND BEAMLINE I04' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9795 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   I04 
_diffrn_source.pdbx_synchrotron_site       Diamond 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9GGZ 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.370 
_reflns.d_resolution_low                               28.780 
_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                                     34572 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.400 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                3.400 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          19.400 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.036 
_reflns.pdbx_Rpim_I_all                                0.020 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       116020 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   1.000 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.031 
_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 
1.370 1.410  ? ? ? ? ? ? 2485 ? ? ? ? ? ? ? ? ? ? ? 3.300 ? ? ? 0.729 0.394 ? 1 1 0.828 ? ? 96.000 ? 0.610 ? ? ? ? ? ? ? ? ? 
6.130 28.780 ? ? ? ? ? ? 417  ? ? ? ? ? ? ? ? ? ? ? 3.200 ? ? ? 0.019 0.011 ? 2 1 1.000 ? ? 97.800 ? 0.016 ? ? ? ? ? ? ? ? ? 
# 
_refine.aniso_B[1][1]                            -0.3700 
_refine.aniso_B[1][2]                            0.0000 
_refine.aniso_B[1][3]                            -0.3100 
_refine.aniso_B[2][2]                            1.7600 
_refine.aniso_B[2][3]                            0.0000 
_refine.aniso_B[3][3]                            -0.9600 
_refine.B_iso_max                                65.410 
_refine.B_iso_mean                               23.2370 
_refine.B_iso_min                                13.570 
_refine.correlation_coeff_Fo_to_Fc               0.9720 
_refine.correlation_coeff_Fo_to_Fc_free          0.9550 
_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                                 9GGZ 
_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                            1.3700 
_refine.ls_d_res_low                             28.7800 
_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                     32779 
_refine.ls_number_reflns_R_free                  1711 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.1500 
_refine.ls_percent_reflns_R_free                 5.0000 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1797 
_refine.ls_R_factor_R_free                       0.2311 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1771 
_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                       0.0680 
_refine.pdbx_overall_ESU_R_Free                  0.0680 
_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                             3.8910 
_refine.overall_SU_ML                            0.0660 
_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                       1.3700 
_refine_hist.d_res_low                        28.7800 
_refine_hist.number_atoms_solvent             77 
_refine_hist.number_atoms_total               1455 
_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       162 
_refine_hist.pdbx_B_iso_mean_ligand           25.75 
_refine_hist.pdbx_B_iso_mean_solvent          30.89 
_refine_hist.pdbx_number_atoms_protein        1301 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         77 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.022  0.013  1406 ? r_bond_refined_d       ? ? 
'X-RAY DIFFRACTION' ? 0.034  0.018  1296 ? r_bond_other_d         ? ? 
'X-RAY DIFFRACTION' ? 2.289  1.709  1907 ? r_angle_refined_deg    ? ? 
'X-RAY DIFFRACTION' ? 2.438  1.644  3004 ? r_angle_other_deg      ? ? 
'X-RAY DIFFRACTION' ? 4.159  5.000  161  ? r_dihedral_angle_1_deg ? ? 
'X-RAY DIFFRACTION' ? 32.605 21.667 78   ? r_dihedral_angle_2_deg ? ? 
'X-RAY DIFFRACTION' ? 13.601 15.000 246  ? r_dihedral_angle_3_deg ? ? 
'X-RAY DIFFRACTION' ? 17.791 15.000 12   ? r_dihedral_angle_4_deg ? ? 
'X-RAY DIFFRACTION' ? 0.131  0.200  185  ? r_chiral_restr         ? ? 
'X-RAY DIFFRACTION' ? 0.012  0.020  1531 ? r_gen_planes_refined   ? ? 
'X-RAY DIFFRACTION' ? 0.022  0.020  293  ? r_gen_planes_other     ? ? 
'X-RAY DIFFRACTION' ? 2.835  2.230  650  ? r_mcbond_it            ? ? 
'X-RAY DIFFRACTION' ? 2.833  2.227  649  ? r_mcbond_other         ? ? 
'X-RAY DIFFRACTION' ? 3.192  3.325  809  ? r_mcangle_it           ? ? 
'X-RAY DIFFRACTION' ? 3.127  3.000  2702 ? r_rigid_bond_restr     ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.3710 
_refine_ls_shell.d_res_low                        1.4070 
_refine_ls_shell.number_reflns_all                2490 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             120 
_refine_ls_shell.number_reflns_R_work             2370 
_refine_ls_shell.percent_reflns_obs               96.6600 
_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                  0.3100 
_refine_ls_shell.redundancy_reflns_all            ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.wR_factor_all                    ? 
_refine_ls_shell.wR_factor_obs                    ? 
_refine_ls_shell.wR_factor_R_free                 ? 
_refine_ls_shell.wR_factor_R_work                 ? 
_refine_ls_shell.pdbx_R_complete                  ? 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.pdbx_phase_error                 ? 
_refine_ls_shell.pdbx_fsc_work                    ? 
_refine_ls_shell.pdbx_fsc_free                    ? 
_refine_ls_shell.R_factor_R_free                  0.3170 
# 
_struct.entry_id                     9GGZ 
_struct.title                        'Human KRas4A (GMPPNP) in complex with compound 31' 
_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        9GGZ 
_struct_keywords.text            'RAS, GTPase, inhibitor, CELL CYCLE' 
_struct_keywords.pdbx_keywords   'CELL CYCLE' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 4 ? 
F N N 5 ? 
G N N 6 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    RASK_HUMAN 
_struct_ref.pdbx_db_accession          P01116 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MTEYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLC
VFAINNTKSFEDIHHYREQIKRVKDSEDVPMVLVGNKCDLPSRTVDTKQAQDLARSYGIPFIETSAKTRQRVEDAFYTLV
REIRQYRLK
;
_struct_ref.pdbx_align_begin           1 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9GGZ 
_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 9GGZ GLY A 1   ? UNP P01116 ?   ?   'expression tag'      -2  1 
1 9GGZ GLY A 2   ? UNP P01116 ?   ?   'expression tag'      -1  2 
1 9GGZ SER A 3   ? UNP P01116 ?   ?   'expression tag'      0   3 
1 9GGZ SER A 121 ? UNP P01116 CYS 118 'engineered mutation' 118 4 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 1900 ? 
1 MORE         -31  ? 
1 'SSA (A^2)'  8170 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 GLY A 18  ? ASN A 29  ? GLY A 15  ASN A 26  1 ? 12 
HELX_P HELX_P2 AA2 TYR A 67  ? GLY A 78  ? TYR A 64  GLY A 75  1 ? 12 
HELX_P HELX_P3 AA3 ASN A 89  ? ASP A 108 ? ASN A 86  ASP A 105 1 ? 20 
HELX_P HELX_P4 AA4 ASP A 129 ? GLY A 141 ? ASP A 126 GLY A 138 1 ? 13 
HELX_P HELX_P5 AA5 ARG A 154 ? LEU A 171 ? ARG A 151 LEU A 168 1 ? 18 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1  metalc ? ? A SER 20  OG  ? ? ? 1_555 C MG  . MG ? ? A SER 17  A MG  202 1_555 ? ? ? ? ? ? ? 2.179 ? ? 
metalc2  metalc ? ? A HIS 30  NE2 ? ? ? 1_555 D CO  . CO ? ? A HIS 27  A CO  203 1_555 ? ? ? ? ? ? ? 2.279 ? ? 
metalc3  metalc ? ? A HIS 97  NE2 ? ? ? 1_555 E CO  . CO ? ? A HIS 94  A CO  204 1_555 ? ? ? ? ? ? ? 2.297 ? ? 
metalc4  metalc ? ? A HIS 98  NE2 ? ? ? 1_555 E CO  . CO ? ? A HIS 95  A CO  204 2_655 ? ? ? ? ? ? ? 2.033 ? ? 
metalc5  metalc ? ? A GLU 101 OE1 ? ? ? 1_555 E CO  . CO ? ? A GLU 98  A CO  204 1_555 ? ? ? ? ? ? ? 2.064 ? ? 
metalc6  metalc ? ? B GNP .   O1G ? ? ? 1_555 C MG  . MG ? ? A GNP 201 A MG  202 1_555 ? ? ? ? ? ? ? 2.199 ? ? 
metalc7  metalc ? ? B GNP .   O2B ? ? ? 1_555 C MG  . MG ? ? A GNP 201 A MG  202 1_555 ? ? ? ? ? ? ? 2.175 ? ? 
metalc8  metalc ? ? C MG  .   MG  ? ? ? 1_555 G HOH . O  ? ? A MG  202 A HOH 311 1_555 ? ? ? ? ? ? ? 2.065 ? ? 
metalc9  metalc ? ? C MG  .   MG  ? ? ? 1_555 G HOH . O  ? ? A MG  202 A HOH 316 1_555 ? ? ? ? ? ? ? 2.018 ? ? 
metalc10 metalc ? ? C MG  .   MG  ? ? ? 1_555 G HOH . O  ? ? A MG  202 A HOH 346 1_555 ? ? ? ? ? ? ? 2.118 ? ? 
metalc11 metalc ? ? E CO  .   CO  ? ? ? 1_555 G HOH . O  ? ? A CO  204 A HOH 315 1_555 ? ? ? ? ? ? ? 2.204 ? ? 
metalc12 metalc ? ? E CO  .   CO  ? ? ? 1_555 G HOH . O  ? ? A CO  204 A HOH 317 1_555 ? ? ? ? ? ? ? 2.195 ? ? 
metalc13 metalc ? ? E CO  .   CO  ? ? ? 1_555 G HOH . O  ? ? A CO  204 A HOH 358 1_555 ? ? ? ? ? ? ? 2.150 ? ? 
# 
_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_555 173.6 ? 
2  OG  ? A SER 20  ? A SER 17  ? 1_555 MG ? C MG . ? A MG 202 ? 1_555 O2B ? B GNP .   ? A GNP 201 ? 1_555 88.4  ? 
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 92.6  ? 
4  OG  ? A SER 20  ? A SER 17  ? 1_555 MG ? C MG . ? A MG 202 ? 1_555 O   ? G HOH .   ? A HOH 311 ? 1_555 87.6  ? 
5  O1G ? B GNP .   ? A GNP 201 ? 1_555 MG ? C MG . ? A MG 202 ? 1_555 O   ? G HOH .   ? A HOH 311 ? 1_555 91.9  ? 
6  O2B ? B GNP .   ? A GNP 201 ? 1_555 MG ? C MG . ? A MG 202 ? 1_555 O   ? G HOH .   ? A HOH 311 ? 1_555 173.6 ? 
7  OG  ? A SER 20  ? A SER 17  ? 1_555 MG ? C MG . ? A MG 202 ? 1_555 O   ? G HOH .   ? A HOH 316 ? 1_555 83.1  ? 
8  O1G ? B GNP .   ? A GNP 201 ? 1_555 MG ? C MG . ? A MG 202 ? 1_555 O   ? G HOH .   ? A HOH 316 ? 1_555 90.6  ? 
9  O2B ? B GNP .   ? A GNP 201 ? 1_555 MG ? C MG . ? A MG 202 ? 1_555 O   ? G HOH .   ? A HOH 316 ? 1_555 90.2  ? 
10 O   ? G HOH .   ? A HOH 311 ? 1_555 MG ? C MG . ? A MG 202 ? 1_555 O   ? G HOH .   ? A HOH 316 ? 1_555 94.3  ? 
11 OG  ? A SER 20  ? A SER 17  ? 1_555 MG ? C MG . ? A MG 202 ? 1_555 O   ? G HOH .   ? A HOH 346 ? 1_555 88.0  ? 
12 O1G ? B GNP .   ? A GNP 201 ? 1_555 MG ? C MG . ? A MG 202 ? 1_555 O   ? G HOH .   ? A HOH 346 ? 1_555 98.3  ? 
13 O2B ? B GNP .   ? A GNP 201 ? 1_555 MG ? C MG . ? A MG 202 ? 1_555 O   ? G HOH .   ? A HOH 346 ? 1_555 90.3  ? 
14 O   ? G HOH .   ? A HOH 311 ? 1_555 MG ? C MG . ? A MG 202 ? 1_555 O   ? G HOH .   ? A HOH 346 ? 1_555 84.5  ? 
15 O   ? G HOH .   ? A HOH 316 ? 1_555 MG ? C MG . ? A MG 202 ? 1_555 O   ? G HOH .   ? A HOH 346 ? 1_555 171.0 ? 
16 NE2 ? A HIS 97  ? A HIS 94  ? 1_555 CO ? E CO . ? A CO 204 ? 1_555 NE2 ? A HIS 98  ? A HIS 95  ? 1_555 63.4  ? 
17 NE2 ? A HIS 97  ? A HIS 94  ? 1_555 CO ? E CO . ? A CO 204 ? 1_555 OE1 ? A GLU 101 ? A GLU 98  ? 1_555 88.7  ? 
18 NE2 ? A HIS 98  ? A HIS 95  ? 1_555 CO ? E CO . ? A CO 204 ? 1_555 OE1 ? A GLU 101 ? A GLU 98  ? 1_555 108.8 ? 
19 NE2 ? A HIS 97  ? A HIS 94  ? 1_555 CO ? E CO . ? A CO 204 ? 1_555 O   ? G HOH .   ? A HOH 315 ? 1_555 175.5 ? 
20 NE2 ? A HIS 98  ? A HIS 95  ? 1_555 CO ? E CO . ? A CO 204 ? 1_555 O   ? G HOH .   ? A HOH 315 ? 1_555 116.8 ? 
21 OE1 ? A GLU 101 ? A GLU 98  ? 1_555 CO ? E CO . ? A CO 204 ? 1_555 O   ? G HOH .   ? A HOH 315 ? 1_555 87.0  ? 
22 NE2 ? A HIS 97  ? A HIS 94  ? 1_555 CO ? E CO . ? A CO 204 ? 1_555 O   ? G HOH .   ? A HOH 317 ? 1_555 89.6  ? 
23 NE2 ? A HIS 98  ? A HIS 95  ? 1_555 CO ? E CO . ? A CO 204 ? 1_555 O   ? G HOH .   ? A HOH 317 ? 1_555 41.8  ? 
24 OE1 ? A GLU 101 ? A GLU 98  ? 1_555 CO ? E CO . ? A CO 204 ? 1_555 O   ? G HOH .   ? A HOH 317 ? 1_555 77.9  ? 
25 O   ? G HOH .   ? A HOH 315 ? 1_555 CO ? E CO . ? A CO 204 ? 1_555 O   ? G HOH .   ? A HOH 317 ? 1_555 88.1  ? 
26 NE2 ? A HIS 97  ? A HIS 94  ? 1_555 CO ? E CO . ? A CO 204 ? 1_555 O   ? G HOH .   ? A HOH 358 ? 1_555 93.6  ? 
27 NE2 ? A HIS 98  ? A HIS 95  ? 1_555 CO ? E CO . ? A CO 204 ? 1_555 O   ? G HOH .   ? A HOH 358 ? 1_555 150.1 ? 
28 OE1 ? A GLU 101 ? A GLU 98  ? 1_555 CO ? E CO . ? A CO 204 ? 1_555 O   ? G HOH .   ? A HOH 358 ? 1_555 88.3  ? 
29 O   ? G HOH .   ? A HOH 315 ? 1_555 CO ? E CO . ? A CO 204 ? 1_555 O   ? G HOH .   ? A HOH 358 ? 1_555 87.7  ? 
30 O   ? G HOH .   ? A HOH 317 ? 1_555 CO ? E CO . ? A CO 204 ? 1_555 O   ? G HOH .   ? A HOH 358 ? 1_555 165.7 ? 
# 
_struct_sheet.id               AA1 
_struct_sheet.type             ? 
_struct_sheet.number_strands   6 
_struct_sheet.details          ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA1 4 5 ? parallel      
AA1 5 6 ? parallel      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 SER A 42  ? ILE A 49  ? SER A 39  ILE A 46  
AA1 2 GLU A 52  ? ASP A 60  ? GLU A 49  ASP A 57  
AA1 3 GLU A 6   ? GLY A 13  ? GLU A 3   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 59  ? O LEU A 56  N LEU A 9   ? N LEU A 6   
AA1 3 4 N VAL A 10  ? N VAL A 7   O LEU A 82  ? O LEU A 79  
AA1 4 5 N PHE A 85  ? N PHE A 82  O ASN A 119 ? O ASN A 116 
AA1 5 6 N LEU A 116 ? N LEU A 113 O ILE A 145 ? O ILE A 142 
# 
_pdbx_entry_details.entry_id                   9GGZ 
_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 
# 
loop_
_pdbx_validate_rmsd_bond.id 
_pdbx_validate_rmsd_bond.PDB_model_num 
_pdbx_validate_rmsd_bond.auth_atom_id_1 
_pdbx_validate_rmsd_bond.auth_asym_id_1 
_pdbx_validate_rmsd_bond.auth_comp_id_1 
_pdbx_validate_rmsd_bond.auth_seq_id_1 
_pdbx_validate_rmsd_bond.PDB_ins_code_1 
_pdbx_validate_rmsd_bond.label_alt_id_1 
_pdbx_validate_rmsd_bond.auth_atom_id_2 
_pdbx_validate_rmsd_bond.auth_asym_id_2 
_pdbx_validate_rmsd_bond.auth_comp_id_2 
_pdbx_validate_rmsd_bond.auth_seq_id_2 
_pdbx_validate_rmsd_bond.PDB_ins_code_2 
_pdbx_validate_rmsd_bond.label_alt_id_2 
_pdbx_validate_rmsd_bond.bond_value 
_pdbx_validate_rmsd_bond.bond_target_value 
_pdbx_validate_rmsd_bond.bond_deviation 
_pdbx_validate_rmsd_bond.bond_standard_deviation 
_pdbx_validate_rmsd_bond.linker_flag 
1 1 CD A GLU 76  ? ? OE1 A GLU 76  ? ? 1.183 1.252 -0.069 0.011 N 
2 1 CD A GLU 76  ? ? OE2 A GLU 76  ? ? 1.175 1.252 -0.077 0.011 N 
3 1 CD A GLU 91  ? ? OE1 A GLU 91  ? ? 1.161 1.252 -0.091 0.011 N 
4 1 CD A GLU 91  ? ? OE2 A GLU 91  ? ? 1.167 1.252 -0.085 0.011 N 
5 1 CD A GLU 143 ? ? OE1 A GLU 143 ? ? 1.173 1.252 -0.079 0.011 N 
# 
_pdbx_validate_rmsd_angle.id                         1 
_pdbx_validate_rmsd_angle.PDB_model_num              1 
_pdbx_validate_rmsd_angle.auth_atom_id_1             CG 
_pdbx_validate_rmsd_angle.auth_asym_id_1             A 
_pdbx_validate_rmsd_angle.auth_comp_id_1             ARG 
_pdbx_validate_rmsd_angle.auth_seq_id_1              135 
_pdbx_validate_rmsd_angle.PDB_ins_code_1             ? 
_pdbx_validate_rmsd_angle.label_alt_id_1             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_2             CD 
_pdbx_validate_rmsd_angle.auth_asym_id_2             A 
_pdbx_validate_rmsd_angle.auth_comp_id_2             ARG 
_pdbx_validate_rmsd_angle.auth_seq_id_2              135 
_pdbx_validate_rmsd_angle.PDB_ins_code_2             ? 
_pdbx_validate_rmsd_angle.label_alt_id_2             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_3             NE 
_pdbx_validate_rmsd_angle.auth_asym_id_3             A 
_pdbx_validate_rmsd_angle.auth_comp_id_3             ARG 
_pdbx_validate_rmsd_angle.auth_seq_id_3              135 
_pdbx_validate_rmsd_angle.PDB_ins_code_3             ? 
_pdbx_validate_rmsd_angle.label_alt_id_3             ? 
_pdbx_validate_rmsd_angle.angle_value                99.06 
_pdbx_validate_rmsd_angle.angle_target_value         111.80 
_pdbx_validate_rmsd_angle.angle_deviation            -12.74 
_pdbx_validate_rmsd_angle.angle_standard_deviation   2.10 
_pdbx_validate_rmsd_angle.linker_flag                N 
# 
_pdbx_validate_torsion.id              1 
_pdbx_validate_torsion.PDB_model_num   1 
_pdbx_validate_torsion.auth_comp_id    LYS 
_pdbx_validate_torsion.auth_asym_id    A 
_pdbx_validate_torsion.auth_seq_id     117 
_pdbx_validate_torsion.PDB_ins_code    ? 
_pdbx_validate_torsion.label_alt_id    ? 
_pdbx_validate_torsion.phi             74.25 
_pdbx_validate_torsion.psi             30.08 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A GLY -2 ? A GLY 1  
2  1 Y 1 A GLY -1 ? A GLY 2  
3  1 Y 1 A SER 0  ? A SER 3  
4  1 Y 1 A GLU 31 ? A GLU 34 
5  1 Y 1 A TYR 32 ? A TYR 35 
6  1 Y 1 A ASP 33 ? A ASP 36 
7  1 Y 1 A PRO 34 ? A PRO 37 
8  1 Y 1 A THR 35 ? A THR 38 
9  1 Y 1 A GLN 61 ? A GLN 64 
10 1 Y 1 A GLU 62 ? A GLU 65 
# 
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 
A1IK8 CBK    C  N N 1   
A1IK8 CBL    C  N N 2   
A1IK8 CBM    C  N N 3   
A1IK8 NBP    N  N N 4   
A1IK8 CBN    C  N N 5   
A1IK8 CBO    C  N N 6   
A1IK8 CBJ    C  N N 7   
A1IK8 NAQ    N  N N 8   
A1IK8 CAB    C  N N 9   
A1IK8 OAA    O  N N 10  
A1IK8 CAR    C  N N 11  
A1IK8 CAS    C  N N 12  
A1IK8 CAT    C  N N 13  
A1IK8 CAU    C  N N 14  
A1IK8 CAV    C  N N 15  
A1IK8 NAW    N  N N 16  
A1IK8 CAX    C  Y N 17  
A1IK8 CAY    C  Y N 18  
A1IK8 OBD    O  N N 19  
A1IK8 CAZ    C  Y N 20  
A1IK8 CBA    C  Y N 21  
A1IK8 CBB    C  Y N 22  
A1IK8 CLBC   CL N N 23  
A1IK8 CBI    C  Y N 24  
A1IK8 SBH    S  N N 25  
A1IK8 CBG    C  N N 26  
A1IK8 NBF    N  N N 27  
A1IK8 SAH    S  N N 28  
A1IK8 OAI    O  N N 29  
A1IK8 OBE    O  N N 30  
A1IK8 CAG    C  Y N 31  
A1IK8 CAF    C  Y N 32  
A1IK8 NAE    N  Y N 33  
A1IK8 CAJ    C  Y N 34  
A1IK8 CAC    C  Y N 35  
A1IK8 CAD    C  Y N 36  
A1IK8 NAK    N  N N 37  
A1IK8 CAL    C  N S 38  
A1IK8 CAM    C  N N 39  
A1IK8 CAN    C  N N 40  
A1IK8 NAO    N  N N 41  
A1IK8 CAP    C  N N 42  
A1IK8 H1     H  N N 43  
A1IK8 H2     H  N N 44  
A1IK8 H3     H  N N 45  
A1IK8 H4     H  N N 46  
A1IK8 H5     H  N N 47  
A1IK8 H6     H  N N 48  
A1IK8 H7     H  N N 49  
A1IK8 H9     H  N N 50  
A1IK8 H10    H  N N 51  
A1IK8 H11    H  N N 52  
A1IK8 H12    H  N N 53  
A1IK8 H13    H  N N 54  
A1IK8 H14    H  N N 55  
A1IK8 H15    H  N N 56  
A1IK8 H16    H  N N 57  
A1IK8 H17    H  N N 58  
A1IK8 H18    H  N N 59  
A1IK8 H19    H  N N 60  
A1IK8 H20    H  N N 61  
A1IK8 H21    H  N N 62  
A1IK8 H22    H  N N 63  
A1IK8 H23    H  N N 64  
A1IK8 H24    H  N N 65  
A1IK8 H25    H  N N 66  
A1IK8 H26    H  N N 67  
A1IK8 H28    H  N N 68  
A1IK8 H29    H  N N 69  
A1IK8 H30    H  N N 70  
A1IK8 H31    H  N N 71  
A1IK8 H32    H  N N 72  
A1IK8 H33    H  N N 73  
A1IK8 H34    H  N N 74  
A1IK8 H35    H  N N 75  
A1IK8 H36    H  N N 76  
A1IK8 H38    H  N N 77  
A1IK8 H39    H  N N 78  
ALA   N      N  N N 79  
ALA   CA     C  N S 80  
ALA   C      C  N N 81  
ALA   O      O  N N 82  
ALA   CB     C  N N 83  
ALA   OXT    O  N N 84  
ALA   H      H  N N 85  
ALA   H2     H  N N 86  
ALA   HA     H  N N 87  
ALA   HB1    H  N N 88  
ALA   HB2    H  N N 89  
ALA   HB3    H  N N 90  
ALA   HXT    H  N N 91  
ARG   N      N  N N 92  
ARG   CA     C  N S 93  
ARG   C      C  N N 94  
ARG   O      O  N N 95  
ARG   CB     C  N N 96  
ARG   CG     C  N N 97  
ARG   CD     C  N N 98  
ARG   NE     N  N N 99  
ARG   CZ     C  N N 100 
ARG   NH1    N  N N 101 
ARG   NH2    N  N N 102 
ARG   OXT    O  N N 103 
ARG   H      H  N N 104 
ARG   H2     H  N N 105 
ARG   HA     H  N N 106 
ARG   HB2    H  N N 107 
ARG   HB3    H  N N 108 
ARG   HG2    H  N N 109 
ARG   HG3    H  N N 110 
ARG   HD2    H  N N 111 
ARG   HD3    H  N N 112 
ARG   HE     H  N N 113 
ARG   HH11   H  N N 114 
ARG   HH12   H  N N 115 
ARG   HH21   H  N N 116 
ARG   HH22   H  N N 117 
ARG   HXT    H  N N 118 
ASN   N      N  N N 119 
ASN   CA     C  N S 120 
ASN   C      C  N N 121 
ASN   O      O  N N 122 
ASN   CB     C  N N 123 
ASN   CG     C  N N 124 
ASN   OD1    O  N N 125 
ASN   ND2    N  N N 126 
ASN   OXT    O  N N 127 
ASN   H      H  N N 128 
ASN   H2     H  N N 129 
ASN   HA     H  N N 130 
ASN   HB2    H  N N 131 
ASN   HB3    H  N N 132 
ASN   HD21   H  N N 133 
ASN   HD22   H  N N 134 
ASN   HXT    H  N N 135 
ASP   N      N  N N 136 
ASP   CA     C  N S 137 
ASP   C      C  N N 138 
ASP   O      O  N N 139 
ASP   CB     C  N N 140 
ASP   CG     C  N N 141 
ASP   OD1    O  N N 142 
ASP   OD2    O  N N 143 
ASP   OXT    O  N N 144 
ASP   H      H  N N 145 
ASP   H2     H  N N 146 
ASP   HA     H  N N 147 
ASP   HB2    H  N N 148 
ASP   HB3    H  N N 149 
ASP   HD2    H  N N 150 
ASP   HXT    H  N N 151 
CO    CO     CO N N 152 
CYS   N      N  N N 153 
CYS   CA     C  N R 154 
CYS   C      C  N N 155 
CYS   O      O  N N 156 
CYS   CB     C  N N 157 
CYS   SG     S  N N 158 
CYS   OXT    O  N N 159 
CYS   H      H  N N 160 
CYS   H2     H  N N 161 
CYS   HA     H  N N 162 
CYS   HB2    H  N N 163 
CYS   HB3    H  N N 164 
CYS   HG     H  N N 165 
CYS   HXT    H  N N 166 
GLN   N      N  N N 167 
GLN   CA     C  N S 168 
GLN   C      C  N N 169 
GLN   O      O  N N 170 
GLN   CB     C  N N 171 
GLN   CG     C  N N 172 
GLN   CD     C  N N 173 
GLN   OE1    O  N N 174 
GLN   NE2    N  N N 175 
GLN   OXT    O  N N 176 
GLN   H      H  N N 177 
GLN   H2     H  N N 178 
GLN   HA     H  N N 179 
GLN   HB2    H  N N 180 
GLN   HB3    H  N N 181 
GLN   HG2    H  N N 182 
GLN   HG3    H  N N 183 
GLN   HE21   H  N N 184 
GLN   HE22   H  N N 185 
GLN   HXT    H  N N 186 
GLU   N      N  N N 187 
GLU   CA     C  N S 188 
GLU   C      C  N N 189 
GLU   O      O  N N 190 
GLU   CB     C  N N 191 
GLU   CG     C  N N 192 
GLU   CD     C  N N 193 
GLU   OE1    O  N N 194 
GLU   OE2    O  N N 195 
GLU   OXT    O  N N 196 
GLU   H      H  N N 197 
GLU   H2     H  N N 198 
GLU   HA     H  N N 199 
GLU   HB2    H  N N 200 
GLU   HB3    H  N N 201 
GLU   HG2    H  N N 202 
GLU   HG3    H  N N 203 
GLU   HE2    H  N N 204 
GLU   HXT    H  N N 205 
GLY   N      N  N N 206 
GLY   CA     C  N N 207 
GLY   C      C  N N 208 
GLY   O      O  N N 209 
GLY   OXT    O  N N 210 
GLY   H      H  N N 211 
GLY   H2     H  N N 212 
GLY   HA2    H  N N 213 
GLY   HA3    H  N N 214 
GLY   HXT    H  N N 215 
GNP   PG     P  N N 216 
GNP   O1G    O  N N 217 
GNP   O2G    O  N N 218 
GNP   O3G    O  N N 219 
GNP   N3B    N  N N 220 
GNP   PB     P  N R 221 
GNP   O1B    O  N N 222 
GNP   O2B    O  N N 223 
GNP   O3A    O  N N 224 
GNP   PA     P  N S 225 
GNP   O1A    O  N N 226 
GNP   O2A    O  N N 227 
GNP   "O5'"  O  N N 228 
GNP   "C5'"  C  N N 229 
GNP   "C4'"  C  N R 230 
GNP   "O4'"  O  N N 231 
GNP   "C3'"  C  N S 232 
GNP   "O3'"  O  N N 233 
GNP   "C2'"  C  N R 234 
GNP   "O2'"  O  N N 235 
GNP   "C1'"  C  N R 236 
GNP   N9     N  Y N 237 
GNP   C8     C  Y N 238 
GNP   N7     N  Y N 239 
GNP   C5     C  Y N 240 
GNP   C6     C  Y N 241 
GNP   O6     O  N N 242 
GNP   N1     N  Y N 243 
GNP   C2     C  Y N 244 
GNP   N2     N  N N 245 
GNP   N3     N  Y N 246 
GNP   C4     C  Y N 247 
GNP   HOG2   H  N N 248 
GNP   HOG3   H  N N 249 
GNP   HNB3   H  N N 250 
GNP   HOB2   H  N N 251 
GNP   HOA2   H  N N 252 
GNP   "H5'2" H  N N 253 
GNP   "H5'1" H  N N 254 
GNP   "H4'"  H  N N 255 
GNP   "H3'"  H  N N 256 
GNP   "HO3'" H  N N 257 
GNP   "H2'"  H  N N 258 
GNP   "HO2'" H  N N 259 
GNP   "H1'"  H  N N 260 
GNP   H8     H  N N 261 
GNP   HN1    H  N N 262 
GNP   HN21   H  N N 263 
GNP   HN22   H  N N 264 
HIS   N      N  N N 265 
HIS   CA     C  N S 266 
HIS   C      C  N N 267 
HIS   O      O  N N 268 
HIS   CB     C  N N 269 
HIS   CG     C  Y N 270 
HIS   ND1    N  Y N 271 
HIS   CD2    C  Y N 272 
HIS   CE1    C  Y N 273 
HIS   NE2    N  Y N 274 
HIS   OXT    O  N N 275 
HIS   H      H  N N 276 
HIS   H2     H  N N 277 
HIS   HA     H  N N 278 
HIS   HB2    H  N N 279 
HIS   HB3    H  N N 280 
HIS   HD1    H  N N 281 
HIS   HD2    H  N N 282 
HIS   HE1    H  N N 283 
HIS   HE2    H  N N 284 
HIS   HXT    H  N N 285 
HOH   O      O  N N 286 
HOH   H1     H  N N 287 
HOH   H2     H  N N 288 
ILE   N      N  N N 289 
ILE   CA     C  N S 290 
ILE   C      C  N N 291 
ILE   O      O  N N 292 
ILE   CB     C  N S 293 
ILE   CG1    C  N N 294 
ILE   CG2    C  N N 295 
ILE   CD1    C  N N 296 
ILE   OXT    O  N N 297 
ILE   H      H  N N 298 
ILE   H2     H  N N 299 
ILE   HA     H  N N 300 
ILE   HB     H  N N 301 
ILE   HG12   H  N N 302 
ILE   HG13   H  N N 303 
ILE   HG21   H  N N 304 
ILE   HG22   H  N N 305 
ILE   HG23   H  N N 306 
ILE   HD11   H  N N 307 
ILE   HD12   H  N N 308 
ILE   HD13   H  N N 309 
ILE   HXT    H  N N 310 
LEU   N      N  N N 311 
LEU   CA     C  N S 312 
LEU   C      C  N N 313 
LEU   O      O  N N 314 
LEU   CB     C  N N 315 
LEU   CG     C  N N 316 
LEU   CD1    C  N N 317 
LEU   CD2    C  N N 318 
LEU   OXT    O  N N 319 
LEU   H      H  N N 320 
LEU   H2     H  N N 321 
LEU   HA     H  N N 322 
LEU   HB2    H  N N 323 
LEU   HB3    H  N N 324 
LEU   HG     H  N N 325 
LEU   HD11   H  N N 326 
LEU   HD12   H  N N 327 
LEU   HD13   H  N N 328 
LEU   HD21   H  N N 329 
LEU   HD22   H  N N 330 
LEU   HD23   H  N N 331 
LEU   HXT    H  N N 332 
LYS   N      N  N N 333 
LYS   CA     C  N S 334 
LYS   C      C  N N 335 
LYS   O      O  N N 336 
LYS   CB     C  N N 337 
LYS   CG     C  N N 338 
LYS   CD     C  N N 339 
LYS   CE     C  N N 340 
LYS   NZ     N  N N 341 
LYS   OXT    O  N N 342 
LYS   H      H  N N 343 
LYS   H2     H  N N 344 
LYS   HA     H  N N 345 
LYS   HB2    H  N N 346 
LYS   HB3    H  N N 347 
LYS   HG2    H  N N 348 
LYS   HG3    H  N N 349 
LYS   HD2    H  N N 350 
LYS   HD3    H  N N 351 
LYS   HE2    H  N N 352 
LYS   HE3    H  N N 353 
LYS   HZ1    H  N N 354 
LYS   HZ2    H  N N 355 
LYS   HZ3    H  N N 356 
LYS   HXT    H  N N 357 
MET   N      N  N N 358 
MET   CA     C  N S 359 
MET   C      C  N N 360 
MET   O      O  N N 361 
MET   CB     C  N N 362 
MET   CG     C  N N 363 
MET   SD     S  N N 364 
MET   CE     C  N N 365 
MET   OXT    O  N N 366 
MET   H      H  N N 367 
MET   H2     H  N N 368 
MET   HA     H  N N 369 
MET   HB2    H  N N 370 
MET   HB3    H  N N 371 
MET   HG2    H  N N 372 
MET   HG3    H  N N 373 
MET   HE1    H  N N 374 
MET   HE2    H  N N 375 
MET   HE3    H  N N 376 
MET   HXT    H  N N 377 
MG    MG     MG N N 378 
PHE   N      N  N N 379 
PHE   CA     C  N S 380 
PHE   C      C  N N 381 
PHE   O      O  N N 382 
PHE   CB     C  N N 383 
PHE   CG     C  Y N 384 
PHE   CD1    C  Y N 385 
PHE   CD2    C  Y N 386 
PHE   CE1    C  Y N 387 
PHE   CE2    C  Y N 388 
PHE   CZ     C  Y N 389 
PHE   OXT    O  N N 390 
PHE   H      H  N N 391 
PHE   H2     H  N N 392 
PHE   HA     H  N N 393 
PHE   HB2    H  N N 394 
PHE   HB3    H  N N 395 
PHE   HD1    H  N N 396 
PHE   HD2    H  N N 397 
PHE   HE1    H  N N 398 
PHE   HE2    H  N N 399 
PHE   HZ     H  N N 400 
PHE   HXT    H  N N 401 
PRO   N      N  N N 402 
PRO   CA     C  N S 403 
PRO   C      C  N N 404 
PRO   O      O  N N 405 
PRO   CB     C  N N 406 
PRO   CG     C  N N 407 
PRO   CD     C  N N 408 
PRO   OXT    O  N N 409 
PRO   H      H  N N 410 
PRO   HA     H  N N 411 
PRO   HB2    H  N N 412 
PRO   HB3    H  N N 413 
PRO   HG2    H  N N 414 
PRO   HG3    H  N N 415 
PRO   HD2    H  N N 416 
PRO   HD3    H  N N 417 
PRO   HXT    H  N N 418 
SER   N      N  N N 419 
SER   CA     C  N S 420 
SER   C      C  N N 421 
SER   O      O  N N 422 
SER   CB     C  N N 423 
SER   OG     O  N N 424 
SER   OXT    O  N N 425 
SER   H      H  N N 426 
SER   H2     H  N N 427 
SER   HA     H  N N 428 
SER   HB2    H  N N 429 
SER   HB3    H  N N 430 
SER   HG     H  N N 431 
SER   HXT    H  N N 432 
THR   N      N  N N 433 
THR   CA     C  N S 434 
THR   C      C  N N 435 
THR   O      O  N N 436 
THR   CB     C  N R 437 
THR   OG1    O  N N 438 
THR   CG2    C  N N 439 
THR   OXT    O  N N 440 
THR   H      H  N N 441 
THR   H2     H  N N 442 
THR   HA     H  N N 443 
THR   HB     H  N N 444 
THR   HG1    H  N N 445 
THR   HG21   H  N N 446 
THR   HG22   H  N N 447 
THR   HG23   H  N N 448 
THR   HXT    H  N N 449 
TYR   N      N  N N 450 
TYR   CA     C  N S 451 
TYR   C      C  N N 452 
TYR   O      O  N N 453 
TYR   CB     C  N N 454 
TYR   CG     C  Y N 455 
TYR   CD1    C  Y N 456 
TYR   CD2    C  Y N 457 
TYR   CE1    C  Y N 458 
TYR   CE2    C  Y N 459 
TYR   CZ     C  Y N 460 
TYR   OH     O  N N 461 
TYR   OXT    O  N N 462 
TYR   H      H  N N 463 
TYR   H2     H  N N 464 
TYR   HA     H  N N 465 
TYR   HB2    H  N N 466 
TYR   HB3    H  N N 467 
TYR   HD1    H  N N 468 
TYR   HD2    H  N N 469 
TYR   HE1    H  N N 470 
TYR   HE2    H  N N 471 
TYR   HH     H  N N 472 
TYR   HXT    H  N N 473 
VAL   N      N  N N 474 
VAL   CA     C  N S 475 
VAL   C      C  N N 476 
VAL   O      O  N N 477 
VAL   CB     C  N N 478 
VAL   CG1    C  N N 479 
VAL   CG2    C  N N 480 
VAL   OXT    O  N N 481 
VAL   H      H  N N 482 
VAL   H2     H  N N 483 
VAL   HA     H  N N 484 
VAL   HB     H  N N 485 
VAL   HG11   H  N N 486 
VAL   HG12   H  N N 487 
VAL   HG13   H  N N 488 
VAL   HG21   H  N N 489 
VAL   HG22   H  N N 490 
VAL   HG23   H  N N 491 
VAL   HXT    H  N N 492 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
A1IK8 CLBC  CBB    sing N N 1   
A1IK8 OAI   SAH    doub N N 2   
A1IK8 CAF   NAE    doub Y N 3   
A1IK8 CAF   CAG    sing Y N 4   
A1IK8 SBH   CBI    sing N N 5   
A1IK8 SBH   CBG    sing N N 6   
A1IK8 NAE   CAD    sing Y N 7   
A1IK8 SAH   OBE    doub N N 8   
A1IK8 SAH   CAG    sing N N 9   
A1IK8 SAH   NBF    sing N N 10  
A1IK8 CBB   CBI    doub Y N 11  
A1IK8 CBB   CBA    sing Y N 12  
A1IK8 CAG   CAJ    doub Y N 13  
A1IK8 CAL   CAM    sing N N 14  
A1IK8 CAL   CAP    sing N N 15  
A1IK8 CAL   NAK    sing N N 16  
A1IK8 CBI   CAX    sing Y N 17  
A1IK8 CAM   CAN    sing N N 18  
A1IK8 CAP   NAO    sing N N 19  
A1IK8 CBA   CAZ    doub Y N 20  
A1IK8 NAO   CAN    sing N N 21  
A1IK8 CAD   NAK    sing N N 22  
A1IK8 CAD   CAC    doub Y N 23  
A1IK8 CBG   NBF    doub N N 24  
A1IK8 CBG   NAW    sing N N 25  
A1IK8 CAJ   CAC    sing Y N 26  
A1IK8 CAX   NAW    sing N N 27  
A1IK8 CAX   CAY    doub Y N 28  
A1IK8 CAC   CAB    sing N N 29  
A1IK8 NAW   CAV    sing N N 30  
A1IK8 CAZ   CAY    sing Y N 31  
A1IK8 CAY   OBD    sing N N 32  
A1IK8 CAB   OAA    doub N N 33  
A1IK8 CAB   NAQ    sing N N 34  
A1IK8 CAV   CAU    sing N N 35  
A1IK8 CAT   CAU    sing N N 36  
A1IK8 CAT   CAS    sing N N 37  
A1IK8 CAR   NAQ    sing N N 38  
A1IK8 CAR   CAS    sing N N 39  
A1IK8 NAQ   CBJ    sing N N 40  
A1IK8 CBJ   CBK    sing N N 41  
A1IK8 CBJ   CBO    sing N N 42  
A1IK8 CBK   CBL    sing N N 43  
A1IK8 CBO   CBN    sing N N 44  
A1IK8 CBL   CBM    sing N N 45  
A1IK8 CBN   CBM    sing N N 46  
A1IK8 CBM   NBP    sing N N 47  
A1IK8 CBK   H1     sing N N 48  
A1IK8 CBK   H2     sing N N 49  
A1IK8 CBL   H3     sing N N 50  
A1IK8 CBL   H4     sing N N 51  
A1IK8 CBM   H5     sing N N 52  
A1IK8 NBP   H6     sing N N 53  
A1IK8 NBP   H7     sing N N 54  
A1IK8 CBN   H9     sing N N 55  
A1IK8 CBN   H10    sing N N 56  
A1IK8 CBO   H11    sing N N 57  
A1IK8 CBO   H12    sing N N 58  
A1IK8 CBJ   H13    sing N N 59  
A1IK8 CAR   H14    sing N N 60  
A1IK8 CAR   H15    sing N N 61  
A1IK8 CAS   H16    sing N N 62  
A1IK8 CAS   H17    sing N N 63  
A1IK8 CAT   H18    sing N N 64  
A1IK8 CAT   H19    sing N N 65  
A1IK8 CAU   H20    sing N N 66  
A1IK8 CAU   H21    sing N N 67  
A1IK8 CAV   H22    sing N N 68  
A1IK8 CAV   H23    sing N N 69  
A1IK8 OBD   H24    sing N N 70  
A1IK8 CAZ   H25    sing N N 71  
A1IK8 CBA   H26    sing N N 72  
A1IK8 CAF   H28    sing N N 73  
A1IK8 CAJ   H29    sing N N 74  
A1IK8 NAK   H30    sing N N 75  
A1IK8 CAL   H31    sing N N 76  
A1IK8 CAM   H32    sing N N 77  
A1IK8 CAM   H33    sing N N 78  
A1IK8 CAN   H34    sing N N 79  
A1IK8 CAN   H35    sing N N 80  
A1IK8 NAO   H36    sing N N 81  
A1IK8 CAP   H38    sing N N 82  
A1IK8 CAP   H39    sing N N 83  
ALA   N     CA     sing N N 84  
ALA   N     H      sing N N 85  
ALA   N     H2     sing N N 86  
ALA   CA    C      sing N N 87  
ALA   CA    CB     sing N N 88  
ALA   CA    HA     sing N N 89  
ALA   C     O      doub N N 90  
ALA   C     OXT    sing N N 91  
ALA   CB    HB1    sing N N 92  
ALA   CB    HB2    sing N N 93  
ALA   CB    HB3    sing N N 94  
ALA   OXT   HXT    sing N N 95  
ARG   N     CA     sing N N 96  
ARG   N     H      sing N N 97  
ARG   N     H2     sing N N 98  
ARG   CA    C      sing N N 99  
ARG   CA    CB     sing N N 100 
ARG   CA    HA     sing N N 101 
ARG   C     O      doub N N 102 
ARG   C     OXT    sing N N 103 
ARG   CB    CG     sing N N 104 
ARG   CB    HB2    sing N N 105 
ARG   CB    HB3    sing N N 106 
ARG   CG    CD     sing N N 107 
ARG   CG    HG2    sing N N 108 
ARG   CG    HG3    sing N N 109 
ARG   CD    NE     sing N N 110 
ARG   CD    HD2    sing N N 111 
ARG   CD    HD3    sing N N 112 
ARG   NE    CZ     sing N N 113 
ARG   NE    HE     sing N N 114 
ARG   CZ    NH1    sing N N 115 
ARG   CZ    NH2    doub N N 116 
ARG   NH1   HH11   sing N N 117 
ARG   NH1   HH12   sing N N 118 
ARG   NH2   HH21   sing N N 119 
ARG   NH2   HH22   sing N N 120 
ARG   OXT   HXT    sing N N 121 
ASN   N     CA     sing N N 122 
ASN   N     H      sing N N 123 
ASN   N     H2     sing N N 124 
ASN   CA    C      sing N N 125 
ASN   CA    CB     sing N N 126 
ASN   CA    HA     sing N N 127 
ASN   C     O      doub N N 128 
ASN   C     OXT    sing N N 129 
ASN   CB    CG     sing N N 130 
ASN   CB    HB2    sing N N 131 
ASN   CB    HB3    sing N N 132 
ASN   CG    OD1    doub N N 133 
ASN   CG    ND2    sing N N 134 
ASN   ND2   HD21   sing N N 135 
ASN   ND2   HD22   sing N N 136 
ASN   OXT   HXT    sing N N 137 
ASP   N     CA     sing N N 138 
ASP   N     H      sing N N 139 
ASP   N     H2     sing N N 140 
ASP   CA    C      sing N N 141 
ASP   CA    CB     sing N N 142 
ASP   CA    HA     sing N N 143 
ASP   C     O      doub N N 144 
ASP   C     OXT    sing N N 145 
ASP   CB    CG     sing N N 146 
ASP   CB    HB2    sing N N 147 
ASP   CB    HB3    sing N N 148 
ASP   CG    OD1    doub N N 149 
ASP   CG    OD2    sing N N 150 
ASP   OD2   HD2    sing N N 151 
ASP   OXT   HXT    sing N N 152 
CYS   N     CA     sing N N 153 
CYS   N     H      sing N N 154 
CYS   N     H2     sing N N 155 
CYS   CA    C      sing N N 156 
CYS   CA    CB     sing N N 157 
CYS   CA    HA     sing N N 158 
CYS   C     O      doub N N 159 
CYS   C     OXT    sing N N 160 
CYS   CB    SG     sing N N 161 
CYS   CB    HB2    sing N N 162 
CYS   CB    HB3    sing N N 163 
CYS   SG    HG     sing N N 164 
CYS   OXT   HXT    sing N N 165 
GLN   N     CA     sing N N 166 
GLN   N     H      sing N N 167 
GLN   N     H2     sing N N 168 
GLN   CA    C      sing N N 169 
GLN   CA    CB     sing N N 170 
GLN   CA    HA     sing N N 171 
GLN   C     O      doub N N 172 
GLN   C     OXT    sing N N 173 
GLN   CB    CG     sing N N 174 
GLN   CB    HB2    sing N N 175 
GLN   CB    HB3    sing N N 176 
GLN   CG    CD     sing N N 177 
GLN   CG    HG2    sing N N 178 
GLN   CG    HG3    sing N N 179 
GLN   CD    OE1    doub N N 180 
GLN   CD    NE2    sing N N 181 
GLN   NE2   HE21   sing N N 182 
GLN   NE2   HE22   sing N N 183 
GLN   OXT   HXT    sing N N 184 
GLU   N     CA     sing N N 185 
GLU   N     H      sing N N 186 
GLU   N     H2     sing N N 187 
GLU   CA    C      sing N N 188 
GLU   CA    CB     sing N N 189 
GLU   CA    HA     sing N N 190 
GLU   C     O      doub N N 191 
GLU   C     OXT    sing N N 192 
GLU   CB    CG     sing N N 193 
GLU   CB    HB2    sing N N 194 
GLU   CB    HB3    sing N N 195 
GLU   CG    CD     sing N N 196 
GLU   CG    HG2    sing N N 197 
GLU   CG    HG3    sing N N 198 
GLU   CD    OE1    doub N N 199 
GLU   CD    OE2    sing N N 200 
GLU   OE2   HE2    sing N N 201 
GLU   OXT   HXT    sing N N 202 
GLY   N     CA     sing N N 203 
GLY   N     H      sing N N 204 
GLY   N     H2     sing N N 205 
GLY   CA    C      sing N N 206 
GLY   CA    HA2    sing N N 207 
GLY   CA    HA3    sing N N 208 
GLY   C     O      doub N N 209 
GLY   C     OXT    sing N N 210 
GLY   OXT   HXT    sing N N 211 
GNP   PG    O1G    doub N N 212 
GNP   PG    O2G    sing N N 213 
GNP   PG    O3G    sing N N 214 
GNP   PG    N3B    sing N N 215 
GNP   O2G   HOG2   sing N N 216 
GNP   O3G   HOG3   sing N N 217 
GNP   N3B   PB     sing N N 218 
GNP   N3B   HNB3   sing N N 219 
GNP   PB    O1B    doub N N 220 
GNP   PB    O2B    sing N N 221 
GNP   PB    O3A    sing N N 222 
GNP   O2B   HOB2   sing N N 223 
GNP   O3A   PA     sing N N 224 
GNP   PA    O1A    doub N N 225 
GNP   PA    O2A    sing N N 226 
GNP   PA    "O5'"  sing N N 227 
GNP   O2A   HOA2   sing N N 228 
GNP   "O5'" "C5'"  sing N N 229 
GNP   "C5'" "C4'"  sing N N 230 
GNP   "C5'" "H5'2" sing N N 231 
GNP   "C5'" "H5'1" sing N N 232 
GNP   "C4'" "O4'"  sing N N 233 
GNP   "C4'" "C3'"  sing N N 234 
GNP   "C4'" "H4'"  sing N N 235 
GNP   "O4'" "C1'"  sing N N 236 
GNP   "C3'" "O3'"  sing N N 237 
GNP   "C3'" "C2'"  sing N N 238 
GNP   "C3'" "H3'"  sing N N 239 
GNP   "O3'" "HO3'" sing N N 240 
GNP   "C2'" "O2'"  sing N N 241 
GNP   "C2'" "C1'"  sing N N 242 
GNP   "C2'" "H2'"  sing N N 243 
GNP   "O2'" "HO2'" sing N N 244 
GNP   "C1'" N9     sing N N 245 
GNP   "C1'" "H1'"  sing N N 246 
GNP   N9    C8     sing Y N 247 
GNP   N9    C4     sing Y N 248 
GNP   C8    N7     doub Y N 249 
GNP   C8    H8     sing N N 250 
GNP   N7    C5     sing Y N 251 
GNP   C5    C6     sing Y N 252 
GNP   C5    C4     doub Y N 253 
GNP   C6    O6     doub N N 254 
GNP   C6    N1     sing Y N 255 
GNP   N1    C2     sing Y N 256 
GNP   N1    HN1    sing N N 257 
GNP   C2    N2     sing N N 258 
GNP   C2    N3     doub Y N 259 
GNP   N2    HN21   sing N N 260 
GNP   N2    HN22   sing N N 261 
GNP   N3    C4     sing Y N 262 
HIS   N     CA     sing N N 263 
HIS   N     H      sing N N 264 
HIS   N     H2     sing N N 265 
HIS   CA    C      sing N N 266 
HIS   CA    CB     sing N N 267 
HIS   CA    HA     sing N N 268 
HIS   C     O      doub N N 269 
HIS   C     OXT    sing N N 270 
HIS   CB    CG     sing N N 271 
HIS   CB    HB2    sing N N 272 
HIS   CB    HB3    sing N N 273 
HIS   CG    ND1    sing Y N 274 
HIS   CG    CD2    doub Y N 275 
HIS   ND1   CE1    doub Y N 276 
HIS   ND1   HD1    sing N N 277 
HIS   CD2   NE2    sing Y N 278 
HIS   CD2   HD2    sing N N 279 
HIS   CE1   NE2    sing Y N 280 
HIS   CE1   HE1    sing N N 281 
HIS   NE2   HE2    sing N N 282 
HIS   OXT   HXT    sing N N 283 
HOH   O     H1     sing N N 284 
HOH   O     H2     sing N N 285 
ILE   N     CA     sing N N 286 
ILE   N     H      sing N N 287 
ILE   N     H2     sing N N 288 
ILE   CA    C      sing N N 289 
ILE   CA    CB     sing N N 290 
ILE   CA    HA     sing N N 291 
ILE   C     O      doub N N 292 
ILE   C     OXT    sing N N 293 
ILE   CB    CG1    sing N N 294 
ILE   CB    CG2    sing N N 295 
ILE   CB    HB     sing N N 296 
ILE   CG1   CD1    sing N N 297 
ILE   CG1   HG12   sing N N 298 
ILE   CG1   HG13   sing N N 299 
ILE   CG2   HG21   sing N N 300 
ILE   CG2   HG22   sing N N 301 
ILE   CG2   HG23   sing N N 302 
ILE   CD1   HD11   sing N N 303 
ILE   CD1   HD12   sing N N 304 
ILE   CD1   HD13   sing N N 305 
ILE   OXT   HXT    sing N N 306 
LEU   N     CA     sing N N 307 
LEU   N     H      sing N N 308 
LEU   N     H2     sing N N 309 
LEU   CA    C      sing N N 310 
LEU   CA    CB     sing N N 311 
LEU   CA    HA     sing N N 312 
LEU   C     O      doub N N 313 
LEU   C     OXT    sing N N 314 
LEU   CB    CG     sing N N 315 
LEU   CB    HB2    sing N N 316 
LEU   CB    HB3    sing N N 317 
LEU   CG    CD1    sing N N 318 
LEU   CG    CD2    sing N N 319 
LEU   CG    HG     sing N N 320 
LEU   CD1   HD11   sing N N 321 
LEU   CD1   HD12   sing N N 322 
LEU   CD1   HD13   sing N N 323 
LEU   CD2   HD21   sing N N 324 
LEU   CD2   HD22   sing N N 325 
LEU   CD2   HD23   sing N N 326 
LEU   OXT   HXT    sing N N 327 
LYS   N     CA     sing N N 328 
LYS   N     H      sing N N 329 
LYS   N     H2     sing N N 330 
LYS   CA    C      sing N N 331 
LYS   CA    CB     sing N N 332 
LYS   CA    HA     sing N N 333 
LYS   C     O      doub N N 334 
LYS   C     OXT    sing N N 335 
LYS   CB    CG     sing N N 336 
LYS   CB    HB2    sing N N 337 
LYS   CB    HB3    sing N N 338 
LYS   CG    CD     sing N N 339 
LYS   CG    HG2    sing N N 340 
LYS   CG    HG3    sing N N 341 
LYS   CD    CE     sing N N 342 
LYS   CD    HD2    sing N N 343 
LYS   CD    HD3    sing N N 344 
LYS   CE    NZ     sing N N 345 
LYS   CE    HE2    sing N N 346 
LYS   CE    HE3    sing N N 347 
LYS   NZ    HZ1    sing N N 348 
LYS   NZ    HZ2    sing N N 349 
LYS   NZ    HZ3    sing N N 350 
LYS   OXT   HXT    sing N N 351 
MET   N     CA     sing N N 352 
MET   N     H      sing N N 353 
MET   N     H2     sing N N 354 
MET   CA    C      sing N N 355 
MET   CA    CB     sing N N 356 
MET   CA    HA     sing N N 357 
MET   C     O      doub N N 358 
MET   C     OXT    sing N N 359 
MET   CB    CG     sing N N 360 
MET   CB    HB2    sing N N 361 
MET   CB    HB3    sing N N 362 
MET   CG    SD     sing N N 363 
MET   CG    HG2    sing N N 364 
MET   CG    HG3    sing N N 365 
MET   SD    CE     sing N N 366 
MET   CE    HE1    sing N N 367 
MET   CE    HE2    sing N N 368 
MET   CE    HE3    sing N N 369 
MET   OXT   HXT    sing N N 370 
PHE   N     CA     sing N N 371 
PHE   N     H      sing N N 372 
PHE   N     H2     sing N N 373 
PHE   CA    C      sing N N 374 
PHE   CA    CB     sing N N 375 
PHE   CA    HA     sing N N 376 
PHE   C     O      doub N N 377 
PHE   C     OXT    sing N N 378 
PHE   CB    CG     sing N N 379 
PHE   CB    HB2    sing N N 380 
PHE   CB    HB3    sing N N 381 
PHE   CG    CD1    doub Y N 382 
PHE   CG    CD2    sing Y N 383 
PHE   CD1   CE1    sing Y N 384 
PHE   CD1   HD1    sing N N 385 
PHE   CD2   CE2    doub Y N 386 
PHE   CD2   HD2    sing N N 387 
PHE   CE1   CZ     doub Y N 388 
PHE   CE1   HE1    sing N N 389 
PHE   CE2   CZ     sing Y N 390 
PHE   CE2   HE2    sing N N 391 
PHE   CZ    HZ     sing N N 392 
PHE   OXT   HXT    sing N N 393 
PRO   N     CA     sing N N 394 
PRO   N     CD     sing N N 395 
PRO   N     H      sing N N 396 
PRO   CA    C      sing N N 397 
PRO   CA    CB     sing N N 398 
PRO   CA    HA     sing N N 399 
PRO   C     O      doub N N 400 
PRO   C     OXT    sing N N 401 
PRO   CB    CG     sing N N 402 
PRO   CB    HB2    sing N N 403 
PRO   CB    HB3    sing N N 404 
PRO   CG    CD     sing N N 405 
PRO   CG    HG2    sing N N 406 
PRO   CG    HG3    sing N N 407 
PRO   CD    HD2    sing N N 408 
PRO   CD    HD3    sing N N 409 
PRO   OXT   HXT    sing N N 410 
SER   N     CA     sing N N 411 
SER   N     H      sing N N 412 
SER   N     H2     sing N N 413 
SER   CA    C      sing N N 414 
SER   CA    CB     sing N N 415 
SER   CA    HA     sing N N 416 
SER   C     O      doub N N 417 
SER   C     OXT    sing N N 418 
SER   CB    OG     sing N N 419 
SER   CB    HB2    sing N N 420 
SER   CB    HB3    sing N N 421 
SER   OG    HG     sing N N 422 
SER   OXT   HXT    sing N N 423 
THR   N     CA     sing N N 424 
THR   N     H      sing N N 425 
THR   N     H2     sing N N 426 
THR   CA    C      sing N N 427 
THR   CA    CB     sing N N 428 
THR   CA    HA     sing N N 429 
THR   C     O      doub N N 430 
THR   C     OXT    sing N N 431 
THR   CB    OG1    sing N N 432 
THR   CB    CG2    sing N N 433 
THR   CB    HB     sing N N 434 
THR   OG1   HG1    sing N N 435 
THR   CG2   HG21   sing N N 436 
THR   CG2   HG22   sing N N 437 
THR   CG2   HG23   sing N N 438 
THR   OXT   HXT    sing N N 439 
TYR   N     CA     sing N N 440 
TYR   N     H      sing N N 441 
TYR   N     H2     sing N N 442 
TYR   CA    C      sing N N 443 
TYR   CA    CB     sing N N 444 
TYR   CA    HA     sing N N 445 
TYR   C     O      doub N N 446 
TYR   C     OXT    sing N N 447 
TYR   CB    CG     sing N N 448 
TYR   CB    HB2    sing N N 449 
TYR   CB    HB3    sing N N 450 
TYR   CG    CD1    doub Y N 451 
TYR   CG    CD2    sing Y N 452 
TYR   CD1   CE1    sing Y N 453 
TYR   CD1   HD1    sing N N 454 
TYR   CD2   CE2    doub Y N 455 
TYR   CD2   HD2    sing N N 456 
TYR   CE1   CZ     doub Y N 457 
TYR   CE1   HE1    sing N N 458 
TYR   CE2   CZ     sing Y N 459 
TYR   CE2   HE2    sing N N 460 
TYR   CZ    OH     sing N N 461 
TYR   OH    HH     sing N N 462 
TYR   OXT   HXT    sing N N 463 
VAL   N     CA     sing N N 464 
VAL   N     H      sing N N 465 
VAL   N     H2     sing N N 466 
VAL   CA    C      sing N N 467 
VAL   CA    CB     sing N N 468 
VAL   CA    HA     sing N N 469 
VAL   C     O      doub N N 470 
VAL   C     OXT    sing N N 471 
VAL   CB    CG1    sing N N 472 
VAL   CB    CG2    sing N N 473 
VAL   CB    HB     sing N N 474 
VAL   CG1   HG11   sing N N 475 
VAL   CG1   HG12   sing N N 476 
VAL   CG1   HG13   sing N N 477 
VAL   CG2   HG21   sing N N 478 
VAL   CG2   HG22   sing N N 479 
VAL   CG2   HG23   sing N N 480 
VAL   OXT   HXT    sing N N 481 
# 
_pdbx_audit_support.funding_organization   'Cancer Research UK' 
_pdbx_audit_support.country                'United Kingdom' 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      Other 
_pdbx_initial_refinement_model.accession_code   ? 
_pdbx_initial_refinement_model.details          'unreleased crystal structure' 
# 
_atom_sites.entry_id                    9GGZ 
_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]   0.013840 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.004666 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.028681 
_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]   0.015168 
_atom_sites.fract_transf_vector[1]      0.000000 
_atom_sites.fract_transf_vector[2]      0.000000 
_atom_sites.fract_transf_vector[3]      0.000000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
CL 
CO 
MG 
N  
O  
P  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N     . MET   A 1 4   ? 7.894  1.760   25.054 1.00 43.54 ? 1   MET   A N     1 
ATOM   2    C  CA    . MET   A 1 4   ? 9.186  2.517   24.941 1.00 34.77 ? 1   MET   A CA    1 
ATOM   3    C  C     . MET   A 1 4   ? 9.939  2.039   23.691 1.00 27.43 ? 1   MET   A C     1 
ATOM   4    O  O     . MET   A 1 4   ? 10.023 0.860   23.565 1.00 31.91 ? 1   MET   A O     1 
ATOM   5    C  CB    . MET   A 1 4   ? 10.103 2.230   26.129 1.00 35.92 ? 1   MET   A CB    1 
ATOM   6    C  CG    . MET   A 1 4   ? 11.410 3.008   26.035 1.00 32.46 ? 1   MET   A CG    1 
ATOM   7    S  SD    . MET   A 1 4   ? 12.394 2.981   27.507 1.00 31.47 ? 1   MET   A SD    1 
ATOM   8    C  CE    . MET   A 1 4   ? 11.128 3.413   28.701 1.00 26.33 ? 1   MET   A CE    1 
ATOM   9    N  N     . THR   A 1 5   ? 10.354 2.962   22.839 1.00 28.35 ? 2   THR   A N     1 
ATOM   10   C  CA    . THR   A 1 5   ? 11.091 2.544   21.606 1.00 28.76 ? 2   THR   A CA    1 
ATOM   11   C  C     . THR   A 1 5   ? 12.367 1.781   21.969 1.00 26.86 ? 2   THR   A C     1 
ATOM   12   O  O     . THR   A 1 5   ? 13.078 2.212   22.810 1.00 26.26 ? 2   THR   A O     1 
ATOM   13   C  CB    . THR   A 1 5   ? 11.393 3.728   20.700 1.00 30.15 ? 2   THR   A CB    1 
ATOM   14   O  OG1   . THR   A 1 5   ? 10.272 4.542   20.402 1.00 34.66 ? 2   THR   A OG1   1 
ATOM   15   C  CG2   . THR   A 1 5   ? 11.986 3.284   19.381 1.00 37.49 ? 2   THR   A CG2   1 
ATOM   16   N  N     . GLU   A 1 6   ? 12.533 0.653   21.310 1.00 26.82 ? 3   GLU   A N     1 
ATOM   17   C  CA    . GLU   A 1 6   ? 13.677 -0.249  21.484 1.00 26.62 ? 3   GLU   A CA    1 
ATOM   18   C  C     . GLU   A 1 6   ? 14.485 -0.265  20.168 1.00 27.03 ? 3   GLU   A C     1 
ATOM   19   O  O     . GLU   A 1 6   ? 13.892 -0.184  19.125 1.00 29.97 ? 3   GLU   A O     1 
ATOM   20   C  CB    . GLU   A 1 6   ? 13.094 -1.632  21.549 1.00 34.93 ? 3   GLU   A CB    1 
ATOM   21   C  CG    . GLU   A 1 6   ? 13.991 -2.654  22.161 1.00 40.16 ? 3   GLU   A CG    1 
ATOM   22   C  CD    . GLU   A 1 6   ? 13.141 -3.476  23.117 1.00 37.00 ? 3   GLU   A CD    1 
ATOM   23   O  OE1   . GLU   A 1 6   ? 12.456 -2.859  23.950 1.00 49.56 ? 3   GLU   A OE1   1 
ATOM   24   O  OE2   . GLU   A 1 6   ? 13.125 -4.668  22.988 1.00 43.75 ? 3   GLU   A OE2   1 
ATOM   25   N  N     . TYR   A 1 7   ? 15.805 -0.279  20.319 1.00 21.26 ? 4   TYR   A N     1 
ATOM   26   C  CA    . TYR   A 1 7   ? 16.740 -0.353  19.157 1.00 18.51 ? 4   TYR   A CA    1 
ATOM   27   C  C     . TYR   A 1 7   ? 17.682 -1.541  19.341 1.00 18.24 ? 4   TYR   A C     1 
ATOM   28   O  O     . TYR   A 1 7   ? 18.338 -1.627  20.337 1.00 20.18 ? 4   TYR   A O     1 
ATOM   29   C  CB    . TYR   A 1 7   ? 17.531 0.940   19.086 1.00 19.96 ? 4   TYR   A CB    1 
ATOM   30   C  CG    . TYR   A 1 7   ? 16.733 2.159   18.739 1.00 20.90 ? 4   TYR   A CG    1 
ATOM   31   C  CD1   . TYR   A 1 7   ? 16.045 2.251   17.553 1.00 24.09 ? 4   TYR   A CD1   1 
ATOM   32   C  CD2   . TYR   A 1 7   ? 16.620 3.197   19.644 1.00 21.33 ? 4   TYR   A CD2   1 
ATOM   33   C  CE1   . TYR   A 1 7   ? 15.309 3.378   17.257 1.00 25.22 ? 4   TYR   A CE1   1 
ATOM   34   C  CE2   . TYR   A 1 7   ? 15.922 4.339   19.355 1.00 21.60 ? 4   TYR   A CE2   1 
ATOM   35   C  CZ    . TYR   A 1 7   ? 15.237 4.415   18.165 1.00 21.15 ? 4   TYR   A CZ    1 
ATOM   36   O  OH    . TYR   A 1 7   ? 14.569 5.543   17.897 1.00 26.18 ? 4   TYR   A OH    1 
ATOM   37   N  N     . LYS   A 1 8   ? 17.652 -2.436  18.357 1.00 19.24 ? 5   LYS   A N     1 
ATOM   38   C  CA    . LYS   A 1 8   ? 18.566 -3.598  18.349 1.00 20.34 ? 5   LYS   A CA    1 
ATOM   39   C  C     . LYS   A 1 8   ? 19.869 -3.162  17.628 1.00 16.08 ? 5   LYS   A C     1 
ATOM   40   O  O     . LYS   A 1 8   ? 19.807 -2.955  16.408 1.00 18.11 ? 5   LYS   A O     1 
ATOM   41   C  CB    . LYS   A 1 8   ? 17.946 -4.787  17.636 1.00 22.32 ? 5   LYS   A CB    1 
ATOM   42   C  CG    . LYS   A 1 8   ? 16.663 -5.310  18.299 1.00 25.45 ? 5   LYS   A CG    1 
ATOM   43   C  CD    . LYS   A 1 8   ? 16.951 -6.442  19.191 1.00 28.21 ? 5   LYS   A CD    1 
ATOM   44   C  CE    . LYS   A 1 8   ? 15.740 -6.892  20.008 1.00 34.49 ? 5   LYS   A CE    1 
ATOM   45   N  NZ    . LYS   A 1 8   ? 14.433 -6.537  19.395 1.00 35.30 ? 5   LYS   A NZ    1 
ATOM   46   N  N     . LEU   A 1 9   ? 20.921 -2.938  18.413 1.00 18.00 ? 6   LEU   A N     1 
ATOM   47   C  CA    . LEU   A 1 9   ? 22.262 -2.557  17.909 1.00 16.17 ? 6   LEU   A CA    1 
ATOM   48   C  C     . LEU   A 1 9   ? 23.160 -3.792  17.915 1.00 17.05 ? 6   LEU   A C     1 
ATOM   49   O  O     . LEU   A 1 9   ? 23.109 -4.673  18.784 1.00 17.69 ? 6   LEU   A O     1 
ATOM   50   C  CB    . LEU   A 1 9   ? 22.846 -1.424  18.735 1.00 15.96 ? 6   LEU   A CB    1 
ATOM   51   C  CG    . LEU   A 1 9   ? 21.943 -0.229  19.004 1.00 19.37 ? 6   LEU   A CG    1 
ATOM   52   C  CD1   . LEU   A 1 9   ? 22.688 0.892   19.730 1.00 20.15 ? 6   LEU   A CD1   1 
ATOM   53   C  CD2   . LEU   A 1 9   ? 21.319 0.299   17.715 1.00 20.09 ? 6   LEU   A CD2   1 
ATOM   54   N  N     . VAL   A 1 10  ? 24.011 -3.846  16.886 1.00 16.86 ? 7   VAL   A N     1 
ATOM   55   C  CA    . VAL   A 1 10  ? 24.973 -4.959  16.745 1.00 15.47 ? 7   VAL   A CA    1 
ATOM   56   C  C     . VAL   A 1 10  ? 26.374 -4.364  16.538 1.00 15.40 ? 7   VAL   A C     1 
ATOM   57   O  O     . VAL   A 1 10  ? 26.536 -3.419  15.731 1.00 15.76 ? 7   VAL   A O     1 
ATOM   58   C  CB    . VAL   A 1 10  ? 24.651 -5.908  15.594 1.00 17.65 ? 7   VAL   A CB    1 
ATOM   59   C  CG1   . VAL   A 1 10  ? 25.557 -7.128  15.655 1.00 17.73 ? 7   VAL   A CG1   1 
ATOM   60   C  CG2   . VAL   A 1 10  ? 23.183 -6.314  15.602 1.00 17.45 ? 7   VAL   A CG2   1 
ATOM   61   N  N     . VAL   A 1 11  ? 27.319 -4.846  17.330 1.00 14.22 ? 8   VAL   A N     1 
ATOM   62   C  CA    . VAL   A 1 11  ? 28.749 -4.418  17.190 1.00 14.50 ? 8   VAL   A CA    1 
ATOM   63   C  C     . VAL   A 1 11  ? 29.521 -5.550  16.526 1.00 16.13 ? 8   VAL   A C     1 
ATOM   64   O  O     . VAL   A 1 11  ? 29.533 -6.682  17.039 1.00 16.56 ? 8   VAL   A O     1 
ATOM   65   C  CB    . VAL   A 1 11  ? 29.349 -4.110  18.566 1.00 16.12 ? 8   VAL   A CB    1 
ATOM   66   C  CG1   . VAL   A 1 11  ? 30.763 -3.545  18.464 1.00 17.65 ? 8   VAL   A CG1   1 
ATOM   67   C  CG2   . VAL   A 1 11  ? 28.467 -3.172  19.372 1.00 17.27 ? 8   VAL   A CG2   1 
ATOM   68   N  N     . VAL   A 1 12  ? 30.034 -5.248  15.305 1.00 15.66 ? 9   VAL   A N     1 
ATOM   69   C  CA    . VAL   A 1 12  ? 30.760 -6.256  14.470 1.00 15.59 ? 9   VAL   A CA    1 
ATOM   70   C  C     . VAL   A 1 12  ? 32.177 -5.739  14.143 1.00 15.40 ? 9   VAL   A C     1 
ATOM   71   O  O     . VAL   A 1 12  ? 32.460 -4.542  14.268 1.00 16.55 ? 9   VAL   A O     1 
ATOM   72   C  CB    . VAL   A 1 12  ? 30.008 -6.603  13.175 1.00 15.20 ? 9   VAL   A CB    1 
ATOM   73   C  CG1   . VAL   A 1 12  ? 28.624 -7.118  13.497 1.00 16.70 ? 9   VAL   A CG1   1 
ATOM   74   C  CG2   . VAL   A 1 12  ? 29.935 -5.411  12.224 1.00 16.63 ? 9   VAL   A CG2   1 
ATOM   75   N  N     . GLY   A 1 13  ? 33.024 -6.694  13.728 1.00 15.64 ? 10  GLY   A N     1 
ATOM   76   C  CA    . GLY   A 1 13  ? 34.399 -6.336  13.366 1.00 15.46 ? 10  GLY   A CA    1 
ATOM   77   C  C     . GLY   A 1 13  ? 35.309 -7.462  13.693 1.00 16.76 ? 10  GLY   A C     1 
ATOM   78   O  O     . GLY   A 1 13  ? 34.953 -8.443  14.341 1.00 17.06 ? 10  GLY   A O     1 
ATOM   79   N  N     . ALA   A 1 14  ? 36.555 -7.312  13.226 1.00 16.99 ? 11  ALA   A N     1 
ATOM   80   C  CA    . ALA   A 1 14  ? 37.543 -8.397  13.353 1.00 18.09 ? 11  ALA   A CA    1 
ATOM   81   C  C     . ALA   A 1 14  ? 37.971 -8.662  14.801 1.00 19.35 ? 11  ALA   A C     1 
ATOM   82   O  O     . ALA   A 1 14  ? 37.809 -7.822  15.639 1.00 20.02 ? 11  ALA   A O     1 
ATOM   83   C  CB    . ALA   A 1 14  ? 38.744 -8.053  12.456 1.00 20.85 ? 11  ALA   A CB    1 
ATOM   84   N  N     . GLY   A 1 15  ? 38.664 -9.767  15.008 1.00 21.25 ? 12  GLY   A N     1 
ATOM   85   C  CA    . GLY   A 1 15  ? 39.140 -10.103 16.351 1.00 23.00 ? 12  GLY   A CA    1 
ATOM   86   C  C     . GLY   A 1 15  ? 40.012 -9.036  16.961 1.00 19.91 ? 12  GLY   A C     1 
ATOM   87   O  O     . GLY   A 1 15  ? 40.896 -8.554  16.283 1.00 22.75 ? 12  GLY   A O     1 
ATOM   88   N  N     . GLY   A 1 16  ? 39.807 -8.715  18.242 1.00 21.51 ? 13  GLY   A N     1 
ATOM   89   C  CA    . GLY   A 1 16  ? 40.630 -7.774  19.003 1.00 21.31 ? 13  GLY   A CA    1 
ATOM   90   C  C     . GLY   A 1 16  ? 40.499 -6.317  18.682 1.00 20.11 ? 13  GLY   A C     1 
ATOM   91   O  O     . GLY   A 1 16  ? 41.224 -5.592  19.186 1.00 21.02 ? 13  GLY   A O     1 
ATOM   92   N  N     . VAL   A 1 17  ? 39.514 -5.904  17.898 1.00 17.47 ? 14  VAL   A N     1 
ATOM   93   C  CA    . VAL   A 1 17  ? 39.398 -4.462  17.580 1.00 18.21 ? 14  VAL   A CA    1 
ATOM   94   C  C     . VAL   A 1 17  ? 38.860 -3.648  18.738 1.00 17.49 ? 14  VAL   A C     1 
ATOM   95   O  O     . VAL   A 1 17  ? 39.018 -2.393  18.717 1.00 18.04 ? 14  VAL   A O     1 
ATOM   96   C  CB    . VAL   A 1 17  ? 38.587 -4.201  16.312 1.00 18.09 ? 14  VAL   A CB    1 
ATOM   97   C  CG1   . VAL   A 1 17  ? 39.210 -4.842  15.084 1.00 16.54 ? 14  VAL   A CG1   1 
ATOM   98   C  CG2   . VAL   A 1 17  ? 37.144 -4.656  16.439 1.00 16.59 ? 14  VAL   A CG2   1 
ATOM   99   N  N     . GLY   A 1 18  ? 38.188 -4.339  19.672 1.00 17.77 ? 15  GLY   A N     1 
ATOM   100  C  CA    . GLY   A 1 18  ? 37.635 -3.590  20.817 1.00 18.52 ? 15  GLY   A CA    1 
ATOM   101  C  C     . GLY   A 1 18  ? 36.103 -3.602  20.879 1.00 18.10 ? 15  GLY   A C     1 
ATOM   102  O  O     . GLY   A 1 18  ? 35.614 -2.739  21.547 1.00 19.04 ? 15  GLY   A O     1 
ATOM   103  N  N     . LYS   A 1 19  ? 35.468 -4.561  20.249 1.00 16.86 ? 16  LYS   A N     1 
ATOM   104  C  CA    . LYS   A 1 19  ? 33.971 -4.631  20.261 1.00 15.99 ? 16  LYS   A CA    1 
ATOM   105  C  C     . LYS   A 1 19  ? 33.466 -4.764  21.718 1.00 19.05 ? 16  LYS   A C     1 
ATOM   106  O  O     . LYS   A 1 19  ? 32.676 -3.931  22.094 1.00 17.51 ? 16  LYS   A O     1 
ATOM   107  C  CB    . LYS   A 1 19  ? 33.556 -5.846  19.452 1.00 17.75 ? 16  LYS   A CB    1 
ATOM   108  C  CG    . LYS   A 1 19  ? 33.828 -5.742  17.938 1.00 19.78 ? 16  LYS   A CG    1 
ATOM   109  C  CD    . LYS   A 1 19  ? 33.377 -6.928  17.146 1.00 19.77 ? 16  LYS   A CD    1 
ATOM   110  C  CE    . LYS   A 1 19  ? 33.939 -8.257  17.551 1.00 19.35 ? 16  LYS   A CE    1 
ATOM   111  N  NZ    . LYS   A 1 19  ? 35.444 -8.294  17.415 1.00 19.16 ? 16  LYS   A NZ    1 
ATOM   112  N  N     . SER   A 1 20  ? 33.983 -5.729  22.438 1.00 17.95 ? 17  SER   A N     1 
ATOM   113  C  CA    . SER   A 1 20  ? 33.550 -5.922  23.851 1.00 17.18 ? 17  SER   A CA    1 
ATOM   114  C  C     . SER   A 1 20  ? 33.927 -4.700  24.673 1.00 18.43 ? 17  SER   A C     1 
ATOM   115  O  O     . SER   A 1 20  ? 33.098 -4.232  25.469 1.00 19.58 ? 17  SER   A O     1 
ATOM   116  C  CB    . SER   A 1 20  ? 34.116 -7.165  24.398 1.00 18.77 ? 17  SER   A CB    1 
ATOM   117  O  OG    . SER   A 1 20  ? 33.681 -8.251  23.641 1.00 20.60 ? 17  SER   A OG    1 
ATOM   118  N  N     . ALA   A 1 21  ? 35.132 -4.158  24.538 1.00 17.99 ? 18  ALA   A N     1 
ATOM   119  C  CA    . ALA   A 1 21  ? 35.545 -2.999  25.343 1.00 19.16 ? 18  ALA   A CA    1 
ATOM   120  C  C     . ALA   A 1 21  ? 34.658 -1.792  25.057 1.00 18.87 ? 18  ALA   A C     1 
ATOM   121  O  O     . ALA   A 1 21  ? 34.350 -1.063  25.995 1.00 20.23 ? 18  ALA   A O     1 
ATOM   122  C  CB    . ALA   A 1 21  ? 37.049 -2.691  25.159 1.00 20.59 ? 18  ALA   A CB    1 
ATOM   123  N  N     . LEU   A 1 22  ? 34.284 -1.557  23.814 1.00 18.42 ? 19  LEU   A N     1 
ATOM   124  C  CA    . LEU   A 1 22  ? 33.388 -0.410  23.500 1.00 17.73 ? 19  LEU   A CA    1 
ATOM   125  C  C     . LEU   A 1 22  ? 32.020 -0.617  24.179 1.00 19.65 ? 19  LEU   A C     1 
ATOM   126  O  O     . LEU   A 1 22  ? 31.477 0.375   24.717 1.00 18.44 ? 19  LEU   A O     1 
ATOM   127  C  CB    . LEU   A 1 22  ? 33.188 -0.308  21.991 1.00 17.36 ? 19  LEU   A CB    1 
ATOM   128  C  CG    . LEU   A 1 22  ? 34.373 0.327   21.272 1.00 17.48 ? 19  LEU   A CG    1 
ATOM   129  C  CD1   . LEU   A 1 22  ? 34.248 0.121   19.783 1.00 18.96 ? 19  LEU   A CD1   1 
ATOM   130  C  CD2   . LEU   A 1 22  ? 34.463 1.804   21.564 1.00 18.44 ? 19  LEU   A CD2   1 
ATOM   131  N  N     . THR   A 1 23  ? 31.494 -1.808  24.051 1.00 18.28 ? 20  THR   A N     1 
ATOM   132  C  CA    . THR   A 1 23  ? 30.155 -2.127  24.656 1.00 18.64 ? 20  THR   A CA    1 
ATOM   133  C  C     . THR   A 1 23  ? 30.200 -1.978  26.189 1.00 19.75 ? 20  THR   A C     1 
ATOM   134  O  O     . THR   A 1 23  ? 29.347 -1.288  26.689 1.00 21.98 ? 20  THR   A O     1 
ATOM   135  C  CB    . THR   A 1 23  ? 29.740 -3.515  24.213 1.00 18.87 ? 20  THR   A CB    1 
ATOM   136  O  OG1   . THR   A 1 23  ? 29.736 -3.602  22.790 1.00 20.02 ? 20  THR   A OG1   1 
ATOM   137  C  CG2   . THR   A 1 23  ? 28.328 -3.855  24.663 1.00 19.74 ? 20  THR   A CG2   1 
ATOM   138  N  N     . ILE   A 1 24  ? 31.163 -2.575  26.863 1.00 20.17 ? 21  ILE   A N     1 
ATOM   139  C  CA    . ILE   A 1 24  ? 31.302 -2.478  28.352 1.00 20.76 ? 21  ILE   A CA    1 
ATOM   140  C  C     . ILE   A 1 24  ? 31.545 -1.040  28.750 1.00 20.78 ? 21  ILE   A C     1 
ATOM   141  O  O     . ILE   A 1 24  ? 31.066 -0.604  29.733 1.00 20.21 ? 21  ILE   A O     1 
ATOM   142  C  CB    . ILE   A 1 24  ? 32.344 -3.467  28.856 1.00 21.57 ? 21  ILE   A CB    1 
ATOM   143  C  CG1   . ILE   A 1 24  ? 31.865 -4.847  28.466 1.00 22.21 ? 21  ILE   A CG1   1 
ATOM   144  C  CG2   . ILE   A 1 24  ? 32.595 -3.308  30.352 1.00 26.58 ? 21  ILE   A CG2   1 
ATOM   145  C  CD1   . ILE   A 1 24  ? 32.791 -5.943  28.648 1.00 30.48 ? 21  ILE   A CD1   1 
ATOM   146  N  N     . GLN   A 1 25  ? 32.252 -0.286  27.925 1.00 20.11 ? 22  GLN   A N     1 
ATOM   147  C  CA    . GLN   A 1 25  ? 32.477 1.136   28.280 1.00 20.81 ? 22  GLN   A CA    1 
ATOM   148  C  C     . GLN   A 1 25  ? 31.121 1.861   28.231 1.00 22.85 ? 22  GLN   A C     1 
ATOM   149  O  O     . GLN   A 1 25  ? 30.860 2.640   29.169 1.00 24.60 ? 22  GLN   A O     1 
ATOM   150  C  CB    . GLN   A 1 25  ? 33.544 1.627   27.296 1.00 22.37 ? 22  GLN   A CB    1 
ATOM   151  C  CG    . GLN   A 1 25  ? 34.149 2.949   27.601 1.00 26.57 ? 22  GLN   A CG    1 
ATOM   152  C  CD    . GLN   A 1 25  ? 34.687 3.242   28.967 1.00 23.68 ? 22  GLN   A CD    1 
ATOM   153  O  OE1   . GLN   A 1 25  ? 33.917 3.624   29.846 1.00 28.10 ? 22  GLN   A OE1   1 
ATOM   154  N  NE2   . GLN   A 1 25  ? 35.970 3.094   29.227 1.00 26.23 ? 22  GLN   A NE2   1 
ATOM   155  N  N     . LEU   A 1 26  ? 30.286 1.615   27.234 1.00 21.52 ? 23  LEU   A N     1 
ATOM   156  C  CA    . LEU   A 1 26  ? 28.960 2.276   27.195 1.00 22.69 ? 23  LEU   A CA    1 
ATOM   157  C  C     . LEU   A 1 26  ? 28.116 1.821   28.399 1.00 21.21 ? 23  LEU   A C     1 
ATOM   158  O  O     . LEU   A 1 26  ? 27.516 2.667   28.935 1.00 24.65 ? 23  LEU   A O     1 
ATOM   159  C  CB    . LEU   A 1 26  ? 28.223 1.869   25.927 1.00 21.39 ? 23  LEU   A CB    1 
ATOM   160  C  CG    . LEU   A 1 26  ? 26.947 2.657   25.662 1.00 22.09 ? 23  LEU   A CG    1 
ATOM   161  C  CD1   . LEU   A 1 26  ? 27.200 4.071   25.231 1.00 22.20 ? 23  LEU   A CD1   1 
ATOM   162  C  CD2   . LEU   A 1 26  ? 26.019 1.955   24.706 1.00 21.46 ? 23  LEU   A CD2   1 
ATOM   163  N  N     . ILE   A 1 27  ? 28.156 0.544   28.701 1.00 21.92 ? 24  ILE   A N     1 
ATOM   164  C  CA    . ILE   A 1 27  ? 27.269 -0.005  29.781 1.00 22.23 ? 24  ILE   A CA    1 
ATOM   165  C  C     . ILE   A 1 27  ? 27.839 0.367   31.157 1.00 26.29 ? 24  ILE   A C     1 
ATOM   166  O  O     . ILE   A 1 27  ? 27.082 0.931   32.006 1.00 26.00 ? 24  ILE   A O     1 
ATOM   167  C  CB    . ILE   A 1 27  ? 27.200 -1.522  29.619 1.00 23.26 ? 24  ILE   A CB    1 
ATOM   168  C  CG1   . ILE   A 1 27  ? 26.507 -1.935  28.328 1.00 23.07 ? 24  ILE   A CG1   1 
ATOM   169  C  CG2   . ILE   A 1 27  ? 26.568 -2.200  30.844 1.00 25.71 ? 24  ILE   A CG2   1 
ATOM   170  C  CD1   . ILE   A 1 27  ? 25.145 -1.272  28.096 1.00 23.76 ? 24  ILE   A CD1   1 
ATOM   171  N  N     . GLN   A 1 28  ? 29.076 0.016   31.443 1.00 24.15 ? 25  GLN   A N     1 
ATOM   172  C  CA    . GLN   A 1 28  ? 29.631 0.177   32.810 1.00 22.47 ? 25  GLN   A CA    1 
ATOM   173  C  C     . GLN   A 1 28  ? 30.414 1.445   33.081 1.00 25.13 ? 25  GLN   A C     1 
ATOM   174  O  O     . GLN   A 1 28  ? 30.823 1.618   34.205 1.00 24.05 ? 25  GLN   A O     1 
ATOM   175  C  CB    . GLN   A 1 28  ? 30.585 -0.958  33.096 1.00 22.88 ? 25  GLN   A CB    1 
ATOM   176  C  CG    . GLN   A 1 28  ? 29.995 -2.328  32.935 1.00 23.14 ? 25  GLN   A CG    1 
ATOM   177  C  CD    . GLN   A 1 28  ? 30.987 -3.354  33.393 1.00 25.61 ? 25  GLN   A CD    1 
ATOM   178  O  OE1   . GLN   A 1 28  ? 32.026 -3.018  33.869 1.00 29.66 ? 25  GLN   A OE1   1 
ATOM   179  N  NE2   . GLN   A 1 28  ? 30.658 -4.606  33.311 1.00 28.53 ? 25  GLN   A NE2   1 
ATOM   180  N  N     . ASN   A 1 29  ? 30.770 2.178   32.015 1.00 24.39 ? 26  ASN   A N     1 
ATOM   181  C  CA    . ASN   A 1 29  ? 31.624 3.390   32.083 1.00 26.39 ? 26  ASN   A CA    1 
ATOM   182  C  C     . ASN   A 1 29  ? 33.008 2.968   32.538 1.00 25.13 ? 26  ASN   A C     1 
ATOM   183  O  O     . ASN   A 1 29  ? 33.647 3.746   33.044 1.00 26.84 ? 26  ASN   A O     1 
ATOM   184  C  CB    . ASN   A 1 29  ? 31.080 4.527   32.959 1.00 28.54 ? 26  ASN   A CB    1 
ATOM   185  C  CG    . ASN   A 1 29  ? 30.200 5.460   32.198 1.00 33.30 ? 26  ASN   A CG    1 
ATOM   186  O  OD1   . ASN   A 1 29  ? 30.596 6.568   31.940 1.00 42.40 ? 26  ASN   A OD1   1 
ATOM   187  N  ND2   . ASN   A 1 29  ? 29.039 4.999   31.799 1.00 42.25 ? 26  ASN   A ND2   1 
ATOM   188  N  N     . HIS   A 1 30  ? 33.351 1.732   32.266 1.00 24.12 ? 27  HIS   A N     1 
ATOM   189  C  CA    . HIS   A 1 30  ? 34.592 1.089   32.735 1.00 25.62 ? 27  HIS   A CA    1 
ATOM   190  C  C     . HIS   A 1 30  ? 35.296 0.419   31.562 1.00 23.69 ? 27  HIS   A C     1 
ATOM   191  O  O     . HIS   A 1 30  ? 34.629 -0.164  30.706 1.00 23.51 ? 27  HIS   A O     1 
ATOM   192  C  CB    . HIS   A 1 30  ? 34.225 0.135   33.882 1.00 25.30 ? 27  HIS   A CB    1 
ATOM   193  C  CG    . HIS   A 1 30  ? 35.417 -0.361  34.613 1.00 22.79 ? 27  HIS   A CG    1 
ATOM   194  N  ND1   . HIS   A 1 30  ? 36.155 0.479   35.426 1.00 26.57 ? 27  HIS   A ND1   1 
ATOM   195  C  CD2   . HIS   A 1 30  ? 35.957 -1.596  34.696 1.00 24.53 ? 27  HIS   A CD2   1 
ATOM   196  C  CE1   . HIS   A 1 30  ? 37.207 -0.201  35.874 1.00 24.87 ? 27  HIS   A CE1   1 
ATOM   197  N  NE2   . HIS   A 1 30  ? 37.076 -1.487  35.485 1.00 25.90 ? 27  HIS   A NE2   1 
ATOM   198  N  N     . PHE   A 1 31  ? 36.635 0.484   31.630 1.00 25.49 ? 28  PHE   A N     1 
ATOM   199  C  CA    . PHE   A 1 31  ? 37.498 -0.181  30.605 1.00 22.91 ? 28  PHE   A CA    1 
ATOM   200  C  C     . PHE   A 1 31  ? 37.845 -1.529  31.175 1.00 24.52 ? 28  PHE   A C     1 
ATOM   201  O  O     . PHE   A 1 31  ? 38.551 -1.613  32.128 1.00 28.20 ? 28  PHE   A O     1 
ATOM   202  C  CB    . PHE   A 1 31  ? 38.747 0.625   30.243 1.00 22.38 ? 28  PHE   A CB    1 
ATOM   203  C  CG    . PHE   A 1 31  ? 39.673 0.014   29.203 1.00 22.34 ? 28  PHE   A CG    1 
ATOM   204  C  CD1   . PHE   A 1 31  ? 39.225 -0.269  27.932 1.00 23.10 ? 28  PHE   A CD1   1 
ATOM   205  C  CD2   . PHE   A 1 31  ? 40.989 -0.264  29.508 1.00 24.87 ? 28  PHE   A CD2   1 
ATOM   206  C  CE1   . PHE   A 1 31  ? 40.081 -0.791  26.966 1.00 25.26 ? 28  PHE   A CE1   1 
ATOM   207  C  CE2   . PHE   A 1 31  ? 41.842 -0.790  28.548 1.00 25.42 ? 28  PHE   A CE2   1 
ATOM   208  C  CZ    . PHE   A 1 31  ? 41.380 -1.060  27.292 1.00 27.83 ? 28  PHE   A CZ    1 
ATOM   209  N  N     . VAL   A 1 32  ? 37.373 -2.541  30.481 1.00 31.23 ? 29  VAL   A N     1 
ATOM   210  C  CA    . VAL   A 1 32  ? 37.503 -3.973  30.827 1.00 39.88 ? 29  VAL   A CA    1 
ATOM   211  C  C     . VAL   A 1 32  ? 38.993 -4.320  30.845 1.00 41.03 ? 29  VAL   A C     1 
ATOM   212  O  O     . VAL   A 1 32  ? 39.682 -3.872  29.962 1.00 49.31 ? 29  VAL   A O     1 
ATOM   213  C  CB    . VAL   A 1 32  ? 36.781 -4.767  29.726 1.00 44.81 ? 29  VAL   A CB    1 
ATOM   214  C  CG1   . VAL   A 1 32  ? 37.314 -4.345  28.367 1.00 43.05 ? 29  VAL   A CG1   1 
ATOM   215  C  CG2   . VAL   A 1 32  ? 36.924 -6.264  29.902 1.00 49.30 ? 29  VAL   A CG2   1 
ATOM   216  N  N     . ASP   A 1 33  ? 39.466 -5.079  31.823 1.00 44.02 ? 30  ASP   A N     1 
ATOM   217  C  CA    . ASP   A 1 33  ? 40.892 -5.471  31.694 1.00 43.93 ? 30  ASP   A CA    1 
ATOM   218  C  C     . ASP   A 1 33  ? 40.926 -6.869  31.093 1.00 40.00 ? 30  ASP   A C     1 
ATOM   219  O  O     . ASP   A 1 33  ? 41.989 -7.422  31.192 1.00 39.63 ? 30  ASP   A O     1 
ATOM   220  C  CB    . ASP   A 1 33  ? 41.649 -5.393  33.016 1.00 49.14 ? 30  ASP   A CB    1 
ATOM   221  C  CG    . ASP   A 1 33  ? 40.859 -5.950  34.181 1.00 40.38 ? 30  ASP   A CG    1 
ATOM   222  O  OD1   . ASP   A 1 33  ? 40.519 -7.133  34.151 1.00 49.30 ? 30  ASP   A OD1   1 
ATOM   223  O  OD2   . ASP   A 1 33  ? 40.543 -5.161  35.062 1.00 52.87 ? 30  ASP   A OD2   1 
ATOM   224  N  N     . ILE   A 1 39  ? 32.794 -13.193 27.175 1.00 48.45 ? 36  ILE   A N     1 
ATOM   225  C  CA    . ILE   A 1 39  ? 31.787 -14.061 26.492 1.00 47.71 ? 36  ILE   A CA    1 
ATOM   226  C  C     . ILE   A 1 39  ? 30.817 -13.157 25.711 1.00 46.41 ? 36  ILE   A C     1 
ATOM   227  O  O     . ILE   A 1 39  ? 30.387 -12.151 26.257 1.00 43.91 ? 36  ILE   A O     1 
ATOM   228  C  CB    . ILE   A 1 39  ? 31.056 -14.912 27.545 1.00 51.34 ? 36  ILE   A CB    1 
ATOM   229  C  CG1   . ILE   A 1 39  ? 30.190 -16.006 26.914 1.00 55.69 ? 36  ILE   A CG1   1 
ATOM   230  C  CG2   . ILE   A 1 39  ? 30.277 -14.006 28.480 1.00 58.14 ? 36  ILE   A CG2   1 
ATOM   231  C  CD1   . ILE   A 1 39  ? 29.468 -16.898 27.926 1.00 52.20 ? 36  ILE   A CD1   1 
ATOM   232  N  N     . GLU   A 1 40  ? 30.518 -13.492 24.463 1.00 40.10 ? 37  GLU   A N     1 
ATOM   233  C  CA    . GLU   A 1 40  ? 29.632 -12.594 23.689 1.00 35.42 ? 37  GLU   A CA    1 
ATOM   234  C  C     . GLU   A 1 40  ? 28.189 -12.657 24.193 1.00 38.28 ? 37  GLU   A C     1 
ATOM   235  O  O     . GLU   A 1 40  ? 27.555 -13.721 24.107 1.00 46.26 ? 37  GLU   A O     1 
ATOM   236  C  CB    . GLU   A 1 40  ? 29.742 -12.904 22.196 1.00 33.66 ? 37  GLU   A CB    1 
ATOM   237  C  CG    . GLU   A 1 40  ? 31.048 -12.414 21.618 1.00 33.26 ? 37  GLU   A CG    1 
ATOM   238  C  CD    . GLU   A 1 40  ? 32.056 -13.521 21.790 1.00 39.56 ? 37  GLU   A CD    1 
ATOM   239  O  OE1   . GLU   A 1 40  ? 31.656 -14.673 21.991 1.00 44.50 ? 37  GLU   A OE1   1 
ATOM   240  O  OE2   . GLU   A 1 40  ? 33.232 -13.228 21.689 1.00 40.61 ? 37  GLU   A OE2   1 
ATOM   241  N  N     . ASP   A 1 41  ? 27.695 -11.498 24.596 1.00 31.91 ? 38  ASP   A N     1 
ATOM   242  C  CA    . ASP   A 1 41  ? 26.297 -11.465 25.065 1.00 31.43 ? 38  ASP   A CA    1 
ATOM   243  C  C     . ASP   A 1 41  ? 25.645 -10.177 24.590 1.00 23.97 ? 38  ASP   A C     1 
ATOM   244  O  O     . ASP   A 1 41  ? 26.170 -9.491  23.738 1.00 23.99 ? 38  ASP   A O     1 
ATOM   245  C  CB    . ASP   A 1 41  ? 26.205 -11.547 26.591 1.00 35.03 ? 38  ASP   A CB    1 
ATOM   246  C  CG    . ASP   A 1 41  ? 25.065 -12.439 27.118 1.00 40.72 ? 38  ASP   A CG    1 
ATOM   247  O  OD1   . ASP   A 1 41  ? 23.983 -12.471 26.518 1.00 38.40 ? 38  ASP   A OD1   1 
ATOM   248  O  OD2   . ASP   A 1 41  ? 25.343 -13.173 28.036 1.00 49.74 ? 38  ASP   A OD2   1 
ATOM   249  N  N     . SER   A 1 42  ? 24.482 -9.901  25.170 1.00 27.23 ? 39  SER   A N     1 
ATOM   250  C  CA    . SER   A 1 42  ? 23.649 -8.713  24.901 1.00 24.41 ? 39  SER   A CA    1 
ATOM   251  C  C     . SER   A 1 42  ? 23.551 -7.901  26.187 1.00 22.90 ? 39  SER   A C     1 
ATOM   252  O  O     . SER   A 1 42  ? 23.788 -8.471  27.257 1.00 25.76 ? 39  SER   A O     1 
ATOM   253  C  CB    . SER   A 1 42  ? 22.311 -9.058  24.368 1.00 27.00 ? 39  SER   A CB    1 
ATOM   254  O  OG    . SER   A 1 42  ? 21.702 -9.990  25.231 1.00 30.85 ? 39  SER   A OG    1 
ATOM   255  N  N     . TYR   A 1 43  ? 23.338 -6.619  26.029 1.00 21.38 ? 40  TYR   A N     1 
ATOM   256  C  CA    . TYR   A 1 43  ? 23.362 -5.612  27.110 1.00 22.62 ? 40  TYR   A CA    1 
ATOM   257  C  C     . TYR   A 1 43  ? 22.222 -4.655  26.841 1.00 23.36 ? 40  TYR   A C     1 
ATOM   258  O  O     . TYR   A 1 43  ? 21.882 -4.378  25.703 1.00 23.94 ? 40  TYR   A O     1 
ATOM   259  C  CB    . TYR   A 1 43  ? 24.667 -4.814  27.066 1.00 25.82 ? 40  TYR   A CB    1 
ATOM   260  C  CG    . TYR   A 1 43  ? 25.914 -5.644  27.224 1.00 25.69 ? 40  TYR   A CG    1 
ATOM   261  C  CD1   . TYR   A 1 43  ? 26.505 -6.291  26.157 1.00 23.87 ? 40  TYR   A CD1   1 
ATOM   262  C  CD2   . TYR   A 1 43  ? 26.517 -5.773  28.455 1.00 30.70 ? 40  TYR   A CD2   1 
ATOM   263  C  CE1   . TYR   A 1 43  ? 27.614 -7.090  26.335 1.00 28.56 ? 40  TYR   A CE1   1 
ATOM   264  C  CE2   . TYR   A 1 43  ? 27.655 -6.533  28.632 1.00 32.86 ? 40  TYR   A CE2   1 
ATOM   265  C  CZ    . TYR   A 1 43  ? 28.216 -7.191  27.567 1.00 31.34 ? 40  TYR   A CZ    1 
ATOM   266  O  OH    . TYR   A 1 43  ? 29.325 -7.956  27.743 1.00 30.56 ? 40  TYR   A OH    1 
ATOM   267  N  N     . ARG   A 1 44  ? 21.632 -4.159  27.928 1.00 27.33 ? 41  ARG   A N     1 
ATOM   268  C  CA    . ARG   A 1 44  ? 20.464 -3.271  27.815 1.00 24.46 ? 41  ARG   A CA    1 
ATOM   269  C  C     . ARG   A 1 44  ? 20.751 -1.961  28.530 1.00 25.45 ? 41  ARG   A C     1 
ATOM   270  O  O     . ARG   A 1 44  ? 21.330 -2.000  29.596 1.00 26.32 ? 41  ARG   A O     1 
ATOM   271  C  CB    . ARG   A 1 44  ? 19.287 -4.016  28.456 1.00 29.29 ? 41  ARG   A CB    1 
ATOM   272  C  CG    . ARG   A 1 44  ? 18.820 -5.161  27.586 1.00 34.81 ? 41  ARG   A CG    1 
ATOM   273  C  CD    . ARG   A 1 44  ? 17.741 -6.082  28.126 1.00 40.17 ? 41  ARG   A CD    1 
ATOM   274  N  NE    . ARG   A 1 44  ? 16.394 -5.558  28.252 1.00 46.92 ? 41  ARG   A NE    1 
ATOM   275  C  CZ    . ARG   A 1 44  ? 15.403 -5.775  27.393 1.00 43.38 ? 41  ARG   A CZ    1 
ATOM   276  N  NH1   . ARG   A 1 44  ? 15.600 -6.456  26.275 1.00 49.12 ? 41  ARG   A NH1   1 
ATOM   277  N  NH2   . ARG   A 1 44  ? 14.207 -5.301  27.664 1.00 52.14 ? 41  ARG   A NH2   1 
ATOM   278  N  N     . LYS   A 1 45  ? 20.331 -0.858  27.972 1.00 22.07 ? 42  LYS   A N     1 
ATOM   279  C  CA    . LYS   A 1 45  ? 20.553 0.457   28.567 1.00 23.44 ? 42  LYS   A CA    1 
ATOM   280  C  C     . LYS   A 1 45  ? 19.505 1.444   28.054 1.00 23.21 ? 42  LYS   A C     1 
ATOM   281  O  O     . LYS   A 1 45  ? 19.324 1.575   26.875 1.00 23.34 ? 42  LYS   A O     1 
ATOM   282  C  CB    . LYS   A 1 45  ? 22.010 0.910   28.387 1.00 25.45 ? 42  LYS   A CB    1 
ATOM   283  C  CG    . LYS   A 1 45  ? 22.318 2.320   28.848 1.00 30.95 ? 42  LYS   A CG    1 
ATOM   284  C  CD    . LYS   A 1 45  ? 23.695 2.890   28.565 1.00 31.84 ? 42  LYS   A CD    1 
ATOM   285  C  CE    . LYS   A 1 45  ? 24.127 3.689   29.774 1.00 35.52 ? 42  LYS   A CE    1 
ATOM   286  N  NZ    . LYS   A 1 45  ? 25.405 4.395   29.655 1.00 35.31 ? 42  LYS   A NZ    1 
ATOM   287  N  N     . GLN   A 1 46  ? 18.704 2.004   28.966 1.00 24.69 ? 43  GLN   A N     1 
ATOM   288  C  CA    . GLN   A 1 46  ? 17.756 3.072   28.609 1.00 25.65 ? 43  GLN   A CA    1 
ATOM   289  C  C     . GLN   A 1 46  ? 18.521 4.390   28.590 1.00 23.32 ? 43  GLN   A C     1 
ATOM   290  O  O     . GLN   A 1 46  ? 19.254 4.721   29.580 1.00 27.78 ? 43  GLN   A O     1 
ATOM   291  C  CB    . GLN   A 1 46  ? 16.605 3.095   29.631 1.00 23.94 ? 43  GLN   A CB    1 
ATOM   292  C  CG    . GLN   A 1 46  ? 15.563 4.177   29.370 1.00 25.67 ? 43  GLN   A CG    1 
ATOM   293  C  CD    . GLN   A 1 46  ? 14.405 4.156   30.320 1.00 23.20 ? 43  GLN   A CD    1 
ATOM   294  O  OE1   . GLN   A 1 46  ? 13.891 3.073   30.523 1.00 25.56 ? 43  GLN   A OE1   1 
ATOM   295  N  NE2   . GLN   A 1 46  ? 14.075 5.358   30.733 1.00 26.43 ? 43  GLN   A NE2   1 
ATOM   296  N  N     . VAL   A 1 47  ? 18.311 5.164   27.531 1.00 23.43 ? 44  VAL   A N     1 
ATOM   297  C  CA    . VAL   A 1 47  ? 19.035 6.442   27.312 1.00 25.31 ? 44  VAL   A CA    1 
ATOM   298  C  C     . VAL   A 1 47  ? 18.018 7.435   26.764 1.00 24.74 ? 44  VAL   A C     1 
ATOM   299  O  O     . VAL   A 1 47  ? 16.976 6.992   26.260 1.00 26.47 ? 44  VAL   A O     1 
ATOM   300  C  CB    . VAL   A 1 47  ? 20.213 6.236   26.344 1.00 27.79 ? 44  VAL   A CB    1 
ATOM   301  C  CG1   . VAL   A 1 47  ? 21.264 5.298   26.925 1.00 27.09 ? 44  VAL   A CG1   1 
ATOM   302  C  CG2   . VAL   A 1 47  ? 19.710 5.693   25.007 1.00 28.23 ? 44  VAL   A CG2   1 
ATOM   303  N  N     . VAL   A 1 48  ? 18.311 8.718   26.873 1.00 26.16 ? 45  VAL   A N     1 
ATOM   304  C  CA    . VAL   A 1 48  ? 17.561 9.813   26.215 1.00 27.32 ? 45  VAL   A CA    1 
ATOM   305  C  C     . VAL   A 1 48  ? 18.498 10.370  25.143 1.00 29.78 ? 45  VAL   A C     1 
ATOM   306  O  O     . VAL   A 1 48  ? 19.622 10.761  25.495 1.00 31.56 ? 45  VAL   A O     1 
ATOM   307  C  CB    . VAL   A 1 48  ? 17.148 10.893  27.232 1.00 29.34 ? 45  VAL   A CB    1 
ATOM   308  C  CG1   . VAL   A 1 48  ? 16.318 11.987  26.597 1.00 30.61 ? 45  VAL   A CG1   1 
ATOM   309  C  CG2   . VAL   A 1 48  ? 16.417 10.312  28.430 1.00 30.18 ? 45  VAL   A CG2   1 
ATOM   310  N  N     . ILE   A 1 49  ? 18.063 10.347  23.891 1.00 25.95 ? 46  ILE   A N     1 
ATOM   311  C  CA    . ILE   A 1 49  ? 18.791 10.936  22.731 1.00 26.21 ? 46  ILE   A CA    1 
ATOM   312  C  C     . ILE   A 1 49  ? 17.845 11.928  22.035 1.00 25.80 ? 46  ILE   A C     1 
ATOM   313  O  O     . ILE   A 1 49  ? 16.728 11.510  21.637 1.00 26.57 ? 46  ILE   A O     1 
ATOM   314  C  CB    . ILE   A 1 49  ? 19.246 9.793   21.805 1.00 26.15 ? 46  ILE   A CB    1 
ATOM   315  C  CG1   . ILE   A 1 49  ? 20.221 8.828   22.481 1.00 26.73 ? 46  ILE   A CG1   1 
ATOM   316  C  CG2   . ILE   A 1 49  ? 19.824 10.354  20.531 1.00 28.43 ? 46  ILE   A CG2   1 
ATOM   317  C  CD1   . ILE   A 1 49  ? 20.378 7.494   21.763 1.00 25.15 ? 46  ILE   A CD1   1 
ATOM   318  N  N     . ASP   A 1 50  ? 18.209 13.205  21.943 1.00 31.57 ? 47  ASP   A N     1 
ATOM   319  C  CA    . ASP   A 1 50  ? 17.387 14.234  21.248 1.00 29.55 ? 47  ASP   A CA    1 
ATOM   320  C  C     . ASP   A 1 50  ? 16.010 14.363  21.909 1.00 31.96 ? 47  ASP   A C     1 
ATOM   321  O  O     . ASP   A 1 50  ? 15.045 14.564  21.172 1.00 29.91 ? 47  ASP   A O     1 
ATOM   322  C  CB    . ASP   A 1 50  ? 17.249 13.894  19.751 1.00 29.89 ? 47  ASP   A CB    1 
ATOM   323  C  CG    . ASP   A 1 50  ? 18.561 14.103  19.037 1.00 27.23 ? 47  ASP   A CG    1 
ATOM   324  O  OD1   . ASP   A 1 50  ? 19.285 15.007  19.508 1.00 33.68 ? 47  ASP   A OD1   1 
ATOM   325  O  OD2   . ASP   A 1 50  ? 18.903 13.323  18.084 1.00 30.02 ? 47  ASP   A OD2   1 
ATOM   326  N  N     . GLY   A 1 51  ? 15.927 14.234  23.239 1.00 38.81 ? 48  GLY   A N     1 
ATOM   327  C  CA    . GLY   A 1 51  ? 14.684 14.412  24.000 1.00 38.38 ? 48  GLY   A CA    1 
ATOM   328  C  C     . GLY   A 1 51  ? 13.759 13.224  23.865 1.00 30.89 ? 48  GLY   A C     1 
ATOM   329  O  O     . GLY   A 1 51  ? 12.606 13.316  24.342 1.00 37.74 ? 48  GLY   A O     1 
ATOM   330  N  N     . GLU   A 1 52  ? 14.199 12.129  23.238 1.00 30.20 ? 49  GLU   A N     1 
ATOM   331  C  CA    . GLU   A 1 52  ? 13.380 10.899  23.138 1.00 30.00 ? 49  GLU   A CA    1 
ATOM   332  C  C     . GLU   A 1 52  ? 14.064 9.763   23.886 1.00 29.16 ? 49  GLU   A C     1 
ATOM   333  O  O     . GLU   A 1 52  ? 15.187 9.468   23.626 1.00 28.61 ? 49  GLU   A O     1 
ATOM   334  C  CB    . GLU   A 1 52  ? 13.138 10.422  21.706 1.00 30.14 ? 49  GLU   A CB    1 
ATOM   335  C  CG    . GLU   A 1 52  ? 12.447 11.446  20.877 1.00 29.57 ? 49  GLU   A CG    1 
ATOM   336  C  CD    . GLU   A 1 52  ? 12.543 11.088  19.427 1.00 40.82 ? 49  GLU   A CD    1 
ATOM   337  O  OE1   . GLU   A 1 52  ? 12.600 9.891   19.123 1.00 41.76 ? 49  GLU   A OE1   1 
ATOM   338  O  OE2   . GLU   A 1 52  ? 12.604 12.014  18.631 1.00 51.76 ? 49  GLU   A OE2   1 
ATOM   339  N  N     . THR   A 1 53  ? 13.316 9.148   24.798 1.00 28.44 ? 50  THR   A N     1 
ATOM   340  C  CA    . THR   A 1 53  ? 13.802 8.017   25.605 1.00 28.10 ? 50  THR   A CA    1 
ATOM   341  C  C     . THR   A 1 53  ? 13.744 6.761   24.747 1.00 25.35 ? 50  THR   A C     1 
ATOM   342  O  O     . THR   A 1 53  ? 12.833 6.611   24.005 1.00 26.89 ? 50  THR   A O     1 
ATOM   343  C  CB    . THR   A 1 53  ? 12.842 7.833   26.801 1.00 28.32 ? 50  THR   A CB    1 
ATOM   344  O  OG1   . THR   A 1 53  ? 12.911 9.092   27.443 1.00 36.13 ? 50  THR   A OG1   1 
ATOM   345  C  CG2   . THR   A 1 53  ? 13.300 6.764   27.748 1.00 30.72 ? 50  THR   A CG2   1 
ATOM   346  N  N     . CYS   A 1 54  ? 14.708 5.887   24.884 1.00 24.17 ? 51  CYS   A N     1 
ATOM   347  C  CA    . CYS   A 1 54  ? 14.620 4.608   24.169 1.00 25.47 ? 51  CYS   A CA    1 
ATOM   348  C  C     . CYS   A 1 54  ? 15.425 3.545   24.882 1.00 24.23 ? 51  CYS   A C     1 
ATOM   349  O  O     . CYS   A 1 54  ? 16.195 3.889   25.722 1.00 22.71 ? 51  CYS   A O     1 
ATOM   350  C  CB    . CYS   A 1 54  ? 15.229 4.696   22.768 1.00 24.89 ? 51  CYS   A CB    1 
ATOM   351  S  SG    . CYS   A 1 54  ? 16.969 5.240   22.745 1.00 25.82 ? 51  CYS   A SG    1 
ATOM   352  N  N     . LEU   A 1 55  ? 15.205 2.314   24.508 1.00 21.41 ? 52  LEU   A N     1 
ATOM   353  C  CA    . LEU   A 1 55  ? 15.968 1.247   25.152 1.00 21.96 ? 52  LEU   A CA    1 
ATOM   354  C  C     . LEU   A 1 55  ? 16.952 0.708   24.100 1.00 21.92 ? 52  LEU   A C     1 
ATOM   355  O  O     . LEU   A 1 55  ? 16.524 0.257   23.143 1.00 21.88 ? 52  LEU   A O     1 
ATOM   356  C  CB    . LEU   A 1 55  ? 14.985 0.173   25.640 1.00 28.34 ? 52  LEU   A CB    1 
ATOM   357  C  CG    . LEU   A 1 55  ? 15.606 -1.006  26.371 1.00 30.75 ? 52  LEU   A CG    1 
ATOM   358  C  CD1   . LEU   A 1 55  ? 16.121 -0.605  27.734 1.00 30.09 ? 52  LEU   A CD1   1 
ATOM   359  C  CD2   . LEU   A 1 55  ? 14.619 -2.160  26.481 1.00 37.76 ? 52  LEU   A CD2   1 
ATOM   360  N  N     . LEU   A 1 56  ? 18.200 0.712   24.472 1.00 20.75 ? 53  LEU   A N     1 
ATOM   361  C  CA    . LEU   A 1 56  ? 19.198 0.101   23.563 1.00 20.93 ? 53  LEU   A CA    1 
ATOM   362  C  C     . LEU   A 1 56  ? 19.386 -1.339  23.986 1.00 20.76 ? 53  LEU   A C     1 
ATOM   363  O  O     . LEU   A 1 56  ? 19.528 -1.586  25.170 1.00 24.69 ? 53  LEU   A O     1 
ATOM   364  C  CB    . LEU   A 1 56  ? 20.521 0.854   23.678 1.00 21.50 ? 53  LEU   A CB    1 
ATOM   365  C  CG    . LEU   A 1 56  ? 20.476 2.361   23.555 1.00 23.07 ? 53  LEU   A CG    1 
ATOM   366  C  CD1   . LEU   A 1 56  ? 21.844 2.996   23.634 1.00 26.02 ? 53  LEU   A CD1   1 
ATOM   367  C  CD2   . LEU   A 1 56  ? 19.741 2.798   22.311 1.00 23.30 ? 53  LEU   A CD2   1 
ATOM   368  N  N     . ASP   A 1 57  ? 19.306 -2.248  23.033 1.00 18.78 ? 54  ASP   A N     1 
ATOM   369  C  CA    . ASP   A 1 57  ? 19.546 -3.686  23.192 1.00 18.43 ? 54  ASP   A CA    1 
ATOM   370  C  C     . ASP   A 1 57  ? 20.774 -3.971  22.304 1.00 21.19 ? 54  ASP   A C     1 
ATOM   371  O  O     . ASP   A 1 57  ? 20.542 -4.121  21.123 1.00 19.79 ? 54  ASP   A O     1 
ATOM   372  C  CB    . ASP   A 1 57  ? 18.297 -4.462  22.775 1.00 21.70 ? 54  ASP   A CB    1 
ATOM   373  C  CG    . ASP   A 1 57  ? 18.340 -5.941  23.014 1.00 23.17 ? 54  ASP   A CG    1 
ATOM   374  O  OD1   . ASP   A 1 57  ? 19.293 -6.437  23.510 1.00 22.82 ? 54  ASP   A OD1   1 
ATOM   375  O  OD2   . ASP   A 1 57  ? 17.336 -6.572  22.738 1.00 30.25 ? 54  ASP   A OD2   1 
ATOM   376  N  N     . ILE   A 1 58  ? 21.893 -4.213  22.939 1.00 18.15 ? 55  ILE   A N     1 
ATOM   377  C  CA    . ILE   A 1 58  ? 23.170 -4.283  22.157 1.00 16.97 ? 55  ILE   A CA    1 
ATOM   378  C  C     . ILE   A 1 58  ? 23.727 -5.697  22.141 1.00 18.42 ? 55  ILE   A C     1 
ATOM   379  O  O     . ILE   A 1 58  ? 23.929 -6.265  23.167 1.00 21.52 ? 55  ILE   A O     1 
ATOM   380  C  CB    . ILE   A 1 58  ? 24.137 -3.268  22.759 1.00 17.38 ? 55  ILE   A CB    1 
ATOM   381  C  CG1   . ILE   A 1 58  ? 23.581 -1.854  22.717 1.00 18.48 ? 55  ILE   A CG1   1 
ATOM   382  C  CG2   . ILE   A 1 58  ? 25.471 -3.370  21.994 1.00 19.78 ? 55  ILE   A CG2   1 
ATOM   383  C  CD1   . ILE   A 1 58  ? 24.284 -0.872  23.566 1.00 23.54 ? 55  ILE   A CD1   1 
ATOM   384  N  N     . LEU   A 1 59  ? 24.046 -6.200  20.942 1.00 16.48 ? 56  LEU   A N     1 
ATOM   385  C  CA    . LEU   A 1 59  ? 24.633 -7.553  20.842 1.00 17.52 ? 56  LEU   A CA    1 
ATOM   386  C  C     . LEU   A 1 59  ? 26.125 -7.384  20.520 1.00 18.95 ? 56  LEU   A C     1 
ATOM   387  O  O     . LEU   A 1 59  ? 26.453 -6.690  19.515 1.00 16.99 ? 56  LEU   A O     1 
ATOM   388  C  CB    . LEU   A 1 59  ? 23.960 -8.351  19.725 1.00 18.06 ? 56  LEU   A CB    1 
ATOM   389  C  CG    . LEU   A 1 59  ? 24.491 -9.758  19.510 1.00 18.18 ? 56  LEU   A CG    1 
ATOM   390  C  CD1   . LEU   A 1 59  ? 24.201 -10.661 20.717 1.00 20.69 ? 56  LEU   A CD1   1 
ATOM   391  C  CD2   . LEU   A 1 59  ? 23.928 -10.319 18.233 1.00 19.55 ? 56  LEU   A CD2   1 
ATOM   392  N  N     . ASP   A 1 60  ? 26.973 -7.926  21.375 1.00 17.17 ? 57  ASP   A N     1 
ATOM   393  C  CA    . ASP   A 1 60  ? 28.448 -8.005  21.169 1.00 18.59 ? 57  ASP   A CA    1 
ATOM   394  C  C     . ASP   A 1 60  ? 28.775 -9.288  20.394 1.00 21.64 ? 57  ASP   A C     1 
ATOM   395  O  O     . ASP   A 1 60  ? 28.497 -10.357 20.845 1.00 31.84 ? 57  ASP   A O     1 
ATOM   396  C  CB    . ASP   A 1 60  ? 29.129 -7.937  22.531 1.00 21.19 ? 57  ASP   A CB    1 
ATOM   397  C  CG    . ASP   A 1 60  ? 30.627 -7.942  22.511 1.00 20.01 ? 57  ASP   A CG    1 
ATOM   398  O  OD1   . ASP   A 1 60  ? 31.165 -7.550  21.446 1.00 20.55 ? 57  ASP   A OD1   1 
ATOM   399  O  OD2   . ASP   A 1 60  ? 31.207 -8.254  23.561 1.00 20.71 ? 57  ASP   A OD2   1 
ATOM   400  N  N     . THR   A 1 61  ? 29.287 -9.147  19.165 1.00 19.65 ? 58  THR   A N     1 
ATOM   401  C  CA    . THR   A 1 61  ? 29.534 -10.350 18.360 1.00 20.04 ? 58  THR   A CA    1 
ATOM   402  C  C     . THR   A 1 61  ? 31.008 -10.764 18.390 1.00 24.27 ? 58  THR   A C     1 
ATOM   403  O  O     . THR   A 1 61  ? 31.807 -10.025 18.884 1.00 25.73 ? 58  THR   A O     1 
ATOM   404  C  CB    . THR   A 1 61  ? 29.097 -10.164 16.902 1.00 20.33 ? 58  THR   A CB    1 
ATOM   405  O  OG1   . THR   A 1 61  ? 29.942 -9.194  16.286 1.00 18.73 ? 58  THR   A OG1   1 
ATOM   406  C  CG2   . THR   A 1 61  ? 27.687 -9.641  16.786 1.00 19.59 ? 58  THR   A CG2   1 
ATOM   407  N  N     . ALA   A 1 62  ? 31.265 -11.940 17.865 1.00 23.79 ? 59  ALA   A N     1 
ATOM   408  C  CA    . ALA   A 1 62  ? 32.643 -12.464 17.807 1.00 27.38 ? 59  ALA   A CA    1 
ATOM   409  C  C     . ALA   A 1 62  ? 33.323 -12.062 16.486 1.00 26.76 ? 59  ALA   A C     1 
ATOM   410  O  O     . ALA   A 1 62  ? 32.682 -11.805 15.502 1.00 26.89 ? 59  ALA   A O     1 
ATOM   411  C  CB    . ALA   A 1 62  ? 32.596 -13.946 18.005 1.00 33.24 ? 59  ALA   A CB    1 
ATOM   412  N  N     . GLY   A 1 63  ? 34.649 -11.992 16.493 1.00 27.02 ? 60  GLY   A N     1 
ATOM   413  C  CA    . GLY   A 1 63  ? 35.397 -11.700 15.260 1.00 30.47 ? 60  GLY   A CA    1 
ATOM   414  C  C     . GLY   A 1 63  ? 35.576 -12.991 14.499 1.00 32.73 ? 60  GLY   A C     1 
ATOM   415  O  O     . GLY   A 1 63  ? 35.726 -12.911 13.272 1.00 46.82 ? 60  GLY   A O     1 
ATOM   416  N  N     . GLU   A 1 66  ? 31.585 -18.162 15.101 1.00 47.42 ? 63  GLU   A N     1 
ATOM   417  C  CA    . GLU   A 1 66  ? 30.100 -18.096 15.083 1.00 42.32 ? 63  GLU   A CA    1 
ATOM   418  C  C     . GLU   A 1 66  ? 29.540 -18.939 13.957 1.00 42.64 ? 63  GLU   A C     1 
ATOM   419  O  O     . GLU   A 1 66  ? 30.107 -19.001 12.858 1.00 48.46 ? 63  GLU   A O     1 
ATOM   420  C  CB    . GLU   A 1 66  ? 29.547 -16.712 14.754 1.00 42.55 ? 63  GLU   A CB    1 
ATOM   421  C  CG    . GLU   A 1 66  ? 29.449 -15.840 15.964 1.00 44.84 ? 63  GLU   A CG    1 
ATOM   422  C  CD    . GLU   A 1 66  ? 29.407 -14.364 15.685 1.00 34.71 ? 63  GLU   A CD    1 
ATOM   423  O  OE1   . GLU   A 1 66  ? 29.434 -14.023 14.544 1.00 33.40 ? 63  GLU   A OE1   1 
ATOM   424  O  OE2   . GLU   A 1 66  ? 29.336 -13.612 16.620 1.00 30.50 ? 63  GLU   A OE2   1 
ATOM   425  N  N     . TYR   A 1 67  ? 28.409 -19.532 14.274 1.00 43.15 ? 64  TYR   A N     1 
ATOM   426  C  CA    . TYR   A 1 67  ? 27.616 -20.342 13.338 1.00 35.47 ? 64  TYR   A CA    1 
ATOM   427  C  C     . TYR   A 1 67  ? 26.965 -19.382 12.348 1.00 32.93 ? 64  TYR   A C     1 
ATOM   428  O  O     . TYR   A 1 67  ? 26.371 -18.420 12.752 1.00 32.38 ? 64  TYR   A O     1 
ATOM   429  C  CB    . TYR   A 1 67  ? 26.590 -21.067 14.198 1.00 36.01 ? 64  TYR   A CB    1 
ATOM   430  C  CG    . TYR   A 1 67  ? 25.554 -21.906 13.505 1.00 29.14 ? 64  TYR   A CG    1 
ATOM   431  C  CD1   . TYR   A 1 67  ? 25.833 -22.793 12.488 1.00 31.44 ? 64  TYR   A CD1   1 
ATOM   432  C  CD2   . TYR   A 1 67  ? 24.263 -21.828 13.950 1.00 34.34 ? 64  TYR   A CD2   1 
ATOM   433  C  CE1   . TYR   A 1 67  ? 24.840 -23.571 11.926 1.00 26.50 ? 64  TYR   A CE1   1 
ATOM   434  C  CE2   . TYR   A 1 67  ? 23.262 -22.566 13.387 1.00 32.46 ? 64  TYR   A CE2   1 
ATOM   435  C  CZ    . TYR   A 1 67  ? 23.541 -23.466 12.392 1.00 24.43 ? 64  TYR   A CZ    1 
ATOM   436  O  OH    . TYR   A 1 67  ? 22.530 -24.191 11.892 1.00 23.31 ? 64  TYR   A OH    1 
ATOM   437  N  N     . SER   A 1 68  ? 27.092 -19.700 11.071 1.00 32.18 ? 65  SER   A N     1 
ATOM   438  C  CA    . SER   A 1 68  ? 26.585 -18.873 9.960  1.00 35.08 ? 65  SER   A CA    1 
ATOM   439  C  C     . SER   A 1 68  ? 25.097 -18.552 10.146 1.00 31.92 ? 65  SER   A C     1 
ATOM   440  O  O     . SER   A 1 68  ? 24.750 -17.408 10.070 1.00 29.07 ? 65  SER   A O     1 
ATOM   441  C  CB    . SER   A 1 68  ? 26.821 -19.607 8.685  1.00 38.40 ? 65  SER   A CB    1 
ATOM   442  O  OG    . SER   A 1 68  ? 26.314 -18.881 7.589  1.00 42.34 ? 65  SER   A OG    1 
ATOM   443  N  N     . ALA   A 1 69  ? 24.262 -19.571 10.341 1.00 30.82 ? 66  ALA   A N     1 
ATOM   444  C  CA    . ALA   A 1 69  ? 22.810 -19.314 10.490 1.00 31.08 ? 66  ALA   A CA    1 
ATOM   445  C  C     . ALA   A 1 69  ? 22.573 -18.317 11.641 1.00 31.76 ? 66  ALA   A C     1 
ATOM   446  O  O     . ALA   A 1 69  ? 21.690 -17.463 11.519 1.00 29.14 ? 66  ALA   A O     1 
ATOM   447  C  CB    . ALA   A 1 69  ? 22.071 -20.606 10.701 1.00 31.21 ? 66  ALA   A CB    1 
ATOM   448  N  N     . MET   A 1 70  ? 23.328 -18.395 12.739 1.00 30.67 ? 67  MET   A N     1 
ATOM   449  C  CA    . MET   A 1 70  ? 23.164 -17.419 13.848 1.00 28.16 ? 67  MET   A CA    1 
ATOM   450  C  C     . MET   A 1 70  ? 23.645 -16.025 13.426 1.00 27.91 ? 67  MET   A C     1 
ATOM   451  O  O     . MET   A 1 70  ? 23.058 -15.044 13.822 1.00 24.07 ? 67  MET   A O     1 
ATOM   452  C  CB    . MET   A 1 70  ? 23.947 -17.852 15.078 1.00 29.81 ? 67  MET   A CB    1 
ATOM   453  C  CG    . MET   A 1 70  ? 23.511 -17.078 16.295 1.00 35.37 ? 67  MET   A CG    1 
ATOM   454  S  SD    . MET   A 1 70  ? 23.885 -17.901 17.846 1.00 45.05 ? 67  MET   A SD    1 
ATOM   455  C  CE    . MET   A 1 70  ? 23.081 -19.468 17.550 1.00 35.38 ? 67  MET   A CE    1 
ATOM   456  N  N     . ARG   A 1 71  ? 24.741 -15.956 12.650 1.00 24.47 ? 68  ARG   A N     1 
ATOM   457  C  CA    . ARG   A 1 71  ? 25.255 -14.647 12.192 1.00 22.45 ? 68  ARG   A CA    1 
ATOM   458  C  C     . ARG   A 1 71  ? 24.195 -13.992 11.318 1.00 20.50 ? 68  ARG   A C     1 
ATOM   459  O  O     . ARG   A 1 71  ? 24.003 -12.850 11.427 1.00 19.35 ? 68  ARG   A O     1 
ATOM   460  C  CB    . ARG   A 1 71  ? 26.564 -14.880 11.411 1.00 27.30 ? 68  ARG   A CB    1 
ATOM   461  C  CG    . ARG   A 1 71  ? 27.176 -13.613 10.837 1.00 29.86 ? 68  ARG   A CG    1 
ATOM   462  C  CD    . ARG   A 1 71  ? 28.190 -13.842 9.691  1.00 35.11 ? 68  ARG   A CD    1 
ATOM   463  N  NE    . ARG   A 1 71  ? 27.503 -14.828 8.897  1.00 39.85 ? 68  ARG   A NE    1 
ATOM   464  C  CZ    . ARG   A 1 71  ? 27.765 -15.298 7.714  1.00 39.11 ? 68  ARG   A CZ    1 
ATOM   465  N  NH1   . ARG   A 1 71  ? 28.831 -14.911 7.049  1.00 44.29 ? 68  ARG   A NH1   1 
ATOM   466  N  NH2   . ARG   A 1 71  ? 26.974 -16.213 7.207  1.00 38.71 ? 68  ARG   A NH2   1 
ATOM   467  N  N     . ASP   A 1 72  ? 23.575 -14.779 10.447 1.00 19.54 ? 69  ASP   A N     1 
ATOM   468  C  CA    . ASP   A 1 72  ? 22.507 -14.253 9.567  1.00 23.14 ? 69  ASP   A CA    1 
ATOM   469  C  C     . ASP   A 1 72  ? 21.340 -13.778 10.454 1.00 23.20 ? 69  ASP   A C     1 
ATOM   470  O  O     . ASP   A 1 72  ? 20.819 -12.759 10.171 1.00 20.00 ? 69  ASP   A O     1 
ATOM   471  C  CB    . ASP   A 1 72  ? 22.034 -15.283 8.535  1.00 26.12 ? 69  ASP   A CB    1 
ATOM   472  C  CG    . ASP   A 1 72  ? 23.064 -15.670 7.466  1.00 30.16 ? 69  ASP   A CG    1 
ATOM   473  O  OD1   . ASP   A 1 72  ? 24.092 -15.045 7.393  1.00 28.48 ? 69  ASP   A OD1   1 
ATOM   474  O  OD2   . ASP   A 1 72  ? 22.821 -16.642 6.811  1.00 35.07 ? 69  ASP   A OD2   1 
ATOM   475  N  N     . GLN   A 1 73  ? 21.045 -14.511 11.517 1.00 21.38 ? 70  GLN   A N     1 
ATOM   476  C  CA    . GLN   A 1 73  ? 19.879 -14.103 12.356 1.00 22.63 ? 70  GLN   A CA    1 
ATOM   477  C  C     . GLN   A 1 73  ? 20.135 -12.759 13.027 1.00 21.88 ? 70  GLN   A C     1 
ATOM   478  O  O     . GLN   A 1 73  ? 19.314 -11.902 12.985 1.00 20.39 ? 70  GLN   A O     1 
ATOM   479  C  CB    . GLN   A 1 73  ? 19.616 -15.144 13.432 1.00 22.14 ? 70  GLN   A CB    1 
ATOM   480  C  CG    . GLN   A 1 73  ? 18.394 -14.760 14.278 1.00 23.99 ? 70  GLN   A CG    1 
ATOM   481  C  CD    . GLN   A 1 73  ? 17.158 -14.659 13.435 1.00 22.85 ? 70  GLN   A CD    1 
ATOM   482  O  OE1   . GLN   A 1 73  ? 16.760 -15.616 12.834 1.00 26.63 ? 70  GLN   A OE1   1 
ATOM   483  N  NE2   . GLN   A 1 73  ? 16.594 -13.494 13.371 1.00 22.68 ? 70  GLN   A NE2   1 
ATOM   484  N  N     . TYR   A 1 74  ? 21.346 -12.566 13.560 1.00 18.76 ? 71  TYR   A N     1 
ATOM   485  C  CA    . TYR   A 1 74  ? 21.627 -11.277 14.232 1.00 19.81 ? 71  TYR   A CA    1 
ATOM   486  C  C     . TYR   A 1 74  ? 21.678 -10.154 13.196 1.00 19.72 ? 71  TYR   A C     1 
ATOM   487  O  O     . TYR   A 1 74  ? 21.393 -9.063  13.456 1.00 18.46 ? 71  TYR   A O     1 
ATOM   488  C  CB    . TYR   A 1 74  ? 22.741 -11.337 15.274 1.00 18.35 ? 71  TYR   A CB    1 
ATOM   489  C  CG    . TYR   A 1 74  ? 24.180 -11.440 14.795 1.00 20.20 ? 71  TYR   A CG    1 
ATOM   490  C  CD1   . TYR   A 1 74  ? 24.752 -10.488 13.961 1.00 17.87 ? 71  TYR   A CD1   1 
ATOM   491  C  CD2   . TYR   A 1 74  ? 24.970 -12.461 15.270 1.00 21.27 ? 71  TYR   A CD2   1 
ATOM   492  C  CE1   . TYR   A 1 74  ? 26.104 -10.585 13.615 1.00 17.79 ? 71  TYR   A CE1   1 
ATOM   493  C  CE2   . TYR   A 1 74  ? 26.317 -12.559 14.950 1.00 21.44 ? 71  TYR   A CE2   1 
ATOM   494  C  CZ    . TYR   A 1 74  ? 26.874 -11.610 14.119 1.00 21.05 ? 71  TYR   A CZ    1 
ATOM   495  O  OH    . TYR   A 1 74  ? 28.204 -11.789 13.822 1.00 20.71 ? 71  TYR   A OH    1 
ATOM   496  N  N     . MET   A 1 75  ? 22.127 -10.502 11.978 1.00 18.60 ? 72  MET   A N     1 
ATOM   497  C  CA    . MET   A 1 75  ? 22.106 -9.486  10.922 1.00 18.86 ? 72  MET   A CA    1 
ATOM   498  C  C     . MET   A 1 75  ? 20.666 -9.144  10.508 1.00 21.59 ? 72  MET   A C     1 
ATOM   499  O  O     . MET   A 1 75  ? 20.405 -8.046  10.226 1.00 20.27 ? 72  MET   A O     1 
ATOM   500  C  CB    . MET   A 1 75  ? 22.976 -9.975  9.756  1.00 19.41 ? 72  MET   A CB    1 
ATOM   501  C  CG    . MET   A 1 75  ? 24.451 -9.943  10.153 1.00 18.33 ? 72  MET   A CG    1 
ATOM   502  S  SD    . MET   A 1 75  ? 25.548 -10.295 8.695  1.00 18.85 ? 72  MET   A SD    1 
ATOM   503  C  CE    . MET   A 1 75  ? 27.117 -10.000 9.504  1.00 19.45 ? 72  MET   A CE    1 
ATOM   504  N  N     . ARG   A 1 76  ? 19.805 -10.140 10.504 1.00 19.64 ? 73  ARG   A N     1 
ATOM   505  C  CA    . ARG   A 1 76  ? 18.369 -9.933  10.150 1.00 20.80 ? 73  ARG   A CA    1 
ATOM   506  C  C     . ARG   A 1 76  ? 17.665 -9.125  11.267 1.00 20.38 ? 73  ARG   A C     1 
ATOM   507  O  O     . ARG   A 1 76  ? 17.043 -8.157  10.979 1.00 20.66 ? 73  ARG   A O     1 
ATOM   508  C  CB    . ARG   A 1 76  ? 17.793 -11.334 9.963  1.00 24.07 ? 73  ARG   A CB    1 
ATOM   509  C  CG    . ARG   A 1 76  ? 16.403 -11.432 9.363  1.00 33.02 ? 73  ARG   A CG    1 
ATOM   510  C  CD    . ARG   A 1 76  ? 16.118 -12.842 8.858  1.00 38.76 ? 73  ARG   A CD    1 
ATOM   511  N  NE    . ARG   A 1 76  ? 16.372 -13.983 9.728  1.00 39.04 ? 73  ARG   A NE    1 
ATOM   512  C  CZ    . ARG   A 1 76  ? 17.277 -14.928 9.533  1.00 40.58 ? 73  ARG   A CZ    1 
ATOM   513  N  NH1   . ARG   A 1 76  ? 17.384 -15.929 10.376 1.00 37.19 ? 73  ARG   A NH1   1 
ATOM   514  N  NH2   . ARG   A 1 76  ? 18.096 -14.871 8.488  1.00 42.19 ? 73  ARG   A NH2   1 
ATOM   515  N  N     . THR   A 1 77  ? 17.963 -9.466  12.504 1.00 21.01 ? 74  THR   A N     1 
ATOM   516  C  CA    . THR   A 1 77  ? 17.310 -8.800  13.672 1.00 20.35 ? 74  THR   A CA    1 
ATOM   517  C  C     . THR   A 1 77  ? 17.896 -7.409  13.895 1.00 20.48 ? 74  THR   A C     1 
ATOM   518  O  O     . THR   A 1 77  ? 17.192 -6.492  14.259 1.00 19.35 ? 74  THR   A O     1 
ATOM   519  C  CB    . THR   A 1 77  ? 17.451 -9.676  14.913 1.00 20.29 ? 74  THR   A CB    1 
ATOM   520  O  OG1   . THR   A 1 77  ? 16.676 -10.834 14.616 1.00 21.34 ? 74  THR   A OG1   1 
ATOM   521  C  CG2   . THR   A 1 77  ? 16.970 -8.973  16.172 1.00 22.39 ? 74  THR   A CG2   1 
ATOM   522  N  N     . GLY   A 1 78  ? 19.209 -7.233  13.644 1.00 16.65 ? 75  GLY   A N     1 
ATOM   523  C  CA    . GLY   A 1 78  ? 19.849 -5.954  13.939 1.00 15.05 ? 75  GLY   A CA    1 
ATOM   524  C  C     . GLY   A 1 78  ? 19.254 -4.794  13.166 1.00 18.04 ? 75  GLY   A C     1 
ATOM   525  O  O     . GLY   A 1 78  ? 19.107 -4.909  11.913 1.00 19.15 ? 75  GLY   A O     1 
ATOM   526  N  N     . GLU   A 1 79  ? 19.065 -3.673  13.838 1.00 17.75 ? 76  GLU   A N     1 
ATOM   527  C  CA    . GLU   A 1 79  ? 18.507 -2.468  13.198 1.00 17.86 ? 76  GLU   A CA    1 
ATOM   528  C  C     . GLU   A 1 79  ? 19.629 -1.514  12.756 1.00 17.90 ? 76  GLU   A C     1 
ATOM   529  O  O     . GLU   A 1 79  ? 19.418 -0.741  11.897 1.00 20.11 ? 76  GLU   A O     1 
ATOM   530  C  CB    . GLU   A 1 79  ? 17.418 -1.826  14.088 1.00 18.52 ? 76  GLU   A CB    1 
ATOM   531  C  CG    . GLU   A 1 79  ? 16.212 -2.728  14.288 1.00 21.39 ? 76  GLU   A CG    1 
ATOM   532  C  CD    . GLU   A 1 79  ? 15.282 -2.192  15.375 1.00 29.87 ? 76  GLU   A CD    1 
ATOM   533  O  OE1   . GLU   A 1 79  ? 15.675 -2.076  16.485 1.00 23.68 ? 76  GLU   A OE1   1 
ATOM   534  O  OE2   . GLU   A 1 79  ? 14.224 -1.845  15.000 1.00 38.53 ? 76  GLU   A OE2   1 
ATOM   535  N  N     . GLY   A 1 80  ? 20.722 -1.565  13.497 1.00 16.37 ? 77  GLY   A N     1 
ATOM   536  C  CA    . GLY   A 1 80  ? 21.866 -0.676  13.237 1.00 19.17 ? 77  GLY   A CA    1 
ATOM   537  C  C     . GLY   A 1 80  ? 23.125 -1.388  13.633 1.00 17.46 ? 77  GLY   A C     1 
ATOM   538  O  O     . GLY   A 1 80  ? 23.135 -2.200  14.499 1.00 15.54 ? 77  GLY   A O     1 
ATOM   539  N  N     . PHE   A 1 81  ? 24.171 -1.162  12.810 1.00 13.71 ? 78  PHE   A N     1 
ATOM   540  C  CA    . PHE   A 1 81  ? 25.476 -1.850  13.015 1.00 14.85 ? 78  PHE   A CA    1 
ATOM   541  C  C     . PHE   A 1 81  ? 26.654 -0.905  13.250 1.00 16.60 ? 78  PHE   A C     1 
ATOM   542  O  O     . PHE   A 1 81  ? 26.851 0.037   12.563 1.00 16.22 ? 78  PHE   A O     1 
ATOM   543  C  CB    . PHE   A 1 81  ? 25.737 -2.772  11.825 1.00 13.57 ? 78  PHE   A CB    1 
ATOM   544  C  CG    . PHE   A 1 81  ? 24.662 -3.811  11.653 1.00 14.40 ? 78  PHE   A CG    1 
ATOM   545  C  CD1   . PHE   A 1 81  ? 23.482 -3.495  11.012 1.00 16.22 ? 78  PHE   A CD1   1 
ATOM   546  C  CD2   . PHE   A 1 81  ? 24.850 -5.077  12.128 1.00 14.64 ? 78  PHE   A CD2   1 
ATOM   547  C  CE1   . PHE   A 1 81  ? 22.489 -4.449  10.934 1.00 15.46 ? 78  PHE   A CE1   1 
ATOM   548  C  CE2   . PHE   A 1 81  ? 23.862 -6.033  12.016 1.00 17.35 ? 78  PHE   A CE2   1 
ATOM   549  C  CZ    . PHE   A 1 81  ? 22.698 -5.700  11.401 1.00 17.53 ? 78  PHE   A CZ    1 
ATOM   550  N  N     . LEU   A 1 82  ? 27.386 -1.192  14.298 1.00 13.99 ? 79  LEU   A N     1 
ATOM   551  C  CA    . LEU   A 1 82  ? 28.684 -0.489  14.487 1.00 13.82 ? 79  LEU   A CA    1 
ATOM   552  C  C     . LEU   A 1 82  ? 29.721 -1.408  13.849 1.00 17.61 ? 79  LEU   A C     1 
ATOM   553  O  O     . LEU   A 1 82  ? 29.912 -2.458  14.295 1.00 16.85 ? 79  LEU   A O     1 
ATOM   554  C  CB    . LEU   A 1 82  ? 29.064 -0.349  15.961 1.00 18.34 ? 79  LEU   A CB    1 
ATOM   555  C  CG    . LEU   A 1 82  ? 28.480 0.799   16.785 1.00 20.53 ? 79  LEU   A CG    1 
ATOM   556  C  CD1   . LEU   A 1 82  ? 29.198 0.933   18.122 1.00 20.32 ? 79  LEU   A CD1   1 
ATOM   557  C  CD2   . LEU   A 1 82  ? 28.441 2.127   16.095 1.00 18.14 ? 79  LEU   A CD2   1 
ATOM   558  N  N     . CYS   A 1 83  ? 30.323 -0.897  12.785 1.00 14.60 ? 80  CYS   A N     1 
ATOM   559  C  CA    . CYS   A 1 83  ? 31.386 -1.664  12.073 1.00 14.55 ? 80  CYS   A CA    1 
ATOM   560  C  C     . CYS   A 1 83  ? 32.738 -1.151  12.561 1.00 16.44 ? 80  CYS   A C     1 
ATOM   561  O  O     . CYS   A 1 83  ? 33.069 -0.059  12.220 1.00 14.74 ? 80  CYS   A O     1 
ATOM   562  C  CB    . CYS   A 1 83  ? 31.194 -1.435  10.584 1.00 14.68 ? 80  CYS   A CB    1 
ATOM   563  S  SG    . CYS   A 1 83  ? 29.644 -2.185  9.990  1.00 19.95 ? 80  CYS   A SG    1 
ATOM   564  N  N     . VAL   A 1 84  ? 33.356 -1.952  13.403 1.00 15.03 ? 81  VAL   A N     1 
ATOM   565  C  CA    . VAL   A 1 84  ? 34.562 -1.517  14.132 1.00 14.90 ? 81  VAL   A CA    1 
ATOM   566  C  C     . VAL   A 1 84  ? 35.829 -2.121  13.496 1.00 16.52 ? 81  VAL   A C     1 
ATOM   567  O  O     . VAL   A 1 84  ? 35.866 -3.239  13.265 1.00 16.12 ? 81  VAL   A O     1 
ATOM   568  C  CB    . VAL   A 1 84  ? 34.442 -1.934  15.612 1.00 14.63 ? 81  VAL   A CB    1 
ATOM   569  C  CG1   . VAL   A 1 84  ? 35.537 -1.270  16.404 1.00 15.68 ? 81  VAL   A CG1   1 
ATOM   570  C  CG2   . VAL   A 1 84  ? 33.049 -1.540  16.175 1.00 16.07 ? 81  VAL   A CG2   1 
ATOM   571  N  N     . PHE   A 1 85  ? 36.771 -1.220  13.361 1.00 14.71 ? 82  PHE   A N     1 
ATOM   572  C  CA    . PHE   A 1 85  ? 38.179 -1.588  13.009 1.00 15.54 ? 82  PHE   A CA    1 
ATOM   573  C  C     . PHE   A 1 85  ? 39.076 -0.930  14.075 1.00 17.43 ? 82  PHE   A C     1 
ATOM   574  O  O     . PHE   A 1 85  ? 38.650 -0.055  14.773 1.00 16.15 ? 82  PHE   A O     1 
ATOM   575  C  CB    . PHE   A 1 85  ? 38.555 -1.239  11.540 1.00 16.41 ? 82  PHE   A CB    1 
ATOM   576  C  CG    . PHE   A 1 85  ? 38.749 0.228   11.345 1.00 16.93 ? 82  PHE   A CG    1 
ATOM   577  C  CD1   . PHE   A 1 85  ? 37.720 1.064   10.994 1.00 16.20 ? 82  PHE   A CD1   1 
ATOM   578  C  CD2   . PHE   A 1 85  ? 40.005 0.800   11.426 1.00 17.28 ? 82  PHE   A CD2   1 
ATOM   579  C  CE1   . PHE   A 1 85  ? 37.884 2.418   10.838 1.00 19.75 ? 82  PHE   A CE1   1 
ATOM   580  C  CE2   . PHE   A 1 85  ? 40.151 2.156   11.314 1.00 19.15 ? 82  PHE   A CE2   1 
ATOM   581  C  CZ    . PHE   A 1 85  ? 39.130 2.971   10.952 1.00 18.49 ? 82  PHE   A CZ    1 
ATOM   582  N  N     . ALA   A 1 86  ? 40.329 -1.400  14.181 1.00 17.58 ? 83  ALA   A N     1 
ATOM   583  C  CA    . ALA   A 1 86  ? 41.297 -0.741  15.068 1.00 17.59 ? 83  ALA   A CA    1 
ATOM   584  C  C     . ALA   A 1 86  ? 42.244 0.073   14.174 1.00 17.90 ? 83  ALA   A C     1 
ATOM   585  O  O     . ALA   A 1 86  ? 42.666 -0.454  13.113 1.00 20.02 ? 83  ALA   A O     1 
ATOM   586  C  CB    . ALA   A 1 86  ? 42.012 -1.740  15.911 1.00 17.60 ? 83  ALA   A CB    1 
ATOM   587  N  N     . ILE   A 1 87  ? 42.634 1.243   14.628 1.00 17.34 ? 84  ILE   A N     1 
ATOM   588  C  CA    . ILE   A 1 87  ? 43.497 2.203   13.861 1.00 18.47 ? 84  ILE   A CA    1 
ATOM   589  C  C     . ILE   A 1 87  ? 44.928 1.668   13.748 1.00 20.27 ? 84  ILE   A C     1 
ATOM   590  O  O     . ILE   A 1 87  ? 45.647 2.221   12.908 1.00 22.72 ? 84  ILE   A O     1 
ATOM   591  C  CB    . ILE   A 1 87  ? 43.429 3.628   14.417 1.00 20.08 ? 84  ILE   A CB    1 
ATOM   592  C  CG1   . ILE   A 1 87  ? 44.100 3.703   15.794 1.00 23.08 ? 84  ILE   A CG1   1 
ATOM   593  C  CG2   . ILE   A 1 87  ? 42.014 4.204   14.343 1.00 20.92 ? 84  ILE   A CG2   1 
ATOM   594  C  CD1   . ILE   A 1 87  ? 44.647 5.046   16.144 1.00 25.68 ? 84  ILE   A CD1   1 
ATOM   595  N  N     . ASN   A 1 88  ? 45.314 0.676   14.511 1.00 19.32 ? 85  ASN   A N     1 
ATOM   596  C  CA    . ASN   A 1 88  ? 46.640 0.045   14.324 1.00 20.10 ? 85  ASN   A CA    1 
ATOM   597  C  C     . ASN   A 1 88  ? 46.506 -1.334  13.669 1.00 22.48 ? 85  ASN   A C     1 
ATOM   598  O  O     . ASN   A 1 88  ? 47.366 -2.157  13.834 1.00 26.50 ? 85  ASN   A O     1 
ATOM   599  C  CB    . ASN   A 1 88  ? 47.329 -0.067  15.665 1.00 24.60 ? 85  ASN   A CB    1 
ATOM   600  C  CG    . ASN   A 1 88  ? 46.604 -0.959  16.648 1.00 22.81 ? 85  ASN   A CG    1 
ATOM   601  O  OD1   . ASN   A 1 88  ? 45.418 -1.202  16.496 1.00 22.40 ? 85  ASN   A OD1   1 
ATOM   602  N  ND2   . ASN   A 1 88  ? 47.317 -1.505  17.595 1.00 24.37 ? 85  ASN   A ND2   1 
ATOM   603  N  N     . ASN   A 1 89  ? 45.447 -1.595  12.934 1.00 20.18 ? 86  ASN   A N     1 
ATOM   604  C  CA    . ASN   A 1 89  ? 45.256 -2.949  12.359 1.00 20.04 ? 86  ASN   A CA    1 
ATOM   605  C  C     . ASN   A 1 89  ? 44.656 -2.763  10.975 1.00 23.38 ? 86  ASN   A C     1 
ATOM   606  O  O     . ASN   A 1 89  ? 43.455 -2.631  10.788 1.00 20.80 ? 86  ASN   A O     1 
ATOM   607  C  CB    . ASN   A 1 89  ? 44.423 -3.879  13.251 1.00 22.08 ? 86  ASN   A CB    1 
ATOM   608  C  CG    . ASN   A 1 89  ? 44.187 -5.275  12.712 1.00 22.06 ? 86  ASN   A CG    1 
ATOM   609  O  OD1   . ASN   A 1 89  ? 44.395 -5.547  11.521 1.00 21.62 ? 86  ASN   A OD1   1 
ATOM   610  N  ND2   . ASN   A 1 89  ? 43.668 -6.161  13.559 1.00 23.35 ? 86  ASN   A ND2   1 
ATOM   611  N  N     . THR   A 1 90  ? 45.505 -2.879  9.955  1.00 23.78 ? 87  THR   A N     1 
ATOM   612  C  CA    . THR   A 1 90  ? 45.107 -2.585  8.538  1.00 23.99 ? 87  THR   A CA    1 
ATOM   613  C  C     . THR   A 1 90  ? 44.172 -3.693  8.074  1.00 20.06 ? 87  THR   A C     1 
ATOM   614  O  O     . THR   A 1 90  ? 43.203 -3.369  7.394  1.00 21.52 ? 87  THR   A O     1 
ATOM   615  C  CB    . THR   A 1 90  ? 46.307 -2.384  7.605  1.00 23.76 ? 87  THR   A CB    1 
ATOM   616  O  OG1   . THR   A 1 90  ? 47.081 -3.547  7.875  1.00 30.49 ? 87  THR   A OG1   1 
ATOM   617  C  CG2   . THR   A 1 90  ? 47.014 -1.070  7.866  1.00 23.92 ? 87  THR   A CG2   1 
ATOM   618  N  N     . LYS   A 1 91  ? 44.386 -4.921  8.512  1.00 20.06 ? 88  LYS   A N     1 
ATOM   619  C  CA    . LYS   A 1 91  ? 43.525 -6.040  8.046  1.00 20.86 ? 88  LYS   A CA    1 
ATOM   620  C  C     . LYS   A 1 91  ? 42.101 -5.762  8.574  1.00 18.59 ? 88  LYS   A C     1 
ATOM   621  O  O     . LYS   A 1 91  ? 41.148 -6.010  7.864  1.00 16.81 ? 88  LYS   A O     1 
ATOM   622  C  CB    . LYS   A 1 91  ? 44.025 -7.419  8.467  1.00 22.82 ? 88  LYS   A CB    1 
ATOM   623  C  CG    . LYS   A 1 91  ? 43.099 -8.573  8.111  1.00 26.49 ? 88  LYS   A CG    1 
ATOM   624  C  CD    . LYS   A 1 91  ? 43.522 -9.919  8.676  1.00 28.92 ? 88  LYS   A CD    1 
ATOM   625  C  CE    . LYS   A 1 91  ? 42.738 -11.095 8.119  1.00 34.79 ? 88  LYS   A CE    1 
ATOM   626  N  NZ    . LYS   A 1 91  ? 41.303 -11.008 8.465  1.00 36.22 ? 88  LYS   A NZ    1 
ATOM   627  N  N     . SER   A 1 92  ? 41.989 -5.298  9.811  1.00 18.21 ? 89  SER   A N     1 
ATOM   628  C  CA    . SER   A 1 92  ? 40.650 -5.052  10.414 1.00 17.12 ? 89  SER   A CA    1 
ATOM   629  C  C     . SER   A 1 92  ? 39.893 -3.991  9.622  1.00 16.33 ? 89  SER   A C     1 
ATOM   630  O  O     . SER   A 1 92  ? 38.640 -4.079  9.430  1.00 15.75 ? 89  SER   A O     1 
ATOM   631  C  CB    . SER   A 1 92  ? 40.817 -4.708  11.885 1.00 15.72 ? 89  SER   A CB    1 
ATOM   632  O  OG    . SER   A 1 92  ? 41.235 -3.384  12.144 1.00 18.10 ? 89  SER   A OG    1 
ATOM   633  N  N     . PHE   A 1 93  ? 40.606 -2.996  9.117  1.00 17.39 ? 90  PHE   A N     1 
ATOM   634  C  CA    . PHE   A 1 93  ? 40.010 -1.930  8.299  1.00 16.49 ? 90  PHE   A CA    1 
ATOM   635  C  C     . PHE   A 1 93  ? 39.582 -2.484  6.942  1.00 17.95 ? 90  PHE   A C     1 
ATOM   636  O  O     . PHE   A 1 93  ? 38.505 -2.227  6.448  1.00 15.85 ? 90  PHE   A O     1 
ATOM   637  C  CB    . PHE   A 1 93  ? 40.997 -0.783  8.143  1.00 15.45 ? 90  PHE   A CB    1 
ATOM   638  C  CG    . PHE   A 1 93  ? 40.500 0.295   7.235  1.00 17.82 ? 90  PHE   A CG    1 
ATOM   639  C  CD1   . PHE   A 1 93  ? 39.489 1.144   7.628  1.00 17.90 ? 90  PHE   A CD1   1 
ATOM   640  C  CD2   . PHE   A 1 93  ? 41.057 0.476   5.958  1.00 19.52 ? 90  PHE   A CD2   1 
ATOM   641  C  CE1   . PHE   A 1 93  ? 39.051 2.178   6.820  1.00 19.82 ? 90  PHE   A CE1   1 
ATOM   642  C  CE2   . PHE   A 1 93  ? 40.535 1.463   5.138  1.00 18.86 ? 90  PHE   A CE2   1 
ATOM   643  C  CZ    . PHE   A 1 93  ? 39.512 2.306   5.538  1.00 21.52 ? 90  PHE   A CZ    1 
ATOM   644  N  N     . GLU   A 1 94  ? 40.465 -3.247  6.288  1.00 19.05 ? 91  GLU   A N     1 
ATOM   645  C  CA    . GLU   A 1 94  ? 40.140 -3.860  4.984  1.00 18.91 ? 91  GLU   A CA    1 
ATOM   646  C  C     . GLU   A 1 94  ? 38.955 -4.806  5.125  1.00 18.14 ? 91  GLU   A C     1 
ATOM   647  O  O     . GLU   A 1 94  ? 38.141 -4.797  4.271  1.00 18.89 ? 91  GLU   A O     1 
ATOM   648  C  CB    . GLU   A 1 94  ? 41.374 -4.603  4.457  1.00 19.01 ? 91  GLU   A CB    1 
ATOM   649  C  CG    . GLU   A 1 94  ? 42.423 -3.614  3.926  1.00 24.44 ? 91  GLU   A CG    1 
ATOM   650  C  CD    . GLU   A 1 94  ? 41.977 -2.624  2.856  1.00 24.61 ? 91  GLU   A CD    1 
ATOM   651  O  OE1   . GLU   A 1 94  ? 41.207 -2.934  2.044  1.00 31.40 ? 91  GLU   A OE1   1 
ATOM   652  O  OE2   . GLU   A 1 94  ? 42.427 -1.548  2.881  1.00 39.29 ? 91  GLU   A OE2   1 
ATOM   653  N  N     . ASP   A 1 95  ? 38.857 -5.480  6.282  1.00 16.42 ? 92  ASP   A N     1 
ATOM   654  C  CA    . ASP   A 1 95  ? 37.758 -6.450  6.558  1.00 17.87 ? 92  ASP   A CA    1 
ATOM   655  C  C     . ASP   A 1 95  ? 36.365 -5.794  6.757  1.00 17.27 ? 92  ASP   A C     1 
ATOM   656  O  O     . ASP   A 1 95  ? 35.454 -6.475  6.520  1.00 17.17 ? 92  ASP   A O     1 
ATOM   657  C  CB    . ASP   A 1 95  ? 38.071 -7.376  7.716  1.00 21.14 ? 92  ASP   A CB    1 
ATOM   658  C  CG    . ASP   A 1 95  ? 39.121 -8.412  7.392  1.00 25.90 ? 92  ASP   A CG    1 
ATOM   659  O  OD1   . ASP   A 1 95  ? 39.432 -8.554  6.223  1.00 26.32 ? 92  ASP   A OD1   1 
ATOM   660  O  OD2   . ASP   A 1 95  ? 39.581 -8.996  8.318  1.00 28.47 ? 92  ASP   A OD2   1 
ATOM   661  N  N     . ILE   A 1 96  ? 36.329 -4.491  6.887  1.00 15.55 ? 93  ILE   A N     1 
ATOM   662  C  CA    . ILE   A 1 96  ? 35.037 -3.741  6.956  1.00 16.37 ? 93  ILE   A CA    1 
ATOM   663  C  C     . ILE   A 1 96  ? 34.206 -4.019  5.688  1.00 15.73 ? 93  ILE   A C     1 
ATOM   664  O  O     . ILE   A 1 96  ? 33.014 -4.153  5.752  1.00 15.55 ? 93  ILE   A O     1 
ATOM   665  C  CB    . ILE   A 1 96  ? 35.276 -2.250  7.186  1.00 16.35 ? 93  ILE   A CB    1 
ATOM   666  C  CG1   . ILE   A 1 96  ? 35.939 -1.943  8.536  1.00 16.92 ? 93  ILE   A CG1   1 
ATOM   667  C  CG2   . ILE   A 1 96  ? 33.990 -1.467  6.972  1.00 17.83 ? 93  ILE   A CG2   1 
ATOM   668  C  CD1   . ILE   A 1 96  ? 35.053 -2.267  9.749  1.00 18.26 ? 93  ILE   A CD1   1 
ATOM   669  N  N     . HIS   A 1 97  ? 34.866 -4.136  4.530  1.00 15.22 ? 94  HIS   A N     1 
ATOM   670  C  CA    . HIS   A 1 97  ? 34.166 -4.462  3.273  1.00 14.79 ? 94  HIS   A CA    1 
ATOM   671  C  C     . HIS   A 1 97  ? 33.329 -5.732  3.468  1.00 17.32 ? 94  HIS   A C     1 
ATOM   672  O  O     . HIS   A 1 97  ? 32.221 -5.732  3.020  1.00 16.13 ? 94  HIS   A O     1 
ATOM   673  C  CB    . HIS   A 1 97  ? 35.266 -4.679  2.170  1.00 15.92 ? 94  HIS   A CB    1 
ATOM   674  C  CG    . HIS   A 1 97  ? 34.740 -5.376  0.961  1.00 17.85 ? 94  HIS   A CG    1 
ATOM   675  N  ND1   . HIS   A 1 97  ? 34.220 -4.701  -0.059 1.00 18.86 ? 94  HIS   A ND1   1 
ATOM   676  C  CD2   . HIS   A 1 97  ? 34.568 -6.668  0.687  1.00 18.62 ? 94  HIS   A CD2   1 
ATOM   677  C  CE1   . HIS   A 1 97  ? 33.754 -5.550  -0.927 1.00 19.72 ? 94  HIS   A CE1   1 
ATOM   678  N  NE2   . HIS   A 1 97  ? 33.983 -6.730  -0.521 1.00 18.98 ? 94  HIS   A NE2   1 
ATOM   679  N  N     . HIS   A 1 98  ? 33.883 -6.730  4.128  1.00 16.17 ? 95  HIS   A N     1 
ATOM   680  C  CA    . HIS   A 1 98  ? 33.267 -8.080  4.272  1.00 16.91 ? 95  HIS   A CA    1 
ATOM   681  C  C     . HIS   A 1 98  ? 32.063 -7.981  5.239  1.00 17.17 ? 95  HIS   A C     1 
ATOM   682  O  O     . HIS   A 1 98  ? 30.992 -8.529  4.907  1.00 16.41 ? 95  HIS   A O     1 
ATOM   683  C  CB    . HIS   A 1 98  ? 34.320 -9.127  4.686  1.00 17.77 ? 95  HIS   A CB    1 
ATOM   684  C  CG    . HIS   A 1 98  ? 35.414 -9.270  3.660  1.00 23.06 ? 95  HIS   A CG    1 
ATOM   685  N  ND1   . HIS   A 1 98  ? 35.404 -10.309 2.757  1.00 31.63 ? 95  HIS   A ND1   1 
ATOM   686  C  CD2   . HIS   A 1 98  ? 36.509 -8.521  3.370  1.00 20.96 ? 95  HIS   A CD2   1 
ATOM   687  C  CE1   . HIS   A 1 98  ? 36.472 -10.243 1.966  1.00 31.89 ? 95  HIS   A CE1   1 
ATOM   688  N  NE2   . HIS   A 1 98  ? 37.187 -9.142  2.320  1.00 21.88 ? 95  HIS   A NE2   1 
ATOM   689  N  N     . TYR   A 1 99  ? 32.208 -7.276  6.346  1.00 15.69 ? 96  TYR   A N     1 
ATOM   690  C  CA    . TYR   A 1 99  ? 31.088 -7.176  7.327  1.00 16.15 ? 96  TYR   A CA    1 
ATOM   691  C  C     . TYR   A 1 99  ? 29.959 -6.396  6.663  1.00 17.53 ? 96  TYR   A C     1 
ATOM   692  O  O     . TYR   A 1 99  ? 28.794 -6.859  6.673  1.00 18.72 ? 96  TYR   A O     1 
ATOM   693  C  CB    . TYR   A 1 99  ? 31.585 -6.473  8.598  1.00 17.13 ? 96  TYR   A CB    1 
ATOM   694  C  CG    . TYR   A 1 99  ? 32.539 -7.328  9.380  1.00 19.23 ? 96  TYR   A CG    1 
ATOM   695  C  CD1   . TYR   A 1 99  ? 32.090 -8.447  10.093 1.00 20.06 ? 96  TYR   A CD1   1 
ATOM   696  C  CD2   . TYR   A 1 99  ? 33.886 -7.035  9.401  1.00 19.25 ? 96  TYR   A CD2   1 
ATOM   697  C  CE1   . TYR   A 1 99  ? 32.964 -9.286  10.759 1.00 20.71 ? 96  TYR   A CE1   1 
ATOM   698  C  CE2   . TYR   A 1 99  ? 34.766 -7.862  10.075 1.00 21.13 ? 96  TYR   A CE2   1 
ATOM   699  C  CZ    . TYR   A 1 99  ? 34.321 -8.981  10.745 1.00 19.13 ? 96  TYR   A CZ    1 
ATOM   700  O  OH    . TYR   A 1 99  ? 35.210 -9.776  11.388 1.00 23.18 ? 96  TYR   A OH    1 
ATOM   701  N  N     . ARG   A 1 100 ? 30.266 -5.279  6.006  1.00 15.27 ? 97  ARG   A N     1 
ATOM   702  C  CA    . ARG   A 1 100 ? 29.249 -4.483  5.286  1.00 16.61 ? 97  ARG   A CA    1 
ATOM   703  C  C     . ARG   A 1 100 ? 28.540 -5.354  4.243  1.00 16.02 ? 97  ARG   A C     1 
ATOM   704  O  O     . ARG   A 1 100 ? 27.269 -5.324  4.130  1.00 17.50 ? 97  ARG   A O     1 
ATOM   705  C  CB    . ARG   A 1 100 ? 29.860 -3.212  4.692  1.00 16.98 ? 97  ARG   A CB    1 
ATOM   706  C  CG    . ARG   A 1 100 ? 28.872 -2.344  3.918  1.00 19.12 ? 97  ARG   A CG    1 
ATOM   707  C  CD    . ARG   A 1 100 ? 29.410 -0.971  3.516  1.00 22.56 ? 97  ARG   A CD    1 
ATOM   708  N  NE    . ARG   A 1 100 ? 28.663 -0.294  2.466  1.00 25.60 ? 97  ARG   A NE    1 
ATOM   709  C  CZ    . ARG   A 1 100 ? 28.800 -0.483  1.142  1.00 31.87 ? 97  ARG   A CZ    1 
ATOM   710  N  NH1   . ARG   A 1 100 ? 29.613 -1.408  0.660  1.00 23.67 ? 97  ARG   A NH1   1 
ATOM   711  N  NH2   . ARG   A 1 100 ? 28.077 0.234   0.288  1.00 36.56 ? 97  ARG   A NH2   1 
ATOM   712  N  N     . GLU   A 1 101 ? 29.288 -6.068  3.423  1.00 17.04 ? 98  GLU   A N     1 
ATOM   713  C  CA    . GLU   A 1 101 ? 28.728 -6.911  2.351  1.00 18.92 ? 98  GLU   A CA    1 
ATOM   714  C  C     . GLU   A 1 101 ? 27.767 -7.931  2.992  1.00 18.60 ? 98  GLU   A C     1 
ATOM   715  O  O     . GLU   A 1 101 ? 26.666 -8.147  2.435  1.00 19.22 ? 98  GLU   A O     1 
ATOM   716  C  CB    . GLU   A 1 101 ? 29.828 -7.579  1.514  1.00 19.58 ? 98  GLU   A CB    1 
ATOM   717  C  CG    . GLU   A 1 101 ? 29.309 -8.539  0.476  1.00 23.04 ? 98  GLU   A CG    1 
ATOM   718  C  CD    . GLU   A 1 101 ? 30.404 -9.124  -0.399 1.00 26.34 ? 98  GLU   A CD    1 
ATOM   719  O  OE1   . GLU   A 1 101 ? 31.447 -8.427  -0.557 1.00 19.77 ? 98  GLU   A OE1   1 
ATOM   720  O  OE2   . GLU   A 1 101 ? 30.200 -10.239 -0.937 1.00 32.37 ? 98  GLU   A OE2   1 
ATOM   721  N  N     . GLN   A 1 102 ? 28.205 -8.617  4.042  1.00 17.91 ? 99  GLN   A N     1 
ATOM   722  C  CA    . GLN   A 1 102 ? 27.404 -9.694  4.672  1.00 18.89 ? 99  GLN   A CA    1 
ATOM   723  C  C     . GLN   A 1 102 ? 26.066 -9.095  5.190  1.00 19.99 ? 99  GLN   A C     1 
ATOM   724  O  O     . GLN   A 1 102 ? 25.021 -9.698  4.933  1.00 18.78 ? 99  GLN   A O     1 
ATOM   725  C  CB    . GLN   A 1 102 ? 28.175 -10.328 5.828  1.00 17.77 ? 99  GLN   A CB    1 
ATOM   726  C  CG    . GLN   A 1 102 ? 29.346 -11.206 5.455  1.00 22.54 ? 99  GLN   A CG    1 
ATOM   727  C  CD    . GLN   A 1 102 ? 30.253 -11.543 6.611  1.00 24.91 ? 99  GLN   A CD    1 
ATOM   728  O  OE1   . GLN   A 1 102 ? 30.037 -11.178 7.760  1.00 30.28 ? 99  GLN   A OE1   1 
ATOM   729  N  NE2   . GLN   A 1 102 ? 31.347 -12.200 6.305  1.00 37.64 ? 99  GLN   A NE2   1 
ATOM   730  N  N     . ILE   A 1 103 ? 26.103 -7.917  5.784  1.00 15.30 ? 100 ILE   A N     1 
ATOM   731  C  CA    . ILE   A 1 103 ? 24.899 -7.280  6.402  1.00 17.91 ? 100 ILE   A CA    1 
ATOM   732  C  C     . ILE   A 1 103 ? 23.943 -6.893  5.276  1.00 19.21 ? 100 ILE   A C     1 
ATOM   733  O  O     . ILE   A 1 103 ? 22.751 -7.206  5.342  1.00 19.45 ? 100 ILE   A O     1 
ATOM   734  C  CB    . ILE   A 1 103 ? 25.310 -6.080  7.265  1.00 16.67 ? 100 ILE   A CB    1 
ATOM   735  C  CG1   . ILE   A 1 103 ? 26.116 -6.506  8.494  1.00 18.14 ? 100 ILE   A CG1   1 
ATOM   736  C  CG2   . ILE   A 1 103 ? 24.092 -5.281  7.641  1.00 18.90 ? 100 ILE   A CG2   1 
ATOM   737  C  CD1   . ILE   A 1 103 ? 26.950 -5.410  9.105  1.00 15.87 ? 100 ILE   A CD1   1 
ATOM   738  N  N     . LYS   A 1 104 ? 24.460 -6.264  4.220  1.00 20.37 ? 101 LYS   A N     1 
ATOM   739  C  CA    . LYS   A 1 104 ? 23.620 -5.795  3.101  1.00 22.09 ? 101 LYS   A CA    1 
ATOM   740  C  C     . LYS   A 1 104 ? 22.987 -6.997  2.409  1.00 20.43 ? 101 LYS   A C     1 
ATOM   741  O  O     . LYS   A 1 104 ? 21.834 -6.882  1.990  1.00 22.29 ? 101 LYS   A O     1 
ATOM   742  C  CB    . LYS   A 1 104 ? 24.455 -4.960  2.144  1.00 21.26 ? 101 LYS   A CB    1 
ATOM   743  C  CG    . LYS   A 1 104 ? 24.687 -3.534  2.630  1.00 22.48 ? 101 LYS   A CG    1 
ATOM   744  C  CD    . LYS   A 1 104 ? 25.700 -2.760  1.795  1.00 29.82 ? 101 LYS   A CD    1 
ATOM   745  C  CE    . LYS   A 1 104 ? 25.313 -2.545  0.341  1.00 39.23 ? 101 LYS   A CE    1 
ATOM   746  N  NZ    . LYS   A 1 104 ? 26.490 -2.655  -0.569 1.00 39.46 ? 101 LYS   A NZ    1 
ATOM   747  N  N     . ARG   A 1 105 ? 23.685 -8.122  2.359  1.00 19.29 ? 102 ARG   A N     1 
ATOM   748  C  CA    . ARG   A 1 105 ? 23.197 -9.346  1.676  1.00 22.58 ? 102 ARG   A CA    1 
ATOM   749  C  C     . ARG   A 1 105 ? 22.021 -9.906  2.464  1.00 22.59 ? 102 ARG   A C     1 
ATOM   750  O  O     . ARG   A 1 105 ? 21.014 -10.229 1.864  1.00 24.49 ? 102 ARG   A O     1 
ATOM   751  C  CB    . ARG   A 1 105 ? 24.274 -10.429 1.564  1.00 24.17 ? 102 ARG   A CB    1 
ATOM   752  C  CG    . ARG   A 1 105 ? 23.777 -11.707 0.908  1.00 28.77 ? 102 ARG   A CG    1 
ATOM   753  C  CD    . ARG   A 1 105 ? 24.918 -12.634 0.549  1.00 34.15 ? 102 ARG   A CD    1 
ATOM   754  N  NE    . ARG   A 1 105 ? 25.713 -12.026 -0.508 1.00 45.17 ? 102 ARG   A NE    1 
ATOM   755  C  CZ    . ARG   A 1 105 ? 26.959 -11.560 -0.392 1.00 39.76 ? 102 ARG   A CZ    1 
ATOM   756  N  NH1   . ARG   A 1 105 ? 27.525 -11.004 -1.440 1.00 38.17 ? 102 ARG   A NH1   1 
ATOM   757  N  NH2   . ARG   A 1 105 ? 27.645 -11.659 0.738  1.00 43.46 ? 102 ARG   A NH2   1 
ATOM   758  N  N     . VAL   A 1 106 ? 22.191 -10.044 3.769  1.00 22.72 ? 103 VAL   A N     1 
ATOM   759  C  CA    . VAL   A 1 106 ? 21.148 -10.617 4.676  1.00 20.29 ? 103 VAL   A CA    1 
ATOM   760  C  C     . VAL   A 1 106 ? 19.926 -9.708  4.697  1.00 24.12 ? 103 VAL   A C     1 
ATOM   761  O  O     . VAL   A 1 106 ? 18.825 -10.234 4.565  1.00 26.38 ? 103 VAL   A O     1 
ATOM   762  C  CB    . VAL   A 1 106 ? 21.761 -10.771 6.070  1.00 21.12 ? 103 VAL   A CB    1 
ATOM   763  C  CG1   . VAL   A 1 106 ? 20.637 -10.971 7.084  1.00 23.06 ? 103 VAL   A CG1   1 
ATOM   764  C  CG2   . VAL   A 1 106 ? 22.695 -11.949 6.094  1.00 23.45 ? 103 VAL   A CG2   1 
ATOM   765  N  N     . LYS   A 1 107 ? 20.127 -8.408  4.763  1.00 21.10 ? 104 LYS   A N     1 
ATOM   766  C  CA    . LYS   A 1 107 ? 19.059 -7.378  4.813  1.00 25.25 ? 104 LYS   A CA    1 
ATOM   767  C  C     . LYS   A 1 107 ? 18.492 -7.086  3.418  1.00 26.10 ? 104 LYS   A C     1 
ATOM   768  O  O     . LYS   A 1 107 ? 17.505 -6.409  3.313  1.00 28.82 ? 104 LYS   A O     1 
ATOM   769  C  CB    . LYS   A 1 107 ? 19.547 -6.191  5.640  1.00 28.32 ? 104 LYS   A CB    1 
ATOM   770  C  CG    . LYS   A 1 107 ? 19.891 -6.656  7.044  1.00 29.68 ? 104 LYS   A CG    1 
ATOM   771  C  CD    . LYS   A 1 107 ? 20.218 -5.645  8.093  1.00 28.05 ? 104 LYS   A CD    1 
ATOM   772  C  CE    . LYS   A 1 107 ? 19.016 -4.966  8.695  1.00 21.63 ? 104 LYS   A CE    1 
ATOM   773  N  NZ    . LYS   A 1 107 ? 18.259 -5.859  9.632  1.00 25.06 ? 104 LYS   A NZ    1 
ATOM   774  N  N     . ASP   A 1 108 ? 19.139 -7.609  2.377  1.00 27.19 ? 105 ASP   A N     1 
ATOM   775  C  CA    . ASP   A 1 108 ? 18.686 -7.410  0.979  1.00 26.11 ? 105 ASP   A CA    1 
ATOM   776  C  C     . ASP   A 1 108 ? 18.443 -5.931  0.717  1.00 29.58 ? 105 ASP   A C     1 
ATOM   777  O  O     . ASP   A 1 108 ? 17.475 -5.612  0.071  1.00 34.09 ? 105 ASP   A O     1 
ATOM   778  C  CB    . ASP   A 1 108 ? 17.454 -8.252  0.671  1.00 31.09 ? 105 ASP   A CB    1 
ATOM   779  C  CG    . ASP   A 1 108 ? 17.135 -8.188  -0.808 1.00 34.90 ? 105 ASP   A CG    1 
ATOM   780  O  OD1   . ASP   A 1 108 ? 18.072 -8.093  -1.582 1.00 39.91 ? 105 ASP   A OD1   1 
ATOM   781  O  OD2   . ASP   A 1 108 ? 15.959 -8.156  -1.142 1.00 37.21 ? 105 ASP   A OD2   1 
ATOM   782  N  N     . SER   A 1 109 ? 19.296 -5.076  1.260  1.00 28.79 ? 106 SER   A N     1 
ATOM   783  C  CA    . SER   A 1 109 ? 19.130 -3.622  1.138  1.00 31.18 ? 106 SER   A CA    1 
ATOM   784  C  C     . SER   A 1 109 ? 20.516 -2.984  1.015  1.00 31.21 ? 106 SER   A C     1 
ATOM   785  O  O     . SER   A 1 109 ? 21.430 -3.451  1.670  1.00 30.51 ? 106 SER   A O     1 
ATOM   786  C  CB    . SER   A 1 109 ? 18.429 -3.092  2.360  1.00 34.52 ? 106 SER   A CB    1 
ATOM   787  O  OG    . SER   A 1 109 ? 18.300 -1.698  2.291  1.00 35.19 ? 106 SER   A OG    1 
ATOM   788  N  N     . GLU   A 1 110 ? 20.634 -1.935  0.199  1.00 35.41 ? 107 GLU   A N     1 
ATOM   789  C  CA    . GLU   A 1 110 ? 21.873 -1.131  0.070  1.00 38.74 ? 107 GLU   A CA    1 
ATOM   790  C  C     . GLU   A 1 110 ? 21.969 -0.134  1.217  1.00 38.50 ? 107 GLU   A C     1 
ATOM   791  O  O     . GLU   A 1 110 ? 23.006 0.471   1.415  1.00 39.25 ? 107 GLU   A O     1 
ATOM   792  C  CB    . GLU   A 1 110 ? 21.724 -0.165  -1.102 1.00 42.24 ? 107 GLU   A CB    1 
ATOM   793  C  CG    . GLU   A 1 110 ? 21.609 -0.837  -2.427 1.00 42.88 ? 107 GLU   A CG    1 
ATOM   794  C  CD    . GLU   A 1 110 ? 22.796 -1.715  -2.716 1.00 48.82 ? 107 GLU   A CD    1 
ATOM   795  O  OE1   . GLU   A 1 110 ? 23.912 -1.306  -2.397 1.00 56.63 ? 107 GLU   A OE1   1 
ATOM   796  O  OE2   . GLU   A 1 110 ? 22.582 -2.775  -3.347 1.00 65.41 ? 107 GLU   A OE2   1 
ATOM   797  N  N     . ASP   A 1 111 ? 20.818 0.063   1.837  1.00 35.13 ? 108 ASP   A N     1 
ATOM   798  C  CA    . ASP   A 1 111 ? 20.620 1.104   2.853  1.00 34.33 ? 108 ASP   A CA    1 
ATOM   799  C  C     . ASP   A 1 111 ? 20.373 0.418   4.187  1.00 30.03 ? 108 ASP   A C     1 
ATOM   800  O  O     . ASP   A 1 111 ? 19.317 -0.151  4.349  1.00 31.70 ? 108 ASP   A O     1 
ATOM   801  C  CB    . ASP   A 1 111 ? 19.341 1.808   2.450  1.00 39.83 ? 108 ASP   A CB    1 
ATOM   802  C  CG    . ASP   A 1 111 ? 19.065 3.073   3.206  1.00 41.96 ? 108 ASP   A CG    1 
ATOM   803  O  OD1   . ASP   A 1 111 ? 19.874 3.423   4.074  1.00 52.66 ? 108 ASP   A OD1   1 
ATOM   804  O  OD2   . ASP   A 1 111 ? 18.064 3.673   2.904  1.00 44.28 ? 108 ASP   A OD2   1 
ATOM   805  N  N     . VAL   A 1 112 ? 21.392 0.336   5.007  1.00 25.43 ? 109 VAL   A N     1 
ATOM   806  C  CA    . VAL   A 1 112 ? 21.275 -0.253  6.378  1.00 20.60 ? 109 VAL   A CA    1 
ATOM   807  C  C     . VAL   A 1 112 ? 21.926 0.728   7.348  1.00 19.90 ? 109 VAL   A C     1 
ATOM   808  O  O     . VAL   A 1 112 ? 22.998 1.143   7.083  1.00 18.81 ? 109 VAL   A O     1 
ATOM   809  C  CB    . VAL   A 1 112 ? 21.896 -1.656  6.467  1.00 20.92 ? 109 VAL   A CB    1 
ATOM   810  C  CG1   . VAL   A 1 112 ? 21.895 -2.170  7.892  1.00 18.59 ? 109 VAL   A CG1   1 
ATOM   811  C  CG2   . VAL   A 1 112 ? 21.209 -2.654  5.564  1.00 23.29 ? 109 VAL   A CG2   1 
ATOM   812  N  N     . PRO   A 1 113 ? 21.307 1.159   8.481  1.00 17.59 ? 110 PRO   A N     1 
ATOM   813  C  CA    . PRO   A 1 113 ? 21.964 2.076   9.380  1.00 18.05 ? 110 PRO   A CA    1 
ATOM   814  C  C     . PRO   A 1 113 ? 23.247 1.413   9.886  1.00 19.37 ? 110 PRO   A C     1 
ATOM   815  O  O     . PRO   A 1 113 ? 23.227 0.338   10.262 1.00 17.31 ? 110 PRO   A O     1 
ATOM   816  C  CB    . PRO   A 1 113 ? 20.937 2.229   10.533 1.00 16.81 ? 110 PRO   A CB    1 
ATOM   817  C  CG    . PRO   A 1 113 ? 19.653 2.032   9.809  1.00 20.86 ? 110 PRO   A CG    1 
ATOM   818  C  CD    . PRO   A 1 113 ? 19.887 0.874   8.879  1.00 18.88 ? 110 PRO   A CD    1 
ATOM   819  N  N     . MET   A 1 114 ? 24.319 2.177   9.747  1.00 15.33 ? 111 MET   A N     1 
ATOM   820  C  CA    . MET   A 1 114 ? 25.681 1.694   10.087 1.00 16.92 ? 111 MET   A CA    1 
ATOM   821  C  C     . MET   A 1 114 ? 26.523 2.917   10.424 1.00 19.07 ? 111 MET   A C     1 
ATOM   822  O  O     . MET   A 1 114 ? 26.297 3.984   9.862  1.00 16.28 ? 111 MET   A O     1 
ATOM   823  C  CB    . MET   A 1 114 ? 26.394 1.013   8.906  1.00 19.50 ? 111 MET   A CB    1 
ATOM   824  C  CG    . MET   A 1 114 ? 25.845 -0.312  8.453  1.00 17.93 ? 111 MET   A CG    1 
ATOM   825  S  SD    . MET   A 1 114 ? 27.060 -1.093  7.370  1.00 26.28 ? 111 MET   A SD    1 
ATOM   826  C  CE    . MET   A 1 114 ? 25.967 -2.281  6.570  1.00 28.93 ? 111 MET   A CE    1 
ATOM   827  N  N     . VAL   A 1 115 ? 27.474 2.718   11.312 1.00 14.92 ? 112 VAL   A N     1 
ATOM   828  C  CA    . VAL   A 1 115 ? 28.513 3.727   11.643 1.00 14.68 ? 112 VAL   A CA    1 
ATOM   829  C  C     . VAL   A 1 115 ? 29.861 2.989   11.585 1.00 15.67 ? 112 VAL   A C     1 
ATOM   830  O  O     . VAL   A 1 115 ? 29.998 1.862   12.120 1.00 15.20 ? 112 VAL   A O     1 
ATOM   831  C  CB    . VAL   A 1 115 ? 28.298 4.388   13.017 1.00 15.89 ? 112 VAL   A CB    1 
ATOM   832  C  CG1   . VAL   A 1 115 ? 29.436 5.335   13.399 1.00 18.03 ? 112 VAL   A CG1   1 
ATOM   833  C  CG2   . VAL   A 1 115 ? 26.985 5.153   13.019 1.00 16.80 ? 112 VAL   A CG2   1 
ATOM   834  N  N     . LEU   A 1 116 ? 30.807 3.623   10.882 1.00 14.97 ? 113 LEU   A N     1 
ATOM   835  C  CA    . LEU   A 1 116 ? 32.180 3.068   10.879 1.00 14.90 ? 113 LEU   A CA    1 
ATOM   836  C  C     . LEU   A 1 116 ? 32.918 3.613   12.107 1.00 16.84 ? 113 LEU   A C     1 
ATOM   837  O  O     . LEU   A 1 116 ? 32.907 4.772   12.266 1.00 15.65 ? 113 LEU   A O     1 
ATOM   838  C  CB    . LEU   A 1 116 ? 32.834 3.531   9.559  1.00 15.51 ? 113 LEU   A CB    1 
ATOM   839  C  CG    . LEU   A 1 116 ? 34.284 3.087   9.375  1.00 14.74 ? 113 LEU   A CG    1 
ATOM   840  C  CD1   . LEU   A 1 116 ? 34.363 1.611   9.263  1.00 15.95 ? 113 LEU   A CD1   1 
ATOM   841  C  CD2   . LEU   A 1 116 ? 34.909 3.752   8.141  1.00 17.04 ? 113 LEU   A CD2   1 
ATOM   842  N  N     . VAL   A 1 117 ? 33.532 2.713   12.841 1.00 14.99 ? 114 VAL   A N     1 
ATOM   843  C  CA    . VAL   A 1 117 ? 34.266 3.111   14.056 1.00 14.45 ? 114 VAL   A CA    1 
ATOM   844  C  C     . VAL   A 1 117 ? 35.738 2.667   13.928 1.00 18.06 ? 114 VAL   A C     1 
ATOM   845  O  O     . VAL   A 1 117 ? 35.973 1.519   13.830 1.00 17.29 ? 114 VAL   A O     1 
ATOM   846  C  CB    . VAL   A 1 117 ? 33.583 2.503   15.311 1.00 16.25 ? 114 VAL   A CB    1 
ATOM   847  C  CG1   . VAL   A 1 117 ? 34.356 2.781   16.574 1.00 17.32 ? 114 VAL   A CG1   1 
ATOM   848  C  CG2   . VAL   A 1 117 ? 32.136 2.980   15.439 1.00 15.17 ? 114 VAL   A CG2   1 
ATOM   849  N  N     . GLY   A 1 118 ? 36.599 3.651   14.120 1.00 17.70 ? 115 GLY   A N     1 
ATOM   850  C  CA    . GLY   A 1 118 ? 38.043 3.367   14.229 1.00 16.36 ? 115 GLY   A CA    1 
ATOM   851  C  C     . GLY   A 1 118 ? 38.395 3.445   15.705 1.00 17.40 ? 115 GLY   A C     1 
ATOM   852  O  O     . GLY   A 1 118 ? 38.480 4.514   16.159 1.00 18.85 ? 115 GLY   A O     1 
ATOM   853  N  N     . ASN   A 1 119 ? 38.597 2.302   16.298 1.00 16.75 ? 116 ASN   A N     1 
ATOM   854  C  CA    . ASN   A 1 119 ? 38.839 2.237   17.757 1.00 17.97 ? 116 ASN   A CA    1 
ATOM   855  C  C     . ASN   A 1 119 ? 40.355 2.294   18.026 1.00 19.50 ? 116 ASN   A C     1 
ATOM   856  O  O     . ASN   A 1 119 ? 41.132 2.083   17.073 1.00 20.00 ? 116 ASN   A O     1 
ATOM   857  C  CB    . ASN   A 1 119 ? 38.087 1.028   18.338 1.00 16.88 ? 116 ASN   A CB    1 
ATOM   858  C  CG    . ASN   A 1 119 ? 38.053 1.002   19.852 1.00 17.95 ? 116 ASN   A CG    1 
ATOM   859  O  OD1   . ASN   A 1 119 ? 37.875 2.039   20.405 1.00 17.89 ? 116 ASN   A OD1   1 
ATOM   860  N  ND2   . ASN   A 1 119 ? 38.522 -0.079  20.386 1.00 18.00 ? 116 ASN   A ND2   1 
ATOM   861  N  N     . LYS   A 1 120 ? 40.768 2.510   19.263 1.00 18.65 ? 117 LYS   A N     1 
ATOM   862  C  CA    . LYS   A 1 120 ? 42.136 2.593   19.795 1.00 21.80 ? 117 LYS   A CA    1 
ATOM   863  C  C     . LYS   A 1 120 ? 42.753 3.917   19.377 1.00 22.16 ? 117 LYS   A C     1 
ATOM   864  O  O     . LYS   A 1 120 ? 43.947 3.899   19.149 1.00 22.03 ? 117 LYS   A O     1 
ATOM   865  C  CB    . LYS   A 1 120 ? 42.938 1.306   19.556 1.00 19.64 ? 117 LYS   A CB    1 
ATOM   866  C  CG    . LYS   A 1 120 ? 42.184 -0.013  19.647 1.00 17.92 ? 117 LYS   A CG    1 
ATOM   867  C  CD    . LYS   A 1 120 ? 43.060 -1.162  19.906 1.00 20.70 ? 117 LYS   A CD    1 
ATOM   868  C  CE    . LYS   A 1 120 ? 42.394 -2.505  19.948 1.00 19.88 ? 117 LYS   A CE    1 
ATOM   869  N  NZ    . LYS   A 1 120 ? 43.336 -3.622  20.100 1.00 23.25 ? 117 LYS   A NZ    1 
ATOM   870  N  N     . SER   A 1 121 ? 41.977 4.969   19.203 1.00 22.06 ? 118 SER   A N     1 
ATOM   871  C  CA    . SER   A 1 121 ? 42.486 6.312   18.823 1.00 21.56 ? 118 SER   A CA    1 
ATOM   872  C  C     . SER   A 1 121 ? 43.572 6.822   19.790 1.00 22.80 ? 118 SER   A C     1 
ATOM   873  O  O     . SER   A 1 121 ? 44.310 7.757   19.446 1.00 27.01 ? 118 SER   A O     1 
ATOM   874  C  CB    . SER   A 1 121 ? 41.400 7.304   18.631 1.00 25.31 ? 118 SER   A CB    1 
ATOM   875  O  OG    . SER   A 1 121 ? 40.807 7.648   19.894 1.00 26.66 ? 118 SER   A OG    1 
ATOM   876  N  N     . ASP   A 1 122 ? 43.626 6.289   21.003 1.00 21.37 ? 119 ASP   A N     1 
ATOM   877  C  CA    . ASP   A 1 122 ? 44.645 6.643   22.020 1.00 25.77 ? 119 ASP   A CA    1 
ATOM   878  C  C     . ASP   A 1 122 ? 46.031 6.099   21.647 1.00 23.74 ? 119 ASP   A C     1 
ATOM   879  O  O     . ASP   A 1 122 ? 47.022 6.504   22.274 1.00 29.66 ? 119 ASP   A O     1 
ATOM   880  C  CB    . ASP   A 1 122 ? 44.307 6.052   23.391 1.00 27.91 ? 119 ASP   A CB    1 
ATOM   881  C  CG    . ASP   A 1 122 ? 44.130 4.534   23.345 1.00 22.85 ? 119 ASP   A CG    1 
ATOM   882  O  OD1   . ASP   A 1 122 ? 43.127 4.052   22.738 1.00 25.11 ? 119 ASP   A OD1   1 
ATOM   883  O  OD2   . ASP   A 1 122 ? 44.987 3.829   23.863 1.00 26.59 ? 119 ASP   A OD2   1 
ATOM   884  N  N     . LEU   A 1 123 ? 46.086 5.126   20.749 1.00 25.37 ? 120 LEU   A N     1 
ATOM   885  C  CA    . LEU   A 1 123 ? 47.395 4.486   20.454 1.00 25.28 ? 120 LEU   A CA    1 
ATOM   886  C  C     . LEU   A 1 123 ? 48.319 5.325   19.541 1.00 28.95 ? 120 LEU   A C     1 
ATOM   887  O  O     . LEU   A 1 123 ? 47.844 6.054   18.705 1.00 28.37 ? 120 LEU   A O     1 
ATOM   888  C  CB    . LEU   A 1 123 ? 47.177 3.094   19.882 1.00 27.70 ? 120 LEU   A CB    1 
ATOM   889  C  CG    . LEU   A 1 123 ? 46.701 2.010   20.843 1.00 26.84 ? 120 LEU   A CG    1 
ATOM   890  C  CD1   . LEU   A 1 123 ? 46.509 0.707   20.134 1.00 25.71 ? 120 LEU   A CD1   1 
ATOM   891  C  CD2   . LEU   A 1 123 ? 47.642 1.833   22.020 1.00 29.01 ? 120 LEU   A CD2   1 
ATOM   892  N  N     . PRO   A 1 124 ? 49.650 5.282   19.725 1.00 28.44 ? 121 PRO   A N     1 
ATOM   893  C  CA    . PRO   A 1 124 ? 50.553 6.042   18.819 1.00 29.59 ? 121 PRO   A CA    1 
ATOM   894  C  C     . PRO   A 1 124 ? 51.034 5.200   17.635 1.00 26.92 ? 121 PRO   A C     1 
ATOM   895  O  O     . PRO   A 1 124 ? 51.976 5.613   16.966 1.00 33.14 ? 121 PRO   A O     1 
ATOM   896  C  CB    . PRO   A 1 124 ? 51.682 6.285   19.811 1.00 29.35 ? 121 PRO   A CB    1 
ATOM   897  C  CG    . PRO   A 1 124 ? 51.813 4.996   20.539 1.00 30.23 ? 121 PRO   A CG    1 
ATOM   898  C  CD    . PRO   A 1 124 ? 50.366 4.562   20.769 1.00 28.91 ? 121 PRO   A CD    1 
ATOM   899  N  N     . SER   A 1 125 ? 50.530 4.006   17.481 1.00 29.77 ? 122 SER   A N     1 
ATOM   900  C  CA    . SER   A 1 125 ? 50.954 3.070   16.416 1.00 27.99 ? 122 SER   A CA    1 
ATOM   901  C  C     . SER   A 1 125 ? 49.953 3.019   15.266 1.00 25.90 ? 122 SER   A C     1 
ATOM   902  O  O     . SER   A 1 125 ? 49.742 1.977   14.777 1.00 29.00 ? 122 SER   A O     1 
ATOM   903  C  CB    . SER   A 1 125 ? 51.149 1.735   17.007 1.00 30.16 ? 122 SER   A CB    1 
ATOM   904  O  OG    . SER   A 1 125 ? 50.006 1.419   17.856 1.00 32.20 ? 122 SER   A OG    1 
ATOM   905  N  N     . ARG   A 1 126 ? 49.395 4.156   14.894 1.00 27.29 ? 123 ARG   A N     1 
ATOM   906  C  CA    . ARG   A 1 126 ? 48.373 4.245   13.825 1.00 23.54 ? 123 ARG   A CA    1 
ATOM   907  C  C     . ARG   A 1 126 ? 48.913 3.778   12.465 1.00 25.34 ? 123 ARG   A C     1 
ATOM   908  O  O     . ARG   A 1 126 ? 49.972 4.331   12.020 1.00 25.64 ? 123 ARG   A O     1 
ATOM   909  C  CB    . ARG   A 1 126 ? 47.900 5.682   13.663 1.00 23.69 ? 123 ARG   A CB    1 
ATOM   910  C  CG    . ARG   A 1 126 ? 46.907 5.926   12.558 1.00 22.76 ? 123 ARG   A CG    1 
ATOM   911  C  CD    . ARG   A 1 126 ? 46.517 7.338   12.305 1.00 25.48 ? 123 ARG   A CD    1 
ATOM   912  N  NE    . ARG   A 1 126 ? 45.722 7.920   13.405 1.00 27.81 ? 123 ARG   A NE    1 
ATOM   913  C  CZ    . ARG   A 1 126 ? 44.396 7.879   13.503 1.00 25.09 ? 123 ARG   A CZ    1 
ATOM   914  N  NH1   . ARG   A 1 126 ? 43.667 7.240   12.614 1.00 27.68 ? 123 ARG   A NH1   1 
ATOM   915  N  NH2   . ARG   A 1 126 ? 43.831 8.458   14.552 1.00 25.67 ? 123 ARG   A NH2   1 
ATOM   916  N  N     . THR   A 1 127 ? 48.246 2.801   11.867 1.00 24.35 ? 124 THR   A N     1 
ATOM   917  C  CA    . THR   A 1 127 ? 48.515 2.281   10.501 1.00 23.27 ? 124 THR   A CA    1 
ATOM   918  C  C     . THR   A 1 127 ? 47.366 2.654   9.567  1.00 24.61 ? 124 THR   A C     1 
ATOM   919  O  O     . THR   A 1 127 ? 47.476 2.433   8.358  1.00 24.47 ? 124 THR   A O     1 
ATOM   920  C  CB    . THR   A 1 127 ? 48.832 0.799   10.538 1.00 25.31 ? 124 THR   A CB    1 
ATOM   921  O  OG1   . THR   A 1 127 ? 47.682 0.074   11.008 1.00 28.86 ? 124 THR   A OG1   1 
ATOM   922  C  CG2   . THR   A 1 127 ? 50.039 0.484   11.389 1.00 29.83 ? 124 THR   A CG2   1 
ATOM   923  N  N     . VAL   A 1 128 ? 46.245 3.141   10.102 1.00 24.32 ? 125 VAL   A N     1 
ATOM   924  C  CA    . VAL   A 1 128 ? 45.138 3.582   9.215  1.00 21.92 ? 125 VAL   A CA    1 
ATOM   925  C  C     . VAL   A 1 128 ? 44.916 5.083   9.380  1.00 25.21 ? 125 VAL   A C     1 
ATOM   926  O  O     . VAL   A 1 128 ? 44.491 5.489   10.480 1.00 23.92 ? 125 VAL   A O     1 
ATOM   927  C  CB    . VAL   A 1 128 ? 43.829 2.783   9.459  1.00 20.97 ? 125 VAL   A CB    1 
ATOM   928  C  CG1   . VAL   A 1 128 ? 42.715 3.171   8.527  1.00 24.19 ? 125 VAL   A CG1   1 
ATOM   929  C  CG2   . VAL   A 1 128 ? 44.063 1.301   9.472  1.00 22.36 ? 125 VAL   A CG2   1 
ATOM   930  N  N     . ASP   A 1 129 ? 45.107 5.894   8.335  1.00 27.36 ? 126 ASP   A N     1 
ATOM   931  C  CA    . ASP   A 1 129 ? 44.949 7.363   8.414  1.00 29.29 ? 126 ASP   A CA    1 
ATOM   932  C  C     . ASP   A 1 129 ? 43.474 7.659   8.588  1.00 25.73 ? 126 ASP   A C     1 
ATOM   933  O  O     . ASP   A 1 129 ? 42.650 6.938   7.974  1.00 24.25 ? 126 ASP   A O     1 
ATOM   934  C  CB    . ASP   A 1 129 ? 45.476 8.091   7.168  1.00 33.86 ? 126 ASP   A CB    1 
ATOM   935  C  CG    . ASP   A 1 129 ? 46.975 8.165   7.108  1.00 39.44 ? 126 ASP   A CG    1 
ATOM   936  O  OD1   . ASP   A 1 129 ? 47.616 7.786   8.109  1.00 41.11 ? 126 ASP   A OD1   1 
ATOM   937  O  OD2   . ASP   A 1 129 ? 47.467 8.596   6.065  1.00 47.31 ? 126 ASP   A OD2   1 
ATOM   938  N  N     . THR   A 1 130 ? 43.175 8.651   9.420  1.00 24.66 ? 127 THR   A N     1 
ATOM   939  C  CA    . THR   A 1 130 ? 41.808 9.194   9.575  1.00 24.44 ? 127 THR   A CA    1 
ATOM   940  C  C     . THR   A 1 130 ? 41.226 9.484   8.194  1.00 24.88 ? 127 THR   A C     1 
ATOM   941  O  O     . THR   A 1 130 ? 40.059 9.091   7.961  1.00 22.65 ? 127 THR   A O     1 
ATOM   942  C  CB    . THR   A 1 130 ? 41.807 10.419  10.488 1.00 28.33 ? 127 THR   A CB    1 
ATOM   943  O  OG1   . THR   A 1 130 ? 42.431 9.972   11.690 1.00 26.89 ? 127 THR   A OG1   1 
ATOM   944  C  CG2   . THR   A 1 130 ? 40.413 10.929  10.764 1.00 27.64 ? 127 THR   A CG2   1 
ATOM   945  N  N     . LYS   A 1 131 ? 42.001 10.090  7.292  1.00 25.37 ? 128 LYS   A N     1 
ATOM   946  C  CA    . LYS   A 1 131 ? 41.439 10.526  5.980  1.00 26.15 ? 128 LYS   A CA    1 
ATOM   947  C  C     . LYS   A 1 131 ? 40.997 9.301   5.160  1.00 22.07 ? 128 LYS   A C     1 
ATOM   948  O  O     . LYS   A 1 131 ? 39.961 9.369   4.482  1.00 22.83 ? 128 LYS   A O     1 
ATOM   949  C  CB    . LYS   A 1 131 ? 42.473 11.349  5.199  1.00 28.48 ? 128 LYS   A CB    1 
ATOM   950  C  CG    . LYS   A 1 131 ? 41.900 12.058  3.972  1.00 36.52 ? 128 LYS   A CG    1 
ATOM   951  C  CD    . LYS   A 1 131 ? 42.876 12.978  3.250  1.00 40.10 ? 128 LYS   A CD    1 
ATOM   952  C  CE    . LYS   A 1 131 ? 43.373 12.390  1.945  1.00 47.05 ? 128 LYS   A CE    1 
ATOM   953  N  NZ    . LYS   A 1 131 ? 44.609 13.056  1.475  1.00 52.84 ? 128 LYS   A NZ    1 
ATOM   954  N  N     . GLN   A 1 132 ? 41.765 8.213   5.230  1.00 22.94 ? 129 GLN   A N     1 
ATOM   955  C  CA    . GLN   A 1 132 ? 41.477 6.970   4.468  1.00 21.39 ? 129 GLN   A CA    1 
ATOM   956  C  C     . GLN   A 1 132 ? 40.112 6.431   4.915  1.00 21.09 ? 129 GLN   A C     1 
ATOM   957  O  O     . GLN   A 1 132 ? 39.265 6.132   4.070  1.00 20.12 ? 129 GLN   A O     1 
ATOM   958  C  CB    . GLN   A 1 132 ? 42.557 5.890   4.658  1.00 22.15 ? 129 GLN   A CB    1 
ATOM   959  C  CG    . GLN   A 1 132 ? 42.304 4.667   3.789  1.00 23.80 ? 129 GLN   A CG    1 
ATOM   960  C  CD    . GLN   A 1 132 ? 43.268 3.502   3.916  1.00 25.55 ? 129 GLN   A CD    1 
ATOM   961  O  OE1   . GLN   A 1 132 ? 44.092 3.449   4.820  1.00 29.57 ? 129 GLN   A OE1   1 
ATOM   962  N  NE2   . GLN   A 1 132 ? 43.111 2.504   3.019  1.00 31.98 ? 129 GLN   A NE2   1 
ATOM   963  N  N     . ALA   A 1 133 ? 39.925 6.339   6.229  1.00 19.03 ? 130 ALA   A N     1 
ATOM   964  C  CA    . ALA   A 1 133 ? 38.662 5.801   6.811  1.00 18.63 ? 130 ALA   A CA    1 
ATOM   965  C  C     . ALA   A 1 133 ? 37.534 6.811   6.537  1.00 19.65 ? 130 ALA   A C     1 
ATOM   966  O  O     . ALA   A 1 133 ? 36.414 6.383   6.184  1.00 19.08 ? 130 ALA   A O     1 
ATOM   967  C  CB    . ALA   A 1 133 ? 38.838 5.474   8.278  1.00 20.02 ? 130 ALA   A CB    1 
ATOM   968  N  N     . GLN   A 1 134 ? 37.806 8.100   6.632  1.00 19.70 ? 131 GLN   A N     1 
ATOM   969  C  CA    . GLN   A 1 134 ? 36.773 9.109   6.306  1.00 19.64 ? 131 GLN   A CA    1 
ATOM   970  C  C     . GLN   A 1 134 ? 36.276 8.920   4.875  1.00 20.77 ? 131 GLN   A C     1 
ATOM   971  O  O     . GLN   A 1 134 ? 35.068 8.926   4.578  1.00 20.74 ? 131 GLN   A O     1 
ATOM   972  C  CB    . GLN   A 1 134 ? 37.306 10.515  6.485  1.00 21.00 ? 131 GLN   A CB    1 
ATOM   973  C  CG    . GLN   A 1 134 ? 36.200 11.545  6.331  1.00 28.33 ? 131 GLN   A CG    1 
ATOM   974  C  CD    . GLN   A 1 134 ? 35.044 11.252  7.252  1.00 33.27 ? 131 GLN   A CD    1 
ATOM   975  O  OE1   . GLN   A 1 134 ? 34.001 10.695  6.856  1.00 35.51 ? 131 GLN   A OE1   1 
ATOM   976  N  NE2   . GLN   A 1 134 ? 35.235 11.652  8.501  1.00 43.30 ? 131 GLN   A NE2   1 
ATOM   977  N  N     . ASP   A 1 135 ? 37.213 8.785   3.948  1.00 21.64 ? 132 ASP   A N     1 
ATOM   978  C  CA    . ASP   A 1 135 ? 36.851 8.677   2.515  1.00 20.33 ? 132 ASP   A CA    1 
ATOM   979  C  C     . ASP   A 1 135 ? 36.063 7.387   2.289  1.00 17.75 ? 132 ASP   A C     1 
ATOM   980  O  O     . ASP   A 1 135 ? 35.110 7.429   1.501  1.00 18.06 ? 132 ASP   A O     1 
ATOM   981  C  CB    . ASP   A 1 135 ? 38.080 8.776   1.598  1.00 21.23 ? 132 ASP   A CB    1 
ATOM   982  C  CG    . ASP   A 1 135 ? 38.674 10.181  1.538  1.00 21.21 ? 132 ASP   A CG    1 
ATOM   983  O  OD1   . ASP   A 1 135 ? 37.886 11.143  1.644  1.00 27.93 ? 132 ASP   A OD1   1 
ATOM   984  O  OD2   . ASP   A 1 135 ? 39.941 10.306  1.435  1.00 25.89 ? 132 ASP   A OD2   1 
ATOM   985  N  N     . LEU   A 1 136 ? 36.469 6.274   2.910  1.00 17.32 ? 133 LEU   A N     1 
ATOM   986  C  CA    . LEU   A 1 136 ? 35.705 5.010   2.782  1.00 17.76 ? 133 LEU   A CA    1 
ATOM   987  C  C     . LEU   A 1 136 ? 34.276 5.239   3.298  1.00 18.71 ? 133 LEU   A C     1 
ATOM   988  O  O     . LEU   A 1 136 ? 33.319 4.795   2.634  1.00 17.36 ? 133 LEU   A O     1 
ATOM   989  C  CB    . LEU   A 1 136 ? 36.356 3.863   3.540  1.00 17.15 ? 133 LEU   A CB    1 
ATOM   990  C  CG    . LEU   A 1 136 ? 35.708 2.492   3.324  1.00 18.52 ? 133 LEU   A CG    1 
ATOM   991  C  CD1   . LEU   A 1 136 ? 35.916 2.004   1.883  1.00 18.95 ? 133 LEU   A CD1   1 
ATOM   992  C  CD2   . LEU   A 1 136 ? 36.230 1.484   4.332  1.00 17.97 ? 133 LEU   A CD2   1 
ATOM   993  N  N     . ALA   A 1 137 ? 34.142 5.811   4.487  1.00 17.39 ? 134 ALA   A N     1 
ATOM   994  C  CA    . ALA   A 1 137 ? 32.805 6.038   5.076  1.00 19.45 ? 134 ALA   A CA    1 
ATOM   995  C  C     . ALA   A 1 137 ? 31.982 6.918   4.131  1.00 19.73 ? 134 ALA   A C     1 
ATOM   996  O  O     . ALA   A 1 137 ? 30.781 6.600   3.904  1.00 19.15 ? 134 ALA   A O     1 
ATOM   997  C  CB    . ALA   A 1 137 ? 32.972 6.677   6.433  1.00 18.99 ? 134 ALA   A CB    1 
ATOM   998  N  N     . ARG   A 1 138 ? 32.609 7.931   3.515  1.00 18.38 ? 135 ARG   A N     1 
ATOM   999  C  CA    . ARG   A 1 138 ? 31.867 8.752   2.535  1.00 20.82 ? 135 ARG   A CA    1 
ATOM   1000 C  C     . ARG   A 1 138 ? 31.401 7.888   1.351  1.00 19.92 ? 135 ARG   A C     1 
ATOM   1001 O  O     . ARG   A 1 138 ? 30.332 8.094   0.863  1.00 22.10 ? 135 ARG   A O     1 
ATOM   1002 C  CB    . ARG   A 1 138 ? 32.777 9.866   2.020  1.00 22.73 ? 135 ARG   A CB    1 
ATOM   1003 C  CG    . ARG   A 1 138 ? 32.452 11.245  2.539  1.00 33.33 ? 135 ARG   A CG    1 
ATOM   1004 C  CD    . ARG   A 1 138 ? 33.147 12.343  1.775  1.00 35.43 ? 135 ARG   A CD    1 
ATOM   1005 N  NE    . ARG   A 1 138 ? 34.411 12.320  2.447  1.00 38.03 ? 135 ARG   A NE    1 
ATOM   1006 C  CZ    . ARG   A 1 138 ? 35.076 13.373  2.802  1.00 42.02 ? 135 ARG   A CZ    1 
ATOM   1007 N  NH1   . ARG   A 1 138 ? 36.226 13.237  3.427  1.00 43.39 ? 135 ARG   A NH1   1 
ATOM   1008 N  NH2   . ARG   A 1 138 ? 34.621 14.560  2.461  1.00 53.08 ? 135 ARG   A NH2   1 
ATOM   1009 N  N     A SER   A 1 139 ? 32.251 6.984   0.870  0.50 20.00 ? 136 SER   A N     1 
ATOM   1010 N  N     B SER   A 1 139 ? 32.248 6.973   0.870  0.50 19.98 ? 136 SER   A N     1 
ATOM   1011 C  CA    A SER   A 1 139 ? 31.865 6.111   -0.252 0.50 20.90 ? 136 SER   A CA    1 
ATOM   1012 C  CA    B SER   A 1 139 ? 31.853 6.106   -0.266 0.50 20.33 ? 136 SER   A CA    1 
ATOM   1013 C  C     A SER   A 1 139 ? 30.656 5.266   0.155  0.50 19.81 ? 136 SER   A C     1 
ATOM   1014 C  C     B SER   A 1 139 ? 30.682 5.202   0.136  0.50 19.89 ? 136 SER   A C     1 
ATOM   1015 O  O     A SER   A 1 139 ? 29.802 5.111   -0.603 0.50 21.49 ? 136 SER   A O     1 
ATOM   1016 O  O     B SER   A 1 139 ? 29.753 5.131   -0.630 0.50 21.66 ? 136 SER   A O     1 
ATOM   1017 C  CB    A SER   A 1 139 ? 33.040 5.242   -0.669 0.50 19.32 ? 136 SER   A CB    1 
ATOM   1018 C  CB    B SER   A 1 139 ? 33.023 5.295   -0.786 0.50 18.59 ? 136 SER   A CB    1 
ATOM   1019 O  OG    A SER   A 1 139 ? 32.699 4.480   -1.802 0.50 21.17 ? 136 SER   A OG    1 
ATOM   1020 O  OG    B SER   A 1 139 ? 33.283 4.178   0.042  0.50 16.75 ? 136 SER   A OG    1 
ATOM   1021 N  N     . TYR   A 1 140 ? 30.613 4.851   1.432  1.00 17.99 ? 137 TYR   A N     1 
ATOM   1022 C  CA    . TYR   A 1 140 ? 29.525 3.978   1.942  1.00 18.35 ? 137 TYR   A CA    1 
ATOM   1023 C  C     . TYR   A 1 140 ? 28.282 4.818   2.311  1.00 19.79 ? 137 TYR   A C     1 
ATOM   1024 O  O     . TYR   A 1 140 ? 27.226 4.217   2.443  1.00 20.86 ? 137 TYR   A O     1 
ATOM   1025 C  CB    . TYR   A 1 140 ? 30.023 3.254   3.191  1.00 19.26 ? 137 TYR   A CB    1 
ATOM   1026 C  CG    . TYR   A 1 140 ? 31.025 2.144   3.003  1.00 17.84 ? 137 TYR   A CG    1 
ATOM   1027 C  CD1   . TYR   A 1 140 ? 31.331 1.587   1.760  1.00 17.85 ? 137 TYR   A CD1   1 
ATOM   1028 C  CD2   . TYR   A 1 140 ? 31.755 1.718   4.084  1.00 17.28 ? 137 TYR   A CD2   1 
ATOM   1029 C  CE1   . TYR   A 1 140 ? 32.235 0.545   1.690  1.00 17.48 ? 137 TYR   A CE1   1 
ATOM   1030 C  CE2   . TYR   A 1 140 ? 32.648 0.682   4.028  1.00 20.63 ? 137 TYR   A CE2   1 
ATOM   1031 C  CZ    . TYR   A 1 140 ? 32.938 0.125   2.799  1.00 18.53 ? 137 TYR   A CZ    1 
ATOM   1032 O  OH    . TYR   A 1 140 ? 33.831 -0.884  2.776  1.00 20.37 ? 137 TYR   A OH    1 
ATOM   1033 N  N     . GLY   A 1 141 ? 28.429 6.123   2.430  1.00 18.35 ? 138 GLY   A N     1 
ATOM   1034 C  CA    . GLY   A 1 141 ? 27.306 7.005   2.833  1.00 18.68 ? 138 GLY   A CA    1 
ATOM   1035 C  C     . GLY   A 1 141 ? 26.999 6.818   4.306  1.00 19.70 ? 138 GLY   A C     1 
ATOM   1036 O  O     . GLY   A 1 141 ? 25.835 6.958   4.696  1.00 21.78 ? 138 GLY   A O     1 
ATOM   1037 N  N     . ILE   A 1 142 ? 28.010 6.536   5.114  1.00 17.83 ? 139 ILE   A N     1 
ATOM   1038 C  CA    . ILE   A 1 142 ? 27.745 6.331   6.576  1.00 16.75 ? 139 ILE   A CA    1 
ATOM   1039 C  C     . ILE   A 1 142 ? 28.650 7.220   7.415  1.00 17.45 ? 139 ILE   A C     1 
ATOM   1040 O  O     . ILE   A 1 142 ? 29.712 7.654   6.931  1.00 18.95 ? 139 ILE   A O     1 
ATOM   1041 C  CB    . ILE   A 1 142 ? 27.926 4.856   6.970  1.00 16.93 ? 139 ILE   A CB    1 
ATOM   1042 C  CG1   . ILE   A 1 142 ? 29.403 4.422   6.917  1.00 15.93 ? 139 ILE   A CG1   1 
ATOM   1043 C  CG2   . ILE   A 1 142 ? 27.016 3.947   6.171  1.00 17.38 ? 139 ILE   A CG2   1 
ATOM   1044 C  CD1   . ILE   A 1 142 ? 29.656 2.983   7.247  1.00 16.62 ? 139 ILE   A CD1   1 
ATOM   1045 N  N     . PRO   A 1 143 ? 28.298 7.558   8.679  1.00 17.21 ? 140 PRO   A N     1 
ATOM   1046 C  CA    . PRO   A 1 143 ? 29.197 8.317   9.505  1.00 16.65 ? 140 PRO   A CA    1 
ATOM   1047 C  C     . PRO   A 1 143 ? 30.452 7.533   9.923  1.00 17.64 ? 140 PRO   A C     1 
ATOM   1048 O  O     . PRO   A 1 143 ? 30.455 6.396   9.957  1.00 18.69 ? 140 PRO   A O     1 
ATOM   1049 C  CB    . PRO   A 1 143 ? 28.350 8.618   10.782 1.00 16.43 ? 140 PRO   A CB    1 
ATOM   1050 C  CG    . PRO   A 1 143 ? 26.970 8.557   10.230 1.00 17.37 ? 140 PRO   A CG    1 
ATOM   1051 C  CD    . PRO   A 1 143 ? 26.984 7.345   9.333  1.00 18.34 ? 140 PRO   A CD    1 
ATOM   1052 N  N     . PHE   A 1 144 ? 31.507 8.288   10.173 1.00 18.94 ? 141 PHE   A N     1 
ATOM   1053 C  CA    . PHE   A 1 144 ? 32.765 7.716   10.660 1.00 18.44 ? 141 PHE   A CA    1 
ATOM   1054 C  C     . PHE   A 1 144 ? 33.146 8.447   11.949 1.00 20.68 ? 141 PHE   A C     1 
ATOM   1055 O  O     . PHE   A 1 144 ? 33.073 9.628   11.964 1.00 22.52 ? 141 PHE   A O     1 
ATOM   1056 C  CB    . PHE   A 1 144 ? 33.866 7.848   9.588  1.00 19.75 ? 141 PHE   A CB    1 
ATOM   1057 C  CG    . PHE   A 1 144 ? 35.228 7.565   10.156 1.00 19.60 ? 141 PHE   A CG    1 
ATOM   1058 C  CD1   . PHE   A 1 144 ? 35.539 6.337   10.675 1.00 20.57 ? 141 PHE   A CD1   1 
ATOM   1059 C  CD2   . PHE   A 1 144 ? 36.228 8.522   10.123 1.00 21.74 ? 141 PHE   A CD2   1 
ATOM   1060 C  CE1   . PHE   A 1 144 ? 36.760 6.079   11.259 1.00 19.74 ? 141 PHE   A CE1   1 
ATOM   1061 C  CE2   . PHE   A 1 144 ? 37.472 8.236   10.641 1.00 23.29 ? 141 PHE   A CE2   1 
ATOM   1062 C  CZ    . PHE   A 1 144 ? 37.750 7.019   11.177 1.00 21.40 ? 141 PHE   A CZ    1 
ATOM   1063 N  N     . ILE   A 1 145 ? 33.509 7.675   12.965 1.00 19.39 ? 142 ILE   A N     1 
ATOM   1064 C  CA    . ILE   A 1 145 ? 33.923 8.214   14.289 1.00 18.28 ? 142 ILE   A CA    1 
ATOM   1065 C  C     . ILE   A 1 145 ? 35.109 7.403   14.770 1.00 18.98 ? 142 ILE   A C     1 
ATOM   1066 O  O     . ILE   A 1 145 ? 35.100 6.226   14.691 1.00 18.54 ? 142 ILE   A O     1 
ATOM   1067 C  CB    . ILE   A 1 145 ? 32.752 8.130   15.332 1.00 21.54 ? 142 ILE   A CB    1 
ATOM   1068 C  CG1   . ILE   A 1 145 ? 31.533 8.930   14.888 1.00 27.81 ? 142 ILE   A CG1   1 
ATOM   1069 C  CG2   . ILE   A 1 145 ? 33.193 8.592   16.713 1.00 22.31 ? 142 ILE   A CG2   1 
ATOM   1070 C  CD1   . ILE   A 1 145 ? 30.374 8.878   15.891 1.00 29.70 ? 142 ILE   A CD1   1 
ATOM   1071 N  N     . GLU   A 1 146 ? 36.082 8.116   15.313 1.00 19.75 ? 143 GLU   A N     1 
ATOM   1072 C  CA    . GLU   A 1 146 ? 37.215 7.431   15.935 1.00 19.63 ? 143 GLU   A CA    1 
ATOM   1073 C  C     . GLU   A 1 146 ? 36.985 7.438   17.453 1.00 21.25 ? 143 GLU   A C     1 
ATOM   1074 O  O     . GLU   A 1 146 ? 36.683 8.463   17.966 1.00 21.55 ? 143 GLU   A O     1 
ATOM   1075 C  CB    . GLU   A 1 146 ? 38.534 8.152   15.649 1.00 18.89 ? 143 GLU   A CB    1 
ATOM   1076 C  CG    . GLU   A 1 146 ? 39.030 7.869   14.248 1.00 23.49 ? 143 GLU   A CG    1 
ATOM   1077 C  CD    . GLU   A 1 146 ? 40.487 8.187   14.039 1.00 24.34 ? 143 GLU   A CD    1 
ATOM   1078 O  OE1   . GLU   A 1 146 ? 41.105 8.755   14.858 1.00 25.49 ? 143 GLU   A OE1   1 
ATOM   1079 O  OE2   . GLU   A 1 146 ? 40.925 7.869   12.921 1.00 23.50 ? 143 GLU   A OE2   1 
ATOM   1080 N  N     . THR   A 1 147 ? 37.260 6.314   18.051 1.00 18.34 ? 144 THR   A N     1 
ATOM   1081 C  CA    . THR   A 1 147 ? 36.960 6.164   19.496 1.00 19.21 ? 144 THR   A CA    1 
ATOM   1082 C  C     . THR   A 1 147 ? 38.124 5.530   20.222 1.00 19.34 ? 144 THR   A C     1 
ATOM   1083 O  O     . THR   A 1 147 ? 39.004 4.942   19.581 1.00 18.50 ? 144 THR   A O     1 
ATOM   1084 C  CB    . THR   A 1 147 ? 35.824 5.133   19.639 1.00 18.77 ? 144 THR   A CB    1 
ATOM   1085 O  OG1   . THR   A 1 147 ? 36.128 3.850   19.115 1.00 17.89 ? 144 THR   A OG1   1 
ATOM   1086 C  CG2   . THR   A 1 147 ? 34.486 5.581   19.102 1.00 18.52 ? 144 THR   A CG2   1 
ATOM   1087 N  N     . SER   A 1 148 ? 38.161 5.744   21.539 1.00 20.30 ? 145 SER   A N     1 
ATOM   1088 C  CA    . SER   A 1 148 ? 39.029 4.988   22.446 1.00 22.17 ? 145 SER   A CA    1 
ATOM   1089 C  C     . SER   A 1 148 ? 38.149 4.348   23.533 1.00 21.76 ? 145 SER   A C     1 
ATOM   1090 O  O     . SER   A 1 148 ? 37.631 5.131   24.322 1.00 22.56 ? 145 SER   A O     1 
ATOM   1091 C  CB    . SER   A 1 148 ? 40.051 5.847   23.121 1.00 21.35 ? 145 SER   A CB    1 
ATOM   1092 O  OG    . SER   A 1 148 ? 40.809 5.037   23.950 1.00 21.93 ? 145 SER   A OG    1 
ATOM   1093 N  N     . ALA   A 1 149 ? 38.110 3.034   23.569 1.00 18.94 ? 146 ALA   A N     1 
ATOM   1094 C  CA    . ALA   A 1 149 ? 37.369 2.345   24.649 1.00 20.36 ? 146 ALA   A CA    1 
ATOM   1095 C  C     . ALA   A 1 149 ? 38.217 2.583   25.877 1.00 24.67 ? 146 ALA   A C     1 
ATOM   1096 O  O     . ALA   A 1 149 ? 37.652 2.711   26.904 1.00 24.97 ? 146 ALA   A O     1 
ATOM   1097 C  CB    . ALA   A 1 149 ? 37.240 0.893   24.389 1.00 22.14 ? 146 ALA   A CB    1 
ATOM   1098 N  N     . LYS   A 1 150 ? 39.524 2.705   25.782 1.00 21.14 ? 147 LYS   A N     1 
ATOM   1099 C  CA    . LYS   A 1 150 ? 40.397 2.892   26.975 1.00 23.74 ? 147 LYS   A CA    1 
ATOM   1100 C  C     . LYS   A 1 150 ? 40.117 4.227   27.680 1.00 24.00 ? 147 LYS   A C     1 
ATOM   1101 O  O     . LYS   A 1 150 ? 39.989 4.228   28.919 1.00 29.85 ? 147 LYS   A O     1 
ATOM   1102 C  CB    . LYS   A 1 150 ? 41.865 2.840   26.504 1.00 24.86 ? 147 LYS   A CB    1 
ATOM   1103 C  CG    . LYS   A 1 150 ? 42.875 2.844   27.638 1.00 30.27 ? 147 LYS   A CG    1 
ATOM   1104 C  CD    . LYS   A 1 150 ? 44.290 2.856   27.164 1.00 32.96 ? 147 LYS   A CD    1 
ATOM   1105 C  CE    . LYS   A 1 150 ? 45.316 3.005   28.269 1.00 37.60 ? 147 LYS   A CE    1 
ATOM   1106 N  NZ    . LYS   A 1 150 ? 46.577 3.635   27.788 1.00 38.71 ? 147 LYS   A NZ    1 
ATOM   1107 N  N     . THR   A 1 151 ? 39.959 5.316   26.960 1.00 26.30 ? 148 THR   A N     1 
ATOM   1108 C  CA    . THR   A 1 151 ? 39.760 6.640   27.591 1.00 28.72 ? 148 THR   A CA    1 
ATOM   1109 C  C     . THR   A 1 151 ? 38.309 7.119   27.525 1.00 27.69 ? 148 THR   A C     1 
ATOM   1110 O  O     . THR   A 1 151 ? 38.047 8.193   28.074 1.00 29.43 ? 148 THR   A O     1 
ATOM   1111 C  CB    . THR   A 1 151 ? 40.649 7.700   26.949 1.00 33.67 ? 148 THR   A CB    1 
ATOM   1112 O  OG1   . THR   A 1 151 ? 40.135 7.907   25.640 1.00 28.41 ? 148 THR   A OG1   1 
ATOM   1113 C  CG2   . THR   A 1 151 ? 42.079 7.242   26.863 1.00 35.23 ? 148 THR   A CG2   1 
ATOM   1114 N  N     . ARG   A 1 152 ? 37.441 6.385   26.834 1.00 25.19 ? 149 ARG   A N     1 
ATOM   1115 C  CA    . ARG   A 1 152 ? 35.989 6.655   26.620 1.00 26.04 ? 149 ARG   A CA    1 
ATOM   1116 C  C     . ARG   A 1 152 ? 35.765 7.743   25.569 1.00 26.57 ? 149 ARG   A C     1 
ATOM   1117 O  O     . ARG   A 1 152 ? 34.670 8.085   25.274 1.00 27.79 ? 149 ARG   A O     1 
ATOM   1118 C  CB    . ARG   A 1 152 ? 35.193 6.794   27.944 1.00 27.22 ? 149 ARG   A CB    1 
ATOM   1119 C  CG    . ARG   A 1 152 ? 33.696 6.646   27.730 1.00 34.11 ? 149 ARG   A CG    1 
ATOM   1120 C  CD    . ARG   A 1 152 ? 32.995 6.472   29.108 1.00 37.15 ? 149 ARG   A CD    1 
ATOM   1121 N  NE    . ARG   A 1 152 ? 31.599 6.041   29.078 1.00 40.21 ? 149 ARG   A NE    1 
ATOM   1122 C  CZ    . ARG   A 1 152 ? 30.558 6.819   28.780 1.00 47.42 ? 149 ARG   A CZ    1 
ATOM   1123 N  NH1   . ARG   A 1 152 ? 30.724 8.091   28.470 1.00 49.49 ? 149 ARG   A NH1   1 
ATOM   1124 N  NH2   . ARG   A 1 152 ? 29.330 6.325   28.812 1.00 53.67 ? 149 ARG   A NH2   1 
ATOM   1125 N  N     . GLN   A 1 153 ? 36.857 8.150   24.903 1.00 24.87 ? 150 GLN   A N     1 
ATOM   1126 C  CA    . GLN   A 1 153 ? 36.755 9.213   23.894 1.00 25.57 ? 150 GLN   A CA    1 
ATOM   1127 C  C     . GLN   A 1 153 ? 35.793 8.809   22.771 1.00 21.22 ? 150 GLN   A C     1 
ATOM   1128 O  O     . GLN   A 1 153 ? 35.964 7.745   22.235 1.00 21.42 ? 150 GLN   A O     1 
ATOM   1129 C  CB    . GLN   A 1 153 ? 38.142 9.390   23.278 1.00 29.14 ? 150 GLN   A CB    1 
ATOM   1130 C  CG    . GLN   A 1 153 ? 38.141 10.433  22.195 1.00 35.83 ? 150 GLN   A CG    1 
ATOM   1131 C  CD    . GLN   A 1 153 ? 38.491 11.772  22.763 1.00 41.78 ? 150 GLN   A CD    1 
ATOM   1132 O  OE1   . GLN   A 1 153 ? 38.641 11.922  23.968 1.00 53.45 ? 150 GLN   A OE1   1 
ATOM   1133 N  NE2   . GLN   A 1 153 ? 38.649 12.750  21.896 1.00 49.52 ? 150 GLN   A NE2   1 
ATOM   1134 N  N     . ARG   A 1 154 ? 34.714 9.565   22.603 1.00 21.40 ? 151 ARG   A N     1 
ATOM   1135 C  CA    . ARG   A 1 154 ? 33.684 9.413   21.544 1.00 22.49 ? 151 ARG   A CA    1 
ATOM   1136 C  C     . ARG   A 1 154 ? 32.910 8.085   21.619 1.00 23.02 ? 151 ARG   A C     1 
ATOM   1137 O  O     . ARG   A 1 154 ? 32.273 7.790   20.681 1.00 20.70 ? 151 ARG   A O     1 
ATOM   1138 C  CB    . ARG   A 1 154 ? 34.327 9.571   20.148 1.00 22.63 ? 151 ARG   A CB    1 
ATOM   1139 C  CG    . ARG   A 1 154 ? 34.875 10.960  19.933 1.00 22.24 ? 151 ARG   A CG    1 
ATOM   1140 C  CD    . ARG   A 1 154 ? 34.879 11.350  18.474 1.00 27.27 ? 151 ARG   A CD    1 
ATOM   1141 N  NE    . ARG   A 1 154 ? 33.581 11.916  18.232 1.00 31.99 ? 151 ARG   A NE    1 
ATOM   1142 C  CZ    . ARG   A 1 154 ? 33.045 12.232  17.083 1.00 29.36 ? 151 ARG   A CZ    1 
ATOM   1143 N  NH1   . ARG   A 1 154 ? 33.713 12.067  15.958 1.00 33.43 ? 151 ARG   A NH1   1 
ATOM   1144 N  NH2   . ARG   A 1 154 ? 31.832 12.745  17.061 1.00 32.66 ? 151 ARG   A NH2   1 
ATOM   1145 N  N     . VAL   A 1 155 ? 32.975 7.339   22.708 1.00 19.67 ? 152 VAL   A N     1 
ATOM   1146 C  CA    . VAL   A 1 155 ? 32.226 6.056   22.735 1.00 19.20 ? 152 VAL   A CA    1 
ATOM   1147 C  C     . VAL   A 1 155 ? 30.707 6.289   22.692 1.00 20.98 ? 152 VAL   A C     1 
ATOM   1148 O  O     . VAL   A 1 155 ? 30.048 5.665   21.955 1.00 18.89 ? 152 VAL   A O     1 
ATOM   1149 C  CB    . VAL   A 1 155 ? 32.623 5.197   23.941 1.00 19.23 ? 152 VAL   A CB    1 
ATOM   1150 C  CG1   . VAL   A 1 155 ? 31.731 3.985   24.034 1.00 20.10 ? 152 VAL   A CG1   1 
ATOM   1151 C  CG2   . VAL   A 1 155 ? 34.076 4.767   23.809 1.00 20.38 ? 152 VAL   A CG2   1 
ATOM   1152 N  N     . GLU   A 1 156 ? 30.198 7.191   23.530 1.00 20.96 ? 153 GLU   A N     1 
ATOM   1153 C  CA    . GLU   A 1 156 ? 28.737 7.446   23.479 1.00 21.24 ? 153 GLU   A CA    1 
ATOM   1154 C  C     . GLU   A 1 156 ? 28.343 8.016   22.107 1.00 20.42 ? 153 GLU   A C     1 
ATOM   1155 O  O     . GLU   A 1 156 ? 27.378 7.608   21.577 1.00 20.07 ? 153 GLU   A O     1 
ATOM   1156 C  CB    . GLU   A 1 156 ? 28.445 8.349   24.676 1.00 22.66 ? 153 GLU   A CB    1 
ATOM   1157 C  CG    . GLU   A 1 156 ? 27.003 8.771   24.738 1.00 31.26 ? 153 GLU   A CG    1 
ATOM   1158 C  CD    . GLU   A 1 156 ? 26.850 9.890   25.743 1.00 32.71 ? 153 GLU   A CD    1 
ATOM   1159 O  OE1   . GLU   A 1 156 ? 26.670 11.002  25.331 1.00 38.48 ? 153 GLU   A OE1   1 
ATOM   1160 O  OE2   . GLU   A 1 156 ? 27.033 9.604   26.884 1.00 36.58 ? 153 GLU   A OE2   1 
ATOM   1161 N  N     . ASP   A 1 157 ? 29.180 8.905   21.557 1.00 20.81 ? 154 ASP   A N     1 
ATOM   1162 C  CA    . ASP   A 1 157 ? 28.949 9.516   20.224 1.00 19.45 ? 154 ASP   A CA    1 
ATOM   1163 C  C     . ASP   A 1 157 ? 28.794 8.418   19.159 1.00 20.04 ? 154 ASP   A C     1 
ATOM   1164 O  O     . ASP   A 1 157 ? 27.916 8.544   18.357 1.00 18.48 ? 154 ASP   A O     1 
ATOM   1165 C  CB    . ASP   A 1 157 ? 30.143 10.388  19.839 1.00 22.04 ? 154 ASP   A CB    1 
ATOM   1166 C  CG    . ASP   A 1 157 ? 30.280 11.732  20.512 1.00 28.47 ? 154 ASP   A CG    1 
ATOM   1167 O  OD1   . ASP   A 1 157 ? 29.377 12.144  21.207 1.00 29.59 ? 154 ASP   A OD1   1 
ATOM   1168 O  OD2   . ASP   A 1 157 ? 31.335 12.349  20.366 1.00 32.40 ? 154 ASP   A OD2   1 
ATOM   1169 N  N     . ALA   A 1 158 ? 29.593 7.360   19.239 1.00 17.64 ? 155 ALA   A N     1 
ATOM   1170 C  CA    . ALA   A 1 158 ? 29.486 6.283   18.226 1.00 19.17 ? 155 ALA   A CA    1 
ATOM   1171 C  C     . ALA   A 1 158 ? 28.124 5.597   18.325 1.00 17.79 ? 155 ALA   A C     1 
ATOM   1172 O  O     . ALA   A 1 158 ? 27.425 5.474   17.346 1.00 17.80 ? 155 ALA   A O     1 
ATOM   1173 C  CB    . ALA   A 1 158 ? 30.605 5.297   18.393 1.00 21.04 ? 155 ALA   A CB    1 
ATOM   1174 N  N     . PHE   A 1 159 ? 27.740 5.190   19.521 1.00 16.74 ? 156 PHE   A N     1 
ATOM   1175 C  CA    . PHE   A 1 159 ? 26.460 4.469   19.694 1.00 17.32 ? 156 PHE   A CA    1 
ATOM   1176 C  C     . PHE   A 1 159 ? 25.273 5.420   19.434 1.00 17.90 ? 156 PHE   A C     1 
ATOM   1177 O  O     . PHE   A 1 159 ? 24.283 4.983   18.838 1.00 19.09 ? 156 PHE   A O     1 
ATOM   1178 C  CB    . PHE   A 1 159 ? 26.393 3.894   21.104 1.00 17.54 ? 156 PHE   A CB    1 
ATOM   1179 C  CG    . PHE   A 1 159 ? 27.187 2.629   21.293 1.00 17.14 ? 156 PHE   A CG    1 
ATOM   1180 C  CD1   . PHE   A 1 159 ? 26.656 1.403   20.921 1.00 18.16 ? 156 PHE   A CD1   1 
ATOM   1181 C  CD2   . PHE   A 1 159 ? 28.489 2.663   21.783 1.00 18.20 ? 156 PHE   A CD2   1 
ATOM   1182 C  CE1   . PHE   A 1 159 ? 27.363 0.230   21.117 1.00 17.25 ? 156 PHE   A CE1   1 
ATOM   1183 C  CE2   . PHE   A 1 159 ? 29.174 1.478   21.993 1.00 18.73 ? 156 PHE   A CE2   1 
ATOM   1184 C  CZ    . PHE   A 1 159 ? 28.647 0.277   21.623 1.00 20.52 ? 156 PHE   A CZ    1 
ATOM   1185 N  N     . TYR   A 1 160 ? 25.334 6.655   19.914 1.00 17.28 ? 157 TYR   A N     1 
ATOM   1186 C  CA    . TYR   A 1 160 ? 24.183 7.595   19.789 1.00 19.40 ? 157 TYR   A CA    1 
ATOM   1187 C  C     . TYR   A 1 160 ? 24.047 8.022   18.327 1.00 19.04 ? 157 TYR   A C     1 
ATOM   1188 O  O     . TYR   A 1 160 ? 22.925 8.187   17.833 1.00 19.46 ? 157 TYR   A O     1 
ATOM   1189 C  CB    . TYR   A 1 160 ? 24.355 8.803   20.702 1.00 21.04 ? 157 TYR   A CB    1 
ATOM   1190 C  CG    . TYR   A 1 160 ? 24.049 8.552   22.159 1.00 23.47 ? 157 TYR   A CG    1 
ATOM   1191 C  CD1   . TYR   A 1 160 ? 24.001 7.279   22.716 1.00 20.96 ? 157 TYR   A CD1   1 
ATOM   1192 C  CD2   . TYR   A 1 160 ? 23.920 9.636   22.989 1.00 28.73 ? 157 TYR   A CD2   1 
ATOM   1193 C  CE1   . TYR   A 1 160 ? 23.726 7.098   24.073 1.00 25.47 ? 157 TYR   A CE1   1 
ATOM   1194 C  CE2   . TYR   A 1 160 ? 23.631 9.478   24.330 1.00 28.63 ? 157 TYR   A CE2   1 
ATOM   1195 C  CZ    . TYR   A 1 160 ? 23.559 8.211   24.890 1.00 30.01 ? 157 TYR   A CZ    1 
ATOM   1196 O  OH    . TYR   A 1 160 ? 23.243 8.093   26.224 1.00 32.40 ? 157 TYR   A OH    1 
ATOM   1197 N  N     . THR   A 1 161 ? 25.171 8.130   17.597 1.00 18.31 ? 158 THR   A N     1 
ATOM   1198 C  CA    . THR   A 1 161 ? 25.123 8.465   16.155 1.00 17.44 ? 158 THR   A CA    1 
ATOM   1199 C  C     . THR   A 1 161 ? 24.419 7.305   15.425 1.00 16.24 ? 158 THR   A C     1 
ATOM   1200 O  O     . THR   A 1 161 ? 23.597 7.576   14.546 1.00 17.97 ? 158 THR   A O     1 
ATOM   1201 C  CB    . THR   A 1 161 ? 26.524 8.761   15.604 1.00 17.54 ? 158 THR   A CB    1 
ATOM   1202 O  OG1   . THR   A 1 161 ? 27.051 9.921   16.235 1.00 20.58 ? 158 THR   A OG1   1 
ATOM   1203 C  CG2   . THR   A 1 161 ? 26.481 8.990   14.108 1.00 18.47 ? 158 THR   A CG2   1 
ATOM   1204 N  N     . LEU   A 1 162 ? 24.689 6.066   15.821 1.00 16.80 ? 159 LEU   A N     1 
ATOM   1205 C  CA    . LEU   A 1 162 ? 24.044 4.890   15.233 1.00 15.11 ? 159 LEU   A CA    1 
ATOM   1206 C  C     . LEU   A 1 162 ? 22.530 4.982   15.486 1.00 17.83 ? 159 LEU   A C     1 
ATOM   1207 O  O     . LEU   A 1 162 ? 21.752 4.738   14.564 1.00 15.75 ? 159 LEU   A O     1 
ATOM   1208 C  CB    . LEU   A 1 162 ? 24.659 3.582   15.717 1.00 14.39 ? 159 LEU   A CB    1 
ATOM   1209 C  CG    . LEU   A 1 162 ? 24.049 2.315   15.125 1.00 15.13 ? 159 LEU   A CG    1 
ATOM   1210 C  CD1   . LEU   A 1 162 ? 24.145 2.301   13.588 1.00 16.44 ? 159 LEU   A CD1   1 
ATOM   1211 C  CD2   . LEU   A 1 162 ? 24.666 1.064   15.712 1.00 14.69 ? 159 LEU   A CD2   1 
ATOM   1212 N  N     . VAL   A 1 163 ? 22.124 5.291   16.725 1.00 16.75 ? 160 VAL   A N     1 
ATOM   1213 C  CA    . VAL   A 1 163 ? 20.657 5.431   16.980 1.00 17.78 ? 160 VAL   A CA    1 
ATOM   1214 C  C     . VAL   A 1 163 ? 20.070 6.536   16.089 1.00 18.00 ? 160 VAL   A C     1 
ATOM   1215 O  O     . VAL   A 1 163 ? 18.956 6.334   15.505 1.00 18.08 ? 160 VAL   A O     1 
ATOM   1216 C  CB    . VAL   A 1 163 ? 20.428 5.671   18.467 1.00 18.55 ? 160 VAL   A CB    1 
ATOM   1217 C  CG1   . VAL   A 1 163 ? 18.956 6.042   18.687 1.00 19.28 ? 160 VAL   A CG1   1 
ATOM   1218 C  CG2   . VAL   A 1 163 ? 20.849 4.444   19.258 1.00 19.63 ? 160 VAL   A CG2   1 
ATOM   1219 N  N     . ARG   A 1 164 ? 20.757 7.668   15.942 1.00 17.71 ? 161 ARG   A N     1 
ATOM   1220 C  CA    . ARG   A 1 164 ? 20.242 8.769   15.088 1.00 16.56 ? 161 ARG   A CA    1 
ATOM   1221 C  C     . ARG   A 1 164 ? 20.101 8.301   13.627 1.00 19.00 ? 161 ARG   A C     1 
ATOM   1222 O  O     . ARG   A 1 164 ? 19.171 8.682   13.007 1.00 19.15 ? 161 ARG   A O     1 
ATOM   1223 C  CB    . ARG   A 1 164 ? 21.107 10.018  15.238 1.00 21.14 ? 161 ARG   A CB    1 
ATOM   1224 C  CG    . ARG   A 1 164 ? 21.059 10.652  16.627 1.00 24.55 ? 161 ARG   A CG    1 
ATOM   1225 C  CD    . ARG   A 1 164 ? 21.865 11.917  16.780 1.00 27.02 ? 161 ARG   A CD    1 
ATOM   1226 N  NE    . ARG   A 1 164 ? 21.473 12.743  17.911 1.00 30.81 ? 161 ARG   A NE    1 
ATOM   1227 C  CZ    . ARG   A 1 164 ? 22.183 12.916  18.997 1.00 27.89 ? 161 ARG   A CZ    1 
ATOM   1228 N  NH1   . ARG   A 1 164 ? 23.358 12.348  19.113 1.00 33.00 ? 161 ARG   A NH1   1 
ATOM   1229 N  NH2   . ARG   A 1 164 ? 21.733 13.703  19.959 1.00 36.81 ? 161 ARG   A NH2   1 
ATOM   1230 N  N     . GLU   A 1 165 ? 21.037 7.447   13.183 1.00 18.23 ? 162 GLU   A N     1 
ATOM   1231 C  CA    . GLU   A 1 165 ? 20.941 6.925   11.788 1.00 19.07 ? 162 GLU   A CA    1 
ATOM   1232 C  C     . GLU   A 1 165 ? 19.703 6.028   11.643 1.00 19.07 ? 162 GLU   A C     1 
ATOM   1233 O  O     . GLU   A 1 165 ? 19.036 6.080   10.606 1.00 19.62 ? 162 GLU   A O     1 
ATOM   1234 C  CB    . GLU   A 1 165 ? 22.226 6.155   11.461 1.00 17.90 ? 162 GLU   A CB    1 
ATOM   1235 C  CG    . GLU   A 1 165 ? 23.422 7.075   11.213 1.00 19.77 ? 162 GLU   A CG    1 
ATOM   1236 C  CD    . GLU   A 1 165 ? 23.357 7.840   9.910  1.00 21.39 ? 162 GLU   A CD    1 
ATOM   1237 O  OE1   . GLU   A 1 165 ? 23.244 7.173   8.893  1.00 22.30 ? 162 GLU   A OE1   1 
ATOM   1238 O  OE2   . GLU   A 1 165 ? 23.396 9.028   9.950  1.00 25.13 ? 162 GLU   A OE2   1 
ATOM   1239 N  N     . ILE   A 1 166 ? 19.429 5.243   12.701 1.00 18.30 ? 163 ILE   A N     1 
ATOM   1240 C  CA    . ILE   A 1 166 ? 18.258 4.323   12.649 1.00 18.95 ? 163 ILE   A CA    1 
ATOM   1241 C  C     . ILE   A 1 166 ? 17.003 5.200   12.612 1.00 20.15 ? 163 ILE   A C     1 
ATOM   1242 O  O     . ILE   A 1 166 ? 16.133 4.936   11.818 1.00 18.79 ? 163 ILE   A O     1 
ATOM   1243 C  CB    . ILE   A 1 166 ? 18.234 3.338   13.836 1.00 18.83 ? 163 ILE   A CB    1 
ATOM   1244 C  CG1   . ILE   A 1 166 ? 19.432 2.354   13.816 1.00 17.88 ? 163 ILE   A CG1   1 
ATOM   1245 C  CG2   . ILE   A 1 166 ? 16.888 2.606   13.875 1.00 20.26 ? 163 ILE   A CG2   1 
ATOM   1246 C  CD1   . ILE   A 1 166 ? 19.580 1.545   15.103 1.00 18.34 ? 163 ILE   A CD1   1 
ATOM   1247 N  N     . ARG   A 1 167 ? 16.964 6.267   13.408 1.00 19.40 ? 164 ARG   A N     1 
ATOM   1248 C  CA    . ARG   A 1 167 ? 15.783 7.161   13.432 1.00 20.06 ? 164 ARG   A CA    1 
ATOM   1249 C  C     . ARG   A 1 167 ? 15.633 7.815   12.057 1.00 23.25 ? 164 ARG   A C     1 
ATOM   1250 O  O     . ARG   A 1 167 ? 14.504 7.967   11.585 1.00 24.71 ? 164 ARG   A O     1 
ATOM   1251 C  CB    . ARG   A 1 167 ? 15.968 8.214   14.520 1.00 21.44 ? 164 ARG   A CB    1 
ATOM   1252 C  CG    . ARG   A 1 167 ? 15.767 7.629   15.912 1.00 22.24 ? 164 ARG   A CG    1 
ATOM   1253 C  CD    . ARG   A 1 167 ? 16.114 8.633   16.992 1.00 23.75 ? 164 ARG   A CD    1 
ATOM   1254 N  NE    . ARG   A 1 167 ? 15.773 8.084   18.295 1.00 24.40 ? 164 ARG   A NE    1 
ATOM   1255 C  CZ    . ARG   A 1 167 ? 15.940 8.754   19.435 1.00 27.40 ? 164 ARG   A CZ    1 
ATOM   1256 N  NH1   . ARG   A 1 167 ? 16.396 9.997   19.389 1.00 29.71 ? 164 ARG   A NH1   1 
ATOM   1257 N  NH2   . ARG   A 1 167 ? 15.588 8.205   20.592 1.00 30.54 ? 164 ARG   A NH2   1 
ATOM   1258 N  N     . GLN   A 1 168 ? 16.738 8.292   11.471 1.00 21.59 ? 165 GLN   A N     1 
ATOM   1259 C  CA    . GLN   A 1 168 ? 16.639 8.950   10.136 1.00 23.75 ? 165 GLN   A CA    1 
ATOM   1260 C  C     . GLN   A 1 168 ? 16.119 7.922   9.126  1.00 24.79 ? 165 GLN   A C     1 
ATOM   1261 O  O     . GLN   A 1 168 ? 15.263 8.250   8.340  1.00 27.11 ? 165 GLN   A O     1 
ATOM   1262 C  CB    . GLN   A 1 168 ? 17.964 9.640   9.762  1.00 28.76 ? 165 GLN   A CB    1 
ATOM   1263 C  CG    . GLN   A 1 168 ? 18.285 10.810  10.683 1.00 37.84 ? 165 GLN   A CG    1 
ATOM   1264 C  CD    . GLN   A 1 168 ? 19.460 11.711  10.466 1.00 40.42 ? 165 GLN   A CD    1 
ATOM   1265 O  OE1   . GLN   A 1 168 ? 19.617 12.306  9.413  1.00 51.35 ? 165 GLN   A OE1   1 
ATOM   1266 N  NE2   . GLN   A 1 168 ? 20.234 11.896  11.517 1.00 51.70 ? 165 GLN   A NE2   1 
ATOM   1267 N  N     . TYR   A 1 169 ? 16.581 6.689   9.229  1.00 22.55 ? 166 TYR   A N     1 
ATOM   1268 C  CA    . TYR   A 1 169 ? 16.160 5.609   8.302  1.00 22.43 ? 166 TYR   A CA    1 
ATOM   1269 C  C     . TYR   A 1 169 ? 14.654 5.369   8.417  1.00 27.24 ? 166 TYR   A C     1 
ATOM   1270 O  O     . TYR   A 1 169 ? 14.023 5.118   7.412  1.00 27.63 ? 166 TYR   A O     1 
ATOM   1271 C  CB    . TYR   A 1 169 ? 16.954 4.334   8.585  1.00 23.86 ? 166 TYR   A CB    1 
ATOM   1272 C  CG    . TYR   A 1 169 ? 16.608 3.134   7.753  1.00 28.25 ? 166 TYR   A CG    1 
ATOM   1273 C  CD1   . TYR   A 1 169 ? 16.988 3.056   6.413  1.00 34.95 ? 166 TYR   A CD1   1 
ATOM   1274 C  CD2   . TYR   A 1 169 ? 15.982 2.034   8.315  1.00 30.58 ? 166 TYR   A CD2   1 
ATOM   1275 C  CE1   . TYR   A 1 169 ? 16.687 1.940   5.644  1.00 40.52 ? 166 TYR   A CE1   1 
ATOM   1276 C  CE2   . TYR   A 1 169 ? 15.689 0.907   7.562  1.00 37.55 ? 166 TYR   A CE2   1 
ATOM   1277 C  CZ    . TYR   A 1 169 ? 16.039 0.865   6.223  1.00 37.27 ? 166 TYR   A CZ    1 
ATOM   1278 O  OH    . TYR   A 1 169 ? 15.746 -0.224  5.463  1.00 39.13 ? 166 TYR   A OH    1 
ATOM   1279 N  N     . ARG   A 1 170 ? 14.147 5.423   9.652  1.00 27.67 ? 167 ARG   A N     1 
ATOM   1280 C  CA    . ARG   A 1 170 ? 12.712 5.096   9.900  1.00 27.65 ? 167 ARG   A CA    1 
ATOM   1281 C  C     . ARG   A 1 170 ? 11.800 6.189   9.357  1.00 29.19 ? 167 ARG   A C     1 
ATOM   1282 O  O     . ARG   A 1 170 ? 10.630 5.913   9.249  1.00 34.79 ? 167 ARG   A O     1 
ATOM   1283 C  CB    . ARG   A 1 170 ? 12.467 4.819   11.385 1.00 27.13 ? 167 ARG   A CB    1 
ATOM   1284 C  CG    . ARG   A 1 170 ? 12.953 3.457   11.840 1.00 32.26 ? 167 ARG   A CG    1 
ATOM   1285 C  CD    . ARG   A 1 170 ? 12.705 3.248   13.311 1.00 29.94 ? 167 ARG   A CD    1 
ATOM   1286 N  NE    . ARG   A 1 170 ? 13.261 2.061   13.889 1.00 30.74 ? 167 ARG   A NE    1 
ATOM   1287 C  CZ    . ARG   A 1 170 ? 13.249 1.818   15.171 1.00 30.58 ? 167 ARG   A CZ    1 
ATOM   1288 N  NH1   . ARG   A 1 170 ? 12.663 2.655   15.995 1.00 38.24 ? 167 ARG   A NH1   1 
ATOM   1289 N  NH2   . ARG   A 1 170 ? 13.822 0.744   15.643 1.00 48.36 ? 167 ARG   A NH2   1 
ATOM   1290 N  N     . LEU   A 1 171 ? 12.333 7.359   9.082  1.00 29.44 ? 168 LEU   A N     1 
ATOM   1291 C  CA    . LEU   A 1 171 ? 11.512 8.425   8.467  1.00 33.82 ? 168 LEU   A CA    1 
ATOM   1292 C  C     . LEU   A 1 171 ? 11.455 8.321   6.930  1.00 35.36 ? 168 LEU   A C     1 
ATOM   1293 O  O     . LEU   A 1 171 ? 10.654 9.039   6.334  1.00 36.04 ? 168 LEU   A O     1 
ATOM   1294 C  CB    . LEU   A 1 171 ? 12.036 9.785   8.919  1.00 38.92 ? 168 LEU   A CB    1 
ATOM   1295 C  CG    . LEU   A 1 171 ? 11.355 10.236  10.213 1.00 42.01 ? 168 LEU   A CG    1 
ATOM   1296 C  CD1   . LEU   A 1 171 ? 11.431 9.136   11.238 1.00 45.40 ? 168 LEU   A CD1   1 
ATOM   1297 C  CD2   . LEU   A 1 171 ? 11.871 11.546  10.745 1.00 39.44 ? 168 LEU   A CD2   1 
ATOM   1298 N  N     . LYS   A 1 172 ? 12.199 7.408   6.337  1.00 31.09 ? 169 LYS   A N     1 
ATOM   1299 C  CA    . LYS   A 1 172 ? 12.355 7.288   4.862  1.00 31.88 ? 169 LYS   A CA    1 
ATOM   1300 C  C     . LYS   A 1 172 ? 11.126 6.609   4.238  1.00 36.65 ? 169 LYS   A C     1 
ATOM   1301 O  O     . LYS   A 1 172 ? 11.044 6.509   2.997  1.00 41.19 ? 169 LYS   A O     1 
ATOM   1302 C  CB    . LYS   A 1 172 ? 13.648 6.524   4.548  1.00 31.37 ? 169 LYS   A CB    1 
ATOM   1303 C  CG    . LYS   A 1 172 ? 14.922 7.290   4.873  1.00 34.99 ? 169 LYS   A CG    1 
ATOM   1304 C  CD    . LYS   A 1 172 ? 16.143 6.833   4.084  1.00 38.19 ? 169 LYS   A CD    1 
ATOM   1305 C  CE    . LYS   A 1 172 ? 17.365 7.677   4.363  1.00 40.83 ? 169 LYS   A CE    1 
ATOM   1306 N  NZ    . LYS   A 1 172 ? 17.940 7.388   5.698  1.00 45.54 ? 169 LYS   A NZ    1 
ATOM   1307 O  OXT   . LYS   A 1 172 ? 10.193 6.160   4.928  1.00 42.52 ? 169 LYS   A OXT   1 
HETATM 1308 P  PG    . GNP   B 2 .   ? 37.037 -10.509 20.003 1.00 25.57 ? 201 GNP   A PG    1 
HETATM 1309 O  O1G   . GNP   B 2 .   ? 35.776 -10.777 20.753 1.00 25.13 ? 201 GNP   A O1G   1 
HETATM 1310 O  O2G   . GNP   B 2 .   ? 37.768 -11.691 20.295 1.00 29.86 ? 201 GNP   A O2G   1 
HETATM 1311 O  O3G   . GNP   B 2 .   ? 36.610 -10.445 18.612 1.00 26.95 ? 201 GNP   A O3G   1 
HETATM 1312 N  N3B   . GNP   B 2 .   ? 37.719 -9.228  20.664 1.00 22.81 ? 201 GNP   A N3B   1 
HETATM 1313 P  PB    . GNP   B 2 .   ? 37.154 -7.732  20.741 1.00 20.51 ? 201 GNP   A PB    1 
HETATM 1314 O  O1B   . GNP   B 2 .   ? 36.902 -7.036  19.434 1.00 18.98 ? 201 GNP   A O1B   1 
HETATM 1315 O  O2B   . GNP   B 2 .   ? 35.830 -7.720  21.565 1.00 20.43 ? 201 GNP   A O2B   1 
HETATM 1316 O  O3A   . GNP   B 2 .   ? 38.110 -6.809  21.554 1.00 23.52 ? 201 GNP   A O3A   1 
HETATM 1317 P  PA    . GNP   B 2 .   ? 38.324 -6.580  23.133 1.00 22.39 ? 201 GNP   A PA    1 
HETATM 1318 O  O1A   . GNP   B 2 .   ? 38.460 -7.929  23.613 1.00 22.92 ? 201 GNP   A O1A   1 
HETATM 1319 O  O2A   . GNP   B 2 .   ? 37.335 -5.559  23.566 1.00 22.23 ? 201 GNP   A O2A   1 
HETATM 1320 O  "O5'" . GNP   B 2 .   ? 39.815 -5.936  23.158 1.00 22.15 ? 201 GNP   A "O5'" 1 
HETATM 1321 C  "C5'" . GNP   B 2 .   ? 40.995 -6.632  22.617 1.00 25.22 ? 201 GNP   A "C5'" 1 
HETATM 1322 C  "C4'" . GNP   B 2 .   ? 42.212 -5.962  23.202 1.00 19.45 ? 201 GNP   A "C4'" 1 
HETATM 1323 O  "O4'" . GNP   B 2 .   ? 42.207 -4.583  22.815 1.00 20.60 ? 201 GNP   A "O4'" 1 
HETATM 1324 C  "C3'" . GNP   B 2 .   ? 42.253 -5.959  24.730 1.00 23.80 ? 201 GNP   A "C3'" 1 
HETATM 1325 O  "O3'" . GNP   B 2 .   ? 43.598 -6.085  25.159 1.00 25.60 ? 201 GNP   A "O3'" 1 
HETATM 1326 C  "C2'" . GNP   B 2 .   ? 41.672 -4.586  25.041 1.00 24.14 ? 201 GNP   A "C2'" 1 
HETATM 1327 O  "O2'" . GNP   B 2 .   ? 42.151 -4.139  26.271 1.00 27.94 ? 201 GNP   A "O2'" 1 
HETATM 1328 C  "C1'" . GNP   B 2 .   ? 42.289 -3.742  23.933 1.00 22.73 ? 201 GNP   A "C1'" 1 
HETATM 1329 N  N9    . GNP   B 2 .   ? 41.556 -2.522  23.643 1.00 20.69 ? 201 GNP   A N9    1 
HETATM 1330 C  C8    . GNP   B 2 .   ? 40.224 -2.430  23.291 1.00 18.00 ? 201 GNP   A C8    1 
HETATM 1331 N  N7    . GNP   B 2 .   ? 39.859 -1.216  23.066 1.00 18.25 ? 201 GNP   A N7    1 
HETATM 1332 C  C5    . GNP   B 2 .   ? 41.004 -0.452  23.201 1.00 19.43 ? 201 GNP   A C5    1 
HETATM 1333 C  C6    . GNP   B 2 .   ? 41.212 0.929   23.045 1.00 21.10 ? 201 GNP   A C6    1 
HETATM 1334 O  O6    . GNP   B 2 .   ? 40.448 1.799   22.677 1.00 21.22 ? 201 GNP   A O6    1 
HETATM 1335 N  N1    . GNP   B 2 .   ? 42.562 1.283   23.233 1.00 20.55 ? 201 GNP   A N1    1 
HETATM 1336 C  C2    . GNP   B 2 .   ? 43.510 0.411   23.650 1.00 21.70 ? 201 GNP   A C2    1 
HETATM 1337 N  N2    . GNP   B 2 .   ? 44.728 0.939   23.820 1.00 26.90 ? 201 GNP   A N2    1 
HETATM 1338 N  N3    . GNP   B 2 .   ? 43.327 -0.885  23.788 1.00 21.87 ? 201 GNP   A N3    1 
HETATM 1339 C  C4    . GNP   B 2 .   ? 42.033 -1.255  23.588 1.00 20.98 ? 201 GNP   A C4    1 
HETATM 1340 MG MG    . MG    C 3 .   ? 34.821 -9.511  22.277 1.00 19.38 ? 202 MG    A MG    1 
HETATM 1341 CO CO    . CO    D 4 .   ? 38.520 -3.025  36.347 1.00 42.49 ? 203 CO    A CO    1 
HETATM 1342 CO CO    . CO    E 4 .   ? 33.265 -8.680  -1.500 1.00 21.46 ? 204 CO    A CO    1 
HETATM 1343 C  CBK   . A1IK8 F 5 .   ? 22.003 -16.431 24.347 1.00 35.99 ? 205 A1IK8 A CBK   1 
HETATM 1344 C  CBL   . A1IK8 F 5 .   ? 22.120 -17.457 25.434 1.00 38.95 ? 205 A1IK8 A CBL   1 
HETATM 1345 C  CBM   . A1IK8 F 5 .   ? 23.123 -16.889 26.478 1.00 34.19 ? 205 A1IK8 A CBM   1 
HETATM 1346 N  NBP   . A1IK8 F 5 .   ? 22.513 -15.668 27.041 1.00 42.44 ? 205 A1IK8 A NBP   1 
HETATM 1347 C  CBN   . A1IK8 F 5 .   ? 24.480 -16.530 25.850 1.00 37.81 ? 205 A1IK8 A CBN   1 
HETATM 1348 C  CBO   . A1IK8 F 5 .   ? 24.271 -15.493 24.737 1.00 33.99 ? 205 A1IK8 A CBO   1 
HETATM 1349 C  CBJ   . A1IK8 F 5 .   ? 23.377 -16.164 23.718 1.00 34.35 ? 205 A1IK8 A CBJ   1 
HETATM 1350 N  NAQ   . A1IK8 F 5 .   ? 23.208 -15.407 22.437 1.00 26.51 ? 205 A1IK8 A NAQ   1 
HETATM 1351 C  CAB   . A1IK8 F 5 .   ? 22.797 -16.122 21.373 1.00 26.40 ? 205 A1IK8 A CAB   1 
HETATM 1352 O  OAA   . A1IK8 F 5 .   ? 22.628 -17.346 21.466 1.00 33.68 ? 205 A1IK8 A OAA   1 
HETATM 1353 C  CAR   . A1IK8 F 5 .   ? 23.511 -13.968 22.361 1.00 24.36 ? 205 A1IK8 A CAR   1 
HETATM 1354 C  CAS   . A1IK8 F 5 .   ? 22.492 -13.009 22.976 1.00 28.46 ? 205 A1IK8 A CAS   1 
HETATM 1355 C  CAT   . A1IK8 F 5 .   ? 21.179 -12.895 22.175 1.00 26.38 ? 205 A1IK8 A CAT   1 
HETATM 1356 C  CAU   . A1IK8 F 5 .   ? 20.461 -11.712 22.546 1.00 22.35 ? 205 A1IK8 A CAU   1 
HETATM 1357 C  CAV   . A1IK8 F 5 .   ? 19.141 -11.611 21.762 1.00 23.61 ? 205 A1IK8 A CAV   1 
HETATM 1358 N  NAW   . A1IK8 F 5 .   ? 19.379 -11.131 20.348 1.00 22.30 ? 205 A1IK8 A NAW   1 
HETATM 1359 C  CAX   . A1IK8 F 5 .   ? 19.695 -9.837  20.114 1.00 22.26 ? 205 A1IK8 A CAX   1 
HETATM 1360 C  CAY   . A1IK8 F 5 .   ? 19.861 -8.752  20.934 1.00 21.25 ? 205 A1IK8 A CAY   1 
HETATM 1361 O  OBD   . A1IK8 F 5 .   ? 19.630 -8.828  22.303 1.00 22.80 ? 205 A1IK8 A OBD   1 
HETATM 1362 C  CAZ   . A1IK8 F 5 .   ? 20.206 -7.476  20.508 1.00 21.20 ? 205 A1IK8 A CAZ   1 
HETATM 1363 C  CBA   . A1IK8 F 5 .   ? 20.429 -7.318  19.126 1.00 19.49 ? 205 A1IK8 A CBA   1 
HETATM 1364 C  CBB   . A1IK8 F 5 .   ? 20.272 -8.404  18.294 1.00 19.35 ? 205 A1IK8 A CBB   1 
HETATM 1365 CL CLBC  . A1IK8 F 5 .   ? 20.539 -8.216  16.575 1.00 21.54 ? 205 A1IK8 A CLBC  1 
HETATM 1366 C  CBI   . A1IK8 F 5 .   ? 19.926 -9.648  18.750 1.00 21.41 ? 205 A1IK8 A CBI   1 
HETATM 1367 S  SBH   . A1IK8 F 5 .   ? 19.737 -11.030 17.885 1.00 21.96 ? 205 A1IK8 A SBH   1 
HETATM 1368 C  CBG   . A1IK8 F 5 .   ? 19.367 -11.938 19.284 1.00 23.87 ? 205 A1IK8 A CBG   1 
HETATM 1369 N  NBF   . A1IK8 F 5 .   ? 19.096 -13.228 19.293 1.00 23.85 ? 205 A1IK8 A NBF   1 
HETATM 1370 S  SAH   . A1IK8 F 5 .   ? 19.414 -14.222 18.165 1.00 25.91 ? 205 A1IK8 A SAH   1 
HETATM 1371 O  OAI   . A1IK8 F 5 .   ? 19.256 -13.482 16.901 1.00 28.22 ? 205 A1IK8 A OAI   1 
HETATM 1372 O  OBE   . A1IK8 F 5 .   ? 18.568 -15.432 18.322 1.00 32.31 ? 205 A1IK8 A OBE   1 
HETATM 1373 C  CAG   . A1IK8 F 5 .   ? 20.983 -14.595 18.548 1.00 23.46 ? 205 A1IK8 A CAG   1 
HETATM 1374 C  CAF   . A1IK8 F 5 .   ? 22.023 -14.171 17.695 1.00 24.17 ? 205 A1IK8 A CAF   1 
HETATM 1375 N  NAE   . A1IK8 F 5 .   ? 23.285 -14.447 18.121 1.00 25.54 ? 205 A1IK8 A NAE   1 
HETATM 1376 C  CAJ   . A1IK8 F 5 .   ? 21.291 -15.201 19.777 1.00 25.40 ? 205 A1IK8 A CAJ   1 
HETATM 1377 C  CAC   . A1IK8 F 5 .   ? 22.590 -15.505 20.133 1.00 28.65 ? 205 A1IK8 A CAC   1 
HETATM 1378 C  CAD   . A1IK8 F 5 .   ? 23.615 -15.057 19.244 1.00 27.82 ? 205 A1IK8 A CAD   1 
HETATM 1379 N  NAK   . A1IK8 F 5 .   ? 24.914 -15.298 19.551 1.00 30.40 ? 205 A1IK8 A NAK   1 
HETATM 1380 C  CAL   . A1IK8 F 5 .   ? 25.985 -14.963 18.570 1.00 30.94 ? 205 A1IK8 A CAL   1 
HETATM 1381 C  CAM   . A1IK8 F 5 .   ? 26.231 -13.534 18.758 1.00 36.88 ? 205 A1IK8 A CAM   1 
HETATM 1382 C  CAN   . A1IK8 F 5 .   ? 27.317 -13.665 19.814 1.00 34.57 ? 205 A1IK8 A CAN   1 
HETATM 1383 N  NAO   . A1IK8 F 5 .   ? 28.232 -14.622 19.195 1.00 34.16 ? 205 A1IK8 A NAO   1 
HETATM 1384 C  CAP   . A1IK8 F 5 .   ? 27.349 -15.701 18.775 1.00 36.89 ? 205 A1IK8 A CAP   1 
HETATM 1385 O  O     . HOH   G 6 .   ? 24.223 4.882   8.346  1.00 17.90 ? 301 HOH   A O     1 
HETATM 1386 O  O     . HOH   G 6 .   ? 41.961 -5.134  0.951  1.00 32.76 ? 302 HOH   A O     1 
HETATM 1387 O  O     . HOH   G 6 .   ? 27.778 -4.901  -0.448 1.00 38.77 ? 303 HOH   A O     1 
HETATM 1388 O  O     . HOH   G 6 .   ? 47.028 4.494   25.325 1.00 32.69 ? 304 HOH   A O     1 
HETATM 1389 O  O     . HOH   G 6 .   ? 42.148 8.928   1.703  1.00 24.64 ? 305 HOH   A O     1 
HETATM 1390 O  O     . HOH   G 6 .   ? 30.178 -9.444  25.655 1.00 32.40 ? 306 HOH   A O     1 
HETATM 1391 O  O     . HOH   G 6 .   ? 20.545 4.290   6.465  1.00 32.28 ? 307 HOH   A O     1 
HETATM 1392 O  O     . HOH   G 6 .   ? 14.633 -5.987  14.630 1.00 36.24 ? 308 HOH   A O     1 
HETATM 1393 O  O     . HOH   G 6 .   ? 17.205 11.650  16.944 1.00 30.63 ? 309 HOH   A O     1 
HETATM 1394 O  O     . HOH   G 6 .   ? 32.093 8.639   25.491 1.00 25.16 ? 310 HOH   A O     1 
HETATM 1395 O  O     . HOH   G 6 .   ? 33.920 -11.142 23.167 1.00 25.31 ? 311 HOH   A O     1 
HETATM 1396 O  O     . HOH   G 6 .   ? 31.957 1.941   -1.612 1.00 27.18 ? 312 HOH   A O     1 
HETATM 1397 O  O     . HOH   G 6 .   ? 30.565 9.883   5.762  1.00 27.31 ? 313 HOH   A O     1 
HETATM 1398 O  O     . HOH   G 6 .   ? 30.721 -11.930 10.216 1.00 28.90 ? 314 HOH   A O     1 
HETATM 1399 O  O     . HOH   G 6 .   ? 32.449 -10.556 -2.320 1.00 24.34 ? 315 HOH   A O     1 
HETATM 1400 O  O     . HOH   G 6 .   ? 33.274 -9.143  21.034 1.00 21.28 ? 316 HOH   A O     1 
HETATM 1401 O  O     . HOH   G 6 .   ? 33.582 -9.732  0.400  1.00 27.96 ? 317 HOH   A O     1 
HETATM 1402 O  O     . HOH   G 6 .   ? 42.165 9.291   21.536 1.00 32.95 ? 318 HOH   A O     1 
HETATM 1403 O  O     . HOH   G 6 .   ? 29.709 -10.215 12.198 1.00 20.95 ? 319 HOH   A O     1 
HETATM 1404 O  O     . HOH   G 6 .   ? 40.758 10.504  16.909 1.00 34.81 ? 320 HOH   A O     1 
HETATM 1405 O  O     . HOH   G 6 .   ? 50.016 -1.625  17.926 1.00 40.69 ? 321 HOH   A O     1 
HETATM 1406 O  O     . HOH   G 6 .   ? 35.533 -1.578  28.393 1.00 22.89 ? 322 HOH   A O     1 
HETATM 1407 O  O     . HOH   G 6 .   ? 26.901 11.548  22.181 1.00 37.98 ? 323 HOH   A O     1 
HETATM 1408 O  O     . HOH   G 6 .   ? 14.656 0.035   12.712 1.00 33.21 ? 324 HOH   A O     1 
HETATM 1409 O  O     . HOH   G 6 .   ? 25.401 12.056  17.326 1.00 34.29 ? 325 HOH   A O     1 
HETATM 1410 O  O     . HOH   G 6 .   ? 37.119 -5.163  11.608 1.00 18.44 ? 326 HOH   A O     1 
HETATM 1411 O  O     . HOH   G 6 .   ? 44.472 -3.622  17.406 1.00 21.69 ? 327 HOH   A O     1 
HETATM 1412 O  O     . HOH   G 6 .   ? 31.097 -3.647  1.265  1.00 24.25 ? 328 HOH   A O     1 
HETATM 1413 O  O     . HOH   G 6 .   ? 20.287 14.707  22.967 1.00 37.47 ? 329 HOH   A O     1 
HETATM 1414 O  O     . HOH   G 6 .   ? 34.329 11.898  24.044 1.00 31.86 ? 330 HOH   A O     1 
HETATM 1415 O  O     . HOH   G 6 .   ? 37.562 -10.195 9.985  1.00 33.76 ? 331 HOH   A O     1 
HETATM 1416 O  O     . HOH   G 6 .   ? 45.768 -5.392  23.572 1.00 31.83 ? 332 HOH   A O     1 
HETATM 1417 O  O     . HOH   G 6 .   ? 16.898 -0.410  10.743 1.00 31.14 ? 333 HOH   A O     1 
HETATM 1418 O  O     . HOH   G 6 .   ? 31.696 -9.404  14.120 1.00 18.74 ? 334 HOH   A O     1 
HETATM 1419 O  O     . HOH   G 6 .   ? 12.106 2.614   32.626 1.00 26.33 ? 335 HOH   A O     1 
HETATM 1420 O  O     . HOH   G 6 .   ? 12.630 5.453   15.836 1.00 33.35 ? 336 HOH   A O     1 
HETATM 1421 O  O     . HOH   G 6 .   ? 27.010 5.562   -1.051 1.00 36.85 ? 337 HOH   A O     1 
HETATM 1422 O  O     . HOH   G 6 .   ? 24.439 1.687   4.726  1.00 30.95 ? 338 HOH   A O     1 
HETATM 1423 O  O     . HOH   G 6 .   ? 48.309 -2.666  10.834 1.00 28.09 ? 339 HOH   A O     1 
HETATM 1424 O  O     . HOH   G 6 .   ? 38.827 12.869  4.453  1.00 39.66 ? 340 HOH   A O     1 
HETATM 1425 O  O     . HOH   G 6 .   ? 24.507 4.271   3.212  1.00 33.55 ? 341 HOH   A O     1 
HETATM 1426 O  O     . HOH   G 6 .   ? 23.981 -8.200  30.066 1.00 33.71 ? 342 HOH   A O     1 
HETATM 1427 O  O     . HOH   G 6 .   ? 24.522 8.526   6.651  1.00 35.80 ? 343 HOH   A O     1 
HETATM 1428 O  O     . HOH   G 6 .   ? 45.050 -2.850  22.229 1.00 27.43 ? 344 HOH   A O     1 
HETATM 1429 O  O     . HOH   G 6 .   ? 26.197 -16.524 21.773 1.00 39.88 ? 345 HOH   A O     1 
HETATM 1430 O  O     . HOH   G 6 .   ? 36.268 -9.732  23.808 1.00 23.77 ? 346 HOH   A O     1 
HETATM 1431 O  O     . HOH   G 6 .   ? 25.014 6.096   27.406 1.00 40.85 ? 347 HOH   A O     1 
HETATM 1432 O  O     . HOH   G 6 .   ? 14.579 12.993  16.829 1.00 36.18 ? 348 HOH   A O     1 
HETATM 1433 O  O     . HOH   G 6 .   ? 28.437 10.153  1.402  1.00 31.33 ? 349 HOH   A O     1 
HETATM 1434 O  O     . HOH   G 6 .   ? 36.207 11.037  15.027 1.00 29.95 ? 350 HOH   A O     1 
HETATM 1435 O  O     . HOH   G 6 .   ? 42.587 -5.417  16.119 1.00 26.85 ? 351 HOH   A O     1 
HETATM 1436 O  O     . HOH   G 6 .   ? 34.725 -1.672  0.141  1.00 21.81 ? 352 HOH   A O     1 
HETATM 1437 O  O     . HOH   G 6 .   ? 41.130 5.786   10.924 1.00 27.68 ? 353 HOH   A O     1 
HETATM 1438 O  O     . HOH   G 6 .   ? 14.630 -10.384 12.615 1.00 35.28 ? 354 HOH   A O     1 
HETATM 1439 O  O     . HOH   G 6 .   ? 24.252 0.522   31.482 1.00 35.08 ? 355 HOH   A O     1 
HETATM 1440 O  O     . HOH   G 6 .   ? 44.423 11.425  8.189  1.00 34.74 ? 356 HOH   A O     1 
HETATM 1441 O  O     . HOH   G 6 .   ? 37.413 -1.871  3.766  1.00 27.81 ? 357 HOH   A O     1 
HETATM 1442 O  O     . HOH   G 6 .   ? 32.442 -7.675  -3.213 1.00 22.59 ? 358 HOH   A O     1 
HETATM 1443 O  O     . HOH   G 6 .   ? 13.526 -3.051  18.236 1.00 31.35 ? 359 HOH   A O     1 
HETATM 1444 O  O     . HOH   G 6 .   ? 45.511 10.154  10.399 1.00 30.33 ? 360 HOH   A O     1 
HETATM 1445 O  O     . HOH   G 6 .   ? 13.313 6.333   20.530 1.00 31.17 ? 361 HOH   A O     1 
HETATM 1446 O  O     . HOH   G 6 .   ? 31.093 10.314  23.331 1.00 23.08 ? 362 HOH   A O     1 
HETATM 1447 O  O     . HOH   G 6 .   ? 22.935 -20.170 22.390 1.00 41.00 ? 363 HOH   A O     1 
HETATM 1448 O  O     . HOH   G 6 .   ? 12.452 8.787   1.648  1.00 33.00 ? 364 HOH   A O     1 
HETATM 1449 O  O     . HOH   G 6 .   ? 31.581 11.086  9.077  1.00 32.30 ? 365 HOH   A O     1 
HETATM 1450 O  O     . HOH   G 6 .   ? 39.130 -0.747  1.970  1.00 26.25 ? 366 HOH   A O     1 
HETATM 1451 O  O     . HOH   G 6 .   ? 46.957 -3.058  20.174 1.00 26.44 ? 367 HOH   A O     1 
HETATM 1452 O  O     . HOH   G 6 .   ? 28.865 -22.135 10.586 1.00 39.00 ? 368 HOH   A O     1 
HETATM 1453 O  O     . HOH   G 6 .   ? 25.979 -7.041  -0.351 1.00 33.00 ? 369 HOH   A O     1 
HETATM 1454 O  O     . HOH   G 6 .   ? 17.768 11.220  14.059 1.00 31.97 ? 370 HOH   A O     1 
HETATM 1455 O  O     . HOH   G 6 .   ? 12.373 7.435   13.811 1.00 38.31 ? 371 HOH   A O     1 
HETATM 1456 O  O     . HOH   G 6 .   ? 23.355 4.746   5.722  1.00 28.83 ? 372 HOH   A O     1 
HETATM 1457 O  O     . HOH   G 6 .   ? 31.712 -11.016 2.423  1.00 34.59 ? 373 HOH   A O     1 
HETATM 1458 O  O     . HOH   G 6 .   ? 44.600 8.990   2.822  1.00 33.86 ? 374 HOH   A O     1 
HETATM 1459 O  O     . HOH   G 6 .   ? 46.540 -5.306  16.698 1.00 29.09 ? 375 HOH   A O     1 
HETATM 1460 O  O     . HOH   G 6 .   ? 28.356 10.550  4.189  1.00 39.84 ? 376 HOH   A O     1 
HETATM 1461 O  O     . HOH   G 6 .   ? 9.545  2.183   32.415 1.00 42.83 ? 377 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   ? 0.3984 0.6170 0.6389 -0.0165 0.3456  -0.0858 1   MET   A N     
2    C  CA    . MET   A 4   ? 0.3306 0.5532 0.4372 0.0051  0.1237  -0.0675 1   MET   A CA    
3    C  C     . MET   A 4   ? 0.2111 0.3799 0.4511 -0.0068 0.0930  -0.0632 1   MET   A C     
4    O  O     . MET   A 4   ? 0.2909 0.4139 0.5076 0.0460  0.1433  -0.0378 1   MET   A O     
5    C  CB    . MET   A 4   ? 0.3490 0.6259 0.3897 -0.0679 0.1237  -0.1076 1   MET   A CB    
6    C  CG    . MET   A 4   ? 0.3430 0.6676 0.2227 -0.0686 0.2192  -0.0724 1   MET   A CG    
7    S  SD    . MET   A 4   ? 0.3531 0.4891 0.3533 0.0549  0.1226  0.0033  1   MET   A SD    
8    C  CE    . MET   A 4   ? 0.2421 0.4244 0.3339 0.0179  0.0614  -0.0294 1   MET   A CE    
9    N  N     . THR   A 5   ? 0.2165 0.4685 0.3918 0.0825  0.0714  -0.0511 2   THR   A N     
10   C  CA    . THR   A 5   ? 0.2292 0.4949 0.3685 0.0235  0.0678  -0.0369 2   THR   A CA    
11   C  C     . THR   A 5   ? 0.1901 0.4730 0.3575 0.0108  0.0812  -0.1164 2   THR   A C     
12   O  O     . THR   A 5   ? 0.2555 0.4375 0.3046 -0.0169 0.0512  -0.0467 2   THR   A O     
13   C  CB    . THR   A 5   ? 0.2201 0.5461 0.3794 0.0451  -0.0033 0.0396  2   THR   A CB    
14   O  OG1   . THR   A 5   ? 0.3160 0.6345 0.3663 0.1181  -0.0037 0.0792  2   THR   A OG1   
15   C  CG2   . THR   A 5   ? 0.3280 0.6769 0.4194 -0.0158 0.0290  -0.0006 2   THR   A CG2   
16   N  N     . GLU   A 6   ? 0.1493 0.4420 0.4278 -0.0051 0.0583  -0.1065 3   GLU   A N     
17   C  CA    . GLU   A 6   ? 0.2005 0.4676 0.3432 0.0575  0.1284  -0.0919 3   GLU   A CA    
18   C  C     . GLU   A 6   ? 0.1731 0.5697 0.2842 0.0211  0.0809  -0.0456 3   GLU   A C     
19   O  O     . GLU   A 6   ? 0.0897 0.6556 0.3933 -0.0087 0.0496  -0.0890 3   GLU   A O     
20   C  CB    . GLU   A 6   ? 0.3142 0.5582 0.4545 -0.0332 0.2239  -0.0429 3   GLU   A CB    
21   C  CG    . GLU   A 6   ? 0.3655 0.6526 0.5077 -0.0124 0.1697  -0.0061 3   GLU   A CG    
22   C  CD    . GLU   A 6   ? 0.5365 0.3791 0.4902 -0.0234 0.1108  -0.0447 3   GLU   A CD    
23   O  OE1   . GLU   A 6   ? 0.6836 0.5857 0.6137 0.0179  0.1532  -0.1497 3   GLU   A OE1   
24   O  OE2   . GLU   A 6   ? 0.6288 0.3839 0.6494 -0.0649 -0.0005 0.0409  3   GLU   A OE2   
25   N  N     . TYR   A 7   ? 0.1785 0.3616 0.2675 0.0004  0.0455  -0.0540 4   TYR   A N     
26   C  CA    . TYR   A 7   ? 0.2299 0.2661 0.2071 0.0190  0.0281  0.0024  4   TYR   A CA    
27   C  C     . TYR   A 7   ? 0.1572 0.2863 0.2492 0.0103  0.0440  0.0180  4   TYR   A C     
28   O  O     . TYR   A 7   ? 0.2211 0.3372 0.2085 0.0712  0.0474  0.0123  4   TYR   A O     
29   C  CB    . TYR   A 7   ? 0.2278 0.2915 0.2388 0.0121  0.0459  0.0282  4   TYR   A CB    
30   C  CG    . TYR   A 7   ? 0.2062 0.3478 0.2401 0.0406  0.0086  0.0017  4   TYR   A CG    
31   C  CD1   . TYR   A 7   ? 0.3525 0.3243 0.2382 0.1108  -0.0170 -0.0227 4   TYR   A CD1   
32   C  CD2   . TYR   A 7   ? 0.2141 0.2542 0.3419 -0.0064 0.0351  0.0040  4   TYR   A CD2   
33   C  CE1   . TYR   A 7   ? 0.2774 0.3725 0.3081 0.1283  -0.0654 -0.0077 4   TYR   A CE1   
34   C  CE2   . TYR   A 7   ? 0.2532 0.3234 0.2438 0.0506  0.0116  -0.0186 4   TYR   A CE2   
35   C  CZ    . TYR   A 7   ? 0.1785 0.3492 0.2758 0.0651  0.0232  -0.0031 4   TYR   A CZ    
36   O  OH    . TYR   A 7   ? 0.2553 0.4031 0.3362 0.0947  -0.0257 0.0450  4   TYR   A OH    
37   N  N     . LYS   A 8   ? 0.1482 0.3535 0.2293 0.0067  0.0172  0.0157  5   LYS   A N     
38   C  CA    . LYS   A 8   ? 0.1872 0.3684 0.2173 0.0239  0.0402  0.0449  5   LYS   A CA    
39   C  C     . LYS   A 8   ? 0.1433 0.2446 0.2229 0.0103  0.0100  -0.0011 5   LYS   A C     
40   O  O     . LYS   A 8   ? 0.1512 0.3200 0.2167 0.0243  0.0133  -0.0114 5   LYS   A O     
41   C  CB    . LYS   A 8   ? 0.1478 0.3644 0.3356 -0.0055 0.0079  0.0703  5   LYS   A CB    
42   C  CG    . LYS   A 8   ? 0.1355 0.4013 0.4299 0.0387  0.0789  0.0321  5   LYS   A CG    
43   C  CD    . LYS   A 8   ? 0.2505 0.3855 0.4356 -0.1063 -0.0321 0.0493  5   LYS   A CD    
44   C  CE    . LYS   A 8   ? 0.2653 0.4690 0.5759 -0.1999 -0.0363 0.0745  5   LYS   A CE    
45   N  NZ    . LYS   A 8   ? 0.3453 0.4918 0.5039 -0.0845 0.0035  0.1132  5   LYS   A NZ    
46   N  N     . LEU   A 9   ? 0.1469 0.3505 0.1864 -0.0591 0.0449  0.0184  6   LEU   A N     
47   C  CA    . LEU   A 9   ? 0.1398 0.3219 0.1527 -0.0184 0.0512  0.0323  6   LEU   A CA    
48   C  C     . LEU   A 9   ? 0.1447 0.2898 0.2133 -0.0335 0.0031  0.0104  6   LEU   A C     
49   O  O     . LEU   A 9   ? 0.1404 0.2950 0.2367 0.0044  0.0239  0.0193  6   LEU   A O     
50   C  CB    . LEU   A 9   ? 0.1625 0.2491 0.1949 -0.0168 0.0402  0.0503  6   LEU   A CB    
51   C  CG    . LEU   A 9   ? 0.1894 0.3173 0.2292 0.0226  0.0347  -0.0021 6   LEU   A CG    
52   C  CD1   . LEU   A 9   ? 0.1991 0.3461 0.2201 0.0070  0.0413  -0.0068 6   LEU   A CD1   
53   C  CD2   . LEU   A 9   ? 0.2020 0.3145 0.2468 0.0302  0.0245  0.0417  6   LEU   A CD2   
54   N  N     . VAL   A 10  ? 0.1524 0.2748 0.2131 -0.0192 0.0148  0.0037  7   VAL   A N     
55   C  CA    . VAL   A 10  ? 0.1304 0.2490 0.2083 -0.0256 0.0022  0.0253  7   VAL   A CA    
56   C  C     . VAL   A 10  ? 0.1519 0.2184 0.2149 -0.0428 0.0145  0.0046  7   VAL   A C     
57   O  O     . VAL   A 10  ? 0.1264 0.2743 0.1981 -0.0103 0.0194  0.0236  7   VAL   A O     
58   C  CB    . VAL   A 10  ? 0.1628 0.2632 0.2444 -0.0903 0.0376  -0.0117 7   VAL   A CB    
59   C  CG1   . VAL   A 10  ? 0.2010 0.2662 0.2063 -0.0815 0.0575  -0.0269 7   VAL   A CG1   
60   C  CG2   . VAL   A 10  ? 0.1459 0.2708 0.2461 -0.0531 0.0244  0.0095  7   VAL   A CG2   
61   N  N     . VAL   A 11  ? 0.1402 0.1707 0.2293 -0.0124 0.0428  0.0165  8   VAL   A N     
62   C  CA    . VAL   A 11  ? 0.1351 0.2227 0.1930 -0.0099 0.0492  0.0346  8   VAL   A CA    
63   C  C     . VAL   A 11  ? 0.1467 0.2700 0.1960 0.0269  0.0035  0.0061  8   VAL   A C     
64   O  O     . VAL   A 11  ? 0.1506 0.2816 0.1968 0.0113  0.0375  -0.0060 8   VAL   A O     
65   C  CB    . VAL   A 11  ? 0.1472 0.2695 0.1958 -0.0037 0.0362  0.0372  8   VAL   A CB    
66   C  CG1   . VAL   A 11  ? 0.1436 0.3253 0.2017 -0.0379 -0.0149 -0.0386 8   VAL   A CG1   
67   C  CG2   . VAL   A 11  ? 0.1865 0.2726 0.1970 -0.0222 0.0549  0.0063  8   VAL   A CG2   
68   N  N     . VAL   A 12  ? 0.1472 0.2234 0.2243 0.0212  0.0299  0.0070  9   VAL   A N     
69   C  CA    . VAL   A 12  ? 0.1500 0.2066 0.2355 -0.0047 0.0245  -0.0135 9   VAL   A CA    
70   C  C     . VAL   A 12  ? 0.1520 0.2655 0.1676 0.0027  0.0216  -0.0282 9   VAL   A C     
71   O  O     . VAL   A 12  ? 0.1054 0.2630 0.2604 -0.0055 0.0318  -0.0245 9   VAL   A O     
72   C  CB    . VAL   A 12  ? 0.1352 0.2053 0.2369 -0.0114 0.0282  -0.0103 9   VAL   A CB    
73   C  CG1   . VAL   A 12  ? 0.1362 0.2398 0.2585 -0.0076 0.0215  0.0164  9   VAL   A CG1   
74   C  CG2   . VAL   A 12  ? 0.1479 0.2482 0.2357 -0.0382 0.0165  0.0125  9   VAL   A CG2   
75   N  N     . GLY   A 13  ? 0.1582 0.2322 0.2036 -0.0073 0.0408  -0.0024 10  GLY   A N     
76   C  CA    . GLY   A 13  ? 0.1514 0.2028 0.2330 0.0027  0.0213  -0.0079 10  GLY   A CA    
77   C  C     . GLY   A 13  ? 0.1526 0.2512 0.2330 0.0353  -0.0036 0.0041  10  GLY   A C     
78   O  O     . GLY   A 13  ? 0.1714 0.2310 0.2456 0.0505  0.0266  0.0071  10  GLY   A O     
79   N  N     . ALA   A 14  ? 0.1475 0.2510 0.2471 0.0225  0.0005  -0.0170 11  ALA   A N     
80   C  CA    . ALA   A 14  ? 0.1551 0.2312 0.3011 0.0181  0.0329  0.0093  11  ALA   A CA    
81   C  C     . ALA   A 14  ? 0.1986 0.2097 0.3269 0.0210  -0.0136 -0.0037 11  ALA   A C     
82   O  O     . ALA   A 14  ? 0.2375 0.2250 0.2979 0.0260  0.0132  0.0006  11  ALA   A O     
83   C  CB    . ALA   A 14  ? 0.1718 0.3346 0.2856 0.0186  0.0512  0.0008  11  ALA   A CB    
84   N  N     . GLY   A 15  ? 0.2700 0.2464 0.2909 0.0742  0.0317  0.0070  12  GLY   A N     
85   C  CA    . GLY   A 15  ? 0.2737 0.3217 0.2782 0.0910  0.0315  -0.0161 12  GLY   A CA    
86   C  C     . GLY   A 15  ? 0.1812 0.2877 0.2873 0.0978  0.0254  0.0323  12  GLY   A C     
87   O  O     . GLY   A 15  ? 0.1765 0.4075 0.2803 0.0671  0.0257  0.0232  12  GLY   A O     
88   N  N     . GLY   A 16  ? 0.1531 0.3912 0.2730 0.0624  0.0399  0.0038  13  GLY   A N     
89   C  CA    . GLY   A 16  ? 0.1400 0.3862 0.2831 0.0478  0.0228  -0.0098 13  GLY   A CA    
90   C  C     . GLY   A 16  ? 0.1548 0.3946 0.2146 0.0266  0.0224  0.0068  13  GLY   A C     
91   O  O     . GLY   A 16  ? 0.1267 0.3964 0.2755 0.0354  0.0161  -0.0132 13  GLY   A O     
92   N  N     . VAL   A 17  ? 0.1242 0.3453 0.1941 0.0286  0.0283  -0.0008 14  VAL   A N     
93   C  CA    . VAL   A 17  ? 0.1044 0.3514 0.2360 -0.0153 0.0818  0.0176  14  VAL   A CA    
94   C  C     . VAL   A 17  ? 0.1395 0.3013 0.2237 0.0217  0.0357  0.0247  14  VAL   A C     
95   O  O     . VAL   A 17  ? 0.1565 0.3233 0.2057 -0.0116 0.0527  -0.0173 14  VAL   A O     
96   C  CB    . VAL   A 17  ? 0.1297 0.2841 0.2735 0.0184  0.0238  0.0156  14  VAL   A CB    
97   C  CG1   . VAL   A 17  ? 0.1549 0.1965 0.2767 0.0034  0.0254  0.0282  14  VAL   A CG1   
98   C  CG2   . VAL   A 17  ? 0.1461 0.2018 0.2825 -0.0209 0.0240  -0.0055 14  VAL   A CG2   
99   N  N     . GLY   A 18  ? 0.1594 0.2877 0.2280 -0.0408 0.0315  0.0226  15  GLY   A N     
100  C  CA    . GLY   A 18  ? 0.1915 0.3456 0.1666 -0.0215 0.0018  0.0330  15  GLY   A CA    
101  C  C     . GLY   A 18  ? 0.1852 0.2761 0.2262 -0.0388 -0.0056 0.0289  15  GLY   A C     
102  O  O     . GLY   A 18  ? 0.1682 0.3298 0.2254 -0.0490 0.0352  0.0119  15  GLY   A O     
103  N  N     . LYS   A 19  ? 0.1351 0.2541 0.2513 0.0142  0.0510  0.0011  16  LYS   A N     
104  C  CA    . LYS   A 19  ? 0.1360 0.2428 0.2286 0.0156  0.0265  0.0307  16  LYS   A CA    
105  C  C     . LYS   A 19  ? 0.2179 0.2704 0.2353 -0.0478 0.0318  0.0236  16  LYS   A C     
106  O  O     . LYS   A 19  ? 0.1542 0.3425 0.1686 -0.0090 0.0160  0.0453  16  LYS   A O     
107  C  CB    . LYS   A 19  ? 0.1505 0.3061 0.2177 0.0001  0.0323  0.0000  16  LYS   A CB    
108  C  CG    . LYS   A 19  ? 0.1737 0.3509 0.2268 -0.0183 0.0411  0.0019  16  LYS   A CG    
109  C  CD    . LYS   A 19  ? 0.1946 0.3344 0.2222 0.0189  0.0421  -0.0260 16  LYS   A CD    
110  C  CE    . LYS   A 19  ? 0.1757 0.2698 0.2895 -0.0645 0.0042  -0.0607 16  LYS   A CE    
111  N  NZ    . LYS   A 19  ? 0.1889 0.2329 0.3059 -0.0096 -0.0175 0.0128  16  LYS   A NZ    
112  N  N     . SER   A 20  ? 0.1556 0.3001 0.2262 -0.0355 0.0343  0.0281  17  SER   A N     
113  C  CA    . SER   A 20  ? 0.1168 0.3128 0.2232 -0.0439 0.0477  0.0262  17  SER   A CA    
114  C  C     . SER   A 20  ? 0.1364 0.3086 0.2553 -0.0372 0.0088  0.0107  17  SER   A C     
115  O  O     . SER   A 20  ? 0.1550 0.3660 0.2229 0.0090  0.0265  0.0235  17  SER   A O     
116  C  CB    . SER   A 20  ? 0.1053 0.3598 0.2479 0.0015  0.0268  0.0443  17  SER   A CB    
117  O  OG    . SER   A 20  ? 0.1792 0.3482 0.2552 0.0134  0.0096  0.0627  17  SER   A OG    
118  N  N     . ALA   A 21  ? 0.1298 0.3398 0.2139 -0.0402 0.0105  -0.0042 18  ALA   A N     
119  C  CA    . ALA   A 21  ? 0.1713 0.3676 0.1889 -0.0315 0.0449  0.0058  18  ALA   A CA    
120  C  C     . ALA   A 21  ? 0.1529 0.3713 0.1926 -0.0271 0.0301  -0.0126 18  ALA   A C     
121  O  O     . ALA   A 21  ? 0.1861 0.4064 0.1761 -0.0359 0.0400  -0.0070 18  ALA   A O     
122  C  CB    . ALA   A 21  ? 0.1499 0.3715 0.2608 -0.0362 0.0145  0.0233  18  ALA   A CB    
123  N  N     . LEU   A 22  ? 0.1420 0.3740 0.1838 -0.0135 0.0369  -0.0204 19  LEU   A N     
124  C  CA    . LEU   A 22  ? 0.1964 0.2920 0.1851 -0.0402 0.0544  -0.0177 19  LEU   A CA    
125  C  C     . LEU   A 22  ? 0.1692 0.3395 0.2376 -0.0260 0.0233  0.0260  19  LEU   A C     
126  O  O     . LEU   A 22  ? 0.1650 0.3473 0.1883 -0.0076 0.0291  0.0432  19  LEU   A O     
127  C  CB    . LEU   A 22  ? 0.1676 0.2964 0.1955 -0.0445 0.0594  0.0030  19  LEU   A CB    
128  C  CG    . LEU   A 22  ? 0.1921 0.2925 0.1793 -0.0743 0.0535  -0.0030 19  LEU   A CG    
129  C  CD1   . LEU   A 22  ? 0.2027 0.3299 0.1877 -0.0923 0.0402  -0.0095 19  LEU   A CD1   
130  C  CD2   . LEU   A 22  ? 0.1906 0.2856 0.2242 -0.0540 0.0779  0.0311  19  LEU   A CD2   
131  N  N     . THR   A 23  ? 0.1716 0.3323 0.1904 0.0036  0.0577  -0.0199 20  THR   A N     
132  C  CA    . THR   A 23  ? 0.1538 0.3254 0.2290 -0.0005 0.0445  0.0458  20  THR   A CA    
133  C  C     . THR   A 23  ? 0.2777 0.2481 0.2245 -0.0046 0.0153  -0.0041 20  THR   A C     
134  O  O     . THR   A 23  ? 0.2129 0.3924 0.2296 0.0169  0.0425  0.0165  20  THR   A O     
135  C  CB    . THR   A 23  ? 0.1384 0.3573 0.2209 -0.0288 0.0244  0.0127  20  THR   A CB    
136  O  OG1   . THR   A 23  ? 0.2311 0.2793 0.2499 -0.0212 0.0336  0.0332  20  THR   A OG1   
137  C  CG2   . THR   A 23  ? 0.1329 0.3295 0.2875 -0.0154 0.0484  0.0518  20  THR   A CG2   
138  N  N     . ILE   A 24  ? 0.1599 0.4078 0.1986 -0.0294 0.0553  0.0223  21  ILE   A N     
139  C  CA    . ILE   A 24  ? 0.2390 0.3898 0.1597 0.0143  0.0640  0.0438  21  ILE   A CA    
140  C  C     . ILE   A 24  ? 0.2410 0.3700 0.1783 -0.0049 0.0526  0.0543  21  ILE   A C     
141  O  O     . ILE   A 24  ? 0.2540 0.3262 0.1874 -0.0551 0.0765  0.0242  21  ILE   A O     
142  C  CB    . ILE   A 24  ? 0.2164 0.3731 0.2298 -0.0045 0.0487  0.0440  21  ILE   A CB    
143  C  CG1   . ILE   A 24  ? 0.2833 0.3758 0.1845 -0.0246 0.0897  0.0409  21  ILE   A CG1   
144  C  CG2   . ILE   A 24  ? 0.4055 0.3935 0.2108 0.0059  0.0783  0.0298  21  ILE   A CG2   
145  C  CD1   . ILE   A 24  ? 0.4146 0.4547 0.2886 0.0653  0.0404  0.0329  21  ILE   A CD1   
146  N  N     . GLN   A 25  ? 0.2577 0.3203 0.1857 -0.0500 0.0359  -0.0112 22  GLN   A N     
147  C  CA    . GLN   A 25  ? 0.2879 0.3198 0.1827 -0.0243 0.0216  0.0488  22  GLN   A CA    
148  C  C     . GLN   A 25  ? 0.2778 0.3982 0.1920 -0.0224 -0.0115 -0.0060 22  GLN   A C     
149  O  O     . GLN   A 25  ? 0.2619 0.4971 0.1753 -0.0450 0.0552  -0.0395 22  GLN   A O     
150  C  CB    . GLN   A 25  ? 0.3397 0.3488 0.1615 -0.0464 0.0499  0.0297  22  GLN   A CB    
151  C  CG    . GLN   A 25  ? 0.3974 0.4642 0.1479 -0.0896 0.0676  -0.0310 22  GLN   A CG    
152  C  CD    . GLN   A 25  ? 0.2849 0.4427 0.1719 -0.0452 0.0397  -0.0190 22  GLN   A CD    
153  O  OE1   . GLN   A 25  ? 0.2378 0.5231 0.3068 -0.0472 0.1139  -0.0545 22  GLN   A OE1   
154  N  NE2   . GLN   A 25  ? 0.3149 0.4827 0.1989 -0.0174 0.0161  -0.0687 22  GLN   A NE2   
155  N  N     . LEU   A 26  ? 0.2428 0.4182 0.1566 -0.0030 0.0352  0.0082  23  LEU   A N     
156  C  CA    . LEU   A 26  ? 0.2785 0.4000 0.1833 0.0224  0.0249  0.0206  23  LEU   A CA    
157  C  C     . LEU   A 26  ? 0.2305 0.3642 0.2110 -0.0100 0.0314  -0.0098 23  LEU   A C     
158  O  O     . LEU   A 26  ? 0.3003 0.4433 0.1929 0.0246  0.0448  -0.0538 23  LEU   A O     
159  C  CB    . LEU   A 26  ? 0.2585 0.3429 0.2112 0.0203  0.0315  0.0138  23  LEU   A CB    
160  C  CG    . LEU   A 26  ? 0.2756 0.3520 0.2116 0.0120  0.0074  0.0026  23  LEU   A CG    
161  C  CD1   . LEU   A 26  ? 0.2752 0.3635 0.2045 -0.0434 0.0536  -0.0435 23  LEU   A CD1   
162  C  CD2   . LEU   A 26  ? 0.2282 0.3328 0.2544 0.0157  0.0073  0.0153  23  LEU   A CD2   
163  N  N     . ILE   A 27  ? 0.2009 0.4107 0.2212 0.0190  0.1184  -0.0189 24  ILE   A N     
164  C  CA    . ILE   A 27  ? 0.2065 0.4430 0.1952 0.0147  0.0728  0.0392  24  ILE   A CA    
165  C  C     . ILE   A 27  ? 0.3269 0.4705 0.2016 0.1308  0.0351  -0.0046 24  ILE   A C     
166  O  O     . ILE   A 27  ? 0.2912 0.4719 0.2244 0.0241  0.0710  -0.0753 24  ILE   A O     
167  C  CB    . ILE   A 27  ? 0.2135 0.4603 0.2097 -0.0064 0.0684  0.0421  24  ILE   A CB    
168  C  CG1   . ILE   A 27  ? 0.1736 0.4622 0.2406 -0.0010 0.0729  0.0727  24  ILE   A CG1   
169  C  CG2   . ILE   A 27  ? 0.3086 0.4105 0.2575 -0.0469 0.0822  0.0654  24  ILE   A CG2   
170  C  CD1   . ILE   A 27  ? 0.1773 0.4126 0.3127 -0.0022 0.0369  0.0088  24  ILE   A CD1   
171  N  N     . GLN   A 28  ? 0.2365 0.4994 0.1814 0.0129  0.0368  0.0318  25  GLN   A N     
172  C  CA    . GLN   A 28  ? 0.2027 0.4795 0.1713 -0.0281 0.0858  -0.0163 25  GLN   A CA    
173  C  C     . GLN   A 28  ? 0.3260 0.3981 0.2305 0.0244  0.0111  -0.0024 25  GLN   A C     
174  O  O     . GLN   A 28  ? 0.2942 0.4260 0.1934 0.0195  0.0557  -0.0265 25  GLN   A O     
175  C  CB    . GLN   A 28  ? 0.2366 0.4120 0.2207 -0.0391 0.1132  -0.0551 25  GLN   A CB    
176  C  CG    . GLN   A 28  ? 0.2353 0.4018 0.2419 -0.0193 0.0882  -0.0448 25  GLN   A CG    
177  C  CD    . GLN   A 28  ? 0.3328 0.4180 0.2222 -0.0113 0.0418  -0.0196 25  GLN   A CD    
178  O  OE1   . GLN   A 28  ? 0.3217 0.4857 0.3192 -0.0211 0.0833  0.0147  25  GLN   A OE1   
179  N  NE2   . GLN   A 28  ? 0.3561 0.3997 0.3282 0.0695  0.0987  -0.0015 25  GLN   A NE2   
180  N  N     . ASN   A 29  ? 0.3276 0.3982 0.2008 0.0342  0.0365  -0.0314 26  ASN   A N     
181  C  CA    . ASN   A 29  ? 0.3977 0.3910 0.2136 0.0073  0.0590  -0.0127 26  ASN   A CA    
182  C  C     . ASN   A 29  ? 0.3626 0.3590 0.2331 -0.0311 0.0829  -0.0060 26  ASN   A C     
183  O  O     . ASN   A 29  ? 0.3284 0.4624 0.2287 -0.0507 0.0492  0.0019  26  ASN   A O     
184  C  CB    . ASN   A 29  ? 0.4636 0.3854 0.2353 -0.0323 0.0950  -0.0459 26  ASN   A CB    
185  C  CG    . ASN   A 29  ? 0.5373 0.2954 0.4325 -0.0389 -0.0056 -0.0694 26  ASN   A CG    
186  O  OD1   . ASN   A 29  ? 0.6668 0.4789 0.4654 -0.1871 0.0225  0.0920  26  ASN   A OD1   
187  N  ND2   . ASN   A 29  ? 0.5057 0.5276 0.5720 -0.0976 0.0353  -0.0012 26  ASN   A ND2   
188  N  N     . HIS   A 30  ? 0.3277 0.4294 0.1590 0.0138  0.0650  -0.0275 27  HIS   A N     
189  C  CA    . HIS   A 30  ? 0.3836 0.4008 0.1890 0.0322  0.0481  0.0079  27  HIS   A CA    
190  C  C     . HIS   A 30  ? 0.2383 0.4380 0.2235 -0.0661 0.0796  -0.0224 27  HIS   A C     
191  O  O     . HIS   A 30  ? 0.2385 0.4237 0.2309 -0.0329 0.0650  -0.0531 27  HIS   A O     
192  C  CB    . HIS   A 30  ? 0.2670 0.4734 0.2207 -0.0261 0.0370  0.0602  27  HIS   A CB    
193  C  CG    . HIS   A 30  ? 0.2475 0.3907 0.2274 -0.0279 0.0701  0.0418  27  HIS   A CG    
194  N  ND1   . HIS   A 30  ? 0.2235 0.4502 0.3359 -0.0454 0.0652  0.0160  27  HIS   A ND1   
195  C  CD2   . HIS   A 30  ? 0.2481 0.3998 0.2840 -0.0047 0.0510  0.0005  27  HIS   A CD2   
196  C  CE1   . HIS   A 30  ? 0.2141 0.4271 0.3037 -0.0451 0.0958  0.0175  27  HIS   A CE1   
197  N  NE2   . HIS   A 30  ? 0.3033 0.3717 0.3090 -0.0037 0.0162  0.0360  27  HIS   A NE2   
198  N  N     . PHE   A 31  ? 0.2399 0.5015 0.2268 -0.0308 0.0655  -0.0522 28  PHE   A N     
199  C  CA    . PHE   A 31  ? 0.2383 0.3851 0.2470 -0.0242 0.0351  -0.0717 28  PHE   A CA    
200  C  C     . PHE   A 31  ? 0.2301 0.4714 0.2300 -0.0716 0.0237  0.0271  28  PHE   A C     
201  O  O     . PHE   A 31  ? 0.3197 0.4822 0.2695 0.0082  -0.0291 0.0728  28  PHE   A O     
202  C  CB    . PHE   A 31  ? 0.2400 0.3789 0.2312 -0.0187 0.0383  -0.0492 28  PHE   A CB    
203  C  CG    . PHE   A 31  ? 0.2084 0.4440 0.1961 0.0005  0.0145  -0.0386 28  PHE   A CG    
204  C  CD1   . PHE   A 31  ? 0.2076 0.4625 0.2074 0.0135  0.0029  -0.0482 28  PHE   A CD1   
205  C  CD2   . PHE   A 31  ? 0.2034 0.5060 0.2354 -0.0077 -0.0013 -0.0292 28  PHE   A CD2   
206  C  CE1   . PHE   A 31  ? 0.2000 0.5161 0.2435 -0.0097 0.0148  -0.0859 28  PHE   A CE1   
207  C  CE2   . PHE   A 31  ? 0.1778 0.4707 0.3173 -0.0356 0.0163  -0.0742 28  PHE   A CE2   
208  C  CZ    . PHE   A 31  ? 0.2312 0.5405 0.2854 0.0255  0.0220  -0.0573 28  PHE   A CZ    
209  N  N     . VAL   A 32  ? 0.3226 0.4417 0.4220 0.0057  -0.0299 0.0020  29  VAL   A N     
210  C  CA    . VAL   A 32  ? 0.5053 0.5041 0.5056 0.1216  0.0250  0.0173  29  VAL   A CA    
211  C  C     . VAL   A 32  ? 0.4422 0.6730 0.4438 0.0445  -0.0616 0.0653  29  VAL   A C     
212  O  O     . VAL   A 32  ? 0.6058 0.7989 0.4688 -0.0354 0.0225  0.0503  29  VAL   A O     
213  C  CB    . VAL   A 32  ? 0.6095 0.5432 0.5498 0.0546  -0.0346 0.0459  29  VAL   A CB    
214  C  CG1   . VAL   A 32  ? 0.4950 0.5752 0.5652 0.1615  -0.0797 0.1117  29  VAL   A CG1   
215  C  CG2   . VAL   A 32  ? 0.6771 0.5588 0.6373 0.0090  -0.0022 -0.0222 29  VAL   A CG2   
216  N  N     . ASP   A 33  ? 0.5584 0.6090 0.5052 0.2357  -0.1166 -0.0338 30  ASP   A N     
217  C  CA    . ASP   A 33  ? 0.5446 0.5521 0.5724 0.1666  -0.0175 -0.0032 30  ASP   A CA    
218  C  C     . ASP   A 33  ? 0.5868 0.5102 0.4227 0.2298  -0.0517 0.0446  30  ASP   A C     
219  O  O     . ASP   A 33  ? 0.4955 0.5881 0.4220 0.1635  0.0835  0.0584  30  ASP   A O     
220  C  CB    . ASP   A 33  ? 0.6950 0.6145 0.5575 0.0914  -0.0177 0.0234  30  ASP   A CB    
221  C  CG    . ASP   A 33  ? 0.7214 0.3839 0.4289 0.1080  -0.0764 -0.0270 30  ASP   A CG    
222  O  OD1   . ASP   A 33  ? 0.7298 0.4591 0.6841 0.0474  0.0217  0.0871  30  ASP   A OD1   
223  O  OD2   . ASP   A 33  ? 0.8353 0.6540 0.5194 0.2012  0.0444  -0.0885 30  ASP   A OD2   
224  N  N     . ILE   A 39  ? 0.5100 0.6556 0.6750 -0.0234 -0.1152 0.0862  36  ILE   A N     
225  C  CA    . ILE   A 39  ? 0.5357 0.6254 0.6516 -0.0364 -0.0806 0.0884  36  ILE   A CA    
226  C  C     . ILE   A 39  ? 0.6302 0.5638 0.5694 0.0169  -0.1679 -0.0635 36  ILE   A C     
227  O  O     . ILE   A 39  ? 0.4798 0.5792 0.6093 -0.0335 -0.0757 -0.0310 36  ILE   A O     
228  C  CB    . ILE   A 39  ? 0.5899 0.6146 0.7462 -0.0368 0.0435  0.0650  36  ILE   A CB    
229  C  CG1   . ILE   A 39  ? 0.7157 0.6031 0.7971 -0.1261 0.0940  0.0827  36  ILE   A CG1   
230  C  CG2   . ILE   A 39  ? 0.7365 0.7978 0.6748 0.0405  0.1034  0.0855  36  ILE   A CG2   
231  C  CD1   . ILE   A 39  ? 0.6540 0.5127 0.8163 -0.0558 0.1059  0.0583  36  ILE   A CD1   
232  N  N     . GLU   A 40  ? 0.5836 0.4544 0.4854 -0.0201 -0.0393 0.0111  37  GLU   A N     
233  C  CA    . GLU   A 40  ? 0.4665 0.4456 0.4333 -0.0365 0.0633  0.0407  37  GLU   A CA    
234  C  C     . GLU   A 40  ? 0.4640 0.4331 0.5571 -0.0013 0.0916  0.0073  37  GLU   A C     
235  O  O     . GLU   A 40  ? 0.5755 0.4479 0.7343 -0.0622 0.1058  0.0995  37  GLU   A O     
236  C  CB    . GLU   A 40  ? 0.4309 0.4502 0.3977 -0.0272 0.1055  0.0825  37  GLU   A CB    
237  C  CG    . GLU   A 40  ? 0.3397 0.4840 0.4398 0.0023  0.0519  0.0710  37  GLU   A CG    
238  C  CD    . GLU   A 40  ? 0.3904 0.4316 0.6809 0.0100  0.0796  0.0922  37  GLU   A CD    
239  O  OE1   . GLU   A 40  ? 0.5699 0.4534 0.6671 -0.1070 0.0817  -0.0198 37  GLU   A OE1   
240  O  OE2   . GLU   A 40  ? 0.4266 0.5629 0.5531 -0.0715 0.0355  -0.0460 37  GLU   A OE2   
241  N  N     . ASP   A 41  ? 0.3296 0.4318 0.4509 -0.0030 0.0784  0.0673  38  ASP   A N     
242  C  CA    . ASP   A 41  ? 0.2960 0.4386 0.4593 0.0321  0.0472  0.0809  38  ASP   A CA    
243  C  C     . ASP   A 41  ? 0.1919 0.2976 0.4211 -0.0747 0.0217  0.0854  38  ASP   A C     
244  O  O     . ASP   A 41  ? 0.1845 0.3803 0.3463 -0.0254 0.0281  0.0754  38  ASP   A O     
245  C  CB    . ASP   A 41  ? 0.4470 0.4331 0.4507 0.0085  -0.0072 0.1979  38  ASP   A CB    
246  C  CG    . ASP   A 41  ? 0.5351 0.4851 0.5267 -0.0292 0.0436  0.2859  38  ASP   A CG    
247  O  OD1   . ASP   A 41  ? 0.4635 0.4369 0.5584 0.0236  0.1396  0.1956  38  ASP   A OD1   
248  O  OD2   . ASP   A 41  ? 0.7480 0.6571 0.4847 0.1173  0.0997  0.2900  38  ASP   A OD2   
249  N  N     . SER   A 42  ? 0.3276 0.3592 0.3476 -0.0485 0.1329  0.0979  39  SER   A N     
250  C  CA    . SER   A 42  ? 0.2917 0.3820 0.2535 -0.0736 0.0183  0.1115  39  SER   A CA    
251  C  C     . SER   A 42  ? 0.2408 0.3905 0.2386 -0.0820 0.0297  0.1131  39  SER   A C     
252  O  O     . SER   A 42  ? 0.2945 0.4290 0.2550 -0.0445 0.0026  0.1111  39  SER   A O     
253  C  CB    . SER   A 42  ? 0.2715 0.3555 0.3985 -0.0838 0.0238  0.0766  39  SER   A CB    
254  O  OG    . SER   A 42  ? 0.3128 0.4858 0.3734 -0.1038 0.1144  0.0842  39  SER   A OG    
255  N  N     . TYR   A 43  ? 0.2048 0.3880 0.2194 -0.0325 0.0385  0.0194  40  TYR   A N     
256  C  CA    . TYR   A 43  ? 0.2786 0.4015 0.1791 0.0041  0.0355  0.0236  40  TYR   A CA    
257  C  C     . TYR   A 43  ? 0.3140 0.4005 0.1729 0.0110  0.0347  0.0664  40  TYR   A C     
258  O  O     . TYR   A 43  ? 0.2558 0.4670 0.1865 0.0669  0.0124  0.0401  40  TYR   A O     
259  C  CB    . TYR   A 43  ? 0.2886 0.4091 0.2833 -0.0109 -0.0813 0.0142  40  TYR   A CB    
260  C  CG    . TYR   A 43  ? 0.2132 0.4404 0.3224 -0.0476 -0.0272 0.0138  40  TYR   A CG    
261  C  CD1   . TYR   A 43  ? 0.2700 0.3671 0.2698 -0.0794 0.0027  0.0767  40  TYR   A CD1   
262  C  CD2   . TYR   A 43  ? 0.3672 0.4456 0.3534 0.0331  -0.0915 0.0666  40  TYR   A CD2   
263  C  CE1   . TYR   A 43  ? 0.2409 0.5257 0.3183 -0.0406 0.0308  0.1076  40  TYR   A CE1   
264  C  CE2   . TYR   A 43  ? 0.3108 0.6434 0.2940 0.0914  -0.1189 0.0004  40  TYR   A CE2   
265  C  CZ    . TYR   A 43  ? 0.3269 0.5103 0.3532 0.0507  -0.0224 0.0523  40  TYR   A CZ    
266  O  OH    . TYR   A 43  ? 0.3539 0.4467 0.3604 0.0423  -0.0789 0.0478  40  TYR   A OH    
267  N  N     . ARG   A 44  ? 0.3342 0.5143 0.1897 0.0524  0.0260  0.0364  41  ARG   A N     
268  C  CA    . ARG   A 44  ? 0.2759 0.4476 0.2056 0.0204  0.0313  0.0363  41  ARG   A CA    
269  C  C     . ARG   A 44  ? 0.2330 0.4693 0.2646 0.0032  -0.0368 0.0201  41  ARG   A C     
270  O  O     . ARG   A 44  ? 0.3029 0.4734 0.2236 0.0370  -0.0165 -0.0019 41  ARG   A O     
271  C  CB    . ARG   A 44  ? 0.3572 0.4203 0.3354 0.0009  0.0537  0.1212  41  ARG   A CB    
272  C  CG    . ARG   A 44  ? 0.3331 0.5098 0.4795 -0.0749 0.0742  0.0697  41  ARG   A CG    
273  C  CD    . ARG   A 44  ? 0.4172 0.5186 0.5903 -0.1812 0.1117  -0.0626 41  ARG   A CD    
274  N  NE    . ARG   A 44  ? 0.4594 0.6408 0.6823 -0.0945 -0.0761 -0.0698 41  ARG   A NE    
275  C  CZ    . ARG   A 44  ? 0.4391 0.5959 0.6130 0.0039  -0.0350 -0.1675 41  ARG   A CZ    
276  N  NH1   . ARG   A 44  ? 0.5703 0.5927 0.7033 0.0671  0.0538  -0.2172 41  ARG   A NH1   
277  N  NH2   . ARG   A 44  ? 0.4593 0.7695 0.7522 0.0823  0.0715  -0.0386 41  ARG   A NH2   
278  N  N     . LYS   A 45  ? 0.2244 0.4433 0.1706 0.0309  0.0294  0.0161  42  LYS   A N     
279  C  CA    . LYS   A 45  ? 0.2629 0.4193 0.2084 0.0026  0.0134  0.0381  42  LYS   A CA    
280  C  C     . LYS   A 45  ? 0.1922 0.4649 0.2244 0.0459  0.0244  -0.0152 42  LYS   A C     
281  O  O     . LYS   A 45  ? 0.2569 0.4378 0.1922 0.0774  0.0712  -0.0238 42  LYS   A O     
282  C  CB    . LYS   A 45  ? 0.2602 0.4225 0.2844 0.0316  0.0317  0.0427  42  LYS   A CB    
283  C  CG    . LYS   A 45  ? 0.3790 0.4171 0.3796 0.0155  0.0157  0.0374  42  LYS   A CG    
284  C  CD    . LYS   A 45  ? 0.3231 0.5345 0.3521 0.0429  -0.0098 0.0099  42  LYS   A CD    
285  C  CE    . LYS   A 45  ? 0.4328 0.5041 0.4126 0.0333  -0.0509 0.0023  42  LYS   A CE    
286  N  NZ    . LYS   A 45  ? 0.4572 0.4373 0.4470 0.0225  0.0329  -0.0389 42  LYS   A NZ    
287  N  N     . GLN   A 46  ? 0.2711 0.4329 0.2341 0.0352  0.0724  -0.0014 43  GLN   A N     
288  C  CA    . GLN   A 46  ? 0.3503 0.3489 0.2754 0.0405  0.0589  -0.0100 43  GLN   A CA    
289  C  C     . GLN   A 46  ? 0.2712 0.3727 0.2421 0.0643  0.0671  0.0035  43  GLN   A C     
290  O  O     . GLN   A 46  ? 0.3730 0.4745 0.2080 -0.0032 0.0826  0.0058  43  GLN   A O     
291  C  CB    . GLN   A 46  ? 0.3540 0.2979 0.2576 0.0114  0.0643  0.0094  43  GLN   A CB    
292  C  CG    . GLN   A 46  ? 0.2949 0.3954 0.2848 0.0352  0.1267  0.0443  43  GLN   A CG    
293  C  CD    . GLN   A 46  ? 0.2611 0.3814 0.2390 0.0095  0.0840  -0.0310 43  GLN   A CD    
294  O  OE1   . GLN   A 46  ? 0.2387 0.4595 0.2728 -0.0269 0.1037  0.0329  43  GLN   A OE1   
295  N  NE2   . GLN   A 46  ? 0.3646 0.4070 0.2327 0.0678  0.0772  0.0171  43  GLN   A NE2   
296  N  N     . VAL   A 47  ? 0.2711 0.3851 0.2338 0.0367  0.0289  0.0002  44  VAL   A N     
297  C  CA    . VAL   A 47  ? 0.4147 0.3376 0.2092 0.0249  0.0642  -0.0359 44  VAL   A CA    
298  C  C     . VAL   A 47  ? 0.3431 0.3544 0.2422 0.0255  0.0296  -0.0559 44  VAL   A C     
299  O  O     . VAL   A 47  ? 0.4124 0.3630 0.2302 -0.0411 0.0321  -0.0145 44  VAL   A O     
300  C  CB    . VAL   A 47  ? 0.3637 0.4539 0.2381 0.0243  0.0573  0.0153  44  VAL   A CB    
301  C  CG1   . VAL   A 47  ? 0.3465 0.4512 0.2314 0.0016  0.0425  0.0056  44  VAL   A CG1   
302  C  CG2   . VAL   A 47  ? 0.3785 0.5305 0.1633 0.0327  0.1540  -0.0366 44  VAL   A CG2   
303  N  N     . VAL   A 48  ? 0.3926 0.3702 0.2311 -0.0409 0.0685  -0.0118 45  VAL   A N     
304  C  CA    . VAL   A 48  ? 0.4104 0.3895 0.2380 -0.0385 0.0139  -0.0503 45  VAL   A CA    
305  C  C     . VAL   A 48  ? 0.4326 0.4419 0.2569 -0.0826 0.0295  -0.0552 45  VAL   A C     
306  O  O     . VAL   A 48  ? 0.4417 0.5211 0.2362 -0.0949 0.0486  -0.0423 45  VAL   A O     
307  C  CB    . VAL   A 48  ? 0.4477 0.3130 0.3539 -0.0152 0.0674  -0.0381 45  VAL   A CB    
308  C  CG1   . VAL   A 48  ? 0.4842 0.3308 0.3478 0.0466  0.0553  -0.0478 45  VAL   A CG1   
309  C  CG2   . VAL   A 48  ? 0.4865 0.3473 0.3128 0.0669  0.0584  0.0203  45  VAL   A CG2   
310  N  N     . ILE   A 49  ? 0.4159 0.3153 0.2548 -0.0747 0.0464  -0.0396 46  ILE   A N     
311  C  CA    . ILE   A 49  ? 0.3705 0.3341 0.2910 -0.0830 0.0667  -0.0255 46  ILE   A CA    
312  C  C     . ILE   A 49  ? 0.4198 0.3405 0.2199 -0.0805 0.0648  0.0054  46  ILE   A C     
313  O  O     . ILE   A 49  ? 0.3803 0.3711 0.2581 -0.0304 0.0321  0.0131  46  ILE   A O     
314  C  CB    . ILE   A 49  ? 0.3981 0.3155 0.2798 -0.0510 0.0664  0.0125  46  ILE   A CB    
315  C  CG1   . ILE   A 49  ? 0.3770 0.3624 0.2761 -0.0342 0.0576  -0.0004 46  ILE   A CG1   
316  C  CG2   . ILE   A 49  ? 0.3887 0.4100 0.2815 -0.1215 0.0997  -0.0446 46  ILE   A CG2   
317  C  CD1   . ILE   A 49  ? 0.3669 0.3624 0.2261 -0.0111 0.0587  0.0311  46  ILE   A CD1   
318  N  N     . ASP   A 50  ? 0.4890 0.3616 0.3489 -0.1116 0.0314  -0.0653 47  ASP   A N     
319  C  CA    . ASP   A 50  ? 0.5028 0.2806 0.3392 -0.1006 0.0731  -0.0157 47  ASP   A CA    
320  C  C     . ASP   A 50  ? 0.4445 0.3535 0.4162 -0.0211 -0.0236 -0.0699 47  ASP   A C     
321  O  O     . ASP   A 50  ? 0.4669 0.2925 0.3771 0.0556  0.0170  -0.0053 47  ASP   A O     
322  C  CB    . ASP   A 50  ? 0.3814 0.4320 0.3219 -0.0972 0.0661  0.0458  47  ASP   A CB    
323  C  CG    . ASP   A 50  ? 0.2443 0.4567 0.3337 -0.0478 0.0094  -0.0731 47  ASP   A CG    
324  O  OD1   . ASP   A 50  ? 0.4893 0.3971 0.3932 -0.1214 0.0478  -0.0534 47  ASP   A OD1   
325  O  OD2   . ASP   A 50  ? 0.4615 0.3194 0.3597 0.0094  0.1138  0.0089  47  ASP   A OD2   
326  N  N     . GLY   A 51  ? 0.5133 0.5099 0.4513 -0.0778 0.1184  -0.0488 48  GLY   A N     
327  C  CA    . GLY   A 51  ? 0.4929 0.4761 0.4891 -0.0749 0.0863  -0.1076 48  GLY   A CA    
328  C  C     . GLY   A 51  ? 0.4722 0.2709 0.4305 0.0209  0.2109  0.0183  48  GLY   A C     
329  O  O     . GLY   A 51  ? 0.4794 0.4206 0.5338 0.0073  0.2328  -0.0385 48  GLY   A O     
330  N  N     . GLU   A 52  ? 0.5353 0.3351 0.2769 0.0103  0.0982  -0.0476 49  GLU   A N     
331  C  CA    . GLU   A 52  ? 0.4285 0.3713 0.3397 0.0475  0.1036  -0.0166 49  GLU   A CA    
332  C  C     . GLU   A 52  ? 0.4275 0.3016 0.3788 0.0334  0.1453  -0.0272 49  GLU   A C     
333  O  O     . GLU   A 52  ? 0.3554 0.4147 0.3170 0.0000  0.0617  0.0563  49  GLU   A O     
334  C  CB    . GLU   A 52  ? 0.3834 0.4257 0.3359 0.1138  0.0622  0.0236  49  GLU   A CB    
335  C  CG    . GLU   A 52  ? 0.2734 0.4064 0.4435 0.0772  0.0939  0.0458  49  GLU   A CG    
336  C  CD    . GLU   A 52  ? 0.6961 0.4323 0.4225 -0.0348 -0.0726 0.0494  49  GLU   A CD    
337  O  OE1   . GLU   A 52  ? 0.5016 0.4791 0.6060 0.1620  -0.1412 -0.0210 49  GLU   A OE1   
338  O  OE2   . GLU   A 52  ? 0.8786 0.4335 0.6544 -0.0735 -0.0948 0.1127  49  GLU   A OE2   
339  N  N     . THR   A 53  ? 0.3101 0.4411 0.3292 0.0773  0.0950  0.0451  50  THR   A N     
340  C  CA    . THR   A 53  ? 0.3729 0.3626 0.3320 0.0203  0.1127  0.0416  50  THR   A CA    
341  C  C     . THR   A 53  ? 0.3172 0.3646 0.2813 0.0181  0.0436  0.0616  50  THR   A C     
342  O  O     . THR   A 53  ? 0.2959 0.3949 0.3306 0.0491  0.0520  -0.0104 50  THR   A O     
343  C  CB    . THR   A 53  ? 0.4444 0.3501 0.2815 0.0266  0.1185  0.0282  50  THR   A CB    
344  O  OG1   . THR   A 53  ? 0.6052 0.4210 0.3465 -0.0783 0.1387  -0.0263 50  THR   A OG1   
345  C  CG2   . THR   A 53  ? 0.4974 0.3969 0.2729 0.0371  0.0752  0.0211  50  THR   A CG2   
346  N  N     . CYS   A 54  ? 0.2665 0.3705 0.2811 0.0056  0.0686  0.0108  51  CYS   A N     
347  C  CA    . CYS   A 54  ? 0.3099 0.4148 0.2428 -0.0020 0.0597  -0.0242 51  CYS   A CA    
348  C  C     . CYS   A 54  ? 0.2110 0.4472 0.2624 -0.0122 0.0594  -0.0432 51  CYS   A C     
349  O  O     . CYS   A 54  ? 0.2721 0.3582 0.2326 -0.0157 0.0541  0.0296  51  CYS   A O     
350  C  CB    . CYS   A 54  ? 0.2720 0.3784 0.2951 0.0048  0.1021  0.0647  51  CYS   A CB    
351  S  SG    . CYS   A 54  ? 0.2702 0.4526 0.2580 0.0021  0.0728  0.0249  51  CYS   A SG    
352  N  N     . LEU   A 55  ? 0.2155 0.3605 0.2371 0.0127  0.0863  0.0415  52  LEU   A N     
353  C  CA    . LEU   A 55  ? 0.2863 0.3406 0.2073 0.0427  0.0764  0.0108  52  LEU   A CA    
354  C  C     . LEU   A 55  ? 0.2584 0.3933 0.1810 0.0251  0.0573  0.0014  52  LEU   A C     
355  O  O     . LEU   A 55  ? 0.2108 0.3690 0.2513 0.0210  0.0419  -0.0396 52  LEU   A O     
356  C  CB    . LEU   A 55  ? 0.3149 0.4275 0.3341 0.0226  0.1363  0.0379  52  LEU   A CB    
357  C  CG    . LEU   A 55  ? 0.4067 0.4397 0.3219 0.0030  0.0567  0.0207  52  LEU   A CG    
358  C  CD1   . LEU   A 55  ? 0.3683 0.4332 0.3416 0.0258  0.0792  -0.0456 52  LEU   A CD1   
359  C  CD2   . LEU   A 55  ? 0.5548 0.4361 0.4438 -0.0497 0.0771  0.0550  52  LEU   A CD2   
360  N  N     . LEU   A 56  ? 0.2472 0.3565 0.1848 0.0580  0.0407  -0.0373 53  LEU   A N     
361  C  CA    . LEU   A 56  ? 0.2524 0.3962 0.1466 0.0368  0.0410  -0.0314 53  LEU   A CA    
362  C  C     . LEU   A 56  ? 0.1838 0.4082 0.1966 0.0255  -0.0076 0.0190  53  LEU   A C     
363  O  O     . LEU   A 56  ? 0.3038 0.4438 0.1903 0.0781  0.0278  0.0208  53  LEU   A O     
364  C  CB    . LEU   A 56  ? 0.2857 0.3528 0.1783 0.0076  0.0729  -0.0468 53  LEU   A CB    
365  C  CG    . LEU   A 56  ? 0.2892 0.3777 0.2094 0.0256  0.0332  -0.0089 53  LEU   A CG    
366  C  CD1   . LEU   A 56  ? 0.3189 0.4218 0.2478 -0.0112 0.0638  -0.0060 53  LEU   A CD1   
367  C  CD2   . LEU   A 56  ? 0.2634 0.4048 0.2170 0.0187  0.0874  0.0824  53  LEU   A CD2   
368  N  N     . ASP   A 57  ? 0.1350 0.3694 0.2092 0.0229  0.0231  0.0308  54  ASP   A N     
369  C  CA    . ASP   A 57  ? 0.1817 0.3350 0.1833 -0.0191 0.0609  0.0223  54  ASP   A CA    
370  C  C     . ASP   A 57  ? 0.1890 0.4206 0.1954 0.0347  0.0605  0.0417  54  ASP   A C     
371  O  O     . ASP   A 57  ? 0.1354 0.3856 0.2306 0.0119  0.0689  0.0367  54  ASP   A O     
372  C  CB    . ASP   A 57  ? 0.1339 0.4038 0.2865 0.0107  0.0380  0.0168  54  ASP   A CB    
373  C  CG    . ASP   A 57  ? 0.1866 0.4159 0.2775 -0.0652 0.0327  0.0290  54  ASP   A CG    
374  O  OD1   . ASP   A 57  ? 0.2059 0.3958 0.2651 -0.0545 0.0461  0.0266  54  ASP   A OD1   
375  O  OD2   . ASP   A 57  ? 0.2091 0.4722 0.4681 -0.1010 0.0653  0.0308  54  ASP   A OD2   
376  N  N     . ILE   A 58  ? 0.1557 0.3185 0.2153 0.0052  0.0604  0.0608  55  ILE   A N     
377  C  CA    . ILE   A 58  ? 0.1502 0.2988 0.1956 -0.0238 0.0434  0.0421  55  ILE   A CA    
378  C  C     . ILE   A 58  ? 0.1507 0.3193 0.2299 0.0005  0.0385  0.0598  55  ILE   A C     
379  O  O     . ILE   A 58  ? 0.2145 0.3805 0.2224 0.0095  0.0587  0.0799  55  ILE   A O     
380  C  CB    . ILE   A 58  ? 0.1856 0.2995 0.1751 -0.0360 0.0438  0.0192  55  ILE   A CB    
381  C  CG1   . ILE   A 58  ? 0.1649 0.2873 0.2499 -0.0635 0.0562  0.0427  55  ILE   A CG1   
382  C  CG2   . ILE   A 58  ? 0.1545 0.3632 0.2336 -0.0541 0.0360  -0.0142 55  ILE   A CG2   
383  C  CD1   . ILE   A 58  ? 0.2922 0.3207 0.2816 -0.0445 0.0291  0.0221  55  ILE   A CD1   
384  N  N     . LEU   A 59  ? 0.1318 0.2705 0.2237 -0.0375 0.0374  0.0409  56  LEU   A N     
385  C  CA    . LEU   A 59  ? 0.1768 0.2283 0.2604 -0.0837 0.0607  0.0708  56  LEU   A CA    
386  C  C     . LEU   A 59  ? 0.1475 0.2874 0.2852 -0.0115 0.0454  0.1001  56  LEU   A C     
387  O  O     . LEU   A 59  ? 0.1253 0.2489 0.2713 -0.0156 0.0313  0.0879  56  LEU   A O     
388  C  CB    . LEU   A 59  ? 0.1307 0.2888 0.2667 -0.0230 0.0370  0.0158  56  LEU   A CB    
389  C  CG    . LEU   A 59  ? 0.1876 0.2354 0.2675 -0.0688 0.0481  0.0252  56  LEU   A CG    
390  C  CD1   . LEU   A 59  ? 0.2097 0.2231 0.3532 -0.0457 0.0050  0.0855  56  LEU   A CD1   
391  C  CD2   . LEU   A 59  ? 0.1858 0.2488 0.3080 -0.0455 0.0278  -0.0108 56  LEU   A CD2   
392  N  N     . ASP   A 60  ? 0.1215 0.2992 0.2313 -0.0475 0.0294  0.0473  57  ASP   A N     
393  C  CA    . ASP   A 60  ? 0.1093 0.3288 0.2680 -0.0620 0.0124  0.0427  57  ASP   A CA    
394  C  C     . ASP   A 60  ? 0.2073 0.3079 0.3069 -0.0444 0.0490  0.0477  57  ASP   A C     
395  O  O     . ASP   A 60  ? 0.4346 0.3572 0.4177 -0.0163 0.1960  0.0862  57  ASP   A O     
396  C  CB    . ASP   A 60  ? 0.1587 0.4005 0.2457 0.0358  0.0032  0.0383  57  ASP   A CB    
397  C  CG    . ASP   A 60  ? 0.1542 0.3282 0.2777 0.0150  0.0050  0.0297  57  ASP   A CG    
398  O  OD1   . ASP   A 60  ? 0.1626 0.3341 0.2840 -0.0227 -0.0117 0.0724  57  ASP   A OD1   
399  O  OD2   . ASP   A 60  ? 0.1482 0.3579 0.2806 -0.0645 0.0025  0.0824  57  ASP   A OD2   
400  N  N     . THR   A 61  ? 0.2223 0.2387 0.2854 -0.0886 0.0423  0.0372  58  THR   A N     
401  C  CA    . THR   A 61  ? 0.2689 0.1999 0.2923 -0.0741 0.0013  0.0519  58  THR   A CA    
402  C  C     . THR   A 61  ? 0.2981 0.2651 0.3587 -0.0459 0.0081  0.0396  58  THR   A C     
403  O  O     . THR   A 61  ? 0.3079 0.3609 0.3085 -0.0422 -0.0123 0.0220  58  THR   A O     
404  C  CB    . THR   A 61  ? 0.2515 0.2251 0.2956 -0.0340 -0.0141 0.0728  58  THR   A CB    
405  O  OG1   . THR   A 61  ? 0.2257 0.2092 0.2766 -0.0147 0.0304  0.0101  58  THR   A OG1   
406  C  CG2   . THR   A 61  ? 0.2591 0.2078 0.2771 -0.0161 -0.0021 -0.0138 58  THR   A CG2   
407  N  N     . ALA   A 62  ? 0.1964 0.2615 0.4458 -0.0201 0.0246  0.0668  59  ALA   A N     
408  C  CA    . ALA   A 62  ? 0.2287 0.2786 0.5329 0.0344  -0.0260 0.0149  59  ALA   A CA    
409  C  C     . ALA   A 62  ? 0.2307 0.2788 0.5069 0.0679  -0.0517 0.0410  59  ALA   A C     
410  O  O     . ALA   A 62  ? 0.2545 0.3216 0.4454 0.0082  -0.0059 0.0004  59  ALA   A O     
411  C  CB    . ALA   A 62  ? 0.3912 0.2639 0.6078 -0.0050 -0.0154 0.0101  59  ALA   A CB    
412  N  N     . GLY   A 63  ? 0.2295 0.3059 0.4912 0.0738  -0.0425 0.0976  60  GLY   A N     
413  C  CA    . GLY   A 63  ? 0.3858 0.3216 0.4503 0.0474  0.0303  -0.0334 60  GLY   A CA    
414  C  C     . GLY   A 63  ? 0.3325 0.4615 0.4494 -0.0060 0.0872  -0.1692 60  GLY   A C     
415  O  O     . GLY   A 63  ? 0.6270 0.6073 0.5447 0.0699  0.1703  -0.1318 60  GLY   A O     
416  N  N     . GLU   A 66  ? 0.5717 0.5113 0.7187 -0.0665 0.0667  0.0278  63  GLU   A N     
417  C  CA    . GLU   A 66  ? 0.5703 0.4227 0.6149 0.0248  0.0350  -0.0111 63  GLU   A CA    
418  C  C     . GLU   A 66  ? 0.5558 0.5301 0.5342 -0.0884 0.0445  0.0469  63  GLU   A C     
419  O  O     . GLU   A 66  ? 0.5980 0.6192 0.6239 0.1167  0.1443  0.0988  63  GLU   A O     
420  C  CB    . GLU   A 66  ? 0.5462 0.4036 0.6668 0.0557  0.0668  -0.0871 63  GLU   A CB    
421  C  CG    . GLU   A 66  ? 0.6247 0.3899 0.6891 0.0414  0.0688  -0.0714 63  GLU   A CG    
422  C  CD    . GLU   A 66  ? 0.4114 0.4076 0.4996 0.0572  -0.0005 0.0317  63  GLU   A CD    
423  O  OE1   . GLU   A 66  ? 0.3231 0.4061 0.5395 -0.0091 0.0020  0.0799  63  GLU   A OE1   
424  O  OE2   . GLU   A 66  ? 0.2391 0.3328 0.5868 -0.0159 0.0281  0.0380  63  GLU   A OE2   
425  N  N     . TYR   A 67  ? 0.4823 0.5871 0.5700 -0.0686 -0.0085 -0.0208 64  TYR   A N     
426  C  CA    . TYR   A 67  ? 0.4308 0.4054 0.5115 -0.0161 -0.0446 0.0218  64  TYR   A CA    
427  C  C     . TYR   A 67  ? 0.4201 0.3352 0.4956 -0.0288 -0.0307 -0.0150 64  TYR   A C     
428  O  O     . TYR   A 67  ? 0.3420 0.3294 0.5587 -0.0069 -0.0481 0.0599  64  TYR   A O     
429  C  CB    . TYR   A 67  ? 0.4407 0.3936 0.5338 -0.0825 -0.0708 0.0056  64  TYR   A CB    
430  C  CG    . TYR   A 67  ? 0.4068 0.2959 0.4042 -0.0163 -0.0439 0.0163  64  TYR   A CG    
431  C  CD1   . TYR   A 67  ? 0.3617 0.2739 0.5587 -0.0313 -0.0342 -0.0400 64  TYR   A CD1   
432  C  CD2   . TYR   A 67  ? 0.4453 0.3728 0.4865 -0.1019 0.0617  -0.0414 64  TYR   A CD2   
433  C  CE1   . TYR   A 67  ? 0.3171 0.2423 0.4472 0.0264  -0.0146 -0.0470 64  TYR   A CE1   
434  C  CE2   . TYR   A 67  ? 0.4682 0.3730 0.3919 -0.0584 0.0900  -0.1289 64  TYR   A CE2   
435  C  CZ    . TYR   A 67  ? 0.3353 0.2403 0.3524 -0.0150 0.0258  -0.0691 64  TYR   A CZ    
436  O  OH    . TYR   A 67  ? 0.3417 0.2794 0.2643 -0.0333 0.0098  -0.0179 64  TYR   A OH    
437  N  N     . SER   A 68  ? 0.2994 0.4603 0.4629 -0.0838 -0.0028 0.0377  65  SER   A N     
438  C  CA    . SER   A 68  ? 0.4235 0.4179 0.4914 -0.0498 0.0120  0.0513  65  SER   A CA    
439  C  C     . SER   A 68  ? 0.4241 0.2114 0.5772 -0.0790 0.0413  0.0100  65  SER   A C     
440  O  O     . SER   A 68  ? 0.4398 0.2735 0.3911 0.0040  0.0374  0.0457  65  SER   A O     
441  C  CB    . SER   A 68  ? 0.4821 0.4170 0.5597 0.0142  0.0299  -0.0218 65  SER   A CB    
442  O  OG    . SER   A 68  ? 0.6945 0.4036 0.5103 -0.1023 -0.0042 -0.0303 65  SER   A OG    
443  N  N     . ALA   A 69  ? 0.3806 0.1702 0.6201 -0.0123 0.0462  0.0830  66  ALA   A N     
444  C  CA    . ALA   A 69  ? 0.3603 0.2949 0.5256 -0.0365 0.0034  0.0369  66  ALA   A CA    
445  C  C     . ALA   A 69  ? 0.4130 0.2676 0.5260 0.0000  -0.0805 0.0444  66  ALA   A C     
446  O  O     . ALA   A 69  ? 0.2537 0.2767 0.5768 -0.0458 0.0100  0.0460  66  ALA   A O     
447  C  CB    . ALA   A 69  ? 0.4189 0.2301 0.5366 -0.0042 -0.0428 0.0386  66  ALA   A CB    
448  N  N     . MET   A 70  ? 0.3902 0.3302 0.4446 -0.0411 -0.0148 0.0434  67  MET   A N     
449  C  CA    . MET   A 70  ? 0.3093 0.2916 0.4690 0.0027  -0.0293 0.0327  67  MET   A CA    
450  C  C     . MET   A 70  ? 0.3048 0.3306 0.4249 -0.0296 0.0509  0.0154  67  MET   A C     
451  O  O     . MET   A 70  ? 0.2308 0.3093 0.3743 -0.0654 0.0132  -0.0042 67  MET   A O     
452  C  CB    . MET   A 70  ? 0.4049 0.3609 0.3668 -0.0411 0.0313  0.0920  67  MET   A CB    
453  C  CG    . MET   A 70  ? 0.4320 0.4710 0.4408 -0.0166 -0.0218 -0.0184 67  MET   A CG    
454  S  SD    . MET   A 70  ? 0.6367 0.5225 0.5525 0.0006  -0.0176 0.0242  67  MET   A SD    
455  C  CE    . MET   A 70  ? 0.4830 0.3385 0.5227 0.0650  -0.0083 -0.0066 67  MET   A CE    
456  N  N     . ARG   A 71  ? 0.3349 0.1915 0.4032 0.0398  0.0463  0.0816  68  ARG   A N     
457  C  CA    . ARG   A 71  ? 0.2340 0.1939 0.4248 -0.0188 0.0429  -0.0014 68  ARG   A CA    
458  C  C     . ARG   A 71  ? 0.1819 0.2253 0.3715 -0.0816 0.0445  -0.0367 68  ARG   A C     
459  O  O     . ARG   A 71  ? 0.2172 0.2176 0.3001 -0.0402 0.0548  0.0017  68  ARG   A O     
460  C  CB    . ARG   A 71  ? 0.2251 0.3167 0.4952 -0.0016 0.0646  0.0037  68  ARG   A CB    
461  C  CG    . ARG   A 71  ? 0.2047 0.3076 0.6222 -0.0156 0.0562  -0.0094 68  ARG   A CG    
462  C  CD    . ARG   A 71  ? 0.2825 0.3967 0.6548 -0.0473 0.0908  -0.0191 68  ARG   A CD    
463  N  NE    . ARG   A 71  ? 0.4696 0.4453 0.5991 0.0087  0.0525  -0.0611 68  ARG   A NE    
464  C  CZ    . ARG   A 71  ? 0.4447 0.5278 0.5135 -0.0862 0.0332  -0.0056 68  ARG   A CZ    
465  N  NH1   . ARG   A 71  ? 0.4136 0.6017 0.6672 -0.0907 0.0496  0.0077  68  ARG   A NH1   
466  N  NH2   . ARG   A 71  ? 0.3577 0.4889 0.6239 0.0358  -0.0532 -0.0360 68  ARG   A NH2   
467  N  N     . ASP   A 72  ? 0.2157 0.2061 0.3207 -0.0270 0.0039  -0.0086 69  ASP   A N     
468  C  CA    . ASP   A 72  ? 0.2425 0.2727 0.3639 0.0442  -0.0016 -0.0534 69  ASP   A CA    
469  C  C     . ASP   A 72  ? 0.2355 0.2718 0.3741 -0.0012 0.0556  0.0214  69  ASP   A C     
470  O  O     . ASP   A 72  ? 0.2081 0.2250 0.3265 -0.0367 0.0555  -0.0230 69  ASP   A O     
471  C  CB    . ASP   A 72  ? 0.2676 0.3642 0.3605 0.0130  -0.0393 -0.0632 69  ASP   A CB    
472  C  CG    . ASP   A 72  ? 0.3738 0.3965 0.3755 -0.0380 0.0039  -0.1149 69  ASP   A CG    
473  O  OD1   . ASP   A 72  ? 0.3117 0.4070 0.3633 0.0089  0.0686  -0.0641 69  ASP   A OD1   
474  O  OD2   . ASP   A 72  ? 0.4116 0.4118 0.5088 0.0637  -0.0777 -0.1549 69  ASP   A OD2   
475  N  N     . GLN   A 73  ? 0.2130 0.2263 0.3731 -0.0568 0.0110  0.0217  70  GLN   A N     
476  C  CA    . GLN   A 73  ? 0.1680 0.2953 0.3963 -0.0134 -0.0113 -0.0005 70  GLN   A CA    
477  C  C     . GLN   A 73  ? 0.2088 0.2787 0.3437 -0.0321 -0.0119 0.0371  70  GLN   A C     
478  O  O     . GLN   A 73  ? 0.1947 0.2323 0.3476 -0.0585 0.0279  0.0425  70  GLN   A O     
479  C  CB    . GLN   A 73  ? 0.2216 0.2501 0.3693 -0.0404 -0.0031 -0.0207 70  GLN   A CB    
480  C  CG    . GLN   A 73  ? 0.2698 0.2533 0.3884 -0.0903 0.0328  -0.0255 70  GLN   A CG    
481  C  CD    . GLN   A 73  ? 0.2765 0.2392 0.3525 -0.0901 0.0484  0.0052  70  GLN   A CD    
482  O  OE1   . GLN   A 73  ? 0.2312 0.3528 0.4279 -0.0564 -0.0223 -0.0901 70  GLN   A OE1   
483  N  NE2   . GLN   A 73  ? 0.1960 0.3216 0.3441 -0.0544 0.0612  0.0611  70  GLN   A NE2   
484  N  N     . TYR   A 74  ? 0.1667 0.2881 0.2579 -0.0244 0.0388  0.0123  71  TYR   A N     
485  C  CA    . TYR   A 74  ? 0.1439 0.2911 0.3175 -0.0456 0.0196  0.0421  71  TYR   A CA    
486  C  C     . TYR   A 74  ? 0.1831 0.2391 0.3268 -0.0275 -0.0038 0.0183  71  TYR   A C     
487  O  O     . TYR   A 74  ? 0.1739 0.2523 0.2748 -0.0420 0.0443  -0.0226 71  TYR   A O     
488  C  CB    . TYR   A 74  ? 0.1697 0.2342 0.2933 -0.0049 0.0101  0.0591  71  TYR   A CB    
489  C  CG    . TYR   A 74  ? 0.1776 0.3146 0.2750 -0.0402 0.0236  0.0310  71  TYR   A CG    
490  C  CD1   . TYR   A 74  ? 0.2046 0.2240 0.2503 -0.0154 0.0230  -0.0080 71  TYR   A CD1   
491  C  CD2   . TYR   A 74  ? 0.1884 0.2628 0.3567 -0.0752 -0.0109 0.0450  71  TYR   A CD2   
492  C  CE1   . TYR   A 74  ? 0.2041 0.2175 0.2542 -0.0455 0.0329  -0.0055 71  TYR   A CE1   
493  C  CE2   . TYR   A 74  ? 0.1978 0.3031 0.3137 -0.0179 -0.0204 0.0083  71  TYR   A CE2   
494  C  CZ    . TYR   A 74  ? 0.1682 0.3401 0.2914 -0.0192 0.0315  -0.0145 71  TYR   A CZ    
495  O  OH    . TYR   A 74  ? 0.1500 0.2784 0.3585 -0.0320 0.0533  0.0108  71  TYR   A OH    
496  N  N     . MET   A 75  ? 0.1635 0.2258 0.3172 -0.0411 -0.0088 0.0077  72  MET   A N     
497  C  CA    . MET   A 75  ? 0.2107 0.2045 0.3012 -0.0111 0.0443  -0.0249 72  MET   A CA    
498  C  C     . MET   A 75  ? 0.2417 0.2931 0.2853 -0.0180 0.0259  0.0085  72  MET   A C     
499  O  O     . MET   A 75  ? 0.1909 0.2778 0.3013 -0.0308 -0.0395 -0.0026 72  MET   A O     
500  C  CB    . MET   A 75  ? 0.1975 0.2941 0.2458 -0.0604 0.0160  -0.0035 72  MET   A CB    
501  C  CG    . MET   A 75  ? 0.2073 0.2470 0.2420 -0.0510 0.0377  -0.0146 72  MET   A CG    
502  S  SD    . MET   A 75  ? 0.1983 0.2615 0.2564 -0.0349 0.0423  -0.0097 72  MET   A SD    
503  C  CE    . MET   A 75  ? 0.2131 0.2781 0.2475 -0.0469 0.0763  -0.0017 72  MET   A CE    
504  N  N     . ARG   A 76  ? 0.2255 0.2282 0.2922 0.0308  0.0056  -0.0193 73  ARG   A N     
505  C  CA    . ARG   A 76  ? 0.2109 0.2833 0.2961 -0.0181 -0.0208 -0.0045 73  ARG   A CA    
506  C  C     . ARG   A 76  ? 0.2193 0.2291 0.3259 -0.0349 -0.0055 0.0125  73  ARG   A C     
507  O  O     . ARG   A 76  ? 0.2218 0.2243 0.3389 -0.0311 -0.0019 -0.0005 73  ARG   A O     
508  C  CB    . ARG   A 76  ? 0.2755 0.2805 0.3584 -0.0191 0.0212  -0.0066 73  ARG   A CB    
509  C  CG    . ARG   A 76  ? 0.3296 0.4168 0.5082 -0.0107 -0.0121 -0.0268 73  ARG   A CG    
510  C  CD    . ARG   A 76  ? 0.4238 0.4405 0.6081 -0.1318 -0.0760 -0.0179 73  ARG   A CD    
511  N  NE    . ARG   A 76  ? 0.3935 0.4785 0.6113 -0.0789 -0.0094 -0.0299 73  ARG   A NE    
512  C  CZ    . ARG   A 76  ? 0.5529 0.3927 0.5960 -0.0419 0.0772  0.0181  73  ARG   A CZ    
513  N  NH1   . ARG   A 76  ? 0.3344 0.4775 0.6012 -0.0473 -0.0648 0.0841  73  ARG   A NH1   
514  N  NH2   . ARG   A 76  ? 0.4952 0.5234 0.5844 -0.0911 0.0713  -0.0853 73  ARG   A NH2   
515  N  N     . THR   A 77  ? 0.1450 0.3250 0.3282 -0.0456 -0.0012 -0.0233 74  THR   A N     
516  C  CA    . THR   A 77  ? 0.1588 0.2984 0.3158 -0.0446 0.0003  -0.0321 74  THR   A CA    
517  C  C     . THR   A 77  ? 0.1409 0.2849 0.3521 -0.0362 0.0229  -0.0034 74  THR   A C     
518  O  O     . THR   A 77  ? 0.1875 0.2648 0.2827 -0.0503 0.0314  -0.0404 74  THR   A O     
519  C  CB    . THR   A 77  ? 0.1876 0.2714 0.3117 -0.0531 0.0063  -0.0203 74  THR   A CB    
520  O  OG1   . THR   A 77  ? 0.1840 0.3254 0.3014 -0.0693 0.0531  -0.0645 74  THR   A OG1   
521  C  CG2   . THR   A 77  ? 0.2190 0.3607 0.2707 -0.0644 0.0155  0.0005  74  THR   A CG2   
522  N  N     . GLY   A 78  ? 0.1375 0.2416 0.2534 -0.0253 0.0435  -0.0266 75  GLY   A N     
523  C  CA    . GLY   A 78  ? 0.1472 0.1984 0.2261 -0.0061 0.0650  -0.0021 75  GLY   A CA    
524  C  C     . GLY   A 78  ? 0.1317 0.2568 0.2968 -0.0105 0.0202  0.0229  75  GLY   A C     
525  O  O     . GLY   A 78  ? 0.1374 0.3114 0.2787 0.0027  0.0060  0.0054  75  GLY   A O     
526  N  N     . GLU   A 79  ? 0.0936 0.3232 0.2576 -0.0045 0.0365  0.0079  76  GLU   A N     
527  C  CA    . GLU   A 79  ? 0.1344 0.2895 0.2545 0.0049  0.0111  -0.0109 76  GLU   A CA    
528  C  C     . GLU   A 79  ? 0.1421 0.2793 0.2585 0.0254  0.0107  0.0390  76  GLU   A C     
529  O  O     . GLU   A 79  ? 0.1874 0.3109 0.2658 0.0117  -0.0006 0.0567  76  GLU   A O     
530  C  CB    . GLU   A 79  ? 0.1388 0.3069 0.2577 -0.0140 0.0360  -0.0224 76  GLU   A CB    
531  C  CG    . GLU   A 79  ? 0.1440 0.3591 0.3093 -0.0507 -0.0193 -0.0110 76  GLU   A CG    
532  C  CD    . GLU   A 79  ? 0.2045 0.6062 0.3239 0.0836  -0.0300 -0.0909 76  GLU   A CD    
533  O  OE1   . GLU   A 79  ? 0.1365 0.4544 0.3086 0.0243  0.0093  -0.0557 76  GLU   A OE1   
534  O  OE2   . GLU   A 79  ? 0.2289 0.7503 0.4844 0.1008  -0.0133 -0.0115 76  GLU   A OE2   
535  N  N     . GLY   A 80  ? 0.1852 0.2376 0.1989 0.0007  -0.0057 0.0382  77  GLY   A N     
536  C  CA    . GLY   A 80  ? 0.2128 0.2401 0.2754 0.0066  0.0368  0.0509  77  GLY   A CA    
537  C  C     . GLY   A 80  ? 0.2006 0.2128 0.2499 -0.0195 0.0340  0.0366  77  GLY   A C     
538  O  O     . GLY   A 80  ? 0.1076 0.2342 0.2484 0.0015  0.0319  0.0207  77  GLY   A O     
539  N  N     . PHE   A 81  ? 0.1796 0.1495 0.1918 0.0166  0.0216  0.0204  78  PHE   A N     
540  C  CA    . PHE   A 81  ? 0.1879 0.1861 0.1899 0.0111  0.0198  0.0112  78  PHE   A CA    
541  C  C     . PHE   A 81  ? 0.1778 0.2068 0.2458 0.0254  0.0053  -0.0293 78  PHE   A C     
542  O  O     . PHE   A 81  ? 0.1444 0.2459 0.2257 0.0279  -0.0034 -0.0020 78  PHE   A O     
543  C  CB    . PHE   A 81  ? 0.1211 0.2021 0.1922 0.0318  0.0146  0.0085  78  PHE   A CB    
544  C  CG    . PHE   A 81  ? 0.1490 0.2190 0.1791 0.0002  0.0276  0.0065  78  PHE   A CG    
545  C  CD1   . PHE   A 81  ? 0.1564 0.2750 0.1846 -0.0193 0.0050  0.0191  78  PHE   A CD1   
546  C  CD2   . PHE   A 81  ? 0.2023 0.1920 0.1618 -0.0420 0.0396  -0.0188 78  PHE   A CD2   
547  C  CE1   . PHE   A 81  ? 0.1589 0.2158 0.2127 0.0125  0.0076  -0.0608 78  PHE   A CE1   
548  C  CE2   . PHE   A 81  ? 0.2036 0.1967 0.2590 -0.0386 0.0119  -0.0507 78  PHE   A CE2   
549  C  CZ    . PHE   A 81  ? 0.2282 0.2085 0.2291 -0.0103 0.0464  -0.0147 78  PHE   A CZ    
550  N  N     . LEU   A 82  ? 0.1061 0.2354 0.1899 -0.0314 0.0642  0.0185  79  LEU   A N     
551  C  CA    . LEU   A 82  ? 0.1670 0.1567 0.2013 -0.0324 0.0273  0.0286  79  LEU   A CA    
552  C  C     . LEU   A 82  ? 0.1847 0.2335 0.2508 0.0288  -0.0063 0.0040  79  LEU   A C     
553  O  O     . LEU   A 82  ? 0.1010 0.2729 0.2662 0.0087  0.0672  0.0345  79  LEU   A O     
554  C  CB    . LEU   A 82  ? 0.2420 0.2317 0.2230 0.0028  -0.0091 0.0044  79  LEU   A CB    
555  C  CG    . LEU   A 82  ? 0.3076 0.2668 0.2057 0.0537  0.0130  0.0245  79  LEU   A CG    
556  C  CD1   . LEU   A 82  ? 0.3428 0.2429 0.1863 -0.0872 0.0260  0.0278  79  LEU   A CD1   
557  C  CD2   . LEU   A 82  ? 0.2684 0.2422 0.1786 0.0759  0.0440  -0.0172 79  LEU   A CD2   
558  N  N     . CYS   A 83  ? 0.1622 0.1746 0.2178 0.0303  -0.0173 0.0084  80  CYS   A N     
559  C  CA    . CYS   A 83  ? 0.1307 0.2058 0.2160 0.0204  0.0105  0.0336  80  CYS   A CA    
560  C  C     . CYS   A 83  ? 0.1783 0.2569 0.1894 0.0120  0.0034  -0.0249 80  CYS   A C     
561  O  O     . CYS   A 83  ? 0.1269 0.2597 0.1733 0.0102  0.0153  -0.0168 80  CYS   A O     
562  C  CB    . CYS   A 83  ? 0.1244 0.2273 0.2061 -0.0165 0.0225  0.0381  80  CYS   A CB    
563  S  SG    . CYS   A 83  ? 0.1602 0.3411 0.2566 -0.0372 -0.0121 0.0038  80  CYS   A SG    
564  N  N     . VAL   A 84  ? 0.1203 0.2509 0.1999 -0.0370 0.0418  -0.0064 81  VAL   A N     
565  C  CA    . VAL   A 84  ? 0.1425 0.2485 0.1751 -0.0232 0.0079  -0.0118 81  VAL   A CA    
566  C  C     . VAL   A 84  ? 0.1280 0.2856 0.2141 -0.0088 -0.0112 -0.0388 81  VAL   A C     
567  O  O     . VAL   A 84  ? 0.1183 0.3036 0.1905 -0.0339 0.0415  -0.0232 81  VAL   A O     
568  C  CB    . VAL   A 84  ? 0.1095 0.2487 0.1975 -0.0008 0.0269  -0.0019 81  VAL   A CB    
569  C  CG1   . VAL   A 84  ? 0.1093 0.2779 0.2086 -0.0197 0.0412  0.0015  81  VAL   A CG1   
570  C  CG2   . VAL   A 84  ? 0.1218 0.2739 0.2147 0.0023  0.0414  -0.0169 81  VAL   A CG2   
571  N  N     . PHE   A 85  ? 0.1235 0.2417 0.1935 0.0174  0.0062  -0.0072 82  PHE   A N     
572  C  CA    . PHE   A 85  ? 0.1267 0.2777 0.1860 0.0260  0.0149  -0.0206 82  PHE   A CA    
573  C  C     . PHE   A 85  ? 0.1570 0.2498 0.2552 -0.0291 0.0254  -0.0583 82  PHE   A C     
574  O  O     . PHE   A 85  ? 0.1566 0.2538 0.2030 -0.0178 0.0059  -0.0180 82  PHE   A O     
575  C  CB    . PHE   A 85  ? 0.1121 0.3173 0.1938 0.0066  0.0580  -0.0089 82  PHE   A CB    
576  C  CG    . PHE   A 85  ? 0.1384 0.3153 0.1894 -0.0612 0.0417  -0.0093 82  PHE   A CG    
577  C  CD1   . PHE   A 85  ? 0.1381 0.3123 0.1650 -0.0426 0.0499  -0.0540 82  PHE   A CD1   
578  C  CD2   . PHE   A 85  ? 0.1273 0.3675 0.1617 -0.0417 0.0476  -0.0590 82  PHE   A CD2   
579  C  CE1   . PHE   A 85  ? 0.2298 0.3221 0.1982 -0.0283 0.0409  -0.0582 82  PHE   A CE1   
580  C  CE2   . PHE   A 85  ? 0.1686 0.3767 0.1821 -0.0540 0.0611  -0.0342 82  PHE   A CE2   
581  C  CZ    . PHE   A 85  ? 0.2325 0.3141 0.1556 -0.0607 0.0474  -0.0228 82  PHE   A CZ    
582  N  N     . ALA   A 86  ? 0.1536 0.3343 0.1799 -0.0088 0.0056  -0.0116 83  ALA   A N     
583  C  CA    . ALA   A 86  ? 0.1170 0.3394 0.2116 -0.0253 0.0267  -0.0060 83  ALA   A CA    
584  C  C     . ALA   A 86  ? 0.1342 0.3441 0.2018 -0.0524 0.0202  -0.0586 83  ALA   A C     
585  O  O     . ALA   A 86  ? 0.1455 0.4226 0.1923 -0.0132 0.0336  -0.0507 83  ALA   A O     
586  C  CB    . ALA   A 86  ? 0.1258 0.3474 0.1955 -0.0063 0.0497  -0.0083 83  ALA   A CB    
587  N  N     . ILE   A 87  ? 0.1804 0.3208 0.1575 -0.0722 0.0328  -0.0276 84  ILE   A N     
588  C  CA    . ILE   A 87  ? 0.1563 0.3239 0.2214 -0.0540 0.0294  0.0152  84  ILE   A CA    
589  C  C     . ILE   A 87  ? 0.1152 0.4117 0.2433 -0.0857 0.0132  0.0009  84  ILE   A C     
590  O  O     . ILE   A 87  ? 0.1919 0.4401 0.2312 -0.1232 0.0881  -0.0665 84  ILE   A O     
591  C  CB    . ILE   A 87  ? 0.1943 0.3457 0.2227 -0.0883 0.0888  -0.0086 84  ILE   A CB    
592  C  CG1   . ILE   A 87  ? 0.3014 0.3930 0.1825 -0.0840 0.0707  0.0000  84  ILE   A CG1   
593  C  CG2   . ILE   A 87  ? 0.2350 0.3472 0.2123 -0.0714 0.0901  -0.0146 84  ILE   A CG2   
594  C  CD1   . ILE   A 87  ? 0.2685 0.3801 0.3269 -0.0573 0.0606  -0.0312 84  ILE   A CD1   
595  N  N     . ASN   A 88  ? 0.1724 0.3673 0.1942 -0.0225 0.0333  -0.0422 85  ASN   A N     
596  C  CA    . ASN   A 88  ? 0.1207 0.4036 0.2395 -0.0391 0.0485  -0.0192 85  ASN   A CA    
597  C  C     . ASN   A 88  ? 0.2239 0.3859 0.2444 -0.0190 0.0200  -0.0111 85  ASN   A C     
598  O  O     . ASN   A 88  ? 0.1939 0.5429 0.2699 -0.0024 0.0192  -0.0213 85  ASN   A O     
599  C  CB    . ASN   A 88  ? 0.2199 0.4612 0.2533 -0.0105 0.0076  -0.0412 85  ASN   A CB    
600  C  CG    . ASN   A 88  ? 0.1556 0.5131 0.1979 -0.0139 -0.0251 -0.0038 85  ASN   A CG    
601  O  OD1   . ASN   A 88  ? 0.1345 0.5206 0.1960 0.0059  0.0405  0.0027  85  ASN   A OD1   
602  N  ND2   . ASN   A 88  ? 0.1905 0.4932 0.2420 0.1005  -0.0122 -0.0418 85  ASN   A ND2   
603  N  N     . ASN   A 89  ? 0.1648 0.4115 0.1902 0.0191  0.0554  -0.0075 86  ASN   A N     
604  C  CA    . ASN   A 89  ? 0.1178 0.4134 0.2302 0.0287  0.0274  -0.0066 86  ASN   A CA    
605  C  C     . ASN   A 89  ? 0.1582 0.5261 0.2038 0.0216  0.0430  -0.0108 86  ASN   A C     
606  O  O     . ASN   A 89  ? 0.1532 0.4066 0.2304 0.0513  0.0484  -0.0134 86  ASN   A O     
607  C  CB    . ASN   A 89  ? 0.1618 0.4334 0.2437 0.0063  0.0330  -0.0081 86  ASN   A CB    
608  C  CG    . ASN   A 89  ? 0.2167 0.3906 0.2306 0.0878  0.0358  0.0042  86  ASN   A CG    
609  O  OD1   . ASN   A 89  ? 0.2291 0.3875 0.2046 0.0868  0.0033  -0.0247 86  ASN   A OD1   
610  N  ND2   . ASN   A 89  ? 0.1667 0.3967 0.3235 0.0600  -0.0219 0.0372  86  ASN   A ND2   
611  N  N     . THR   A 90  ? 0.1439 0.5341 0.2253 0.0956  0.0434  -0.0024 87  THR   A N     
612  C  CA    . THR   A 90  ? 0.2409 0.4850 0.1856 -0.0020 0.0501  -0.0542 87  THR   A CA    
613  C  C     . THR   A 90  ? 0.2065 0.3730 0.1824 0.0370  0.0782  -0.0175 87  THR   A C     
614  O  O     . THR   A 90  ? 0.1764 0.4008 0.2401 0.0049  0.0499  -0.0156 87  THR   A O     
615  C  CB    . THR   A 90  ? 0.2080 0.4656 0.2289 -0.0145 0.0404  0.0114  87  THR   A CB    
616  O  OG1   . THR   A 90  ? 0.3267 0.5612 0.2705 0.0754  0.0477  -0.0373 87  THR   A OG1   
617  C  CG2   . THR   A 90  ? 0.1444 0.4949 0.2695 -0.0136 0.0546  -0.0569 87  THR   A CG2   
618  N  N     . LYS   A 91  ? 0.1444 0.4027 0.2148 0.0886  0.0493  0.0205  88  LYS   A N     
619  C  CA    . LYS   A 91  ? 0.2315 0.3409 0.2200 0.1062  0.0608  -0.0448 88  LYS   A CA    
620  C  C     . LYS   A 91  ? 0.1827 0.3046 0.2189 0.0458  0.0114  -0.0530 88  LYS   A C     
621  O  O     . LYS   A 91  ? 0.1771 0.2706 0.1909 0.0417  0.0312  -0.0165 88  LYS   A O     
622  C  CB    . LYS   A 91  ? 0.2293 0.3539 0.2839 0.0898  0.0834  0.0060  88  LYS   A CB    
623  C  CG    . LYS   A 91  ? 0.2741 0.3397 0.3925 0.1267  0.0158  -0.0444 88  LYS   A CG    
624  C  CD    . LYS   A 91  ? 0.2450 0.3196 0.5340 0.0881  -0.0250 -0.0228 88  LYS   A CD    
625  C  CE    . LYS   A 91  ? 0.3786 0.3859 0.5574 0.0341  -0.0373 -0.0249 88  LYS   A CE    
626  N  NZ    . LYS   A 91  ? 0.4324 0.3848 0.5587 0.0089  0.0277  0.0518  88  LYS   A NZ    
627  N  N     . SER   A 92  ? 0.1627 0.3461 0.1831 0.0730  0.0272  -0.0036 89  SER   A N     
628  C  CA    . SER   A 92  ? 0.1530 0.2788 0.2184 0.0553  0.0305  -0.0184 89  SER   A CA    
629  C  C     . SER   A 92  ? 0.1867 0.2843 0.1491 -0.0021 -0.0111 -0.0139 89  SER   A C     
630  O  O     . SER   A 92  ? 0.1461 0.2485 0.2036 0.0149  0.0130  -0.0198 89  SER   A O     
631  C  CB    . SER   A 92  ? 0.1086 0.3140 0.1744 0.0277  0.0718  0.0465  89  SER   A CB    
632  O  OG    . SER   A 92  ? 0.1273 0.3447 0.2156 0.0370  0.0089  -0.0130 89  SER   A OG    
633  N  N     . PHE   A 93  ? 0.1406 0.2840 0.2359 -0.0041 0.0214  -0.0675 90  PHE   A N     
634  C  CA    . PHE   A 93  ? 0.1369 0.2915 0.1979 -0.0271 0.0416  -0.0272 90  PHE   A CA    
635  C  C     . PHE   A 93  ? 0.1840 0.2728 0.2249 -0.0125 0.0347  -0.0520 90  PHE   A C     
636  O  O     . PHE   A 93  ? 0.1530 0.2330 0.2161 -0.0078 0.0572  -0.0093 90  PHE   A O     
637  C  CB    . PHE   A 93  ? 0.1299 0.2680 0.1890 -0.0282 0.0616  -0.0600 90  PHE   A CB    
638  C  CG    . PHE   A 93  ? 0.1714 0.2843 0.2210 -0.0704 0.0551  -0.0206 90  PHE   A CG    
639  C  CD1   . PHE   A 93  ? 0.1678 0.3401 0.1723 -0.0423 0.0361  -0.0319 90  PHE   A CD1   
640  C  CD2   . PHE   A 93  ? 0.1935 0.3351 0.2128 -0.0763 0.0496  -0.0354 90  PHE   A CD2   
641  C  CE1   . PHE   A 93  ? 0.1430 0.3506 0.2594 -0.0681 0.0513  0.0107  90  PHE   A CE1   
642  C  CE2   . PHE   A 93  ? 0.2188 0.2993 0.1984 -0.0541 0.0775  -0.0351 90  PHE   A CE2   
643  C  CZ    . PHE   A 93  ? 0.1925 0.3996 0.2253 0.0012  0.0449  -0.0521 90  PHE   A CZ    
644  N  N     . GLU   A 94  ? 0.1928 0.3234 0.2074 0.0550  0.0142  -0.0240 91  GLU   A N     
645  C  CA    . GLU   A 94  ? 0.2006 0.2987 0.2191 0.0151  0.0361  -0.0413 91  GLU   A CA    
646  C  C     . GLU   A 94  ? 0.1820 0.2860 0.2209 0.0427  0.0210  -0.0328 91  GLU   A C     
647  O  O     . GLU   A 94  ? 0.2172 0.2941 0.2062 -0.0084 0.0383  -0.0490 91  GLU   A O     
648  C  CB    . GLU   A 94  ? 0.1984 0.3513 0.1723 0.0096  0.0575  -0.0530 91  GLU   A CB    
649  C  CG    . GLU   A 94  ? 0.2749 0.4261 0.2276 -0.0432 0.1108  -0.0007 91  GLU   A CG    
650  C  CD    . GLU   A 94  ? 0.2905 0.3691 0.2755 -0.0010 0.1583  -0.0154 91  GLU   A CD    
651  O  OE1   . GLU   A 94  ? 0.3379 0.5112 0.3440 -0.0061 0.1032  0.0495  91  GLU   A OE1   
652  O  OE2   . GLU   A 94  ? 0.5125 0.4237 0.5565 -0.0130 0.1580  -0.0081 91  GLU   A OE2   
653  N  N     . ASP   A 95  ? 0.1811 0.2365 0.2060 0.0332  -0.0031 -0.0526 92  ASP   A N     
654  C  CA    . ASP   A 95  ? 0.1915 0.2735 0.2137 0.0340  0.0199  -0.0434 92  ASP   A CA    
655  C  C     . ASP   A 95  ? 0.2026 0.2506 0.2028 0.0606  -0.0086 -0.0268 92  ASP   A C     
656  O  O     . ASP   A 95  ? 0.1778 0.3121 0.1623 0.0425  0.0136  0.0307  92  ASP   A O     
657  C  CB    . ASP   A 95  ? 0.1739 0.2832 0.3459 0.0269  0.0041  0.0314  92  ASP   A CB    
658  C  CG    . ASP   A 95  ? 0.2429 0.3202 0.4206 0.0765  0.0100  0.0306  92  ASP   A CG    
659  O  OD1   . ASP   A 95  ? 0.2682 0.2645 0.4671 0.0033  0.0271  -0.0225 92  ASP   A OD1   
660  O  OD2   . ASP   A 95  ? 0.2594 0.2780 0.5443 0.0002  -0.0308 0.1117  92  ASP   A OD2   
661  N  N     . ILE   A 96  ? 0.1500 0.2470 0.1938 -0.0074 0.0220  0.0371  93  ILE   A N     
662  C  CA    . ILE   A 96  ? 0.1555 0.2707 0.1956 0.0211  0.0449  0.0065  93  ILE   A CA    
663  C  C     . ILE   A 96  ? 0.1843 0.2102 0.2031 0.0388  0.0245  -0.0106 93  ILE   A C     
664  O  O     . ILE   A 96  ? 0.1613 0.2228 0.2065 -0.0074 0.0217  0.0029  93  ILE   A O     
665  C  CB    . ILE   A 96  ? 0.1823 0.2427 0.1961 0.0138  0.0093  0.0277  93  ILE   A CB    
666  C  CG1   . ILE   A 96  ? 0.1753 0.2795 0.1880 0.0714  0.0131  0.0260  93  ILE   A CG1   
667  C  CG2   . ILE   A 96  ? 0.1918 0.2676 0.2179 0.0044  -0.0082 -0.0134 93  ILE   A CG2   
668  C  CD1   . ILE   A 96  ? 0.1544 0.3022 0.2368 0.0405  0.0531  -0.0222 93  ILE   A CD1   
669  N  N     . HIS   A 97  ? 0.1634 0.2049 0.2099 0.0113  0.0364  0.0175  94  HIS   A N     
670  C  CA    . HIS   A 97  ? 0.1893 0.1940 0.1784 0.0472  0.0337  0.0179  94  HIS   A CA    
671  C  C     . HIS   A 97  ? 0.2127 0.2562 0.1889 -0.0005 0.0277  0.0189  94  HIS   A C     
672  O  O     . HIS   A 97  ? 0.1856 0.2239 0.2032 0.0034  0.0461  -0.0132 94  HIS   A O     
673  C  CB    . HIS   A 97  ? 0.1227 0.2634 0.2187 0.0248  0.0356  -0.0119 94  HIS   A CB    
674  C  CG    . HIS   A 97  ? 0.1380 0.3104 0.2298 -0.0004 0.0504  -0.0260 94  HIS   A CG    
675  N  ND1   . HIS   A 97  ? 0.1154 0.3569 0.2443 -0.0255 0.0519  -0.0269 94  HIS   A ND1   
676  C  CD2   . HIS   A 97  ? 0.1919 0.3389 0.1764 -0.0527 0.0545  -0.0209 94  HIS   A CD2   
677  C  CE1   . HIS   A 97  ? 0.1662 0.3764 0.2064 0.0069  0.0518  -0.0147 94  HIS   A CE1   
678  N  NE2   . HIS   A 97  ? 0.1428 0.3158 0.2626 -0.0583 0.0252  -0.0411 94  HIS   A NE2   
679  N  N     . HIS   A 98  ? 0.1796 0.2205 0.2143 0.0010  0.0309  -0.0228 95  HIS   A N     
680  C  CA    . HIS   A 98  ? 0.2142 0.2060 0.2222 -0.0159 0.0487  -0.0304 95  HIS   A CA    
681  C  C     . HIS   A 98  ? 0.1863 0.2267 0.2393 0.0156  0.0318  -0.0137 95  HIS   A C     
682  O  O     . HIS   A 98  ? 0.2206 0.2051 0.1976 0.0067  0.0238  -0.0162 95  HIS   A O     
683  C  CB    . HIS   A 98  ? 0.2170 0.2045 0.2536 -0.0149 0.0290  -0.0201 95  HIS   A CB    
684  C  CG    . HIS   A 98  ? 0.2779 0.2929 0.3053 -0.0245 0.0849  -0.0115 95  HIS   A CG    
685  N  ND1   . HIS   A 98  ? 0.3727 0.3521 0.4767 -0.0742 0.1327  -0.1021 95  HIS   A ND1   
686  C  CD2   . HIS   A 98  ? 0.2443 0.3161 0.2360 0.0353  0.1018  0.0525  95  HIS   A CD2   
687  C  CE1   . HIS   A 98  ? 0.3568 0.3815 0.4733 -0.0505 0.1491  -0.0460 95  HIS   A CE1   
688  N  NE2   . HIS   A 98  ? 0.2489 0.2639 0.3184 0.0273  0.1098  0.0161  95  HIS   A NE2   
689  N  N     . TYR   A 99  ? 0.1488 0.2074 0.2400 -0.0426 0.0428  -0.0013 96  TYR   A N     
690  C  CA    . TYR   A 99  ? 0.1632 0.2336 0.2168 -0.0158 0.0427  -0.0072 96  TYR   A CA    
691  C  C     . TYR   A 99  ? 0.1800 0.2415 0.2442 -0.0248 -0.0033 -0.0059 96  TYR   A C     
692  O  O     . TYR   A 99  ? 0.1704 0.3091 0.2315 -0.0436 0.0444  -0.0296 96  TYR   A O     
693  C  CB    . TYR   A 99  ? 0.2083 0.2492 0.1933 -0.0602 0.0549  -0.0035 96  TYR   A CB    
694  C  CG    . TYR   A 99  ? 0.2334 0.3060 0.1912 -0.0519 0.0495  0.0204  96  TYR   A CG    
695  C  CD1   . TYR   A 99  ? 0.2550 0.2718 0.2351 -0.0357 0.0897  0.0028  96  TYR   A CD1   
696  C  CD2   . TYR   A 99  ? 0.2508 0.2466 0.2340 -0.0815 0.0218  -0.0121 96  TYR   A CD2   
697  C  CE1   . TYR   A 99  ? 0.2487 0.2958 0.2422 -0.0356 0.0630  -0.0166 96  TYR   A CE1   
698  C  CE2   . TYR   A 99  ? 0.2650 0.2965 0.2412 -0.0238 0.0729  0.0050  96  TYR   A CE2   
699  C  CZ    . TYR   A 99  ? 0.2463 0.2685 0.2118 -0.0438 -0.0075 0.0083  96  TYR   A CZ    
700  O  OH    . TYR   A 99  ? 0.2916 0.2896 0.2993 -0.0268 -0.0550 0.0278  96  TYR   A OH    
701  N  N     . ARG   A 100 ? 0.1573 0.2164 0.2062 -0.0080 0.0277  -0.0361 97  ARG   A N     
702  C  CA    . ARG   A 100 ? 0.1644 0.2517 0.2149 0.0010  0.0419  0.0016  97  ARG   A CA    
703  C  C     . ARG   A 100 ? 0.1484 0.2795 0.1805 0.0150  0.0265  -0.0142 97  ARG   A C     
704  O  O     . ARG   A 100 ? 0.1407 0.2788 0.2453 0.0216  0.0321  -0.0112 97  ARG   A O     
705  C  CB    . ARG   A 100 ? 0.2063 0.2124 0.2264 -0.0011 0.0184  -0.0027 97  ARG   A CB    
706  C  CG    . ARG   A 100 ? 0.2277 0.2256 0.2731 0.0137  0.0079  0.0032  97  ARG   A CG    
707  C  CD    . ARG   A 100 ? 0.2203 0.2958 0.3410 -0.0637 -0.0675 0.0311  97  ARG   A CD    
708  N  NE    . ARG   A 100 ? 0.2559 0.3630 0.3538 -0.0472 -0.0591 0.0663  97  ARG   A NE    
709  C  CZ    . ARG   A 100 ? 0.3737 0.4058 0.4311 0.0319  -0.0108 -0.0168 97  ARG   A CZ    
710  N  NH1   . ARG   A 100 ? 0.3437 0.3067 0.2488 -0.0423 0.0495  -0.0085 97  ARG   A NH1   
711  N  NH2   . ARG   A 100 ? 0.5034 0.3667 0.5188 -0.0095 -0.0436 0.0749  97  ARG   A NH2   
712  N  N     . GLU   A 101 ? 0.1770 0.2841 0.1862 0.0060  0.0435  -0.0218 98  GLU   A N     
713  C  CA    . GLU   A 101 ? 0.1530 0.3104 0.2553 -0.0424 0.0294  -0.0433 98  GLU   A CA    
714  C  C     . GLU   A 101 ? 0.2072 0.2392 0.2601 -0.0254 0.0173  -0.0430 98  GLU   A C     
715  O  O     . GLU   A 101 ? 0.1961 0.2858 0.2483 -0.0483 0.0389  -0.0376 98  GLU   A O     
716  C  CB    . GLU   A 101 ? 0.1643 0.2913 0.2881 -0.0394 0.0502  -0.0429 98  GLU   A CB    
717  C  CG    . GLU   A 101 ? 0.1896 0.3699 0.3157 -0.0549 0.0465  -0.0706 98  GLU   A CG    
718  C  CD    . GLU   A 101 ? 0.1614 0.4047 0.4346 -0.0543 0.0907  -0.0580 98  GLU   A CD    
719  O  OE1   . GLU   A 101 ? 0.1846 0.2976 0.2690 -0.0461 0.0825  -0.0331 98  GLU   A OE1   
720  O  OE2   . GLU   A 101 ? 0.3950 0.4367 0.3979 0.0150  0.0751  -0.0766 98  GLU   A OE2   
721  N  N     . GLN   A 102 ? 0.1818 0.2619 0.2365 -0.0375 0.0517  -0.0573 99  GLN   A N     
722  C  CA    . GLN   A 102 ? 0.1840 0.2651 0.2683 -0.0239 0.0272  -0.0196 99  GLN   A CA    
723  C  C     . GLN   A 102 ? 0.1824 0.2470 0.3298 -0.0464 0.0654  -0.0377 99  GLN   A C     
724  O  O     . GLN   A 102 ? 0.2005 0.2733 0.2396 -0.0616 0.0509  -0.0251 99  GLN   A O     
725  C  CB    . GLN   A 102 ? 0.1614 0.2059 0.3078 -0.0030 0.0514  0.0258  99  GLN   A CB    
726  C  CG    . GLN   A 102 ? 0.2569 0.2177 0.3818 0.0402  0.0866  0.0057  99  GLN   A CG    
727  C  CD    . GLN   A 102 ? 0.3299 0.2185 0.3979 -0.0008 0.0505  -0.0063 99  GLN   A CD    
728  O  OE1   . GLN   A 102 ? 0.3052 0.4487 0.3965 0.0430  0.0469  -0.0063 99  GLN   A OE1   
729  N  NE2   . GLN   A 102 ? 0.4440 0.4431 0.5431 0.1136  0.1098  -0.0949 99  GLN   A NE2   
730  N  N     . ILE   A 103 ? 0.0951 0.2458 0.2401 -0.0132 0.0149  -0.0031 100 ILE   A N     
731  C  CA    . ILE   A 103 ? 0.1150 0.2965 0.2689 -0.0271 0.0643  -0.0168 100 ILE   A CA    
732  C  C     . ILE   A 103 ? 0.2076 0.2539 0.2680 -0.0017 0.0172  -0.0501 100 ILE   A C     
733  O  O     . ILE   A 103 ? 0.1872 0.2992 0.2527 0.0252  0.0351  0.0001  100 ILE   A O     
734  C  CB    . ILE   A 103 ? 0.0982 0.2752 0.2599 -0.0055 0.0216  -0.0033 100 ILE   A CB    
735  C  CG1   . ILE   A 103 ? 0.2046 0.2962 0.1884 -0.0338 0.0352  0.0062  100 ILE   A CG1   
736  C  CG2   . ILE   A 103 ? 0.1680 0.3104 0.2397 0.0398  0.0242  -0.0325 100 ILE   A CG2   
737  C  CD1   . ILE   A 103 ? 0.2072 0.2147 0.1808 -0.0170 0.0345  0.0192  100 ILE   A CD1   
738  N  N     . LYS   A 104 ? 0.1769 0.2903 0.3067 -0.0087 0.0138  -0.0192 101 LYS   A N     
739  C  CA    . LYS   A 104 ? 0.2389 0.3080 0.2922 -0.0430 0.0176  0.0154  101 LYS   A CA    
740  C  C     . LYS   A 104 ? 0.2232 0.2902 0.2628 -0.0452 0.0052  0.0360  101 LYS   A C     
741  O  O     . LYS   A 104 ? 0.2354 0.3408 0.2704 -0.0300 -0.0451 -0.0297 101 LYS   A O     
742  C  CB    . LYS   A 104 ? 0.2624 0.2959 0.2494 -0.0826 -0.0304 0.0127  101 LYS   A CB    
743  C  CG    . LYS   A 104 ? 0.2535 0.2877 0.3129 -0.0105 -0.0231 0.0028  101 LYS   A CG    
744  C  CD    . LYS   A 104 ? 0.3504 0.4011 0.3812 -0.0339 0.0101  0.1054  101 LYS   A CD    
745  C  CE    . LYS   A 104 ? 0.5327 0.5963 0.3615 -0.0358 -0.0227 0.0404  101 LYS   A CE    
746  N  NZ    . LYS   A 104 ? 0.5399 0.5636 0.3956 0.0128  -0.0380 -0.0321 101 LYS   A NZ    
747  N  N     . ARG   A 105 ? 0.1915 0.2812 0.2601 -0.0538 0.0294  -0.0105 102 ARG   A N     
748  C  CA    . ARG   A 105 ? 0.2499 0.3421 0.2659 -0.0629 -0.0205 -0.0578 102 ARG   A CA    
749  C  C     . ARG   A 105 ? 0.3028 0.3127 0.2428 -0.0940 -0.0219 -0.0411 102 ARG   A C     
750  O  O     . ARG   A 105 ? 0.2556 0.3969 0.2781 -0.0642 -0.0099 -0.0604 102 ARG   A O     
751  C  CB    . ARG   A 105 ? 0.2736 0.3439 0.3006 -0.0608 0.0221  -0.0275 102 ARG   A CB    
752  C  CG    . ARG   A 105 ? 0.3629 0.3383 0.3917 -0.0255 0.0102  -0.0625 102 ARG   A CG    
753  C  CD    . ARG   A 105 ? 0.4157 0.4015 0.4804 0.0298  0.0144  -0.0229 102 ARG   A CD    
754  N  NE    . ARG   A 105 ? 0.4974 0.6417 0.5771 -0.1462 0.0001  0.0386  102 ARG   A NE    
755  C  CZ    . ARG   A 105 ? 0.4975 0.5768 0.4362 -0.1075 -0.0284 0.0029  102 ARG   A CZ    
756  N  NH1   . ARG   A 105 ? 0.4723 0.5074 0.4705 -0.1022 -0.0117 0.0346  102 ARG   A NH1   
757  N  NH2   . ARG   A 105 ? 0.5498 0.6348 0.4664 -0.0436 -0.0379 -0.0296 102 ARG   A NH2   
758  N  N     . VAL   A 106 ? 0.2684 0.3327 0.2621 -0.0924 -0.0138 -0.0283 103 VAL   A N     
759  C  CA    . VAL   A 106 ? 0.2753 0.2160 0.2795 -0.0923 -0.0154 -0.0250 103 VAL   A CA    
760  C  C     . VAL   A 106 ? 0.2364 0.3446 0.3353 -0.0936 -0.0265 -0.0330 103 VAL   A C     
761  O  O     . VAL   A 106 ? 0.2460 0.4484 0.3078 -0.1338 0.0110  -0.0513 103 VAL   A O     
762  C  CB    . VAL   A 106 ? 0.2696 0.2642 0.2686 -0.0675 0.0043  0.0518  103 VAL   A CB    
763  C  CG1   . VAL   A 106 ? 0.2873 0.3012 0.2876 -0.1125 0.0153  -0.0335 103 VAL   A CG1   
764  C  CG2   . VAL   A 106 ? 0.3446 0.2591 0.2871 -0.0445 -0.0436 0.0044  103 VAL   A CG2   
765  N  N     . LYS   A 107 ? 0.1829 0.3352 0.2833 -0.0193 -0.0042 -0.0353 104 LYS   A N     
766  C  CA    . LYS   A 107 ? 0.2088 0.3913 0.3591 0.0271  0.0090  -0.0558 104 LYS   A CA    
767  C  C     . LYS   A 107 ? 0.1682 0.4569 0.3665 0.0348  0.0220  -0.0594 104 LYS   A C     
768  O  O     . LYS   A 107 ? 0.2341 0.4509 0.4099 0.0654  -0.0528 -0.1093 104 LYS   A O     
769  C  CB    . LYS   A 107 ? 0.2270 0.4391 0.4098 0.0204  -0.0254 -0.0801 104 LYS   A CB    
770  C  CG    . LYS   A 107 ? 0.3103 0.4233 0.3939 -0.0371 -0.0211 -0.0584 104 LYS   A CG    
771  C  CD    . LYS   A 107 ? 0.2665 0.3687 0.4303 -0.0161 0.0112  -0.0557 104 LYS   A CD    
772  C  CE    . LYS   A 107 ? 0.2835 0.2949 0.2435 -0.0285 -0.0148 -0.0512 104 LYS   A CE    
773  N  NZ    . LYS   A 107 ? 0.2800 0.4271 0.2448 -0.0315 0.0197  -0.0112 104 LYS   A NZ    
774  N  N     . ASP   A 108 ? 0.2585 0.4726 0.3018 0.0320  -0.0002 -0.0697 105 ASP   A N     
775  C  CA    . ASP   A 108 ? 0.2351 0.4420 0.3148 -0.0348 -0.0212 -0.0472 105 ASP   A CA    
776  C  C     . ASP   A 108 ? 0.2684 0.4785 0.3768 0.0042  -0.0553 -0.0257 105 ASP   A C     
777  O  O     . ASP   A 108 ? 0.3387 0.5136 0.4429 0.0414  -0.1095 0.0043  105 ASP   A O     
778  C  CB    . ASP   A 108 ? 0.2573 0.5176 0.4063 -0.0490 -0.0757 -0.0434 105 ASP   A CB    
779  C  CG    . ASP   A 108 ? 0.3549 0.5946 0.3765 0.0108  -0.0126 -0.0598 105 ASP   A CG    
780  O  OD1   . ASP   A 108 ? 0.4213 0.7026 0.3925 -0.0308 0.0480  -0.0498 105 ASP   A OD1   
781  O  OD2   . ASP   A 108 ? 0.4253 0.4856 0.5029 -0.0005 -0.1399 -0.0514 105 ASP   A OD2   
782  N  N     . SER   A 109 ? 0.2945 0.4513 0.3478 -0.0075 -0.0853 0.0130  106 SER   A N     
783  C  CA    . SER   A 109 ? 0.4244 0.4591 0.3010 -0.0100 -0.0787 -0.0458 106 SER   A CA    
784  C  C     . SER   A 109 ? 0.3846 0.4881 0.3131 0.0511  0.0148  0.0594  106 SER   A C     
785  O  O     . SER   A 109 ? 0.3151 0.4677 0.3761 0.0530  0.0130  0.0162  106 SER   A O     
786  C  CB    . SER   A 109 ? 0.4302 0.4283 0.4529 0.0111  0.0182  -0.0608 106 SER   A CB    
787  O  OG    . SER   A 109 ? 0.4153 0.4259 0.4959 0.0249  0.0120  -0.0134 106 SER   A OG    
788  N  N     . GLU   A 110 ? 0.4767 0.4370 0.4314 -0.0136 -0.0444 0.0706  107 GLU   A N     
789  C  CA    . GLU   A 110 ? 0.5122 0.4991 0.4607 -0.0259 0.0124  0.0422  107 GLU   A CA    
790  C  C     . GLU   A 110 ? 0.3454 0.6066 0.5107 -0.0186 0.0326  -0.0194 107 GLU   A C     
791  O  O     . GLU   A 110 ? 0.5150 0.5562 0.4201 -0.1147 -0.0430 0.0535  107 GLU   A O     
792  C  CB    . GLU   A 110 ? 0.6020 0.4661 0.5366 -0.0406 0.0027  0.0437  107 GLU   A CB    
793  C  CG    . GLU   A 110 ? 0.6150 0.4492 0.5650 0.0114  0.0428  -0.0036 107 GLU   A CG    
794  C  CD    . GLU   A 110 ? 0.4937 0.5211 0.8401 -0.0056 0.0195  0.0016  107 GLU   A CD    
795  O  OE1   . GLU   A 110 ? 0.5820 0.6774 0.8922 -0.1175 0.0169  -0.0628 107 GLU   A OE1   
796  O  OE2   . GLU   A 110 ? 0.8198 0.6245 1.0409 -0.1156 0.0499  -0.0696 107 GLU   A OE2   
797  N  N     . ASP   A 111 ? 0.3957 0.5250 0.4138 -0.0275 0.0903  0.0118  108 ASP   A N     
798  C  CA    . ASP   A 111 ? 0.4596 0.4662 0.3785 0.0429  0.0133  0.0443  108 ASP   A CA    
799  C  C     . ASP   A 111 ? 0.2836 0.5310 0.3264 -0.0146 -0.0136 0.0088  108 ASP   A C     
800  O  O     . ASP   A 111 ? 0.2854 0.3945 0.5246 -0.0342 -0.1238 -0.0033 108 ASP   A O     
801  C  CB    . ASP   A 111 ? 0.5673 0.5374 0.4086 0.0923  -0.0738 0.0140  108 ASP   A CB    
802  C  CG    . ASP   A 111 ? 0.5115 0.4818 0.6007 0.0490  -0.0784 0.0210  108 ASP   A CG    
803  O  OD1   . ASP   A 111 ? 0.5941 0.7510 0.6554 -0.1515 -0.0794 0.0522  108 ASP   A OD1   
804  O  OD2   . ASP   A 111 ? 0.4865 0.4990 0.6967 -0.0110 -0.0929 0.1439  108 ASP   A OD2   
805  N  N     . VAL   A 112 ? 0.2456 0.4769 0.2435 -0.0251 -0.0036 -0.0240 109 VAL   A N     
806  C  CA    . VAL   A 112 ? 0.1849 0.3312 0.2665 -0.0120 0.0478  0.0103  109 VAL   A CA    
807  C  C     . VAL   A 112 ? 0.2733 0.2113 0.2712 0.0030  0.0360  0.0232  109 VAL   A C     
808  O  O     . VAL   A 112 ? 0.2465 0.2702 0.1977 0.0564  0.0152  0.0172  109 VAL   A O     
809  C  CB    . VAL   A 112 ? 0.1998 0.3367 0.2583 0.0254  -0.0079 -0.0277 109 VAL   A CB    
810  C  CG1   . VAL   A 112 ? 0.1812 0.2261 0.2988 0.0426  -0.0365 0.0269  109 VAL   A CG1   
811  C  CG2   . VAL   A 112 ? 0.3009 0.3015 0.2825 0.0599  0.0023  -0.0405 109 VAL   A CG2   
812  N  N     . PRO   A 113 ? 0.1397 0.2594 0.2692 0.0294  0.0050  0.0271  110 PRO   A N     
813  C  CA    . PRO   A 113 ? 0.1955 0.2524 0.2377 0.0453  0.0410  -0.0078 110 PRO   A CA    
814  C  C     . PRO   A 113 ? 0.1903 0.2642 0.2814 0.0170  0.0191  -0.0372 110 PRO   A C     
815  O  O     . PRO   A 113 ? 0.1307 0.2866 0.2402 0.0440  0.0178  -0.0006 110 PRO   A O     
816  C  CB    . PRO   A 113 ? 0.1778 0.2676 0.1931 0.0601  0.0127  0.0089  110 PRO   A CB    
817  C  CG    . PRO   A 113 ? 0.1684 0.3450 0.2789 0.0785  -0.0099 0.0085  110 PRO   A CG    
818  C  CD    . PRO   A 113 ? 0.1497 0.2905 0.2771 -0.0153 -0.0005 0.0241  110 PRO   A CD    
819  N  N     . MET   A 114 ? 0.2078 0.1910 0.1836 0.0219  0.0039  0.0397  111 MET   A N     
820  C  CA    . MET   A 114 ? 0.1687 0.2587 0.2155 0.0228  0.0303  0.0156  111 MET   A CA    
821  C  C     . MET   A 114 ? 0.2109 0.2699 0.2435 0.0222  0.0465  -0.0214 111 MET   A C     
822  O  O     . MET   A 114 ? 0.1567 0.2573 0.2044 0.0146  0.0516  -0.0343 111 MET   A O     
823  C  CB    . MET   A 114 ? 0.2761 0.2889 0.1759 -0.0494 0.0365  -0.0250 111 MET   A CB    
824  C  CG    . MET   A 114 ? 0.2431 0.2413 0.1968 0.0015  0.0241  -0.0027 111 MET   A CG    
825  S  SD    . MET   A 114 ? 0.3795 0.3814 0.2376 0.1355  0.0600  -0.0413 111 MET   A SD    
826  C  CE    . MET   A 114 ? 0.4472 0.3242 0.3278 0.0949  0.0891  -0.0503 111 MET   A CE    
827  N  N     . VAL   A 115 ? 0.1780 0.2004 0.1884 0.0073  0.0647  -0.0202 112 VAL   A N     
828  C  CA    . VAL   A 115 ? 0.1975 0.1895 0.1707 -0.0130 0.0269  0.0464  112 VAL   A CA    
829  C  C     . VAL   A 115 ? 0.1668 0.2173 0.2112 -0.0158 0.0222  0.0037  112 VAL   A C     
830  O  O     . VAL   A 115 ? 0.1658 0.2345 0.1770 0.0051  0.0548  -0.0159 112 VAL   A O     
831  C  CB    . VAL   A 115 ? 0.2139 0.2094 0.1803 -0.0113 0.0290  0.0197  112 VAL   A CB    
832  C  CG1   . VAL   A 115 ? 0.2431 0.2503 0.1914 -0.0268 0.0407  0.0037  112 VAL   A CG1   
833  C  CG2   . VAL   A 115 ? 0.2188 0.2643 0.1550 0.0094  0.0388  0.0028  112 VAL   A CG2   
834  N  N     . LEU   A 116 ? 0.1954 0.1754 0.1978 0.0272  0.0408  0.0379  113 LEU   A N     
835  C  CA    . LEU   A 116 ? 0.2032 0.1728 0.1900 0.0240  0.0211  0.0184  113 LEU   A CA    
836  C  C     . LEU   A 116 ? 0.1785 0.2531 0.2081 -0.0240 0.0759  -0.0311 113 LEU   A C     
837  O  O     . LEU   A 116 ? 0.1715 0.2334 0.1898 0.0001  0.0568  -0.0021 113 LEU   A O     
838  C  CB    . LEU   A 116 ? 0.1754 0.2576 0.1562 0.0189  -0.0026 -0.0018 113 LEU   A CB    
839  C  CG    . LEU   A 116 ? 0.1732 0.2087 0.1779 0.0064  0.0126  -0.0228 113 LEU   A CG    
840  C  CD1   . LEU   A 116 ? 0.1951 0.2058 0.2051 -0.0228 0.0459  -0.0037 113 LEU   A CD1   
841  C  CD2   . LEU   A 116 ? 0.1591 0.2824 0.2057 -0.0076 0.0229  -0.0159 113 LEU   A CD2   
842  N  N     . VAL   A 117 ? 0.1507 0.2215 0.1971 -0.0419 0.0552  -0.0458 114 VAL   A N     
843  C  CA    . VAL   A 117 ? 0.1931 0.1776 0.1784 -0.0088 0.0195  -0.0087 114 VAL   A CA    
844  C  C     . VAL   A 117 ? 0.1670 0.3265 0.1924 0.0013  0.0000  -0.0018 114 VAL   A C     
845  O  O     . VAL   A 117 ? 0.1662 0.3182 0.1723 -0.0813 0.0288  0.0149  114 VAL   A O     
846  C  CB    . VAL   A 117 ? 0.1758 0.2212 0.2203 -0.0113 0.0486  -0.0016 114 VAL   A CB    
847  C  CG1   . VAL   A 117 ? 0.2129 0.2617 0.1831 -0.0174 0.0414  -0.0144 114 VAL   A CG1   
848  C  CG2   . VAL   A 117 ? 0.1730 0.1698 0.2336 -0.0078 0.0501  0.0002  114 VAL   A CG2   
849  N  N     . GLY   A 118 ? 0.1737 0.3194 0.1792 -0.0279 0.0451  -0.0346 115 GLY   A N     
850  C  CA    . GLY   A 118 ? 0.1659 0.2480 0.2077 -0.0077 0.0732  -0.0298 115 GLY   A CA    
851  C  C     . GLY   A 118 ? 0.1535 0.3106 0.1968 -0.0333 0.1009  -0.0625 115 GLY   A C     
852  O  O     . GLY   A 118 ? 0.1935 0.2931 0.2293 -0.0538 0.0346  -0.0802 115 GLY   A O     
853  N  N     . ASN   A 119 ? 0.1503 0.3064 0.1797 -0.0734 0.0354  -0.0498 116 ASN   A N     
854  C  CA    . ASN   A 119 ? 0.1861 0.3263 0.1704 -0.1324 0.0303  -0.0479 116 ASN   A CA    
855  C  C     . ASN   A 119 ? 0.1675 0.3799 0.1933 -0.1487 0.0515  -0.0306 116 ASN   A C     
856  O  O     . ASN   A 119 ? 0.1795 0.3916 0.1888 -0.1134 0.0539  -0.0532 116 ASN   A O     
857  C  CB    . ASN   A 119 ? 0.1536 0.3035 0.1843 -0.1006 0.0404  -0.0199 116 ASN   A CB    
858  C  CG    . ASN   A 119 ? 0.1396 0.3378 0.2045 -0.0855 -0.0066 -0.0381 116 ASN   A CG    
859  O  OD1   . ASN   A 119 ? 0.1880 0.3034 0.1882 -0.0957 0.0318  -0.0117 116 ASN   A OD1   
860  N  ND2   . ASN   A 119 ? 0.0805 0.3961 0.2070 -0.0376 0.0255  -0.0246 116 ASN   A ND2   
861  N  N     . LYS   A 120 ? 0.1833 0.3707 0.1546 -0.0238 0.0510  -0.0355 117 LYS   A N     
862  C  CA    . LYS   A 120 ? 0.2114 0.4062 0.2105 -0.0396 -0.0328 -0.0425 117 LYS   A CA    
863  C  C     . LYS   A 120 ? 0.1933 0.4469 0.2017 -0.0571 -0.0291 0.0044  117 LYS   A C     
864  O  O     . LYS   A 120 ? 0.1890 0.4406 0.2074 -0.1216 0.0382  -0.0763 117 LYS   A O     
865  C  CB    . LYS   A 120 ? 0.1877 0.3551 0.2032 -0.0693 0.0145  -0.0348 117 LYS   A CB    
866  C  CG    . LYS   A 120 ? 0.2028 0.3390 0.1391 -0.0439 0.0068  -0.0270 117 LYS   A CG    
867  C  CD    . LYS   A 120 ? 0.1925 0.4027 0.1912 0.0000  0.0227  -0.0373 117 LYS   A CD    
868  C  CE    . LYS   A 120 ? 0.1848 0.3904 0.1799 -0.0038 0.0189  -0.0550 117 LYS   A CE    
869  N  NZ    . LYS   A 120 ? 0.2043 0.4015 0.2774 -0.0223 0.0325  -0.0180 117 LYS   A NZ    
870  N  N     . SER   A 121 ? 0.2491 0.3988 0.1901 -0.0576 0.0170  0.0148  118 SER   A N     
871  C  CA    . SER   A 121 ? 0.2551 0.3882 0.1756 -0.0794 0.0539  -0.0320 118 SER   A CA    
872  C  C     . SER   A 121 ? 0.2932 0.3663 0.2066 -0.0971 0.0289  -0.0387 118 SER   A C     
873  O  O     . SER   A 121 ? 0.3016 0.4612 0.2634 -0.1353 0.0633  -0.0576 118 SER   A O     
874  C  CB    . SER   A 121 ? 0.3597 0.3973 0.2046 -0.0722 0.0523  -0.0085 118 SER   A CB    
875  O  OG    . SER   A 121 ? 0.3381 0.4345 0.2402 -0.0952 0.0664  -0.0501 118 SER   A OG    
876  N  N     . ASP   A 122 ? 0.1785 0.4172 0.2162 -0.0707 0.0158  -0.0303 119 ASP   A N     
877  C  CA    . ASP   A 122 ? 0.1933 0.5280 0.2578 -0.0877 0.0166  -0.0769 119 ASP   A CA    
878  C  C     . ASP   A 122 ? 0.2156 0.4446 0.2416 -0.0111 -0.0480 -0.0691 119 ASP   A C     
879  O  O     . ASP   A 122 ? 0.2540 0.5977 0.2750 -0.1684 -0.0234 -0.0140 119 ASP   A O     
880  C  CB    . ASP   A 122 ? 0.2832 0.5053 0.2718 -0.1120 0.0186  -0.0615 119 ASP   A CB    
881  C  CG    . ASP   A 122 ? 0.2733 0.4452 0.1496 -0.0680 -0.0430 -0.0013 119 ASP   A CG    
882  O  OD1   . ASP   A 122 ? 0.2301 0.5078 0.2158 -0.1152 -0.0124 -0.0265 119 ASP   A OD1   
883  O  OD2   . ASP   A 122 ? 0.2115 0.5485 0.2502 -0.0997 -0.0413 0.0361  119 ASP   A OD2   
884  N  N     . LEU   A 123 ? 0.2185 0.4544 0.2910 -0.0800 0.0016  -0.0912 120 LEU   A N     
885  C  CA    . LEU   A 123 ? 0.2354 0.4595 0.2655 -0.0081 -0.0360 0.0156  120 LEU   A CA    
886  C  C     . LEU   A 123 ? 0.2362 0.4500 0.4136 -0.0724 -0.0464 0.0864  120 LEU   A C     
887  O  O     . LEU   A 123 ? 0.2263 0.4368 0.4147 -0.0569 -0.0126 0.0486  120 LEU   A O     
888  C  CB    . LEU   A 123 ? 0.2613 0.4839 0.3071 -0.0822 0.0678  0.0092  120 LEU   A CB    
889  C  CG    . LEU   A 123 ? 0.2205 0.4506 0.3485 -0.0643 0.0361  0.0295  120 LEU   A CG    
890  C  CD1   . LEU   A 123 ? 0.1366 0.4698 0.3702 -0.0221 0.0553  0.0097  120 LEU   A CD1   
891  C  CD2   . LEU   A 123 ? 0.1634 0.5631 0.3757 -0.0946 0.0523  -0.0121 120 LEU   A CD2   
892  N  N     . PRO   A 124 ? 0.2450 0.5001 0.3355 -0.1173 -0.0159 0.0605  121 PRO   A N     
893  C  CA    . PRO   A 124 ? 0.2188 0.5707 0.3347 -0.1017 0.0462  0.0175  121 PRO   A CA    
894  C  C     . PRO   A 124 ? 0.1618 0.4985 0.3625 -0.1094 0.0442  0.0017  121 PRO   A C     
895  O  O     . PRO   A 124 ? 0.3608 0.5592 0.3388 -0.0781 0.1476  0.1027  121 PRO   A O     
896  C  CB    . PRO   A 124 ? 0.2089 0.4654 0.4405 -0.1245 0.0434  -0.0318 121 PRO   A CB    
897  C  CG    . PRO   A 124 ? 0.2204 0.5188 0.4092 -0.1194 0.0089  -0.0032 121 PRO   A CG    
898  C  CD    . PRO   A 124 ? 0.2038 0.4880 0.4064 -0.0855 -0.0168 0.0685  121 PRO   A CD    
899  N  N     . SER   A 125 ? 0.2645 0.5547 0.3117 -0.1513 0.0594  -0.0521 122 SER   A N     
900  C  CA    . SER   A 125 ? 0.2365 0.4890 0.3379 -0.1213 0.0828  -0.0279 122 SER   A CA    
901  C  C     . SER   A 125 ? 0.2185 0.4253 0.3402 -0.1280 0.0498  0.0281  122 SER   A C     
902  O  O     . SER   A 125 ? 0.1388 0.5428 0.4200 -0.0971 0.0711  -0.0699 122 SER   A O     
903  C  CB    . SER   A 125 ? 0.2502 0.4813 0.4142 -0.0935 0.0851  -0.0201 122 SER   A CB    
904  O  OG    . SER   A 125 ? 0.3131 0.5048 0.4053 -0.1304 0.1289  -0.0764 122 SER   A OG    
905  N  N     . ARG   A 126 ? 0.3043 0.4669 0.2657 -0.0974 0.0672  -0.0080 123 ARG   A N     
906  C  CA    . ARG   A 126 ? 0.2301 0.3910 0.2729 -0.0958 0.0620  -0.0600 123 ARG   A CA    
907  C  C     . ARG   A 126 ? 0.2062 0.4888 0.2676 -0.1186 0.0603  -0.0584 123 ARG   A C     
908  O  O     . ARG   A 126 ? 0.2074 0.4382 0.3283 -0.0833 0.0542  -0.0010 123 ARG   A O     
909  C  CB    . ARG   A 126 ? 0.2552 0.3863 0.2584 -0.1022 0.0959  -0.0684 123 ARG   A CB    
910  C  CG    . ARG   A 126 ? 0.1963 0.3712 0.2972 -0.1043 0.0715  -0.0834 123 ARG   A CG    
911  C  CD    . ARG   A 126 ? 0.2689 0.4047 0.2944 -0.1086 0.0894  -0.0520 123 ARG   A CD    
912  N  NE    . ARG   A 126 ? 0.2832 0.4438 0.3295 -0.0772 0.0606  -0.1041 123 ARG   A NE    
913  C  CZ    . ARG   A 126 ? 0.2759 0.4237 0.2533 -0.1052 0.0831  -0.0420 123 ARG   A CZ    
914  N  NH1   . ARG   A 126 ? 0.2352 0.5463 0.2701 -0.1233 0.0552  -0.0474 123 ARG   A NH1   
915  N  NH2   . ARG   A 126 ? 0.2886 0.4100 0.2766 -0.0883 0.0516  -0.0725 123 ARG   A NH2   
916  N  N     . THR   A 127 ? 0.1990 0.4709 0.2550 -0.1203 0.0717  -0.0483 124 THR   A N     
917  C  CA    . THR   A 127 ? 0.1646 0.4745 0.2450 -0.1110 0.1043  -0.0150 124 THR   A CA    
918  C  C     . THR   A 127 ? 0.2507 0.4519 0.2325 -0.0768 0.0624  -0.0653 124 THR   A C     
919  O  O     . THR   A 127 ? 0.2444 0.4336 0.2516 -0.0933 0.0660  -0.0678 124 THR   A O     
920  C  CB    . THR   A 127 ? 0.1915 0.4639 0.3061 -0.0446 0.0807  -0.0112 124 THR   A CB    
921  O  OG1   . THR   A 127 ? 0.1819 0.5939 0.3205 -0.0879 0.0948  -0.0848 124 THR   A OG1   
922  C  CG2   . THR   A 127 ? 0.2047 0.5942 0.3342 -0.0161 0.0618  -0.0185 124 THR   A CG2   
923  N  N     . VAL   A 128 ? 0.2228 0.4543 0.2469 -0.0799 0.0489  -0.0892 125 VAL   A N     
924  C  CA    . VAL   A 128 ? 0.2295 0.4071 0.1961 -0.0920 0.0829  -0.0293 125 VAL   A CA    
925  C  C     . VAL   A 128 ? 0.2506 0.4509 0.2562 -0.0872 0.0096  -0.0542 125 VAL   A C     
926  O  O     . VAL   A 128 ? 0.2428 0.4167 0.2493 -0.1144 0.0479  -0.0154 125 VAL   A O     
927  C  CB    . VAL   A 128 ? 0.1895 0.4004 0.2068 -0.0545 0.0789  -0.0315 125 VAL   A CB    
928  C  CG1   . VAL   A 128 ? 0.2470 0.4748 0.1973 -0.0825 0.0704  -0.0326 125 VAL   A CG1   
929  C  CG2   . VAL   A 128 ? 0.2158 0.3882 0.2455 -0.0841 0.0529  -0.0539 125 VAL   A CG2   
930  N  N     . ASP   A 129 ? 0.2548 0.4324 0.3522 -0.1019 0.0702  -0.0074 126 ASP   A N     
931  C  CA    . ASP   A 129 ? 0.3083 0.4214 0.3830 -0.0713 0.0730  0.0167  126 ASP   A CA    
932  C  C     . ASP   A 129 ? 0.3030 0.3200 0.3544 -0.1094 0.0590  -0.0029 126 ASP   A C     
933  O  O     . ASP   A 129 ? 0.3012 0.3442 0.2758 -0.1137 0.0378  0.0334  126 ASP   A O     
934  C  CB    . ASP   A 129 ? 0.3170 0.4827 0.4868 -0.0965 0.1284  0.0671  126 ASP   A CB    
935  C  CG    . ASP   A 129 ? 0.3330 0.6299 0.5355 -0.0913 0.0140  0.0980  126 ASP   A CG    
936  O  OD1   . ASP   A 129 ? 0.4637 0.5340 0.5641 -0.1695 -0.0490 0.1292  126 ASP   A OD1   
937  O  OD2   . ASP   A 129 ? 0.4548 0.7131 0.6297 -0.0649 0.0701  0.2184  126 ASP   A OD2   
938  N  N     . THR   A 130 ? 0.3254 0.3066 0.3048 -0.0880 -0.0018 0.0008  127 THR   A N     
939  C  CA    . THR   A 130 ? 0.2903 0.2924 0.3458 -0.1177 0.0386  0.0132  127 THR   A CA    
940  C  C     . THR   A 130 ? 0.3670 0.2942 0.2840 -0.1324 0.0651  -0.0542 127 THR   A C     
941  O  O     . THR   A 130 ? 0.3224 0.3220 0.2161 -0.1092 0.0555  -0.0270 127 THR   A O     
942  C  CB    . THR   A 130 ? 0.3547 0.3628 0.3589 -0.0917 0.0216  -0.0299 127 THR   A CB    
943  O  OG1   . THR   A 130 ? 0.3325 0.3482 0.3408 -0.1405 0.0570  -0.0311 127 THR   A OG1   
944  C  CG2   . THR   A 130 ? 0.3546 0.4129 0.2826 -0.0964 0.0374  -0.0562 127 THR   A CG2   
945  N  N     . LYS   A 131 ? 0.2996 0.3624 0.3018 -0.1440 0.0615  -0.0304 128 LYS   A N     
946  C  CA    . LYS   A 131 ? 0.3664 0.3432 0.2838 -0.1093 0.0853  0.0164  128 LYS   A CA    
947  C  C     . LYS   A 131 ? 0.3207 0.3262 0.1914 -0.0904 0.0886  0.0497  128 LYS   A C     
948  O  O     . LYS   A 131 ? 0.3041 0.3226 0.2405 -0.0969 0.0873  -0.0194 128 LYS   A O     
949  C  CB    . LYS   A 131 ? 0.3552 0.3233 0.4034 -0.1409 0.0843  0.0020  128 LYS   A CB    
950  C  CG    . LYS   A 131 ? 0.5040 0.4251 0.4586 -0.0949 0.0899  0.0622  128 LYS   A CG    
951  C  CD    . LYS   A 131 ? 0.5769 0.4766 0.4699 -0.0915 0.1404  0.1110  128 LYS   A CD    
952  C  CE    . LYS   A 131 ? 0.6970 0.5048 0.5859 -0.0323 0.1444  -0.0105 128 LYS   A CE    
953  N  NZ    . LYS   A 131 ? 0.7525 0.6413 0.6135 -0.0788 0.0946  0.0462  128 LYS   A NZ    
954  N  N     . GLN   A 132 ? 0.3275 0.2716 0.2724 -0.1299 0.0957  0.0223  129 GLN   A N     
955  C  CA    . GLN   A 132 ? 0.3241 0.2199 0.2687 -0.0836 0.0809  0.0324  129 GLN   A CA    
956  C  C     . GLN   A 132 ? 0.2921 0.3149 0.1942 -0.0757 0.0680  -0.0041 129 GLN   A C     
957  O  O     . GLN   A 132 ? 0.2315 0.3381 0.1949 -0.0366 0.0837  0.0257  129 GLN   A O     
958  C  CB    . GLN   A 132 ? 0.2695 0.3206 0.2513 -0.0484 0.0649  0.0422  129 GLN   A CB    
959  C  CG    . GLN   A 132 ? 0.3472 0.2617 0.2952 -0.0397 0.1117  0.0429  129 GLN   A CG    
960  C  CD    . GLN   A 132 ? 0.2904 0.3459 0.3342 0.0061  0.0659  -0.0345 129 GLN   A CD    
961  O  OE1   . GLN   A 132 ? 0.3242 0.4339 0.3651 -0.0108 0.0360  0.0052  129 GLN   A OE1   
962  N  NE2   . GLN   A 132 ? 0.4377 0.3932 0.3841 -0.1077 0.1895  -0.0860 129 GLN   A NE2   
963  N  N     . ALA   A 133 ? 0.2177 0.3035 0.2018 -0.0813 0.0456  -0.0440 130 ALA   A N     
964  C  CA    . ALA   A 133 ? 0.2782 0.2299 0.1996 -0.0900 0.0737  0.0012  130 ALA   A CA    
965  C  C     . ALA   A 133 ? 0.3290 0.2763 0.1411 -0.0657 0.0440  -0.0065 130 ALA   A C     
966  O  O     . ALA   A 133 ? 0.2579 0.2474 0.2195 -0.0316 0.0809  0.0182  130 ALA   A O     
967  C  CB    . ALA   A 133 ? 0.2922 0.2630 0.2054 -0.0736 0.0238  0.0125  130 ALA   A CB    
968  N  N     . GLN   A 134 ? 0.2896 0.2589 0.2001 -0.0498 0.0747  0.0082  131 GLN   A N     
969  C  CA    . GLN   A 134 ? 0.2546 0.2801 0.2113 -0.0440 0.0635  -0.0145 131 GLN   A CA    
970  C  C     . GLN   A 134 ? 0.3010 0.2563 0.2319 -0.0740 0.0529  -0.0252 131 GLN   A C     
971  O  O     . GLN   A 134 ? 0.3067 0.2500 0.2313 0.0226  0.0831  -0.0107 131 GLN   A O     
972  C  CB    . GLN   A 134 ? 0.3499 0.2773 0.1706 -0.0622 0.0392  -0.0184 131 GLN   A CB    
973  C  CG    . GLN   A 134 ? 0.3675 0.3886 0.3202 -0.0192 0.0169  0.0077  131 GLN   A CG    
974  C  CD    . GLN   A 134 ? 0.4628 0.3889 0.4122 -0.0450 0.1179  -0.0960 131 GLN   A CD    
975  O  OE1   . GLN   A 134 ? 0.4491 0.3856 0.5143 0.0004  0.0866  -0.0079 131 GLN   A OE1   
976  N  NE2   . GLN   A 134 ? 0.8181 0.3904 0.4365 -0.0277 0.0520  -0.1091 131 GLN   A NE2   
977  N  N     . ASP   A 135 ? 0.2832 0.2844 0.2544 -0.0708 0.0599  -0.0175 132 ASP   A N     
978  C  CA    . ASP   A 135 ? 0.2900 0.2388 0.2434 -0.0282 0.0551  -0.0170 132 ASP   A CA    
979  C  C     . ASP   A 135 ? 0.2400 0.2153 0.2189 0.0033  0.0906  -0.0094 132 ASP   A C     
980  O  O     . ASP   A 135 ? 0.2331 0.2255 0.2276 -0.0296 0.0880  -0.0105 132 ASP   A O     
981  C  CB    . ASP   A 135 ? 0.3150 0.2141 0.2775 -0.0534 0.0939  -0.0381 132 ASP   A CB    
982  C  CG    . ASP   A 135 ? 0.3741 0.2095 0.2222 -0.0567 0.0346  0.0307  132 ASP   A CG    
983  O  OD1   . ASP   A 135 ? 0.5198 0.2567 0.2843 -0.0008 0.0907  0.0521  132 ASP   A OD1   
984  O  OD2   . ASP   A 135 ? 0.4039 0.2895 0.2900 -0.1118 0.0584  -0.0431 132 ASP   A OD2   
985  N  N     . LEU   A 136 ? 0.2391 0.2411 0.1777 -0.0269 0.0589  0.0059  133 LEU   A N     
986  C  CA    . LEU   A 136 ? 0.2310 0.2613 0.1826 -0.0463 0.0374  -0.0043 133 LEU   A CA    
987  C  C     . LEU   A 136 ? 0.2567 0.2557 0.1983 0.0002  0.0639  -0.0082 133 LEU   A C     
988  O  O     . LEU   A 136 ? 0.2253 0.2507 0.1836 0.0385  0.0630  0.0098  133 LEU   A O     
989  C  CB    . LEU   A 136 ? 0.2072 0.2726 0.1717 -0.0066 0.0332  -0.0366 133 LEU   A CB    
990  C  CG    . LEU   A 136 ? 0.1921 0.2989 0.2123 -0.0355 0.0088  -0.0047 133 LEU   A CG    
991  C  CD1   . LEU   A 136 ? 0.2248 0.2586 0.2365 0.0088  0.0050  -0.0218 133 LEU   A CD1   
992  C  CD2   . LEU   A 136 ? 0.1772 0.2667 0.2388 -0.0562 0.0192  -0.0027 133 LEU   A CD2   
993  N  N     . ALA   A 137 ? 0.2266 0.2316 0.2025 0.0086  0.0551  0.0028  134 ALA   A N     
994  C  CA    . ALA   A 137 ? 0.2275 0.3351 0.1764 0.0071  0.0659  -0.0116 134 ALA   A CA    
995  C  C     . ALA   A 137 ? 0.2900 0.3000 0.1593 -0.0075 0.0735  -0.0040 134 ALA   A C     
996  O  O     . ALA   A 137 ? 0.2473 0.2726 0.2077 0.0251  0.0674  0.0291  134 ALA   A O     
997  C  CB    . ALA   A 137 ? 0.2563 0.2935 0.1715 0.0210  0.0630  -0.0216 134 ALA   A CB    
998  N  N     . ARG   A 138 ? 0.2755 0.2494 0.1732 0.0126  0.0749  -0.0312 135 ARG   A N     
999  C  CA    . ARG   A 138 ? 0.2769 0.2704 0.2437 0.0439  0.0946  -0.0243 135 ARG   A CA    
1000 C  C     . ARG   A 138 ? 0.3432 0.2382 0.1753 0.0242  0.0509  0.0262  135 ARG   A C     
1001 O  O     . ARG   A 138 ? 0.3257 0.3171 0.1968 0.0839  0.0792  -0.0371 135 ARG   A O     
1002 C  CB    . ARG   A 138 ? 0.2884 0.2742 0.3011 -0.0040 0.0120  0.0027  135 ARG   A CB    
1003 C  CG    . ARG   A 138 ? 0.4714 0.3417 0.4530 -0.0416 0.1824  -0.0597 135 ARG   A CG    
1004 C  CD    . ARG   A 138 ? 0.4520 0.3594 0.5347 -0.0235 0.1116  0.0267  135 ARG   A CD    
1005 N  NE    . ARG   A 138 ? 0.5715 0.3580 0.5151 -0.1089 0.0200  0.0513  135 ARG   A NE    
1006 C  CZ    . ARG   A 138 ? 0.5690 0.3272 0.7004 -0.0182 0.0074  -0.0546 135 ARG   A CZ    
1007 N  NH1   . ARG   A 138 ? 0.7437 0.3507 0.5541 -0.0536 -0.1081 0.0622  135 ARG   A NH1   
1008 N  NH2   . ARG   A 138 ? 0.7742 0.4967 0.7459 0.1341  0.0149  0.0462  135 ARG   A NH2   
1009 N  N     A SER   A 139 ? 0.2256 0.3331 0.2009 0.0197  0.0771  0.0058  136 SER   A N     
1010 N  N     B SER   A 139 ? 0.2293 0.3090 0.2207 0.0176  0.0874  0.0203  136 SER   A N     
1011 C  CA    A SER   A 139 ? 0.2774 0.3213 0.1954 0.0301  0.0391  0.0165  136 SER   A CA    
1012 C  CA    B SER   A 139 ? 0.2825 0.2698 0.2201 0.0411  0.0626  0.0306  136 SER   A CA    
1013 C  C     A SER   A 139 ? 0.2709 0.2886 0.1929 0.0358  0.0519  -0.0370 136 SER   A C     
1014 C  C     B SER   A 139 ? 0.2623 0.2889 0.2044 0.0347  0.0655  -0.0231 136 SER   A C     
1015 O  O     A SER   A 139 ? 0.2612 0.3839 0.1713 0.0171  0.0671  -0.0108 136 SER   A O     
1016 O  O     B SER   A 139 ? 0.2661 0.3638 0.1929 0.0235  0.0679  -0.0022 136 SER   A O     
1017 C  CB    A SER   A 139 ? 0.2296 0.3358 0.1685 0.0106  0.0337  0.0387  136 SER   A CB    
1018 C  CB    B SER   A 139 ? 0.2533 0.2254 0.2274 0.0056  0.0873  0.0605  136 SER   A CB    
1019 O  OG    A SER   A 139 ? 0.2071 0.4219 0.1751 -0.0074 0.0189  0.0200  136 SER   A OG    
1020 O  OG    B SER   A 139 ? 0.2305 0.2122 0.1934 0.0064  0.1006  0.0410  136 SER   A OG    
1021 N  N     . TYR   A 140 ? 0.2648 0.2136 0.2050 0.0133  0.0436  -0.0246 137 TYR   A N     
1022 C  CA    . TYR   A 140 ? 0.2566 0.1659 0.2745 0.0083  0.0033  -0.0204 137 TYR   A CA    
1023 C  C     . TYR   A 140 ? 0.2426 0.2740 0.2352 0.0137  0.0047  -0.0655 137 TYR   A C     
1024 O  O     . TYR   A 140 ? 0.2293 0.2593 0.3037 0.0296  0.0094  -0.0087 137 TYR   A O     
1025 C  CB    . TYR   A 140 ? 0.2275 0.2659 0.2383 0.0018  0.0198  0.0206  137 TYR   A CB    
1026 C  CG    . TYR   A 140 ? 0.2665 0.2401 0.1709 -0.0150 0.0551  0.0126  137 TYR   A CG    
1027 C  CD1   . TYR   A 140 ? 0.2338 0.2339 0.2102 0.0131  0.0248  -0.0208 137 TYR   A CD1   
1028 C  CD2   . TYR   A 140 ? 0.2688 0.2091 0.1785 -0.0427 0.0348  0.0348  137 TYR   A CD2   
1029 C  CE1   . TYR   A 140 ? 0.2463 0.2304 0.1875 0.0215  0.0516  -0.0017 137 TYR   A CE1   
1030 C  CE2   . TYR   A 140 ? 0.2854 0.2341 0.2643 -0.0274 0.0491  0.0111  137 TYR   A CE2   
1031 C  CZ    . TYR   A 140 ? 0.2196 0.2405 0.2440 -0.0286 0.0111  0.0191  137 TYR   A CZ    
1032 O  OH    . TYR   A 140 ? 0.2428 0.2355 0.2957 -0.0355 0.0434  0.0093  137 TYR   A OH    
1033 N  N     . GLY   A 141 ? 0.2518 0.2655 0.1797 0.0797  0.0299  0.0071  138 GLY   A N     
1034 C  CA    . GLY   A 141 ? 0.1951 0.2960 0.2186 0.0658  0.0370  0.0082  138 GLY   A CA    
1035 C  C     . GLY   A 141 ? 0.1873 0.3497 0.2112 0.0160  0.0290  0.0162  138 GLY   A C     
1036 O  O     . GLY   A 141 ? 0.2226 0.4131 0.1916 0.0300  0.0612  -0.0065 138 GLY   A O     
1037 N  N     . ILE   A 142 ? 0.2349 0.2990 0.1436 0.0391  0.0554  0.0002  139 ILE   A N     
1038 C  CA    . ILE   A 142 ? 0.2245 0.2396 0.1721 0.0138  0.0809  0.0181  139 ILE   A CA    
1039 C  C     . ILE   A 142 ? 0.2581 0.2023 0.2023 0.0221  0.0670  0.0094  139 ILE   A C     
1040 O  O     . ILE   A 142 ? 0.2883 0.2120 0.2196 0.0110  0.0809  0.0067  139 ILE   A O     
1041 C  CB    . ILE   A 142 ? 0.2226 0.2382 0.1823 0.0424  0.0541  0.0124  139 ILE   A CB    
1042 C  CG1   . ILE   A 142 ? 0.2097 0.2326 0.1627 0.0144  0.0545  0.0285  139 ILE   A CG1   
1043 C  CG2   . ILE   A 142 ? 0.1818 0.2826 0.1958 0.0361  0.0180  -0.0019 139 ILE   A CG2   
1044 C  CD1   . ILE   A 142 ? 0.2174 0.2147 0.1991 -0.0159 0.0375  0.0088  139 ILE   A CD1   
1045 N  N     . PRO   A 143 ? 0.2251 0.2194 0.2093 0.0251  0.0387  -0.0035 140 PRO   A N     
1046 C  CA    . PRO   A 143 ? 0.2472 0.1992 0.1859 0.0125  0.0761  0.0149  140 PRO   A CA    
1047 C  C     . PRO   A 143 ? 0.2624 0.2040 0.2036 0.0195  0.0529  -0.0086 140 PRO   A C     
1048 O  O     . PRO   A 143 ? 0.2675 0.2108 0.2315 0.0411  0.1029  0.0260  140 PRO   A O     
1049 C  CB    . PRO   A 143 ? 0.2580 0.2034 0.1626 0.0358  0.0350  -0.0294 140 PRO   A CB    
1050 C  CG    . PRO   A 143 ? 0.2348 0.2093 0.2158 -0.0333 0.0591  0.0118  140 PRO   A CG    
1051 C  CD    . PRO   A 143 ? 0.2016 0.2355 0.2595 0.0438  0.0390  -0.0229 140 PRO   A CD    
1052 N  N     . PHE   A 144 ? 0.3243 0.1790 0.2160 -0.0085 0.0641  0.0056  141 PHE   A N     
1053 C  CA    . PHE   A 144 ? 0.2872 0.2096 0.2037 -0.0281 0.0891  0.0191  141 PHE   A CA    
1054 C  C     . PHE   A 144 ? 0.2602 0.2945 0.2309 0.0110  0.1039  -0.0139 141 PHE   A C     
1055 O  O     . PHE   A 144 ? 0.3299 0.2998 0.2259 -0.0356 0.0563  -0.0092 141 PHE   A O     
1056 C  CB    . PHE   A 144 ? 0.3149 0.2403 0.1952 -0.0377 0.0983  -0.0062 141 PHE   A CB    
1057 C  CG    . PHE   A 144 ? 0.2924 0.2472 0.2049 -0.0962 0.0734  -0.0642 141 PHE   A CG    
1058 C  CD1   . PHE   A 144 ? 0.2511 0.2830 0.2475 0.0045  0.0355  -0.0802 141 PHE   A CD1   
1059 C  CD2   . PHE   A 144 ? 0.3304 0.2014 0.2940 -0.0817 0.0505  -0.0701 141 PHE   A CD2   
1060 C  CE1   . PHE   A 144 ? 0.2725 0.2971 0.1805 -0.0563 0.0167  -0.0445 141 PHE   A CE1   
1061 C  CE2   . PHE   A 144 ? 0.3090 0.2717 0.3040 -0.0853 0.0372  -0.0412 141 PHE   A CE2   
1062 C  CZ    . PHE   A 144 ? 0.2741 0.2850 0.2538 -0.0599 -0.0085 -0.0599 141 PHE   A CZ    
1063 N  N     . ILE   A 145 ? 0.2733 0.2623 0.2008 0.0155  0.0474  -0.0558 142 ILE   A N     
1064 C  CA    . ILE   A 145 ? 0.2513 0.2606 0.1825 -0.0558 0.0497  -0.0299 142 ILE   A CA    
1065 C  C     . ILE   A 145 ? 0.2665 0.2820 0.1723 -0.0417 0.0755  -0.0738 142 ILE   A C     
1066 O  O     . ILE   A 145 ? 0.2031 0.2742 0.2271 -0.0715 0.0474  -0.0531 142 ILE   A O     
1067 C  CB    . ILE   A 145 ? 0.2450 0.3862 0.1872 -0.0268 0.0469  -0.0511 142 ILE   A CB    
1068 C  CG1   . ILE   A 145 ? 0.3810 0.3539 0.3217 0.0431  0.0454  -0.0628 142 ILE   A CG1   
1069 C  CG2   . ILE   A 145 ? 0.2789 0.3747 0.1938 -0.0252 0.0759  -0.0826 142 ILE   A CG2   
1070 C  CD1   . ILE   A 145 ? 0.3753 0.3134 0.4397 0.0180  0.1091  -0.0015 142 ILE   A CD1   
1071 N  N     . GLU   A 146 ? 0.2796 0.2247 0.2462 -0.0594 0.0776  -0.0656 143 GLU   A N     
1072 C  CA    . GLU   A 146 ? 0.2160 0.2907 0.2390 -0.0794 0.0674  -0.0438 143 GLU   A CA    
1073 C  C     . GLU   A 146 ? 0.2707 0.2868 0.2498 -0.0819 0.0597  -0.0653 143 GLU   A C     
1074 O  O     . GLU   A 146 ? 0.2768 0.2905 0.2515 -0.0776 0.0384  -0.0253 143 GLU   A O     
1075 C  CB    . GLU   A 146 ? 0.2299 0.2286 0.2592 -0.0890 0.0504  -0.0804 143 GLU   A CB    
1076 C  CG    . GLU   A 146 ? 0.2543 0.3976 0.2404 -0.1176 0.0619  -0.0612 143 GLU   A CG    
1077 C  CD    . GLU   A 146 ? 0.2461 0.4346 0.2439 -0.0922 0.0619  -0.0844 143 GLU   A CD    
1078 O  OE1   . GLU   A 146 ? 0.2825 0.4543 0.2315 -0.1621 0.0822  -0.0463 143 GLU   A OE1   
1079 O  OE2   . GLU   A 146 ? 0.2627 0.3576 0.2725 -0.0994 0.1105  -0.0655 143 GLU   A OE2   
1080 N  N     . THR   A 147 ? 0.1886 0.3255 0.1826 -0.0905 0.0360  -0.0523 144 THR   A N     
1081 C  CA    . THR   A 147 ? 0.2422 0.3141 0.1736 -0.1024 0.0142  -0.0677 144 THR   A CA    
1082 C  C     . THR   A 147 ? 0.2689 0.3031 0.1626 -0.0791 0.0448  -0.0681 144 THR   A C     
1083 O  O     . THR   A 147 ? 0.2005 0.3026 0.1995 -0.0550 0.0211  -0.0441 144 THR   A O     
1084 C  CB    . THR   A 147 ? 0.2212 0.2843 0.2076 -0.0648 0.0149  -0.0260 144 THR   A CB    
1085 O  OG1   . THR   A 147 ? 0.1965 0.2820 0.2010 -0.0890 0.0529  -0.0248 144 THR   A OG1   
1086 C  CG2   . THR   A 147 ? 0.1813 0.3481 0.1741 -0.0229 0.0452  -0.0490 144 THR   A CG2   
1087 N  N     . SER   A 148 ? 0.2655 0.3409 0.1648 -0.0953 0.0522  -0.0504 145 SER   A N     
1088 C  CA    . SER   A 148 ? 0.2440 0.3560 0.2423 -0.0779 0.0464  -0.0359 145 SER   A CA    
1089 C  C     . SER   A 148 ? 0.2143 0.3501 0.2623 -0.0438 0.0398  0.0062  145 SER   A C     
1090 O  O     . SER   A 148 ? 0.2021 0.4078 0.2472 -0.0885 0.0313  -0.0225 145 SER   A O     
1091 C  CB    . SER   A 148 ? 0.2570 0.3255 0.2285 -0.0734 0.0461  -0.0398 145 SER   A CB    
1092 O  OG    . SER   A 148 ? 0.1951 0.4099 0.2282 -0.0612 0.0279  -0.0223 145 SER   A OG    
1093 N  N     . ALA   A 149 ? 0.1831 0.3532 0.1831 -0.0096 0.0820  -0.0483 146 ALA   A N     
1094 C  CA    . ALA   A 149 ? 0.1774 0.4007 0.1953 0.0002  0.0407  0.0218  146 ALA   A CA    
1095 C  C     . ALA   A 149 ? 0.1692 0.5331 0.2349 -0.0006 0.0125  -0.0433 146 ALA   A C     
1096 O  O     . ALA   A 149 ? 0.2414 0.4340 0.2732 0.0081  0.0468  -0.0863 146 ALA   A O     
1097 C  CB    . ALA   A 149 ? 0.1663 0.4159 0.2587 -0.0408 0.0510  0.0112  146 ALA   A CB    
1098 N  N     . LYS   A 150 ? 0.1835 0.4064 0.2134 -0.0441 0.0259  -0.0434 147 LYS   A N     
1099 C  CA    . LYS   A 150 ? 0.2346 0.4467 0.2207 -0.0804 0.0214  0.0030  147 LYS   A CA    
1100 C  C     . LYS   A 150 ? 0.2875 0.4478 0.1766 -0.0627 -0.0389 -0.0100 147 LYS   A C     
1101 O  O     . LYS   A 150 ? 0.3538 0.5904 0.1899 -0.0286 0.0276  -0.0368 147 LYS   A O     
1102 C  CB    . LYS   A 150 ? 0.2216 0.4685 0.2545 -0.0819 0.0172  -0.0604 147 LYS   A CB    
1103 C  CG    . LYS   A 150 ? 0.2600 0.6491 0.2409 -0.0751 0.0094  0.0092  147 LYS   A CG    
1104 C  CD    . LYS   A 150 ? 0.2764 0.6789 0.2971 -0.0828 0.0555  -0.0299 147 LYS   A CD    
1105 C  CE    . LYS   A 150 ? 0.3497 0.7207 0.3582 -0.0732 -0.0102 0.0034  147 LYS   A CE    
1106 N  NZ    . LYS   A 150 ? 0.4406 0.7211 0.3088 -0.0983 -0.0098 0.0508  147 LYS   A NZ    
1107 N  N     . THR   A 151 ? 0.3069 0.4847 0.2076 -0.0202 -0.0156 -0.0174 148 THR   A N     
1108 C  CA    . THR   A 151 ? 0.3858 0.4651 0.2400 -0.0303 -0.0271 -0.0472 148 THR   A CA    
1109 C  C     . THR   A 151 ? 0.4060 0.3566 0.2893 -0.0155 -0.0129 -0.0725 148 THR   A C     
1110 O  O     . THR   A 151 ? 0.4076 0.3577 0.3527 0.0225  -0.0954 -0.0877 148 THR   A O     
1111 C  CB    . THR   A 151 ? 0.4228 0.5673 0.2890 -0.0792 -0.0445 -0.0647 148 THR   A CB    
1112 O  OG1   . THR   A 151 ? 0.3509 0.4978 0.2307 -0.0601 0.0492  -0.0345 148 THR   A OG1   
1113 C  CG2   . THR   A 151 ? 0.3883 0.6214 0.3287 -0.0872 0.0361  -0.0726 148 THR   A CG2   
1114 N  N     . ARG   A 152 ? 0.3129 0.4492 0.1949 -0.0366 0.0540  -0.0665 149 ARG   A N     
1115 C  CA    . ARG   A 152 ? 0.3413 0.4260 0.2219 0.0054  0.0458  -0.0211 149 ARG   A CA    
1116 C  C     . ARG   A 152 ? 0.3310 0.4078 0.2706 -0.0187 0.0862  -0.0091 149 ARG   A C     
1117 O  O     . ARG   A 152 ? 0.3507 0.4018 0.3033 -0.0565 0.0430  -0.0664 149 ARG   A O     
1118 C  CB    . ARG   A 152 ? 0.3522 0.3987 0.2831 0.0115  0.1067  -0.0589 149 ARG   A CB    
1119 C  CG    . ARG   A 152 ? 0.3678 0.5755 0.3526 -0.0122 0.1260  -0.0166 149 ARG   A CG    
1120 C  CD    . ARG   A 152 ? 0.3752 0.6418 0.3946 0.0145  0.1893  -0.0890 149 ARG   A CD    
1121 N  NE    . ARG   A 152 ? 0.3860 0.7084 0.4332 -0.0113 0.1502  -0.0241 149 ARG   A NE    
1122 C  CZ    . ARG   A 152 ? 0.4400 0.6817 0.6797 -0.0322 0.0616  -0.0255 149 ARG   A CZ    
1123 N  NH1   . ARG   A 152 ? 0.5604 0.6164 0.7034 0.0722  0.0276  -0.1498 149 ARG   A NH1   
1124 N  NH2   . ARG   A 152 ? 0.4012 0.8969 0.7409 0.0112  0.0941  -0.1649 149 ARG   A NH2   
1125 N  N     . GLN   A 153 ? 0.2366 0.4393 0.2690 -0.0906 -0.0074 -0.0358 150 GLN   A N     
1126 C  CA    . GLN   A 153 ? 0.2684 0.3902 0.3129 -0.1019 0.0003  -0.0492 150 GLN   A CA    
1127 C  C     . GLN   A 153 ? 0.2072 0.3110 0.2879 -0.0939 0.0405  -0.0599 150 GLN   A C     
1128 O  O     . GLN   A 153 ? 0.2211 0.3244 0.2681 -0.0473 0.0442  -0.0430 150 GLN   A O     
1129 C  CB    . GLN   A 153 ? 0.2738 0.5474 0.2858 -0.1161 -0.0259 -0.0163 150 GLN   A CB    
1130 C  CG    . GLN   A 153 ? 0.3844 0.5352 0.4414 -0.0687 -0.0425 0.0286  150 GLN   A CG    
1131 C  CD    . GLN   A 153 ? 0.6394 0.5181 0.4298 -0.1548 -0.0608 0.0622  150 GLN   A CD    
1132 O  OE1   . GLN   A 153 ? 0.8077 0.7694 0.4537 -0.0491 -0.0656 0.0188  150 GLN   A OE1   
1133 N  NE2   . GLN   A 153 ? 0.6044 0.6760 0.6011 -0.2331 -0.0185 0.1987  150 GLN   A NE2   
1134 N  N     . ARG   A 154 ? 0.2910 0.3446 0.1773 -0.0547 0.0525  -0.0464 151 ARG   A N     
1135 C  CA    . ARG   A 154 ? 0.2690 0.3798 0.2055 -0.0603 0.0671  -0.0385 151 ARG   A CA    
1136 C  C     . ARG   A 154 ? 0.2660 0.3786 0.2300 -0.0422 0.0303  -0.0214 151 ARG   A C     
1137 O  O     . ARG   A 154 ? 0.2066 0.3762 0.2036 -0.0366 0.0655  -0.0214 151 ARG   A O     
1138 C  CB    . ARG   A 154 ? 0.3216 0.3121 0.2258 -0.0561 0.1094  -0.0828 151 ARG   A CB    
1139 C  CG    . ARG   A 154 ? 0.2563 0.2911 0.2976 -0.0545 0.0210  -0.0600 151 ARG   A CG    
1140 C  CD    . ARG   A 154 ? 0.3993 0.3263 0.3104 -0.0201 0.0619  -0.0533 151 ARG   A CD    
1141 N  NE    . ARG   A 154 ? 0.4291 0.4344 0.3519 0.0110  0.0283  -0.0004 151 ARG   A NE    
1142 C  CZ    . ARG   A 154 ? 0.3762 0.3501 0.3892 0.0019  0.0145  -0.0069 151 ARG   A CZ    
1143 N  NH1   . ARG   A 154 ? 0.4714 0.3664 0.4323 -0.0295 0.0762  -0.0020 151 ARG   A NH1   
1144 N  NH2   . ARG   A 154 ? 0.3697 0.4315 0.4395 0.0263  0.0879  0.0150  151 ARG   A NH2   
1145 N  N     . VAL   A 155 ? 0.2439 0.3049 0.1983 -0.0145 0.0471  -0.0253 152 VAL   A N     
1146 C  CA    . VAL   A 155 ? 0.2447 0.2788 0.2058 -0.0005 0.0777  -0.0198 152 VAL   A CA    
1147 C  C     . VAL   A 155 ? 0.2617 0.2890 0.2462 -0.0324 0.0186  -0.0566 152 VAL   A C     
1148 O  O     . VAL   A 155 ? 0.2265 0.2731 0.2182 -0.0437 0.0786  -0.0397 152 VAL   A O     
1149 C  CB    . VAL   A 155 ? 0.2293 0.2799 0.2211 -0.0187 0.0104  -0.0260 152 VAL   A CB    
1150 C  CG1   . VAL   A 155 ? 0.2173 0.3284 0.2177 -0.0627 0.0271  -0.0345 152 VAL   A CG1   
1151 C  CG2   . VAL   A 155 ? 0.2439 0.2472 0.2830 0.0188  0.0285  -0.0154 152 VAL   A CG2   
1152 N  N     . GLU   A 156 ? 0.2480 0.3318 0.2166 -0.0301 -0.0073 -0.0581 153 GLU   A N     
1153 C  CA    . GLU   A 156 ? 0.2631 0.2719 0.2719 0.0143  0.0457  -0.0703 153 GLU   A CA    
1154 C  C     . GLU   A 156 ? 0.2274 0.2694 0.2788 -0.0158 0.0407  -0.0489 153 GLU   A C     
1155 O  O     . GLU   A 156 ? 0.2529 0.3047 0.2049 -0.0212 0.0470  -0.0592 153 GLU   A O     
1156 C  CB    . GLU   A 156 ? 0.2872 0.3241 0.2495 -0.0250 0.0768  -0.0609 153 GLU   A CB    
1157 C  CG    . GLU   A 156 ? 0.3468 0.4985 0.3423 0.0218  0.0768  -0.0764 153 GLU   A CG    
1158 C  CD    . GLU   A 156 ? 0.4331 0.4196 0.3900 -0.0172 0.0239  -0.0706 153 GLU   A CD    
1159 O  OE1   . GLU   A 156 ? 0.4814 0.4735 0.5069 0.0816  0.0240  -0.0803 153 GLU   A OE1   
1160 O  OE2   . GLU   A 156 ? 0.5064 0.5742 0.3090 0.0485  0.1234  -0.1589 153 GLU   A OE2   
1161 N  N     . ASP   A 157 ? 0.2303 0.3025 0.2577 -0.0269 0.0133  -0.0499 154 ASP   A N     
1162 C  CA    . ASP   A 157 ? 0.1858 0.3158 0.2372 -0.0125 0.0189  -0.0396 154 ASP   A CA    
1163 C  C     . ASP   A 157 ? 0.2206 0.2878 0.2527 -0.0038 0.0609  -0.0499 154 ASP   A C     
1164 O  O     . ASP   A 157 ? 0.2243 0.2364 0.2411 -0.0233 0.0644  -0.0208 154 ASP   A O     
1165 C  CB    . ASP   A 157 ? 0.2560 0.3124 0.2688 -0.0224 0.0610  -0.0198 154 ASP   A CB    
1166 C  CG    . ASP   A 157 ? 0.3195 0.2807 0.4812 -0.0290 0.0755  -0.0250 154 ASP   A CG    
1167 O  OD1   . ASP   A 157 ? 0.3536 0.3537 0.4170 -0.0612 0.0699  -0.0082 154 ASP   A OD1   
1168 O  OD2   . ASP   A 157 ? 0.4173 0.3767 0.4370 -0.1478 0.0052  0.0071  154 ASP   A OD2   
1169 N  N     . ALA   A 158 ? 0.1642 0.2894 0.2167 -0.0309 0.0507  -0.0246 155 ALA   A N     
1170 C  CA    . ALA   A 158 ? 0.2389 0.2889 0.2003 -0.0509 0.0420  -0.0118 155 ALA   A CA    
1171 C  C     . ALA   A 158 ? 0.2431 0.2462 0.1865 -0.0248 0.0934  -0.0497 155 ALA   A C     
1172 O  O     . ALA   A 158 ? 0.2242 0.2528 0.1991 0.0194  0.0616  -0.0025 155 ALA   A O     
1173 C  CB    . ALA   A 158 ? 0.2762 0.3461 0.1768 -0.0109 0.0416  0.0250  155 ALA   A CB    
1174 N  N     . PHE   A 159 ? 0.1753 0.2954 0.1650 -0.0164 0.0448  -0.0248 156 PHE   A N     
1175 C  CA    . PHE   A 159 ? 0.1991 0.2748 0.1842 -0.0339 0.0175  0.0011  156 PHE   A CA    
1176 C  C     . PHE   A 159 ? 0.2451 0.2809 0.1540 0.0054  0.0405  0.0353  156 PHE   A C     
1177 O  O     . PHE   A 159 ? 0.2165 0.3228 0.1859 0.0409  0.0510  -0.0175 156 PHE   A O     
1178 C  CB    . PHE   A 159 ? 0.1930 0.3072 0.1661 -0.0111 0.0145  0.0003  156 PHE   A CB    
1179 C  CG    . PHE   A 159 ? 0.2165 0.2943 0.1405 0.0059  0.0059  0.0055  156 PHE   A CG    
1180 C  CD1   . PHE   A 159 ? 0.2311 0.3131 0.1455 0.0071  0.0378  -0.0176 156 PHE   A CD1   
1181 C  CD2   . PHE   A 159 ? 0.2173 0.3282 0.1457 -0.0169 0.0251  0.0229  156 PHE   A CD2   
1182 C  CE1   . PHE   A 159 ? 0.2159 0.2890 0.1503 -0.0131 0.0327  -0.0062 156 PHE   A CE1   
1183 C  CE2   . PHE   A 159 ? 0.2246 0.3432 0.1437 0.0000  0.0314  0.0107  156 PHE   A CE2   
1184 C  CZ    . PHE   A 159 ? 0.2426 0.3767 0.1601 0.0120  0.0089  -0.0142 156 PHE   A CZ    
1185 N  N     . TYR   A 160 ? 0.2047 0.2826 0.1691 -0.0192 0.0152  -0.0010 157 TYR   A N     
1186 C  CA    . TYR   A 160 ? 0.2332 0.3095 0.1943 -0.0054 0.0249  0.0185  157 TYR   A CA    
1187 C  C     . TYR   A 160 ? 0.2543 0.2691 0.2000 0.0298  0.0526  0.0304  157 TYR   A C     
1188 O  O     . TYR   A 160 ? 0.2317 0.2946 0.2129 0.0236  0.0614  -0.0216 157 TYR   A O     
1189 C  CB    . TYR   A 160 ? 0.2525 0.3061 0.2408 0.0360  0.0635  0.0086  157 TYR   A CB    
1190 C  CG    . TYR   A 160 ? 0.2683 0.3725 0.2509 -0.0541 0.0853  -0.0069 157 TYR   A CG    
1191 C  CD1   . TYR   A 160 ? 0.1809 0.3810 0.2343 -0.0077 0.0942  -0.0093 157 TYR   A CD1   
1192 C  CD2   . TYR   A 160 ? 0.3874 0.4504 0.2538 -0.1068 0.1133  -0.0551 157 TYR   A CD2   
1193 C  CE1   . TYR   A 160 ? 0.2782 0.4467 0.2426 -0.0831 0.1152  -0.0166 157 TYR   A CE1   
1194 C  CE2   . TYR   A 160 ? 0.4222 0.4232 0.2424 -0.0949 0.0966  -0.0464 157 TYR   A CE2   
1195 C  CZ    . TYR   A 160 ? 0.4672 0.4541 0.2190 -0.0578 0.0806  -0.0158 157 TYR   A CZ    
1196 O  OH    . TYR   A 160 ? 0.4549 0.5567 0.2192 -0.0321 0.1123  -0.0515 157 TYR   A OH    
1197 N  N     . THR   A 161 ? 0.2225 0.2718 0.2013 -0.0174 0.0385  -0.0302 158 THR   A N     
1198 C  CA    . THR   A 161 ? 0.2210 0.2194 0.2222 -0.0422 0.0418  -0.0117 158 THR   A CA    
1199 C  C     . THR   A 161 ? 0.1767 0.1956 0.2446 -0.0247 0.0560  -0.0195 158 THR   A C     
1200 O  O     . THR   A 161 ? 0.2140 0.2496 0.2191 0.0120  0.0604  -0.0234 158 THR   A O     
1201 C  CB    . THR   A 161 ? 0.1986 0.2501 0.2177 -0.0396 0.0109  -0.0137 158 THR   A CB    
1202 O  OG1   . THR   A 161 ? 0.2933 0.2536 0.2348 -0.0225 0.0436  -0.0677 158 THR   A OG1   
1203 C  CG2   . THR   A 161 ? 0.2028 0.2751 0.2236 -0.0540 0.0258  0.0160  158 THR   A CG2   
1204 N  N     . LEU   A 162 ? 0.2164 0.2424 0.1791 0.0279  0.0682  0.0011  159 LEU   A N     
1205 C  CA    . LEU   A 162 ? 0.1762 0.2376 0.1602 0.0297  0.0452  -0.0037 159 LEU   A CA    
1206 C  C     . LEU   A 162 ? 0.1948 0.2941 0.1882 0.0512  0.0497  0.0000  159 LEU   A C     
1207 O  O     . LEU   A 162 ? 0.2015 0.2216 0.1752 0.0050  0.0477  0.0169  159 LEU   A O     
1208 C  CB    . LEU   A 162 ? 0.1429 0.2420 0.1617 0.0466  0.0089  -0.0280 159 LEU   A CB    
1209 C  CG    . LEU   A 162 ? 0.1555 0.2219 0.1974 0.0357  0.0257  -0.0318 159 LEU   A CG    
1210 C  CD1   . LEU   A 162 ? 0.2198 0.2083 0.1962 0.0200  0.0512  -0.0054 159 LEU   A CD1   
1211 C  CD2   . LEU   A 162 ? 0.1670 0.2235 0.1676 0.0224  0.0552  -0.0457 159 LEU   A CD2   
1212 N  N     . VAL   A 163 ? 0.1974 0.2580 0.1807 0.0691  0.0416  0.0312  160 VAL   A N     
1213 C  CA    . VAL   A 163 ? 0.1820 0.2863 0.2071 0.0477  0.0348  0.0005  160 VAL   A CA    
1214 C  C     . VAL   A 163 ? 0.2397 0.2565 0.1876 0.0666  0.0493  -0.0138 160 VAL   A C     
1215 O  O     . VAL   A 163 ? 0.1976 0.2774 0.2120 0.0619  0.0507  0.0333  160 VAL   A O     
1216 C  CB    . VAL   A 163 ? 0.2032 0.2930 0.2086 0.0815  0.0237  0.0008  160 VAL   A CB    
1217 C  CG1   . VAL   A 163 ? 0.1720 0.3366 0.2239 0.0145  0.0528  0.0105  160 VAL   A CG1   
1218 C  CG2   . VAL   A 163 ? 0.2577 0.3151 0.1731 0.0875  0.0388  0.0130  160 VAL   A CG2   
1219 N  N     . ARG   A 164 ? 0.2095 0.2611 0.2021 0.0727  0.0373  0.0187  161 ARG   A N     
1220 C  CA    . ARG   A 164 ? 0.1663 0.2395 0.2235 0.0628  0.0293  0.0054  161 ARG   A CA    
1221 C  C     . ARG   A 164 ? 0.2901 0.2290 0.2026 0.0561  0.0374  0.0317  161 ARG   A C     
1222 O  O     . ARG   A 164 ? 0.2566 0.2504 0.2206 0.0406  0.0439  0.0365  161 ARG   A O     
1223 C  CB    . ARG   A 164 ? 0.2817 0.2726 0.2487 0.0055  0.0167  0.0191  161 ARG   A CB    
1224 C  CG    . ARG   A 164 ? 0.3506 0.3476 0.2342 -0.0559 0.0905  0.0411  161 ARG   A CG    
1225 C  CD    . ARG   A 164 ? 0.3233 0.3651 0.3382 -0.0706 0.0972  0.0290  161 ARG   A CD    
1226 N  NE    . ARG   A 164 ? 0.4519 0.3941 0.3245 -0.1111 0.0248  0.0051  161 ARG   A NE    
1227 C  CZ    . ARG   A 164 ? 0.3529 0.4024 0.3044 -0.0506 0.0593  -0.0300 161 ARG   A CZ    
1228 N  NH1   . ARG   A 164 ? 0.4459 0.2814 0.5263 -0.0162 0.0209  0.1139  161 ARG   A NH1   
1229 N  NH2   . ARG   A 164 ? 0.5286 0.4649 0.4050 -0.0802 0.1355  -0.0878 161 ARG   A NH2   
1230 N  N     . GLU   A 165 ? 0.2148 0.2592 0.2185 0.0698  0.0080  0.0372  162 GLU   A N     
1231 C  CA    . GLU   A 165 ? 0.2496 0.2298 0.2449 0.0581  -0.0245 -0.0116 162 GLU   A CA    
1232 C  C     . GLU   A 165 ? 0.2242 0.2707 0.2295 0.0479  0.0161  0.0080  162 GLU   A C     
1233 O  O     . GLU   A 165 ? 0.2045 0.3238 0.2168 0.0245  0.0168  0.0161  162 GLU   A O     
1234 C  CB    . GLU   A 165 ? 0.2135 0.2780 0.1883 0.0236  0.0060  -0.0015 162 GLU   A CB    
1235 C  CG    . GLU   A 165 ? 0.2402 0.2544 0.2564 -0.0075 0.0176  -0.0153 162 GLU   A CG    
1236 C  CD    . GLU   A 165 ? 0.2907 0.2372 0.2848 -0.0886 -0.0041 0.0138  162 GLU   A CD    
1237 O  OE1   . GLU   A 165 ? 0.3641 0.2662 0.2167 0.0417  0.0365  0.0102  162 GLU   A OE1   
1238 O  OE2   . GLU   A 165 ? 0.4479 0.2487 0.2581 -0.0442 0.0412  -0.0058 162 GLU   A OE2   
1239 N  N     . ILE   A 166 ? 0.2099 0.2559 0.2293 0.0912  0.0091  0.0251  163 ILE   A N     
1240 C  CA    . ILE   A 166 ? 0.2230 0.2852 0.2118 0.0528  -0.0187 -0.0147 163 ILE   A CA    
1241 C  C     . ILE   A 166 ? 0.2186 0.2859 0.2610 0.0440  0.0010  0.0047  163 ILE   A C     
1242 O  O     . ILE   A 166 ? 0.2007 0.2865 0.2265 0.0713  0.0302  -0.0370 163 ILE   A O     
1243 C  CB    . ILE   A 166 ? 0.2027 0.2918 0.2210 0.0509  -0.0173 0.0076  163 ILE   A CB    
1244 C  CG1   . ILE   A 166 ? 0.1542 0.3196 0.2056 0.0416  0.0273  0.0150  163 ILE   A CG1   
1245 C  CG2   . ILE   A 166 ? 0.2523 0.2915 0.2260 0.0349  0.0212  0.0193  163 ILE   A CG2   
1246 C  CD1   . ILE   A 166 ? 0.1861 0.2234 0.2872 -0.0264 -0.0104 0.0147  163 ILE   A CD1   
1247 N  N     . ARG   A 167 ? 0.1929 0.2978 0.2462 0.1011  0.0249  0.0070  164 ARG   A N     
1248 C  CA    . ARG   A 167 ? 0.1749 0.3166 0.2706 0.1010  0.0003  -0.0188 164 ARG   A CA    
1249 C  C     . ARG   A 167 ? 0.2358 0.3635 0.2839 0.1081  -0.0143 0.0112  164 ARG   A C     
1250 O  O     . ARG   A 167 ? 0.2227 0.4018 0.3142 0.1100  -0.0122 -0.0195 164 ARG   A O     
1251 C  CB    . ARG   A 167 ? 0.2222 0.3056 0.2867 0.0726  0.0320  -0.0382 164 ARG   A CB    
1252 C  CG    . ARG   A 167 ? 0.2109 0.3061 0.3279 0.0604  0.0223  -0.0391 164 ARG   A CG    
1253 C  CD    . ARG   A 167 ? 0.3192 0.2957 0.2874 0.0381  -0.0106 0.0033  164 ARG   A CD    
1254 N  NE    . ARG   A 167 ? 0.3153 0.3607 0.2508 0.1043  0.0271  -0.0076 164 ARG   A NE    
1255 C  CZ    . ARG   A 167 ? 0.3844 0.3679 0.2887 0.0557  0.0120  -0.0370 164 ARG   A CZ    
1256 N  NH1   . ARG   A 167 ? 0.4037 0.4198 0.3050 -0.0281 0.0205  -0.0247 164 ARG   A NH1   
1257 N  NH2   . ARG   A 167 ? 0.3996 0.4533 0.3074 0.0725  0.0482  -0.0021 164 ARG   A NH2   
1258 N  N     . GLN   A 168 ? 0.3059 0.2444 0.2698 0.0774  -0.0245 0.0049  165 GLN   A N     
1259 C  CA    . GLN   A 168 ? 0.2888 0.3376 0.2757 0.0706  -0.0392 0.0421  165 GLN   A CA    
1260 C  C     . GLN   A 168 ? 0.3106 0.3120 0.3190 0.0762  -0.0718 0.0396  165 GLN   A C     
1261 O  O     . GLN   A 168 ? 0.3789 0.3859 0.2651 0.1957  -0.0506 -0.0089 165 GLN   A O     
1262 C  CB    . GLN   A 168 ? 0.3836 0.3683 0.3406 0.0149  0.0342  0.0601  165 GLN   A CB    
1263 C  CG    . GLN   A 168 ? 0.5541 0.4688 0.4147 -0.0420 0.0592  0.0001  165 GLN   A CG    
1264 C  CD    . GLN   A 168 ? 0.5227 0.5739 0.4391 -0.0312 0.0274  0.0737  165 GLN   A CD    
1265 O  OE1   . GLN   A 168 ? 0.8737 0.5320 0.5453 -0.0040 0.1443  0.1063  165 GLN   A OE1   
1266 N  NE2   . GLN   A 168 ? 0.6856 0.7263 0.5522 0.0765  -0.1229 0.0689  165 GLN   A NE2   
1267 N  N     . TYR   A 169 ? 0.3516 0.3052 0.1999 0.0960  -0.0365 -0.0131 166 TYR   A N     
1268 C  CA    . TYR   A 169 ? 0.1954 0.3633 0.2935 0.0874  -0.0178 -0.0793 166 TYR   A CA    
1269 C  C     . TYR   A 169 ? 0.2261 0.5033 0.3056 0.0315  0.0097  -0.0408 166 TYR   A C     
1270 O  O     . TYR   A 169 ? 0.2404 0.4656 0.3436 0.0805  -0.0059 -0.0786 166 TYR   A O     
1271 C  CB    . TYR   A 169 ? 0.2835 0.3505 0.2725 0.0679  -0.0172 -0.0101 166 TYR   A CB    
1272 C  CG    . TYR   A 169 ? 0.3574 0.3411 0.3747 0.0612  -0.0645 -0.0208 166 TYR   A CG    
1273 C  CD1   . TYR   A 169 ? 0.5440 0.4144 0.3694 -0.0349 -0.0729 -0.0488 166 TYR   A CD1   
1274 C  CD2   . TYR   A 169 ? 0.3913 0.4336 0.3369 0.0458  -0.0368 -0.0284 166 TYR   A CD2   
1275 C  CE1   . TYR   A 169 ? 0.6297 0.4008 0.5089 -0.0190 -0.0076 -0.1089 166 TYR   A CE1   
1276 C  CE2   . TYR   A 169 ? 0.5908 0.3483 0.4876 0.0177  -0.0732 0.0116  166 TYR   A CE2   
1277 C  CZ    . TYR   A 169 ? 0.5918 0.3430 0.4812 0.0295  -0.0600 -0.1108 166 TYR   A CZ    
1278 O  OH    . TYR   A 169 ? 0.5791 0.3663 0.5410 0.0040  -0.1190 -0.1102 166 TYR   A OH    
1279 N  N     . ARG   A 170 ? 0.1860 0.5415 0.3235 0.1521  0.0072  -0.1420 167 ARG   A N     
1280 C  CA    . ARG   A 170 ? 0.2610 0.5079 0.2817 0.0427  0.0445  -0.0633 167 ARG   A CA    
1281 C  C     . ARG   A 170 ? 0.3149 0.4737 0.3202 0.0527  0.0152  -0.0215 167 ARG   A C     
1282 O  O     . ARG   A 170 ? 0.3216 0.5640 0.4363 0.0307  0.0283  -0.0298 167 ARG   A O     
1283 C  CB    . ARG   A 170 ? 0.2897 0.4480 0.2929 0.0571  -0.0114 -0.0083 167 ARG   A CB    
1284 C  CG    . ARG   A 170 ? 0.3742 0.4390 0.4122 0.0597  0.0289  -0.0159 167 ARG   A CG    
1285 C  CD    . ARG   A 170 ? 0.3320 0.3869 0.4187 0.0493  -0.0799 0.0820  167 ARG   A CD    
1286 N  NE    . ARG   A 170 ? 0.3032 0.3911 0.4736 0.0294  -0.0884 0.0581  167 ARG   A NE    
1287 C  CZ    . ARG   A 170 ? 0.3827 0.3070 0.4719 -0.0119 0.0929  0.0128  167 ARG   A CZ    
1288 N  NH1   . ARG   A 170 ? 0.5029 0.5338 0.4161 0.0677  0.1258  -0.0188 167 ARG   A NH1   
1289 N  NH2   . ARG   A 170 ? 0.6274 0.4788 0.7310 0.0304  -0.0600 0.1389  167 ARG   A NH2   
1290 N  N     . LEU   A 171 ? 0.2797 0.4258 0.4128 0.1387  0.0139  -0.0731 168 LEU   A N     
1291 C  CA    . LEU   A 171 ? 0.3524 0.5071 0.4255 0.2004  -0.0937 -0.0755 168 LEU   A CA    
1292 C  C     . LEU   A 171 ? 0.3986 0.5433 0.4015 0.1971  0.0969  -0.0183 168 LEU   A C     
1293 O  O     . LEU   A 171 ? 0.3845 0.5585 0.4262 0.1427  0.0333  -0.0055 168 LEU   A O     
1294 C  CB    . LEU   A 171 ? 0.4712 0.4865 0.5210 0.1700  -0.0949 -0.0556 168 LEU   A CB    
1295 C  CG    . LEU   A 171 ? 0.5253 0.5514 0.5194 0.0834  -0.0159 0.0009  168 LEU   A CG    
1296 C  CD1   . LEU   A 171 ? 0.5762 0.5654 0.5830 0.2516  -0.0654 0.0441  168 LEU   A CD1   
1297 C  CD2   . LEU   A 171 ? 0.5629 0.5904 0.3451 0.0463  -0.0279 -0.0005 168 LEU   A CD2   
1298 N  N     . LYS   A 172 ? 0.3354 0.5064 0.3395 0.1323  -0.0008 -0.0713 169 LYS   A N     
1299 C  CA    . LYS   A 172 ? 0.3513 0.5291 0.3307 0.0292  -0.0059 0.0288  169 LYS   A CA    
1300 C  C     . LYS   A 172 ? 0.4974 0.5590 0.3359 -0.0798 -0.0484 0.0134  169 LYS   A C     
1301 O  O     . LYS   A 172 ? 0.5539 0.6791 0.3318 -0.0659 0.0403  0.0630  169 LYS   A O     
1302 C  CB    . LYS   A 172 ? 0.3350 0.5299 0.3268 0.0263  -0.0151 0.0267  169 LYS   A CB    
1303 C  CG    . LYS   A 172 ? 0.3759 0.5344 0.4190 0.0090  0.0359  -0.0100 169 LYS   A CG    
1304 C  CD    . LYS   A 172 ? 0.3657 0.6264 0.4589 0.0196  0.0631  0.0335  169 LYS   A CD    
1305 C  CE    . LYS   A 172 ? 0.5609 0.5278 0.4624 -0.0691 0.0722  -0.0033 169 LYS   A CE    
1306 N  NZ    . LYS   A 172 ? 0.5415 0.6495 0.5391 -0.0519 0.0194  -0.0238 169 LYS   A NZ    
1307 O  OXT   . LYS   A 172 ? 0.5192 0.6044 0.4919 -0.0318 0.0243  0.0270  169 LYS   A OXT   
1308 P  PG    . GNP   B .   ? 0.3082 0.3053 0.3580 0.0842  0.0257  0.0365  201 GNP   A PG    
1309 O  O1G   . GNP   B .   ? 0.3261 0.2501 0.3784 0.0134  -0.0253 0.0160  201 GNP   A O1G   
1310 O  O2G   . GNP   B .   ? 0.3900 0.3668 0.3775 0.0991  0.0353  0.1195  201 GNP   A O2G   
1311 O  O3G   . GNP   B .   ? 0.4052 0.2599 0.3588 0.0196  0.0160  0.0207  201 GNP   A O3G   
1312 N  N3B   . GNP   B .   ? 0.2657 0.3196 0.2812 0.0335  0.0590  0.0417  201 GNP   A N3B   
1313 P  PB    . GNP   B .   ? 0.2081 0.3176 0.2535 0.0098  0.0365  0.0309  201 GNP   A PB    
1314 O  O1B   . GNP   B .   ? 0.1412 0.3243 0.2554 0.0500  0.0261  -0.0140 201 GNP   A O1B   
1315 O  O2B   . GNP   B .   ? 0.2361 0.2955 0.2444 0.0420  0.0326  0.0254  201 GNP   A O2B   
1316 O  O3A   . GNP   B .   ? 0.1827 0.4405 0.2703 -0.0400 0.0021  -0.0091 201 GNP   A O3A   
1317 P  PA    . GNP   B .   ? 0.1932 0.3795 0.2779 0.0169  -0.0119 0.0332  201 GNP   A PA    
1318 O  O1A   . GNP   B .   ? 0.1574 0.3555 0.3578 0.0045  -0.0042 0.0445  201 GNP   A O1A   
1319 O  O2A   . GNP   B .   ? 0.2471 0.3399 0.2577 0.0032  -0.0020 0.0119  201 GNP   A O2A   
1320 O  "O5'" . GNP   B .   ? 0.1853 0.3964 0.2599 -0.0187 -0.0168 0.0324  201 GNP   A "O5'" 
1321 C  "C5'" . GNP   B .   ? 0.2593 0.4134 0.2856 0.0116  0.0261  0.0047  201 GNP   A "C5'" 
1322 C  "C4'" . GNP   B .   ? 0.1411 0.3465 0.2512 0.1097  -0.0032 -0.0081 201 GNP   A "C4'" 
1323 O  "O4'" . GNP   B .   ? 0.1491 0.3470 0.2866 0.0587  -0.0009 -0.0076 201 GNP   A "O4'" 
1324 C  "C3'" . GNP   B .   ? 0.1647 0.4709 0.2687 0.0179  -0.0352 -0.0135 201 GNP   A "C3'" 
1325 O  "O3'" . GNP   B .   ? 0.1822 0.4757 0.3146 0.0503  -0.0642 0.0088  201 GNP   A "O3'" 
1326 C  "C2'" . GNP   B .   ? 0.1767 0.4576 0.2829 0.0269  -0.0297 0.0152  201 GNP   A "C2'" 
1327 O  "O2'" . GNP   B .   ? 0.2523 0.5469 0.2622 0.0192  -0.0103 0.0058  201 GNP   A "O2'" 
1328 C  "C1'" . GNP   B .   ? 0.1411 0.4635 0.2589 0.0079  -0.0130 -0.0276 201 GNP   A "C1'" 
1329 N  N9    . GNP   B .   ? 0.1477 0.4404 0.1979 -0.0318 0.0298  -0.0185 201 GNP   A N9    
1330 C  C8    . GNP   B .   ? 0.1480 0.3773 0.1586 -0.0205 0.0438  -0.0265 201 GNP   A C8    
1331 N  N7    . GNP   B .   ? 0.1289 0.3526 0.2118 -0.0171 0.0404  -0.0222 201 GNP   A N7    
1332 C  C5    . GNP   B .   ? 0.1408 0.4175 0.1796 -0.0517 0.0352  -0.0579 201 GNP   A C5    
1333 C  C6    . GNP   B .   ? 0.1502 0.4206 0.2308 0.0131  0.0544  -0.0546 201 GNP   A C6    
1334 O  O6    . GNP   B .   ? 0.1558 0.4437 0.2067 -0.0061 0.0441  -0.0279 201 GNP   A O6    
1335 N  N1    . GNP   B .   ? 0.1734 0.4102 0.1972 -0.0331 0.0231  0.0078  201 GNP   A N1    
1336 C  C2    . GNP   B .   ? 0.1728 0.4410 0.2106 -0.0405 -0.0171 0.0257  201 GNP   A C2    
1337 N  N2    . GNP   B .   ? 0.2028 0.4945 0.3249 -0.1089 -0.0296 0.0187  201 GNP   A N2    
1338 N  N3    . GNP   B .   ? 0.1471 0.4364 0.2472 -0.0506 0.0172  0.0065  201 GNP   A N3    
1339 C  C4    . GNP   B .   ? 0.1516 0.4594 0.1859 -0.0388 0.0431  -0.0302 201 GNP   A C4    
1340 MG MG    . MG    C .   ? 0.1709 0.2867 0.2784 0.0345  0.0083  0.0832  202 MG    A MG    
1341 CO CO    . CO    D .   ? 0.5248 0.6025 0.4869 0.0285  -0.0034 0.0431  203 CO    A CO    
1342 CO CO    . CO    E .   ? 0.2365 0.2770 0.3016 -0.0469 0.0669  -0.0155 204 CO    A CO    
1343 C  CBK   . A1IK8 F .   ? 0.4954 0.5472 0.3246 -0.1159 0.0183  0.0520  205 A1IK8 A CBK   
1344 C  CBL   . A1IK8 F .   ? 0.5323 0.5074 0.4401 -0.0565 -0.0470 0.0591  205 A1IK8 A CBL   
1345 C  CBM   . A1IK8 F .   ? 0.5196 0.3522 0.4271 -0.0642 0.0112  0.0185  205 A1IK8 A CBM   
1346 N  NBP   . A1IK8 F .   ? 0.6523 0.4833 0.4768 0.0318  0.0510  -0.0399 205 A1IK8 A NBP   
1347 C  CBN   . A1IK8 F .   ? 0.5156 0.5375 0.3834 -0.0058 -0.0035 0.0906  205 A1IK8 A CBN   
1348 C  CBO   . A1IK8 F .   ? 0.4275 0.5347 0.3291 -0.0470 -0.0305 0.0812  205 A1IK8 A CBO   
1349 C  CBJ   . A1IK8 F .   ? 0.4150 0.5305 0.3594 -0.0482 -0.0420 0.0850  205 A1IK8 A CBJ   
1350 N  NAQ   . A1IK8 F .   ? 0.2921 0.3780 0.3369 -0.0644 -0.0557 0.0423  205 A1IK8 A NAQ   
1351 C  CAB   . A1IK8 F .   ? 0.3374 0.3607 0.3048 -0.0950 0.0205  0.0292  205 A1IK8 A CAB   
1352 O  OAA   . A1IK8 F .   ? 0.4139 0.3893 0.4763 -0.0695 -0.0642 0.0981  205 A1IK8 A OAA   
1353 C  CAR   . A1IK8 F .   ? 0.2387 0.3588 0.3280 -0.0315 -0.0570 0.0285  205 A1IK8 A CAR   
1354 C  CAS   . A1IK8 F .   ? 0.2714 0.4052 0.4047 -0.0474 -0.0108 0.0017  205 A1IK8 A CAS   
1355 C  CAT   . A1IK8 F .   ? 0.2641 0.3664 0.3718 -0.0795 0.0073  0.0201  205 A1IK8 A CAT   
1356 C  CAU   . A1IK8 F .   ? 0.2437 0.3055 0.2997 -0.1097 -0.0312 0.0435  205 A1IK8 A CAU   
1357 C  CAV   . A1IK8 F .   ? 0.1881 0.4157 0.2932 -0.1091 0.0068  0.0411  205 A1IK8 A CAV   
1358 N  NAW   . A1IK8 F .   ? 0.1601 0.3808 0.3064 -0.1168 0.0136  0.0499  205 A1IK8 A NAW   
1359 C  CAX   . A1IK8 F .   ? 0.1611 0.3390 0.3455 -0.0423 0.0143  0.0176  205 A1IK8 A CAX   
1360 C  CAY   . A1IK8 F .   ? 0.1623 0.3600 0.2849 -0.0236 0.0311  0.0299  205 A1IK8 A CAY   
1361 O  OBD   . A1IK8 F .   ? 0.1598 0.4227 0.2837 -0.0845 0.0444  0.0526  205 A1IK8 A OBD   
1362 C  CAZ   . A1IK8 F .   ? 0.1915 0.2938 0.3200 -0.0104 0.0158  -0.0151 205 A1IK8 A CAZ   
1363 C  CBA   . A1IK8 F .   ? 0.1115 0.3206 0.3083 -0.0235 -0.0132 0.0089  205 A1IK8 A CBA   
1364 C  CBB   . A1IK8 F .   ? 0.1312 0.2999 0.3037 -0.0601 0.0016  0.0244  205 A1IK8 A CBB   
1365 CL CLBC  . A1IK8 F .   ? 0.1798 0.3468 0.2918 -0.0512 0.0372  0.0342  205 A1IK8 A CLBC  
1366 C  CBI   . A1IK8 F .   ? 0.1529 0.3123 0.3482 -0.0564 0.0424  0.0644  205 A1IK8 A CBI   
1367 S  SBH   . A1IK8 F .   ? 0.1695 0.3273 0.3372 -0.0670 0.0354  0.0500  205 A1IK8 A SBH   
1368 C  CBG   . A1IK8 F .   ? 0.2839 0.2915 0.3314 -0.1033 -0.0092 0.0496  205 A1IK8 A CBG   
1369 N  NBF   . A1IK8 F .   ? 0.2037 0.2895 0.4126 -0.1182 0.0210  0.0210  205 A1IK8 A NBF   
1370 S  SAH   . A1IK8 F .   ? 0.3119 0.3391 0.3332 -0.1084 -0.0090 0.0431  205 A1IK8 A SAH   
1371 O  OAI   . A1IK8 F .   ? 0.3394 0.3487 0.3838 -0.0565 -0.0978 0.0416  205 A1IK8 A OAI   
1372 O  OBE   . A1IK8 F .   ? 0.3922 0.4097 0.4258 -0.1928 -0.0084 0.0103  205 A1IK8 A OBE   
1373 C  CAG   . A1IK8 F .   ? 0.2673 0.3026 0.3213 -0.0460 0.0513  0.0374  205 A1IK8 A CAG   
1374 C  CAF   . A1IK8 F .   ? 0.2690 0.4168 0.2323 -0.0088 0.0187  0.0708  205 A1IK8 A CAF   
1375 N  NAE   . A1IK8 F .   ? 0.2622 0.3462 0.3617 -0.0668 -0.0373 0.0695  205 A1IK8 A NAE   
1376 C  CAJ   . A1IK8 F .   ? 0.2407 0.3441 0.3801 -0.1191 0.0526  0.0755  205 A1IK8 A CAJ   
1377 C  CAC   . A1IK8 F .   ? 0.3049 0.3966 0.3871 -0.1042 -0.0233 0.1087  205 A1IK8 A CAC   
1378 C  CAD   . A1IK8 F .   ? 0.2920 0.4197 0.3452 -0.0973 -0.0138 0.0895  205 A1IK8 A CAD   
1379 N  NAK   . A1IK8 F .   ? 0.3374 0.3776 0.4400 -0.0726 -0.0422 0.0572  205 A1IK8 A NAK   
1380 C  CAL   . A1IK8 F .   ? 0.3327 0.3914 0.4515 -0.0621 -0.0121 -0.0229 205 A1IK8 A CAL   
1381 C  CAM   . A1IK8 F .   ? 0.4242 0.4271 0.5499 -0.0333 -0.0103 -0.0721 205 A1IK8 A CAM   
1382 C  CAN   . A1IK8 F .   ? 0.4124 0.3442 0.5567 -0.0976 -0.0368 -0.0865 205 A1IK8 A CAN   
1383 N  NAO   . A1IK8 F .   ? 0.3238 0.4046 0.5694 -0.0363 -0.0030 0.0037  205 A1IK8 A NAO   
1384 C  CAP   . A1IK8 F .   ? 0.4051 0.3671 0.6293 -0.0526 -0.0181 0.0475  205 A1IK8 A CAP   
1385 O  O     . HOH   G .   ? 0.2101 0.2565 0.2133 -0.0241 0.0500  0.0376  301 HOH   A O     
1386 O  O     . HOH   G .   ? 0.3906 0.5278 0.3264 0.0846  -0.0157 -0.0958 302 HOH   A O     
1387 O  O     . HOH   G .   ? 0.4548 0.4772 0.5411 0.1260  0.1204  0.0941  303 HOH   A O     
1388 O  O     . HOH   G .   ? 0.3218 0.5983 0.3217 -0.1488 -0.0070 -0.0666 304 HOH   A O     
1389 O  O     . HOH   G .   ? 0.2638 0.3739 0.2983 -0.0857 0.0668  0.0109  305 HOH   A O     
1390 O  O     . HOH   G .   ? 0.3527 0.4984 0.3799 0.1216  0.1302  0.1220  306 HOH   A O     
1391 O  O     . HOH   G .   ? 0.3333 0.4277 0.4655 0.0527  0.0115  0.0240  307 HOH   A O     
1392 O  O     . HOH   G .   ? 0.3595 0.4835 0.5339 0.0320  0.0794  0.0361  308 HOH   A O     
1393 O  O     . HOH   G .   ? 0.3782 0.3549 0.4306 -0.0006 0.0630  -0.0428 309 HOH   A O     
1394 O  O     . HOH   G .   ? 0.4490 0.3264 0.1805 -0.0179 0.0293  -0.0633 310 HOH   A O     
1395 O  O     . HOH   G .   ? 0.2539 0.3694 0.3382 0.0300  0.0277  0.0629  311 HOH   A O     
1396 O  O     . HOH   G .   ? 0.4082 0.4011 0.2234 -0.0333 0.0078  0.0585  312 HOH   A O     
1397 O  O     . HOH   G .   ? 0.4139 0.2826 0.3408 -0.0075 0.1506  -0.0095 313 HOH   A O     
1398 O  O     . HOH   G .   ? 0.4779 0.2918 0.3284 -0.0720 0.0745  0.0038  314 HOH   A O     
1399 O  O     . HOH   G .   ? 0.2510 0.3142 0.3594 -0.0487 0.0356  -0.0744 315 HOH   A O     
1400 O  O     . HOH   G .   ? 0.1833 0.3490 0.2761 -0.0135 0.0198  0.0187  316 HOH   A O     
1401 O  O     . HOH   G .   ? 0.4361 0.2727 0.3534 -0.0881 -0.0081 0.0249  317 HOH   A O     
1402 O  O     . HOH   G .   ? 0.4878 0.4386 0.3255 -0.1103 0.0222  -0.0941 318 HOH   A O     
1403 O  O     . HOH   G .   ? 0.2690 0.2467 0.2802 0.0114  0.0560  0.0059  319 HOH   A O     
1404 O  O     . HOH   G .   ? 0.4562 0.4375 0.4287 0.0074  -0.0459 -0.0633 320 HOH   A O     
1405 O  O     . HOH   G .   ? 0.4274 0.5720 0.5464 0.0172  -0.0283 0.0172  321 HOH   A O     
1406 O  O     . HOH   G .   ? 0.2630 0.3572 0.2495 0.0115  0.0133  -0.0621 322 HOH   A O     
1407 O  O     . HOH   G .   ? 0.3478 0.5417 0.5534 -0.1112 0.0735  -0.0437 323 HOH   A O     
1408 O  O     . HOH   G .   ? 0.2408 0.4330 0.5880 0.0748  -0.0095 0.0449  324 HOH   A O     
1409 O  O     . HOH   G .   ? 0.3960 0.3973 0.5093 0.0849  -0.0416 -0.1421 325 HOH   A O     
1410 O  O     . HOH   G .   ? 0.1336 0.2935 0.2734 -0.0009 0.0587  -0.0586 326 HOH   A O     
1411 O  O     . HOH   G .   ? 0.2034 0.3983 0.2221 0.0193  0.0326  0.0072  327 HOH   A O     
1412 O  O     . HOH   G .   ? 0.2459 0.4280 0.2473 -0.0611 0.0172  0.0156  328 HOH   A O     
1413 O  O     . HOH   G .   ? 0.5174 0.4554 0.4510 -0.0709 0.0762  0.0003  329 HOH   A O     
1414 O  O     . HOH   G .   ? 0.4211 0.3887 0.4005 -0.0390 -0.0372 -0.1490 330 HOH   A O     
1415 O  O     . HOH   G .   ? 0.3040 0.5183 0.4603 0.0352  0.0586  0.0112  331 HOH   A O     
1416 O  O     . HOH   G .   ? 0.2249 0.5511 0.4331 -0.0299 0.0046  0.0638  332 HOH   A O     
1417 O  O     . HOH   G .   ? 0.3451 0.4815 0.3564 0.0066  -0.0443 0.1082  333 HOH   A O     
1418 O  O     . HOH   G .   ? 0.1528 0.2405 0.3186 0.0028  0.0673  0.0617  334 HOH   A O     
1419 O  O     . HOH   G .   ? 0.2368 0.4786 0.2849 0.0869  0.0872  0.0935  335 HOH   A O     
1420 O  O     . HOH   G .   ? 0.2587 0.5424 0.4658 0.0553  -0.0722 -0.0122 336 HOH   A O     
1421 O  O     . HOH   G .   ? 0.3509 0.6438 0.4052 0.1209  0.0406  0.0016  337 HOH   A O     
1422 O  O     . HOH   G .   ? 0.2962 0.5724 0.3074 -0.0236 0.0720  0.0034  338 HOH   A O     
1423 O  O     . HOH   G .   ? 0.1818 0.5391 0.3461 0.0145  0.0188  -0.0457 339 HOH   A O     
1424 O  O     . HOH   G .   ? 0.5814 0.4052 0.5200 0.0054  0.1258  0.0296  340 HOH   A O     
1425 O  O     . HOH   G .   ? 0.3389 0.5714 0.3643 -0.0198 0.0123  -0.0579 341 HOH   A O     
1426 O  O     . HOH   G .   ? 0.5804 0.4123 0.2882 0.0780  0.0416  0.0461  342 HOH   A O     
1427 O  O     . HOH   G .   ? 0.6100 0.4879 0.2622 0.1168  0.0757  0.0105  343 HOH   A O     
1428 O  O     . HOH   G .   ? 0.1871 0.5706 0.2842 -0.0166 0.0073  -0.0176 344 HOH   A O     
1429 O  O     . HOH   G .   ? 0.5615 0.4548 0.4987 -0.0546 -0.0913 0.0193  345 HOH   A O     
1430 O  O     . HOH   G .   ? 0.1787 0.4157 0.3088 0.0455  -0.0415 0.0935  346 HOH   A O     
1431 O  O     . HOH   G .   ? 0.5069 0.5626 0.4826 -0.0240 0.1976  -0.1529 347 HOH   A O     
1432 O  O     . HOH   G .   ? 0.4064 0.3977 0.5706 0.0052  -0.0185 -0.0400 348 HOH   A O     
1433 O  O     . HOH   G .   ? 0.3872 0.3081 0.4949 0.1748  0.0611  0.0150  349 HOH   A O     
1434 O  O     . HOH   G .   ? 0.4203 0.2798 0.4376 -0.0584 0.0448  -0.0403 350 HOH   A O     
1435 O  O     . HOH   G .   ? 0.2212 0.4726 0.3261 0.0235  0.0619  -0.0383 351 HOH   A O     
1436 O  O     . HOH   G .   ? 0.2934 0.2530 0.2819 0.0158  0.0700  0.0101  352 HOH   A O     
1437 O  O     . HOH   G .   ? 0.3012 0.3834 0.3671 -0.0858 0.0766  0.0046  353 HOH   A O     
1438 O  O     . HOH   G .   ? 0.2693 0.5373 0.5337 -0.0854 0.0104  -0.0013 354 HOH   A O     
1439 O  O     . HOH   G .   ? 0.4966 0.4420 0.3942 0.0893  0.0190  -0.0186 355 HOH   A O     
1440 O  O     . HOH   G .   ? 0.3942 0.4941 0.4315 -0.2147 0.0217  0.0197  356 HOH   A O     
1441 O  O     . HOH   G .   ? 0.3217 0.3924 0.3425 0.0734  0.0347  -0.0763 357 HOH   A O     
1442 O  O     . HOH   G .   ? 0.3030 0.2578 0.2974 -0.0760 0.0273  0.0017  358 HOH   A O     
1443 O  O     . HOH   G .   ? 0.2966 0.4537 0.4405 -0.0047 0.0538  -0.0829 359 HOH   A O     
1444 O  O     . HOH   G .   ? 0.3247 0.3958 0.4319 -0.1626 0.0667  -0.0729 360 HOH   A O     
1445 O  O     . HOH   G .   ? 0.3340 0.4049 0.4451 0.0261  -0.0024 0.0517  361 HOH   A O     
1446 O  O     . HOH   G .   ? 0.3109 0.3016 0.2643 -0.0514 0.0756  -0.0693 362 HOH   A O     
1447 O  O     . HOH   G .   ? 0.4178 0.6672 0.4726 0.0380  0.1313  0.0625  363 HOH   A O     
1448 O  O     . HOH   G .   ? 0.5321 0.3916 0.3299 0.0233  0.0164  0.0080  364 HOH   A O     
1449 O  O     . HOH   G .   ? 0.4361 0.2947 0.4964 -0.0409 -0.0523 0.0448  365 HOH   A O     
1450 O  O     . HOH   G .   ? 0.3241 0.3291 0.3441 0.0205  -0.0279 -0.0177 366 HOH   A O     
1451 O  O     . HOH   G .   ? 0.2936 0.3928 0.3180 0.0156  0.0322  -0.0123 367 HOH   A O     
1452 O  O     . HOH   G .   ? 0.6224 0.3964 0.4627 -0.0230 0.0694  -0.0029 368 HOH   A O     
1453 O  O     . HOH   G .   ? 0.2527 0.6631 0.3380 -0.0348 0.0584  -0.0321 369 HOH   A O     
1454 O  O     . HOH   G .   ? 0.3617 0.3693 0.4834 -0.0215 -0.0486 0.0283  370 HOH   A O     
1455 O  O     . HOH   G .   ? 0.3344 0.5951 0.5261 0.1699  -0.0797 -0.1611 371 HOH   A O     
1456 O  O     . HOH   G .   ? 0.2769 0.5610 0.2574 0.0147  0.0206  -0.0295 372 HOH   A O     
1457 O  O     . HOH   G .   ? 0.3413 0.5354 0.4374 0.0149  0.0181  -0.0526 373 HOH   A O     
1458 O  O     . HOH   G .   ? 0.3164 0.5247 0.4452 -0.0334 0.0331  -0.0985 374 HOH   A O     
1459 O  O     . HOH   G .   ? 0.2601 0.4433 0.4016 0.0391  0.0764  -0.0310 375 HOH   A O     
1460 O  O     . HOH   G .   ? 0.5604 0.4878 0.4652 0.0139  0.0047  0.0436  376 HOH   A O     
1461 O  O     . HOH   G .   ? 0.5237 0.7734 0.3302 -0.0034 0.0458  0.0696  377 HOH   A O     
# 
