data_9GGW
# 
_entry.id   9GGW 
# 
_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   9GGW         pdb_00009ggw 10.2210/pdb9ggw/pdb 
WWPDB D_1292140436 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-04-16 ? 
2 'Structure model' 1 1 2025-05-21 ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' citation        
2 2 'Structure model' citation_author 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 2 'Structure model' '_citation.journal_volume'          
2 2 'Structure model' '_citation.page_first'              
3 2 'Structure model' '_citation.page_last'               
4 2 'Structure model' '_citation_author.identifier_ORCID' 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9GGW 
_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 . 9G4B unspecified 
PDB . 9G0Y unspecified 
PDB . 9GH2 unspecified 
PDB . 9GH1 unspecified 
PDB . 9GH0 unspecified 
PDB . 9GGZ unspecified 
PDB . 9GGY unspecified 
PDB . 9GGX unspecified 
PDB . 9GGV unspecified 
PDB . 9GGU unspecified 
PDB . 9GGT unspecified 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              alexander.schuettelkopf@cancer.org.uk 
_pdbx_contact_author.name_first         Alexander 
_pdbx_contact_author.name_last          Schuettelkopf 
_pdbx_contact_author.name_mi            W. 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-9424-8730 
# 
_audit_author.name               'Schuettelkopf, A.W.' 
_audit_author.pdbx_ordinal       1 
_audit_author.identifier_ORCID   0000-0002-9424-8730 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            J.Med.Chem. 
_citation.journal_id_ASTM           JMCMAR 
_citation.journal_id_CSD            0151 
_citation.journal_id_ISSN           0022-2623 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            68 
_citation.language                  ? 
_citation.page_first                9129 
_citation.page_last                 9161 
_citation.title                     
'Reversible Small Molecule Multivariant Ras Inhibitors Display Tunable Affinity for the Active and Inactive Forms of Ras.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1021/acs.jmedchem.4c02929 
_citation.pdbx_database_id_PubMed   40162713 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Parry, C.W.'        1  ? 
primary 'Pellicano, F.'      2  ? 
primary 'Schuttelkopf, A.W.' 3  ? 
primary 'Beyer, K.S.'        4  ? 
primary 'Bower, J.'          5  ? 
primary 'Bryson, A.'         6  ? 
primary 'Cameron, K.'        7  ? 
primary 'Cerutti, N.M.'      8  ? 
primary 'Clark, J.P.'        9  ? 
primary 'Davidson, S.C.'     10 ? 
primary 'Davies, K.'         11 ? 
primary 'Drysdale, M.J.'     12 ? 
primary 'Engelman, J.'       13 ? 
primary 'Estevan-Barber, A.' 14 ? 
primary 'Gohlke, A.'         15 ? 
primary 'Gray, C.H.'         16 ? 
primary 'Guthy, D.A.'        17 ? 
primary 'Hong, M.'           18 ? 
primary 'Hopkins, A.'        19 ? 
primary 'Hutchinson, L.D.'   20 ? 
primary 'Konczal, J.'        21 ? 
primary 'Maira, M.'          22 ? 
primary 'McArthur, D.'       23 ? 
primary 'Mezna, M.'          24 ? 
primary 'McKinnon, H.'       25 ? 
primary 'Nepravishta, R.'    26 ? 
primary 'Ostermann, N.'      27 ? 
primary 'Pasquali, C.C.'     28 ? 
primary 'Pollock, K.'        29 ? 
primary 'Pugliese, A.'       30 ? 
primary 'Rooney, N.'         31 ? 
primary 'Schmiedeberg, N.'   32 ? 
primary 'Shaw, P.'           33 ? 
primary 'Velez-Vega, C.'     34 ? 
primary 'West, C.'           35 ? 
primary 'West, R.'           36 ? 
primary 'Zecri, F.'          37 ? 
primary 'Taylor, J.B.'       38 ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'GTPase KRas' 19607.078 2   3.6.5.2 C118S ? ? 
2 non-polymer syn "GUANOSINE-5'-DIPHOSPHATE" 443.201   2   ?       ?     ? ? 
3 non-polymer syn 'MAGNESIUM ION' 24.305    2   ?       ?     ? ? 
4 non-polymer syn 
;11-(4-aminocyclohexyl)-16-chloro-1,15-dihydroxy-10,10-dioxo-10lambda6-thia-2,11lambda6-diaza-1lambda6,15lambda6-diphospha-3-phosphoniapentacyclo[7.5.1.01,15.03,15.013,15]hexadecan-12-one
;
566.112   2   ?       ?     ? ? 
5 non-polymer syn 1,2-ETHANEDIOL 62.068    2   ?       ?     ? ? 
6 water       nat water 18.015    130 ?       ?     ? ? 
# 
_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,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 "GUANOSINE-5'-DIPHOSPHATE" GDP   
3 'MAGNESIUM ION' MG    
4 
;11-(4-aminocyclohexyl)-16-chloro-1,15-dihydroxy-10,10-dioxo-10lambda6-thia-2,11lambda6-diaza-1lambda6,15lambda6-diphospha-3-phosphoniapentacyclo[7.5.1.01,15.03,15.013,15]hexadecan-12-one
;
A1ILA 
5 1,2-ETHANEDIOL EDO   
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 
A1ILA non-polymer         . 
;11-(4-aminocyclohexyl)-16-chloro-1,15-dihydroxy-10,10-dioxo-10lambda6-thia-2,11lambda6-diaza-1lambda6,15lambda6-diphospha-3-phosphoniapentacyclo[7.5.1.01,15.03,15.013,15]hexadecan-12-one
;
?                 'C25 H30 Cl N4 O5 S2 1' 566.112 
ALA   'L-peptide linking' y ALANINE ?                 'C3 H7 N O2'            89.093  
ARG   'L-peptide linking' y ARGININE ?                 'C6 H15 N4 O2 1'        175.209 
ASN   'L-peptide linking' y ASPARAGINE ?                 'C4 H8 N2 O3'           132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID' ?                 'C4 H7 N O4'            133.103 
CYS   'L-peptide linking' y CYSTEINE ?                 'C3 H7 N O2 S'          121.158 
EDO   non-polymer         . 1,2-ETHANEDIOL 'ETHYLENE GLYCOL' 'C2 H6 O2'              62.068  
GDP   'RNA linking'       n "GUANOSINE-5'-DIPHOSPHATE" ?                 'C10 H15 N5 O11 P2'     443.201 
GLN   'L-peptide linking' y GLUTAMINE ?                 'C5 H10 N2 O3'          146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID' ?                 'C5 H9 N O4'            147.129 
GLY   'peptide linking'   y GLYCINE ?                 'C2 H5 N O2'            75.067  
HIS   'L-peptide linking' y HISTIDINE ?                 'C6 H10 N3 O2 1'        156.162 
HOH   non-polymer         . WATER ?                 'H2 O'                  18.015  
ILE   'L-peptide linking' y ISOLEUCINE ?                 'C6 H13 N O2'           131.173 
LEU   'L-peptide linking' y LEUCINE ?                 'C6 H13 N O2'           131.173 
LYS   'L-peptide linking' y LYSINE ?                 'C6 H15 N2 O2 1'        147.195 
MET   'L-peptide linking' y METHIONINE ?                 'C5 H11 N O2 S'         149.211 
MG    non-polymer         . 'MAGNESIUM ION' ?                 'Mg 2'                  24.305  
PHE   'L-peptide linking' y PHENYLALANINE ?                 'C9 H11 N O2'           165.189 
PRO   'L-peptide linking' y PROLINE ?                 'C5 H9 N O2'            115.130 
SER   'L-peptide linking' y SERINE ?                 'C3 H7 N O3'            105.093 
THR   'L-peptide linking' y THREONINE ?                 'C4 H9 N O3'            119.119 
TYR   'L-peptide linking' y TYROSINE ?                 'C9 H11 N O3'           181.189 
VAL   'L-peptide linking' y VALINE ?                 'C5 H11 N O2'           117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   GLY 1   -2  ?   ?   ?   A . n 
A 1 2   GLY 2   -1  ?   ?   ?   A . n 
A 1 3   SER 3   0   0   SER SER A . n 
A 1 4   MET 4   1   1   MET MET A . n 
A 1 5   THR 5   2   2   THR THR A . n 
A 1 6   GLU 6   3   3   GLU GLU A . n 
A 1 7   TYR 7   4   4   TYR TYR A . n 
A 1 8   LYS 8   5   5   LYS LYS A . n 
A 1 9   LEU 9   6   6   LEU LEU A . n 
A 1 10  VAL 10  7   7   VAL VAL A . n 
A 1 11  VAL 11  8   8   VAL VAL A . n 
A 1 12  VAL 12  9   9   VAL VAL A . n 
A 1 13  GLY 13  10  10  GLY GLY A . n 
A 1 14  ALA 14  11  11  ALA ALA A . n 
A 1 15  GLY 15  12  12  GLY GLY A . n 
A 1 16  GLY 16  13  13  GLY GLY A . n 
A 1 17  VAL 17  14  14  VAL VAL A . n 
A 1 18  GLY 18  15  15  GLY GLY A . n 
A 1 19  LYS 19  16  16  LYS LYS A . n 
A 1 20  SER 20  17  17  SER SER A . n 
A 1 21  ALA 21  18  18  ALA ALA A . n 
A 1 22  LEU 22  19  19  LEU LEU A . n 
A 1 23  THR 23  20  20  THR THR A . n 
A 1 24  ILE 24  21  21  ILE ILE A . n 
A 1 25  GLN 25  22  22  GLN GLN A . n 
A 1 26  LEU 26  23  23  LEU LEU A . n 
A 1 27  ILE 27  24  24  ILE ILE A . n 
A 1 28  GLN 28  25  25  GLN GLN A . n 
A 1 29  ASN 29  26  26  ASN ASN A . n 
A 1 30  HIS 30  27  27  HIS HIS A . n 
A 1 31  PHE 31  28  28  PHE PHE A . n 
A 1 32  VAL 32  29  29  VAL VAL A . n 
A 1 33  ASP 33  30  30  ASP ASP A . n 
A 1 34  GLU 34  31  31  GLU GLU A . n 
A 1 35  TYR 35  32  32  TYR TYR A . n 
A 1 36  ASP 36  33  33  ASP ASP A . n 
A 1 37  PRO 37  34  34  PRO PRO A . n 
A 1 38  THR 38  35  35  THR THR A . n 
A 1 39  ILE 39  36  36  ILE ILE A . n 
A 1 40  GLU 40  37  37  GLU GLU A . n 
A 1 41  ASP 41  38  38  ASP ASP A . n 
A 1 42  SER 42  39  39  SER SER A . n 
A 1 43  TYR 43  40  40  TYR TYR A . n 
A 1 44  ARG 44  41  41  ARG ARG A . n 
A 1 45  LYS 45  42  42  LYS LYS A . n 
A 1 46  GLN 46  43  43  GLN GLN A . n 
A 1 47  VAL 47  44  44  VAL VAL A . n 
A 1 48  VAL 48  45  45  VAL VAL A . n 
A 1 49  ILE 49  46  46  ILE ILE A . n 
A 1 50  ASP 50  47  47  ASP ASP A . n 
A 1 51  GLY 51  48  48  GLY GLY A . n 
A 1 52  GLU 52  49  49  GLU GLU A . n 
A 1 53  THR 53  50  50  THR THR A . n 
A 1 54  CYS 54  51  51  CYS CYS A . n 
A 1 55  LEU 55  52  52  LEU LEU A . n 
A 1 56  LEU 56  53  53  LEU LEU A . n 
A 1 57  ASP 57  54  54  ASP ASP A . n 
A 1 58  ILE 58  55  55  ILE ILE A . n 
A 1 59  LEU 59  56  56  LEU LEU A . n 
A 1 60  ASP 60  57  57  ASP ASP A . n 
A 1 61  THR 61  58  58  THR THR A . n 
A 1 62  ALA 62  59  59  ALA ALA A . n 
A 1 63  GLY 63  60  60  GLY GLY A . n 
A 1 64  GLN 64  61  61  GLN GLN A . n 
A 1 65  GLU 65  62  62  GLU GLU A . n 
A 1 66  GLU 66  63  63  GLU GLU A . n 
A 1 67  TYR 67  64  64  TYR TYR A . n 
A 1 68  SER 68  65  65  SER SER A . n 
A 1 69  ALA 69  66  66  ALA ALA A . n 
A 1 70  MET 70  67  67  MET MET A . n 
A 1 71  ARG 71  68  68  ARG ARG A . n 
A 1 72  ASP 72  69  69  ASP ASP A . n 
A 1 73  GLN 73  70  70  GLN GLN A . n 
A 1 74  TYR 74  71  71  TYR TYR A . n 
A 1 75  MET 75  72  72  MET MET A . n 
A 1 76  ARG 76  73  73  ARG ARG A . n 
A 1 77  THR 77  74  74  THR THR A . n 
A 1 78  GLY 78  75  75  GLY GLY A . n 
A 1 79  GLU 79  76  76  GLU GLU A . n 
A 1 80  GLY 80  77  77  GLY GLY A . n 
A 1 81  PHE 81  78  78  PHE PHE A . n 
A 1 82  LEU 82  79  79  LEU LEU A . n 
A 1 83  CYS 83  80  80  CYS CYS A . n 
A 1 84  VAL 84  81  81  VAL VAL A . n 
A 1 85  PHE 85  82  82  PHE PHE A . n 
A 1 86  ALA 86  83  83  ALA ALA A . n 
A 1 87  ILE 87  84  84  ILE ILE A . n 
A 1 88  ASN 88  85  85  ASN ASN A . n 
A 1 89  ASN 89  86  86  ASN ASN A . n 
A 1 90  THR 90  87  87  THR THR A . n 
A 1 91  LYS 91  88  88  LYS LYS A . n 
A 1 92  SER 92  89  89  SER SER A . n 
A 1 93  PHE 93  90  90  PHE PHE A . n 
A 1 94  GLU 94  91  91  GLU GLU A . n 
A 1 95  ASP 95  92  92  ASP ASP A . n 
A 1 96  ILE 96  93  93  ILE ILE A . n 
A 1 97  HIS 97  94  94  HIS HIS A . n 
A 1 98  HIS 98  95  95  HIS HIS A . n 
A 1 99  TYR 99  96  96  TYR TYR A . n 
A 1 100 ARG 100 97  97  ARG ARG A . n 
A 1 101 GLU 101 98  98  GLU GLU A . n 
A 1 102 GLN 102 99  99  GLN GLN A . n 
A 1 103 ILE 103 100 100 ILE ILE A . n 
A 1 104 LYS 104 101 101 LYS LYS A . n 
A 1 105 ARG 105 102 102 ARG ARG A . n 
A 1 106 VAL 106 103 103 VAL VAL A . n 
A 1 107 LYS 107 104 104 LYS LYS A . n 
A 1 108 ASP 108 105 105 ASP ASP A . n 
A 1 109 SER 109 106 106 SER SER A . n 
A 1 110 GLU 110 107 107 GLU GLU A . n 
A 1 111 ASP 111 108 108 ASP ASP A . n 
A 1 112 VAL 112 109 109 VAL VAL A . n 
A 1 113 PRO 113 110 110 PRO PRO A . n 
A 1 114 MET 114 111 111 MET MET A . n 
A 1 115 VAL 115 112 112 VAL VAL A . n 
A 1 116 LEU 116 113 113 LEU LEU A . n 
A 1 117 VAL 117 114 114 VAL VAL A . n 
A 1 118 GLY 118 115 115 GLY GLY A . n 
A 1 119 ASN 119 116 116 ASN ASN A . n 
A 1 120 LYS 120 117 117 LYS LYS A . n 
A 1 121 SER 121 118 118 SER SER A . n 
A 1 122 ASP 122 119 119 ASP ASP A . n 
A 1 123 LEU 123 120 120 LEU LEU A . n 
A 1 124 PRO 124 121 121 PRO PRO A . n 
A 1 125 SER 125 122 122 SER SER A . n 
A 1 126 ARG 126 123 123 ARG ARG A . n 
A 1 127 THR 127 124 124 THR THR A . n 
A 1 128 VAL 128 125 125 VAL VAL A . n 
A 1 129 ASP 129 126 126 ASP ASP A . n 
A 1 130 THR 130 127 127 THR THR A . n 
A 1 131 LYS 131 128 128 LYS LYS A . n 
A 1 132 GLN 132 129 129 GLN GLN A . n 
A 1 133 ALA 133 130 130 ALA ALA A . n 
A 1 134 GLN 134 131 131 GLN GLN A . n 
A 1 135 ASP 135 132 132 ASP ASP A . n 
A 1 136 LEU 136 133 133 LEU LEU A . n 
A 1 137 ALA 137 134 134 ALA ALA A . n 
A 1 138 ARG 138 135 135 ARG ARG A . n 
A 1 139 SER 139 136 136 SER SER A . n 
A 1 140 TYR 140 137 137 TYR TYR A . n 
A 1 141 GLY 141 138 138 GLY GLY A . n 
A 1 142 ILE 142 139 139 ILE ILE A . n 
A 1 143 PRO 143 140 140 PRO PRO A . n 
A 1 144 PHE 144 141 141 PHE PHE A . n 
A 1 145 ILE 145 142 142 ILE ILE A . n 
A 1 146 GLU 146 143 143 GLU GLU A . n 
A 1 147 THR 147 144 144 THR THR A . n 
A 1 148 SER 148 145 145 SER SER A . n 
A 1 149 ALA 149 146 146 ALA ALA A . n 
A 1 150 LYS 150 147 147 LYS LYS A . n 
A 1 151 THR 151 148 148 THR THR A . n 
A 1 152 ARG 152 149 149 ARG ARG A . n 
A 1 153 GLN 153 150 150 GLN GLN A . n 
A 1 154 ARG 154 151 151 ARG ARG A . n 
A 1 155 VAL 155 152 152 VAL VAL A . n 
A 1 156 GLU 156 153 153 GLU GLU A . n 
A 1 157 ASP 157 154 154 ASP ASP A . n 
A 1 158 ALA 158 155 155 ALA ALA A . n 
A 1 159 PHE 159 156 156 PHE PHE A . n 
A 1 160 TYR 160 157 157 TYR TYR A . n 
A 1 161 THR 161 158 158 THR THR A . n 
A 1 162 LEU 162 159 159 LEU LEU A . n 
A 1 163 VAL 163 160 160 VAL VAL A . n 
A 1 164 ARG 164 161 161 ARG ARG A . n 
A 1 165 GLU 165 162 162 GLU GLU A . n 
A 1 166 ILE 166 163 163 ILE ILE A . n 
A 1 167 ARG 167 164 164 ARG ARG A . n 
A 1 168 GLN 168 165 165 GLN GLN A . n 
A 1 169 TYR 169 166 166 TYR TYR A . n 
A 1 170 ARG 170 167 167 ARG ARG A . n 
A 1 171 LEU 171 168 168 LEU LEU A . n 
A 1 172 LYS 172 169 ?   ?   ?   A . n 
B 1 1   GLY 1   -2  ?   ?   ?   B . n 
B 1 2   GLY 2   -1  ?   ?   ?   B . n 
B 1 3   SER 3   0   ?   ?   ?   B . n 
B 1 4   MET 4   1   1   MET MET B . n 
B 1 5   THR 5   2   2   THR THR B . n 
B 1 6   GLU 6   3   3   GLU GLU B . n 
B 1 7   TYR 7   4   4   TYR TYR B . n 
B 1 8   LYS 8   5   5   LYS LYS B . n 
B 1 9   LEU 9   6   6   LEU LEU B . n 
B 1 10  VAL 10  7   7   VAL VAL B . n 
B 1 11  VAL 11  8   8   VAL VAL B . n 
B 1 12  VAL 12  9   9   VAL VAL B . n 
B 1 13  GLY 13  10  10  GLY GLY B . n 
B 1 14  ALA 14  11  11  ALA ALA B . n 
B 1 15  GLY 15  12  12  GLY GLY B . n 
B 1 16  GLY 16  13  13  GLY GLY B . n 
B 1 17  VAL 17  14  14  VAL VAL B . n 
B 1 18  GLY 18  15  15  GLY GLY B . n 
B 1 19  LYS 19  16  16  LYS LYS B . n 
B 1 20  SER 20  17  17  SER SER B . n 
B 1 21  ALA 21  18  18  ALA ALA B . n 
B 1 22  LEU 22  19  19  LEU LEU B . n 
B 1 23  THR 23  20  20  THR THR B . n 
B 1 24  ILE 24  21  21  ILE ILE B . n 
B 1 25  GLN 25  22  22  GLN GLN B . n 
B 1 26  LEU 26  23  23  LEU LEU B . n 
B 1 27  ILE 27  24  24  ILE ILE B . n 
B 1 28  GLN 28  25  25  GLN GLN B . n 
B 1 29  ASN 29  26  26  ASN ASN B . n 
B 1 30  HIS 30  27  27  HIS HIS B . n 
B 1 31  PHE 31  28  28  PHE PHE B . n 
B 1 32  VAL 32  29  29  VAL VAL B . n 
B 1 33  ASP 33  30  30  ASP ASP B . n 
B 1 34  GLU 34  31  31  GLU GLU B . n 
B 1 35  TYR 35  32  32  TYR TYR B . n 
B 1 36  ASP 36  33  33  ASP ASP B . n 
B 1 37  PRO 37  34  34  PRO PRO B . n 
B 1 38  THR 38  35  35  THR THR B . n 
B 1 39  ILE 39  36  36  ILE ILE B . n 
B 1 40  GLU 40  37  37  GLU GLU B . n 
B 1 41  ASP 41  38  38  ASP ASP B . n 
B 1 42  SER 42  39  39  SER SER B . n 
B 1 43  TYR 43  40  40  TYR TYR B . n 
B 1 44  ARG 44  41  41  ARG ARG B . n 
B 1 45  LYS 45  42  42  LYS LYS B . n 
B 1 46  GLN 46  43  43  GLN GLN B . n 
B 1 47  VAL 47  44  44  VAL VAL B . n 
B 1 48  VAL 48  45  45  VAL VAL B . n 
B 1 49  ILE 49  46  46  ILE ILE B . n 
B 1 50  ASP 50  47  47  ASP ASP B . n 
B 1 51  GLY 51  48  48  GLY GLY B . n 
B 1 52  GLU 52  49  49  GLU GLU B . n 
B 1 53  THR 53  50  50  THR THR B . n 
B 1 54  CYS 54  51  51  CYS CYS B . n 
B 1 55  LEU 55  52  52  LEU LEU B . n 
B 1 56  LEU 56  53  53  LEU LEU B . n 
B 1 57  ASP 57  54  54  ASP ASP B . n 
B 1 58  ILE 58  55  55  ILE ILE B . n 
B 1 59  LEU 59  56  56  LEU LEU B . n 
B 1 60  ASP 60  57  57  ASP ASP B . n 
B 1 61  THR 61  58  58  THR THR B . n 
B 1 62  ALA 62  59  59  ALA ALA B . n 
B 1 63  GLY 63  60  ?   ?   ?   B . n 
B 1 64  GLN 64  61  ?   ?   ?   B . n 
B 1 65  GLU 65  62  ?   ?   ?   B . n 
B 1 66  GLU 66  63  ?   ?   ?   B . n 
B 1 67  TYR 67  64  64  TYR TYR B . n 
B 1 68  SER 68  65  65  SER SER B . n 
B 1 69  ALA 69  66  66  ALA ALA B . n 
B 1 70  MET 70  67  67  MET MET B . n 
B 1 71  ARG 71  68  68  ARG ARG B . n 
B 1 72  ASP 72  69  69  ASP ASP B . n 
B 1 73  GLN 73  70  70  GLN GLN B . n 
B 1 74  TYR 74  71  71  TYR TYR B . n 
B 1 75  MET 75  72  72  MET MET B . n 
B 1 76  ARG 76  73  73  ARG ARG B . n 
B 1 77  THR 77  74  74  THR THR B . n 
B 1 78  GLY 78  75  75  GLY GLY B . n 
B 1 79  GLU 79  76  76  GLU GLU B . n 
B 1 80  GLY 80  77  77  GLY GLY B . n 
B 1 81  PHE 81  78  78  PHE PHE B . n 
B 1 82  LEU 82  79  79  LEU LEU B . n 
B 1 83  CYS 83  80  80  CYS CYS B . n 
B 1 84  VAL 84  81  81  VAL VAL B . n 
B 1 85  PHE 85  82  82  PHE PHE B . n 
B 1 86  ALA 86  83  83  ALA ALA B . n 
B 1 87  ILE 87  84  84  ILE ILE B . n 
B 1 88  ASN 88  85  85  ASN ASN B . n 
B 1 89  ASN 89  86  86  ASN ASN B . n 
B 1 90  THR 90  87  87  THR THR B . n 
B 1 91  LYS 91  88  88  LYS LYS B . n 
B 1 92  SER 92  89  89  SER SER B . n 
B 1 93  PHE 93  90  90  PHE PHE B . n 
B 1 94  GLU 94  91  91  GLU GLU B . n 
B 1 95  ASP 95  92  92  ASP ASP B . n 
B 1 96  ILE 96  93  93  ILE ILE B . n 
B 1 97  HIS 97  94  94  HIS HIS B . n 
B 1 98  HIS 98  95  95  HIS HIS B . n 
B 1 99  TYR 99  96  96  TYR TYR B . n 
B 1 100 ARG 100 97  97  ARG ARG B . n 
B 1 101 GLU 101 98  98  GLU GLU B . n 
B 1 102 GLN 102 99  99  GLN GLN B . n 
B 1 103 ILE 103 100 100 ILE ILE B . n 
B 1 104 LYS 104 101 101 LYS LYS B . n 
B 1 105 ARG 105 102 102 ARG ARG B . n 
B 1 106 VAL 106 103 103 VAL VAL B . n 
B 1 107 LYS 107 104 104 LYS LYS B . n 
B 1 108 ASP 108 105 105 ASP ASP B . n 
B 1 109 SER 109 106 106 SER SER B . n 
B 1 110 GLU 110 107 107 GLU GLU B . n 
B 1 111 ASP 111 108 108 ASP ASP B . n 
B 1 112 VAL 112 109 109 VAL VAL B . n 
B 1 113 PRO 113 110 110 PRO PRO B . n 
B 1 114 MET 114 111 111 MET MET B . n 
B 1 115 VAL 115 112 112 VAL VAL B . n 
B 1 116 LEU 116 113 113 LEU LEU B . n 
B 1 117 VAL 117 114 114 VAL VAL B . n 
B 1 118 GLY 118 115 115 GLY GLY B . n 
B 1 119 ASN 119 116 116 ASN ASN B . n 
B 1 120 LYS 120 117 117 LYS LYS B . n 
B 1 121 SER 121 118 118 SER SER B . n 
B 1 122 ASP 122 119 119 ASP ASP B . n 
B 1 123 LEU 123 120 120 LEU LEU B . n 
B 1 124 PRO 124 121 121 PRO PRO B . n 
B 1 125 SER 125 122 122 SER SER B . n 
B 1 126 ARG 126 123 123 ARG ARG B . n 
B 1 127 THR 127 124 124 THR THR B . n 
B 1 128 VAL 128 125 125 VAL VAL B . n 
B 1 129 ASP 129 126 126 ASP ASP B . n 
B 1 130 THR 130 127 127 THR THR B . n 
B 1 131 LYS 131 128 128 LYS LYS B . n 
B 1 132 GLN 132 129 129 GLN GLN B . n 
B 1 133 ALA 133 130 130 ALA ALA B . n 
B 1 134 GLN 134 131 131 GLN GLN B . n 
B 1 135 ASP 135 132 132 ASP ASP B . n 
B 1 136 LEU 136 133 133 LEU LEU B . n 
B 1 137 ALA 137 134 134 ALA ALA B . n 
B 1 138 ARG 138 135 135 ARG ARG B . n 
B 1 139 SER 139 136 136 SER SER B . n 
B 1 140 TYR 140 137 137 TYR TYR B . n 
B 1 141 GLY 141 138 138 GLY GLY B . n 
B 1 142 ILE 142 139 139 ILE ILE B . n 
B 1 143 PRO 143 140 140 PRO PRO B . n 
B 1 144 PHE 144 141 141 PHE PHE B . n 
B 1 145 ILE 145 142 142 ILE ILE B . n 
B 1 146 GLU 146 143 143 GLU GLU B . n 
B 1 147 THR 147 144 144 THR THR B . n 
B 1 148 SER 148 145 145 SER SER B . n 
B 1 149 ALA 149 146 146 ALA ALA B . n 
B 1 150 LYS 150 147 147 LYS LYS B . n 
B 1 151 THR 151 148 148 THR THR B . n 
B 1 152 ARG 152 149 149 ARG ARG B . n 
B 1 153 GLN 153 150 150 GLN GLN B . n 
B 1 154 ARG 154 151 151 ARG ARG B . n 
B 1 155 VAL 155 152 152 VAL VAL B . n 
B 1 156 GLU 156 153 153 GLU GLU B . n 
B 1 157 ASP 157 154 154 ASP ASP B . n 
B 1 158 ALA 158 155 155 ALA ALA B . n 
B 1 159 PHE 159 156 156 PHE PHE B . n 
B 1 160 TYR 160 157 157 TYR TYR B . n 
B 1 161 THR 161 158 158 THR THR B . n 
B 1 162 LEU 162 159 159 LEU LEU B . n 
B 1 163 VAL 163 160 160 VAL VAL B . n 
B 1 164 ARG 164 161 161 ARG ARG B . n 
B 1 165 GLU 165 162 162 GLU GLU B . n 
B 1 166 ILE 166 163 163 ILE ILE B . n 
B 1 167 ARG 167 164 164 ARG ARG B . n 
B 1 168 GLN 168 165 165 GLN GLN B . n 
B 1 169 TYR 169 166 166 TYR TYR B . n 
B 1 170 ARG 170 167 167 ARG ARG B . n 
B 1 171 LEU 171 168 168 LEU LEU B . n 
B 1 172 LYS 172 169 169 LYS LYS B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1ILA 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1ILA 
_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 
C 2 GDP   1  201 1000 GDP   GDP A . 
D 3 MG    1  202 1001 MG    MG  A . 
E 4 A1ILA 1  203 1    A1ILA DRG A . 
F 5 EDO   1  204 1    EDO   EDO A . 
G 2 GDP   1  201 1000 GDP   GDP B . 
H 3 MG    1  202 1001 MG    MG  B . 
I 4 A1ILA 1  203 2    A1ILA DRG B . 
J 5 EDO   1  204 2    EDO   EDO B . 
K 6 HOH   1  301 31   HOH   HOH A . 
K 6 HOH   2  302 236  HOH   HOH A . 
K 6 HOH   3  303 274  HOH   HOH A . 
K 6 HOH   4  304 131  HOH   HOH A . 
K 6 HOH   5  305 132  HOH   HOH A . 
K 6 HOH   6  306 122  HOH   HOH A . 
K 6 HOH   7  307 111  HOH   HOH A . 
K 6 HOH   8  308 63   HOH   HOH A . 
K 6 HOH   9  309 30   HOH   HOH A . 
K 6 HOH   10 310 113  HOH   HOH A . 
K 6 HOH   11 311 162  HOH   HOH A . 
K 6 HOH   12 312 13   HOH   HOH A . 
K 6 HOH   13 313 238  HOH   HOH A . 
K 6 HOH   14 314 239  HOH   HOH A . 
K 6 HOH   15 315 6    HOH   HOH A . 
K 6 HOH   16 316 169  HOH   HOH A . 
K 6 HOH   17 317 50   HOH   HOH A . 
K 6 HOH   18 318 130  HOH   HOH A . 
K 6 HOH   19 319 264  HOH   HOH A . 
K 6 HOH   20 320 11   HOH   HOH A . 
K 6 HOH   21 321 249  HOH   HOH A . 
K 6 HOH   22 322 240  HOH   HOH A . 
K 6 HOH   23 323 280  HOH   HOH A . 
K 6 HOH   24 324 242  HOH   HOH A . 
K 6 HOH   25 325 84   HOH   HOH A . 
K 6 HOH   26 326 51   HOH   HOH A . 
K 6 HOH   27 327 241  HOH   HOH A . 
K 6 HOH   28 328 175  HOH   HOH A . 
K 6 HOH   29 329 243  HOH   HOH A . 
K 6 HOH   30 330 89   HOH   HOH A . 
K 6 HOH   31 331 248  HOH   HOH A . 
K 6 HOH   32 332 278  HOH   HOH A . 
K 6 HOH   33 333 233  HOH   HOH A . 
K 6 HOH   34 334 72   HOH   HOH A . 
K 6 HOH   35 335 245  HOH   HOH A . 
K 6 HOH   36 336 21   HOH   HOH A . 
K 6 HOH   37 337 144  HOH   HOH A . 
K 6 HOH   38 338 269  HOH   HOH A . 
K 6 HOH   39 339 237  HOH   HOH A . 
K 6 HOH   40 340 234  HOH   HOH A . 
K 6 HOH   41 341 180  HOH   HOH A . 
K 6 HOH   42 342 94   HOH   HOH A . 
K 6 HOH   43 343 174  HOH   HOH A . 
K 6 HOH   44 344 29   HOH   HOH A . 
K 6 HOH   45 345 45   HOH   HOH A . 
K 6 HOH   46 346 147  HOH   HOH A . 
K 6 HOH   47 347 107  HOH   HOH A . 
K 6 HOH   48 348 279  HOH   HOH A . 
K 6 HOH   49 349 117  HOH   HOH A . 
K 6 HOH   50 350 54   HOH   HOH A . 
K 6 HOH   51 351 146  HOH   HOH A . 
K 6 HOH   52 352 28   HOH   HOH A . 
K 6 HOH   53 353 68   HOH   HOH A . 
K 6 HOH   54 354 86   HOH   HOH A . 
K 6 HOH   55 355 275  HOH   HOH A . 
K 6 HOH   56 356 148  HOH   HOH A . 
K 6 HOH   57 357 115  HOH   HOH A . 
K 6 HOH   58 358 246  HOH   HOH A . 
K 6 HOH   59 359 232  HOH   HOH A . 
K 6 HOH   60 360 119  HOH   HOH A . 
K 6 HOH   61 361 12   HOH   HOH A . 
K 6 HOH   62 362 33   HOH   HOH A . 
K 6 HOH   63 363 24   HOH   HOH A . 
K 6 HOH   64 364 92   HOH   HOH A . 
K 6 HOH   65 365 106  HOH   HOH A . 
K 6 HOH   66 366 40   HOH   HOH A . 
K 6 HOH   67 367 76   HOH   HOH A . 
K 6 HOH   68 368 235  HOH   HOH A . 
K 6 HOH   69 369 143  HOH   HOH A . 
K 6 HOH   70 370 142  HOH   HOH A . 
K 6 HOH   71 371 260  HOH   HOH A . 
K 6 HOH   72 372 261  HOH   HOH A . 
K 6 HOH   73 373 276  HOH   HOH A . 
K 6 HOH   74 374 118  HOH   HOH A . 
K 6 HOH   75 375 277  HOH   HOH A . 
K 6 HOH   76 376 262  HOH   HOH A . 
L 6 HOH   1  301 272  HOH   HOH B . 
L 6 HOH   2  302 225  HOH   HOH B . 
L 6 HOH   3  303 251  HOH   HOH B . 
L 6 HOH   4  304 219  HOH   HOH B . 
L 6 HOH   5  305 199  HOH   HOH B . 
L 6 HOH   6  306 207  HOH   HOH B . 
L 6 HOH   7  307 23   HOH   HOH B . 
L 6 HOH   8  308 38   HOH   HOH B . 
L 6 HOH   9  309 192  HOH   HOH B . 
L 6 HOH   10 310 255  HOH   HOH B . 
L 6 HOH   11 311 210  HOH   HOH B . 
L 6 HOH   12 312 263  HOH   HOH B . 
L 6 HOH   13 313 265  HOH   HOH B . 
L 6 HOH   14 314 105  HOH   HOH B . 
L 6 HOH   15 315 250  HOH   HOH B . 
L 6 HOH   16 316 259  HOH   HOH B . 
L 6 HOH   17 317 205  HOH   HOH B . 
L 6 HOH   18 318 96   HOH   HOH B . 
L 6 HOH   19 319 203  HOH   HOH B . 
L 6 HOH   20 320 201  HOH   HOH B . 
L 6 HOH   21 321 273  HOH   HOH B . 
L 6 HOH   22 322 254  HOH   HOH B . 
L 6 HOH   23 323 258  HOH   HOH B . 
L 6 HOH   24 324 252  HOH   HOH B . 
L 6 HOH   25 325 195  HOH   HOH B . 
L 6 HOH   26 326 218  HOH   HOH B . 
L 6 HOH   27 327 226  HOH   HOH B . 
L 6 HOH   28 328 202  HOH   HOH B . 
L 6 HOH   29 329 78   HOH   HOH B . 
L 6 HOH   30 330 197  HOH   HOH B . 
L 6 HOH   31 331 41   HOH   HOH B . 
L 6 HOH   32 332 8    HOH   HOH B . 
L 6 HOH   33 333 82   HOH   HOH B . 
L 6 HOH   34 334 97   HOH   HOH B . 
L 6 HOH   35 335 271  HOH   HOH B . 
L 6 HOH   36 336 110  HOH   HOH B . 
L 6 HOH   37 337 116  HOH   HOH B . 
L 6 HOH   38 338 196  HOH   HOH B . 
L 6 HOH   39 339 231  HOH   HOH B . 
L 6 HOH   40 340 121  HOH   HOH B . 
L 6 HOH   41 341 81   HOH   HOH B . 
L 6 HOH   42 342 224  HOH   HOH B . 
L 6 HOH   43 343 194  HOH   HOH B . 
L 6 HOH   44 344 228  HOH   HOH B . 
L 6 HOH   45 345 20   HOH   HOH B . 
L 6 HOH   46 346 214  HOH   HOH B . 
L 6 HOH   47 347 257  HOH   HOH B . 
L 6 HOH   48 348 267  HOH   HOH B . 
L 6 HOH   49 349 191  HOH   HOH B . 
L 6 HOH   50 350 128  HOH   HOH B . 
L 6 HOH   51 351 220  HOH   HOH B . 
L 6 HOH   52 352 270  HOH   HOH B . 
L 6 HOH   53 353 268  HOH   HOH B . 
L 6 HOH   54 354 221  HOH   HOH B . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 0 A ARG 151 ? NE  ? A ARG 154 NE  
2  1 Y 0 A ARG 151 ? CZ  ? A ARG 154 CZ  
3  1 Y 0 A ARG 151 ? NH1 ? A ARG 154 NH1 
4  1 Y 0 A ARG 151 ? NH2 ? A ARG 154 NH2 
5  1 Y 0 B GLU 31  ? CG  ? B GLU 34  CG  
6  1 Y 0 B GLU 31  ? CD  ? B GLU 34  CD  
7  1 Y 0 B GLU 31  ? OE1 ? B GLU 34  OE1 
8  1 Y 0 B GLU 31  ? OE2 ? B GLU 34  OE2 
9  1 Y 0 B LYS 128 ? CD  ? B LYS 131 CD  
10 1 Y 0 B LYS 128 ? CE  ? B LYS 131 CE  
11 1 Y 0 B LYS 128 ? NZ  ? B LYS 131 NZ  
# 
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     ? ? ? .        2 
? 'data extraction' ? ? ? ? ? ? ? ? ? ? ? PDB_EXTRACT ? ? ? 3.22     3 
? 'data reduction'  ? ? ? ? ? ? ? ? ? ? ? XDS         ? ? ? .        4 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9GGW 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     37.065 
_cell.length_a_esd                 ? 
_cell.length_b                     41.054 
_cell.length_b_esd                 ? 
_cell.length_c                     209.005 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_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                         9GGW 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9GGW 
_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             2.03 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          39.34 
_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               ? 
_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              7.9 
_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    '25% PEG 8000, 300 mM LiCl, 100 mM bis-tris propane' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            292 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS3 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2017-07-24 
_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   0.97998 
_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 I03' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.97998 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   I03 
_diffrn_source.pdbx_synchrotron_site       Diamond 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9GGW 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.818 
_reflns.d_resolution_low                               209.005 
_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                                     29802 
_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                           99.9 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.3 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          10.5 
_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                                0.166 
_reflns.pdbx_Rpim_I_all                                0.088 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.997 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.144 
_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 
1.818 1.849   ? ? ? ? ? ? 1501 ? ? ? ? ? ? ? ? ? ? ? 6.5 ? ? ? 1.001 0.529 ? 1 1 0.737 ? ? 99.9   ? 0.913 ? ? ? ? ? ? ? ? ? 
4.934 209.005 ? ? ? ? ? ? 1653 ? ? ? ? ? ? ? ? ? ? ? 5.8 ? ? ? 0.059 0.031 ? 2 1 0.998 ? ? 99.500 ? 0.051 ? ? ? ? ? ? ? ? ? 
# 
_refine.aniso_B[1][1]                            2.3200 
_refine.aniso_B[1][2]                            0.0000 
_refine.aniso_B[1][3]                            0.0000 
_refine.aniso_B[2][2]                            -2.4100 
_refine.aniso_B[2][3]                            0.0000 
_refine.aniso_B[3][3]                            0.0900 
_refine.B_iso_max                                43.000 
_refine.B_iso_mean                               23.7570 
_refine.B_iso_min                                11.620 
_refine.correlation_coeff_Fo_to_Fc               0.9340 
_refine.correlation_coeff_Fo_to_Fc_free          0.9110 
_refine.details                                  'U VALUES      : WITH TLS ADDED HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9GGW 
_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                            1.8200 
_refine.ls_d_res_low                             104.5000 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     28292 
_refine.ls_number_reflns_R_free                  1496 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.8800 
_refine.ls_percent_reflns_R_free                 5.0000 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2358 
_refine.ls_R_factor_R_free                       0.2681 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2342 
_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                       0.1830 
_refine.pdbx_overall_ESU_R_Free                  0.1600 
_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                             10.3930 
_refine.overall_SU_ML                            0.1350 
_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                       1.8200 
_refine_hist.d_res_low                        104.5000 
_refine_hist.number_atoms_solvent             130 
_refine_hist.number_atoms_total               2959 
_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       334 
_refine_hist.pdbx_B_iso_mean_ligand           22.67 
_refine_hist.pdbx_B_iso_mean_solvent          26.80 
_refine_hist.pdbx_number_atoms_protein        2689 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         140 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.020  0.013  2867 ? r_bond_refined_d       ? ? 
'X-RAY DIFFRACTION' ? 0.035  0.018  2614 ? r_bond_other_d         ? ? 
'X-RAY DIFFRACTION' ? 2.083  1.728  3890 ? r_angle_refined_deg    ? ? 
'X-RAY DIFFRACTION' ? 2.408  1.639  6054 ? r_angle_other_deg      ? ? 
'X-RAY DIFFRACTION' ? 4.755  5.000  331  ? r_dihedral_angle_1_deg ? ? 
'X-RAY DIFFRACTION' ? 34.353 22.000 160  ? r_dihedral_angle_2_deg ? ? 
'X-RAY DIFFRACTION' ? 14.028 15.000 491  ? r_dihedral_angle_3_deg ? ? 
'X-RAY DIFFRACTION' ? 23.419 15.000 23   ? r_dihedral_angle_4_deg ? ? 
'X-RAY DIFFRACTION' ? 0.129  0.200  375  ? r_chiral_restr         ? ? 
'X-RAY DIFFRACTION' ? 0.011  0.020  3131 ? r_gen_planes_refined   ? ? 
'X-RAY DIFFRACTION' ? 0.019  0.020  604  ? r_gen_planes_other     ? ? 
'X-RAY DIFFRACTION' ? 0.277  0.334  1333 ? r_mcbond_it            ? ? 
'X-RAY DIFFRACTION' ? 0.277  0.334  1332 ? r_mcbond_other         ? ? 
'X-RAY DIFFRACTION' ? 0.491  0.499  1661 ? r_mcangle_it           ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.8200 
_refine_ls_shell.d_res_low                        1.8650 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             103 
_refine_ls_shell.number_reflns_R_work             2090 
_refine_ls_shell.percent_reflns_obs               99.8600 
_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                  0.3120 
_refine_ls_shell.redundancy_reflns_all            ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.wR_factor_all                    ? 
_refine_ls_shell.wR_factor_obs                    ? 
_refine_ls_shell.wR_factor_R_free                 ? 
_refine_ls_shell.wR_factor_R_work                 ? 
_refine_ls_shell.pdbx_R_complete                  ? 
_refine_ls_shell.pdbx_total_number_of_bins_used   ? 
_refine_ls_shell.pdbx_phase_error                 ? 
_refine_ls_shell.pdbx_fsc_work                    ? 
_refine_ls_shell.pdbx_fsc_free                    ? 
_refine_ls_shell.R_factor_R_free                  0.2980 
# 
_struct.entry_id                     9GGW 
_struct.title                        'Human KRas4A (GDP) in complex with compound 16' 
_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        9GGW 
_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 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 4 ? 
F N N 5 ? 
G N N 2 ? 
H N N 3 ? 
I N N 4 ? 
J N N 5 ? 
K N N 6 ? 
L 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 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 9GGW A 4 ? 172 ? P01116 1 ? 169 ? 1 169 
2 1 9GGW B 4 ? 172 ? P01116 1 ? 169 ? 1 169 
# 
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 9GGW GLY A 1   ? UNP P01116 ?   ?   'expression tag'      -2  1 
1 9GGW GLY A 2   ? UNP P01116 ?   ?   'expression tag'      -1  2 
1 9GGW SER A 3   ? UNP P01116 ?   ?   'expression tag'      0   3 
1 9GGW SER A 121 ? UNP P01116 CYS 118 'engineered mutation' 118 4 
2 9GGW GLY B 1   ? UNP P01116 ?   ?   'expression tag'      -2  5 
2 9GGW GLY B 2   ? UNP P01116 ?   ?   'expression tag'      -1  6 
2 9GGW SER B 3   ? UNP P01116 ?   ?   'expression tag'      0   7 
2 9GGW SER B 121 ? UNP P01116 CYS 118 'engineered mutation' 118 8 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,E,F,K 
2 1 B,G,H,I,J,L 
# 
_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                1 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 GLY A 18  ? ASN A 29  ? GLY A 15  ASN A 26  1 ? 12 
HELX_P HELX_P2  AA2 SER A 68  ? GLY A 78  ? SER A 65  GLY A 75  1 ? 11 
HELX_P HELX_P3  AA3 ASN A 89  ? ASP A 108 ? ASN A 86  ASP A 105 1 ? 20 
HELX_P HELX_P4  AA4 ASP A 129 ? GLY A 141 ? ASP A 126 GLY A 138 1 ? 13 
HELX_P HELX_P5  AA5 ARG A 154 ? LEU A 171 ? ARG A 151 LEU A 168 1 ? 18 
HELX_P HELX_P6  AA6 GLY B 18  ? ASN B 29  ? GLY B 15  ASN B 26  1 ? 12 
HELX_P HELX_P7  AA7 SER B 68  ? GLY B 78  ? SER B 65  GLY B 75  1 ? 11 
HELX_P HELX_P8  AA8 ASN B 89  ? ASP B 95  ? ASN B 86  ASP B 92  1 ? 7  
HELX_P HELX_P9  AA9 ASP B 95  ? ASP B 108 ? ASP B 92  ASP B 105 1 ? 14 
HELX_P HELX_P10 AB1 ASP B 129 ? GLY B 141 ? ASP B 126 GLY B 138 1 ? 13 
HELX_P HELX_P11 AB2 ARG B 154 ? LEU B 171 ? ARG B 151 LEU B 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 D MG  . MG ? ? A SER 17  A MG  202 1_555 ? ? ? ? ? ? ? 2.027 ? ? 
metalc2  metalc ? ? C GDP .  O1B ? ? ? 1_555 D MG  . MG ? ? A GDP 201 A MG  202 1_555 ? ? ? ? ? ? ? 2.176 ? ? 
metalc3  metalc ? ? D MG  .  MG  ? ? ? 1_555 K HOH . O  ? ? A MG  202 A HOH 302 1_555 ? ? ? ? ? ? ? 2.231 ? ? 
metalc4  metalc ? ? D MG  .  MG  ? ? ? 1_555 K HOH . O  ? ? A MG  202 A HOH 313 1_555 ? ? ? ? ? ? ? 2.018 ? ? 
metalc5  metalc ? ? D MG  .  MG  ? ? ? 1_555 K HOH . O  ? ? A MG  202 A HOH 314 1_555 ? ? ? ? ? ? ? 2.111 ? ? 
metalc6  metalc ? ? D MG  .  MG  ? ? ? 1_555 K HOH . O  ? ? A MG  202 A HOH 339 1_555 ? ? ? ? ? ? ? 2.147 ? ? 
metalc7  metalc ? ? B SER 20 OG  ? ? ? 1_555 H MG  . MG ? ? B SER 17  B MG  202 1_555 ? ? ? ? ? ? ? 2.166 ? ? 
metalc8  metalc ? ? G GDP .  O1B ? ? ? 1_555 H MG  . MG ? ? B GDP 201 B MG  202 1_555 ? ? ? ? ? ? ? 2.104 ? ? 
metalc9  metalc ? ? H MG  .  MG  ? ? ? 1_555 L HOH . O  ? ? B MG  202 B HOH 303 1_555 ? ? ? ? ? ? ? 2.023 ? ? 
metalc10 metalc ? ? H MG  .  MG  ? ? ? 1_555 L HOH . O  ? ? B MG  202 B HOH 324 1_555 ? ? ? ? ? ? ? 1.901 ? ? 
metalc11 metalc ? ? H MG  .  MG  ? ? ? 1_555 L HOH . O  ? ? B MG  202 B HOH 328 1_555 ? ? ? ? ? ? ? 2.129 ? ? 
metalc12 metalc ? ? H MG  .  MG  ? ? ? 1_555 L HOH . O  ? ? B MG  202 B HOH 331 1_555 ? ? ? ? ? ? ? 2.077 ? ? 
# 
_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 ? D MG . ? A MG 202 ? 1_555 O1B ? C GDP . ? A GDP 201 ? 1_555 90.6  ? 
2  OG  ? A SER 20 ? A SER 17  ? 1_555 MG ? D MG . ? A MG 202 ? 1_555 O   ? K HOH . ? A HOH 302 ? 1_555 87.8  ? 
3  O1B ? C GDP .  ? A GDP 201 ? 1_555 MG ? D MG . ? A MG 202 ? 1_555 O   ? K HOH . ? A HOH 302 ? 1_555 84.2  ? 
4  OG  ? A SER 20 ? A SER 17  ? 1_555 MG ? D MG . ? A MG 202 ? 1_555 O   ? K HOH . ? A HOH 313 ? 1_555 86.8  ? 
5  O1B ? C GDP .  ? A GDP 201 ? 1_555 MG ? D MG . ? A MG 202 ? 1_555 O   ? K HOH . ? A HOH 313 ? 1_555 96.8  ? 
6  O   ? K HOH .  ? A HOH 302 ? 1_555 MG ? D MG . ? A MG 202 ? 1_555 O   ? K HOH . ? A HOH 313 ? 1_555 174.5 ? 
7  OG  ? A SER 20 ? A SER 17  ? 1_555 MG ? D MG . ? A MG 202 ? 1_555 O   ? K HOH . ? A HOH 314 ? 1_555 175.3 ? 
8  O1B ? C GDP .  ? A GDP 201 ? 1_555 MG ? D MG . ? A MG 202 ? 1_555 O   ? K HOH . ? A HOH 314 ? 1_555 93.4  ? 
9  O   ? K HOH .  ? A HOH 302 ? 1_555 MG ? D MG . ? A MG 202 ? 1_555 O   ? K HOH . ? A HOH 314 ? 1_555 95.0  ? 
10 O   ? K HOH .  ? A HOH 313 ? 1_555 MG ? D MG . ? A MG 202 ? 1_555 O   ? K HOH . ? A HOH 314 ? 1_555 90.3  ? 
11 OG  ? A SER 20 ? A SER 17  ? 1_555 MG ? D MG . ? A MG 202 ? 1_555 O   ? K HOH . ? A HOH 339 ? 1_555 87.6  ? 
12 O1B ? C GDP .  ? A GDP 201 ? 1_555 MG ? D MG . ? A MG 202 ? 1_555 O   ? K HOH . ? A HOH 339 ? 1_555 169.4 ? 
13 O   ? K HOH .  ? A HOH 302 ? 1_555 MG ? D MG . ? A MG 202 ? 1_555 O   ? K HOH . ? A HOH 339 ? 1_555 85.3  ? 
14 O   ? K HOH .  ? A HOH 313 ? 1_555 MG ? D MG . ? A MG 202 ? 1_555 O   ? K HOH . ? A HOH 339 ? 1_555 93.5  ? 
15 O   ? K HOH .  ? A HOH 314 ? 1_555 MG ? D MG . ? A MG 202 ? 1_555 O   ? K HOH . ? A HOH 339 ? 1_555 88.9  ? 
16 OG  ? B SER 20 ? B SER 17  ? 1_555 MG ? H MG . ? B MG 202 ? 1_555 O1B ? G GDP . ? B GDP 201 ? 1_555 103.4 ? 
17 OG  ? B SER 20 ? B SER 17  ? 1_555 MG ? H MG . ? B MG 202 ? 1_555 O   ? L HOH . ? B HOH 303 ? 1_555 88.3  ? 
18 O1B ? G GDP .  ? B GDP 201 ? 1_555 MG ? H MG . ? B MG 202 ? 1_555 O   ? L HOH . ? B HOH 303 ? 1_555 104.3 ? 
19 OG  ? B SER 20 ? B SER 17  ? 1_555 MG ? H MG . ? B MG 202 ? 1_555 O   ? L HOH . ? B HOH 324 ? 1_555 88.9  ? 
20 O1B ? G GDP .  ? B GDP 201 ? 1_555 MG ? H MG . ? B MG 202 ? 1_555 O   ? L HOH . ? B HOH 324 ? 1_555 94.3  ? 
21 O   ? L HOH .  ? B HOH 303 ? 1_555 MG ? H MG . ? B MG 202 ? 1_555 O   ? L HOH . ? B HOH 324 ? 1_555 161.4 ? 
22 OG  ? B SER 20 ? B SER 17  ? 1_555 MG ? H MG . ? B MG 202 ? 1_555 O   ? L HOH . ? B HOH 328 ? 1_555 166.8 ? 
23 O1B ? G GDP .  ? B GDP 201 ? 1_555 MG ? H MG . ? B MG 202 ? 1_555 O   ? L HOH . ? B HOH 328 ? 1_555 83.8  ? 
24 O   ? L HOH .  ? B HOH 303 ? 1_555 MG ? H MG . ? B MG 202 ? 1_555 O   ? L HOH . ? B HOH 328 ? 1_555 100.8 ? 
25 O   ? L HOH .  ? B HOH 324 ? 1_555 MG ? H MG . ? B MG 202 ? 1_555 O   ? L HOH . ? B HOH 328 ? 1_555 79.4  ? 
26 OG  ? B SER 20 ? B SER 17  ? 1_555 MG ? H MG . ? B MG 202 ? 1_555 O   ? L HOH . ? B HOH 331 ? 1_555 83.8  ? 
27 O1B ? G GDP .  ? B GDP 201 ? 1_555 MG ? H MG . ? B MG 202 ? 1_555 O   ? L HOH . ? B HOH 331 ? 1_555 164.8 ? 
28 O   ? L HOH .  ? B HOH 303 ? 1_555 MG ? H MG . ? B MG 202 ? 1_555 O   ? L HOH . ? B HOH 331 ? 1_555 89.1  ? 
29 O   ? L HOH .  ? B HOH 324 ? 1_555 MG ? H MG . ? B MG 202 ? 1_555 O   ? L HOH . ? B HOH 331 ? 1_555 72.3  ? 
30 O   ? L HOH .  ? B HOH 328 ? 1_555 MG ? H MG . ? B MG 202 ? 1_555 O   ? L HOH . ? B HOH 331 ? 1_555 86.7  ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 6 ? 
AA2 ? 6 ? 
# 
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      
AA2 1 2 ? anti-parallel 
AA2 2 3 ? parallel      
AA2 3 4 ? parallel      
AA2 4 5 ? parallel      
AA2 5 6 ? parallel      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 ASP A 41  ? ILE A 49  ? ASP A 38  ILE A 46  
AA1 2 GLU A 52  ? ASP A 60  ? GLU A 49  ASP A 57  
AA1 3 THR A 5   ? VAL A 12  ? THR A 2   VAL A 9   
AA1 4 GLY A 80  ? ALA A 86  ? GLY A 77  ALA A 83  
AA1 5 MET A 114 ? ASN A 119 ? MET A 111 ASN A 116 
AA1 6 PHE A 144 ? GLU A 146 ? PHE A 141 GLU A 143 
AA2 1 ASP B 41  ? ILE B 49  ? ASP B 38  ILE B 46  
AA2 2 GLU B 52  ? ASP B 60  ? GLU B 49  ASP B 57  
AA2 3 GLU B 6   ? VAL B 12  ? GLU B 3   VAL B 9   
AA2 4 GLY B 80  ? ALA B 86  ? GLY B 77  ALA B 83  
AA2 5 MET B 114 ? ASN B 119 ? MET B 111 ASN B 116 
AA2 6 PHE B 144 ? GLU B 146 ? PHE B 141 GLU B 143 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N LYS A 45  ? N LYS A 42  O LEU A 56  ? O LEU A 53  
AA1 2 3 O LEU A 59  ? O LEU A 56  N LEU A 9   ? N LEU A 6   
AA1 3 4 N VAL A 12  ? N VAL A 9   O VAL A 84  ? O VAL A 81  
AA1 4 5 N PHE A 85  ? N PHE A 82  O ASN A 119 ? O ASN A 116 
AA1 5 6 N LEU A 116 ? N LEU A 113 O ILE A 145 ? O ILE A 142 
AA2 1 2 N VAL B 47  ? N VAL B 44  O CYS B 54  ? O CYS B 51  
AA2 2 3 O LEU B 59  ? O LEU B 56  N LEU B 9   ? N LEU B 6   
AA2 3 4 N VAL B 10  ? N VAL B 7   O LEU B 82  ? O LEU B 79  
AA2 4 5 N PHE B 85  ? N PHE B 82  O ASN B 119 ? O ASN B 116 
AA2 5 6 N LEU B 116 ? N LEU B 113 O ILE B 145 ? O ILE B 142 
# 
_pdbx_entry_details.entry_id                   9GGW 
_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 37  ? ? OE2 A GLU 37  ? ? 1.146 1.252 -0.106 0.011 N 
2 1 C  A VAL 109 ? ? N   A PRO 110 ? ? 1.477 1.338 0.139  0.019 Y 
3 1 CD A GLU 143 ? ? OE2 A GLU 143 ? ? 1.181 1.252 -0.071 0.011 N 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 C  A VAL 109 ? ? N  A PRO 110 ? ? CA A PRO 110 ? ? 128.86 119.30 9.56  1.50 Y 
2 1 CB A ARG 151 ? ? CG A ARG 151 ? ? CD A ARG 151 ? ? 127.37 111.60 15.77 2.60 N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ASP A 33  ? ? -36.34 117.51 
2 1 LYS A 117 ? ? 74.02  33.18  
3 1 LYS B 117 ? ? 73.57  34.34  
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1 'X-RAY DIFFRACTION' ? refined 11.0713 4.6632  39.2626  0.0362 ? 0.0017  ? 0.0072 ? 0.1900 ? 0.0054  ? 0.2165 ? 1.0448 ? -0.0767 
? 0.2248 ? 1.1264 ? 0.1441  ? 1.9330 ? -0.0227 ? 0.0369 ? -0.0458 ? -0.1846 ? -0.0097 ? 0.0428  ? 0.0571  ? 0.0055  ? 0.0323 ? 
2 'X-RAY DIFFRACTION' ? refined 14.6543 -2.3080 -11.4958 0.3626 ? 0.0136  ? 0.0135 ? 0.1960 ? -0.0036 ? 0.2060 ? 1.6684 ? 0.3124  
? 0.0735 ? 0.1982 ? -0.1066 ? 0.5987 ? -0.0067 ? 0.0110 ? 0.0148  ? 0.0465  ? 0.0065  ? -0.0100 ? -0.0364 ? -0.0010 ? 0.0001 ? 
3 'X-RAY DIFFRACTION' ? refined 14.9279 4.7283  20.1931  0.1786 ? -0.0022 ? 0.0234 ? 0.2657 ? 0.0038  ? 0.2906 ? 0.0075 ? 0.0038  
? 0.0638 ? 0.0734 ? 0.0218  ? 0.6602 ? -0.0026 ? 0.0091 ? 0.0167  ? -0.1122 ? 0.0018  ? 0.0117  ? -0.0622 ? -0.0086 ? 0.0008 ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1 'X-RAY DIFFRACTION' 1 ? ? A 0 ? ? ? A 168 ? ? ? 
2 'X-RAY DIFFRACTION' 2 ? ? B 1 ? ? ? B 169 ? ? ? 
# 
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 LYS 169 ? A LYS 172 
4  1 Y 1 B GLY -2  ? B GLY 1   
5  1 Y 1 B GLY -1  ? B GLY 2   
6  1 Y 1 B SER 0   ? B SER 3   
7  1 Y 1 B GLY 60  ? B GLY 63  
8  1 Y 1 B GLN 61  ? B GLN 64  
9  1 Y 1 B GLU 62  ? B GLU 65  
10 1 Y 1 B GLU 63  ? B GLU 66  
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
A1ILA OBB    O  N N 1   
A1ILA CAS    C  N N 2   
A1ILA CAT    C  Y N 3   
A1ILA CAZ    C  Y N 4   
A1ILA CAU    C  Y N 5   
A1ILA OBA    O  N N 6   
A1ILA CAV    C  Y N 7   
A1ILA CAW    C  Y N 8   
A1ILA CAX    C  Y N 9   
A1ILA SAI    S  N N 10  
A1ILA OAH    O  N N 11  
A1ILA OAY    O  N N 12  
A1ILA NAJ    N  N N 13  
A1ILA CAK    C  Y N 14  
A1ILA SBK    S  Y N 15  
A1ILA CAF    C  Y N 16  
A1ILA CAE    C  Y N 17  
A1ILA CLBI   CL N N 18  
A1ILA CAD    C  Y N 19  
A1ILA CAC    C  Y N 20  
A1ILA CAB    C  Y N 21  
A1ILA OAA    O  N N 22  
A1ILA CAG    C  Y N 23  
A1ILA NAL    N  Y N 24  
A1ILA CAM    C  N N 25  
A1ILA CAN    C  N N 26  
A1ILA CAO    C  N N 27  
A1ILA CAP    C  N N 28  
A1ILA CAQ    C  N N 29  
A1ILA NAR    N  N N 30  
A1ILA CBC    C  N N 31  
A1ILA CBD    C  N N 32  
A1ILA CBE    C  N N 33  
A1ILA CBF    C  N N 34  
A1ILA NBJ    N  N N 35  
A1ILA CBG    C  N N 36  
A1ILA CBH    C  N N 37  
A1ILA H1     H  N N 38  
A1ILA H2     H  N N 39  
A1ILA H3     H  N N 40  
A1ILA H4     H  N N 41  
A1ILA H5     H  N N 42  
A1ILA H6     H  N N 43  
A1ILA H7     H  N N 44  
A1ILA H8     H  N N 45  
A1ILA H9     H  N N 46  
A1ILA H10    H  N N 47  
A1ILA H11    H  N N 48  
A1ILA H12    H  N N 49  
A1ILA H13    H  N N 50  
A1ILA H14    H  N N 51  
A1ILA H15    H  N N 52  
A1ILA H16    H  N N 53  
A1ILA H17    H  N N 54  
A1ILA H18    H  N N 55  
A1ILA H19    H  N N 56  
A1ILA H20    H  N N 57  
A1ILA H21    H  N N 58  
A1ILA H22    H  N N 59  
A1ILA H23    H  N N 60  
A1ILA H24    H  N N 61  
A1ILA H25    H  N N 62  
A1ILA H26    H  N N 63  
A1ILA H28    H  N N 64  
A1ILA H29    H  N N 65  
A1ILA H30    H  N N 66  
A1ILA H31    H  N N 67  
ALA   N      N  N N 68  
ALA   CA     C  N S 69  
ALA   C      C  N N 70  
ALA   O      O  N N 71  
ALA   CB     C  N N 72  
ALA   OXT    O  N N 73  
ALA   H      H  N N 74  
ALA   H2     H  N N 75  
ALA   HA     H  N N 76  
ALA   HB1    H  N N 77  
ALA   HB2    H  N N 78  
ALA   HB3    H  N N 79  
ALA   HXT    H  N N 80  
ARG   N      N  N N 81  
ARG   CA     C  N S 82  
ARG   C      C  N N 83  
ARG   O      O  N N 84  
ARG   CB     C  N N 85  
ARG   CG     C  N N 86  
ARG   CD     C  N N 87  
ARG   NE     N  N N 88  
ARG   CZ     C  N N 89  
ARG   NH1    N  N N 90  
ARG   NH2    N  N N 91  
ARG   OXT    O  N N 92  
ARG   H      H  N N 93  
ARG   H2     H  N N 94  
ARG   HA     H  N N 95  
ARG   HB2    H  N N 96  
ARG   HB3    H  N N 97  
ARG   HG2    H  N N 98  
ARG   HG3    H  N N 99  
ARG   HD2    H  N N 100 
ARG   HD3    H  N N 101 
ARG   HE     H  N N 102 
ARG   HH11   H  N N 103 
ARG   HH12   H  N N 104 
ARG   HH21   H  N N 105 
ARG   HH22   H  N N 106 
ARG   HXT    H  N N 107 
ASN   N      N  N N 108 
ASN   CA     C  N S 109 
ASN   C      C  N N 110 
ASN   O      O  N N 111 
ASN   CB     C  N N 112 
ASN   CG     C  N N 113 
ASN   OD1    O  N N 114 
ASN   ND2    N  N N 115 
ASN   OXT    O  N N 116 
ASN   H      H  N N 117 
ASN   H2     H  N N 118 
ASN   HA     H  N N 119 
ASN   HB2    H  N N 120 
ASN   HB3    H  N N 121 
ASN   HD21   H  N N 122 
ASN   HD22   H  N N 123 
ASN   HXT    H  N N 124 
ASP   N      N  N N 125 
ASP   CA     C  N S 126 
ASP   C      C  N N 127 
ASP   O      O  N N 128 
ASP   CB     C  N N 129 
ASP   CG     C  N N 130 
ASP   OD1    O  N N 131 
ASP   OD2    O  N N 132 
ASP   OXT    O  N N 133 
ASP   H      H  N N 134 
ASP   H2     H  N N 135 
ASP   HA     H  N N 136 
ASP   HB2    H  N N 137 
ASP   HB3    H  N N 138 
ASP   HD2    H  N N 139 
ASP   HXT    H  N N 140 
CYS   N      N  N N 141 
CYS   CA     C  N R 142 
CYS   C      C  N N 143 
CYS   O      O  N N 144 
CYS   CB     C  N N 145 
CYS   SG     S  N N 146 
CYS   OXT    O  N N 147 
CYS   H      H  N N 148 
CYS   H2     H  N N 149 
CYS   HA     H  N N 150 
CYS   HB2    H  N N 151 
CYS   HB3    H  N N 152 
CYS   HG     H  N N 153 
CYS   HXT    H  N N 154 
EDO   C1     C  N N 155 
EDO   O1     O  N N 156 
EDO   C2     C  N N 157 
EDO   O2     O  N N 158 
EDO   H11    H  N N 159 
EDO   H12    H  N N 160 
EDO   HO1    H  N N 161 
EDO   H21    H  N N 162 
EDO   H22    H  N N 163 
EDO   HO2    H  N N 164 
GDP   PB     P  N N 165 
GDP   O1B    O  N N 166 
GDP   O2B    O  N N 167 
GDP   O3B    O  N N 168 
GDP   O3A    O  N N 169 
GDP   PA     P  N N 170 
GDP   O1A    O  N N 171 
GDP   O2A    O  N N 172 
GDP   "O5'"  O  N N 173 
GDP   "C5'"  C  N N 174 
GDP   "C4'"  C  N R 175 
GDP   "O4'"  O  N N 176 
GDP   "C3'"  C  N S 177 
GDP   "O3'"  O  N N 178 
GDP   "C2'"  C  N R 179 
GDP   "O2'"  O  N N 180 
GDP   "C1'"  C  N R 181 
GDP   N9     N  Y N 182 
GDP   C8     C  Y N 183 
GDP   N7     N  Y N 184 
GDP   C5     C  Y N 185 
GDP   C6     C  N N 186 
GDP   O6     O  N N 187 
GDP   N1     N  N N 188 
GDP   C2     C  N N 189 
GDP   N2     N  N N 190 
GDP   N3     N  N N 191 
GDP   C4     C  Y N 192 
GDP   HOB2   H  N N 193 
GDP   HOB3   H  N N 194 
GDP   HOA2   H  N N 195 
GDP   "H5'"  H  N N 196 
GDP   "H5''" H  N N 197 
GDP   "H4'"  H  N N 198 
GDP   "H3'"  H  N N 199 
GDP   "HO3'" H  N N 200 
GDP   "H2'"  H  N N 201 
GDP   "HO2'" H  N N 202 
GDP   "H1'"  H  N N 203 
GDP   H8     H  N N 204 
GDP   HN1    H  N N 205 
GDP   HN21   H  N N 206 
GDP   HN22   H  N N 207 
GLN   N      N  N N 208 
GLN   CA     C  N S 209 
GLN   C      C  N N 210 
GLN   O      O  N N 211 
GLN   CB     C  N N 212 
GLN   CG     C  N N 213 
GLN   CD     C  N N 214 
GLN   OE1    O  N N 215 
GLN   NE2    N  N N 216 
GLN   OXT    O  N N 217 
GLN   H      H  N N 218 
GLN   H2     H  N N 219 
GLN   HA     H  N N 220 
GLN   HB2    H  N N 221 
GLN   HB3    H  N N 222 
GLN   HG2    H  N N 223 
GLN   HG3    H  N N 224 
GLN   HE21   H  N N 225 
GLN   HE22   H  N N 226 
GLN   HXT    H  N N 227 
GLU   N      N  N N 228 
GLU   CA     C  N S 229 
GLU   C      C  N N 230 
GLU   O      O  N N 231 
GLU   CB     C  N N 232 
GLU   CG     C  N N 233 
GLU   CD     C  N N 234 
GLU   OE1    O  N N 235 
GLU   OE2    O  N N 236 
GLU   OXT    O  N N 237 
GLU   H      H  N N 238 
GLU   H2     H  N N 239 
GLU   HA     H  N N 240 
GLU   HB2    H  N N 241 
GLU   HB3    H  N N 242 
GLU   HG2    H  N N 243 
GLU   HG3    H  N N 244 
GLU   HE2    H  N N 245 
GLU   HXT    H  N N 246 
GLY   N      N  N N 247 
GLY   CA     C  N N 248 
GLY   C      C  N N 249 
GLY   O      O  N N 250 
GLY   OXT    O  N N 251 
GLY   H      H  N N 252 
GLY   H2     H  N N 253 
GLY   HA2    H  N N 254 
GLY   HA3    H  N N 255 
GLY   HXT    H  N N 256 
HIS   N      N  N N 257 
HIS   CA     C  N S 258 
HIS   C      C  N N 259 
HIS   O      O  N N 260 
HIS   CB     C  N N 261 
HIS   CG     C  Y N 262 
HIS   ND1    N  Y N 263 
HIS   CD2    C  Y N 264 
HIS   CE1    C  Y N 265 
HIS   NE2    N  Y N 266 
HIS   OXT    O  N N 267 
HIS   H      H  N N 268 
HIS   H2     H  N N 269 
HIS   HA     H  N N 270 
HIS   HB2    H  N N 271 
HIS   HB3    H  N N 272 
HIS   HD1    H  N N 273 
HIS   HD2    H  N N 274 
HIS   HE1    H  N N 275 
HIS   HE2    H  N N 276 
HIS   HXT    H  N N 277 
HOH   O      O  N N 278 
HOH   H1     H  N N 279 
HOH   H2     H  N N 280 
ILE   N      N  N N 281 
ILE   CA     C  N S 282 
ILE   C      C  N N 283 
ILE   O      O  N N 284 
ILE   CB     C  N S 285 
ILE   CG1    C  N N 286 
ILE   CG2    C  N N 287 
ILE   CD1    C  N N 288 
ILE   OXT    O  N N 289 
ILE   H      H  N N 290 
ILE   H2     H  N N 291 
ILE   HA     H  N N 292 
ILE   HB     H  N N 293 
ILE   HG12   H  N N 294 
ILE   HG13   H  N N 295 
ILE   HG21   H  N N 296 
ILE   HG22   H  N N 297 
ILE   HG23   H  N N 298 
ILE   HD11   H  N N 299 
ILE   HD12   H  N N 300 
ILE   HD13   H  N N 301 
ILE   HXT    H  N N 302 
LEU   N      N  N N 303 
LEU   CA     C  N S 304 
LEU   C      C  N N 305 
LEU   O      O  N N 306 
LEU   CB     C  N N 307 
LEU   CG     C  N N 308 
LEU   CD1    C  N N 309 
LEU   CD2    C  N N 310 
LEU   OXT    O  N N 311 
LEU   H      H  N N 312 
LEU   H2     H  N N 313 
LEU   HA     H  N N 314 
LEU   HB2    H  N N 315 
LEU   HB3    H  N N 316 
LEU   HG     H  N N 317 
LEU   HD11   H  N N 318 
LEU   HD12   H  N N 319 
LEU   HD13   H  N N 320 
LEU   HD21   H  N N 321 
LEU   HD22   H  N N 322 
LEU   HD23   H  N N 323 
LEU   HXT    H  N N 324 
LYS   N      N  N N 325 
LYS   CA     C  N S 326 
LYS   C      C  N N 327 
LYS   O      O  N N 328 
LYS   CB     C  N N 329 
LYS   CG     C  N N 330 
LYS   CD     C  N N 331 
LYS   CE     C  N N 332 
LYS   NZ     N  N N 333 
LYS   OXT    O  N N 334 
LYS   H      H  N N 335 
LYS   H2     H  N N 336 
LYS   HA     H  N N 337 
LYS   HB2    H  N N 338 
LYS   HB3    H  N N 339 
LYS   HG2    H  N N 340 
LYS   HG3    H  N N 341 
LYS   HD2    H  N N 342 
LYS   HD3    H  N N 343 
LYS   HE2    H  N N 344 
LYS   HE3    H  N N 345 
LYS   HZ1    H  N N 346 
LYS   HZ2    H  N N 347 
LYS   HZ3    H  N N 348 
LYS   HXT    H  N N 349 
MET   N      N  N N 350 
MET   CA     C  N S 351 
MET   C      C  N N 352 
MET   O      O  N N 353 
MET   CB     C  N N 354 
MET   CG     C  N N 355 
MET   SD     S  N N 356 
MET   CE     C  N N 357 
MET   OXT    O  N N 358 
MET   H      H  N N 359 
MET   H2     H  N N 360 
MET   HA     H  N N 361 
MET   HB2    H  N N 362 
MET   HB3    H  N N 363 
MET   HG2    H  N N 364 
MET   HG3    H  N N 365 
MET   HE1    H  N N 366 
MET   HE2    H  N N 367 
MET   HE3    H  N N 368 
MET   HXT    H  N N 369 
MG    MG     MG N N 370 
PHE   N      N  N N 371 
PHE   CA     C  N S 372 
PHE   C      C  N N 373 
PHE   O      O  N N 374 
PHE   CB     C  N N 375 
PHE   CG     C  Y N 376 
PHE   CD1    C  Y N 377 
PHE   CD2    C  Y N 378 
PHE   CE1    C  Y N 379 
PHE   CE2    C  Y N 380 
PHE   CZ     C  Y N 381 
PHE   OXT    O  N N 382 
PHE   H      H  N N 383 
PHE   H2     H  N N 384 
PHE   HA     H  N N 385 
PHE   HB2    H  N N 386 
PHE   HB3    H  N N 387 
PHE   HD1    H  N N 388 
PHE   HD2    H  N N 389 
PHE   HE1    H  N N 390 
PHE   HE2    H  N N 391 
PHE   HZ     H  N N 392 
PHE   HXT    H  N N 393 
PRO   N      N  N N 394 
PRO   CA     C  N S 395 
PRO   C      C  N N 396 
PRO   O      O  N N 397 
PRO   CB     C  N N 398 
PRO   CG     C  N N 399 
PRO   CD     C  N N 400 
PRO   OXT    O  N N 401 
PRO   H      H  N N 402 
PRO   HA     H  N N 403 
PRO   HB2    H  N N 404 
PRO   HB3    H  N N 405 
PRO   HG2    H  N N 406 
PRO   HG3    H  N N 407 
PRO   HD2    H  N N 408 
PRO   HD3    H  N N 409 
PRO   HXT    H  N N 410 
SER   N      N  N N 411 
SER   CA     C  N S 412 
SER   C      C  N N 413 
SER   O      O  N N 414 
SER   CB     C  N N 415 
SER   OG     O  N N 416 
SER   OXT    O  N N 417 
SER   H      H  N N 418 
SER   H2     H  N N 419 
SER   HA     H  N N 420 
SER   HB2    H  N N 421 
SER   HB3    H  N N 422 
SER   HG     H  N N 423 
SER   HXT    H  N N 424 
THR   N      N  N N 425 
THR   CA     C  N S 426 
THR   C      C  N N 427 
THR   O      O  N N 428 
THR   CB     C  N R 429 
THR   OG1    O  N N 430 
THR   CG2    C  N N 431 
THR   OXT    O  N N 432 
THR   H      H  N N 433 
THR   H2     H  N N 434 
THR   HA     H  N N 435 
THR   HB     H  N N 436 
THR   HG1    H  N N 437 
THR   HG21   H  N N 438 
THR   HG22   H  N N 439 
THR   HG23   H  N N 440 
THR   HXT    H  N N 441 
TYR   N      N  N N 442 
TYR   CA     C  N S 443 
TYR   C      C  N N 444 
TYR   O      O  N N 445 
TYR   CB     C  N N 446 
TYR   CG     C  Y N 447 
TYR   CD1    C  Y N 448 
TYR   CD2    C  Y N 449 
TYR   CE1    C  Y N 450 
TYR   CE2    C  Y N 451 
TYR   CZ     C  Y N 452 
TYR   OH     O  N N 453 
TYR   OXT    O  N N 454 
TYR   H      H  N N 455 
TYR   H2     H  N N 456 
TYR   HA     H  N N 457 
TYR   HB2    H  N N 458 
TYR   HB3    H  N N 459 
TYR   HD1    H  N N 460 
TYR   HD2    H  N N 461 
TYR   HE1    H  N N 462 
TYR   HE2    H  N N 463 
TYR   HH     H  N N 464 
TYR   HXT    H  N N 465 
VAL   N      N  N N 466 
VAL   CA     C  N S 467 
VAL   C      C  N N 468 
VAL   O      O  N N 469 
VAL   CB     C  N N 470 
VAL   CG1    C  N N 471 
VAL   CG2    C  N N 472 
VAL   OXT    O  N N 473 
VAL   H      H  N N 474 
VAL   H2     H  N N 475 
VAL   HA     H  N N 476 
VAL   HB     H  N N 477 
VAL   HG11   H  N N 478 
VAL   HG12   H  N N 479 
VAL   HG13   H  N N 480 
VAL   HG21   H  N N 481 
VAL   HG22   H  N N 482 
VAL   HG23   H  N N 483 
VAL   HXT    H  N N 484 
# 
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 
A1ILA CLBI  CAE    sing N N 1   
A1ILA CAD   CAE    doub Y N 2   
A1ILA CAD   CAC    sing Y N 3   
A1ILA CAE   CAF    sing Y N 4   
A1ILA CAC   CAB    doub Y N 5   
A1ILA CAV   CAW    doub Y N 6   
A1ILA CAV   CAU    sing Y N 7   
A1ILA CAF   SBK    sing Y N 8   
A1ILA CAF   CAG    doub Y N 9   
A1ILA OBA   CAU    sing N N 10  
A1ILA SBK   CAK    sing Y N 11  
A1ILA CAW   CAX    sing Y N 12  
A1ILA CAU   CAT    doub Y N 13  
A1ILA CAB   CAG    sing Y N 14  
A1ILA CAB   OAA    sing N N 15  
A1ILA CAG   NAL    sing Y N 16  
A1ILA OAY   SAI    doub N N 17  
A1ILA CAQ   CAP    sing N N 18  
A1ILA CAQ   NAR    sing N N 19  
A1ILA CAX   SAI    sing N N 20  
A1ILA CAX   CAZ    doub Y N 21  
A1ILA CAK   NAL    doub Y N 22  
A1ILA CAK   NAJ    sing N N 23  
A1ILA NAL   CAM    sing N N 24  
A1ILA CAT   CAZ    sing Y N 25  
A1ILA CAT   CAS    sing N N 26  
A1ILA CAP   CAO    sing N N 27  
A1ILA SAI   NAJ    sing N N 28  
A1ILA SAI   OAH    doub N N 29  
A1ILA NBJ   CBF    sing N N 30  
A1ILA CAO   CAN    sing N N 31  
A1ILA CBH   CBG    sing N N 32  
A1ILA CBH   CBC    sing N N 33  
A1ILA NAR   CAS    sing N N 34  
A1ILA NAR   CBC    sing N N 35  
A1ILA CAN   CAM    sing N N 36  
A1ILA CAS   OBB    doub N N 37  
A1ILA CBG   CBF    sing N N 38  
A1ILA CBC   CBD    sing N N 39  
A1ILA CBF   CBE    sing N N 40  
A1ILA CBD   CBE    sing N N 41  
A1ILA CAZ   H1     sing N N 42  
A1ILA OBA   H2     sing N N 43  
A1ILA CAV   H3     sing N N 44  
A1ILA CAW   H4     sing N N 45  
A1ILA NAJ   H5     sing N N 46  
A1ILA CAD   H6     sing N N 47  
A1ILA CAC   H7     sing N N 48  
A1ILA OAA   H8     sing N N 49  
A1ILA CAM   H9     sing N N 50  
A1ILA CAM   H10    sing N N 51  
A1ILA CAN   H11    sing N N 52  
A1ILA CAN   H12    sing N N 53  
A1ILA CAO   H13    sing N N 54  
A1ILA CAO   H14    sing N N 55  
A1ILA CAP   H15    sing N N 56  
A1ILA CAP   H16    sing N N 57  
A1ILA CAQ   H17    sing N N 58  
A1ILA CAQ   H18    sing N N 59  
A1ILA CBC   H19    sing N N 60  
A1ILA CBD   H20    sing N N 61  
A1ILA CBD   H21    sing N N 62  
A1ILA CBE   H22    sing N N 63  
A1ILA CBE   H23    sing N N 64  
A1ILA CBF   H24    sing N N 65  
A1ILA NBJ   H25    sing N N 66  
A1ILA NBJ   H26    sing N N 67  
A1ILA CBG   H28    sing N N 68  
A1ILA CBG   H29    sing N N 69  
A1ILA CBH   H30    sing N N 70  
A1ILA CBH   H31    sing N N 71  
ALA   N     CA     sing N N 72  
ALA   N     H      sing N N 73  
ALA   N     H2     sing N N 74  
ALA   CA    C      sing N N 75  
ALA   CA    CB     sing N N 76  
ALA   CA    HA     sing N N 77  
ALA   C     O      doub N N 78  
ALA   C     OXT    sing N N 79  
ALA   CB    HB1    sing N N 80  
ALA   CB    HB2    sing N N 81  
ALA   CB    HB3    sing N N 82  
ALA   OXT   HXT    sing N N 83  
ARG   N     CA     sing N N 84  
ARG   N     H      sing N N 85  
ARG   N     H2     sing N N 86  
ARG   CA    C      sing N N 87  
ARG   CA    CB     sing N N 88  
ARG   CA    HA     sing N N 89  
ARG   C     O      doub N N 90  
ARG   C     OXT    sing N N 91  
ARG   CB    CG     sing N N 92  
ARG   CB    HB2    sing N N 93  
ARG   CB    HB3    sing N N 94  
ARG   CG    CD     sing N N 95  
ARG   CG    HG2    sing N N 96  
ARG   CG    HG3    sing N N 97  
ARG   CD    NE     sing N N 98  
ARG   CD    HD2    sing N N 99  
ARG   CD    HD3    sing N N 100 
ARG   NE    CZ     sing N N 101 
ARG   NE    HE     sing N N 102 
ARG   CZ    NH1    sing N N 103 
ARG   CZ    NH2    doub N N 104 
ARG   NH1   HH11   sing N N 105 
ARG   NH1   HH12   sing N N 106 
ARG   NH2   HH21   sing N N 107 
ARG   NH2   HH22   sing N N 108 
ARG   OXT   HXT    sing N N 109 
ASN   N     CA     sing N N 110 
ASN   N     H      sing N N 111 
ASN   N     H2     sing N N 112 
ASN   CA    C      sing N N 113 
ASN   CA    CB     sing N N 114 
ASN   CA    HA     sing N N 115 
ASN   C     O      doub N N 116 
ASN   C     OXT    sing N N 117 
ASN   CB    CG     sing N N 118 
ASN   CB    HB2    sing N N 119 
ASN   CB    HB3    sing N N 120 
ASN   CG    OD1    doub N N 121 
ASN   CG    ND2    sing N N 122 
ASN   ND2   HD21   sing N N 123 
ASN   ND2   HD22   sing N N 124 
ASN   OXT   HXT    sing N N 125 
ASP   N     CA     sing N N 126 
ASP   N     H      sing N N 127 
ASP   N     H2     sing N N 128 
ASP   CA    C      sing N N 129 
ASP   CA    CB     sing N N 130 
ASP   CA    HA     sing N N 131 
ASP   C     O      doub N N 132 
ASP   C     OXT    sing N N 133 
ASP   CB    CG     sing N N 134 
ASP   CB    HB2    sing N N 135 
ASP   CB    HB3    sing N N 136 
ASP   CG    OD1    doub N N 137 
ASP   CG    OD2    sing N N 138 
ASP   OD2   HD2    sing N N 139 
ASP   OXT   HXT    sing N N 140 
CYS   N     CA     sing N N 141 
CYS   N     H      sing N N 142 
CYS   N     H2     sing N N 143 
CYS   CA    C      sing N N 144 
CYS   CA    CB     sing N N 145 
CYS   CA    HA     sing N N 146 
CYS   C     O      doub N N 147 
CYS   C     OXT    sing N N 148 
CYS   CB    SG     sing N N 149 
CYS   CB    HB2    sing N N 150 
CYS   CB    HB3    sing N N 151 
CYS   SG    HG     sing N N 152 
CYS   OXT   HXT    sing N N 153 
EDO   C1    O1     sing N N 154 
EDO   C1    C2     sing N N 155 
EDO   C1    H11    sing N N 156 
EDO   C1    H12    sing N N 157 
EDO   O1    HO1    sing N N 158 
EDO   C2    O2     sing N N 159 
EDO   C2    H21    sing N N 160 
EDO   C2    H22    sing N N 161 
EDO   O2    HO2    sing N N 162 
GDP   PB    O1B    doub N N 163 
GDP   PB    O2B    sing N N 164 
GDP   PB    O3B    sing N N 165 
GDP   PB    O3A    sing N N 166 
GDP   O2B   HOB2   sing N N 167 
GDP   O3B   HOB3   sing N N 168 
GDP   O3A   PA     sing N N 169 
GDP   PA    O1A    doub N N 170 
GDP   PA    O2A    sing N N 171 
GDP   PA    "O5'"  sing N N 172 
GDP   O2A   HOA2   sing N N 173 
GDP   "O5'" "C5'"  sing N N 174 
GDP   "C5'" "C4'"  sing N N 175 
GDP   "C5'" "H5'"  sing N N 176 
GDP   "C5'" "H5''" sing N N 177 
GDP   "C4'" "O4'"  sing N N 178 
GDP   "C4'" "C3'"  sing N N 179 
GDP   "C4'" "H4'"  sing N N 180 
GDP   "O4'" "C1'"  sing N N 181 
GDP   "C3'" "O3'"  sing N N 182 
GDP   "C3'" "C2'"  sing N N 183 
GDP   "C3'" "H3'"  sing N N 184 
GDP   "O3'" "HO3'" sing N N 185 
GDP   "C2'" "O2'"  sing N N 186 
GDP   "C2'" "C1'"  sing N N 187 
GDP   "C2'" "H2'"  sing N N 188 
GDP   "O2'" "HO2'" sing N N 189 
GDP   "C1'" N9     sing N N 190 
GDP   "C1'" "H1'"  sing N N 191 
GDP   N9    C8     sing Y N 192 
GDP   N9    C4     sing Y N 193 
GDP   C8    N7     doub Y N 194 
GDP   C8    H8     sing N N 195 
GDP   N7    C5     sing Y N 196 
GDP   C5    C6     sing N N 197 
GDP   C5    C4     doub Y N 198 
GDP   C6    O6     doub N N 199 
GDP   C6    N1     sing N N 200 
GDP   N1    C2     sing N N 201 
GDP   N1    HN1    sing N N 202 
GDP   C2    N2     sing N N 203 
GDP   C2    N3     doub N N 204 
GDP   N2    HN21   sing N N 205 
GDP   N2    HN22   sing N N 206 
GDP   N3    C4     sing N N 207 
GLN   N     CA     sing N N 208 
GLN   N     H      sing N N 209 
GLN   N     H2     sing N N 210 
GLN   CA    C      sing N N 211 
GLN   CA    CB     sing N N 212 
GLN   CA    HA     sing N N 213 
GLN   C     O      doub N N 214 
GLN   C     OXT    sing N N 215 
GLN   CB    CG     sing N N 216 
GLN   CB    HB2    sing N N 217 
GLN   CB    HB3    sing N N 218 
GLN   CG    CD     sing N N 219 
GLN   CG    HG2    sing N N 220 
GLN   CG    HG3    sing N N 221 
GLN   CD    OE1    doub N N 222 
GLN   CD    NE2    sing N N 223 
GLN   NE2   HE21   sing N N 224 
GLN   NE2   HE22   sing N N 225 
GLN   OXT   HXT    sing N N 226 
GLU   N     CA     sing N N 227 
GLU   N     H      sing N N 228 
GLU   N     H2     sing N N 229 
GLU   CA    C      sing N N 230 
GLU   CA    CB     sing N N 231 
GLU   CA    HA     sing N N 232 
GLU   C     O      doub N N 233 
GLU   C     OXT    sing N N 234 
GLU   CB    CG     sing N N 235 
GLU   CB    HB2    sing N N 236 
GLU   CB    HB3    sing N N 237 
GLU   CG    CD     sing N N 238 
GLU   CG    HG2    sing N N 239 
GLU   CG    HG3    sing N N 240 
GLU   CD    OE1    doub N N 241 
GLU   CD    OE2    sing N N 242 
GLU   OE2   HE2    sing N N 243 
GLU   OXT   HXT    sing N N 244 
GLY   N     CA     sing N N 245 
GLY   N     H      sing N N 246 
GLY   N     H2     sing N N 247 
GLY   CA    C      sing N N 248 
GLY   CA    HA2    sing N N 249 
GLY   CA    HA3    sing N N 250 
GLY   C     O      doub N N 251 
GLY   C     OXT    sing N N 252 
GLY   OXT   HXT    sing N N 253 
HIS   N     CA     sing N N 254 
HIS   N     H      sing N N 255 
HIS   N     H2     sing N N 256 
HIS   CA    C      sing N N 257 
HIS   CA    CB     sing N N 258 
HIS   CA    HA     sing N N 259 
HIS   C     O      doub N N 260 
HIS   C     OXT    sing N N 261 
HIS   CB    CG     sing N N 262 
HIS   CB    HB2    sing N N 263 
HIS   CB    HB3    sing N N 264 
HIS   CG    ND1    sing Y N 265 
HIS   CG    CD2    doub Y N 266 
HIS   ND1   CE1    doub Y N 267 
HIS   ND1   HD1    sing N N 268 
HIS   CD2   NE2    sing Y N 269 
HIS   CD2   HD2    sing N N 270 
HIS   CE1   NE2    sing Y N 271 
HIS   CE1   HE1    sing N N 272 
HIS   NE2   HE2    sing N N 273 
HIS   OXT   HXT    sing N N 274 
HOH   O     H1     sing N N 275 
HOH   O     H2     sing N N 276 
ILE   N     CA     sing N N 277 
ILE   N     H      sing N N 278 
ILE   N     H2     sing N N 279 
ILE   CA    C      sing N N 280 
ILE   CA    CB     sing N N 281 
ILE   CA    HA     sing N N 282 
ILE   C     O      doub N N 283 
ILE   C     OXT    sing N N 284 
ILE   CB    CG1    sing N N 285 
ILE   CB    CG2    sing N N 286 
ILE   CB    HB     sing N N 287 
ILE   CG1   CD1    sing N N 288 
ILE   CG1   HG12   sing N N 289 
ILE   CG1   HG13   sing N N 290 
ILE   CG2   HG21   sing N N 291 
ILE   CG2   HG22   sing N N 292 
ILE   CG2   HG23   sing N N 293 
ILE   CD1   HD11   sing N N 294 
ILE   CD1   HD12   sing N N 295 
ILE   CD1   HD13   sing N N 296 
ILE   OXT   HXT    sing N N 297 
LEU   N     CA     sing N N 298 
LEU   N     H      sing N N 299 
LEU   N     H2     sing N N 300 
LEU   CA    C      sing N N 301 
LEU   CA    CB     sing N N 302 
LEU   CA    HA     sing N N 303 
LEU   C     O      doub N N 304 
LEU   C     OXT    sing N N 305 
LEU   CB    CG     sing N N 306 
LEU   CB    HB2    sing N N 307 
LEU   CB    HB3    sing N N 308 
LEU   CG    CD1    sing N N 309 
LEU   CG    CD2    sing N N 310 
LEU   CG    HG     sing N N 311 
LEU   CD1   HD11   sing N N 312 
LEU   CD1   HD12   sing N N 313 
LEU   CD1   HD13   sing N N 314 
LEU   CD2   HD21   sing N N 315 
LEU   CD2   HD22   sing N N 316 
LEU   CD2   HD23   sing N N 317 
LEU   OXT   HXT    sing N N 318 
LYS   N     CA     sing N N 319 
LYS   N     H      sing N N 320 
LYS   N     H2     sing N N 321 
LYS   CA    C      sing N N 322 
LYS   CA    CB     sing N N 323 
LYS   CA    HA     sing N N 324 
LYS   C     O      doub N N 325 
LYS   C     OXT    sing N N 326 
LYS   CB    CG     sing N N 327 
LYS   CB    HB2    sing N N 328 
LYS   CB    HB3    sing N N 329 
LYS   CG    CD     sing N N 330 
LYS   CG    HG2    sing N N 331 
LYS   CG    HG3    sing N N 332 
LYS   CD    CE     sing N N 333 
LYS   CD    HD2    sing N N 334 
LYS   CD    HD3    sing N N 335 
LYS   CE    NZ     sing N N 336 
LYS   CE    HE2    sing N N 337 
LYS   CE    HE3    sing N N 338 
LYS   NZ    HZ1    sing N N 339 
LYS   NZ    HZ2    sing N N 340 
LYS   NZ    HZ3    sing N N 341 
LYS   OXT   HXT    sing N N 342 
MET   N     CA     sing N N 343 
MET   N     H      sing N N 344 
MET   N     H2     sing N N 345 
MET   CA    C      sing N N 346 
MET   CA    CB     sing N N 347 
MET   CA    HA     sing N N 348 
MET   C     O      doub N N 349 
MET   C     OXT    sing N N 350 
MET   CB    CG     sing N N 351 
MET   CB    HB2    sing N N 352 
MET   CB    HB3    sing N N 353 
MET   CG    SD     sing N N 354 
MET   CG    HG2    sing N N 355 
MET   CG    HG3    sing N N 356 
MET   SD    CE     sing N N 357 
MET   CE    HE1    sing N N 358 
MET   CE    HE2    sing N N 359 
MET   CE    HE3    sing N N 360 
MET   OXT   HXT    sing N N 361 
PHE   N     CA     sing N N 362 
PHE   N     H      sing N N 363 
PHE   N     H2     sing N N 364 
PHE   CA    C      sing N N 365 
PHE   CA    CB     sing N N 366 
PHE   CA    HA     sing N N 367 
PHE   C     O      doub N N 368 
PHE   C     OXT    sing N N 369 
PHE   CB    CG     sing N N 370 
PHE   CB    HB2    sing N N 371 
PHE   CB    HB3    sing N N 372 
PHE   CG    CD1    doub Y N 373 
PHE   CG    CD2    sing Y N 374 
PHE   CD1   CE1    sing Y N 375 
PHE   CD1   HD1    sing N N 376 
PHE   CD2   CE2    doub Y N 377 
PHE   CD2   HD2    sing N N 378 
PHE   CE1   CZ     doub Y N 379 
PHE   CE1   HE1    sing N N 380 
PHE   CE2   CZ     sing Y N 381 
PHE   CE2   HE2    sing N N 382 
PHE   CZ    HZ     sing N N 383 
PHE   OXT   HXT    sing N N 384 
PRO   N     CA     sing N N 385 
PRO   N     CD     sing N N 386 
PRO   N     H      sing N N 387 
PRO   CA    C      sing N N 388 
PRO   CA    CB     sing N N 389 
PRO   CA    HA     sing N N 390 
PRO   C     O      doub N N 391 
PRO   C     OXT    sing N N 392 
PRO   CB    CG     sing N N 393 
PRO   CB    HB2    sing N N 394 
PRO   CB    HB3    sing N N 395 
PRO   CG    CD     sing N N 396 
PRO   CG    HG2    sing N N 397 
PRO   CG    HG3    sing N N 398 
PRO   CD    HD2    sing N N 399 
PRO   CD    HD3    sing N N 400 
PRO   OXT   HXT    sing N N 401 
SER   N     CA     sing N N 402 
SER   N     H      sing N N 403 
SER   N     H2     sing N N 404 
SER   CA    C      sing N N 405 
SER   CA    CB     sing N N 406 
SER   CA    HA     sing N N 407 
SER   C     O      doub N N 408 
SER   C     OXT    sing N N 409 
SER   CB    OG     sing N N 410 
SER   CB    HB2    sing N N 411 
SER   CB    HB3    sing N N 412 
SER   OG    HG     sing N N 413 
SER   OXT   HXT    sing N N 414 
THR   N     CA     sing N N 415 
THR   N     H      sing N N 416 
THR   N     H2     sing N N 417 
THR   CA    C      sing N N 418 
THR   CA    CB     sing N N 419 
THR   CA    HA     sing N N 420 
THR   C     O      doub N N 421 
THR   C     OXT    sing N N 422 
THR   CB    OG1    sing N N 423 
THR   CB    CG2    sing N N 424 
THR   CB    HB     sing N N 425 
THR   OG1   HG1    sing N N 426 
THR   CG2   HG21   sing N N 427 
THR   CG2   HG22   sing N N 428 
THR   CG2   HG23   sing N N 429 
THR   OXT   HXT    sing N N 430 
TYR   N     CA     sing N N 431 
TYR   N     H      sing N N 432 
TYR   N     H2     sing N N 433 
TYR   CA    C      sing N N 434 
TYR   CA    CB     sing N N 435 
TYR   CA    HA     sing N N 436 
TYR   C     O      doub N N 437 
TYR   C     OXT    sing N N 438 
TYR   CB    CG     sing N N 439 
TYR   CB    HB2    sing N N 440 
TYR   CB    HB3    sing N N 441 
TYR   CG    CD1    doub Y N 442 
TYR   CG    CD2    sing Y N 443 
TYR   CD1   CE1    sing Y N 444 
TYR   CD1   HD1    sing N N 445 
TYR   CD2   CE2    doub Y N 446 
TYR   CD2   HD2    sing N N 447 
TYR   CE1   CZ     doub Y N 448 
TYR   CE1   HE1    sing N N 449 
TYR   CE2   CZ     sing Y N 450 
TYR   CE2   HE2    sing N N 451 
TYR   CZ    OH     sing N N 452 
TYR   OH    HH     sing N N 453 
TYR   OXT   HXT    sing N N 454 
VAL   N     CA     sing N N 455 
VAL   N     H      sing N N 456 
VAL   N     H2     sing N N 457 
VAL   CA    C      sing N N 458 
VAL   CA    CB     sing N N 459 
VAL   CA    HA     sing N N 460 
VAL   C     O      doub N N 461 
VAL   C     OXT    sing N N 462 
VAL   CB    CG1    sing N N 463 
VAL   CB    CG2    sing N N 464 
VAL   CB    HB     sing N N 465 
VAL   CG1   HG11   sing N N 466 
VAL   CG1   HG12   sing N N 467 
VAL   CG1   HG13   sing N N 468 
VAL   CG2   HG21   sing N N 469 
VAL   CG2   HG22   sing N N 470 
VAL   CG2   HG23   sing N N 471 
VAL   OXT   HXT    sing N N 472 
# 
_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                    9GGW 
_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]   0.026980 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.024358 
_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]   0.004785 
_atom_sites.fract_transf_vector[1]      0.000000 
_atom_sites.fract_transf_vector[2]      0.000000 
_atom_sites.fract_transf_vector[3]      0.000000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
CL 
MG 
N  
O  
P  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N     . SER   A 1 3   ? -7.105  6.830   58.688  1.00 30.18 ? 0   SER   A N     1 
ATOM   2    C  CA    . SER   A 1 3   ? -5.750  6.280   58.529  1.00 28.52 ? 0   SER   A CA    1 
ATOM   3    C  C     . SER   A 1 3   ? -5.401  6.273   57.032  1.00 27.04 ? 0   SER   A C     1 
ATOM   4    O  O     . SER   A 1 3   ? -6.248  6.080   56.156  1.00 27.46 ? 0   SER   A O     1 
ATOM   5    C  CB    . SER   A 1 3   ? -5.615  4.907   59.171  1.00 29.06 ? 0   SER   A CB    1 
ATOM   6    O  OG    . SER   A 1 3   ? -4.258  4.646   59.510  1.00 28.66 ? 0   SER   A OG    1 
ATOM   7    N  N     . MET   A 1 4   ? -4.147  6.640   56.759  1.00 24.68 ? 1   MET   A N     1 
ATOM   8    C  CA    . MET   A 1 4   ? -3.643  6.851   55.379  1.00 23.32 ? 1   MET   A CA    1 
ATOM   9    C  C     . MET   A 1 4   ? -2.970  5.607   54.817  1.00 22.04 ? 1   MET   A C     1 
ATOM   10   O  O     . MET   A 1 4   ? -2.238  5.019   55.524  1.00 21.71 ? 1   MET   A O     1 
ATOM   11   C  CB    . MET   A 1 4   ? -2.500  7.858   55.403  1.00 22.48 ? 1   MET   A CB    1 
ATOM   12   C  CG    . MET   A 1 4   ? -2.854  9.250   55.410  1.00 22.99 ? 1   MET   A CG    1 
ATOM   13   S  SD    . MET   A 1 4   ? -1.256  10.154  55.201  1.00 22.11 ? 1   MET   A SD    1 
ATOM   14   C  CE    . MET   A 1 4   ? -1.023  10.475  56.929  1.00 22.84 ? 1   MET   A CE    1 
ATOM   15   N  N     . THR   A 1 5   ? -3.273  5.327   53.566  1.00 21.31 ? 2   THR   A N     1 
ATOM   16   C  CA    . THR   A 1 5   ? -2.696  4.214   52.828  1.00 20.39 ? 2   THR   A CA    1 
ATOM   17   C  C     . THR   A 1 5   ? -1.227  4.638   52.582  1.00 19.09 ? 2   THR   A C     1 
ATOM   18   O  O     . THR   A 1 5   ? -1.024  5.759   52.255  1.00 18.66 ? 2   THR   A O     1 
ATOM   19   C  CB    . THR   A 1 5   ? -3.477  4.000   51.530  1.00 20.61 ? 2   THR   A CB    1 
ATOM   20   O  OG1   . THR   A 1 5   ? -4.811  3.570   51.846  1.00 21.91 ? 2   THR   A OG1   1 
ATOM   21   C  CG2   . THR   A 1 5   ? -2.869  2.946   50.648  1.00 20.32 ? 2   THR   A CG2   1 
ATOM   22   N  N     . GLU   A 1 6   ? -0.307  3.737   52.804  1.00 18.68 ? 3   GLU   A N     1 
ATOM   23   C  CA    . GLU   A 1 6   ? 1.123   4.029   52.490  1.00 17.51 ? 3   GLU   A CA    1 
ATOM   24   C  C     . GLU   A 1 6   ? 1.462   3.283   51.215  1.00 16.79 ? 3   GLU   A C     1 
ATOM   25   O  O     . GLU   A 1 6   ? 1.154   2.131   51.134  1.00 17.49 ? 3   GLU   A O     1 
ATOM   26   C  CB    . GLU   A 1 6   ? 2.084   3.598   53.597  1.00 17.95 ? 3   GLU   A CB    1 
ATOM   27   C  CG    . GLU   A 1 6   ? 1.797   4.255   54.927  1.00 18.82 ? 3   GLU   A CG    1 
ATOM   28   C  CD    . GLU   A 1 6   ? 2.800   4.030   56.056  1.00 19.18 ? 3   GLU   A CD    1 
ATOM   29   O  OE1   . GLU   A 1 6   ? 3.855   3.366   55.806  1.00 18.95 ? 3   GLU   A OE1   1 
ATOM   30   O  OE2   . GLU   A 1 6   ? 2.571   4.573   57.123  1.00 19.77 ? 3   GLU   A OE2   1 
ATOM   31   N  N     . TYR   A 1 7   ? 2.060   3.967   50.267  1.00 15.47 ? 4   TYR   A N     1 
ATOM   32   C  CA    . TYR   A 1 7   ? 2.436   3.273   49.030  1.00 14.80 ? 4   TYR   A CA    1 
ATOM   33   C  C     . TYR   A 1 7   ? 3.961   3.053   49.073  1.00 14.11 ? 4   TYR   A C     1 
ATOM   34   O  O     . TYR   A 1 7   ? 4.635   3.995   49.224  1.00 13.73 ? 4   TYR   A O     1 
ATOM   35   C  CB    . TYR   A 1 7   ? 2.068   4.099   47.819  1.00 14.41 ? 4   TYR   A CB    1 
ATOM   36   C  CG    . TYR   A 1 7   ? 0.570   4.109   47.597  1.00 15.12 ? 4   TYR   A CG    1 
ATOM   37   C  CD1   . TYR   A 1 7   ? -0.064  3.031   47.020  1.00 15.62 ? 4   TYR   A CD1   1 
ATOM   38   C  CD2   . TYR   A 1 7   ? -0.206  5.162   48.043  1.00 15.51 ? 4   TYR   A CD2   1 
ATOM   39   C  CE1   . TYR   A 1 7   ? -1.442  3.020   46.824  1.00 16.49 ? 4   TYR   A CE1   1 
ATOM   40   C  CE2   . TYR   A 1 7   ? -1.590  5.156   47.875  1.00 16.39 ? 4   TYR   A CE2   1 
ATOM   41   C  CZ    . TYR   A 1 7   ? -2.203  4.094   47.237  1.00 16.88 ? 4   TYR   A CZ    1 
ATOM   42   O  OH    . TYR   A 1 7   ? -3.563  4.057   47.059  1.00 17.88 ? 4   TYR   A OH    1 
ATOM   43   N  N     . LYS   A 1 8   ? 4.367   1.801   48.980  1.00 14.30 ? 5   LYS   A N     1 
ATOM   44   C  CA    . LYS   A 1 8   ? 5.799   1.463   48.942  1.00 14.01 ? 5   LYS   A CA    1 
ATOM   45   C  C     . LYS   A 1 8   ? 6.279   1.445   47.487  1.00 13.34 ? 5   LYS   A C     1 
ATOM   46   O  O     . LYS   A 1 8   ? 5.976   0.523   46.727  1.00 13.58 ? 5   LYS   A O     1 
ATOM   47   C  CB    . LYS   A 1 8   ? 6.026   0.092   49.588  1.00 14.88 ? 5   LYS   A CB    1 
ATOM   48   C  CG    . LYS   A 1 8   ? 5.860   0.062   51.102  1.00 15.78 ? 5   LYS   A CG    1 
ATOM   49   C  CD    . LYS   A 1 8   ? 5.601   -1.342  51.628  1.00 17.11 ? 5   LYS   A CD    1 
ATOM   50   C  CE    . LYS   A 1 8   ? 5.176   -1.397  53.088  1.00 18.10 ? 5   LYS   A CE    1 
ATOM   51   N  NZ    . LYS   A 1 8   ? 3.816   -0.819  53.296  1.00 18.77 ? 5   LYS   A NZ    1 
ATOM   52   N  N     . LEU   A 1 9   ? 7.058   2.456   47.101  1.00 12.68 ? 6   LEU   A N     1 
ATOM   53   C  CA    . LEU   A 1 9   ? 7.547   2.608   45.752  1.00 12.41 ? 6   LEU   A CA    1 
ATOM   54   C  C     . LEU   A 1 9   ? 9.059   2.383   45.739  1.00 12.16 ? 6   LEU   A C     1 
ATOM   55   O  O     . LEU   A 1 9   ? 9.728   2.769   46.648  1.00 12.02 ? 6   LEU   A O     1 
ATOM   56   C  CB    . LEU   A 1 9   ? 7.250   4.022   45.279  1.00 12.21 ? 6   LEU   A CB    1 
ATOM   57   C  CG    . LEU   A 1 9   ? 5.813   4.462   45.562  1.00 12.56 ? 6   LEU   A CG    1 
ATOM   58   C  CD1   . LEU   A 1 9   ? 5.571   5.903   45.189  1.00 12.50 ? 6   LEU   A CD1   1 
ATOM   59   C  CD2   . LEU   A 1 9   ? 4.847   3.534   44.856  1.00 13.01 ? 6   LEU   A CD2   1 
ATOM   60   N  N     . VAL   A 1 10  ? 9.544   1.815   44.651  1.00 12.20 ? 7   VAL   A N     1 
ATOM   61   C  CA    . VAL   A 1 10  ? 10.971  1.547   44.539  1.00 12.13 ? 7   VAL   A CA    1 
ATOM   62   C  C     . VAL   A 1 10  ? 11.464  2.152   43.232  1.00 12.01 ? 7   VAL   A C     1 
ATOM   63   O  O     . VAL   A 1 10  ? 10.900  1.887   42.221  1.00 12.18 ? 7   VAL   A O     1 
ATOM   64   C  CB    . VAL   A 1 10  ? 11.233  0.039   44.611  1.00 12.56 ? 7   VAL   A CB    1 
ATOM   65   C  CG1   . VAL   A 1 10  ? 12.734  -0.252  44.525  1.00 12.63 ? 7   VAL   A CG1   1 
ATOM   66   C  CG2   . VAL   A 1 10  ? 10.629  -0.571  45.871  1.00 12.83 ? 7   VAL   A CG2   1 
ATOM   67   N  N     . VAL   A 1 11  ? 12.582  2.892   43.276  1.00 11.85 ? 8   VAL   A N     1 
ATOM   68   C  CA    . VAL   A 1 11  ? 13.137  3.514   42.080  1.00 11.87 ? 8   VAL   A CA    1 
ATOM   69   C  C     . VAL   A 1 11  ? 14.374  2.704   41.690  1.00 12.17 ? 8   VAL   A C     1 
ATOM   70   O  O     . VAL   A 1 11  ? 15.298  2.636   42.492  1.00 12.21 ? 8   VAL   A O     1 
ATOM   71   C  CB    . VAL   A 1 11  ? 13.490  4.994   42.294  1.00 11.82 ? 8   VAL   A CB    1 
ATOM   72   C  CG1   . VAL   A 1 11  ? 13.813  5.660   40.981  1.00 12.04 ? 8   VAL   A CG1   1 
ATOM   73   C  CG2   . VAL   A 1 11  ? 12.369  5.745   42.985  1.00 11.69 ? 8   VAL   A CG2   1 
ATOM   74   N  N     . VAL   A 1 12  ? 14.319  2.078   40.507  1.00 12.46 ? 9   VAL   A N     1 
ATOM   75   C  CA    . VAL   A 1 12  ? 15.343  1.180   39.988  1.00 12.92 ? 9   VAL   A CA    1 
ATOM   76   C  C     . VAL   A 1 12  ? 15.886  1.717   38.659  1.00 13.16 ? 9   VAL   A C     1 
ATOM   77   O  O     . VAL   A 1 12  ? 15.274  2.495   37.975  1.00 13.05 ? 9   VAL   A O     1 
ATOM   78   C  CB    . VAL   A 1 12  ? 14.888  -0.290  39.818  1.00 13.38 ? 9   VAL   A CB    1 
ATOM   79   C  CG1   . VAL   A 1 12  ? 14.432  -0.897  41.135  1.00 13.40 ? 9   VAL   A CG1   1 
ATOM   80   C  CG2   . VAL   A 1 12  ? 13.846  -0.496  38.720  1.00 13.59 ? 9   VAL   A CG2   1 
ATOM   81   N  N     . GLY   A 1 13  ? 17.079  1.245   38.303  1.00 13.63 ? 10  GLY   A N     1 
ATOM   82   C  CA    . GLY   A 1 13  ? 17.753  1.634   37.057  1.00 14.07 ? 10  GLY   A CA    1 
ATOM   83   C  C     . GLY   A 1 13  ? 19.245  1.770   37.288  1.00 14.47 ? 10  GLY   A C     1 
ATOM   84   O  O     . GLY   A 1 13  ? 19.654  1.862   38.433  1.00 14.29 ? 10  GLY   A O     1 
ATOM   85   N  N     . ALA   A 1 14  ? 20.005  1.843   36.189  1.00 15.10 ? 11  ALA   A N     1 
ATOM   86   C  CA    . ALA   A 1 14  ? 21.490  1.856   36.208  1.00 15.75 ? 11  ALA   A CA    1 
ATOM   87   C  C     . ALA   A 1 14  ? 21.977  3.072   36.999  1.00 15.52 ? 11  ALA   A C     1 
ATOM   88   O  O     . ALA   A 1 14  ? 21.341  4.100   36.995  1.00 15.07 ? 11  ALA   A O     1 
ATOM   89   C  CB    . ALA   A 1 14  ? 22.036  1.879   34.795  1.00 16.54 ? 11  ALA   A CB    1 
ATOM   90   N  N     . GLY   A 1 15  ? 23.144  2.968   37.638  1.00 15.96 ? 12  GLY   A N     1 
ATOM   91   C  CA    . GLY   A 1 15  ? 23.713  4.127   38.335  1.00 15.93 ? 12  GLY   A CA    1 
ATOM   92   C  C     . GLY   A 1 15  ? 23.831  5.299   37.375  1.00 16.20 ? 12  GLY   A C     1 
ATOM   93   O  O     . GLY   A 1 15  ? 24.113  5.105   36.188  1.00 16.78 ? 12  GLY   A O     1 
ATOM   94   N  N     . GLY   A 1 16  ? 23.510  6.500   37.874  1.00 15.84 ? 13  GLY   A N     1 
ATOM   95   C  CA    . GLY   A 1 16  ? 23.728  7.756   37.153  1.00 16.25 ? 13  GLY   A CA    1 
ATOM   96   C  C     . GLY   A 1 16  ? 22.597  8.183   36.218  1.00 15.96 ? 13  GLY   A C     1 
ATOM   97   O  O     . GLY   A 1 16  ? 22.799  9.120   35.472  1.00 16.46 ? 13  GLY   A O     1 
ATOM   98   N  N     . VAL   A 1 17  ? 21.397  7.572   36.307  1.00 15.26 ? 14  VAL   A N     1 
ATOM   99   C  CA    . VAL   A 1 17  ? 20.274  7.963   35.427  1.00 15.09 ? 14  VAL   A CA    1 
ATOM   100  C  C     . VAL   A 1 17  ? 19.439  9.076   36.090  1.00 14.62 ? 14  VAL   A C     1 
ATOM   101  O  O     . VAL   A 1 17  ? 18.683  9.757   35.408  1.00 14.69 ? 14  VAL   A O     1 
ATOM   102  C  CB    . VAL   A 1 17  ? 19.357  6.780   35.054  1.00 14.79 ? 14  VAL   A CB    1 
ATOM   103  C  CG1   . VAL   A 1 17  ? 20.106  5.722   34.264  1.00 15.41 ? 14  VAL   A CG1   1 
ATOM   104  C  CG2   . VAL   A 1 17  ? 18.700  6.191   36.289  1.00 14.09 ? 14  VAL   A CG2   1 
ATOM   105  N  N     . GLY   A 1 18  ? 19.573  9.209   37.412  1.00 14.26 ? 15  GLY   A N     1 
ATOM   106  C  CA    . GLY   A 1 18  ? 18.977  10.274  38.193  1.00 13.97 ? 15  GLY   A CA    1 
ATOM   107  C  C     . GLY   A 1 18  ? 17.892  9.778   39.140  1.00 13.27 ? 15  GLY   A C     1 
ATOM   108  O  O     . GLY   A 1 18  ? 16.960  10.513  39.416  1.00 13.07 ? 15  GLY   A O     1 
ATOM   109  N  N     . LYS   A 1 19  ? 18.066  8.575   39.692  1.00 13.04 ? 16  LYS   A N     1 
ATOM   110  C  CA    . LYS   A 1 19  ? 17.135  8.001   40.664  1.00 12.53 ? 16  LYS   A CA    1 
ATOM   111  C  C     . LYS   A 1 19  ? 17.088  8.894   41.916  1.00 12.39 ? 16  LYS   A C     1 
ATOM   112  O  O     . LYS   A 1 19  ? 16.022  9.292   42.363  1.00 12.13 ? 16  LYS   A O     1 
ATOM   113  C  CB    . LYS   A 1 19  ? 17.525  6.557   41.017  1.00 12.52 ? 16  LYS   A CB    1 
ATOM   114  C  CG    . LYS   A 1 19  ? 17.484  5.564   39.851  1.00 12.75 ? 16  LYS   A CG    1 
ATOM   115  C  CD    . LYS   A 1 19  ? 17.741  4.116   40.214  1.00 12.87 ? 16  LYS   A CD    1 
ATOM   116  C  CE    . LYS   A 1 19  ? 19.097  3.826   40.817  1.00 13.23 ? 16  LYS   A CE    1 
ATOM   117  N  NZ    . LYS   A 1 19  ? 20.187  4.225   39.902  1.00 13.78 ? 16  LYS   A NZ    1 
ATOM   118  N  N     . SER   A 1 20  ? 18.261  9.284   42.423  1.00 12.70 ? 17  SER   A N     1 
ATOM   119  C  CA    . SER   A 1 20  ? 18.351  10.117  43.616  1.00 12.72 ? 17  SER   A CA    1 
ATOM   120  C  C     . SER   A 1 20  ? 17.824  11.521  43.299  1.00 12.87 ? 17  SER   A C     1 
ATOM   121  O  O     . SER   A 1 20  ? 17.042  12.083  44.078  1.00 12.73 ? 17  SER   A O     1 
ATOM   122  C  CB    . SER   A 1 20  ? 19.781  10.135  44.187  1.00 13.17 ? 17  SER   A CB    1 
ATOM   123  O  OG    . SER   A 1 20  ? 20.214  8.826   44.571  1.00 13.14 ? 17  SER   A OG    1 
ATOM   124  N  N     . ALA   A 1 21  ? 18.216  12.097  42.152  1.00 13.27 ? 18  ALA   A N     1 
ATOM   125  C  CA    . ALA   A 1 21  ? 17.755  13.448  41.811  1.00 13.58 ? 18  ALA   A CA    1 
ATOM   126  C  C     . ALA   A 1 21  ? 16.217  13.492  41.724  1.00 13.22 ? 18  ALA   A C     1 
ATOM   127  O  O     . ALA   A 1 21  ? 15.596  14.435  42.192  1.00 13.35 ? 18  ALA   A O     1 
ATOM   128  C  CB    . ALA   A 1 21  ? 18.373  13.886  40.508  1.00 14.17 ? 18  ALA   A CB    1 
ATOM   129  N  N     . LEU   A 1 22  ? 15.624  12.490  41.071  1.00 12.90 ? 19  LEU   A N     1 
ATOM   130  C  CA    . LEU   A 1 22  ? 14.146  12.415  40.918  1.00 12.67 ? 19  LEU   A CA    1 
ATOM   131  C  C     . LEU   A 1 22  ? 13.448  12.384  42.286  1.00 12.41 ? 19  LEU   A C     1 
ATOM   132  O  O     . LEU   A 1 22  ? 12.394  13.019  42.501  1.00 12.64 ? 19  LEU   A O     1 
ATOM   133  C  CB    . LEU   A 1 22  ? 13.762  11.177  40.109  1.00 12.55 ? 19  LEU   A CB    1 
ATOM   134  C  CG    . LEU   A 1 22  ? 13.956  11.265  38.587  1.00 13.08 ? 19  LEU   A CG    1 
ATOM   135  C  CD1   . LEU   A 1 22  ? 13.890  9.873   37.968  1.00 13.05 ? 19  LEU   A CD1   1 
ATOM   136  C  CD2   . LEU   A 1 22  ? 12.946  12.202  37.916  1.00 13.41 ? 19  LEU   A CD2   1 
ATOM   137  N  N     . THR   A 1 23  ? 13.992  11.567  43.188  1.00 12.16 ? 20  THR   A N     1 
ATOM   138  C  CA    . THR   A 1 23  ? 13.396  11.310  44.497  1.00 11.96 ? 20  THR   A CA    1 
ATOM   139  C  C     . THR   A 1 23  ? 13.523  12.580  45.332  1.00 12.30 ? 20  THR   A C     1 
ATOM   140  O  O     . THR   A 1 23  ? 12.574  13.066  45.893  1.00 12.42 ? 20  THR   A O     1 
ATOM   141  C  CB    . THR   A 1 23  ? 14.094  10.116  45.163  1.00 11.79 ? 20  THR   A CB    1 
ATOM   142  O  OG1   . THR   A 1 23  ? 13.910  8.969   44.323  1.00 11.62 ? 20  THR   A OG1   1 
ATOM   143  C  CG2   . THR   A 1 23  ? 13.611  9.880   46.585  1.00 11.74 ? 20  THR   A CG2   1 
ATOM   144  N  N     . ILE   A 1 24  ? 14.731  13.149  45.346  1.00 12.53 ? 21  ILE   A N     1 
ATOM   145  C  CA    . ILE   A 1 24  ? 14.981  14.376  46.083  1.00 13.04 ? 21  ILE   A CA    1 
ATOM   146  C  C     . ILE   A 1 24  ? 14.137  15.527  45.493  1.00 13.43 ? 21  ILE   A C     1 
ATOM   147  O  O     . ILE   A 1 24  ? 13.708  16.408  46.242  1.00 13.71 ? 21  ILE   A O     1 
ATOM   148  C  CB    . ILE   A 1 24  ? 16.491  14.678  46.139  1.00 13.42 ? 21  ILE   A CB    1 
ATOM   149  C  CG1   . ILE   A 1 24  ? 17.208  13.571  46.923  1.00 13.20 ? 21  ILE   A CG1   1 
ATOM   150  C  CG2   . ILE   A 1 24  ? 16.746  16.052  46.758  1.00 14.06 ? 21  ILE   A CG2   1 
ATOM   151  C  CD1   . ILE   A 1 24  ? 18.738  13.511  46.730  1.00 13.58 ? 21  ILE   A CD1   1 
ATOM   152  N  N     . GLN   A 1 25  ? 13.946  15.550  44.171  1.00 13.58 ? 22  GLN   A N     1 
ATOM   153  C  CA    . GLN   A 1 25  ? 13.124  16.599  43.550  1.00 14.25 ? 22  GLN   A CA    1 
ATOM   154  C  C     . GLN   A 1 25  ? 11.701  16.510  44.113  1.00 14.25 ? 22  GLN   A C     1 
ATOM   155  O  O     . GLN   A 1 25  ? 11.072  17.536  44.423  1.00 14.76 ? 22  GLN   A O     1 
ATOM   156  C  CB    . GLN   A 1 25  ? 13.168  16.478  42.024  1.00 14.41 ? 22  GLN   A CB    1 
ATOM   157  C  CG    . GLN   A 1 25  ? 12.366  17.538  41.283  1.00 15.13 ? 22  GLN   A CG    1 
ATOM   158  C  CD    . GLN   A 1 25  ? 12.730  18.978  41.577  1.00 15.89 ? 22  GLN   A CD    1 
ATOM   159  O  OE1   . GLN   A 1 25  ? 11.993  19.678  42.256  1.00 16.16 ? 22  GLN   A OE1   1 
ATOM   160  N  NE2   . GLN   A 1 25  ? 13.861  19.445  41.060  1.00 16.28 ? 22  GLN   A NE2   1 
ATOM   161  N  N     . LEU   A 1 26  ? 11.219  15.286  44.213  1.00 13.90 ? 23  LEU   A N     1 
ATOM   162  C  CA    . LEU   A 1 26  ? 9.842   15.086  44.761  1.00 14.10 ? 23  LEU   A CA    1 
ATOM   163  C  C     . LEU   A 1 26  ? 9.783   15.491  46.233  1.00 14.41 ? 23  LEU   A C     1 
ATOM   164  O  O     . LEU   A 1 26  ? 8.854   16.128  46.592  1.00 14.78 ? 23  LEU   A O     1 
ATOM   165  C  CB    . LEU   A 1 26  ? 9.367   13.646  44.612  1.00 13.71 ? 23  LEU   A CB    1 
ATOM   166  C  CG    . LEU   A 1 26  ? 7.922   13.389  45.068  1.00 14.00 ? 23  LEU   A CG    1 
ATOM   167  C  CD1   . LEU   A 1 26  ? 6.957   13.751  43.959  1.00 14.25 ? 23  LEU   A CD1   1 
ATOM   168  C  CD2   . LEU   A 1 26  ? 7.722   11.949  45.436  1.00 13.79 ? 23  LEU   A CD2   1 
ATOM   169  N  N     . ILE   A 1 27  ? 10.721  15.038  47.054  1.00 14.29 ? 24  ILE   A N     1 
ATOM   170  C  CA    . ILE   A 1 27  ? 10.723  15.371  48.504  1.00 14.72 ? 24  ILE   A CA    1 
ATOM   171  C  C     . ILE   A 1 27  ? 11.018  16.830  48.821  1.00 15.37 ? 24  ILE   A C     1 
ATOM   172  O  O     . ILE   A 1 27  ? 10.324  17.378  49.644  1.00 15.75 ? 24  ILE   A O     1 
ATOM   173  C  CB    . ILE   A 1 27  ? 11.772  14.521  49.221  1.00 14.81 ? 24  ILE   A CB    1 
ATOM   174  C  CG1   . ILE   A 1 27  ? 11.616  13.035  48.915  1.00 14.46 ? 24  ILE   A CG1   1 
ATOM   175  C  CG2   . ILE   A 1 27  ? 11.841  14.836  50.696  1.00 15.22 ? 24  ILE   A CG2   1 
ATOM   176  C  CD1   . ILE   A 1 27  ? 10.306  12.475  49.333  1.00 14.51 ? 24  ILE   A CD1   1 
ATOM   177  N  N     . GLN   A 1 28  ? 12.046  17.392  48.193  1.00 15.46 ? 25  GLN   A N     1 
ATOM   178  C  CA    . GLN   A 1 28  ? 12.558  18.699  48.636  1.00 16.23 ? 25  GLN   A CA    1 
ATOM   179  C  C     . GLN   A 1 28  ? 12.268  19.818  47.648  1.00 16.78 ? 25  GLN   A C     1 
ATOM   180  O  O     . GLN   A 1 28  ? 12.603  20.901  48.025  1.00 17.34 ? 25  GLN   A O     1 
ATOM   181  C  CB    . GLN   A 1 28  ? 14.093  18.606  48.777  1.00 16.28 ? 25  GLN   A CB    1 
ATOM   182  C  CG    . GLN   A 1 28  ? 14.556  17.673  49.878  1.00 16.18 ? 25  GLN   A CG    1 
ATOM   183  C  CD    . GLN   A 1 28  ? 14.287  18.236  51.247  1.00 16.76 ? 25  GLN   A CD    1 
ATOM   184  O  OE1   . GLN   A 1 28  ? 13.546  19.178  51.389  1.00 17.52 ? 25  GLN   A OE1   1 
ATOM   185  N  NE2   . GLN   A 1 28  ? 14.844  17.634  52.261  1.00 16.61 ? 25  GLN   A NE2   1 
ATOM   186  N  N     . ASN   A 1 29  ? 11.731  19.512  46.468  1.00 16.99 ? 26  ASN   A N     1 
ATOM   187  C  CA    . ASN   A 1 29  ? 11.530  20.548  45.411  1.00 17.74 ? 26  ASN   A CA    1 
ATOM   188  C  C     . ASN   A 1 29  ? 12.873  21.204  45.067  1.00 18.31 ? 26  ASN   A C     1 
ATOM   189  O  O     . ASN   A 1 29  ? 12.932  22.420  44.861  1.00 19.00 ? 26  ASN   A O     1 
ATOM   190  C  CB    . ASN   A 1 29  ? 10.537  21.646  45.802  1.00 18.86 ? 26  ASN   A CB    1 
ATOM   191  C  CG    . ASN   A 1 29  ? 9.117   21.194  45.577  1.00 19.02 ? 26  ASN   A CG    1 
ATOM   192  O  OD1   . ASN   A 1 29  ? 8.475   21.597  44.608  1.00 20.08 ? 26  ASN   A OD1   1 
ATOM   193  N  ND2   . ASN   A 1 29  ? 8.661   20.301  46.427  1.00 18.59 ? 26  ASN   A ND2   1 
ATOM   194  N  N     . HIS   A 1 30  ? 13.931  20.388  45.022  1.00 17.86 ? 27  HIS   A N     1 
ATOM   195  C  CA    . HIS   A 1 30  ? 15.288  20.873  44.802  1.00 18.47 ? 27  HIS   A CA    1 
ATOM   196  C  C     . HIS   A 1 30  ? 16.040  19.844  43.958  1.00 17.91 ? 27  HIS   A C     1 
ATOM   197  O  O     . HIS   A 1 30  ? 15.931  18.653  44.182  1.00 16.90 ? 27  HIS   A O     1 
ATOM   198  C  CB    . HIS   A 1 30  ? 15.969  21.158  46.142  1.00 18.76 ? 27  HIS   A CB    1 
ATOM   199  C  CG    . HIS   A 1 30  ? 17.450  21.423  46.071  1.00 19.50 ? 27  HIS   A CG    1 
ATOM   200  N  ND1   . HIS   A 1 30  ? 17.994  22.573  45.520  1.00 20.50 ? 27  HIS   A ND1   1 
ATOM   201  C  CD2   . HIS   A 1 30  ? 18.488  20.717  46.561  1.00 19.28 ? 27  HIS   A CD2   1 
ATOM   202  C  CE1   . HIS   A 1 30  ? 19.302  22.548  45.647  1.00 20.96 ? 27  HIS   A CE1   1 
ATOM   203  N  NE2   . HIS   A 1 30  ? 19.639  21.413  46.289  1.00 20.21 ? 27  HIS   A NE2   1 
ATOM   204  N  N     . PHE   A 1 31  ? 16.811  20.354  42.997  1.00 18.83 ? 28  PHE   A N     1 
ATOM   205  C  CA    . PHE   A 1 31  ? 17.721  19.547  42.204  1.00 18.76 ? 28  PHE   A CA    1 
ATOM   206  C  C     . PHE   A 1 31  ? 19.084  19.474  42.901  1.00 19.55 ? 28  PHE   A C     1 
ATOM   207  O  O     . PHE   A 1 31  ? 19.742  20.495  43.074  1.00 20.13 ? 28  PHE   A O     1 
ATOM   208  C  CB    . PHE   A 1 31  ? 17.904  20.149  40.811  1.00 19.37 ? 28  PHE   A CB    1 
ATOM   209  C  CG    . PHE   A 1 31  ? 18.851  19.381  39.921  1.00 19.37 ? 28  PHE   A CG    1 
ATOM   210  C  CD1   . PHE   A 1 31  ? 18.619  18.045  39.635  1.00 18.68 ? 28  PHE   A CD1   1 
ATOM   211  C  CD2   . PHE   A 1 31  ? 19.942  20.004  39.330  1.00 20.27 ? 28  PHE   A CD2   1 
ATOM   212  C  CE1   . PHE   A 1 31  ? 19.459  17.344  38.779  1.00 18.86 ? 28  PHE   A CE1   1 
ATOM   213  C  CE2   . PHE   A 1 31  ? 20.796  19.300  38.493  1.00 20.57 ? 28  PHE   A CE2   1 
ATOM   214  C  CZ    . PHE   A 1 31  ? 20.552  17.972  38.207  1.00 19.79 ? 28  PHE   A CZ    1 
ATOM   215  N  N     . VAL   A 1 32  ? 19.526  18.250  43.202  1.00 19.62 ? 29  VAL   A N     1 
ATOM   216  C  CA    . VAL   A 1 32  ? 20.913  18.001  43.673  1.00 20.39 ? 29  VAL   A CA    1 
ATOM   217  C  C     . VAL   A 1 32  ? 21.814  17.687  42.473  1.00 21.29 ? 29  VAL   A C     1 
ATOM   218  O  O     . VAL   A 1 32  ? 21.506  16.798  41.675  1.00 21.58 ? 29  VAL   A O     1 
ATOM   219  C  CB    . VAL   A 1 32  ? 20.956  16.887  44.740  1.00 19.79 ? 29  VAL   A CB    1 
ATOM   220  C  CG1   . VAL   A 1 32  ? 20.322  17.371  46.036  1.00 19.52 ? 29  VAL   A CG1   1 
ATOM   221  C  CG2   . VAL   A 1 32  ? 20.297  15.585  44.276  1.00 19.21 ? 29  VAL   A CG2   1 
ATOM   222  N  N     . ASP   A 1 33  ? 22.902  18.445  42.337  1.00 22.50 ? 30  ASP   A N     1 
ATOM   223  C  CA    . ASP   A 1 33  ? 23.938  18.247  41.274  1.00 23.56 ? 30  ASP   A CA    1 
ATOM   224  C  C     . ASP   A 1 33  ? 24.679  16.941  41.563  1.00 22.59 ? 30  ASP   A C     1 
ATOM   225  O  O     . ASP   A 1 33  ? 24.995  16.218  40.651  1.00 22.90 ? 30  ASP   A O     1 
ATOM   226  C  CB    . ASP   A 1 33  ? 24.926  19.415  41.226  1.00 25.41 ? 30  ASP   A CB    1 
ATOM   227  C  CG    . ASP   A 1 33  ? 24.430  20.554  40.352  1.00 26.86 ? 30  ASP   A CG    1 
ATOM   228  O  OD1   . ASP   A 1 33  ? 24.565  20.469  39.148  1.00 27.71 ? 30  ASP   A OD1   1 
ATOM   229  O  OD2   . ASP   A 1 33  ? 23.876  21.484  40.889  1.00 27.79 ? 30  ASP   A OD2   1 
ATOM   230  N  N     . GLU   A 1 34  ? 24.875  16.662  42.835  1.00 21.48 ? 31  GLU   A N     1 
ATOM   231  C  CA    . GLU   A 1 34  ? 25.481  15.378  43.220  1.00 20.63 ? 31  GLU   A CA    1 
ATOM   232  C  C     . GLU   A 1 34  ? 24.787  14.871  44.485  1.00 19.12 ? 31  GLU   A C     1 
ATOM   233  O  O     . GLU   A 1 34  ? 24.422  15.642  45.332  1.00 18.90 ? 31  GLU   A O     1 
ATOM   234  C  CB    . GLU   A 1 34  ? 26.995  15.525  43.429  1.00 21.94 ? 31  GLU   A CB    1 
ATOM   235  C  CG    . GLU   A 1 34  ? 27.440  16.902  43.825  1.00 23.00 ? 31  GLU   A CG    1 
ATOM   236  C  CD    . GLU   A 1 34  ? 28.970  17.037  43.683  1.00 24.58 ? 31  GLU   A CD    1 
ATOM   237  O  OE1   . GLU   A 1 34  ? 29.502  16.706  42.629  1.00 24.80 ? 31  GLU   A OE1   1 
ATOM   238  O  OE2   . GLU   A 1 34  ? 29.591  17.417  44.663  1.00 25.25 ? 31  GLU   A OE2   1 
ATOM   239  N  N     . TYR   A 1 35  ? 24.648  13.576  44.548  1.00 17.58 ? 32  TYR   A N     1 
ATOM   240  C  CA    . TYR   A 1 35  ? 24.209  12.883  45.769  1.00 16.55 ? 32  TYR   A CA    1 
ATOM   241  C  C     . TYR   A 1 35  ? 24.976  11.565  45.708  1.00 16.33 ? 32  TYR   A C     1 
ATOM   242  O  O     . TYR   A 1 35  ? 24.873  10.908  44.685  1.00 16.09 ? 32  TYR   A O     1 
ATOM   243  C  CB    . TYR   A 1 35  ? 22.699  12.610  45.763  1.00 15.47 ? 32  TYR   A CB    1 
ATOM   244  C  CG    . TYR   A 1 35  ? 22.084  12.229  47.084  1.00 14.95 ? 32  TYR   A CG    1 
ATOM   245  C  CD1   . TYR   A 1 35  ? 22.049  13.113  48.140  1.00 15.09 ? 32  TYR   A CD1   1 
ATOM   246  C  CD2   . TYR   A 1 35  ? 21.488  10.995  47.267  1.00 14.38 ? 32  TYR   A CD2   1 
ATOM   247  C  CE1   . TYR   A 1 35  ? 21.482  12.770  49.350  1.00 14.88 ? 32  TYR   A CE1   1 
ATOM   248  C  CE2   . TYR   A 1 35  ? 20.913  10.638  48.470  1.00 14.06 ? 32  TYR   A CE2   1 
ATOM   249  C  CZ    . TYR   A 1 35  ? 20.875  11.538  49.508  1.00 14.35 ? 32  TYR   A CZ    1 
ATOM   250  O  OH    . TYR   A 1 35  ? 20.283  11.212  50.681  1.00 14.12 ? 32  TYR   A OH    1 
ATOM   251  N  N     . ASP   A 1 36  ? 25.669  11.255  46.789  1.00 16.35 ? 33  ASP   A N     1 
ATOM   252  C  CA    . ASP   A 1 36  ? 26.508  10.073  46.920  1.00 16.70 ? 33  ASP   A CA    1 
ATOM   253  C  C     . ASP   A 1 36  ? 25.892  8.871   46.198  1.00 16.12 ? 33  ASP   A C     1 
ATOM   254  O  O     . ASP   A 1 36  ? 24.827  8.384   46.556  1.00 15.38 ? 33  ASP   A O     1 
ATOM   255  C  CB    . ASP   A 1 36  ? 26.697  9.787   48.406  1.00 16.82 ? 33  ASP   A CB    1 
ATOM   256  C  CG    . ASP   A 1 36  ? 27.519  8.541   48.707  1.00 17.28 ? 33  ASP   A CG    1 
ATOM   257  O  OD1   . ASP   A 1 36  ? 27.703  7.678   47.803  1.00 17.32 ? 33  ASP   A OD1   1 
ATOM   258  O  OD2   . ASP   A 1 36  ? 28.005  8.466   49.841  1.00 17.73 ? 33  ASP   A OD2   1 
ATOM   259  N  N     . PRO   A 1 37  ? 26.562  8.307   45.160  1.00 16.57 ? 34  PRO   A N     1 
ATOM   260  C  CA    . PRO   A 1 37  ? 25.908  7.273   44.363  1.00 16.12 ? 34  PRO   A CA    1 
ATOM   261  C  C     . PRO   A 1 37  ? 25.709  5.919   45.058  1.00 15.93 ? 34  PRO   A C     1 
ATOM   262  O  O     . PRO   A 1 37  ? 24.897  5.125   44.571  1.00 15.48 ? 34  PRO   A O     1 
ATOM   263  C  CB    . PRO   A 1 37  ? 26.751  7.163   43.093  1.00 16.84 ? 34  PRO   A CB    1 
ATOM   264  C  CG    . PRO   A 1 37  ? 27.672  8.355   43.145  1.00 17.60 ? 34  PRO   A CG    1 
ATOM   265  C  CD    . PRO   A 1 37  ? 27.887  8.652   44.613  1.00 17.63 ? 34  PRO   A CD    1 
ATOM   266  N  N     . THR   A 1 38  ? 26.295  5.722   46.224  1.00 16.29 ? 35  THR   A N     1 
ATOM   267  C  CA    . THR   A 1 38  ? 26.217  4.439   46.950  1.00 16.33 ? 35  THR   A CA    1 
ATOM   268  C  C     . THR   A 1 38  ? 25.060  4.410   47.976  1.00 15.79 ? 35  THR   A C     1 
ATOM   269  O  O     . THR   A 1 38  ? 24.907  3.415   48.628  1.00 15.83 ? 35  THR   A O     1 
ATOM   270  C  CB    . THR   A 1 38  ? 27.537  4.207   47.718  1.00 17.32 ? 35  THR   A CB    1 
ATOM   271  O  OG1   . THR   A 1 38  ? 27.634  5.104   48.816  1.00 17.35 ? 35  THR   A OG1   1 
ATOM   272  C  CG2   . THR   A 1 38  ? 28.748  4.359   46.815  1.00 18.21 ? 35  THR   A CG2   1 
ATOM   273  N  N     . ILE   A 1 39  ? 24.353  5.518   48.112  1.00 15.41 ? 36  ILE   A N     1 
ATOM   274  C  CA    . ILE   A 1 39  ? 23.300  5.604   49.152  1.00 15.12 ? 36  ILE   A CA    1 
ATOM   275  C  C     . ILE   A 1 39  ? 21.975  5.036   48.644  1.00 14.38 ? 36  ILE   A C     1 
ATOM   276  O  O     . ILE   A 1 39  ? 21.454  5.574   47.749  1.00 13.89 ? 36  ILE   A O     1 
ATOM   277  C  CB    . ILE   A 1 39  ? 23.114  7.040   49.610  1.00 15.34 ? 36  ILE   A CB    1 
ATOM   278  C  CG1   . ILE   A 1 39  ? 24.332  7.514   50.392  1.00 16.29 ? 36  ILE   A CG1   1 
ATOM   279  C  CG2   . ILE   A 1 39  ? 21.917  7.122   50.531  1.00 14.83 ? 36  ILE   A CG2   1 
ATOM   280  C  CD1   . ILE   A 1 39  ? 24.289  8.949   50.714  1.00 16.66 ? 36  ILE   A CD1   1 
ATOM   281  N  N     . GLU   A 1 40  ? 21.520  3.998   49.327  1.00 14.46 ? 37  GLU   A N     1 
ATOM   282  C  CA    . GLU   A 1 40  ? 20.213  3.331   49.143  1.00 14.05 ? 37  GLU   A CA    1 
ATOM   283  C  C     . GLU   A 1 40  ? 19.414  3.665   50.416  1.00 13.92 ? 37  GLU   A C     1 
ATOM   284  O  O     . GLU   A 1 40  ? 19.844  3.358   51.468  1.00 14.36 ? 37  GLU   A O     1 
ATOM   285  C  CB    . GLU   A 1 40  ? 20.413  1.850   48.868  1.00 14.38 ? 37  GLU   A CB    1 
ATOM   286  C  CG    . GLU   A 1 40  ? 19.171  0.992   49.035  1.00 14.12 ? 37  GLU   A CG    1 
ATOM   287  C  CD    . GLU   A 1 40  ? 19.356  -0.317  48.317  1.00 14.50 ? 37  GLU   A CD    1 
ATOM   288  O  OE1   . GLU   A 1 40  ? 19.666  -0.301  47.161  1.00 14.52 ? 37  GLU   A OE1   1 
ATOM   289  O  OE2   . GLU   A 1 40  ? 19.261  -1.277  48.936  1.00 14.83 ? 37  GLU   A OE2   1 
ATOM   290  N  N     . ASP   A 1 41  ? 18.285  4.341   50.274  1.00 13.52 ? 38  ASP   A N     1 
ATOM   291  C  CA    . ASP   A 1 41  ? 17.562  4.774   51.466  1.00 13.44 ? 38  ASP   A CA    1 
ATOM   292  C  C     . ASP   A 1 41  ? 16.094  5.035   51.133  1.00 12.99 ? 38  ASP   A C     1 
ATOM   293  O  O     . ASP   A 1 41  ? 15.703  5.076   49.940  1.00 12.75 ? 38  ASP   A O     1 
ATOM   294  C  CB    . ASP   A 1 41  ? 18.214  6.025   52.077  1.00 13.68 ? 38  ASP   A CB    1 
ATOM   295  C  CG    . ASP   A 1 41  ? 18.305  5.987   53.596  1.00 14.12 ? 38  ASP   A CG    1 
ATOM   296  O  OD1   . ASP   A 1 41  ? 17.370  5.505   54.236  1.00 14.05 ? 38  ASP   A OD1   1 
ATOM   297  O  OD2   . ASP   A 1 41  ? 19.348  6.381   54.121  1.00 14.57 ? 38  ASP   A OD2   1 
ATOM   298  N  N     . SER   A 1 42  ? 15.312  5.217   52.199  1.00 13.06 ? 39  SER   A N     1 
ATOM   299  C  CA    . SER   A 1 42  ? 13.886  5.479   52.110  1.00 12.89 ? 39  SER   A CA    1 
ATOM   300  C  C     . SER   A 1 42  ? 13.636  6.974   52.280  1.00 12.78 ? 39  SER   A C     1 
ATOM   301  O  O     . SER   A 1 42  ? 14.269  7.616   53.116  1.00 12.80 ? 39  SER   A O     1 
ATOM   302  C  CB    . SER   A 1 42  ? 13.112  4.673   53.132  1.00 13.33 ? 39  SER   A CB    1 
ATOM   303  O  OG    . SER   A 1 42  ? 13.496  4.999   54.449  1.00 13.83 ? 39  SER   A OG    1 
ATOM   304  N  N     . TYR   A 1 43  ? 12.667  7.495   51.521  1.00 12.39 ? 40  TYR   A N     1 
ATOM   305  C  CA    . TYR   A 1 43  ? 12.284  8.898   51.509  1.00 12.47 ? 40  TYR   A CA    1 
ATOM   306  C  C     . TYR   A 1 43  ? 10.749  8.969   51.561  1.00 12.87 ? 40  TYR   A C     1 
ATOM   307  O  O     . TYR   A 1 43  ? 10.100  8.412   50.675  1.00 12.56 ? 40  TYR   A O     1 
ATOM   308  C  CB    . TYR   A 1 43  ? 12.784  9.583   50.236  1.00 12.19 ? 40  TYR   A CB    1 
ATOM   309  C  CG    . TYR   A 1 43  ? 14.289  9.499   50.100  1.00 12.15 ? 40  TYR   A CG    1 
ATOM   310  C  CD1   . TYR   A 1 43  ? 14.901  8.340   49.638  1.00 12.02 ? 40  TYR   A CD1   1 
ATOM   311  C  CD2   . TYR   A 1 43  ? 15.100  10.523  50.554  1.00 12.46 ? 40  TYR   A CD2   1 
ATOM   312  C  CE1   . TYR   A 1 43  ? 16.288  8.223   49.584  1.00 12.26 ? 40  TYR   A CE1   1 
ATOM   313  C  CE2   . TYR   A 1 43  ? 16.483  10.433  50.472  1.00 12.70 ? 40  TYR   A CE2   1 
ATOM   314  C  CZ    . TYR   A 1 43  ? 17.086  9.279   49.992  1.00 12.56 ? 40  TYR   A CZ    1 
ATOM   315  O  OH    . TYR   A 1 43  ? 18.461  9.134   49.934  1.00 12.98 ? 40  TYR   A OH    1 
ATOM   316  N  N     . ARG   A 1 44  ? 10.207  9.626   52.596  1.00 13.72 ? 41  ARG   A N     1 
ATOM   317  C  CA    . ARG   A 1 44  ? 8.735   9.669   52.819  1.00 14.50 ? 41  ARG   A CA    1 
ATOM   318  C  C     . ARG   A 1 44  ? 8.117   11.025  52.496  1.00 14.55 ? 41  ARG   A C     1 
ATOM   319  O  O     . ARG   A 1 44  ? 8.722   12.061  52.836  1.00 14.59 ? 41  ARG   A O     1 
ATOM   320  C  CB    . ARG   A 1 44  ? 8.406   9.391   54.282  1.00 15.75 ? 41  ARG   A CB    1 
ATOM   321  C  CG    . ARG   A 1 44  ? 8.836   8.010   54.743  1.00 16.65 ? 41  ARG   A CG    1 
ATOM   322  C  CD    . ARG   A 1 44  ? 8.346   7.687   56.150  1.00 18.23 ? 41  ARG   A CD    1 
ATOM   323  N  NE    . ARG   A 1 44  ? 7.891   6.301   56.117  1.00 19.53 ? 41  ARG   A NE    1 
ATOM   324  C  CZ    . ARG   A 1 44  ? 6.668   5.902   56.446  1.00 20.76 ? 41  ARG   A CZ    1 
ATOM   325  N  NH1   . ARG   A 1 44  ? 6.350   4.620   56.383  1.00 21.47 ? 41  ARG   A NH1   1 
ATOM   326  N  NH2   . ARG   A 1 44  ? 5.767   6.785   56.837  1.00 21.98 ? 41  ARG   A NH2   1 
ATOM   327  N  N     . LYS   A 1 45  ? 6.921   10.990  51.903  1.00 14.50 ? 42  LYS   A N     1 
ATOM   328  C  CA    . LYS   A 1 45  ? 6.201   12.203  51.691  1.00 14.69 ? 42  LYS   A CA    1 
ATOM   329  C  C     . LYS   A 1 45  ? 4.703   11.947  51.785  1.00 14.87 ? 42  LYS   A C     1 
ATOM   330  O  O     . LYS   A 1 45  ? 4.245   10.966  51.198  1.00 14.57 ? 42  LYS   A O     1 
ATOM   331  C  CB    . LYS   A 1 45  ? 6.477   12.760  50.300  1.00 14.61 ? 42  LYS   A CB    1 
ATOM   332  C  CG    . LYS   A 1 45  ? 6.208   14.246  50.222  1.00 15.40 ? 42  LYS   A CG    1 
ATOM   333  C  CD    . LYS   A 1 45  ? 6.442   14.759  48.839  1.00 15.46 ? 42  LYS   A CD    1 
ATOM   334  C  CE    . LYS   A 1 45  ? 6.068   16.213  48.714  1.00 16.34 ? 42  LYS   A CE    1 
ATOM   335  N  NZ    . LYS   A 1 45  ? 5.968   16.532  47.280  1.00 16.60 ? 42  LYS   A NZ    1 
ATOM   336  N  N     . GLN   A 1 46  ? 4.020   12.832  52.527  1.00 15.31 ? 43  GLN   A N     1 
ATOM   337  C  CA    . GLN   A 1 46  ? 2.563   12.889  52.595  1.00 15.98 ? 43  GLN   A CA    1 
ATOM   338  C  C     . GLN   A 1 46  ? 2.029   13.764  51.451  1.00 15.98 ? 43  GLN   A C     1 
ATOM   339  O  O     . GLN   A 1 46  ? 2.419   14.916  51.299  1.00 16.05 ? 43  GLN   A O     1 
ATOM   340  C  CB    . GLN   A 1 46  ? 2.151   13.437  53.953  1.00 16.75 ? 43  GLN   A CB    1 
ATOM   341  C  CG    . GLN   A 1 46  ? 0.658   13.348  54.197  1.00 17.77 ? 43  GLN   A CG    1 
ATOM   342  C  CD    . GLN   A 1 46  ? 0.350   13.607  55.651  1.00 18.64 ? 43  GLN   A CD    1 
ATOM   343  O  OE1   . GLN   A 1 46  ? 0.958   13.024  56.545  1.00 18.57 ? 43  GLN   A OE1   1 
ATOM   344  N  NE2   . GLN   A 1 46  ? -0.609  14.476  55.898  1.00 19.61 ? 43  GLN   A NE2   1 
ATOM   345  N  N     . VAL   A 1 47  ? 1.132   13.190  50.644  1.00 16.01 ? 44  VAL   A N     1 
ATOM   346  C  CA    . VAL   A 1 47  ? 0.648   13.798  49.408  1.00 16.08 ? 44  VAL   A CA    1 
ATOM   347  C  C     . VAL   A 1 47  ? -0.863  13.573  49.320  1.00 16.92 ? 44  VAL   A C     1 
ATOM   348  O  O     . VAL   A 1 47  ? -1.387  12.791  50.091  1.00 17.19 ? 44  VAL   A O     1 
ATOM   349  C  CB    . VAL   A 1 47  ? 1.350   13.213  48.174  1.00 15.49 ? 44  VAL   A CB    1 
ATOM   350  C  CG1   . VAL   A 1 47  ? 2.854   13.525  48.241  1.00 14.88 ? 44  VAL   A CG1   1 
ATOM   351  C  CG2   . VAL   A 1 47  ? 1.114   11.696  48.026  1.00 15.22 ? 44  VAL   A CG2   1 
ATOM   352  N  N     . VAL   A 1 48  ? -1.483  14.282  48.375  1.00 17.40 ? 45  VAL   A N     1 
ATOM   353  C  CA    . VAL   A 1 48  ? -2.897  14.065  47.983  1.00 18.27 ? 45  VAL   A CA    1 
ATOM   354  C  C     . VAL   A 1 48  ? -2.879  13.765  46.481  1.00 18.01 ? 45  VAL   A C     1 
ATOM   355  O  O     . VAL   A 1 48  ? -2.425  14.602  45.688  1.00 17.91 ? 45  VAL   A O     1 
ATOM   356  C  CB    . VAL   A 1 48  ? -3.788  15.278  48.269  1.00 19.41 ? 45  VAL   A CB    1 
ATOM   357  C  CG1   . VAL   A 1 48  ? -5.240  14.914  48.011  1.00 20.43 ? 45  VAL   A CG1   1 
ATOM   358  C  CG2   . VAL   A 1 48  ? -3.628  15.831  49.680  1.00 19.73 ? 45  VAL   A CG2   1 
ATOM   359  N  N     . ILE   A 1 49  ? -3.288  12.564  46.102  1.00 17.96 ? 46  ILE   A N     1 
ATOM   360  C  CA    . ILE   A 1 49  ? -3.332  12.169  44.714  1.00 17.83 ? 46  ILE   A CA    1 
ATOM   361  C  C     . ILE   A 1 49  ? -4.799  11.906  44.354  1.00 18.92 ? 46  ILE   A C     1 
ATOM   362  O  O     . ILE   A 1 49  ? -5.414  11.034  44.912  1.00 19.28 ? 46  ILE   A O     1 
ATOM   363  C  CB    . ILE   A 1 49  ? -2.423  10.945  44.466  1.00 16.91 ? 46  ILE   A CB    1 
ATOM   364  C  CG1   . ILE   A 1 49  ? -1.003  11.246  44.963  1.00 16.02 ? 46  ILE   A CG1   1 
ATOM   365  C  CG2   . ILE   A 1 49  ? -2.459  10.548  42.996  1.00 16.89 ? 46  ILE   A CG2   1 
ATOM   366  C  CD1   . ILE   A 1 49  ? -0.089  10.034  44.972  1.00 15.26 ? 46  ILE   A CD1   1 
ATOM   367  N  N     . ASP   A 1 50  ? -5.334  12.716  43.451  1.00 19.56 ? 47  ASP   A N     1 
ATOM   368  C  CA    . ASP   A 1 50  ? -6.724  12.587  43.010  1.00 20.76 ? 47  ASP   A CA    1 
ATOM   369  C  C     . ASP   A 1 50  ? -7.683  12.632  44.206  1.00 21.66 ? 47  ASP   A C     1 
ATOM   370  O  O     . ASP   A 1 50  ? -8.734  11.987  44.184  1.00 22.55 ? 47  ASP   A O     1 
ATOM   371  C  CB    . ASP   A 1 50  ? -6.947  11.277  42.259  1.00 20.70 ? 47  ASP   A CB    1 
ATOM   372  C  CG    . ASP   A 1 50  ? -6.014  11.062  41.091  1.00 19.91 ? 47  ASP   A CG    1 
ATOM   373  O  OD1   . ASP   A 1 50  ? -5.725  12.045  40.366  1.00 19.94 ? 47  ASP   A OD1   1 
ATOM   374  O  OD2   . ASP   A 1 50  ? -5.530  9.932   40.953  1.00 19.32 ? 47  ASP   A OD2   1 
ATOM   375  N  N     . GLY   A 1 51  ? -7.299  13.391  45.234  1.00 21.53 ? 48  GLY   A N     1 
ATOM   376  C  CA    . GLY   A 1 51  ? -8.071  13.566  46.435  1.00 22.42 ? 48  GLY   A CA    1 
ATOM   377  C  C     . GLY   A 1 51  ? -7.812  12.507  47.499  1.00 22.01 ? 48  GLY   A C     1 
ATOM   378  O  O     . GLY   A 1 51  ? -8.413  12.551  48.573  1.00 22.78 ? 48  GLY   A O     1 
ATOM   379  N  N     . GLU   A 1 52  ? -6.949  11.530  47.205  1.00 20.93 ? 49  GLU   A N     1 
ATOM   380  C  CA    . GLU   A 1 52  ? -6.566  10.532  48.203  1.00 20.54 ? 49  GLU   A CA    1 
ATOM   381  C  C     . GLU   A 1 52  ? -5.416  11.088  49.045  1.00 19.74 ? 49  GLU   A C     1 
ATOM   382  O  O     . GLU   A 1 52  ? -4.296  11.324  48.489  1.00 18.75 ? 49  GLU   A O     1 
ATOM   383  C  CB    . GLU   A 1 52  ? -6.163  9.212   47.542  1.00 19.93 ? 49  GLU   A CB    1 
ATOM   384  C  CG    . GLU   A 1 52  ? -5.758  8.167   48.572  1.00 19.67 ? 49  GLU   A CG    1 
ATOM   385  C  CD    . GLU   A 1 52  ? -5.189  6.805   48.069  1.00 19.09 ? 49  GLU   A CD    1 
ATOM   386  O  OE1   . GLU   A 1 52  ? -4.876  6.679   46.861  1.00 18.66 ? 49  GLU   A OE1   1 
ATOM   387  O  OE2   . GLU   A 1 52  ? -5.123  5.883   48.927  1.00 19.23 ? 49  GLU   A OE2   1 
ATOM   388  N  N     . THR   A 1 53  ? -5.639  11.266  50.357  1.00 20.24 ? 50  THR   A N     1 
ATOM   389  C  CA    . THR   A 1 53  ? -4.515  11.593  51.225  1.00 19.54 ? 50  THR   A CA    1 
ATOM   390  C  C     . THR   A 1 53  ? -3.763  10.309  51.562  1.00 18.81 ? 50  THR   A C     1 
ATOM   391  O  O     . THR   A 1 53  ? -4.288  9.392   52.148  1.00 19.30 ? 50  THR   A O     1 
ATOM   392  C  CB    . THR   A 1 53  ? -4.906  12.338  52.502  1.00 20.37 ? 50  THR   A CB    1 
ATOM   393  O  OG1   . THR   A 1 53  ? -5.451  13.575  52.064  1.00 21.03 ? 50  THR   A OG1   1 
ATOM   394  C  CG2   . THR   A 1 53  ? -3.703  12.600  53.395  1.00 19.71 ? 50  THR   A CG2   1 
ATOM   395  N  N     . CYS   A 1 54  ? -2.484  10.283  51.175  1.00 17.72 ? 51  CYS   A N     1 
ATOM   396  C  CA    . CYS   A 1 54  ? -1.675  9.069   51.405  1.00 17.08 ? 51  CYS   A CA    1 
ATOM   397  C  C     . CYS   A 1 54  ? -0.189  9.438   51.657  1.00 16.21 ? 51  CYS   A C     1 
ATOM   398  O  O     . CYS   A 1 54  ? 0.121   10.578  51.606  1.00 16.12 ? 51  CYS   A O     1 
ATOM   399  C  CB    . CYS   A 1 54  ? -1.750  8.139   50.210  1.00 16.80 ? 51  CYS   A CB    1 
ATOM   400  S  SG    . CYS   A 1 54  ? -1.287  8.929   48.660  1.00 16.33 ? 51  CYS   A SG    1 
ATOM   401  N  N     . LEU   A 1 55  ? 0.573   8.411   51.969  1.00 16.10 ? 52  LEU   A N     1 
ATOM   402  C  CA    . LEU   A 1 55  ? 2.014   8.523   52.300  1.00 15.68 ? 52  LEU   A CA    1 
ATOM   403  C  C     . LEU   A 1 55  ? 2.771   7.704   51.248  1.00 15.06 ? 52  LEU   A C     1 
ATOM   404  O  O     . LEU   A 1 55  ? 2.385   6.626   51.033  1.00 14.86 ? 52  LEU   A O     1 
ATOM   405  C  CB    . LEU   A 1 55  ? 2.137   7.932   53.703  1.00 16.38 ? 52  LEU   A CB    1 
ATOM   406  C  CG    . LEU   A 1 55  ? 3.387   8.295   54.482  1.00 16.61 ? 52  LEU   A CG    1 
ATOM   407  C  CD1   . LEU   A 1 55  ? 4.550   7.694   53.769  1.00 16.07 ? 52  LEU   A CD1   1 
ATOM   408  C  CD2   . LEU   A 1 55  ? 3.534   9.786   54.599  1.00 16.80 ? 52  LEU   A CD2   1 
ATOM   409  N  N     . LEU   A 1 56  ? 3.816   8.298   50.647  1.00 14.47 ? 53  LEU   A N     1 
ATOM   410  C  CA    . LEU   A 1 56  ? 4.704   7.603   49.691  1.00 14.00 ? 53  LEU   A CA    1 
ATOM   411  C  C     . LEU   A 1 56  ? 5.996   7.252   50.472  1.00 13.87 ? 53  LEU   A C     1 
ATOM   412  O  O     . LEU   A 1 56  ? 6.419   8.069   51.177  1.00 13.64 ? 53  LEU   A O     1 
ATOM   413  C  CB    . LEU   A 1 56  ? 5.019   8.542   48.529  1.00 13.75 ? 53  LEU   A CB    1 
ATOM   414  C  CG    . LEU   A 1 56  ? 3.817   9.137   47.801  1.00 14.22 ? 53  LEU   A CG    1 
ATOM   415  C  CD1   . LEU   A 1 56  ? 4.232   9.875   46.549  1.00 14.11 ? 53  LEU   A CD1   1 
ATOM   416  C  CD2   . LEU   A 1 56  ? 2.847   8.031   47.474  1.00 14.42 ? 53  LEU   A CD2   1 
ATOM   417  N  N     . ASP   A 1 57  ? 6.327   5.979   50.481  1.00 13.86 ? 54  ASP   A N     1 
ATOM   418  C  CA    . ASP   A 1 57  ? 7.514   5.427   51.156  1.00 13.73 ? 54  ASP   A CA    1 
ATOM   419  C  C     . ASP   A 1 57  ? 8.342   4.957   49.971  1.00 13.12 ? 54  ASP   A C     1 
ATOM   420  O  O     . ASP   A 1 57  ? 8.081   3.942   49.474  1.00 12.85 ? 54  ASP   A O     1 
ATOM   421  C  CB    . ASP   A 1 57  ? 7.163   4.408   52.233  1.00 14.41 ? 54  ASP   A CB    1 
ATOM   422  C  CG    . ASP   A 1 57  ? 8.376   3.918   53.008  1.00 14.73 ? 54  ASP   A CG    1 
ATOM   423  O  OD1   . ASP   A 1 57  ? 9.457   4.243   52.597  1.00 14.48 ? 54  ASP   A OD1   1 
ATOM   424  O  OD2   . ASP   A 1 57  ? 8.192   3.206   53.986  1.00 15.59 ? 54  ASP   A OD2   1 
ATOM   425  N  N     . ILE   A 1 58  ? 9.306   5.796   49.594  1.00 12.51 ? 55  ILE   A N     1 
ATOM   426  C  CA    . ILE   A 1 58  ? 10.074  5.609   48.334  1.00 12.26 ? 55  ILE   A CA    1 
ATOM   427  C  C     . ILE   A 1 58  ? 11.488  5.084   48.661  1.00 12.31 ? 55  ILE   A C     1 
ATOM   428  O  O     . ILE   A 1 58  ? 12.177  5.750   49.377  1.00 12.18 ? 55  ILE   A O     1 
ATOM   429  C  CB    . ILE   A 1 58  ? 10.186  6.935   47.560  1.00 12.13 ? 55  ILE   A CB    1 
ATOM   430  C  CG1   . ILE   A 1 58  ? 8.823   7.553   47.197  1.00 12.44 ? 55  ILE   A CG1   1 
ATOM   431  C  CG2   . ILE   A 1 58  ? 11.022  6.779   46.315  1.00 12.13 ? 55  ILE   A CG2   1 
ATOM   432  C  CD1   . ILE   A 1 58  ? 8.832   9.034   46.977  1.00 12.42 ? 55  ILE   A CD1   1 
ATOM   433  N  N     . LEU   A 1 59  ? 11.807  3.929   48.099  1.00 12.41 ? 56  LEU   A N     1 
ATOM   434  C  CA    . LEU   A 1 59  ? 13.195  3.393   48.242  1.00 12.60 ? 56  LEU   A CA    1 
ATOM   435  C  C     . LEU   A 1 59  ? 13.977  3.767   46.984  1.00 12.44 ? 56  LEU   A C     1 
ATOM   436  O  O     . LEU   A 1 59  ? 13.605  3.342   45.934  1.00 12.19 ? 56  LEU   A O     1 
ATOM   437  C  CB    . LEU   A 1 59  ? 13.144  1.885   48.396  1.00 13.19 ? 56  LEU   A CB    1 
ATOM   438  C  CG    . LEU   A 1 59  ? 14.483  1.228   48.711  1.00 13.68 ? 56  LEU   A CG    1 
ATOM   439  C  CD1   . LEU   A 1 59  ? 15.001  1.661   50.059  1.00 13.97 ? 56  LEU   A CD1   1 
ATOM   440  C  CD2   . LEU   A 1 59  ? 14.405  -0.264  48.582  1.00 14.18 ? 56  LEU   A CD2   1 
ATOM   441  N  N     . ASP   A 1 60  ? 15.019  4.578   47.165  1.00 12.38 ? 57  ASP   A N     1 
ATOM   442  C  CA    . ASP   A 1 60  ? 15.931  4.992   46.077  1.00 12.58 ? 57  ASP   A CA    1 
ATOM   443  C  C     . ASP   A 1 60  ? 17.146  4.046   46.230  1.00 12.91 ? 57  ASP   A C     1 
ATOM   444  O  O     . ASP   A 1 60  ? 17.636  3.935   47.310  1.00 12.99 ? 57  ASP   A O     1 
ATOM   445  C  CB    . ASP   A 1 60  ? 16.338  6.443   46.250  1.00 12.61 ? 57  ASP   A CB    1 
ATOM   446  C  CG    . ASP   A 1 60  ? 17.435  6.877   45.302  1.00 12.95 ? 57  ASP   A CG    1 
ATOM   447  O  OD1   . ASP   A 1 60  ? 17.476  6.388   44.226  1.00 12.85 ? 57  ASP   A OD1   1 
ATOM   448  O  OD2   . ASP   A 1 60  ? 18.148  7.767   45.699  1.00 13.30 ? 57  ASP   A OD2   1 
ATOM   449  N  N     . THR   A 1 61  ? 17.435  3.341   45.165  1.00 13.15 ? 58  THR   A N     1 
ATOM   450  C  CA    . THR   A 1 61  ? 18.361  2.187   45.197  1.00 13.96 ? 58  THR   A CA    1 
ATOM   451  C  C     . THR   A 1 61  ? 19.782  2.461   44.668  1.00 14.89 ? 58  THR   A C     1 
ATOM   452  O  O     . THR   A 1 61  ? 19.944  3.348   43.940  1.00 14.75 ? 58  THR   A O     1 
ATOM   453  C  CB    . THR   A 1 61  ? 17.722  1.074   44.374  1.00 13.80 ? 58  THR   A CB    1 
ATOM   454  O  OG1   . THR   A 1 61  ? 17.624  1.528   43.038  1.00 13.59 ? 58  THR   A OG1   1 
ATOM   455  C  CG2   . THR   A 1 61  ? 16.352  0.707   44.911  1.00 13.54 ? 58  THR   A CG2   1 
ATOM   456  N  N     . ALA   A 1 62  ? 20.709  1.583   45.045  1.00 16.39 ? 59  ALA   A N     1 
ATOM   457  C  CA    . ALA   A 1 62  ? 22.132  1.702   44.647  1.00 18.14 ? 59  ALA   A CA    1 
ATOM   458  C  C     . ALA   A 1 62  ? 22.559  0.531   43.753  1.00 20.15 ? 59  ALA   A C     1 
ATOM   459  O  O     . ALA   A 1 62  ? 21.904  -0.488  43.721  1.00 21.21 ? 59  ALA   A O     1 
ATOM   460  C  CB    . ALA   A 1 62  ? 22.965  1.764   45.889  1.00 18.47 ? 59  ALA   A CB    1 
ATOM   461  N  N     . GLY   A 1 63  ? 23.677  0.674   43.043  1.00 22.08 ? 60  GLY   A N     1 
ATOM   462  C  CA    . GLY   A 1 63  ? 24.112  -0.466  42.231  1.00 23.27 ? 60  GLY   A CA    1 
ATOM   463  C  C     . GLY   A 1 63  ? 24.421  -1.675  43.101  1.00 24.90 ? 60  GLY   A C     1 
ATOM   464  O  O     . GLY   A 1 63  ? 24.988  -1.504  44.154  1.00 26.37 ? 60  GLY   A O     1 
ATOM   465  N  N     . GLN   A 1 64  ? 24.010  -2.858  42.719  1.00 25.54 ? 61  GLN   A N     1 
ATOM   466  C  CA    . GLN   A 1 64  ? 24.532  -4.021  43.479  1.00 26.82 ? 61  GLN   A CA    1 
ATOM   467  C  C     . GLN   A 1 64  ? 25.020  -5.049  42.426  1.00 27.22 ? 61  GLN   A C     1 
ATOM   468  O  O     . GLN   A 1 64  ? 24.236  -5.713  41.866  1.00 26.92 ? 61  GLN   A O     1 
ATOM   469  C  CB    . GLN   A 1 64  ? 23.371  -4.563  44.313  1.00 26.83 ? 61  GLN   A CB    1 
ATOM   470  C  CG    . GLN   A 1 64  ? 23.143  -3.735  45.533  1.00 26.98 ? 61  GLN   A CG    1 
ATOM   471  C  CD    . GLN   A 1 64  ? 21.792  -4.082  46.078  1.00 26.16 ? 61  GLN   A CD    1 
ATOM   472  O  OE1   . GLN   A 1 64  ? 20.838  -4.119  45.342  1.00 27.44 ? 61  GLN   A OE1   1 
ATOM   473  N  NE2   . GLN   A 1 64  ? 21.724  -4.332  47.355  1.00 27.59 ? 61  GLN   A NE2   1 
ATOM   474  N  N     . GLU   A 1 65  ? 26.325  -5.190  42.155  1.00 28.19 ? 62  GLU   A N     1 
ATOM   475  C  CA    . GLU   A 1 65  ? 26.735  -6.036  40.982  1.00 29.05 ? 62  GLU   A CA    1 
ATOM   476  C  C     . GLU   A 1 65  ? 26.348  -7.513  41.102  1.00 29.54 ? 62  GLU   A C     1 
ATOM   477  O  O     . GLU   A 1 65  ? 25.892  -8.074  40.127  1.00 30.29 ? 62  GLU   A O     1 
ATOM   478  C  CB    . GLU   A 1 65  ? 28.226  -5.858  40.592  1.00 30.35 ? 62  GLU   A CB    1 
ATOM   479  C  CG    . GLU   A 1 65  ? 28.446  -4.627  39.731  1.00 30.47 ? 62  GLU   A CG    1 
ATOM   480  C  CD    . GLU   A 1 65  ? 27.746  -4.568  38.373  1.00 30.67 ? 62  GLU   A CD    1 
ATOM   481  O  OE1   . GLU   A 1 65  ? 27.862  -3.558  37.689  1.00 30.10 ? 62  GLU   A OE1   1 
ATOM   482  O  OE2   . GLU   A 1 65  ? 27.105  -5.547  37.986  1.00 31.53 ? 62  GLU   A OE2   1 
ATOM   483  N  N     . GLU   A 1 66  ? 26.502  -8.103  42.263  1.00 29.49 ? 63  GLU   A N     1 
ATOM   484  C  CA    . GLU   A 1 66  ? 26.254  -9.553  42.410  1.00 29.90 ? 63  GLU   A CA    1 
ATOM   485  C  C     . GLU   A 1 66  ? 24.847  -9.800  42.961  1.00 28.36 ? 63  GLU   A C     1 
ATOM   486  O  O     . GLU   A 1 66  ? 24.046  -8.832  42.976  1.00 27.52 ? 63  GLU   A O     1 
ATOM   487  C  CB    . GLU   A 1 66  ? 27.371  -10.142 43.285  1.00 31.41 ? 63  GLU   A CB    1 
ATOM   488  C  CG    . GLU   A 1 66  ? 28.681  -10.271 42.509  1.00 33.19 ? 63  GLU   A CG    1 
ATOM   489  C  CD    . GLU   A 1 66  ? 29.888  -10.562 43.383  1.00 34.92 ? 63  GLU   A CD    1 
ATOM   490  O  OE1   . GLU   A 1 66  ? 29.735  -10.439 44.602  1.00 35.43 ? 63  GLU   A OE1   1 
ATOM   491  O  OE2   . GLU   A 1 66  ? 30.972  -10.921 42.835  1.00 36.86 ? 63  GLU   A OE2   1 
ATOM   492  N  N     . TYR   A 1 67  ? 24.554  -11.063 43.307  1.00 27.99 ? 64  TYR   A N     1 
ATOM   493  C  CA    . TYR   A 1 67  ? 23.337  -11.433 44.011  1.00 26.54 ? 64  TYR   A CA    1 
ATOM   494  C  C     . TYR   A 1 67  ? 23.251  -10.624 45.309  1.00 24.59 ? 64  TYR   A C     1 
ATOM   495  O  O     . TYR   A 1 67  ? 24.257  -10.450 46.018  1.00 24.64 ? 64  TYR   A O     1 
ATOM   496  C  CB    . TYR   A 1 67  ? 23.309  -12.931 44.324  1.00 28.61 ? 64  TYR   A CB    1 
ATOM   497  C  CG    . TYR   A 1 67  ? 22.193  -13.315 45.266  1.00 28.79 ? 64  TYR   A CG    1 
ATOM   498  C  CD1   . TYR   A 1 67  ? 20.868  -13.042 44.928  1.00 28.50 ? 64  TYR   A CD1   1 
ATOM   499  C  CD2   . TYR   A 1 67  ? 22.445  -13.892 46.505  1.00 29.88 ? 64  TYR   A CD2   1 
ATOM   500  C  CE1   . TYR   A 1 67  ? 19.825  -13.359 45.783  1.00 28.59 ? 64  TYR   A CE1   1 
ATOM   501  C  CE2   . TYR   A 1 67  ? 21.413  -14.222 47.370  1.00 30.19 ? 64  TYR   A CE2   1 
ATOM   502  C  CZ    . TYR   A 1 67  ? 20.100  -13.960 47.000  1.00 29.52 ? 64  TYR   A CZ    1 
ATOM   503  O  OH    . TYR   A 1 67  ? 19.052  -14.265 47.820  1.00 30.29 ? 64  TYR   A OH    1 
ATOM   504  N  N     . SER   A 1 68  ? 22.047  -10.125 45.607  1.00 22.32 ? 65  SER   A N     1 
ATOM   505  C  CA    . SER   A 1 68  ? 21.801  -9.332  46.791  1.00 21.07 ? 65  SER   A CA    1 
ATOM   506  C  C     . SER   A 1 68  ? 20.474  -9.791  47.408  1.00 20.45 ? 65  SER   A C     1 
ATOM   507  O  O     . SER   A 1 68  ? 19.412  -9.566  46.825  1.00 19.83 ? 65  SER   A O     1 
ATOM   508  C  CB    . SER   A 1 68  ? 21.770  -7.862  46.462  1.00 19.85 ? 65  SER   A CB    1 
ATOM   509  O  OG    . SER   A 1 68  ? 21.475  -7.056  47.597  1.00 19.08 ? 65  SER   A OG    1 
ATOM   510  N  N     . ALA   A 1 69  ? 20.561  -10.438 48.566  1.00 20.76 ? 66  ALA   A N     1 
ATOM   511  C  CA    . ALA   A 1 69  ? 19.394  -10.831 49.365  1.00 20.74 ? 66  ALA   A CA    1 
ATOM   512  C  C     . ALA   A 1 69  ? 18.515  -9.604  49.654  1.00 19.41 ? 66  ALA   A C     1 
ATOM   513  O  O     . ALA   A 1 69  ? 17.252  -9.651  49.614  1.00 18.90 ? 66  ALA   A O     1 
ATOM   514  C  CB    . ALA   A 1 69  ? 19.857  -11.487 50.646  1.00 21.69 ? 66  ALA   A CB    1 
ATOM   515  N  N     . MET   A 1 70  ? 19.163  -8.475  49.964  1.00 18.80 ? 67  MET   A N     1 
ATOM   516  C  CA    . MET   A 1 70  ? 18.385  -7.260  50.336  1.00 17.86 ? 67  MET   A CA    1 
ATOM   517  C  C     . MET   A 1 70  ? 17.665  -6.644  49.126  1.00 17.20 ? 67  MET   A C     1 
ATOM   518  O  O     . MET   A 1 70  ? 16.536  -6.111  49.277  1.00 16.46 ? 67  MET   A O     1 
ATOM   519  C  CB    . MET   A 1 70  ? 19.270  -6.249  51.075  1.00 17.59 ? 67  MET   A CB    1 
ATOM   520  C  CG    . MET   A 1 70  ? 19.778  -6.838  52.384  1.00 18.42 ? 67  MET   A CG    1 
ATOM   521  S  SD    . MET   A 1 70  ? 20.347  -5.639  53.613  1.00 18.12 ? 67  MET   A SD    1 
ATOM   522  C  CE    . MET   A 1 70  ? 18.769  -5.030  54.223  1.00 17.49 ? 67  MET   A CE    1 
ATOM   523  N  N     . ARG   A 1 71  ? 18.211  -6.801  47.930  1.00 17.54 ? 68  ARG   A N     1 
ATOM   524  C  CA    . ARG   A 1 71  ? 17.536  -6.306  46.701  1.00 16.96 ? 68  ARG   A CA    1 
ATOM   525  C  C     . ARG   A 1 71  ? 16.295  -7.185  46.476  1.00 17.00 ? 68  ARG   A C     1 
ATOM   526  O  O     . ARG   A 1 71  ? 15.246  -6.633  46.265  1.00 16.21 ? 68  ARG   A O     1 
ATOM   527  C  CB    . ARG   A 1 71  ? 18.472  -6.396  45.499  1.00 17.77 ? 68  ARG   A CB    1 
ATOM   528  C  CG    . ARG   A 1 71  ? 17.860  -5.907  44.199  1.00 17.77 ? 68  ARG   A CG    1 
ATOM   529  C  CD    . ARG   A 1 71  ? 18.718  -5.730  42.976  1.00 18.67 ? 68  ARG   A CD    1 
ATOM   530  N  NE    . ARG   A 1 71  ? 19.200  -7.023  42.583  1.00 20.31 ? 68  ARG   A NE    1 
ATOM   531  C  CZ    . ARG   A 1 71  ? 20.458  -7.360  42.378  1.00 21.51 ? 68  ARG   A CZ    1 
ATOM   532  N  NH1   . ARG   A 1 71  ? 21.432  -6.460  42.416  1.00 21.91 ? 68  ARG   A NH1   1 
ATOM   533  N  NH2   . ARG   A 1 71  ? 20.715  -8.600  42.054  1.00 22.86 ? 68  ARG   A NH2   1 
ATOM   534  N  N     . ASP   A 1 72  ? 16.461  -8.500  46.585  1.00 17.67 ? 69  ASP   A N     1 
ATOM   535  C  CA    . ASP   A 1 72  ? 15.349  -9.435  46.460  1.00 18.19 ? 69  ASP   A CA    1 
ATOM   536  C  C     . ASP   A 1 72  ? 14.228  -9.015  47.425  1.00 17.70 ? 69  ASP   A C     1 
ATOM   537  O  O     . ASP   A 1 72  ? 13.055  -8.990  47.037  1.00 17.77 ? 69  ASP   A O     1 
ATOM   538  C  CB    . ASP   A 1 72  ? 15.770  -10.882 46.705  1.00 19.39 ? 69  ASP   A CB    1 
ATOM   539  C  CG    . ASP   A 1 72  ? 16.576  -11.489 45.569  1.00 20.00 ? 69  ASP   A CG    1 
ATOM   540  O  OD1   . ASP   A 1 72  ? 16.958  -10.760 44.636  1.00 19.39 ? 69  ASP   A OD1   1 
ATOM   541  O  OD2   . ASP   A 1 72  ? 16.804  -12.688 45.622  1.00 21.25 ? 69  ASP   A OD2   1 
ATOM   542  N  N     . GLN   A 1 73  ? 14.589  -8.659  48.660  1.00 17.57 ? 70  GLN   A N     1 
ATOM   543  C  CA    . GLN   A 1 73  ? 13.606  -8.336  49.679  1.00 17.43 ? 70  GLN   A CA    1 
ATOM   544  C  C     . GLN   A 1 73  ? 12.869  -7.040  49.350  1.00 16.45 ? 70  GLN   A C     1 
ATOM   545  O  O     . GLN   A 1 73  ? 11.659  -6.945  49.615  1.00 16.46 ? 70  GLN   A O     1 
ATOM   546  C  CB    . GLN   A 1 73  ? 14.232  -8.225  51.067  1.00 17.66 ? 70  GLN   A CB    1 
ATOM   547  C  CG    . GLN   A 1 73  ? 13.212  -7.957  52.171  1.00 17.70 ? 70  GLN   A CG    1 
ATOM   548  C  CD    . GLN   A 1 73  ? 12.000  -8.861  52.147  1.00 18.40 ? 70  GLN   A CD    1 
ATOM   549  O  OE1   . GLN   A 1 73  ? 11.939  -9.839  51.409  1.00 18.98 ? 70  GLN   A OE1   1 
ATOM   550  N  NE2   . GLN   A 1 73  ? 11.014  -8.532  52.967  1.00 18.51 ? 70  GLN   A NE2   1 
ATOM   551  N  N     . TYR   A 1 74  ? 13.580  -6.061  48.795  1.00 15.74 ? 71  TYR   A N     1 
ATOM   552  C  CA    . TYR   A 1 74  ? 12.878  -4.809  48.403  1.00 14.92 ? 71  TYR   A CA    1 
ATOM   553  C  C     . TYR   A 1 74  ? 11.965  -5.084  47.215  1.00 14.96 ? 71  TYR   A C     1 
ATOM   554  O  O     . TYR   A 1 74  ? 10.967  -4.404  47.074  1.00 14.62 ? 71  TYR   A O     1 
ATOM   555  C  CB    . TYR   A 1 74  ? 13.766  -3.561  48.316  1.00 14.27 ? 71  TYR   A CB    1 
ATOM   556  C  CG    . TYR   A 1 74  ? 14.686  -3.370  47.143  1.00 14.13 ? 71  TYR   A CG    1 
ATOM   557  C  CD1   . TYR   A 1 74  ? 14.264  -3.298  45.830  1.00 13.99 ? 71  TYR   A CD1   1 
ATOM   558  C  CD2   . TYR   A 1 74  ? 16.032  -3.111  47.388  1.00 14.21 ? 71  TYR   A CD2   1 
ATOM   559  C  CE1   . TYR   A 1 74  ? 15.137  -3.012  44.793  1.00 13.94 ? 71  TYR   A CE1   1 
ATOM   560  C  CE2   . TYR   A 1 74  ? 16.908  -2.851  46.363  1.00 14.20 ? 71  TYR   A CE2   1 
ATOM   561  C  CZ    . TYR   A 1 74  ? 16.490  -2.822  45.060  1.00 14.13 ? 71  TYR   A CZ    1 
ATOM   562  O  OH    . TYR   A 1 74  ? 17.411  -2.525  44.116  1.00 14.17 ? 71  TYR   A OH    1 
ATOM   563  N  N     . MET   A 1 75  ? 12.364  -6.001  46.364  1.00 15.43 ? 72  MET   A N     1 
ATOM   564  C  CA    . MET   A 1 75  ? 11.513  -6.343  45.208  1.00 15.66 ? 72  MET   A CA    1 
ATOM   565  C  C     . MET   A 1 75  ? 10.262  -7.084  45.699  1.00 16.25 ? 72  MET   A C     1 
ATOM   566  O  O     . MET   A 1 75  ? 9.253   -6.847  45.171  1.00 16.23 ? 72  MET   A O     1 
ATOM   567  C  CB    . MET   A 1 75  ? 12.296  -7.121  44.161  1.00 16.13 ? 72  MET   A CB    1 
ATOM   568  C  CG    . MET   A 1 75  ? 13.289  -6.186  43.513  1.00 15.56 ? 72  MET   A CG    1 
ATOM   569  S  SD    . MET   A 1 75  ? 14.116  -6.945  42.175  1.00 16.33 ? 72  MET   A SD    1 
ATOM   570  C  CE    . MET   A 1 75  ? 14.922  -5.516  41.457  1.00 15.58 ? 72  MET   A CE    1 
ATOM   571  N  N     . ARG   A 1 76  ? 10.423  -7.960  46.670  1.00 16.90 ? 73  ARG   A N     1 
ATOM   572  C  CA    . ARG   A 1 76  ? 9.263   -8.633  47.307  1.00 17.67 ? 73  ARG   A CA    1 
ATOM   573  C  C     . ARG   A 1 76  ? 8.375   -7.588  47.999  1.00 17.09 ? 73  ARG   A C     1 
ATOM   574  O  O     . ARG   A 1 76  ? 7.171   -7.668  47.868  1.00 17.42 ? 73  ARG   A O     1 
ATOM   575  C  CB    . ARG   A 1 76  ? 9.757   -9.606  48.374  1.00 18.68 ? 73  ARG   A CB    1 
ATOM   576  C  CG    . ARG   A 1 76  ? 10.367  -10.887 47.841  1.00 19.76 ? 73  ARG   A CG    1 
ATOM   577  C  CD    . ARG   A 1 76  ? 10.650  -11.910 48.920  1.00 20.96 ? 73  ARG   A CD    1 
ATOM   578  N  NE    . ARG   A 1 76  ? 11.654  -12.825 48.439  1.00 21.79 ? 73  ARG   A NE    1 
ATOM   579  C  CZ    . ARG   A 1 76  ? 12.918  -12.874 48.815  1.00 21.93 ? 73  ARG   A CZ    1 
ATOM   580  N  NH1   . ARG   A 1 76  ? 13.354  -12.109 49.794  1.00 21.34 ? 73  ARG   A NH1   1 
ATOM   581  N  NH2   . ARG   A 1 76  ? 13.705  -13.751 48.234  1.00 22.74 ? 73  ARG   A NH2   1 
ATOM   582  N  N     . THR   A 1 77  ? 8.971   -6.598  48.634  1.00 16.39 ? 74  THR   A N     1 
ATOM   583  C  CA    . THR   A 1 77  ? 8.234   -5.679  49.472  1.00 16.10 ? 74  THR   A CA    1 
ATOM   584  C  C     . THR   A 1 77  ? 7.550   -4.577  48.643  1.00 15.47 ? 74  THR   A C     1 
ATOM   585  O  O     . THR   A 1 77  ? 6.438   -4.166  48.961  1.00 15.61 ? 74  THR   A O     1 
ATOM   586  C  CB    . THR   A 1 77  ? 9.141   -5.110  50.581  1.00 15.80 ? 74  THR   A CB    1 
ATOM   587  O  OG1   . THR   A 1 77  ? 9.549   -6.191  51.425  1.00 16.59 ? 74  THR   A OG1   1 
ATOM   588  C  CG2   . THR   A 1 77  ? 8.461   -4.056  51.429  1.00 15.54 ? 74  THR   A CG2   1 
ATOM   589  N  N     . GLY   A 1 78  ? 8.216   -4.082  47.596  1.00 14.90 ? 75  GLY   A N     1 
ATOM   590  C  CA    . GLY   A 1 78  ? 7.759   -2.915  46.861  1.00 14.33 ? 75  GLY   A CA    1 
ATOM   591  C  C     . GLY   A 1 78  ? 6.447   -3.181  46.130  1.00 14.75 ? 75  GLY   A C     1 
ATOM   592  O  O     . GLY   A 1 78  ? 6.226   -4.263  45.592  1.00 15.36 ? 75  GLY   A O     1 
ATOM   593  N  N     . GLU   A 1 79  ? 5.545   -2.195  46.154  1.00 14.65 ? 76  GLU   A N     1 
ATOM   594  C  CA    . GLU   A 1 79  ? 4.209   -2.350  45.549  1.00 15.18 ? 76  GLU   A CA    1 
ATOM   595  C  C     . GLU   A 1 79  ? 4.214   -1.844  44.106  1.00 14.84 ? 76  GLU   A C     1 
ATOM   596  O  O     . GLU   A 1 79  ? 3.504   -2.381  43.259  1.00 15.37 ? 76  GLU   A O     1 
ATOM   597  C  CB    . GLU   A 1 79  ? 3.159   -1.645  46.408  1.00 15.61 ? 76  GLU   A CB    1 
ATOM   598  C  CG    . GLU   A 1 79  ? 3.137   -2.155  47.832  1.00 16.20 ? 76  GLU   A CG    1 
ATOM   599  C  CD    . GLU   A 1 79  ? 2.209   -1.372  48.740  1.00 16.74 ? 76  GLU   A CD    1 
ATOM   600  O  OE1   . GLU   A 1 79  ? 2.144   -0.139  48.610  1.00 16.35 ? 76  GLU   A OE1   1 
ATOM   601  O  OE2   . GLU   A 1 79  ? 1.491   -2.013  49.526  1.00 17.79 ? 76  GLU   A OE2   1 
ATOM   602  N  N     . GLY   A 1 80  ? 5.065   -0.843  43.844  1.00 14.12 ? 77  GLY   A N     1 
ATOM   603  C  CA    . GLY   A 1 80  ? 5.241   -0.249  42.517  1.00 13.89 ? 77  GLY   A CA    1 
ATOM   604  C  C     . GLY   A 1 80  ? 6.701   0.120   42.212  1.00 13.34 ? 77  GLY   A C     1 
ATOM   605  O  O     . GLY   A 1 80  ? 7.353   0.479   43.084  1.00 13.02 ? 77  GLY   A O     1 
ATOM   606  N  N     . PHE   A 1 81  ? 7.065   0.056   40.943  1.00 13.40 ? 78  PHE   A N     1 
ATOM   607  C  CA    . PHE   A 1 81  ? 8.485   0.339   40.557  1.00 13.06 ? 78  PHE   A CA    1 
ATOM   608  C  C     . PHE   A 1 81  ? 8.595   1.377   39.436  1.00 12.96 ? 78  PHE   A C     1 
ATOM   609  O  O     . PHE   A 1 81  ? 7.999   1.180   38.424  1.00 13.32 ? 78  PHE   A O     1 
ATOM   610  C  CB    . PHE   A 1 81  ? 9.115   -0.968  40.076  1.00 13.48 ? 78  PHE   A CB    1 
ATOM   611  C  CG    . PHE   A 1 81  ? 9.158   -2.017  41.147  1.00 13.74 ? 78  PHE   A CG    1 
ATOM   612  C  CD1   . PHE   A 1 81  ? 8.069   -2.841  41.402  1.00 14.26 ? 78  PHE   A CD1   1 
ATOM   613  C  CD2   . PHE   A 1 81  ? 10.309  -2.223  41.885  1.00 13.62 ? 78  PHE   A CD2   1 
ATOM   614  C  CE1   . PHE   A 1 81  ? 8.089   -3.751  42.431  1.00 14.61 ? 78  PHE   A CE1   1 
ATOM   615  C  CE2   . PHE   A 1 81  ? 10.331  -3.150  42.902  1.00 13.96 ? 78  PHE   A CE2   1 
ATOM   616  C  CZ    . PHE   A 1 81  ? 9.238   -3.937  43.163  1.00 14.47 ? 78  PHE   A CZ    1 
ATOM   617  N  N     . LEU   A 1 82  ? 9.393   2.433   39.650  1.00 12.75 ? 79  LEU   A N     1 
ATOM   618  C  CA    . LEU   A 1 82  ? 9.762   3.369   38.568  1.00 13.07 ? 79  LEU   A CA    1 
ATOM   619  C  C     . LEU   A 1 82  ? 11.043  2.773   37.959  1.00 13.30 ? 79  LEU   A C     1 
ATOM   620  O  O     . LEU   A 1 82  ? 11.964  2.683   38.719  1.00 13.04 ? 79  LEU   A O     1 
ATOM   621  C  CB    . LEU   A 1 82  ? 10.138  4.730   39.136  1.00 13.01 ? 79  LEU   A CB    1 
ATOM   622  C  CG    . LEU   A 1 82  ? 9.025   5.716   39.465  1.00 13.32 ? 79  LEU   A CG    1 
ATOM   623  C  CD1   . LEU   A 1 82  ? 9.623   7.080   39.706  1.00 13.26 ? 79  LEU   A CD1   1 
ATOM   624  C  CD2   . LEU   A 1 82  ? 8.004   5.762   38.333  1.00 13.80 ? 79  LEU   A CD2   1 
ATOM   625  N  N     . CYS   A 1 83  ? 11.001  2.336   36.710  1.00 13.84 ? 80  CYS   A N     1 
ATOM   626  C  CA    . CYS   A 1 83  ? 12.159  1.789   35.963  1.00 14.30 ? 80  CYS   A CA    1 
ATOM   627  C  C     . CYS   A 1 83  ? 12.731  2.955   35.164  1.00 14.20 ? 80  CYS   A C     1 
ATOM   628  O  O     . CYS   A 1 83  ? 12.134  3.339   34.192  1.00 14.27 ? 80  CYS   A O     1 
ATOM   629  C  CB    . CYS   A 1 83  ? 11.735  0.665   35.049  1.00 15.12 ? 80  CYS   A CB    1 
ATOM   630  S  SG    . CYS   A 1 83  ? 11.241  -0.778  36.001  1.00 16.01 ? 80  CYS   A SG    1 
ATOM   631  N  N     . VAL   A 1 84  ? 13.860  3.487   35.625  1.00 13.84 ? 81  VAL   A N     1 
ATOM   632  C  CA    . VAL   A 1 84  ? 14.405  4.749   35.089  1.00 13.88 ? 81  VAL   A CA    1 
ATOM   633  C  C     . VAL   A 1 84  ? 15.641  4.524   34.197  1.00 14.43 ? 81  VAL   A C     1 
ATOM   634  O  O     . VAL   A 1 84  ? 16.473  3.752   34.536  1.00 14.30 ? 81  VAL   A O     1 
ATOM   635  C  CB    . VAL   A 1 84  ? 14.774  5.704   36.237  1.00 13.49 ? 81  VAL   A CB    1 
ATOM   636  C  CG1   . VAL   A 1 84  ? 15.252  7.050   35.743  1.00 13.71 ? 81  VAL   A CG1   1 
ATOM   637  C  CG2   . VAL   A 1 84  ? 13.709  5.883   37.299  1.00 13.00 ? 81  VAL   A CG2   1 
ATOM   638  N  N     . PHE   A 1 85  ? 15.630  5.163   33.048  1.00 14.76 ? 82  PHE   A N     1 
ATOM   639  C  CA    . PHE   A 1 85  ? 16.834  5.272   32.191  1.00 15.51 ? 82  PHE   A CA    1 
ATOM   640  C  C     . PHE   A 1 85  ? 17.037  6.761   31.904  1.00 15.76 ? 82  PHE   A C     1 
ATOM   641  O  O     . PHE   A 1 85  ? 16.221  7.578   32.280  1.00 15.37 ? 82  PHE   A O     1 
ATOM   642  C  CB    . PHE   A 1 85  ? 16.743  4.410   30.941  1.00 16.12 ? 82  PHE   A CB    1 
ATOM   643  C  CG    . PHE   A 1 85  ? 15.763  4.949   29.943  1.00 16.29 ? 82  PHE   A CG    1 
ATOM   644  C  CD1   . PHE   A 1 85  ? 14.410  4.700   30.083  1.00 16.01 ? 82  PHE   A CD1   1 
ATOM   645  C  CD2   . PHE   A 1 85  ? 16.189  5.745   28.905  1.00 16.95 ? 82  PHE   A CD2   1 
ATOM   646  C  CE1   . PHE   A 1 85  ? 13.521  5.222   29.167  1.00 16.35 ? 82  PHE   A CE1   1 
ATOM   647  C  CE2   . PHE   A 1 85  ? 15.298  6.243   27.976  1.00 17.40 ? 82  PHE   A CE2   1 
ATOM   648  C  CZ    . PHE   A 1 85  ? 13.954  5.994   28.129  1.00 16.97 ? 82  PHE   A CZ    1 
ATOM   649  N  N     . ALA   A 1 86  ? 18.186  7.088   31.330  1.00 16.47 ? 83  ALA   A N     1 
ATOM   650  C  CA    . ALA   A 1 86  ? 18.497  8.451   30.942  1.00 17.06 ? 83  ALA   A CA    1 
ATOM   651  C  C     . ALA   A 1 86  ? 18.429  8.517   29.408  1.00 18.08 ? 83  ALA   A C     1 
ATOM   652  O  O     . ALA   A 1 86  ? 18.975  7.640   28.724  1.00 18.60 ? 83  ALA   A O     1 
ATOM   653  C  CB    . ALA   A 1 86  ? 19.849  8.862   31.486  1.00 17.43 ? 83  ALA   A CB    1 
ATOM   654  N  N     . ILE   A 1 87  ? 17.774  9.557   28.873  1.00 18.39 ? 84  ILE   A N     1 
ATOM   655  C  CA    . ILE   A 1 87  ? 17.498  9.670   27.425  1.00 19.40 ? 84  ILE   A CA    1 
ATOM   656  C  C     . ILE   A 1 87  ? 18.785  9.897   26.609  1.00 20.34 ? 84  ILE   A C     1 
ATOM   657  O  O     . ILE   A 1 87  ? 18.770  9.824   25.364  1.00 21.05 ? 84  ILE   A O     1 
ATOM   658  C  CB    . ILE   A 1 87  ? 16.458  10.771  27.140  1.00 19.73 ? 84  ILE   A CB    1 
ATOM   659  C  CG1   . ILE   A 1 87  ? 16.976  12.168  27.478  1.00 20.26 ? 84  ILE   A CG1   1 
ATOM   660  C  CG2   . ILE   A 1 87  ? 15.149  10.483  27.860  1.00 18.86 ? 84  ILE   A CG2   1 
ATOM   661  C  CD1   . ILE   A 1 87  ? 16.115  13.257  26.890  1.00 20.93 ? 84  ILE   A CD1   1 
ATOM   662  N  N     . ASN   A 1 88  ? 19.885  10.211  27.297  1.00 20.37 ? 85  ASN   A N     1 
ATOM   663  C  CA    . ASN   A 1 88  ? 21.188  10.379  26.640  1.00 21.56 ? 85  ASN   A CA    1 
ATOM   664  C  C     . ASN   A 1 88  ? 22.136  9.202   26.915  1.00 21.72 ? 85  ASN   A C     1 
ATOM   665  O  O     . ASN   A 1 88  ? 23.354  9.320   26.681  1.00 22.64 ? 85  ASN   A O     1 
ATOM   666  C  CB    . ASN   A 1 88  ? 21.842  11.691  27.071  1.00 21.97 ? 85  ASN   A CB    1 
ATOM   667  C  CG    . ASN   A 1 88  ? 22.279  11.691  28.521  1.00 21.23 ? 85  ASN   A CG    1 
ATOM   668  O  OD1   . ASN   A 1 88  ? 21.815  10.879  29.328  1.00 20.11 ? 85  ASN   A OD1   1 
ATOM   669  N  ND2   . ASN   A 1 88  ? 23.173  12.611  28.851  1.00 21.80 ? 85  ASN   A ND2   1 
ATOM   670  N  N     . ASN   A 1 89  ? 21.618  8.070   27.386  1.00 21.07 ? 86  ASN   A N     1 
ATOM   671  C  CA    . ASN   A 1 89  ? 22.465  6.929   27.729  1.00 21.45 ? 86  ASN   A CA    1 
ATOM   672  C  C     . ASN   A 1 89  ? 21.792  5.623   27.296  1.00 21.45 ? 86  ASN   A C     1 
ATOM   673  O  O     . ASN   A 1 89  ? 21.004  5.041   28.052  1.00 20.61 ? 86  ASN   A O     1 
ATOM   674  C  CB    . ASN   A 1 89  ? 22.841  6.931   29.220  1.00 20.71 ? 86  ASN   A CB    1 
ATOM   675  C  CG    . ASN   A 1 89  ? 23.905  5.905   29.538  1.00 21.15 ? 86  ASN   A CG    1 
ATOM   676  O  OD1   . ASN   A 1 89  ? 23.601  4.734   29.699  1.00 20.74 ? 86  ASN   A OD1   1 
ATOM   677  N  ND2   . ASN   A 1 89  ? 25.177  6.323   29.544  1.00 22.05 ? 86  ASN   A ND2   1 
ATOM   678  N  N     . THR   A 1 90  ? 22.162  5.153   26.099  1.00 22.56 ? 87  THR   A N     1 
ATOM   679  C  CA    . THR   A 1 90  ? 21.639  3.943   25.478  1.00 22.98 ? 87  THR   A CA    1 
ATOM   680  C  C     . THR   A 1 90  ? 21.768  2.720   26.392  1.00 22.58 ? 87  THR   A C     1 
ATOM   681  O  O     . THR   A 1 90  ? 20.836  1.910   26.475  1.00 22.26 ? 87  THR   A O     1 
ATOM   682  C  CB    . THR   A 1 90  ? 22.337  3.675   24.138  1.00 24.73 ? 87  THR   A CB    1 
ATOM   683  O  OG1   . THR   A 1 90  ? 22.005  4.788   23.308  1.00 25.34 ? 87  THR   A OG1   1 
ATOM   684  C  CG2   . THR   A 1 90  ? 21.896  2.372   23.496  1.00 25.24 ? 87  THR   A CG2   1 
ATOM   685  N  N     . LYS   A 1 91  ? 22.914  2.561   27.062  1.00 22.83 ? 88  LYS   A N     1 
ATOM   686  C  CA    . LYS   A 1 91  ? 23.156  1.378   27.911  1.00 22.70 ? 88  LYS   A CA    1 
ATOM   687  C  C     . LYS   A 1 91  ? 22.113  1.284   29.036  1.00 21.02 ? 88  LYS   A C     1 
ATOM   688  O  O     . LYS   A 1 91  ? 21.649  0.186   29.339  1.00 20.84 ? 88  LYS   A O     1 
ATOM   689  C  CB    . LYS   A 1 91  ? 24.584  1.391   28.475  1.00 23.63 ? 88  LYS   A CB    1 
ATOM   690  C  CG    . LYS   A 1 91  ? 24.926  0.232   29.403  1.00 23.97 ? 88  LYS   A CG    1 
ATOM   691  C  CD    . LYS   A 1 91  ? 24.922  -1.115  28.698  1.00 25.19 ? 88  LYS   A CD    1 
ATOM   692  C  CE    . LYS   A 1 91  ? 25.626  -2.201  29.485  1.00 25.82 ? 88  LYS   A CE    1 
ATOM   693  N  NZ    . LYS   A 1 91  ? 25.120  -2.244  30.881  1.00 24.93 ? 88  LYS   A NZ    1 
ATOM   694  N  N     . SER   A 1 92  ? 21.762  2.428   29.641  1.00 19.97 ? 89  SER   A N     1 
ATOM   695  C  CA    . SER   A 1 92  ? 20.763  2.496   30.706  1.00 18.65 ? 89  SER   A CA    1 
ATOM   696  C  C     . SER   A 1 92  ? 19.381  2.089   30.178  1.00 18.28 ? 89  SER   A C     1 
ATOM   697  O  O     . SER   A 1 92  ? 18.618  1.507   30.910  1.00 17.50 ? 89  SER   A O     1 
ATOM   698  C  CB    . SER   A 1 92  ? 20.678  3.861   31.350  1.00 18.07 ? 89  SER   A CB    1 
ATOM   699  O  OG    . SER   A 1 92  ? 19.979  4.782   30.511  1.00 17.91 ? 89  SER   A OG    1 
ATOM   700  N  N     . PHE   A 1 93  ? 19.078  2.443   28.924  1.00 18.79 ? 90  PHE   A N     1 
ATOM   701  C  CA    . PHE   A 1 93  ? 17.851  1.982   28.270  1.00 18.82 ? 90  PHE   A CA    1 
ATOM   702  C  C     . PHE   A 1 93  ? 17.911  0.461   28.059  1.00 19.48 ? 90  PHE   A C     1 
ATOM   703  O  O     . PHE   A 1 93  ? 16.978  -0.238  28.318  1.00 19.23 ? 90  PHE   A O     1 
ATOM   704  C  CB    . PHE   A 1 93  ? 17.626  2.702   26.938  1.00 19.40 ? 90  PHE   A CB    1 
ATOM   705  C  CG    . PHE   A 1 93  ? 16.361  2.264   26.238  1.00 19.50 ? 90  PHE   A CG    1 
ATOM   706  C  CD1   . PHE   A 1 93  ? 15.122  2.657   26.725  1.00 18.80 ? 90  PHE   A CD1   1 
ATOM   707  C  CD2   . PHE   A 1 93  ? 16.401  1.430   25.133  1.00 20.39 ? 90  PHE   A CD2   1 
ATOM   708  C  CE1   . PHE   A 1 93  ? 13.958  2.230   26.112  1.00 19.03 ? 90  PHE   A CE1   1 
ATOM   709  C  CE2   . PHE   A 1 93  ? 15.231  1.017   24.512  1.00 20.66 ? 90  PHE   A CE2   1 
ATOM   710  C  CZ    . PHE   A 1 93  ? 14.011  1.411   25.009  1.00 19.97 ? 90  PHE   A CZ    1 
ATOM   711  N  N     . GLU   A 1 94  ? 19.054  -0.057  27.599  1.00 20.62 ? 91  GLU   A N     1 
ATOM   712  C  CA    . GLU   A 1 94  ? 19.173  -1.476  27.325  1.00 21.58 ? 91  GLU   A CA    1 
ATOM   713  C  C     . GLU   A 1 94  ? 19.078  -2.312  28.601  1.00 21.09 ? 91  GLU   A C     1 
ATOM   714  O  O     . GLU   A 1 94  ? 18.686  -3.483  28.532  1.00 21.65 ? 91  GLU   A O     1 
ATOM   715  C  CB    . GLU   A 1 94  ? 20.502  -1.771  26.652  1.00 23.11 ? 91  GLU   A CB    1 
ATOM   716  C  CG    . GLU   A 1 94  ? 20.555  -1.249  25.234  1.00 24.30 ? 91  GLU   A CG    1 
ATOM   717  C  CD    . GLU   A 1 94  ? 21.962  -1.300  24.691  1.00 25.69 ? 91  GLU   A CD    1 
ATOM   718  O  OE1   . GLU   A 1 94  ? 22.844  -1.755  25.440  1.00 26.35 ? 91  GLU   A OE1   1 
ATOM   719  O  OE2   . GLU   A 1 94  ? 22.177  -0.888  23.536  1.00 26.85 ? 91  GLU   A OE2   1 
ATOM   720  N  N     . ASP   A 1 95  ? 19.480  -1.726  29.734  1.00 20.22 ? 92  ASP   A N     1 
ATOM   721  C  CA    . ASP   A 1 95  ? 19.441  -2.403  31.034  1.00 19.80 ? 92  ASP   A CA    1 
ATOM   722  C  C     . ASP   A 1 95  ? 18.008  -2.554  31.539  1.00 19.06 ? 92  ASP   A C     1 
ATOM   723  O  O     . ASP   A 1 95  ? 17.760  -3.416  32.377  1.00 18.75 ? 92  ASP   A O     1 
ATOM   724  C  CB    . ASP   A 1 95  ? 20.200  -1.630  32.104  1.00 19.24 ? 92  ASP   A CB    1 
ATOM   725  C  CG    . ASP   A 1 95  ? 21.709  -1.659  31.941  1.00 20.18 ? 92  ASP   A CG    1 
ATOM   726  O  OD1   . ASP   A 1 95  ? 22.230  -2.428  31.099  1.00 20.97 ? 92  ASP   A OD1   1 
ATOM   727  O  OD2   . ASP   A 1 95  ? 22.334  -0.879  32.646  1.00 20.09 ? 92  ASP   A OD2   1 
ATOM   728  N  N     . ILE   A 1 96  ? 17.090  -1.708  31.050  1.00 18.86 ? 93  ILE   A N     1 
ATOM   729  C  CA    . ILE   A 1 96  ? 15.703  -1.666  31.576  1.00 18.35 ? 93  ILE   A CA    1 
ATOM   730  C  C     . ILE   A 1 96  ? 15.079  -3.065  31.594  1.00 18.97 ? 93  ILE   A C     1 
ATOM   731  O  O     . ILE   A 1 96  ? 14.447  -3.466  32.585  1.00 18.70 ? 93  ILE   A O     1 
ATOM   732  C  CB    . ILE   A 1 96  ? 14.814  -0.696  30.767  1.00 18.30 ? 93  ILE   A CB    1 
ATOM   733  C  CG1   . ILE   A 1 96  ? 15.172  0.767   31.047  1.00 17.86 ? 93  ILE   A CG1   1 
ATOM   734  C  CG2   . ILE   A 1 96  ? 13.336  -0.952  31.048  1.00 17.99 ? 93  ILE   A CG2   1 
ATOM   735  C  CD1   . ILE   A 1 96  ? 14.805  1.240   32.444  1.00 17.10 ? 93  ILE   A CD1   1 
ATOM   736  N  N     . HIS   A 1 97  ? 15.201  -3.792  30.481  1.00 20.17 ? 94  HIS   A N     1 
ATOM   737  C  CA    . HIS   A 1 97  ? 14.623  -5.128  30.378  1.00 21.14 ? 94  HIS   A CA    1 
ATOM   738  C  C     . HIS   A 1 97  ? 15.106  -6.045  31.519  1.00 21.19 ? 94  HIS   A C     1 
ATOM   739  O  O     . HIS   A 1 97  ? 14.380  -6.923  31.943  1.00 21.19 ? 94  HIS   A O     1 
ATOM   740  C  CB    . HIS   A 1 97  ? 14.918  -5.714  28.994  1.00 22.80 ? 94  HIS   A CB    1 
ATOM   741  C  CG    . HIS   A 1 97  ? 14.503  -7.140  28.862  1.00 24.13 ? 94  HIS   A CG    1 
ATOM   742  N  ND1   . HIS   A 1 97  ? 15.422  -8.176  28.819  1.00 25.29 ? 94  HIS   A ND1   1 
ATOM   743  C  CD2   . HIS   A 1 97  ? 13.272  -7.707  28.803  1.00 24.71 ? 94  HIS   A CD2   1 
ATOM   744  C  CE1   . HIS   A 1 97  ? 14.777  -9.327  28.741  1.00 26.24 ? 94  HIS   A CE1   1 
ATOM   745  N  NE2   . HIS   A 1 97  ? 13.456  -9.063  28.728  1.00 25.84 ? 94  HIS   A NE2   1 
ATOM   746  N  N     . HIS   A 1 98  ? 16.366  -5.882  31.945  1.00 21.33 ? 95  HIS   A N     1 
ATOM   747  C  CA    . HIS   A 1 98  ? 16.938  -6.710  32.999  1.00 21.87 ? 95  HIS   A CA    1 
ATOM   748  C  C     . HIS   A 1 98  ? 16.302  -6.403  34.362  1.00 20.63 ? 95  HIS   A C     1 
ATOM   749  O  O     . HIS   A 1 98  ? 16.059  -7.331  35.110  1.00 20.97 ? 95  HIS   A O     1 
ATOM   750  C  CB    . HIS   A 1 98  ? 18.458  -6.569  33.036  1.00 22.65 ? 95  HIS   A CB    1 
ATOM   751  C  CG    . HIS   A 1 98  ? 19.115  -7.138  31.830  1.00 24.51 ? 95  HIS   A CG    1 
ATOM   752  N  ND1   . HIS   A 1 98  ? 19.126  -8.496  31.562  1.00 25.94 ? 95  HIS   A ND1   1 
ATOM   753  C  CD2   . HIS   A 1 98  ? 19.778  -6.545  30.812  1.00 25.27 ? 95  HIS   A CD2   1 
ATOM   754  C  CE1   . HIS   A 1 98  ? 19.803  -8.718  30.452  1.00 27.11 ? 95  HIS   A CE1   1 
ATOM   755  N  NE2   . HIS   A 1 98  ? 20.207  -7.535  29.964  1.00 26.80 ? 95  HIS   A NE2   1 
ATOM   756  N  N     . TYR   A 1 99  ? 16.029  -5.128  34.668  1.00 19.52 ? 96  TYR   A N     1 
ATOM   757  C  CA    . TYR   A 1 99  ? 15.368  -4.745  35.927  1.00 18.63 ? 96  TYR   A CA    1 
ATOM   758  C  C     . TYR   A 1 99  ? 13.930  -5.285  35.944  1.00 18.81 ? 96  TYR   A C     1 
ATOM   759  O  O     . TYR   A 1 99  ? 13.479  -5.821  36.943  1.00 18.29 ? 96  TYR   A O     1 
ATOM   760  C  CB    . TYR   A 1 99  ? 15.383  -3.229  36.154  1.00 17.85 ? 96  TYR   A CB    1 
ATOM   761  C  CG    . TYR   A 1 99  ? 16.757  -2.666  36.416  1.00 17.79 ? 96  TYR   A CG    1 
ATOM   762  C  CD1   . TYR   A 1 99  ? 17.385  -2.843  37.639  1.00 17.75 ? 96  TYR   A CD1   1 
ATOM   763  C  CD2   . TYR   A 1 99  ? 17.463  -2.017  35.419  1.00 18.17 ? 96  TYR   A CD2   1 
ATOM   764  C  CE1   . TYR   A 1 99  ? 18.678  -2.389  37.874  1.00 17.89 ? 96  TYR   A CE1   1 
ATOM   765  C  CE2   . TYR   A 1 99  ? 18.776  -1.590  35.619  1.00 18.40 ? 96  TYR   A CE2   1 
ATOM   766  C  CZ    . TYR   A 1 99  ? 19.368  -1.736  36.866  1.00 18.12 ? 96  TYR   A CZ    1 
ATOM   767  O  OH    . TYR   A 1 99  ? 20.644  -1.298  37.083  1.00 18.58 ? 96  TYR   A OH    1 
ATOM   768  N  N     . ARG   A 1 100 ? 13.219  -5.121  34.827  1.00 19.29 ? 97  ARG   A N     1 
ATOM   769  C  CA    . ARG   A 1 100 ? 11.858  -5.600  34.737  1.00 19.86 ? 97  ARG   A CA    1 
ATOM   770  C  C     . ARG   A 1 100 ? 11.805  -7.123  34.909  1.00 20.81 ? 97  ARG   A C     1 
ATOM   771  O  O     . ARG   A 1 100 ? 10.882  -7.646  35.557  1.00 21.02 ? 97  ARG   A O     1 
ATOM   772  C  CB    . ARG   A 1 100 ? 11.174  -5.163  33.437  1.00 20.28 ? 97  ARG   A CB    1 
ATOM   773  C  CG    . ARG   A 1 100 ? 9.808   -5.800  33.258  1.00 21.08 ? 97  ARG   A CG    1 
ATOM   774  C  CD    . ARG   A 1 100 ? 9.007   -5.167  32.140  1.00 21.52 ? 97  ARG   A CD    1 
ATOM   775  N  NE    . ARG   A 1 100 ? 7.809   -5.946  31.866  1.00 22.59 ? 97  ARG   A NE    1 
ATOM   776  C  CZ    . ARG   A 1 100 ? 6.639   -5.782  32.487  1.00 22.64 ? 97  ARG   A CZ    1 
ATOM   777  N  NH1   . ARG   A 1 100 ? 6.514   -4.865  33.429  1.00 22.04 ? 97  ARG   A NH1   1 
ATOM   778  N  NH2   . ARG   A 1 100 ? 5.596   -6.541  32.171  1.00 23.74 ? 97  ARG   A NH2   1 
ATOM   779  N  N     . GLU   A 1 101 ? 12.761  -7.839  34.319  1.00 21.53 ? 98  GLU   A N     1 
ATOM   780  C  CA    . GLU   A 1 101 ? 12.727  -9.313  34.416  1.00 22.77 ? 98  GLU   A CA    1 
ATOM   781  C  C     . GLU   A 1 101 ? 12.980  -9.753  35.855  1.00 22.34 ? 98  GLU   A C     1 
ATOM   782  O  O     . GLU   A 1 101 ? 12.333  -10.658 36.329  1.00 22.50 ? 98  GLU   A O     1 
ATOM   783  C  CB    . GLU   A 1 101 ? 13.735  -9.883  33.431  1.00 24.30 ? 98  GLU   A CB    1 
ATOM   784  C  CG    . GLU   A 1 101 ? 13.174  -9.912  32.033  1.00 25.54 ? 98  GLU   A CG    1 
ATOM   785  C  CD    . GLU   A 1 101 ? 11.984  -10.845 31.899  1.00 27.03 ? 98  GLU   A CD    1 
ATOM   786  O  OE1   . GLU   A 1 101 ? 12.007  -11.889 32.524  1.00 28.16 ? 98  GLU   A OE1   1 
ATOM   787  O  OE2   . GLU   A 1 101 ? 11.018  -10.488 31.207  1.00 27.86 ? 98  GLU   A OE2   1 
ATOM   788  N  N     . GLN   A 1 102 ? 13.932  -9.098  36.489  1.00 21.50 ? 99  GLN   A N     1 
ATOM   789  C  CA    . GLN   A 1 102 ? 14.277  -9.420  37.876  1.00 21.50 ? 99  GLN   A CA    1 
ATOM   790  C  C     . GLN   A 1 102 ? 13.080  -9.180  38.800  1.00 20.38 ? 99  GLN   A C     1 
ATOM   791  O  O     . GLN   A 1 102 ? 12.821  -9.990  39.625  1.00 20.77 ? 99  GLN   A O     1 
ATOM   792  C  CB    . GLN   A 1 102 ? 15.365  -8.436  38.265  1.00 21.51 ? 99  GLN   A CB    1 
ATOM   793  C  CG    . GLN   A 1 102 ? 15.941  -8.670  39.625  1.00 22.03 ? 99  GLN   A CG    1 
ATOM   794  C  CD    . GLN   A 1 102 ? 17.331  -8.098  39.601  1.00 22.61 ? 99  GLN   A CD    1 
ATOM   795  O  OE1   . GLN   A 1 102 ? 18.133  -8.444  40.447  1.00 23.86 ? 99  GLN   A OE1   1 
ATOM   796  N  NE2   . GLN   A 1 102 ? 17.602  -7.229  38.637  1.00 22.26 ? 99  GLN   A NE2   1 
ATOM   797  N  N     . ILE   A 1 103 ? 12.420  -8.056  38.637  1.00 19.00 ? 100 ILE   A N     1 
ATOM   798  C  CA    . ILE   A 1 103 ? 11.241  -7.790  39.502  1.00 18.47 ? 100 ILE   A CA    1 
ATOM   799  C  C     . ILE   A 1 103 ? 10.226  -8.918  39.307  1.00 19.29 ? 100 ILE   A C     1 
ATOM   800  O  O     . ILE   A 1 103 ? 9.830   -9.523  40.258  1.00 19.59 ? 100 ILE   A O     1 
ATOM   801  C  CB    . ILE   A 1 103 ? 10.679  -6.402  39.191  1.00 17.42 ? 100 ILE   A CB    1 
ATOM   802  C  CG1   . ILE   A 1 103 ? 11.682  -5.324  39.588  1.00 16.53 ? 100 ILE   A CG1   1 
ATOM   803  C  CG2   . ILE   A 1 103 ? 9.347   -6.214  39.888  1.00 17.25 ? 100 ILE   A CG2   1 
ATOM   804  C  CD1   . ILE   A 1 103 ? 11.540  -4.075  38.836  1.00 16.01 ? 100 ILE   A CD1   1 
ATOM   805  N  N     . LYS   A 1 104 ? 9.949   -9.233  38.070  1.00 19.90 ? 101 LYS   A N     1 
ATOM   806  C  CA    . LYS   A 1 104 ? 8.942   -10.258 37.769  1.00 21.19 ? 101 LYS   A CA    1 
ATOM   807  C  C     . LYS   A 1 104 ? 9.324   -11.622 38.368  1.00 22.29 ? 101 LYS   A C     1 
ATOM   808  O  O     . LYS   A 1 104 ? 8.462   -12.349 38.865  1.00 22.79 ? 101 LYS   A O     1 
ATOM   809  C  CB    . LYS   A 1 104 ? 8.745   -10.388 36.261  1.00 21.90 ? 101 LYS   A CB    1 
ATOM   810  C  CG    . LYS   A 1 104 ? 8.089   -9.179  35.619  1.00 21.40 ? 101 LYS   A CG    1 
ATOM   811  C  CD    . LYS   A 1 104 ? 8.296   -9.142  34.132  1.00 22.17 ? 101 LYS   A CD    1 
ATOM   812  C  CE    . LYS   A 1 104 ? 7.560   -10.222 33.381  1.00 23.61 ? 101 LYS   A CE    1 
ATOM   813  N  NZ    . LYS   A 1 104 ? 8.189   -10.453 32.052  1.00 24.41 ? 101 LYS   A NZ    1 
ATOM   814  N  N     . ARG   A 1 105 ? 10.608  -11.980 38.267  1.00 22.66 ? 102 ARG   A N     1 
ATOM   815  C  CA    . ARG   A 1 105 ? 11.116  -13.286 38.771  1.00 24.06 ? 102 ARG   A CA    1 
ATOM   816  C  C     . ARG   A 1 105 ? 10.979  -13.343 40.296  1.00 23.58 ? 102 ARG   A C     1 
ATOM   817  O  O     . ARG   A 1 105 ? 10.595  -14.409 40.816  1.00 24.38 ? 102 ARG   A O     1 
ATOM   818  C  CB    . ARG   A 1 105 ? 12.580  -13.450 38.350  1.00 24.82 ? 102 ARG   A CB    1 
ATOM   819  C  CG    . ARG   A 1 105 ? 13.296  -14.681 38.886  1.00 26.62 ? 102 ARG   A CG    1 
ATOM   820  C  CD    . ARG   A 1 105 ? 14.797  -14.744 38.511  1.00 27.67 ? 102 ARG   A CD    1 
ATOM   821  N  NE    . ARG   A 1 105 ? 15.517  -13.533 38.878  1.00 27.12 ? 102 ARG   A NE    1 
ATOM   822  C  CZ    . ARG   A 1 105 ? 16.092  -12.707 38.011  1.00 27.30 ? 102 ARG   A CZ    1 
ATOM   823  N  NH1   . ARG   A 1 105 ? 16.725  -11.629 38.443  1.00 26.56 ? 102 ARG   A NH1   1 
ATOM   824  N  NH2   . ARG   A 1 105 ? 16.033  -12.961 36.716  1.00 28.20 ? 102 ARG   A NH2   1 
ATOM   825  N  N     . VAL   A 1 106 ? 11.241  -12.220 40.970  1.00 22.31 ? 103 VAL   A N     1 
ATOM   826  C  CA    . VAL   A 1 106 ? 11.190  -12.154 42.455  1.00 22.18 ? 103 VAL   A CA    1 
ATOM   827  C  C     . VAL   A 1 106 ? 9.754   -12.253 42.947  1.00 22.46 ? 103 VAL   A C     1 
ATOM   828  O  O     . VAL   A 1 106 ? 9.496   -12.992 43.831  1.00 22.99 ? 103 VAL   A O     1 
ATOM   829  C  CB    . VAL   A 1 106 ? 11.873  -10.889 42.989  1.00 20.99 ? 103 VAL   A CB    1 
ATOM   830  C  CG1   . VAL   A 1 106 ? 11.674  -10.754 44.477  1.00 20.80 ? 103 VAL   A CG1   1 
ATOM   831  C  CG2   . VAL   A 1 106 ? 13.340  -10.933 42.637  1.00 21.04 ? 103 VAL   A CG2   1 
ATOM   832  N  N     . LYS   A 1 107 ? 8.883   -11.501 42.300  1.00 22.29 ? 104 LYS   A N     1 
ATOM   833  C  CA    . LYS   A 1 107 ? 7.436   -11.502 42.592  1.00 22.83 ? 104 LYS   A CA    1 
ATOM   834  C  C     . LYS   A 1 107 ? 6.787   -12.789 42.080  1.00 24.77 ? 104 LYS   A C     1 
ATOM   835  O  O     . LYS   A 1 107 ? 5.713   -13.080 42.533  1.00 25.23 ? 104 LYS   A O     1 
ATOM   836  C  CB    . LYS   A 1 107 ? 6.750   -10.324 41.894  1.00 22.02 ? 104 LYS   A CB    1 
ATOM   837  C  CG    . LYS   A 1 107 ? 7.164   -8.925  42.304  1.00 20.68 ? 104 LYS   A CG    1 
ATOM   838  C  CD    . LYS   A 1 107 ? 6.390   -8.456  43.477  1.00 20.55 ? 104 LYS   A CD    1 
ATOM   839  C  CE    . LYS   A 1 107 ? 6.467   -6.988  43.778  1.00 19.16 ? 104 LYS   A CE    1 
ATOM   840  N  NZ    . LYS   A 1 107 ? 6.463   -6.820  45.229  1.00 19.01 ? 104 LYS   A NZ    1 
ATOM   841  N  N     . ASP   A 1 108 ? 7.405   -13.476 41.124  1.00 25.92 ? 105 ASP   A N     1 
ATOM   842  C  CA    . ASP   A 1 108 ? 6.757   -14.623 40.442  1.00 27.63 ? 105 ASP   A CA    1 
ATOM   843  C  C     . ASP   A 1 108 ? 5.426   -14.116 39.873  1.00 28.08 ? 105 ASP   A C     1 
ATOM   844  O  O     . ASP   A 1 108 ? 4.380   -14.679 40.216  1.00 29.08 ? 105 ASP   A O     1 
ATOM   845  C  CB    . ASP   A 1 108 ? 6.711   -15.867 41.313  1.00 28.90 ? 105 ASP   A CB    1 
ATOM   846  C  CG    . ASP   A 1 108 ? 6.125   -17.045 40.584  1.00 30.58 ? 105 ASP   A CG    1 
ATOM   847  O  OD1   . ASP   A 1 108 ? 6.485   -17.250 39.433  1.00 31.10 ? 105 ASP   A OD1   1 
ATOM   848  O  OD2   . ASP   A 1 108 ? 5.312   -17.701 41.179  1.00 31.63 ? 105 ASP   A OD2   1 
ATOM   849  N  N     . SER   A 1 109 ? 5.478   -13.087 39.033  1.00 27.97 ? 106 SER   A N     1 
ATOM   850  C  CA    . SER   A 1 109 ? 4.276   -12.454 38.489  1.00 28.74 ? 106 SER   A CA    1 
ATOM   851  C  C     . SER   A 1 109 ? 4.615   -11.677 37.220  1.00 28.81 ? 106 SER   A C     1 
ATOM   852  O  O     . SER   A 1 109 ? 5.615   -10.972 37.193  1.00 28.43 ? 106 SER   A O     1 
ATOM   853  C  CB    . SER   A 1 109 ? 3.654   -11.536 39.498  1.00 28.15 ? 106 SER   A CB    1 
ATOM   854  O  OG    . SER   A 1 109 ? 2.515   -10.903 38.919  1.00 28.59 ? 106 SER   A OG    1 
ATOM   855  N  N     . GLU   A 1 110 ? 3.766   -11.829 36.198  1.00 30.43 ? 107 GLU   A N     1 
ATOM   856  C  CA    . GLU   A 1 110 ? 4.040   -11.126 34.930  1.00 30.40 ? 107 GLU   A CA    1 
ATOM   857  C  C     . GLU   A 1 110 ? 3.383   -9.757  34.970  1.00 29.22 ? 107 GLU   A C     1 
ATOM   858  O  O     . GLU   A 1 110 ? 3.780   -8.939  34.169  1.00 29.13 ? 107 GLU   A O     1 
ATOM   859  C  CB    . GLU   A 1 110 ? 3.759   -11.979 33.695  1.00 32.61 ? 107 GLU   A CB    1 
ATOM   860  C  CG    . GLU   A 1 110 ? 5.033   -12.461 33.055  1.00 33.58 ? 107 GLU   A CG    1 
ATOM   861  C  CD    . GLU   A 1 110 ? 4.905   -13.560 32.024  1.00 36.02 ? 107 GLU   A CD    1 
ATOM   862  O  OE1   . GLU   A 1 110 ? 4.374   -13.286 30.939  1.00 37.26 ? 107 GLU   A OE1   1 
ATOM   863  O  OE2   . GLU   A 1 110 ? 5.356   -14.688 32.314  1.00 37.94 ? 107 GLU   A OE2   1 
ATOM   864  N  N     . ASP   A 1 111 ? 2.447   -9.549  35.904  1.00 29.00 ? 108 ASP   A N     1 
ATOM   865  C  CA    . ASP   A 1 111 ? 1.815   -8.211  36.060  1.00 27.70 ? 108 ASP   A CA    1 
ATOM   866  C  C     . ASP   A 1 111 ? 2.214   -7.645  37.424  1.00 25.35 ? 108 ASP   A C     1 
ATOM   867  O  O     . ASP   A 1 111 ? 1.733   -8.079  38.442  1.00 26.13 ? 108 ASP   A O     1 
ATOM   868  C  CB    . ASP   A 1 111 ? 0.303   -8.160  35.815  1.00 29.67 ? 108 ASP   A CB    1 
ATOM   869  C  CG    . ASP   A 1 111 ? -0.082  -8.004  34.342  1.00 31.46 ? 108 ASP   A CG    1 
ATOM   870  O  OD1   . ASP   A 1 111 ? 0.589   -8.590  33.499  1.00 32.58 ? 108 ASP   A OD1   1 
ATOM   871  O  OD2   . ASP   A 1 111 ? -1.032  -7.268  34.055  1.00 32.50 ? 108 ASP   A OD2   1 
ATOM   872  N  N     . VAL   A 1 112 ? 3.053   -6.641  37.387  1.00 22.27 ? 109 VAL   A N     1 
ATOM   873  C  CA    . VAL   A 1 112 ? 3.497   -5.955  38.623  1.00 20.52 ? 109 VAL   A CA    1 
ATOM   874  C  C     . VAL   A 1 112 ? 3.380   -4.510  38.260  1.00 19.20 ? 109 VAL   A C     1 
ATOM   875  O  O     . VAL   A 1 112 ? 3.799   -4.132  37.196  1.00 18.90 ? 109 VAL   A O     1 
ATOM   876  C  CB    . VAL   A 1 112 ? 4.992   -6.159  38.911  1.00 19.68 ? 109 VAL   A CB    1 
ATOM   877  C  CG1   . VAL   A 1 112 ? 5.456   -5.208  40.007  1.00 18.68 ? 109 VAL   A CG1   1 
ATOM   878  C  CG2   . VAL   A 1 112 ? 5.326   -7.608  39.186  1.00 20.52 ? 109 VAL   A CG2   1 
ATOM   879  N  N     . PRO   A 1 113 ? 2.781   -3.454  39.101  1.00 18.18 ? 110 PRO   A N     1 
ATOM   880  C  CA    . PRO   A 1 113 ? 2.713   -2.017  38.856  1.00 17.32 ? 110 PRO   A CA    1 
ATOM   881  C  C     . PRO   A 1 113 ? 4.101   -1.438  38.559  1.00 16.53 ? 110 PRO   A C     1 
ATOM   882  O  O     . PRO   A 1 113 ? 5.005   -1.628  39.355  1.00 15.80 ? 110 PRO   A O     1 
ATOM   883  C  CB    . PRO   A 1 113 ? 2.218   -1.454  40.185  1.00 17.17 ? 110 PRO   A CB    1 
ATOM   884  C  CG    . PRO   A 1 113 ? 1.369   -2.579  40.746  1.00 18.12 ? 110 PRO   A CG    1 
ATOM   885  C  CD    . PRO   A 1 113 ? 2.162   -3.818  40.384  1.00 18.51 ? 110 PRO   A CD    1 
ATOM   886  N  N     . MET   A 1 114 ? 4.228   -0.776  37.410  1.00 16.39 ? 111 MET   A N     1 
ATOM   887  C  CA    . MET   A 1 114 ? 5.509   -0.244  36.940  1.00 15.97 ? 111 MET   A CA    1 
ATOM   888  C  C     . MET   A 1 114 ? 5.243   0.935   36.003  1.00 15.49 ? 111 MET   A C     1 
ATOM   889  O  O     . MET   A 1 114 ? 4.285   0.900   35.260  1.00 15.79 ? 111 MET   A O     1 
ATOM   890  C  CB    . MET   A 1 114 ? 6.257   -1.314  36.143  1.00 16.88 ? 111 MET   A CB    1 
ATOM   891  C  CG    . MET   A 1 114 ? 6.967   -2.327  36.980  1.00 17.39 ? 111 MET   A CG    1 
ATOM   892  S  SD    . MET   A 1 114 ? 7.950   -3.509  36.015  1.00 18.68 ? 111 MET   A SD    1 
ATOM   893  C  CE    . MET   A 1 114 ? 8.512   -2.490  34.661  1.00 18.39 ? 111 MET   A CE    1 
ATOM   894  N  N     . VAL   A 1 115 ? 6.132   1.934   36.032  1.00 14.52 ? 112 VAL   A N     1 
ATOM   895  C  CA    . VAL   A 1 115 ? 6.176   3.009   35.060  1.00 14.42 ? 112 VAL   A CA    1 
ATOM   896  C  C     . VAL   A 1 115 ? 7.611   3.071   34.508  1.00 14.26 ? 112 VAL   A C     1 
ATOM   897  O  O     . VAL   A 1 115 ? 8.582   3.003   35.283  1.00 13.75 ? 112 VAL   A O     1 
ATOM   898  C  CB    . VAL   A 1 115 ? 5.757   4.356   35.677  1.00 14.10 ? 112 VAL   A CB    1 
ATOM   899  C  CG1   . VAL   A 1 115 ? 5.961   5.519   34.716  1.00 14.23 ? 112 VAL   A CG1   1 
ATOM   900  C  CG2   . VAL   A 1 115 ? 4.323   4.327   36.194  1.00 14.41 ? 112 VAL   A CG2   1 
ATOM   901  N  N     . LEU   A 1 116 ? 7.728   3.188   33.179  1.00 14.65 ? 113 LEU   A N     1 
ATOM   902  C  CA    . LEU   A 1 116 ? 9.014   3.445   32.515  1.00 14.82 ? 113 LEU   A CA    1 
ATOM   903  C  C     . LEU   A 1 116 ? 9.305   4.947   32.545  1.00 14.63 ? 113 LEU   A C     1 
ATOM   904  O  O     . LEU   A 1 116 ? 8.480   5.745   32.128  1.00 14.81 ? 113 LEU   A O     1 
ATOM   905  C  CB    . LEU   A 1 116 ? 8.973   2.930   31.071  1.00 15.49 ? 113 LEU   A CB    1 
ATOM   906  C  CG    . LEU   A 1 116 ? 10.246  3.175   30.257  1.00 15.75 ? 113 LEU   A CG    1 
ATOM   907  C  CD1   . LEU   A 1 116 ? 11.416  2.400   30.841  1.00 15.54 ? 113 LEU   A CD1   1 
ATOM   908  C  CD2   . LEU   A 1 116 ? 10.029  2.836   28.787  1.00 16.60 ? 113 LEU   A CD2   1 
ATOM   909  N  N     . VAL   A 1 117 ? 10.506  5.329   32.996  1.00 14.28 ? 114 VAL   A N     1 
ATOM   910  C  CA    . VAL   A 1 117 ? 10.819  6.728   33.092  1.00 14.28 ? 114 VAL   A CA    1 
ATOM   911  C  C     . VAL   A 1 117 ? 12.080  7.026   32.277  1.00 14.67 ? 114 VAL   A C     1 
ATOM   912  O  O     . VAL   A 1 117 ? 13.125  6.440   32.533  1.00 14.56 ? 114 VAL   A O     1 
ATOM   913  C  CB    . VAL   A 1 117 ? 10.993  7.166   34.559  1.00 13.80 ? 114 VAL   A CB    1 
ATOM   914  C  CG1   . VAL   A 1 117 ? 11.473  8.609   34.647  1.00 13.97 ? 114 VAL   A CG1   1 
ATOM   915  C  CG2   . VAL   A 1 117 ? 9.743   6.925   35.386  1.00 13.66 ? 114 VAL   A CG2   1 
ATOM   916  N  N     . GLY   A 1 118 ? 11.943  7.930   31.306  1.00 15.21 ? 115 GLY   A N     1 
ATOM   917  C  CA    . GLY   A 1 118 ? 13.075  8.491   30.557  1.00 15.71 ? 115 GLY   A CA    1 
ATOM   918  C  C     . GLY   A 1 118 ? 13.451  9.848   31.128  1.00 15.61 ? 115 GLY   A C     1 
ATOM   919  O  O     . GLY   A 1 118 ? 12.752  10.852  30.888  1.00 15.69 ? 115 GLY   A O     1 
ATOM   920  N  N     . ASN   A 1 119 ? 14.520  9.839   31.928  1.00 15.28 ? 116 ASN   A N     1 
ATOM   921  C  CA    . ASN   A 1 119 ? 15.002  11.029  32.661  1.00 15.26 ? 116 ASN   A CA    1 
ATOM   922  C  C     . ASN   A 1 119 ? 16.004  11.858  31.823  1.00 16.17 ? 116 ASN   A C     1 
ATOM   923  O  O     . ASN   A 1 119 ? 16.539  11.296  30.872  1.00 16.65 ? 116 ASN   A O     1 
ATOM   924  C  CB    . ASN   A 1 119 ? 15.476  10.605  34.056  1.00 14.61 ? 116 ASN   A CB    1 
ATOM   925  C  CG    . ASN   A 1 119 ? 15.713  11.737  35.026  1.00 14.52 ? 116 ASN   A CG    1 
ATOM   926  O  OD1   . ASN   A 1 119 ? 14.980  12.692  34.999  1.00 14.53 ? 116 ASN   A OD1   1 
ATOM   927  N  ND2   . ASN   A 1 119 ? 16.861  11.751  35.670  1.00 14.50 ? 116 ASN   A ND2   1 
ATOM   928  N  N     . LYS   A 1 120 ? 16.243  13.106  32.251  1.00 16.50 ? 117 LYS   A N     1 
ATOM   929  C  CA    . LYS   A 1 120 ? 17.167  14.144  31.709  1.00 17.51 ? 117 LYS   A CA    1 
ATOM   930  C  C     . LYS   A 1 120 ? 16.588  14.724  30.422  1.00 18.39 ? 117 LYS   A C     1 
ATOM   931  O  O     . LYS   A 1 120 ? 17.335  14.976  29.547  1.00 19.13 ? 117 LYS   A O     1 
ATOM   932  C  CB    . LYS   A 1 120 ? 18.588  13.608  31.555  1.00 17.92 ? 117 LYS   A CB    1 
ATOM   933  C  CG    . LYS   A 1 120 ? 19.118  12.801  32.722  1.00 17.26 ? 117 LYS   A CG    1 
ATOM   934  C  CD    . LYS   A 1 120 ? 20.601  12.558  32.687  1.00 17.76 ? 117 LYS   A CD    1 
ATOM   935  C  CE    . LYS   A 1 120 ? 21.070  11.878  33.946  1.00 17.24 ? 117 LYS   A CE    1 
ATOM   936  N  NZ    . LYS   A 1 120 ? 22.501  11.555  33.853  1.00 17.93 ? 117 LYS   A NZ    1 
ATOM   937  N  N     . SER   A 1 121 ? 15.246  14.805  30.354  1.00 18.26 ? 118 SER   A N     1 
ATOM   938  C  CA    . SER   A 1 121 ? 14.522  15.370  29.190  1.00 19.23 ? 118 SER   A CA    1 
ATOM   939  C  C     . SER   A 1 121 ? 14.955  16.813  28.904  1.00 20.34 ? 118 SER   A C     1 
ATOM   940  O  O     . SER   A 1 121 ? 14.599  17.264  27.857  1.00 21.06 ? 118 SER   A O     1 
ATOM   941  C  CB    . SER   A 1 121 ? 13.032  15.287  29.354  1.00 18.82 ? 118 SER   A CB    1 
ATOM   942  O  OG    . SER   A 1 121 ? 12.640  16.094  30.423  1.00 18.51 ? 118 SER   A OG    1 
ATOM   943  N  N     . ASP   A 1 122 ? 15.522  17.512  29.881  1.00 20.38 ? 119 ASP   A N     1 
ATOM   944  C  CA    . ASP   A 1 122 ? 16.085  18.857  29.668  1.00 21.74 ? 119 ASP   A CA    1 
ATOM   945  C  C     . ASP   A 1 122 ? 17.304  18.852  28.732  1.00 23.03 ? 119 ASP   A C     1 
ATOM   946  O  O     . ASP   A 1 122 ? 17.656  19.893  28.218  1.00 24.23 ? 119 ASP   A O     1 
ATOM   947  C  CB    . ASP   A 1 122 ? 16.567  19.475  30.983  1.00 21.44 ? 119 ASP   A CB    1 
ATOM   948  C  CG    . ASP   A 1 122 ? 17.590  18.591  31.684  1.00 20.76 ? 119 ASP   A CG    1 
ATOM   949  O  OD1   . ASP   A 1 122 ? 17.170  17.566  32.223  1.00 19.73 ? 119 ASP   A OD1   1 
ATOM   950  O  OD2   . ASP   A 1 122 ? 18.807  18.908  31.649  1.00 21.34 ? 119 ASP   A OD2   1 
ATOM   951  N  N     . LEU   A 1 123 ? 17.965  17.708  28.554  1.00 23.18 ? 120 LEU   A N     1 
ATOM   952  C  CA    . LEU   A 1 123 ? 19.240  17.669  27.847  1.00 24.77 ? 120 LEU   A CA    1 
ATOM   953  C  C     . LEU   A 1 123 ? 19.009  17.662  26.349  1.00 26.16 ? 120 LEU   A C     1 
ATOM   954  O  O     . LEU   A 1 123 ? 18.309  16.793  25.848  1.00 26.09 ? 120 LEU   A O     1 
ATOM   955  C  CB    . LEU   A 1 123 ? 20.028  16.422  28.236  1.00 24.41 ? 120 LEU   A CB    1 
ATOM   956  C  CG    . LEU   A 1 123 ? 20.583  16.383  29.659  1.00 23.94 ? 120 LEU   A CG    1 
ATOM   957  C  CD1   . LEU   A 1 123 ? 21.444  15.139  29.829  1.00 23.69 ? 120 LEU   A CD1   1 
ATOM   958  C  CD2   . LEU   A 1 123 ? 21.399  17.632  29.969  1.00 24.94 ? 120 LEU   A CD2   1 
ATOM   959  N  N     . PRO   A 1 124 ? 19.659  18.558  25.585  1.00 28.01 ? 121 PRO   A N     1 
ATOM   960  C  CA    . PRO   A 1 124 ? 19.410  18.622  24.147  1.00 29.34 ? 121 PRO   A CA    1 
ATOM   961  C  C     . PRO   A 1 124 ? 19.940  17.405  23.360  1.00 29.73 ? 121 PRO   A C     1 
ATOM   962  O  O     . PRO   A 1 124 ? 19.372  17.073  22.333  1.00 30.72 ? 121 PRO   A O     1 
ATOM   963  C  CB    . PRO   A 1 124 ? 20.133  19.906  23.737  1.00 30.75 ? 121 PRO   A CB    1 
ATOM   964  C  CG    . PRO   A 1 124 ? 21.279  20.011  24.713  1.00 30.63 ? 121 PRO   A CG    1 
ATOM   965  C  CD    . PRO   A 1 124 ? 20.735  19.474  26.016  1.00 28.99 ? 121 PRO   A CD    1 
ATOM   966  N  N     . SER   A 1 125 ? 20.957  16.720  23.844  1.00 29.43 ? 122 SER   A N     1 
ATOM   967  C  CA    . SER   A 1 125 ? 21.567  15.620  23.055  1.00 29.80 ? 122 SER   A CA    1 
ATOM   968  C  C     . SER   A 1 125 ? 21.012  14.215  23.371  1.00 28.54 ? 122 SER   A C     1 
ATOM   969  O  O     . SER   A 1 125 ? 21.761  13.425  23.910  1.00 28.49 ? 122 SER   A O     1 
ATOM   970  C  CB    . SER   A 1 125 ? 23.079  15.627  23.261  1.00 30.51 ? 122 SER   A CB    1 
ATOM   971  O  OG    . SER   A 1 125 ? 23.680  16.888  22.981  1.00 31.97 ? 122 SER   A OG    1 
ATOM   972  N  N     . ARG   A 1 126 ? 19.833  13.845  22.900  1.00 28.02 ? 123 ARG   A N     1 
ATOM   973  C  CA    . ARG   A 1 126 ? 19.252  12.507  23.216  1.00 26.75 ? 123 ARG   A CA    1 
ATOM   974  C  C     . ARG   A 1 126 ? 19.898  11.389  22.393  1.00 26.80 ? 123 ARG   A C     1 
ATOM   975  O  O     . ARG   A 1 126 ? 20.178  11.603  21.239  1.00 27.83 ? 123 ARG   A O     1 
ATOM   976  C  CB    . ARG   A 1 126 ? 17.781  12.478  22.806  1.00 26.88 ? 123 ARG   A CB    1 
ATOM   977  C  CG    . ARG   A 1 126 ? 16.972  13.697  23.205  1.00 27.18 ? 123 ARG   A CG    1 
ATOM   978  C  CD    . ARG   A 1 126 ? 15.530  13.568  22.742  1.00 27.29 ? 123 ARG   A CD    1 
ATOM   979  N  NE    . ARG   A 1 126 ? 15.047  12.251  23.065  1.00 26.70 ? 123 ARG   A NE    1 
ATOM   980  C  CZ    . ARG   A 1 126 ? 14.019  12.018  23.851  1.00 25.97 ? 123 ARG   A CZ    1 
ATOM   981  N  NH1   . ARG   A 1 126 ? 13.669  10.781  24.102  1.00 25.42 ? 123 ARG   A NH1   1 
ATOM   982  N  NH2   . ARG   A 1 126 ? 13.383  13.023  24.401  1.00 25.79 ? 123 ARG   A NH2   1 
ATOM   983  N  N     . THR   A 1 127 ? 20.014  10.206  22.973  1.00 25.57 ? 124 THR   A N     1 
ATOM   984  C  CA    . THR   A 1 127 ? 20.507  9.013   22.261  1.00 25.95 ? 124 THR   A CA    1 
ATOM   985  C  C     . THR   A 1 127 ? 19.426  7.938   22.165  1.00 25.11 ? 124 THR   A C     1 
ATOM   986  O  O     . THR   A 1 127 ? 19.561  7.066   21.336  1.00 25.67 ? 124 THR   A O     1 
ATOM   987  C  CB    . THR   A 1 127 ? 21.805  8.494   22.885  1.00 26.15 ? 124 THR   A CB    1 
ATOM   988  O  OG1   . THR   A 1 127 ? 21.517  8.185   24.243  1.00 24.89 ? 124 THR   A OG1   1 
ATOM   989  C  CG2   . THR   A 1 127 ? 22.913  9.516   22.772  1.00 27.12 ? 124 THR   A CG2   1 
ATOM   990  N  N     . VAL   A 1 128 ? 18.412  8.014   23.028  1.00 23.71 ? 125 VAL   A N     1 
ATOM   991  C  CA    . VAL   A 1 128 ? 17.278  7.052   23.006  1.00 23.19 ? 125 VAL   A CA    1 
ATOM   992  C  C     . VAL   A 1 128 ? 16.059  7.777   22.441  1.00 23.48 ? 125 VAL   A C     1 
ATOM   993  O  O     . VAL   A 1 128 ? 15.593  8.705   23.058  1.00 22.84 ? 125 VAL   A O     1 
ATOM   994  C  CB    . VAL   A 1 128 ? 16.974  6.499   24.409  1.00 21.87 ? 125 VAL   A CB    1 
ATOM   995  C  CG1   . VAL   A 1 128 ? 15.841  5.506   24.375  1.00 21.45 ? 125 VAL   A CG1   1 
ATOM   996  C  CG2   . VAL   A 1 128 ? 18.212  5.866   25.009  1.00 21.73 ? 125 VAL   A CG2   1 
ATOM   997  N  N     . ASP   A 1 129 ? 15.570  7.333   21.280  1.00 24.55 ? 126 ASP   A N     1 
ATOM   998  C  CA    . ASP   A 1 129 ? 14.381  7.867   20.546  1.00 25.31 ? 126 ASP   A CA    1 
ATOM   999  C  C     . ASP   A 1 129 ? 13.140  7.673   21.439  1.00 23.99 ? 126 ASP   A C     1 
ATOM   1000 O  O     . ASP   A 1 129 ? 13.023  6.609   22.007  1.00 23.35 ? 126 ASP   A O     1 
ATOM   1001 C  CB    . ASP   A 1 129 ? 14.150  7.045   19.254  1.00 26.99 ? 126 ASP   A CB    1 
ATOM   1002 C  CG    . ASP   A 1 129 ? 13.744  7.748   17.957  1.00 28.81 ? 126 ASP   A CG    1 
ATOM   1003 O  OD1   . ASP   A 1 129 ? 13.305  8.871   18.000  1.00 29.52 ? 126 ASP   A OD1   1 
ATOM   1004 O  OD2   . ASP   A 1 129 ? 13.845  7.152   16.902  1.00 30.24 ? 126 ASP   A OD2   1 
ATOM   1005 N  N     . THR   A 1 130 ? 12.272  8.685   21.545  1.00 23.64 ? 127 THR   A N     1 
ATOM   1006 C  CA    . THR   A 1 130 ? 11.014  8.591   22.307  1.00 22.72 ? 127 THR   A CA    1 
ATOM   1007 C  C     . THR   A 1 130 ? 10.146  7.437   21.806  1.00 22.93 ? 127 THR   A C     1 
ATOM   1008 O  O     . THR   A 1 130 ? 9.656   6.695   22.603  1.00 22.30 ? 127 THR   A O     1 
ATOM   1009 C  CB    . THR   A 1 130 ? 10.268  9.918   22.262  1.00 22.99 ? 127 THR   A CB    1 
ATOM   1010 O  OG1   . THR   A 1 130 ? 11.083  10.954  22.785  1.00 22.74 ? 127 THR   A OG1   1 
ATOM   1011 C  CG2   . THR   A 1 130 ? 8.955   9.866   23.014  1.00 22.30 ? 127 THR   A CG2   1 
ATOM   1012 N  N     . LYS   A 1 131 ? 9.984   7.320   20.505  1.00 23.97 ? 128 LYS   A N     1 
ATOM   1013 C  CA    . LYS   A 1 131 ? 9.157   6.230   19.962  1.00 24.37 ? 128 LYS   A CA    1 
ATOM   1014 C  C     . LYS   A 1 131 ? 9.633   4.853   20.422  1.00 23.96 ? 128 LYS   A C     1 
ATOM   1015 O  O     . LYS   A 1 131 ? 8.810   4.005   20.691  1.00 23.55 ? 128 LYS   A O     1 
ATOM   1016 C  CB    . LYS   A 1 131 ? 9.185   6.239   18.442  1.00 25.85 ? 128 LYS   A CB    1 
ATOM   1017 C  CG    . LYS   A 1 131 ? 8.078   5.370   17.885  1.00 26.59 ? 128 LYS   A CG    1 
ATOM   1018 C  CD    . LYS   A 1 131 ? 8.112   5.077   16.434  1.00 28.23 ? 128 LYS   A CD    1 
ATOM   1019 C  CE    . LYS   A 1 131 ? 7.568   3.700   16.139  1.00 28.76 ? 128 LYS   A CE    1 
ATOM   1020 N  NZ    . LYS   A 1 131 ? 6.251   3.513   16.755  1.00 28.52 ? 128 LYS   A NZ    1 
ATOM   1021 N  N     . GLN   A 1 132 ? 10.957  4.673   20.475  1.00 23.94 ? 129 GLN   A N     1 
ATOM   1022 C  CA    . GLN   A 1 132 ? 11.543  3.404   20.858  1.00 23.88 ? 129 GLN   A CA    1 
ATOM   1023 C  C     . GLN   A 1 132 ? 11.183  3.090   22.318  1.00 22.43 ? 129 GLN   A C     1 
ATOM   1024 O  O     . GLN   A 1 132 ? 10.790  1.967   22.633  1.00 22.21 ? 129 GLN   A O     1 
ATOM   1025 C  CB    . GLN   A 1 132 ? 13.067  3.433   20.688  1.00 24.54 ? 129 GLN   A CB    1 
ATOM   1026 C  CG    . GLN   A 1 132 ? 13.713  2.056   20.815  1.00 25.09 ? 129 GLN   A CG    1 
ATOM   1027 C  CD    . GLN   A 1 132 ? 15.227  2.068   20.724  1.00 25.77 ? 129 GLN   A CD    1 
ATOM   1028 O  OE1   . GLN   A 1 132 ? 15.853  3.088   20.427  1.00 26.45 ? 129 GLN   A OE1   1 
ATOM   1029 N  NE2   . GLN   A 1 132 ? 15.823  0.912   20.983  1.00 26.20 ? 129 GLN   A NE2   1 
ATOM   1030 N  N     . ALA   A 1 133 ? 11.330  4.092   23.190  1.00 21.41 ? 130 ALA   A N     1 
ATOM   1031 C  CA    . ALA   A 1 133 ? 10.952  3.970   24.590  1.00 20.36 ? 130 ALA   A CA    1 
ATOM   1032 C  C     . ALA   A 1 133 ? 9.434   3.755   24.719  1.00 20.26 ? 130 ALA   A C     1 
ATOM   1033 O  O     . ALA   A 1 133 ? 9.006   2.920   25.510  1.00 19.69 ? 130 ALA   A O     1 
ATOM   1034 C  CB    . ALA   A 1 133 ? 11.396  5.185   25.358  1.00 19.85 ? 130 ALA   A CB    1 
ATOM   1035 N  N     . GLN   A 1 134 ? 8.635   4.497   23.939  1.00 20.75 ? 131 GLN   A N     1 
ATOM   1036 C  CA    . GLN   A 1 134 ? 7.169   4.364   23.984  1.00 21.07 ? 131 GLN   A CA    1 
ATOM   1037 C  C     . GLN   A 1 134 ? 6.761   2.942   23.558  1.00 21.61 ? 131 GLN   A C     1 
ATOM   1038 O  O     . GLN   A 1 134 ? 5.906   2.328   24.183  1.00 21.41 ? 131 GLN   A O     1 
ATOM   1039 C  CB    . GLN   A 1 134 ? 6.491   5.412   23.084  1.00 21.95 ? 131 GLN   A CB    1 
ATOM   1040 C  CG    . GLN   A 1 134 ? 4.964   5.412   23.156  1.00 22.37 ? 131 GLN   A CG    1 
ATOM   1041 C  CD    . GLN   A 1 134 ? 4.479   5.802   24.527  1.00 21.74 ? 131 GLN   A CD    1 
ATOM   1042 O  OE1   . GLN   A 1 134 ? 4.087   4.950   25.329  1.00 21.63 ? 131 GLN   A OE1   1 
ATOM   1043 N  NE2   . GLN   A 1 134 ? 4.599   7.078   24.841  1.00 21.54 ? 131 GLN   A NE2   1 
ATOM   1044 N  N     . ASP   A 1 135 ? 7.390   2.435   22.493  1.00 22.35 ? 132 ASP   A N     1 
ATOM   1045 C  CA    . ASP   A 1 135 ? 7.128   1.093   21.973  1.00 23.13 ? 132 ASP   A CA    1 
ATOM   1046 C  C     . ASP   A 1 135 ? 7.407   0.044   23.059  1.00 22.50 ? 132 ASP   A C     1 
ATOM   1047 O  O     . ASP   A 1 135 ? 6.605   -0.875  23.228  1.00 22.88 ? 132 ASP   A O     1 
ATOM   1048 C  CB    . ASP   A 1 135 ? 7.932   0.813   20.696  1.00 24.16 ? 132 ASP   A CB    1 
ATOM   1049 C  CG    . ASP   A 1 135 ? 7.439   1.554   19.462  1.00 25.31 ? 132 ASP   A CG    1 
ATOM   1050 O  OD1   . ASP   A 1 135 ? 6.335   2.164   19.523  1.00 25.41 ? 132 ASP   A OD1   1 
ATOM   1051 O  OD2   . ASP   A 1 135 ? 8.147   1.508   18.427  1.00 26.22 ? 132 ASP   A OD2   1 
ATOM   1052 N  N     . LEU   A 1 136 ? 8.536   0.170   23.767  1.00 21.81 ? 133 LEU   A N     1 
ATOM   1053 C  CA    . LEU   A 1 136 ? 8.881   -0.771  24.826  1.00 21.39 ? 133 LEU   A CA    1 
ATOM   1054 C  C     . LEU   A 1 136 ? 7.783   -0.783  25.893  1.00 20.91 ? 133 LEU   A C     1 
ATOM   1055 O  O     . LEU   A 1 136 ? 7.294   -1.847  26.280  1.00 21.02 ? 133 LEU   A O     1 
ATOM   1056 C  CB    . LEU   A 1 136 ? 10.224  -0.402  25.466  1.00 20.83 ? 133 LEU   A CB    1 
ATOM   1057 C  CG    . LEU   A 1 136 ? 10.784  -1.461  26.413  1.00 20.51 ? 133 LEU   A CG    1 
ATOM   1058 C  CD1   . LEU   A 1 136 ? 11.327  -2.643  25.621  1.00 21.56 ? 133 LEU   A CD1   1 
ATOM   1059 C  CD2   . LEU   A 1 136 ? 11.842  -0.869  27.332  1.00 19.74 ? 133 LEU   A CD2   1 
ATOM   1060 N  N     . ALA   A 1 137 ? 7.430   0.406   26.384  1.00 20.45 ? 134 ALA   A N     1 
ATOM   1061 C  CA    . ALA   A 1 137 ? 6.355   0.564   27.378  1.00 20.29 ? 134 ALA   A CA    1 
ATOM   1062 C  C     . ALA   A 1 137 ? 5.069   -0.138  26.920  1.00 21.32 ? 134 ALA   A C     1 
ATOM   1063 O  O     . ALA   A 1 137 ? 4.412   -0.823  27.710  1.00 21.11 ? 134 ALA   A O     1 
ATOM   1064 C  CB    . ALA   A 1 137 ? 6.096   2.028   27.637  1.00 19.87 ? 134 ALA   A CB    1 
ATOM   1065 N  N     . ARG   A 1 138 ? 4.725   0.030   25.645  1.00 22.60 ? 135 ARG   A N     1 
ATOM   1066 C  CA    . ARG   A 1 138 ? 3.555   -0.600  25.067  1.00 24.14 ? 135 ARG   A CA    1 
ATOM   1067 C  C     . ARG   A 1 138 ? 3.657   -2.121  25.208  1.00 24.24 ? 135 ARG   A C     1 
ATOM   1068 O  O     . ARG   A 1 138 ? 2.688   -2.753  25.632  1.00 24.49 ? 135 ARG   A O     1 
ATOM   1069 C  CB    . ARG   A 1 138 ? 3.385   -0.238  23.589  1.00 25.94 ? 135 ARG   A CB    1 
ATOM   1070 C  CG    . ARG   A 1 138 ? 2.658   1.075   23.338  1.00 26.97 ? 135 ARG   A CG    1 
ATOM   1071 C  CD    . ARG   A 1 138 ? 2.250   1.184   21.884  1.00 29.08 ? 135 ARG   A CD    1 
ATOM   1072 N  NE    . ARG   A 1 138 ? 2.501   2.534   21.404  1.00 30.20 ? 135 ARG   A NE    1 
ATOM   1073 C  CZ    . ARG   A 1 138 ? 1.674   3.567   21.553  1.00 31.03 ? 135 ARG   A CZ    1 
ATOM   1074 N  NH1   . ARG   A 1 138 ? 0.445   3.362   22.005  1.00 32.06 ? 135 ARG   A NH1   1 
ATOM   1075 N  NH2   . ARG   A 1 138 ? 2.062   4.792   21.206  1.00 31.28 ? 135 ARG   A NH2   1 
ATOM   1076 N  N     . SER   A 1 139 ? 4.819   -2.683  24.854  1.00 24.06 ? 136 SER   A N     1 
ATOM   1077 C  CA    . SER   A 1 139 ? 5.078   -4.143  24.906  1.00 24.36 ? 136 SER   A CA    1 
ATOM   1078 C  C     . SER   A 1 139 ? 4.948   -4.671  26.337  1.00 23.57 ? 136 SER   A C     1 
ATOM   1079 O  O     . SER   A 1 139 ? 4.422   -5.779  26.538  1.00 24.17 ? 136 SER   A O     1 
ATOM   1080 C  CB    . SER   A 1 139 ? 6.423   -4.512  24.305  1.00 24.61 ? 136 SER   A CB    1 
ATOM   1081 O  OG    . SER   A 1 139 ? 7.502   -4.115  25.138  1.00 23.70 ? 136 SER   A OG    1 
ATOM   1082 N  N     . TYR   A 1 140 ? 5.370   -3.871  27.314  1.00 21.99 ? 137 TYR   A N     1 
ATOM   1083 C  CA    . TYR   A 1 140 ? 5.237   -4.225  28.725  1.00 21.38 ? 137 TYR   A CA    1 
ATOM   1084 C  C     . TYR   A 1 140 ? 3.828   -3.933  29.282  1.00 21.33 ? 137 TYR   A C     1 
ATOM   1085 O  O     . TYR   A 1 140 ? 3.491   -4.399  30.373  1.00 21.37 ? 137 TYR   A O     1 
ATOM   1086 C  CB    . TYR   A 1 140 ? 6.238   -3.449  29.583  1.00 20.25 ? 137 TYR   A CB    1 
ATOM   1087 C  CG    . TYR   A 1 140 ? 7.703   -3.684  29.315  1.00 20.24 ? 137 TYR   A CG    1 
ATOM   1088 C  CD1   . TYR   A 1 140 ? 8.166   -4.816  28.661  1.00 21.01 ? 137 TYR   A CD1   1 
ATOM   1089 C  CD2   . TYR   A 1 140 ? 8.635   -2.750  29.739  1.00 19.39 ? 137 TYR   A CD2   1 
ATOM   1090 C  CE1   . TYR   A 1 140 ? 9.515   -4.998  28.412  1.00 21.10 ? 137 TYR   A CE1   1 
ATOM   1091 C  CE2   . TYR   A 1 140 ? 9.991   -2.928  29.511  1.00 19.53 ? 137 TYR   A CE2   1 
ATOM   1092 C  CZ    . TYR   A 1 140 ? 10.428  -4.052  28.839  1.00 20.39 ? 137 TYR   A CZ    1 
ATOM   1093 O  OH    . TYR   A 1 140 ? 11.762  -4.245  28.633  1.00 20.64 ? 137 TYR   A OH    1 
ATOM   1094 N  N     . GLY   A 1 141 ? 3.036   -3.116  28.588  1.00 21.31 ? 138 GLY   A N     1 
ATOM   1095 C  CA    . GLY   A 1 141 ? 1.694   -2.759  29.038  1.00 21.31 ? 138 GLY   A CA    1 
ATOM   1096 C  C     . GLY   A 1 141 ? 1.717   -1.743  30.171  1.00 20.22 ? 138 GLY   A C     1 
ATOM   1097 O  O     . GLY   A 1 141 ? 0.799   -1.726  30.994  1.00 20.41 ? 138 GLY   A O     1 
ATOM   1098 N  N     . ILE   A 1 142 ? 2.733   -0.878  30.164  1.00 19.12 ? 139 ILE   A N     1 
ATOM   1099 C  CA    . ILE   A 1 142 ? 2.884   0.132   31.242  1.00 18.11 ? 139 ILE   A CA    1 
ATOM   1100 C  C     . ILE   A 1 142 ? 3.015   1.555   30.690  1.00 17.70 ? 139 ILE   A C     1 
ATOM   1101 O  O     . ILE   A 1 142 ? 3.388   1.730   29.573  1.00 18.02 ? 139 ILE   A O     1 
ATOM   1102 C  CB    . ILE   A 1 142 ? 4.117   -0.213  32.097  1.00 17.47 ? 139 ILE   A CB    1 
ATOM   1103 C  CG1   . ILE   A 1 142 ? 5.384   0.015   31.287  1.00 17.43 ? 139 ILE   A CG1   1 
ATOM   1104 C  CG2   . ILE   A 1 142 ? 4.055   -1.628  32.631  1.00 17.85 ? 139 ILE   A CG2   1 
ATOM   1105 C  CD1   . ILE   A 1 142 ? 6.684   -0.336  32.033  1.00 16.94 ? 139 ILE   A CD1   1 
ATOM   1106 N  N     . PRO   A 1 143 ? 2.804   2.586   31.521  1.00 17.00 ? 140 PRO   A N     1 
ATOM   1107 C  CA    . PRO   A 1 143 ? 2.980   3.954   31.114  1.00 16.96 ? 140 PRO   A CA    1 
ATOM   1108 C  C     . PRO   A 1 143 ? 4.481   4.274   30.945  1.00 16.50 ? 140 PRO   A C     1 
ATOM   1109 O  O     . PRO   A 1 143 ? 5.272   3.661   31.533  1.00 16.03 ? 140 PRO   A O     1 
ATOM   1110 C  CB    . PRO   A 1 143 ? 2.360   4.819   32.225  1.00 16.64 ? 140 PRO   A CB    1 
ATOM   1111 C  CG    . PRO   A 1 143 ? 1.682   3.845   33.132  1.00 16.70 ? 140 PRO   A CG    1 
ATOM   1112 C  CD    . PRO   A 1 143 ? 2.320   2.505   32.863  1.00 16.72 ? 140 PRO   A CD    1 
ATOM   1113 N  N     . PHE   A 1 144 ? 4.730   5.254   30.106  1.00 16.80 ? 141 PHE   A N     1 
ATOM   1114 C  CA    . PHE   A 1 144 ? 6.047   5.834   29.777  1.00 16.63 ? 141 PHE   A CA    1 
ATOM   1115 C  C     . PHE   A 1 144 ? 5.969   7.339   30.016  1.00 16.63 ? 141 PHE   A C     1 
ATOM   1116 O  O     . PHE   A 1 144 ? 5.104   8.009   29.478  1.00 16.98 ? 141 PHE   A O     1 
ATOM   1117 C  CB    . PHE   A 1 144 ? 6.411   5.530   28.333  1.00 17.34 ? 141 PHE   A CB    1 
ATOM   1118 C  CG    . PHE   A 1 144 ? 7.638   6.252   27.869  1.00 17.41 ? 141 PHE   A CG    1 
ATOM   1119 C  CD1   . PHE   A 1 144 ? 8.771   6.266   28.666  1.00 16.81 ? 141 PHE   A CD1   1 
ATOM   1120 C  CD2   . PHE   A 1 144 ? 7.671   6.918   26.665  1.00 18.14 ? 141 PHE   A CD2   1 
ATOM   1121 C  CE1   . PHE   A 1 144 ? 9.900   6.951   28.260  1.00 17.09 ? 141 PHE   A CE1   1 
ATOM   1122 C  CE2   . PHE   A 1 144 ? 8.810   7.584   26.254  1.00 18.34 ? 141 PHE   A CE2   1 
ATOM   1123 C  CZ    . PHE   A 1 144 ? 9.917   7.603   27.051  1.00 17.82 ? 141 PHE   A CZ    1 
ATOM   1124 N  N     . ILE   A 1 145 ? 6.874   7.853   30.829  1.00 16.24 ? 142 ILE   A N     1 
ATOM   1125 C  CA    . ILE   A 1 145 ? 6.920   9.303   31.122  1.00 16.49 ? 142 ILE   A CA    1 
ATOM   1126 C  C     . ILE   A 1 145 ? 8.358   9.769   30.895  1.00 16.46 ? 142 ILE   A C     1 
ATOM   1127 O  O     . ILE   A 1 145 ? 9.224   9.071   31.320  1.00 16.03 ? 142 ILE   A O     1 
ATOM   1128 C  CB    . ILE   A 1 145 ? 6.512   9.608   32.572  1.00 16.15 ? 142 ILE   A CB    1 
ATOM   1129 C  CG1   . ILE   A 1 145 ? 5.250   8.880   33.051  1.00 16.56 ? 142 ILE   A CG1   1 
ATOM   1130 C  CG2   . ILE   A 1 145 ? 6.437   11.089  32.820  1.00 16.39 ? 142 ILE   A CG2   1 
ATOM   1131 C  CD1   . ILE   A 1 145 ? 3.994   9.443   32.495  1.00 17.43 ? 142 ILE   A CD1   1 
ATOM   1132 N  N     . GLU   A 1 146 ? 8.498   10.899  30.235  1.00 17.06 ? 143 GLU   A N     1 
ATOM   1133 C  CA    . GLU   A 1 146 ? 9.823   11.542  30.075  1.00 17.33 ? 143 GLU   A CA    1 
ATOM   1134 C  C     . GLU   A 1 146 ? 9.898   12.615  31.171  1.00 17.02 ? 143 GLU   A C     1 
ATOM   1135 O  O     . GLU   A 1 146 ? 8.995   13.422  31.247  1.00 17.19 ? 143 GLU   A O     1 
ATOM   1136 C  CB    . GLU   A 1 146 ? 10.026  12.053  28.650  1.00 18.43 ? 143 GLU   A CB    1 
ATOM   1137 C  CG    . GLU   A 1 146 ? 10.476  10.991  27.685  1.00 18.93 ? 143 GLU   A CG    1 
ATOM   1138 C  CD    . GLU   A 1 146 ? 11.001  11.430  26.326  1.00 20.08 ? 143 GLU   A CD    1 
ATOM   1139 O  OE1   . GLU   A 1 146 ? 11.244  12.582  26.136  1.00 20.74 ? 143 GLU   A OE1   1 
ATOM   1140 O  OE2   . GLU   A 1 146 ? 11.141  10.607  25.490  1.00 20.67 ? 143 GLU   A OE2   1 
ATOM   1141 N  N     . THR   A 1 147 ? 10.971  12.625  31.970  1.00 16.59 ? 144 THR   A N     1 
ATOM   1142 C  CA    . THR   A 1 147 ? 11.086  13.565  33.106  1.00 16.24 ? 144 THR   A CA    1 
ATOM   1143 C  C     . THR   A 1 147 ? 12.451  14.283  33.139  1.00 16.45 ? 144 THR   A C     1 
ATOM   1144 O  O     . THR   A 1 147 ? 13.320  13.910  32.415  1.00 16.44 ? 144 THR   A O     1 
ATOM   1145 C  CB    . THR   A 1 147 ? 11.086  12.810  34.439  1.00 15.63 ? 144 THR   A CB    1 
ATOM   1146 O  OG1   . THR   A 1 147 ? 12.196  11.914  34.411  1.00 15.37 ? 144 THR   A OG1   1 
ATOM   1147 C  CG2   . THR   A 1 147 ? 9.812   12.051  34.757  1.00 15.37 ? 144 THR   A CG2   1 
ATOM   1148 N  N     . SER   A 1 148 ? 12.491  15.356  33.920  1.00 16.57 ? 145 SER   A N     1 
ATOM   1149 C  CA    . SER   A 1 148 ? 13.741  16.106  34.204  1.00 16.87 ? 145 SER   A CA    1 
ATOM   1150 C  C     . SER   A 1 148 ? 13.786  16.430  35.683  1.00 16.56 ? 145 SER   A C     1 
ATOM   1151 O  O     . SER   A 1 148 ? 13.101  17.267  36.086  1.00 16.64 ? 145 SER   A O     1 
ATOM   1152 C  CB    . SER   A 1 148 ? 13.911  17.344  33.409  1.00 17.81 ? 145 SER   A CB    1 
ATOM   1153 O  OG    . SER   A 1 148 ? 14.998  18.126  33.882  1.00 18.32 ? 145 SER   A OG    1 
ATOM   1154 N  N     . ALA   A 1 149 ? 14.593  15.702  36.419  1.00 16.08 ? 146 ALA   A N     1 
ATOM   1155 C  CA    . ALA   A 1 149 ? 14.835  16.021  37.809  1.00 16.02 ? 146 ALA   A CA    1 
ATOM   1156 C  C     . ALA   A 1 149 ? 15.372  17.450  37.943  1.00 17.08 ? 146 ALA   A C     1 
ATOM   1157 O  O     . ALA   A 1 149 ? 15.177  18.078  38.984  1.00 17.08 ? 146 ALA   A O     1 
ATOM   1158 C  CB    . ALA   A 1 149 ? 15.789  15.012  38.422  1.00 15.54 ? 146 ALA   A CB    1 
ATOM   1159 N  N     . LYS   A 1 150 ? 16.094  17.921  36.920  1.00 18.26 ? 147 LYS   A N     1 
ATOM   1160 C  CA    . LYS   A 1 150 ? 16.694  19.249  36.938  1.00 19.65 ? 147 LYS   A CA    1 
ATOM   1161 C  C     . LYS   A 1 150 ? 15.645  20.369  36.870  1.00 20.36 ? 147 LYS   A C     1 
ATOM   1162 O  O     . LYS   A 1 150 ? 15.710  21.306  37.656  1.00 20.65 ? 147 LYS   A O     1 
ATOM   1163 C  CB    . LYS   A 1 150 ? 17.708  19.422  35.812  1.00 20.68 ? 147 LYS   A CB    1 
ATOM   1164 C  CG    . LYS   A 1 150 ? 18.501  20.716  35.906  1.00 21.91 ? 147 LYS   A CG    1 
ATOM   1165 C  CD    . LYS   A 1 150 ? 19.529  20.821  34.841  1.00 23.09 ? 147 LYS   A CD    1 
ATOM   1166 C  CE    . LYS   A 1 150 ? 20.082  22.223  34.754  1.00 24.53 ? 147 LYS   A CE    1 
ATOM   1167 N  NZ    . LYS   A 1 150 ? 21.422  22.191  34.142  1.00 25.51 ? 147 LYS   A NZ    1 
ATOM   1168 N  N     . THR   A 1 151 ? 14.698  20.256  35.948  1.00 20.76 ? 148 THR   A N     1 
ATOM   1169 C  CA    . THR   A 1 151 ? 13.737  21.356  35.794  1.00 21.74 ? 148 THR   A CA    1 
ATOM   1170 C  C     . THR   A 1 151 ? 12.385  21.009  36.427  1.00 21.37 ? 148 THR   A C     1 
ATOM   1171 O  O     . THR   A 1 151 ? 11.530  21.785  36.244  1.00 22.14 ? 148 THR   A O     1 
ATOM   1172 C  CB    . THR   A 1 151 ? 13.545  21.676  34.311  1.00 22.72 ? 148 THR   A CB    1 
ATOM   1173 O  OG1   . THR   A 1 151 ? 13.065  20.489  33.708  1.00 22.42 ? 148 THR   A OG1   1 
ATOM   1174 C  CG2   . THR   A 1 151 ? 14.836  21.965  33.595  1.00 23.47 ? 148 THR   A CG2   1 
ATOM   1175 N  N     . ARG   A 1 152 ? 12.235  19.815  36.992  1.00 20.82 ? 149 ARG   A N     1 
ATOM   1176 C  CA    . ARG   A 1 152 ? 11.017  19.293  37.684  1.00 20.53 ? 149 ARG   A CA    1 
ATOM   1177 C  C     . ARG   A 1 152 ? 9.957   18.806  36.669  1.00 20.50 ? 149 ARG   A C     1 
ATOM   1178 O  O     . ARG   A 1 152 ? 8.989   18.254  37.127  1.00 20.25 ? 149 ARG   A O     1 
ATOM   1179 C  CB    . ARG   A 1 152 ? 10.552  20.235  38.811  1.00 21.39 ? 149 ARG   A CB    1 
ATOM   1180 C  CG    . ARG   A 1 152 ? 9.237   19.935  39.493  1.00 21.78 ? 149 ARG   A CG    1 
ATOM   1181 C  CD    . ARG   A 1 152 ? 9.026   20.919  40.610  1.00 22.73 ? 149 ARG   A CD    1 
ATOM   1182 N  NE    . ARG   A 1 152 ? 8.006   20.318  41.421  1.00 22.86 ? 149 ARG   A NE    1 
ATOM   1183 C  CZ    . ARG   A 1 152 ? 8.207   19.489  42.412  1.00 22.47 ? 149 ARG   A CZ    1 
ATOM   1184 N  NH1   . ARG   A 1 152 ? 9.435   19.182  42.775  1.00 22.06 ? 149 ARG   A NH1   1 
ATOM   1185 N  NH2   . ARG   A 1 152 ? 7.191   18.995  43.071  1.00 22.60 ? 149 ARG   A NH2   1 
ATOM   1186 N  N     . GLN   A 1 153 ? 10.233  18.854  35.371  1.00 20.55 ? 150 GLN   A N     1 
ATOM   1187 C  CA    . GLN   A 1 153 ? 9.254   18.440  34.347  1.00 20.84 ? 150 GLN   A CA    1 
ATOM   1188 C  C     . GLN   A 1 153 ? 8.792   17.012  34.598  1.00 19.25 ? 150 GLN   A C     1 
ATOM   1189 O  O     . GLN   A 1 153 ? 9.642   16.155  34.658  1.00 18.39 ? 150 GLN   A O     1 
ATOM   1190 C  CB    . GLN   A 1 153 ? 9.815   18.385  32.933  1.00 21.97 ? 150 GLN   A CB    1 
ATOM   1191 C  CG    . GLN   A 1 153 ? 10.314  19.694  32.382  1.00 23.78 ? 150 GLN   A CG    1 
ATOM   1192 C  CD    . GLN   A 1 153 ? 9.259   20.673  31.969  1.00 25.43 ? 150 GLN   A CD    1 
ATOM   1193 O  OE1   . GLN   A 1 153 ? 8.555   20.421  31.012  1.00 26.82 ? 150 GLN   A OE1   1 
ATOM   1194 N  NE2   . GLN   A 1 153 ? 9.200   21.803  32.653  1.00 26.32 ? 150 GLN   A NE2   1 
ATOM   1195 N  N     . ARG   A 1 154 ? 7.496   16.842  34.825  1.00 18.70 ? 151 ARG   A N     1 
ATOM   1196 C  CA    . ARG   A 1 154 ? 6.849   15.511  34.943  1.00 17.86 ? 151 ARG   A CA    1 
ATOM   1197 C  C     . ARG   A 1 154 ? 7.348   14.680  36.128  1.00 16.89 ? 151 ARG   A C     1 
ATOM   1198 O  O     . ARG   A 1 154 ? 7.027   13.523  36.175  1.00 16.47 ? 151 ARG   A O     1 
ATOM   1199 C  CB    . ARG   A 1 154 ? 6.883   14.826  33.582  1.00 18.23 ? 151 ARG   A CB    1 
ATOM   1200 C  CG    . ARG   A 1 154 ? 6.222   15.719  32.546  1.00 19.45 ? 151 ARG   A CG    1 
ATOM   1201 C  CD    . ARG   A 1 154 ? 6.094   15.465  31.078  1.00 20.31 ? 151 ARG   A CD    1 
ATOM   1202 N  NE    . ARG   A 1 154 ? 5.414   16.636  30.535  0.00 58.00 ? 151 ARG   A NE    1 
ATOM   1203 C  CZ    . ARG   A 1 154 ? 5.653   17.254  29.377  0.00 58.88 ? 151 ARG   A CZ    1 
ATOM   1204 N  NH1   . ARG   A 1 154 ? 6.508   16.774  28.501  0.00 58.94 ? 151 ARG   A NH1   1 
ATOM   1205 N  NH2   . ARG   A 1 154 ? 4.946   18.310  29.058  0.00 59.82 ? 151 ARG   A NH2   1 
ATOM   1206 N  N     . VAL   A 1 155 ? 7.977   15.302  37.110  1.00 16.43 ? 152 VAL   A N     1 
ATOM   1207 C  CA    . VAL   A 1 155 ? 8.490   14.482  38.211  1.00 15.57 ? 152 VAL   A CA    1 
ATOM   1208 C  C     . VAL   A 1 155 ? 7.331   13.945  39.073  1.00 15.49 ? 152 VAL   A C     1 
ATOM   1209 O  O     . VAL   A 1 155 ? 7.192   12.725  39.266  1.00 14.89 ? 152 VAL   A O     1 
ATOM   1210 C  CB    . VAL   A 1 155 ? 9.530   15.224  39.062  1.00 15.39 ? 152 VAL   A CB    1 
ATOM   1211 C  CG1   . VAL   A 1 155 ? 9.891   14.408  40.301  1.00 14.70 ? 152 VAL   A CG1   1 
ATOM   1212 C  CG2   . VAL   A 1 155 ? 10.779  15.518  38.228  1.00 15.62 ? 152 VAL   A CG2   1 
ATOM   1213 N  N     . GLU   A 1 156 ? 6.490   14.852  39.565  1.00 15.91 ? 153 GLU   A N     1 
ATOM   1214 C  CA    . GLU   A 1 156 ? 5.246   14.449  40.265  1.00 16.06 ? 153 GLU   A CA    1 
ATOM   1215 C  C     . GLU   A 1 156 ? 4.431   13.463  39.427  1.00 15.91 ? 153 GLU   A C     1 
ATOM   1216 O  O     . GLU   A 1 156 ? 3.954   12.439  39.954  1.00 15.46 ? 153 GLU   A O     1 
ATOM   1217 C  CB    . GLU   A 1 156 ? 4.383   15.671  40.530  1.00 17.11 ? 153 GLU   A CB    1 
ATOM   1218 C  CG    . GLU   A 1 156 ? 4.633   16.338  41.852  1.00 17.61 ? 153 GLU   A CG    1 
ATOM   1219 C  CD    . GLU   A 1 156 ? 3.516   17.291  42.266  1.00 18.62 ? 153 GLU   A CD    1 
ATOM   1220 O  OE1   . GLU   A 1 156 ? 2.519   17.421  41.532  1.00 19.56 ? 153 GLU   A OE1   1 
ATOM   1221 O  OE2   . GLU   A 1 156 ? 3.652   17.912  43.320  1.00 19.31 ? 153 GLU   A OE2   1 
ATOM   1222 N  N     . ASP   A 1 157 ? 4.241   13.808  38.141  1.00 16.23 ? 154 ASP   A N     1 
ATOM   1223 C  CA    . ASP   A 1 157 ? 3.481   12.986  37.209  1.00 16.51 ? 154 ASP   A CA    1 
ATOM   1224 C  C     . ASP   A 1 157 ? 3.990   11.542  37.272  1.00 15.34 ? 154 ASP   A C     1 
ATOM   1225 O  O     . ASP   A 1 157 ? 3.194   10.606  37.355  1.00 15.03 ? 154 ASP   A O     1 
ATOM   1226 C  CB    . ASP   A 1 157 ? 3.528   13.525  35.767  1.00 17.57 ? 154 ASP   A CB    1 
ATOM   1227 C  CG    . ASP   A 1 157 ? 2.626   14.709  35.428  1.00 18.96 ? 154 ASP   A CG    1 
ATOM   1228 O  OD1   . ASP   A 1 157 ? 1.816   15.180  36.304  1.00 19.66 ? 154 ASP   A OD1   1 
ATOM   1229 O  OD2   . ASP   A 1 157 ? 2.659   15.139  34.230  1.00 20.00 ? 154 ASP   A OD2   1 
ATOM   1230 N  N     . ALA   A 1 158 ? 5.328   11.344  37.215  1.00 14.24 ? 155 ALA   A N     1 
ATOM   1231 C  CA    . ALA   A 1 158 ? 5.882   9.988   37.210  1.00 13.65 ? 155 ALA   A CA    1 
ATOM   1232 C  C     . ALA   A 1 158 ? 5.520   9.216   38.487  1.00 13.29 ? 155 ALA   A C     1 
ATOM   1233 O  O     . ALA   A 1 158 ? 5.079   8.065   38.429  1.00 13.34 ? 155 ALA   A O     1 
ATOM   1234 C  CB    . ALA   A 1 158 ? 7.391   10.001  37.029  1.00 13.30 ? 155 ALA   A CB    1 
ATOM   1235 N  N     . PHE   A 1 159 ? 5.710   9.835   39.644  1.00 13.08 ? 156 PHE   A N     1 
ATOM   1236 C  CA    . PHE   A 1 159 ? 5.370   9.143   40.891  1.00 12.90 ? 156 PHE   A CA    1 
ATOM   1237 C  C     . PHE   A 1 159 ? 3.871   8.916   41.005  1.00 13.39 ? 156 PHE   A C     1 
ATOM   1238 O  O     . PHE   A 1 159 ? 3.450   7.848   41.416  1.00 13.43 ? 156 PHE   A O     1 
ATOM   1239 C  CB    . PHE   A 1 159 ? 5.883   9.898   42.114  1.00 12.70 ? 156 PHE   A CB    1 
ATOM   1240 C  CG    . PHE   A 1 159 ? 7.374   9.759   42.264  1.00 12.28 ? 156 PHE   A CG    1 
ATOM   1241 C  CD1   . PHE   A 1 159 ? 7.915   8.683   42.940  1.00 11.99 ? 156 PHE   A CD1   1 
ATOM   1242 C  CD2   . PHE   A 1 159 ? 8.218   10.705  41.715  1.00 12.32 ? 156 PHE   A CD2   1 
ATOM   1243 C  CE1   . PHE   A 1 159 ? 9.298   8.570   43.084  1.00 11.74 ? 156 PHE   A CE1   1 
ATOM   1244 C  CE2   . PHE   A 1 159 ? 9.600   10.584  41.841  1.00 12.09 ? 156 PHE   A CE2   1 
ATOM   1245 C  CZ    . PHE   A 1 159 ? 10.123  9.513   42.527  1.00 11.80 ? 156 PHE   A CZ    1 
ATOM   1246 N  N     . TYR   A 1 160 ? 3.089   9.931   40.643  1.00 14.12 ? 157 TYR   A N     1 
ATOM   1247 C  CA    . TYR   A 1 160 ? 1.642   9.888   40.840  1.00 14.73 ? 157 TYR   A CA    1 
ATOM   1248 C  C     . TYR   A 1 160 ? 1.007   8.855   39.907  1.00 15.00 ? 157 TYR   A C     1 
ATOM   1249 O  O     . TYR   A 1 160 ? 0.093   8.144   40.315  1.00 15.24 ? 157 TYR   A O     1 
ATOM   1250 C  CB    . TYR   A 1 160 ? 1.036   11.271  40.618  1.00 15.59 ? 157 TYR   A CB    1 
ATOM   1251 C  CG    . TYR   A 1 160 ? 1.233   12.247  41.752  1.00 15.85 ? 157 TYR   A CG    1 
ATOM   1252 C  CD1   . TYR   A 1 160 ? 2.161   12.005  42.755  1.00 15.29 ? 157 TYR   A CD1   1 
ATOM   1253 C  CD2   . TYR   A 1 160 ? 0.497   13.426  41.812  1.00 16.79 ? 157 TYR   A CD2   1 
ATOM   1254 C  CE1   . TYR   A 1 160 ? 2.360   12.906  43.783  1.00 15.52 ? 157 TYR   A CE1   1 
ATOM   1255 C  CE2   . TYR   A 1 160 ? 0.705   14.350  42.828  1.00 17.03 ? 157 TYR   A CE2   1 
ATOM   1256 C  CZ    . TYR   A 1 160 ? 1.641   14.079  43.813  1.00 16.41 ? 157 TYR   A CZ    1 
ATOM   1257 O  OH    . TYR   A 1 160 ? 1.869   14.935  44.861  1.00 16.98 ? 157 TYR   A OH    1 
ATOM   1258 N  N     . THR   A 1 161 ? 1.543   8.764   38.683  1.00 14.82 ? 158 THR   A N     1 
ATOM   1259 C  CA    . THR   A 1 161 ? 1.157   7.729   37.723  1.00 15.18 ? 158 THR   A CA    1 
ATOM   1260 C  C     . THR   A 1 161 ? 1.375   6.342   38.328  1.00 14.92 ? 158 THR   A C     1 
ATOM   1261 O  O     . THR   A 1 161 ? 0.533   5.473   38.188  1.00 15.36 ? 158 THR   A O     1 
ATOM   1262 C  CB    . THR   A 1 161 ? 1.900   7.868   36.389  1.00 15.13 ? 158 THR   A CB    1 
ATOM   1263 O  OG1   . THR   A 1 161 ? 1.518   9.129   35.842  1.00 15.67 ? 158 THR   A OG1   1 
ATOM   1264 C  CG2   . THR   A 1 161 ? 1.573   6.763   35.402  1.00 15.57 ? 158 THR   A CG2   1 
ATOM   1265 N  N     . LEU   A 1 162 ? 2.518   6.140   38.979  1.00 14.39 ? 159 LEU   A N     1 
ATOM   1266 C  CA    . LEU   A 1 162 ? 2.854   4.827   39.555  1.00 14.28 ? 159 LEU   A CA    1 
ATOM   1267 C  C     . LEU   A 1 162 ? 1.837   4.506   40.641  1.00 14.64 ? 159 LEU   A C     1 
ATOM   1268 O  O     . LEU   A 1 162 ? 1.291   3.399   40.658  1.00 14.84 ? 159 LEU   A O     1 
ATOM   1269 C  CB    . LEU   A 1 162 ? 4.284   4.814   40.094  1.00 13.69 ? 159 LEU   A CB    1 
ATOM   1270 C  CG    . LEU   A 1 162 ? 4.789   3.499   40.705  1.00 13.60 ? 159 LEU   A CG    1 
ATOM   1271 C  CD1   . LEU   A 1 162 ? 4.838   2.356   39.690  1.00 13.91 ? 159 LEU   A CD1   1 
ATOM   1272 C  CD2   . LEU   A 1 162 ? 6.156   3.728   41.323  1.00 13.12 ? 159 LEU   A CD2   1 
ATOM   1273 N  N     . VAL   A 1 163 ? 1.552   5.508   41.453  1.00 14.75 ? 160 VAL   A N     1 
ATOM   1274 C  CA    . VAL   A 1 163 ? 0.517   5.292   42.510  1.00 15.43 ? 160 VAL   A CA    1 
ATOM   1275 C  C     . VAL   A 1 163 ? -0.809  4.899   41.837  1.00 16.16 ? 160 VAL   A C     1 
ATOM   1276 O  O     . VAL   A 1 163 ? -1.369  3.976   42.280  1.00 16.63 ? 160 VAL   A O     1 
ATOM   1277 C  CB    . VAL   A 1 163 ? 0.306   6.486   43.437  1.00 15.47 ? 160 VAL   A CB    1 
ATOM   1278 C  CG1   . VAL   A 1 163 ? -0.914  6.266   44.333  1.00 16.21 ? 160 VAL   A CG1   1 
ATOM   1279 C  CG2   . VAL   A 1 163 ? 1.542   6.778   44.243  1.00 14.88 ? 160 VAL   A CG2   1 
ATOM   1280 N  N     . ARG   A 1 164 ? -1.138  5.529   40.727  1.00 16.48 ? 161 ARG   A N     1 
ATOM   1281 C  CA    . ARG   A 1 164 ? -2.397  5.206   39.994  1.00 17.48 ? 161 ARG   A CA    1 
ATOM   1282 C  C     . ARG   A 1 164 ? -2.363  3.772   39.504  1.00 17.72 ? 161 ARG   A C     1 
ATOM   1283 O  O     . ARG   A 1 164 ? -3.389  3.081   39.623  1.00 18.25 ? 161 ARG   A O     1 
ATOM   1284 C  CB    . ARG   A 1 164 ? -2.652  6.212   38.882  1.00 17.90 ? 161 ARG   A CB    1 
ATOM   1285 C  CG    . ARG   A 1 164 ? -2.945  7.589   39.431  1.00 18.12 ? 161 ARG   A CG    1 
ATOM   1286 C  CD    . ARG   A 1 164 ? -3.196  8.666   38.400  1.00 18.73 ? 161 ARG   A CD    1 
ATOM   1287 N  NE    . ARG   A 1 164 ? -3.381  9.938   39.045  1.00 19.03 ? 161 ARG   A NE    1 
ATOM   1288 C  CZ    . ARG   A 1 164 ? -2.693  11.018  38.792  1.00 18.78 ? 161 ARG   A CZ    1 
ATOM   1289 N  NH1   . ARG   A 1 164 ? -1.798  10.989  37.828  1.00 18.48 ? 161 ARG   A NH1   1 
ATOM   1290 N  NH2   . ARG   A 1 164 ? -2.903  12.116  39.480  1.00 18.93 ? 161 ARG   A NH2   1 
ATOM   1291 N  N     . GLU   A 1 165 ? -1.200  3.334   39.025  1.00 16.87 ? 162 GLU   A N     1 
ATOM   1292 C  CA    . GLU   A 1 165 ? -0.995  1.956   38.549  1.00 17.30 ? 162 GLU   A CA    1 
ATOM   1293 C  C     . GLU   A 1 165 ? -1.217  0.983   39.711  1.00 17.66 ? 162 GLU   A C     1 
ATOM   1294 O  O     . GLU   A 1 165 ? -1.877  -0.017  39.507  1.00 18.82 ? 162 GLU   A O     1 
ATOM   1295 C  CB    . GLU   A 1 165 ? 0.423   1.815   37.952  1.00 16.58 ? 162 GLU   A CB    1 
ATOM   1296 C  CG    . GLU   A 1 165 ? 0.546   2.427   36.582  1.00 16.66 ? 162 GLU   A CG    1 
ATOM   1297 C  CD    . GLU   A 1 165 ? -0.343  1.876   35.472  1.00 17.66 ? 162 GLU   A CD    1 
ATOM   1298 O  OE1   . GLU   A 1 165 ? -0.187  0.723   35.089  1.00 17.94 ? 162 GLU   A OE1   1 
ATOM   1299 O  OE2   . GLU   A 1 165 ? -1.183  2.634   35.006  1.00 18.11 ? 162 GLU   A OE2   1 
ATOM   1300 N  N     . ILE   A 1 166 ? -0.711  1.301   40.882  1.00 17.48 ? 163 ILE   A N     1 
ATOM   1301 C  CA    . ILE   A 1 166 ? -0.870  0.455   42.088  1.00 18.31 ? 163 ILE   A CA    1 
ATOM   1302 C  C     . ILE   A 1 166 ? -2.383  0.414   42.434  1.00 19.84 ? 163 ILE   A C     1 
ATOM   1303 O  O     . ILE   A 1 166 ? -2.910  -0.618  42.593  1.00 20.71 ? 163 ILE   A O     1 
ATOM   1304 C  CB    . ILE   A 1 166 ? -0.033  0.967   43.268  1.00 17.64 ? 163 ILE   A CB    1 
ATOM   1305 C  CG1   . ILE   A 1 166 ? 1.469   1.054   42.952  1.00 17.00 ? 163 ILE   A CG1   1 
ATOM   1306 C  CG2   . ILE   A 1 166 ? -0.259  0.115   44.480  1.00 18.16 ? 163 ILE   A CG2   1 
ATOM   1307 C  CD1   . ILE   A 1 166 ? 2.298   1.618   44.084  1.00 16.43 ? 163 ILE   A CD1   1 
ATOM   1308 N  N     . ARG   A 1 167 ? -3.038  1.554   42.445  1.00 20.71 ? 164 ARG   A N     1 
ATOM   1309 C  CA    . ARG   A 1 167 ? -4.494  1.563   42.822  1.00 22.78 ? 164 ARG   A CA    1 
ATOM   1310 C  C     . ARG   A 1 167 ? -5.331  0.713   41.881  1.00 24.82 ? 164 ARG   A C     1 
ATOM   1311 O  O     . ARG   A 1 167 ? -6.176  -0.019  42.368  1.00 26.36 ? 164 ARG   A O     1 
ATOM   1312 C  CB    . ARG   A 1 167 ? -5.043  2.933   42.486  1.00 22.93 ? 164 ARG   A CB    1 
ATOM   1313 C  CG    . ARG   A 1 167 ? -4.977  3.909   43.629  1.00 22.67 ? 164 ARG   A CG    1 
ATOM   1314 C  CD    . ARG   A 1 167 ? -5.817  5.061   43.166  1.00 23.34 ? 164 ARG   A CD    1 
ATOM   1315 N  NE    . ARG   A 1 167 ? -5.494  6.114   44.046  1.00 22.87 ? 164 ARG   A NE    1 
ATOM   1316 C  CZ    . ARG   A 1 167 ? -5.557  7.361   43.722  1.00 22.85 ? 164 ARG   A CZ    1 
ATOM   1317 N  NH1   . ARG   A 1 167 ? -5.872  7.698   42.492  1.00 23.04 ? 164 ARG   A NH1   1 
ATOM   1318 N  NH2   . ARG   A 1 167 ? -5.202  8.250   44.616  1.00 22.68 ? 164 ARG   A NH2   1 
ATOM   1319 N  N     . GLN   A 1 168 ? -5.092  0.838   40.586  1.00 25.54 ? 165 GLN   A N     1 
ATOM   1320 C  CA    . GLN   A 1 168 ? -5.813  0.141   39.512  1.00 27.40 ? 165 GLN   A CA    1 
ATOM   1321 C  C     . GLN   A 1 168 ? -5.534  -1.367  39.525  1.00 28.08 ? 165 GLN   A C     1 
ATOM   1322 O  O     . GLN   A 1 168 ? -6.405  -2.110  39.047  1.00 28.89 ? 165 GLN   A O     1 
ATOM   1323 C  CB    . GLN   A 1 168 ? -5.562  0.826   38.180  1.00 27.56 ? 165 GLN   A CB    1 
ATOM   1324 C  CG    . GLN   A 1 168 ? -5.948  2.299   38.173  1.00 27.81 ? 165 GLN   A CG    1 
ATOM   1325 C  CD    . GLN   A 1 168 ? -5.621  2.939   36.853  1.00 28.18 ? 165 GLN   A CD    1 
ATOM   1326 O  OE1   . GLN   A 1 168 ? -5.642  2.290   35.823  1.00 29.99 ? 165 GLN   A OE1   1 
ATOM   1327 N  NE2   . GLN   A 1 168 ? -5.306  4.219   36.863  1.00 27.86 ? 165 GLN   A NE2   1 
ATOM   1328 N  N     . TYR   A 1 169 ? -4.325  -1.781  39.933  1.00 27.57 ? 166 TYR   A N     1 
ATOM   1329 C  CA    . TYR   A 1 169 ? -4.017  -3.223  40.049  1.00 28.69 ? 166 TYR   A CA    1 
ATOM   1330 C  C     . TYR   A 1 169 ? -5.070  -3.829  41.005  1.00 29.98 ? 166 TYR   A C     1 
ATOM   1331 O  O     . TYR   A 1 169 ? -5.634  -4.843  40.745  1.00 31.17 ? 166 TYR   A O     1 
ATOM   1332 C  CB    . TYR   A 1 169 ? -2.600  -3.328  40.616  1.00 28.28 ? 166 TYR   A CB    1 
ATOM   1333 C  CG    . TYR   A 1 169 ? -2.225  -4.682  41.105  1.00 29.30 ? 166 TYR   A CG    1 
ATOM   1334 C  CD1   . TYR   A 1 169 ? -2.466  -5.043  42.400  1.00 30.02 ? 166 TYR   A CD1   1 
ATOM   1335 C  CD2   . TYR   A 1 169 ? -1.557  -5.577  40.287  1.00 30.15 ? 166 TYR   A CD2   1 
ATOM   1336 C  CE1   . TYR   A 1 169 ? -2.137  -6.297  42.864  1.00 31.35 ? 166 TYR   A CE1   1 
ATOM   1337 C  CE2   . TYR   A 1 169 ? -1.195  -6.834  40.746  1.00 31.02 ? 166 TYR   A CE2   1 
ATOM   1338 C  CZ    . TYR   A 1 169 ? -1.507  -7.200  42.041  1.00 31.75 ? 166 TYR   A CZ    1 
ATOM   1339 O  OH    . TYR   A 1 169 ? -1.229  -8.438  42.554  1.00 33.07 ? 166 TYR   A OH    1 
ATOM   1340 N  N     . ARG   A 1 170 ? -5.294  -3.122  42.092  1.00 30.32 ? 167 ARG   A N     1 
ATOM   1341 C  CA    . ARG   A 1 170 ? -6.215  -3.507  43.192  1.00 31.19 ? 167 ARG   A CA    1 
ATOM   1342 C  C     . ARG   A 1 170 ? -7.696  -3.195  42.878  1.00 32.72 ? 167 ARG   A C     1 
ATOM   1343 O  O     . ARG   A 1 170 ? -8.501  -4.016  43.152  1.00 34.41 ? 167 ARG   A O     1 
ATOM   1344 C  CB    . ARG   A 1 170 ? -5.781  -2.756  44.441  1.00 30.06 ? 167 ARG   A CB    1 
ATOM   1345 C  CG    . ARG   A 1 170 ? -4.284  -2.748  44.651  1.00 28.79 ? 167 ARG   A CG    1 
ATOM   1346 C  CD    . ARG   A 1 170 ? -3.933  -1.720  45.705  1.00 27.79 ? 167 ARG   A CD    1 
ATOM   1347 N  NE    . ARG   A 1 170 ? -2.779  -2.241  46.370  1.00 26.90 ? 167 ARG   A NE    1 
ATOM   1348 C  CZ    . ARG   A 1 170 ? -2.036  -1.603  47.254  1.00 26.46 ? 167 ARG   A CZ    1 
ATOM   1349 N  NH1   . ARG   A 1 170 ? -1.004  -2.240  47.772  1.00 26.07 ? 167 ARG   A NH1   1 
ATOM   1350 N  NH2   . ARG   A 1 170 ? -2.339  -0.389  47.672  1.00 25.73 ? 167 ARG   A NH2   1 
ATOM   1351 N  N     . LEU   A 1 171 ? -7.996  -2.060  42.275  1.00 32.90 ? 168 LEU   A N     1 
ATOM   1352 C  CA    . LEU   A 1 171 ? -9.377  -1.612  41.968  1.00 34.20 ? 168 LEU   A CA    1 
ATOM   1353 C  C     . LEU   A 1 171 ? -9.711  -1.813  40.482  1.00 34.95 ? 168 LEU   A C     1 
ATOM   1354 O  O     . LEU   A 1 171 ? -9.195  -1.094  39.635  1.00 34.00 ? 168 LEU   A O     1 
ATOM   1355 C  CB    . LEU   A 1 171 ? -9.501  -0.148  42.407  1.00 34.31 ? 168 LEU   A CB    1 
ATOM   1356 C  CG    . LEU   A 1 171 ? -9.707  0.096   43.909  1.00 34.58 ? 168 LEU   A CG    1 
ATOM   1357 C  CD1   . LEU   A 1 171 ? -8.697  -0.641  44.764  1.00 34.14 ? 168 LEU   A CD1   1 
ATOM   1358 C  CD2   . LEU   A 1 171 ? -9.764  1.572   44.289  1.00 33.90 ? 168 LEU   A CD2   1 
ATOM   1359 N  N     . MET   B 1 4   ? 32.565  3.784   2.888   1.00 34.66 ? 1   MET   B N     1 
ATOM   1360 C  CA    . MET   B 1 4   ? 31.300  3.011   2.884   1.00 34.17 ? 1   MET   B CA    1 
ATOM   1361 C  C     . MET   B 1 4   ? 31.053  2.418   1.491   1.00 33.27 ? 1   MET   B C     1 
ATOM   1362 O  O     . MET   B 1 4   ? 31.297  3.124   0.512   1.00 32.91 ? 1   MET   B O     1 
ATOM   1363 C  CB    . MET   B 1 4   ? 30.117  3.915   3.244   1.00 34.38 ? 1   MET   B CB    1 
ATOM   1364 C  CG    . MET   B 1 4   ? 28.847  3.128   3.465   1.00 34.18 ? 1   MET   B CG    1 
ATOM   1365 S  SD    . MET   B 1 4   ? 27.553  4.212   3.943   1.00 34.66 ? 1   MET   B SD    1 
ATOM   1366 C  CE    . MET   B 1 4   ? 28.235  4.862   5.469   1.00 35.58 ? 1   MET   B CE    1 
ATOM   1367 N  N     . THR   B 1 5   ? 30.501  1.209   1.458   1.00 32.96 ? 2   THR   B N     1 
ATOM   1368 C  CA    . THR   B 1 5   ? 30.164  0.472   0.217   1.00 32.24 ? 2   THR   B CA    1 
ATOM   1369 C  C     . THR   B 1 5   ? 28.885  1.041   -0.413  1.00 31.57 ? 2   THR   B C     1 
ATOM   1370 O  O     . THR   B 1 5   ? 27.830  1.056   0.224   1.00 32.05 ? 2   THR   B O     1 
ATOM   1371 C  CB    . THR   B 1 5   ? 29.913  -1.032  0.461   1.00 32.29 ? 2   THR   B CB    1 
ATOM   1372 O  OG1   . THR   B 1 5   ? 30.914  -1.611  1.306   1.00 33.12 ? 2   THR   B OG1   1 
ATOM   1373 C  CG2   . THR   B 1 5   ? 29.861  -1.842  -0.825  1.00 31.74 ? 2   THR   B CG2   1 
ATOM   1374 N  N     . GLU   B 1 6   ? 28.988  1.438   -1.673  1.00 30.79 ? 3   GLU   B N     1 
ATOM   1375 C  CA    . GLU   B 1 6   ? 27.837  1.971   -2.440  1.00 29.88 ? 3   GLU   B CA    1 
ATOM   1376 C  C     . GLU   B 1 6   ? 27.342  0.986   -3.506  1.00 28.53 ? 3   GLU   B C     1 
ATOM   1377 O  O     . GLU   B 1 6   ? 28.079  0.125   -3.924  1.00 28.59 ? 3   GLU   B O     1 
ATOM   1378 C  CB    . GLU   B 1 6   ? 28.236  3.276   -3.094  1.00 30.30 ? 3   GLU   B CB    1 
ATOM   1379 C  CG    . GLU   B 1 6   ? 28.743  4.285   -2.107  1.00 31.34 ? 3   GLU   B CG    1 
ATOM   1380 C  CD    . GLU   B 1 6   ? 29.581  5.341   -2.797  1.00 31.97 ? 3   GLU   B CD    1 
ATOM   1381 O  OE1   . GLU   B 1 6   ? 29.834  5.167   -4.014  1.00 32.21 ? 3   GLU   B OE1   1 
ATOM   1382 O  OE2   . GLU   B 1 6   ? 29.940  6.335   -2.140  1.00 32.82 ? 3   GLU   B OE2   1 
ATOM   1383 N  N     . TYR   B 1 7   ? 26.100  1.156   -3.923  1.00 27.60 ? 4   TYR   B N     1 
ATOM   1384 C  CA    . TYR   B 1 7   ? 25.463  0.333   -4.945  1.00 26.65 ? 4   TYR   B CA    1 
ATOM   1385 C  C     . TYR   B 1 7   ? 24.752  1.273   -5.923  1.00 26.24 ? 4   TYR   B C     1 
ATOM   1386 O  O     . TYR   B 1 7   ? 23.874  2.038   -5.534  1.00 26.44 ? 4   TYR   B O     1 
ATOM   1387 C  CB    . TYR   B 1 7   ? 24.514  -0.696  -4.315  1.00 26.26 ? 4   TYR   B CB    1 
ATOM   1388 C  CG    . TYR   B 1 7   ? 25.195  -1.769  -3.498  1.00 26.42 ? 4   TYR   B CG    1 
ATOM   1389 C  CD1   . TYR   B 1 7   ? 25.499  -1.558  -2.162  1.00 26.87 ? 4   TYR   B CD1   1 
ATOM   1390 C  CD2   . TYR   B 1 7   ? 25.542  -2.993  -4.054  1.00 26.29 ? 4   TYR   B CD2   1 
ATOM   1391 C  CE1   . TYR   B 1 7   ? 26.121  -2.531  -1.399  1.00 27.25 ? 4   TYR   B CE1   1 
ATOM   1392 C  CE2   . TYR   B 1 7   ? 26.181  -3.973  -3.307  1.00 26.65 ? 4   TYR   B CE2   1 
ATOM   1393 C  CZ    . TYR   B 1 7   ? 26.461  -3.746  -1.972  1.00 27.13 ? 4   TYR   B CZ    1 
ATOM   1394 O  OH    . TYR   B 1 7   ? 27.068  -4.711  -1.211  1.00 27.69 ? 4   TYR   B OH    1 
ATOM   1395 N  N     . LYS   B 1 8   ? 25.183  1.230   -7.185  1.00 26.20 ? 5   LYS   B N     1 
ATOM   1396 C  CA    . LYS   B 1 8   ? 24.622  2.066   -8.232  1.00 25.86 ? 5   LYS   B CA    1 
ATOM   1397 C  C     . LYS   B 1 8   ? 23.531  1.264   -8.941  1.00 25.28 ? 5   LYS   B C     1 
ATOM   1398 O  O     . LYS   B 1 8   ? 23.822  0.267   -9.584  1.00 24.92 ? 5   LYS   B O     1 
ATOM   1399 C  CB    . LYS   B 1 8   ? 25.702  2.489   -9.226  1.00 26.25 ? 5   LYS   B CB    1 
ATOM   1400 C  CG    . LYS   B 1 8   ? 26.797  3.371   -8.646  1.00 26.91 ? 5   LYS   B CG    1 
ATOM   1401 C  CD    . LYS   B 1 8   ? 27.340  4.365   -9.648  1.00 27.47 ? 5   LYS   B CD    1 
ATOM   1402 C  CE    . LYS   B 1 8   ? 28.380  5.294   -9.059  1.00 28.15 ? 5   LYS   B CE    1 
ATOM   1403 N  NZ    . LYS   B 1 8   ? 29.533  4.534   -8.511  1.00 28.48 ? 5   LYS   B NZ    1 
ATOM   1404 N  N     . LEU   B 1 9   ? 22.277  1.692   -8.785  1.00 25.09 ? 6   LEU   B N     1 
ATOM   1405 C  CA    . LEU   B 1 9   ? 21.133  0.934   -9.293  1.00 24.70 ? 6   LEU   B CA    1 
ATOM   1406 C  C     . LEU   B 1 9   ? 20.416  1.752   -10.354 1.00 24.61 ? 6   LEU   B C     1 
ATOM   1407 O  O     . LEU   B 1 9   ? 20.302  2.975   -10.237 1.00 24.99 ? 6   LEU   B O     1 
ATOM   1408 C  CB    . LEU   B 1 9   ? 20.174  0.620   -8.147  1.00 24.62 ? 6   LEU   B CB    1 
ATOM   1409 C  CG    . LEU   B 1 9   ? 20.785  -0.075  -6.936  1.00 24.66 ? 6   LEU   B CG    1 
ATOM   1410 C  CD1   . LEU   B 1 9   ? 19.688  -0.384  -5.936  1.00 24.72 ? 6   LEU   B CD1   1 
ATOM   1411 C  CD2   . LEU   B 1 9   ? 21.521  -1.340  -7.338  1.00 24.54 ? 6   LEU   B CD2   1 
ATOM   1412 N  N     . VAL   B 1 10  ? 19.951  1.065   -11.396 1.00 24.44 ? 7   VAL   B N     1 
ATOM   1413 C  CA    . VAL   B 1 10  ? 19.237  1.704   -12.487 1.00 24.42 ? 7   VAL   B CA    1 
ATOM   1414 C  C     . VAL   B 1 10  ? 17.897  0.992   -12.676 1.00 24.09 ? 7   VAL   B C     1 
ATOM   1415 O  O     . VAL   B 1 10  ? 17.834  -0.220  -12.748 1.00 23.95 ? 7   VAL   B O     1 
ATOM   1416 C  CB    . VAL   B 1 10  ? 20.062  1.697   -13.788 1.00 24.42 ? 7   VAL   B CB    1 
ATOM   1417 C  CG1   . VAL   B 1 10  ? 19.360  2.479   -14.876 1.00 24.63 ? 7   VAL   B CG1   1 
ATOM   1418 C  CG2   . VAL   B 1 10  ? 21.468  2.235   -13.585 1.00 24.68 ? 7   VAL   B CG2   1 
ATOM   1419 N  N     . VAL   B 1 11  ? 16.832  1.784   -12.755 1.00 24.18 ? 8   VAL   B N     1 
ATOM   1420 C  CA    . VAL   B 1 11  ? 15.502  1.296   -13.000 1.00 24.19 ? 8   VAL   B CA    1 
ATOM   1421 C  C     . VAL   B 1 11  ? 15.170  1.602   -14.461 1.00 24.30 ? 8   VAL   B C     1 
ATOM   1422 O  O     . VAL   B 1 11  ? 15.158  2.763   -14.857 1.00 24.41 ? 8   VAL   B O     1 
ATOM   1423 C  CB    . VAL   B 1 11  ? 14.465  1.948   -12.071 1.00 24.36 ? 8   VAL   B CB    1 
ATOM   1424 C  CG1   . VAL   B 1 11  ? 13.142  1.209   -12.153 1.00 24.39 ? 8   VAL   B CG1   1 
ATOM   1425 C  CG2   . VAL   B 1 11  ? 14.951  2.020   -10.630 1.00 24.54 ? 8   VAL   B CG2   1 
ATOM   1426 N  N     . VAL   B 1 12  ? 14.889  0.550   -15.226 1.00 24.03 ? 9   VAL   B N     1 
ATOM   1427 C  CA    . VAL   B 1 12  ? 14.573  0.671   -16.651 1.00 24.15 ? 9   VAL   B CA    1 
ATOM   1428 C  C     . VAL   B 1 12  ? 13.278  -0.080  -16.940 1.00 23.99 ? 9   VAL   B C     1 
ATOM   1429 O  O     . VAL   B 1 12  ? 12.813  -0.870  -16.136 1.00 23.86 ? 9   VAL   B O     1 
ATOM   1430 C  CB    . VAL   B 1 12  ? 15.718  0.147   -17.535 1.00 24.13 ? 9   VAL   B CB    1 
ATOM   1431 C  CG1   . VAL   B 1 12  ? 17.008  0.888   -17.214 1.00 24.28 ? 9   VAL   B CG1   1 
ATOM   1432 C  CG2   . VAL   B 1 12  ? 15.902  -1.367  -17.416 1.00 23.98 ? 9   VAL   B CG2   1 
ATOM   1433 N  N     . GLY   B 1 13  ? 12.709  0.208   -18.105 1.00 24.06 ? 10  GLY   B N     1 
ATOM   1434 C  CA    . GLY   B 1 13  ? 11.435  -0.300  -18.473 1.00 24.07 ? 10  GLY   B CA    1 
ATOM   1435 C  C     . GLY   B 1 13  ? 10.689  0.711   -19.308 1.00 24.38 ? 10  GLY   B C     1 
ATOM   1436 O  O     . GLY   B 1 13  ? 11.054  1.873   -19.340 1.00 24.58 ? 10  GLY   B O     1 
ATOM   1437 N  N     . ALA   B 1 14  ? 9.602   0.246   -19.930 1.00 24.47 ? 11  ALA   B N     1 
ATOM   1438 C  CA    . ALA   B 1 14  ? 8.776   1.033   -20.814 1.00 24.73 ? 11  ALA   B CA    1 
ATOM   1439 C  C     . ALA   B 1 14  ? 8.072   2.153   -20.047 1.00 24.70 ? 11  ALA   B C     1 
ATOM   1440 O  O     . ALA   B 1 14  ? 7.864   2.071   -18.858 1.00 24.33 ? 11  ALA   B O     1 
ATOM   1441 C  CB    . ALA   B 1 14  ? 7.774   0.133   -21.489 1.00 24.84 ? 11  ALA   B CB    1 
ATOM   1442 N  N     . GLY   B 1 15  ? 7.699   3.208   -20.769 1.00 25.10 ? 12  GLY   B N     1 
ATOM   1443 C  CA    . GLY   B 1 15  ? 6.965   4.302   -20.168 1.00 25.40 ? 12  GLY   B CA    1 
ATOM   1444 C  C     . GLY   B 1 15  ? 5.683   3.804   -19.522 1.00 25.22 ? 12  GLY   B C     1 
ATOM   1445 O  O     . GLY   B 1 15  ? 4.971   3.008   -20.100 1.00 25.11 ? 12  GLY   B O     1 
ATOM   1446 N  N     . GLY   B 1 16  ? 5.430   4.256   -18.293 1.00 25.31 ? 13  GLY   B N     1 
ATOM   1447 C  CA    . GLY   B 1 16  ? 4.176   4.017   -17.607 1.00 25.31 ? 13  GLY   B CA    1 
ATOM   1448 C  C     . GLY   B 1 16  ? 4.156   2.748   -16.764 1.00 24.81 ? 13  GLY   B C     1 
ATOM   1449 O  O     . GLY   B 1 16  ? 3.127   2.422   -16.202 1.00 25.08 ? 13  GLY   B O     1 
ATOM   1450 N  N     . VAL   B 1 17  ? 5.281   2.043   -16.632 1.00 24.53 ? 14  VAL   B N     1 
ATOM   1451 C  CA    . VAL   B 1 17  ? 5.276   0.761   -15.908 1.00 24.23 ? 14  VAL   B CA    1 
ATOM   1452 C  C     . VAL   B 1 17  ? 5.386   0.970   -14.389 1.00 24.33 ? 14  VAL   B C     1 
ATOM   1453 O  O     . VAL   B 1 17  ? 5.034   0.044   -13.650 1.00 24.39 ? 14  VAL   B O     1 
ATOM   1454 C  CB    . VAL   B 1 17  ? 6.373   -0.212  -16.382 1.00 23.82 ? 14  VAL   B CB    1 
ATOM   1455 C  CG1   . VAL   B 1 17  ? 6.201   -0.583  -17.848 1.00 23.93 ? 14  VAL   B CG1   1 
ATOM   1456 C  CG2   . VAL   B 1 17  ? 7.777   0.307   -16.098 1.00 23.72 ? 14  VAL   B CG2   1 
ATOM   1457 N  N     . GLY   B 1 18  ? 5.919   2.118   -13.943 1.00 24.61 ? 15  GLY   B N     1 
ATOM   1458 C  CA    . GLY   B 1 18  ? 6.000   2.468   -12.518 1.00 24.76 ? 15  GLY   B CA    1 
ATOM   1459 C  C     . GLY   B 1 18  ? 7.415   2.655   -11.991 1.00 24.68 ? 15  GLY   B C     1 
ATOM   1460 O  O     . GLY   B 1 18  ? 7.653   2.546   -10.788 1.00 24.97 ? 15  GLY   B O     1 
ATOM   1461 N  N     . LYS   B 1 19  ? 8.365   2.964   -12.867 1.00 24.50 ? 16  LYS   B N     1 
ATOM   1462 C  CA    . LYS   B 1 19  ? 9.749   3.115   -12.439 1.00 24.55 ? 16  LYS   B CA    1 
ATOM   1463 C  C     . LYS   B 1 19  ? 9.822   4.206   -11.368 1.00 24.98 ? 16  LYS   B C     1 
ATOM   1464 O  O     . LYS   B 1 19  ? 10.368  4.000   -10.283 1.00 24.99 ? 16  LYS   B O     1 
ATOM   1465 C  CB    . LYS   B 1 19  ? 10.651  3.456   -13.626 1.00 24.66 ? 16  LYS   B CB    1 
ATOM   1466 C  CG    . LYS   B 1 19  ? 10.651  2.419   -14.744 1.00 24.40 ? 16  LYS   B CG    1 
ATOM   1467 C  CD    . LYS   B 1 19  ? 11.529  2.801   -15.940 1.00 24.58 ? 16  LYS   B CD    1 
ATOM   1468 C  CE    . LYS   B 1 19  ? 11.028  3.983   -16.749 1.00 25.01 ? 16  LYS   B CE    1 
ATOM   1469 N  NZ    . LYS   B 1 19  ? 9.721   3.740   -17.410 1.00 25.15 ? 16  LYS   B NZ    1 
ATOM   1470 N  N     . SER   B 1 20  ? 9.240   5.360   -11.698 1.00 25.46 ? 17  SER   B N     1 
ATOM   1471 C  CA    . SER   B 1 20  ? 9.251   6.542   -10.832 1.00 25.99 ? 17  SER   B CA    1 
ATOM   1472 C  C     . SER   B 1 20  ? 8.541   6.244   -9.505  1.00 26.20 ? 17  SER   B C     1 
ATOM   1473 O  O     . SER   B 1 20  ? 9.076   6.538   -8.427  1.00 26.63 ? 17  SER   B O     1 
ATOM   1474 C  CB    . SER   B 1 20  ? 8.612   7.736   -11.530 1.00 26.29 ? 17  SER   B CB    1 
ATOM   1475 O  OG    . SER   B 1 20  ? 9.490   8.309   -12.493 1.00 26.37 ? 17  SER   B OG    1 
ATOM   1476 N  N     . ALA   B 1 21  ? 7.332   5.676   -9.607  1.00 26.21 ? 18  ALA   B N     1 
ATOM   1477 C  CA    . ALA   B 1 21  ? 6.474   5.392   -8.453  1.00 26.42 ? 18  ALA   B CA    1 
ATOM   1478 C  C     . ALA   B 1 21  ? 7.172   4.447   -7.475  1.00 26.40 ? 18  ALA   B C     1 
ATOM   1479 O  O     . ALA   B 1 21  ? 6.933   4.560   -6.275  1.00 26.65 ? 18  ALA   B O     1 
ATOM   1480 C  CB    . ALA   B 1 21  ? 5.152   4.823   -8.901  1.00 26.23 ? 18  ALA   B CB    1 
ATOM   1481 N  N     . LEU   B 1 22  ? 8.023   3.547   -7.997  1.00 26.18 ? 19  LEU   B N     1 
ATOM   1482 C  CA    . LEU   B 1 22  ? 8.730   2.540   -7.192  1.00 26.25 ? 19  LEU   B CA    1 
ATOM   1483 C  C     . LEU   B 1 22  ? 9.920   3.171   -6.473  1.00 26.64 ? 19  LEU   B C     1 
ATOM   1484 O  O     . LEU   B 1 22  ? 10.144  2.914   -5.297  1.00 26.77 ? 19  LEU   B O     1 
ATOM   1485 C  CB    . LEU   B 1 22  ? 9.204   1.383   -8.076  1.00 25.82 ? 19  LEU   B CB    1 
ATOM   1486 C  CG    . LEU   B 1 22  ? 8.148   0.343   -8.455  1.00 25.78 ? 19  LEU   B CG    1 
ATOM   1487 C  CD1   . LEU   B 1 22  ? 8.666   -0.550  -9.571  1.00 25.57 ? 19  LEU   B CD1   1 
ATOM   1488 C  CD2   . LEU   B 1 22  ? 7.736   -0.509  -7.255  1.00 25.87 ? 19  LEU   B CD2   1 
ATOM   1489 N  N     . THR   B 1 23  ? 10.677  3.990   -7.202  1.00 26.94 ? 20  THR   B N     1 
ATOM   1490 C  CA    . THR   B 1 23  ? 11.788  4.727   -6.637  1.00 27.44 ? 20  THR   B CA    1 
ATOM   1491 C  C     . THR   B 1 23  ? 11.265  5.673   -5.554  1.00 28.04 ? 20  THR   B C     1 
ATOM   1492 O  O     . THR   B 1 23  ? 11.821  5.738   -4.475  1.00 28.53 ? 20  THR   B O     1 
ATOM   1493 C  CB    . THR   B 1 23  ? 12.568  5.484   -7.715  1.00 27.46 ? 20  THR   B CB    1 
ATOM   1494 O  OG1   . THR   B 1 23  ? 12.863  4.581   -8.781  1.00 27.37 ? 20  THR   B OG1   1 
ATOM   1495 C  CG2   . THR   B 1 23  ? 13.849  6.078   -7.167  1.00 27.87 ? 20  THR   B CG2   1 
ATOM   1496 N  N     . ILE   B 1 24  ? 10.169  6.372   -5.847  1.00 28.41 ? 21  ILE   B N     1 
ATOM   1497 C  CA    . ILE   B 1 24  ? 9.628   7.353   -4.923  1.00 29.24 ? 21  ILE   B CA    1 
ATOM   1498 C  C     . ILE   B 1 24  ? 9.072   6.657   -3.679  1.00 29.49 ? 21  ILE   B C     1 
ATOM   1499 O  O     . ILE   B 1 24  ? 9.211   7.192   -2.592  1.00 30.63 ? 21  ILE   B O     1 
ATOM   1500 C  CB    . ILE   B 1 24  ? 8.577   8.249   -5.604  1.00 29.42 ? 21  ILE   B CB    1 
ATOM   1501 C  CG1   . ILE   B 1 24  ? 9.265   9.164   -6.616  1.00 29.41 ? 21  ILE   B CG1   1 
ATOM   1502 C  CG2   . ILE   B 1 24  ? 7.764   9.032   -4.579  1.00 30.20 ? 21  ILE   B CG2   1 
ATOM   1503 C  CD1   . ILE   B 1 24  ? 8.320   9.849   -7.575  1.00 29.69 ? 21  ILE   B CD1   1 
ATOM   1504 N  N     . GLN   B 1 25  ? 8.434   5.493   -3.837  1.00 29.10 ? 22  GLN   B N     1 
ATOM   1505 C  CA    . GLN   B 1 25  ? 7.968   4.761   -2.668  1.00 29.16 ? 22  GLN   B CA    1 
ATOM   1506 C  C     . GLN   B 1 25  ? 9.155   4.444   -1.762  1.00 29.10 ? 22  GLN   B C     1 
ATOM   1507 O  O     . GLN   B 1 25  ? 9.109   4.722   -0.560  1.00 29.70 ? 22  GLN   B O     1 
ATOM   1508 C  CB    . GLN   B 1 25  ? 7.242   3.465   -3.012  1.00 28.69 ? 22  GLN   B CB    1 
ATOM   1509 C  CG    . GLN   B 1 25  ? 5.729   3.590   -2.956  1.00 28.95 ? 22  GLN   B CG    1 
ATOM   1510 C  CD    . GLN   B 1 25  ? 5.123   3.702   -1.570  1.00 29.41 ? 22  GLN   B CD    1 
ATOM   1511 O  OE1   . GLN   B 1 25  ? 5.783   3.955   -0.557  1.00 29.55 ? 22  GLN   B OE1   1 
ATOM   1512 N  NE2   . GLN   B 1 25  ? 3.815   3.527   -1.528  1.00 29.67 ? 22  GLN   B NE2   1 
ATOM   1513 N  N     . LEU   B 1 26  ? 10.194  3.850   -2.353  1.00 28.62 ? 23  LEU   B N     1 
ATOM   1514 C  CA    . LEU   B 1 26  ? 11.343  3.407   -1.597  1.00 28.56 ? 23  LEU   B CA    1 
ATOM   1515 C  C     . LEU   B 1 26  ? 11.948  4.572   -0.811  1.00 29.60 ? 23  LEU   B C     1 
ATOM   1516 O  O     . LEU   B 1 26  ? 12.302  4.412   0.347   1.00 30.07 ? 23  LEU   B O     1 
ATOM   1517 C  CB    . LEU   B 1 26  ? 12.390  2.831   -2.543  1.00 27.92 ? 23  LEU   B CB    1 
ATOM   1518 C  CG    . LEU   B 1 26  ? 13.614  2.267   -1.832  1.00 27.96 ? 23  LEU   B CG    1 
ATOM   1519 C  CD1   . LEU   B 1 26  ? 13.293  0.927   -1.175  1.00 28.04 ? 23  LEU   B CD1   1 
ATOM   1520 C  CD2   . LEU   B 1 26  ? 14.771  2.145   -2.799  1.00 27.54 ? 23  LEU   B CD2   1 
ATOM   1521 N  N     . ILE   B 1 27  ? 12.072  5.731   -1.472  1.00 30.18 ? 24  ILE   B N     1 
ATOM   1522 C  CA    . ILE   B 1 27  ? 12.803  6.869   -0.935  1.00 31.05 ? 24  ILE   B CA    1 
ATOM   1523 C  C     . ILE   B 1 27  ? 11.903  7.678   0.007   1.00 32.22 ? 24  ILE   B C     1 
ATOM   1524 O  O     . ILE   B 1 27  ? 12.287  7.929   1.151   1.00 32.94 ? 24  ILE   B O     1 
ATOM   1525 C  CB    . ILE   B 1 27  ? 13.380  7.738   -2.070  1.00 30.87 ? 24  ILE   B CB    1 
ATOM   1526 C  CG1   . ILE   B 1 27  ? 14.330  6.929   -2.962  1.00 30.20 ? 24  ILE   B CG1   1 
ATOM   1527 C  CG2   . ILE   B 1 27  ? 14.059  8.984   -1.510  1.00 31.65 ? 24  ILE   B CG2   1 
ATOM   1528 C  CD1   . ILE   B 1 27  ? 15.656  6.579   -2.324  1.00 30.12 ? 24  ILE   B CD1   1 
ATOM   1529 N  N     . GLN   B 1 28  ? 10.728  8.087   -0.484  1.00 32.76 ? 25  GLN   B N     1 
ATOM   1530 C  CA    . GLN   B 1 28  ? 9.866   9.050   0.214   1.00 33.91 ? 25  GLN   B CA    1 
ATOM   1531 C  C     . GLN   B 1 28  ? 8.680   8.387   0.918   1.00 34.11 ? 25  GLN   B C     1 
ATOM   1532 O  O     . GLN   B 1 28  ? 7.883   9.068   1.566   1.00 34.78 ? 25  GLN   B O     1 
ATOM   1533 C  CB    . GLN   B 1 28  ? 9.289   10.069  -0.766  1.00 33.99 ? 25  GLN   B CB    1 
ATOM   1534 C  CG    . GLN   B 1 28  ? 10.335  10.845  -1.537  1.00 34.04 ? 25  GLN   B CG    1 
ATOM   1535 C  CD    . GLN   B 1 28  ? 9.695   11.986  -2.288  1.00 34.64 ? 25  GLN   B CD    1 
ATOM   1536 O  OE1   . GLN   B 1 28  ? 8.474   12.120  -2.319  1.00 35.09 ? 25  GLN   B OE1   1 
ATOM   1537 N  NE2   . GLN   B 1 28  ? 10.514  12.820  -2.892  1.00 34.63 ? 25  GLN   B NE2   1 
ATOM   1538 N  N     . ASN   B 1 29  ? 8.524   7.078   0.737   1.00 33.68 ? 26  ASN   B N     1 
ATOM   1539 C  CA    . ASN   B 1 29  ? 7.502   6.314   1.451   1.00 33.82 ? 26  ASN   B CA    1 
ATOM   1540 C  C     . ASN   B 1 29  ? 6.088   6.843   1.141   1.00 33.90 ? 26  ASN   B C     1 
ATOM   1541 O  O     . ASN   B 1 29  ? 5.253   6.961   2.028   1.00 34.66 ? 26  ASN   B O     1 
ATOM   1542 C  CB    . ASN   B 1 29  ? 7.795   6.318   2.955   1.00 34.78 ? 26  ASN   B CB    1 
ATOM   1543 C  CG    . ASN   B 1 29  ? 6.903   5.357   3.707   1.00 35.34 ? 26  ASN   B CG    1 
ATOM   1544 O  OD1   . ASN   B 1 29  ? 6.639   4.257   3.223   1.00 35.70 ? 26  ASN   B OD1   1 
ATOM   1545 N  ND2   . ASN   B 1 29  ? 6.419   5.765   4.875   1.00 36.70 ? 26  ASN   B ND2   1 
ATOM   1546 N  N     . HIS   B 1 30  ? 5.803   7.149   -0.128  1.00 33.30 ? 27  HIS   B N     1 
ATOM   1547 C  CA    . HIS   B 1 30  ? 4.414   7.420   -0.553  1.00 33.09 ? 27  HIS   B CA    1 
ATOM   1548 C  C     . HIS   B 1 30  ? 4.241   7.142   -2.044  1.00 32.30 ? 27  HIS   B C     1 
ATOM   1549 O  O     . HIS   B 1 30  ? 5.224   7.050   -2.772  1.00 32.33 ? 27  HIS   B O     1 
ATOM   1550 C  CB    . HIS   B 1 30  ? 4.004   8.872   -0.270  1.00 33.97 ? 27  HIS   B CB    1 
ATOM   1551 C  CG    . HIS   B 1 30  ? 4.719   9.876   -1.113  1.00 33.85 ? 27  HIS   B CG    1 
ATOM   1552 N  ND1   . HIS   B 1 30  ? 4.070   10.662  -2.050  1.00 34.25 ? 27  HIS   B ND1   1 
ATOM   1553 C  CD2   . HIS   B 1 30  ? 6.021   10.232  -1.150  1.00 33.91 ? 27  HIS   B CD2   1 
ATOM   1554 C  CE1   . HIS   B 1 30  ? 4.949   11.461  -2.626  1.00 34.36 ? 27  HIS   B CE1   1 
ATOM   1555 N  NE2   . HIS   B 1 30  ? 6.155   11.212  -2.094  1.00 34.11 ? 27  HIS   B NE2   1 
ATOM   1556 N  N     . PHE   B 1 31  ? 2.981   7.084   -2.482  1.00 32.33 ? 28  PHE   B N     1 
ATOM   1557 C  CA    . PHE   B 1 31  ? 2.646   6.683   -3.829  1.00 31.80 ? 28  PHE   B CA    1 
ATOM   1558 C  C     . PHE   B 1 31  ? 2.270   7.901   -4.670  1.00 32.73 ? 28  PHE   B C     1 
ATOM   1559 O  O     . PHE   B 1 31  ? 1.344   8.639   -4.334  1.00 33.72 ? 28  PHE   B O     1 
ATOM   1560 C  CB    . PHE   B 1 31  ? 1.484   5.692   -3.829  1.00 31.31 ? 28  PHE   B CB    1 
ATOM   1561 C  CG    . PHE   B 1 31  ? 1.025   5.296   -5.208  1.00 30.63 ? 28  PHE   B CG    1 
ATOM   1562 C  CD1   . PHE   B 1 31  ? 1.923   4.774   -6.131  1.00 30.04 ? 28  PHE   B CD1   1 
ATOM   1563 C  CD2   . PHE   B 1 31  ? -0.296  5.457   -5.591  1.00 30.72 ? 28  PHE   B CD2   1 
ATOM   1564 C  CE1   . PHE   B 1 31  ? 1.503   4.408   -7.402  1.00 29.62 ? 28  PHE   B CE1   1 
ATOM   1565 C  CE2   . PHE   B 1 31  ? -0.712  5.095   -6.863  1.00 30.40 ? 28  PHE   B CE2   1 
ATOM   1566 C  CZ    . PHE   B 1 31  ? 0.182   4.554   -7.759  1.00 29.64 ? 28  PHE   B CZ    1 
ATOM   1567 N  N     . VAL   B 1 32  ? 2.885   8.058   -5.845  1.00 33.03 ? 29  VAL   B N     1 
ATOM   1568 C  CA    . VAL   B 1 32  ? 2.572   9.184   -6.769  1.00 33.93 ? 29  VAL   B CA    1 
ATOM   1569 C  C     . VAL   B 1 32  ? 1.582   8.705   -7.837  1.00 34.48 ? 29  VAL   B C     1 
ATOM   1570 O  O     . VAL   B 1 32  ? 1.970   7.860   -8.651  1.00 34.31 ? 29  VAL   B O     1 
ATOM   1571 C  CB    . VAL   B 1 32  ? 3.844   9.778   -7.383  1.00 33.75 ? 29  VAL   B CB    1 
ATOM   1572 C  CG1   . VAL   B 1 32  ? 4.731   10.416  -6.344  1.00 34.22 ? 29  VAL   B CG1   1 
ATOM   1573 C  CG2   . VAL   B 1 32  ? 4.642   8.726   -8.110  1.00 33.27 ? 29  VAL   B CG2   1 
ATOM   1574 N  N     . ASP   B 1 33  ? 0.373   9.263   -7.784  1.00 35.52 ? 30  ASP   B N     1 
ATOM   1575 C  CA    . ASP   B 1 33  ? -0.851  9.010   -8.601  1.00 35.71 ? 30  ASP   B CA    1 
ATOM   1576 C  C     . ASP   B 1 33  ? -0.664  9.433   -10.057 1.00 35.65 ? 30  ASP   B C     1 
ATOM   1577 O  O     . ASP   B 1 33  ? -1.468  9.064   -10.889 1.00 35.58 ? 30  ASP   B O     1 
ATOM   1578 C  CB    . ASP   B 1 33  ? -2.010  9.834   -8.049  1.00 37.00 ? 30  ASP   B CB    1 
ATOM   1579 C  CG    . ASP   B 1 33  ? -3.340  9.172   -8.266  1.00 37.42 ? 30  ASP   B CG    1 
ATOM   1580 O  OD1   . ASP   B 1 33  ? -3.338  7.950   -8.440  1.00 37.19 ? 30  ASP   B OD1   1 
ATOM   1581 O  OD2   . ASP   B 1 33  ? -4.354  9.881   -8.203  1.00 38.54 ? 30  ASP   B OD2   1 
ATOM   1582 N  N     . GLU   B 1 34  ? 0.295   10.298  -10.285 1.00 35.55 ? 31  GLU   B N     1 
ATOM   1583 C  CA    . GLU   B 1 34  ? 0.627   10.818  -11.615 1.00 35.21 ? 31  GLU   B CA    1 
ATOM   1584 C  C     . GLU   B 1 34  ? 1.965   11.491  -11.414 1.00 34.94 ? 31  GLU   B C     1 
ATOM   1585 O  O     . GLU   B 1 34  ? 2.058   12.248  -10.498 1.00 35.95 ? 31  GLU   B O     1 
ATOM   1586 C  CB    . GLU   B 1 34  ? -0.368  11.936  -11.920 1.00 36.11 ? 31  GLU   B CB    1 
ATOM   1587 C  CG    . GLU   B 1 34  ? -0.278  12.592  -13.276 0.00 67.19 ? 31  GLU   B CG    1 
ATOM   1588 C  CD    . GLU   B 1 34  ? -1.363  13.650  -13.449 0.00 68.19 ? 31  GLU   B CD    1 
ATOM   1589 O  OE1   . GLU   B 1 34  ? -2.126  13.864  -12.492 0.00 68.59 ? 31  GLU   B OE1   1 
ATOM   1590 O  OE2   . GLU   B 1 34  ? -1.451  14.224  -14.542 0.00 68.62 ? 31  GLU   B OE2   1 
ATOM   1591 N  N     . TYR   B 1 35  ? 2.876   11.347  -12.341 1.00 33.79 ? 32  TYR   B N     1 
ATOM   1592 C  CA    . TYR   B 1 35  ? 4.212   11.943  -12.200 1.00 33.24 ? 32  TYR   B CA    1 
ATOM   1593 C  C     . TYR   B 1 35  ? 4.769   12.161  -13.611 1.00 33.21 ? 32  TYR   B C     1 
ATOM   1594 O  O     . TYR   B 1 35  ? 4.477   11.291  -14.432 1.00 32.81 ? 32  TYR   B O     1 
ATOM   1595 C  CB    . TYR   B 1 35  ? 5.084   10.962  -11.425 1.00 32.35 ? 32  TYR   B CB    1 
ATOM   1596 C  CG    . TYR   B 1 35  ? 6.379   11.545  -10.968 1.00 32.29 ? 32  TYR   B CG    1 
ATOM   1597 C  CD1   . TYR   B 1 35  ? 6.450   12.327  -9.832  1.00 32.93 ? 32  TYR   B CD1   1 
ATOM   1598 C  CD2   . TYR   B 1 35  ? 7.521   11.360  -11.695 1.00 31.68 ? 32  TYR   B CD2   1 
ATOM   1599 C  CE1   . TYR   B 1 35  ? 7.641   12.891  -9.420  1.00 32.89 ? 32  TYR   B CE1   1 
ATOM   1600 C  CE2   . TYR   B 1 35  ? 8.707   11.936  -11.317 1.00 32.09 ? 32  TYR   B CE2   1 
ATOM   1601 C  CZ    . TYR   B 1 35  ? 8.772   12.697  -10.170 1.00 32.60 ? 32  TYR   B CZ    1 
ATOM   1602 O  OH    . TYR   B 1 35  ? 9.967   13.234  -9.837  1.00 32.84 ? 32  TYR   B OH    1 
ATOM   1603 N  N     . ASP   B 1 36  ? 5.530   13.251  -13.832 1.00 33.52 ? 33  ASP   B N     1 
ATOM   1604 C  CA    . ASP   B 1 36  ? 6.082   13.621  -15.132 1.00 33.38 ? 33  ASP   B CA    1 
ATOM   1605 C  C     . ASP   B 1 36  ? 6.928   12.474  -15.684 1.00 32.61 ? 33  ASP   B C     1 
ATOM   1606 O  O     . ASP   B 1 36  ? 7.962   12.152  -15.100 1.00 32.40 ? 33  ASP   B O     1 
ATOM   1607 C  CB    . ASP   B 1 36  ? 6.926   14.892  -15.040 1.00 34.16 ? 33  ASP   B CB    1 
ATOM   1608 C  CG    . ASP   B 1 36  ? 7.368   15.417  -16.391 1.00 34.56 ? 33  ASP   B CG    1 
ATOM   1609 O  OD1   . ASP   B 1 36  ? 7.491   14.603  -17.322 1.00 34.06 ? 33  ASP   B OD1   1 
ATOM   1610 O  OD2   . ASP   B 1 36  ? 7.565   16.638  -16.504 1.00 35.78 ? 33  ASP   B OD2   1 
ATOM   1611 N  N     . PRO   B 1 37  ? 6.533   11.866  -16.832 1.00 32.18 ? 34  PRO   B N     1 
ATOM   1612 C  CA    . PRO   B 1 37  ? 7.240   10.712  -17.397 1.00 31.28 ? 34  PRO   B CA    1 
ATOM   1613 C  C     . PRO   B 1 37  ? 8.607   10.959  -18.057 1.00 31.33 ? 34  PRO   B C     1 
ATOM   1614 O  O     . PRO   B 1 37  ? 9.311   9.978   -18.367 1.00 30.83 ? 34  PRO   B O     1 
ATOM   1615 C  CB    . PRO   B 1 37  ? 6.304   10.156  -18.485 1.00 31.22 ? 34  PRO   B CB    1 
ATOM   1616 C  CG    . PRO   B 1 37  ? 5.033   10.959  -18.393 1.00 31.93 ? 34  PRO   B CG    1 
ATOM   1617 C  CD    . PRO   B 1 37  ? 5.352   12.223  -17.629 1.00 32.50 ? 34  PRO   B CD    1 
ATOM   1618 N  N     . THR   B 1 38  ? 8.994   12.223  -18.258 1.00 31.82 ? 35  THR   B N     1 
ATOM   1619 C  CA    . THR   B 1 38  ? 10.257  12.538  -18.935 1.00 31.69 ? 35  THR   B CA    1 
ATOM   1620 C  C     . THR   B 1 38  ? 11.366  12.903  -17.944 1.00 31.54 ? 35  THR   B C     1 
ATOM   1621 O  O     . THR   B 1 38  ? 12.509  13.073  -18.368 1.00 31.59 ? 35  THR   B O     1 
ATOM   1622 C  CB    . THR   B 1 38  ? 10.063  13.657  -19.962 1.00 32.67 ? 35  THR   B CB    1 
ATOM   1623 O  OG1   . THR   B 1 38  ? 9.566   14.816  -19.292 1.00 33.43 ? 35  THR   B OG1   1 
ATOM   1624 C  CG2   . THR   B 1 38  ? 9.110   13.245  -21.064 1.00 32.63 ? 35  THR   B CG2   1 
ATOM   1625 N  N     . ILE   B 1 39  ? 11.050  13.021  -16.645 1.00 31.38 ? 36  ILE   B N     1 
ATOM   1626 C  CA    . ILE   B 1 39  ? 12.091  13.364  -15.650 1.00 31.38 ? 36  ILE   B CA    1 
ATOM   1627 C  C     . ILE   B 1 39  ? 12.925  12.121  -15.334 1.00 30.42 ? 36  ILE   B C     1 
ATOM   1628 O  O     . ILE   B 1 39  ? 12.407  11.107  -14.859 1.00 30.14 ? 36  ILE   B O     1 
ATOM   1629 C  CB    . ILE   B 1 39  ? 11.533  13.960  -14.345 1.00 31.70 ? 36  ILE   B CB    1 
ATOM   1630 C  CG1   . ILE   B 1 39  ? 10.801  15.273  -14.600 1.00 32.73 ? 36  ILE   B CG1   1 
ATOM   1631 C  CG2   . ILE   B 1 39  ? 12.654  14.124  -13.315 1.00 31.69 ? 36  ILE   B CG2   1 
ATOM   1632 C  CD1   . ILE   B 1 39  ? 10.063  15.797  -13.396 1.00 33.23 ? 36  ILE   B CD1   1 
ATOM   1633 N  N     . GLU   B 1 40  ? 14.228  12.254  -15.574 1.00 30.38 ? 37  GLU   B N     1 
ATOM   1634 C  CA    . GLU   B 1 40  ? 15.239  11.266  -15.238 1.00 29.93 ? 37  GLU   B CA    1 
ATOM   1635 C  C     . GLU   B 1 40  ? 16.099  11.872  -14.130 1.00 30.26 ? 37  GLU   B C     1 
ATOM   1636 O  O     . GLU   B 1 40  ? 16.730  12.908  -14.343 1.00 31.09 ? 37  GLU   B O     1 
ATOM   1637 C  CB    . GLU   B 1 40  ? 16.059  10.954  -16.492 1.00 29.68 ? 37  GLU   B CB    1 
ATOM   1638 C  CG    . GLU   B 1 40  ? 17.195  9.978   -16.291 1.00 29.28 ? 37  GLU   B CG    1 
ATOM   1639 C  CD    . GLU   B 1 40  ? 17.693  9.420   -17.614 1.00 29.08 ? 37  GLU   B CD    1 
ATOM   1640 O  OE1   . GLU   B 1 40  ? 18.773  9.865   -18.078 1.00 29.59 ? 37  GLU   B OE1   1 
ATOM   1641 O  OE2   . GLU   B 1 40  ? 16.974  8.584   -18.201 1.00 28.52 ? 37  GLU   B OE2   1 
ATOM   1642 N  N     . ASP   B 1 41  ? 16.088  11.239  -12.953 1.00 29.87 ? 38  ASP   B N     1 
ATOM   1643 C  CA    . ASP   B 1 41  ? 16.688  11.785  -11.759 1.00 30.04 ? 38  ASP   B CA    1 
ATOM   1644 C  C     . ASP   B 1 41  ? 17.165  10.645  -10.850 1.00 29.29 ? 38  ASP   B C     1 
ATOM   1645 O  O     . ASP   B 1 41  ? 16.674  9.522   -10.950 1.00 28.75 ? 38  ASP   B O     1 
ATOM   1646 C  CB    . ASP   B 1 41  ? 15.676  12.669  -11.031 1.00 30.85 ? 38  ASP   B CB    1 
ATOM   1647 C  CG    . ASP   B 1 41  ? 16.245  13.978  -10.505 1.00 32.00 ? 38  ASP   B CG    1 
ATOM   1648 O  OD1   . ASP   B 1 41  ? 17.499  14.090  -10.326 1.00 32.01 ? 38  ASP   B OD1   1 
ATOM   1649 O  OD2   . ASP   B 1 41  ? 15.421  14.889  -10.274 1.00 32.75 ? 38  ASP   B OD2   1 
ATOM   1650 N  N     . SER   B 1 42  ? 18.117  10.960  -9.968  1.00 29.31 ? 39  SER   B N     1 
ATOM   1651 C  CA    . SER   B 1 42  ? 18.726  9.999   -9.049  1.00 28.88 ? 39  SER   B CA    1 
ATOM   1652 C  C     . SER   B 1 42  ? 18.284  10.267  -7.605  1.00 29.16 ? 39  SER   B C     1 
ATOM   1653 O  O     . SER   B 1 42  ? 17.944  11.393  -7.251  1.00 29.88 ? 39  SER   B O     1 
ATOM   1654 C  CB    . SER   B 1 42  ? 20.235  10.009  -9.158  1.00 28.92 ? 39  SER   B CB    1 
ATOM   1655 O  OG    . SER   B 1 42  ? 20.777  11.253  -8.744  1.00 29.66 ? 39  SER   B OG    1 
ATOM   1656 N  N     . TYR   B 1 43  ? 18.308  9.200   -6.810  1.00 28.53 ? 40  TYR   B N     1 
ATOM   1657 C  CA    . TYR   B 1 43  ? 17.969  9.199   -5.372  1.00 28.71 ? 40  TYR   B CA    1 
ATOM   1658 C  C     . TYR   B 1 43  ? 19.033  8.383   -4.616  1.00 28.33 ? 40  TYR   B C     1 
ATOM   1659 O  O     . TYR   B 1 43  ? 19.432  7.378   -5.133  1.00 27.38 ? 40  TYR   B O     1 
ATOM   1660 C  CB    . TYR   B 1 43  ? 16.596  8.578   -5.201  1.00 28.63 ? 40  TYR   B CB    1 
ATOM   1661 C  CG    . TYR   B 1 43  ? 15.469  9.336   -5.846  1.00 29.10 ? 40  TYR   B CG    1 
ATOM   1662 C  CD1   . TYR   B 1 43  ? 15.121  9.120   -7.160  1.00 28.99 ? 40  TYR   B CD1   1 
ATOM   1663 C  CD2   . TYR   B 1 43  ? 14.732  10.252  -5.132  1.00 30.07 ? 40  TYR   B CD2   1 
ATOM   1664 C  CE1   . TYR   B 1 43  ? 14.063  9.779   -7.752  1.00 29.53 ? 40  TYR   B CE1   1 
ATOM   1665 C  CE2   . TYR   B 1 43  ? 13.659  10.915  -5.702  1.00 30.62 ? 40  TYR   B CE2   1 
ATOM   1666 C  CZ    . TYR   B 1 43  ? 13.326  10.686  -7.022  1.00 30.35 ? 40  TYR   B CZ    1 
ATOM   1667 O  OH    . TYR   B 1 43  ? 12.272  11.320  -7.605  1.00 30.99 ? 40  TYR   B OH    1 
ATOM   1668 N  N     . ARG   B 1 44  ? 19.449  8.845   -3.433  1.00 29.00 ? 41  ARG   B N     1 
ATOM   1669 C  CA    . ARG   B 1 44  ? 20.516  8.173   -2.628  1.00 29.06 ? 41  ARG   B CA    1 
ATOM   1670 C  C     . ARG   B 1 44  ? 19.963  7.859   -1.242  1.00 29.51 ? 41  ARG   B C     1 
ATOM   1671 O  O     . ARG   B 1 44  ? 19.432  8.733   -0.685  1.00 30.17 ? 41  ARG   B O     1 
ATOM   1672 C  CB    . ARG   B 1 44  ? 21.777  9.042   -2.555  1.00 29.50 ? 41  ARG   B CB    1 
ATOM   1673 C  CG    . ARG   B 1 44  ? 22.767  8.842   -3.691  1.00 29.30 ? 41  ARG   B CG    1 
ATOM   1674 C  CD    . ARG   B 1 44  ? 23.967  9.783   -3.712  1.00 30.01 ? 41  ARG   B CD    1 
ATOM   1675 N  NE    . ARG   B 1 44  ? 23.497  11.145  -3.855  1.00 30.94 ? 41  ARG   B NE    1 
ATOM   1676 C  CZ    . ARG   B 1 44  ? 22.834  11.611  -4.894  1.00 31.09 ? 41  ARG   B CZ    1 
ATOM   1677 N  NH1   . ARG   B 1 44  ? 22.384  12.851  -4.884  1.00 31.83 ? 41  ARG   B NH1   1 
ATOM   1678 N  NH2   . ARG   B 1 44  ? 22.626  10.841  -5.953  1.00 30.78 ? 41  ARG   B NH2   1 
ATOM   1679 N  N     . LYS   B 1 45  ? 20.116  6.633   -0.728  1.00 29.49 ? 42  LYS   B N     1 
ATOM   1680 C  CA    . LYS   B 1 45  ? 19.491  6.231   0.554   1.00 29.96 ? 42  LYS   B CA    1 
ATOM   1681 C  C     . LYS   B 1 45  ? 20.302  5.136   1.227   1.00 29.93 ? 42  LYS   B C     1 
ATOM   1682 O  O     . LYS   B 1 45  ? 20.417  4.076   0.602   1.00 29.51 ? 42  LYS   B O     1 
ATOM   1683 C  CB    . LYS   B 1 45  ? 18.143  5.560   0.315   1.00 29.63 ? 42  LYS   B CB    1 
ATOM   1684 C  CG    . LYS   B 1 45  ? 17.371  5.186   1.576   1.00 30.13 ? 42  LYS   B CG    1 
ATOM   1685 C  CD    . LYS   B 1 45  ? 16.069  4.507   1.303   1.00 29.76 ? 42  LYS   B CD    1 
ATOM   1686 C  CE    . LYS   B 1 45  ? 15.178  4.388   2.519   1.00 30.39 ? 42  LYS   B CE    1 
ATOM   1687 N  NZ    . LYS   B 1 45  ? 14.128  3.375   2.330   1.00 30.07 ? 42  LYS   B NZ    1 
ATOM   1688 N  N     . GLN   B 1 46  ? 20.758  5.401   2.458   1.00 30.32 ? 43  GLN   B N     1 
ATOM   1689 C  CA    . GLN   B 1 46  ? 21.508  4.498   3.311   1.00 30.43 ? 43  GLN   B CA    1 
ATOM   1690 C  C     . GLN   B 1 46  ? 20.540  3.489   3.955   1.00 30.26 ? 43  GLN   B C     1 
ATOM   1691 O  O     . GLN   B 1 46  ? 19.561  3.880   4.571   1.00 30.65 ? 43  GLN   B O     1 
ATOM   1692 C  CB    . GLN   B 1 46  ? 22.255  5.354   4.331   1.00 31.50 ? 43  GLN   B CB    1 
ATOM   1693 C  CG    . GLN   B 1 46  ? 23.157  4.606   5.285   1.00 31.98 ? 43  GLN   B CG    1 
ATOM   1694 C  CD    . GLN   B 1 46  ? 23.913  5.595   6.144   1.00 33.06 ? 43  GLN   B CD    1 
ATOM   1695 O  OE1   . GLN   B 1 46  ? 24.716  6.389   5.646   1.00 33.06 ? 43  GLN   B OE1   1 
ATOM   1696 N  NE2   . GLN   B 1 46  ? 23.638  5.558   7.440   1.00 33.84 ? 43  GLN   B NE2   1 
ATOM   1697 N  N     . VAL   B 1 47  ? 20.825  2.193   3.778   1.00 29.55 ? 44  VAL   B N     1 
ATOM   1698 C  CA    . VAL   B 1 47  ? 20.010  1.088   4.299   1.00 29.44 ? 44  VAL   B CA    1 
ATOM   1699 C  C     . VAL   B 1 47  ? 20.948  -0.023  4.769   1.00 29.12 ? 44  VAL   B C     1 
ATOM   1700 O  O     . VAL   B 1 47  ? 22.098  -0.069  4.363   1.00 29.25 ? 44  VAL   B O     1 
ATOM   1701 C  CB    . VAL   B 1 47  ? 19.031  0.532   3.245   1.00 28.95 ? 44  VAL   B CB    1 
ATOM   1702 C  CG1   . VAL   B 1 47  ? 17.935  1.533   2.912   1.00 29.03 ? 44  VAL   B CG1   1 
ATOM   1703 C  CG2   . VAL   B 1 47  ? 19.752  0.068   1.980   1.00 28.25 ? 44  VAL   B CG2   1 
ATOM   1704 N  N     . VAL   B 1 48  ? 20.433  -0.902  5.625   1.00 29.14 ? 45  VAL   B N     1 
ATOM   1705 C  CA    . VAL   B 1 48  ? 21.173  -2.055  6.136   1.00 29.16 ? 45  VAL   B CA    1 
ATOM   1706 C  C     . VAL   B 1 48  ? 20.586  -3.312  5.488   1.00 28.60 ? 45  VAL   B C     1 
ATOM   1707 O  O     . VAL   B 1 48  ? 19.408  -3.562  5.606   1.00 28.34 ? 45  VAL   B O     1 
ATOM   1708 C  CB    . VAL   B 1 48  ? 21.137  -2.121  7.677   1.00 29.96 ? 45  VAL   B CB    1 
ATOM   1709 C  CG1   . VAL   B 1 48  ? 21.855  -3.354  8.204   1.00 30.32 ? 45  VAL   B CG1   1 
ATOM   1710 C  CG2   . VAL   B 1 48  ? 21.736  -0.870  8.301   1.00 30.40 ? 45  VAL   B CG2   1 
ATOM   1711 N  N     . ILE   B 1 49  ? 21.437  -4.063  4.775   1.00 28.24 ? 46  ILE   B N     1 
ATOM   1712 C  CA    . ILE   B 1 49  ? 21.065  -5.299  4.071   1.00 27.65 ? 46  ILE   B CA    1 
ATOM   1713 C  C     . ILE   B 1 49  ? 22.076  -6.380  4.444   1.00 27.96 ? 46  ILE   B C     1 
ATOM   1714 O  O     . ILE   B 1 49  ? 23.251  -6.260  4.097   1.00 28.01 ? 46  ILE   B O     1 
ATOM   1715 C  CB    . ILE   B 1 49  ? 21.048  -5.087  2.545   1.00 26.94 ? 46  ILE   B CB    1 
ATOM   1716 C  CG1   . ILE   B 1 49  ? 20.080  -3.969  2.143   1.00 26.56 ? 46  ILE   B CG1   1 
ATOM   1717 C  CG2   . ILE   B 1 49  ? 20.727  -6.397  1.831   1.00 26.78 ? 46  ILE   B CG2   1 
ATOM   1718 C  CD1   . ILE   B 1 49  ? 20.209  -3.519  0.701   1.00 25.96 ? 46  ILE   B CD1   1 
ATOM   1719 N  N     . ASP   B 1 50  ? 21.611  -7.410  5.159   1.00 28.26 ? 47  ASP   B N     1 
ATOM   1720 C  CA    . ASP   B 1 50  ? 22.431  -8.553  5.553   1.00 28.55 ? 47  ASP   B CA    1 
ATOM   1721 C  C     . ASP   B 1 50  ? 23.610  -8.093  6.417   1.00 28.89 ? 47  ASP   B C     1 
ATOM   1722 O  O     . ASP   B 1 50  ? 24.722  -8.602  6.272   1.00 29.00 ? 47  ASP   B O     1 
ATOM   1723 C  CB    . ASP   B 1 50  ? 22.948  -9.313  4.324   1.00 28.23 ? 47  ASP   B CB    1 
ATOM   1724 C  CG    . ASP   B 1 50  ? 21.863  -9.859  3.406   1.00 27.78 ? 47  ASP   B CG    1 
ATOM   1725 O  OD1   . ASP   B 1 50  ? 20.926  -10.485 3.920   1.00 28.18 ? 47  ASP   B OD1   1 
ATOM   1726 O  OD2   . ASP   B 1 50  ? 21.964  -9.650  2.177   1.00 27.30 ? 47  ASP   B OD2   1 
ATOM   1727 N  N     . GLY   B 1 51  ? 23.352  -7.155  7.313   1.00 29.16 ? 48  GLY   B N     1 
ATOM   1728 C  CA    . GLY   B 1 51  ? 24.402  -6.687  8.236   1.00 29.77 ? 48  GLY   B CA    1 
ATOM   1729 C  C     . GLY   B 1 51  ? 25.267  -5.594  7.639   1.00 29.39 ? 48  GLY   B C     1 
ATOM   1730 O  O     . GLY   B 1 51  ? 26.054  -5.033  8.359   1.00 29.89 ? 48  GLY   B O     1 
ATOM   1731 N  N     . GLU   B 1 52  ? 25.091  -5.309  6.353   1.00 28.75 ? 49  GLU   B N     1 
ATOM   1732 C  CA    . GLU   B 1 52  ? 25.913  -4.331  5.610   1.00 28.60 ? 49  GLU   B CA    1 
ATOM   1733 C  C     . GLU   B 1 52  ? 25.220  -2.971  5.529   1.00 28.39 ? 49  GLU   B C     1 
ATOM   1734 O  O     . GLU   B 1 52  ? 24.087  -2.935  5.009   1.00 28.17 ? 49  GLU   B O     1 
ATOM   1735 C  CB    . GLU   B 1 52  ? 26.092  -4.788  4.155   1.00 28.06 ? 49  GLU   B CB    1 
ATOM   1736 C  CG    . GLU   B 1 52  ? 27.022  -3.900  3.369   1.00 27.92 ? 49  GLU   B CG    1 
ATOM   1737 C  CD    . GLU   B 1 52  ? 27.498  -4.429  2.031   1.00 27.55 ? 49  GLU   B CD    1 
ATOM   1738 O  OE1   . GLU   B 1 52  ? 26.677  -5.029  1.309   1.00 27.47 ? 49  GLU   B OE1   1 
ATOM   1739 O  OE2   . GLU   B 1 52  ? 28.691  -4.250  1.716   1.00 28.04 ? 49  GLU   B OE2   1 
ATOM   1740 N  N     . THR   B 1 53  ? 25.846  -1.906  6.000   1.00 28.74 ? 50  THR   B N     1 
ATOM   1741 C  CA    . THR   B 1 53  ? 25.241  -0.575  5.780   1.00 28.72 ? 50  THR   B CA    1 
ATOM   1742 C  C     . THR   B 1 53  ? 25.632  -0.230  4.338   1.00 28.36 ? 50  THR   B C     1 
ATOM   1743 O  O     . THR   B 1 53  ? 26.815  -0.275  4.049   1.00 28.72 ? 50  THR   B O     1 
ATOM   1744 C  CB    . THR   B 1 53  ? 25.656  0.446   6.849   1.00 29.20 ? 50  THR   B CB    1 
ATOM   1745 O  OG1   . THR   B 1 53  ? 25.157  0.045   8.122   1.00 29.73 ? 50  THR   B OG1   1 
ATOM   1746 C  CG2   . THR   B 1 53  ? 25.153  1.834   6.529   1.00 29.02 ? 50  THR   B CG2   1 
ATOM   1747 N  N     . CYS   B 1 54  ? 24.654  0.008   3.497   1.00 28.30 ? 51  CYS   B N     1 
ATOM   1748 C  CA    . CYS   B 1 54  ? 24.827  0.223   2.044   1.00 27.95 ? 51  CYS   B CA    1 
ATOM   1749 C  C     . CYS   B 1 54  ? 24.406  1.657   1.682   1.00 27.83 ? 51  CYS   B C     1 
ATOM   1750 O  O     . CYS   B 1 54  ? 23.566  2.199   2.303   1.00 27.97 ? 51  CYS   B O     1 
ATOM   1751 C  CB    . CYS   B 1 54  ? 23.891  -0.687  1.257   1.00 27.58 ? 51  CYS   B CB    1 
ATOM   1752 S  SG    . CYS   B 1 54  ? 23.932  -2.466  1.593   1.00 28.81 ? 51  CYS   B SG    1 
ATOM   1753 N  N     . LEU   B 1 55  ? 25.088  2.256   0.734   1.00 27.47 ? 52  LEU   B N     1 
ATOM   1754 C  CA    . LEU   B 1 55  ? 24.612  3.551   0.253   1.00 27.30 ? 52  LEU   B CA    1 
ATOM   1755 C  C     . LEU   B 1 55  ? 23.990  3.232   -1.106  1.00 26.36 ? 52  LEU   B C     1 
ATOM   1756 O  O     . LEU   B 1 55  ? 24.677  2.798   -1.936  1.00 25.81 ? 52  LEU   B O     1 
ATOM   1757 C  CB    . LEU   B 1 55  ? 25.814  4.478   0.122   1.00 27.81 ? 52  LEU   B CB    1 
ATOM   1758 C  CG    . LEU   B 1 55  ? 25.561  5.774   -0.631  1.00 28.05 ? 52  LEU   B CG    1 
ATOM   1759 C  CD1   . LEU   B 1 55  ? 24.373  6.488   -0.035  1.00 28.39 ? 52  LEU   B CD1   1 
ATOM   1760 C  CD2   . LEU   B 1 55  ? 26.795  6.665   -0.622  1.00 28.56 ? 52  LEU   B CD2   1 
ATOM   1761 N  N     . LEU   B 1 56  ? 22.697  3.370   -1.269  1.00 26.07 ? 53  LEU   B N     1 
ATOM   1762 C  CA    . LEU   B 1 56  ? 22.138  3.069   -2.607  1.00 25.57 ? 53  LEU   B CA    1 
ATOM   1763 C  C     . LEU   B 1 56  ? 22.119  4.368   -3.401  1.00 25.64 ? 53  LEU   B C     1 
ATOM   1764 O  O     . LEU   B 1 56  ? 21.684  5.293   -2.829  1.00 26.01 ? 53  LEU   B O     1 
ATOM   1765 C  CB    . LEU   B 1 56  ? 20.724  2.539   -2.425  1.00 25.32 ? 53  LEU   B CB    1 
ATOM   1766 C  CG    . LEU   B 1 56  ? 20.585  1.390   -1.436  1.00 25.39 ? 53  LEU   B CG    1 
ATOM   1767 C  CD1   . LEU   B 1 56  ? 19.161  0.927   -1.383  1.00 25.25 ? 53  LEU   B CD1   1 
ATOM   1768 C  CD2   . LEU   B 1 56  ? 21.505  0.241   -1.798  1.00 25.04 ? 53  LEU   B CD2   1 
ATOM   1769 N  N     . ASP   B 1 57  ? 22.570  4.355   -4.653  1.00 25.30 ? 54  ASP   B N     1 
ATOM   1770 C  CA    . ASP   B 1 57  ? 22.553  5.506   -5.593  1.00 25.54 ? 54  ASP   B CA    1 
ATOM   1771 C  C     . ASP   B 1 57  ? 21.677  5.068   -6.780  1.00 25.17 ? 54  ASP   B C     1 
ATOM   1772 O  O     . ASP   B 1 57  ? 22.179  4.436   -7.649  1.00 24.75 ? 54  ASP   B O     1 
ATOM   1773 C  CB    . ASP   B 1 57  ? 23.987  5.945   -5.904  1.00 25.92 ? 54  ASP   B CB    1 
ATOM   1774 C  CG    . ASP   B 1 57  ? 24.087  7.223   -6.713  1.00 26.38 ? 54  ASP   B CG    1 
ATOM   1775 O  OD1   . ASP   B 1 57  ? 23.074  7.792   -7.011  1.00 26.56 ? 54  ASP   B OD1   1 
ATOM   1776 O  OD2   . ASP   B 1 57  ? 25.157  7.582   -7.028  1.00 26.78 ? 54  ASP   B OD2   1 
ATOM   1777 N  N     . ILE   B 1 58  ? 20.394  5.401   -6.763  1.00 25.14 ? 55  ILE   B N     1 
ATOM   1778 C  CA    . ILE   B 1 58  ? 19.395  4.879   -7.730  1.00 24.88 ? 55  ILE   B CA    1 
ATOM   1779 C  C     . ILE   B 1 58  ? 19.071  5.893   -8.834  1.00 25.23 ? 55  ILE   B C     1 
ATOM   1780 O  O     . ILE   B 1 58  ? 18.582  6.962   -8.520  1.00 25.60 ? 55  ILE   B O     1 
ATOM   1781 C  CB    . ILE   B 1 58  ? 18.110  4.482   -6.985  1.00 24.90 ? 55  ILE   B CB    1 
ATOM   1782 C  CG1   . ILE   B 1 58  ? 18.362  3.570   -5.790  1.00 24.88 ? 55  ILE   B CG1   1 
ATOM   1783 C  CG2   . ILE   B 1 58  ? 17.096  3.870   -7.901  1.00 24.61 ? 55  ILE   B CG2   1 
ATOM   1784 C  CD1   . ILE   B 1 58  ? 17.124  3.333   -5.023  1.00 24.91 ? 55  ILE   B CD1   1 
ATOM   1785 N  N     . LEU   B 1 59  ? 19.276  5.492   -10.077 1.00 24.88 ? 56  LEU   B N     1 
ATOM   1786 C  CA    . LEU   B 1 59  ? 18.899  6.315   -11.215 1.00 25.34 ? 56  LEU   B CA    1 
ATOM   1787 C  C     . LEU   B 1 59  ? 17.574  5.817   -11.806 1.00 25.17 ? 56  LEU   B C     1 
ATOM   1788 O  O     . LEU   B 1 59  ? 17.487  4.683   -12.305 1.00 25.09 ? 56  LEU   B O     1 
ATOM   1789 C  CB    . LEU   B 1 59  ? 20.009  6.300   -12.268 1.00 25.31 ? 56  LEU   B CB    1 
ATOM   1790 C  CG    . LEU   B 1 59  ? 19.711  7.119   -13.529 1.00 25.62 ? 56  LEU   B CG    1 
ATOM   1791 C  CD1   . LEU   B 1 59  ? 19.468  8.586   -13.207 1.00 26.08 ? 56  LEU   B CD1   1 
ATOM   1792 C  CD2   . LEU   B 1 59  ? 20.839  6.982   -14.540 1.00 25.74 ? 56  LEU   B CD2   1 
ATOM   1793 N  N     . ASP   B 1 60  ? 16.563  6.691   -11.737 1.00 25.65 ? 57  ASP   B N     1 
ATOM   1794 C  CA    . ASP   B 1 60  ? 15.235  6.497   -12.286 1.00 25.77 ? 57  ASP   B CA    1 
ATOM   1795 C  C     . ASP   B 1 60  ? 15.208  7.036   -13.726 1.00 26.11 ? 57  ASP   B C     1 
ATOM   1796 O  O     . ASP   B 1 60  ? 15.287  8.242   -13.948 1.00 26.58 ? 57  ASP   B O     1 
ATOM   1797 C  CB    . ASP   B 1 60  ? 14.184  7.189   -11.413 1.00 26.22 ? 57  ASP   B CB    1 
ATOM   1798 C  CG    . ASP   B 1 60  ? 12.770  7.181   -11.979 1.00 26.34 ? 57  ASP   B CG    1 
ATOM   1799 O  OD1   . ASP   B 1 60  ? 12.361  6.174   -12.620 1.00 26.05 ? 57  ASP   B OD1   1 
ATOM   1800 O  OD2   . ASP   B 1 60  ? 12.066  8.183   -11.758 1.00 26.93 ? 57  ASP   B OD2   1 
ATOM   1801 N  N     . THR   B 1 61  ? 15.075  6.130   -14.701 1.00 26.06 ? 58  THR   B N     1 
ATOM   1802 C  CA    . THR   B 1 61  ? 15.253  6.487   -16.118 1.00 26.40 ? 58  THR   B CA    1 
ATOM   1803 C  C     . THR   B 1 61  ? 13.914  6.885   -16.747 1.00 27.12 ? 58  THR   B C     1 
ATOM   1804 O  O     . THR   B 1 61  ? 12.853  6.339   -16.378 1.00 27.15 ? 58  THR   B O     1 
ATOM   1805 C  CB    . THR   B 1 61  ? 15.919  5.355   -16.918 1.00 25.87 ? 58  THR   B CB    1 
ATOM   1806 O  OG1   . THR   B 1 61  ? 15.055  4.216   -17.019 1.00 25.24 ? 58  THR   B OG1   1 
ATOM   1807 C  CG2   . THR   B 1 61  ? 17.239  4.944   -16.306 1.00 25.66 ? 58  THR   B CG2   1 
ATOM   1808 N  N     . ALA   B 1 62  ? 13.995  7.781   -17.743 1.00 28.19 ? 59  ALA   B N     1 
ATOM   1809 C  CA    . ALA   B 1 62  ? 12.843  8.323   -18.457 1.00 28.99 ? 59  ALA   B CA    1 
ATOM   1810 C  C     . ALA   B 1 62  ? 13.195  8.589   -19.929 1.00 29.95 ? 59  ALA   B C     1 
ATOM   1811 O  O     . ALA   B 1 62  ? 12.924  7.751   -20.780 1.00 30.41 ? 59  ALA   B O     1 
ATOM   1812 C  CB    . ALA   B 1 62  ? 12.391  9.598   -17.785 1.00 29.64 ? 59  ALA   B CB    1 
ATOM   1813 N  N     . TYR   B 1 67  ? 16.764  7.730   -28.917 1.00 31.59 ? 64  TYR   B N     1 
ATOM   1814 C  CA    . TYR   B 1 67  ? 18.235  7.589   -28.731 1.00 31.34 ? 64  TYR   B CA    1 
ATOM   1815 C  C     . TYR   B 1 67  ? 18.803  8.688   -27.830 1.00 31.15 ? 64  TYR   B C     1 
ATOM   1816 O  O     . TYR   B 1 67  ? 18.467  9.839   -28.024 1.00 31.82 ? 64  TYR   B O     1 
ATOM   1817 C  CB    . TYR   B 1 67  ? 19.011  7.703   -30.057 1.00 32.11 ? 64  TYR   B CB    1 
ATOM   1818 C  CG    . TYR   B 1 67  ? 20.506  7.836   -29.858 1.00 32.26 ? 64  TYR   B CG    1 
ATOM   1819 C  CD1   . TYR   B 1 67  ? 21.285  6.748   -29.508 1.00 31.76 ? 64  TYR   B CD1   1 
ATOM   1820 C  CD2   . TYR   B 1 67  ? 21.125  9.069   -29.812 1.00 32.76 ? 64  TYR   B CD2   1 
ATOM   1821 C  CE1   . TYR   B 1 67  ? 22.643  6.858   -29.249 1.00 31.81 ? 64  TYR   B CE1   1 
ATOM   1822 C  CE2   . TYR   B 1 67  ? 22.492  9.185   -29.566 1.00 32.73 ? 64  TYR   B CE2   1 
ATOM   1823 C  CZ    . TYR   B 1 67  ? 23.272  8.086   -29.269 1.00 32.16 ? 64  TYR   B CZ    1 
ATOM   1824 O  OH    . TYR   B 1 67  ? 24.631  8.181   -29.000 1.00 31.77 ? 64  TYR   B OH    1 
ATOM   1825 N  N     . SER   B 1 68  ? 19.600  8.293   -26.833 1.00 30.28 ? 65  SER   B N     1 
ATOM   1826 C  CA    . SER   B 1 68  ? 20.396  9.251   -26.050 1.00 29.91 ? 65  SER   B CA    1 
ATOM   1827 C  C     . SER   B 1 68  ? 21.779  8.634   -25.830 1.00 29.17 ? 65  SER   B C     1 
ATOM   1828 O  O     . SER   B 1 68  ? 21.828  7.502   -25.534 1.00 28.46 ? 65  SER   B O     1 
ATOM   1829 C  CB    . SER   B 1 68  ? 19.712  9.580   -24.778 1.00 29.70 ? 65  SER   B CB    1 
ATOM   1830 O  OG    . SER   B 1 68  ? 20.474  10.457  -23.995 1.00 30.19 ? 65  SER   B OG    1 
ATOM   1831 N  N     . ALA   B 1 69  ? 22.856  9.392   -25.990 1.00 29.21 ? 66  ALA   B N     1 
ATOM   1832 C  CA    . ALA   B 1 69  ? 24.201  8.895   -25.616 1.00 28.72 ? 66  ALA   B CA    1 
ATOM   1833 C  C     . ALA   B 1 69  ? 24.284  8.698   -24.088 1.00 27.88 ? 66  ALA   B C     1 
ATOM   1834 O  O     . ALA   B 1 69  ? 25.156  8.010   -23.629 1.00 27.36 ? 66  ALA   B O     1 
ATOM   1835 C  CB    . ALA   B 1 69  ? 25.255  9.873   -26.057 1.00 29.34 ? 66  ALA   B CB    1 
ATOM   1836 N  N     . MET   B 1 70  ? 23.402  9.347   -23.346 1.00 27.65 ? 67  MET   B N     1 
ATOM   1837 C  CA    . MET   B 1 70  ? 23.413  9.235   -21.890 1.00 27.26 ? 67  MET   B CA    1 
ATOM   1838 C  C     . MET   B 1 70  ? 22.930  7.850   -21.455 1.00 26.88 ? 67  MET   B C     1 
ATOM   1839 O  O     . MET   B 1 70  ? 23.168  7.473   -20.332 1.00 26.33 ? 67  MET   B O     1 
ATOM   1840 C  CB    . MET   B 1 70  ? 22.552  10.320  -21.243 1.00 27.29 ? 67  MET   B CB    1 
ATOM   1841 C  CG    . MET   B 1 70  ? 23.011  11.727  -21.553 1.00 27.95 ? 67  MET   B CG    1 
ATOM   1842 S  SD    . MET   B 1 70  ? 24.752  12.016  -21.140 1.00 28.05 ? 67  MET   B SD    1 
ATOM   1843 C  CE    . MET   B 1 70  ? 24.719  11.831  -19.358 1.00 27.59 ? 67  MET   B CE    1 
ATOM   1844 N  N     . ARG   B 1 71  ? 22.277  7.099   -22.353 1.00 27.21 ? 68  ARG   B N     1 
ATOM   1845 C  CA    . ARG   B 1 71  ? 21.782  5.774   -22.016 1.00 27.32 ? 68  ARG   B CA    1 
ATOM   1846 C  C     . ARG   B 1 71  ? 22.950  4.801   -21.901 1.00 27.04 ? 68  ARG   B C     1 
ATOM   1847 O  O     . ARG   B 1 71  ? 23.093  4.118   -20.877 1.00 26.49 ? 68  ARG   B O     1 
ATOM   1848 C  CB    . ARG   B 1 71  ? 20.727  5.295   -23.012 1.00 27.99 ? 68  ARG   B CB    1 
ATOM   1849 C  CG    . ARG   B 1 71  ? 19.439  6.094   -22.900 1.00 28.76 ? 68  ARG   B CG    1 
ATOM   1850 C  CD    . ARG   B 1 71  ? 18.180  5.305   -23.226 1.00 29.24 ? 68  ARG   B CD    1 
ATOM   1851 N  NE    . ARG   B 1 71  ? 17.080  6.249   -23.420 1.00 30.08 ? 68  ARG   B NE    1 
ATOM   1852 C  CZ    . ARG   B 1 71  ? 16.571  6.610   -24.597 1.00 31.30 ? 68  ARG   B CZ    1 
ATOM   1853 N  NH1   . ARG   B 1 71  ? 16.968  6.021   -25.716 1.00 31.71 ? 68  ARG   B NH1   1 
ATOM   1854 N  NH2   . ARG   B 1 71  ? 15.665  7.581   -24.656 1.00 32.24 ? 68  ARG   B NH2   1 
ATOM   1855 N  N     . ASP   B 1 72  ? 23.794  4.762   -22.929 1.00 27.23 ? 69  ASP   B N     1 
ATOM   1856 C  CA    . ASP   B 1 72  ? 24.996  3.935   -22.870 1.00 27.32 ? 69  ASP   B CA    1 
ATOM   1857 C  C     . ASP   B 1 72  ? 25.845  4.330   -21.649 1.00 26.77 ? 69  ASP   B C     1 
ATOM   1858 O  O     . ASP   B 1 72  ? 26.502  3.477   -21.057 1.00 26.43 ? 69  ASP   B O     1 
ATOM   1859 C  CB    . ASP   B 1 72  ? 25.798  4.015   -24.175 1.00 28.19 ? 69  ASP   B CB    1 
ATOM   1860 C  CG    . ASP   B 1 72  ? 25.346  3.036   -25.252 1.00 28.76 ? 69  ASP   B CG    1 
ATOM   1861 O  OD1   . ASP   B 1 72  ? 24.235  2.468   -25.133 1.00 28.91 ? 69  ASP   B OD1   1 
ATOM   1862 O  OD2   . ASP   B 1 72  ? 26.109  2.844   -26.217 1.00 29.83 ? 69  ASP   B OD2   1 
ATOM   1863 N  N     . GLN   B 1 73  ? 25.821  5.614   -21.270 1.00 26.60 ? 70  GLN   B N     1 
ATOM   1864 C  CA    . GLN   B 1 73  ? 26.599  6.092   -20.149 1.00 26.47 ? 70  GLN   B CA    1 
ATOM   1865 C  C     . GLN   B 1 73  ? 26.103  5.458   -18.845 1.00 25.82 ? 70  GLN   B C     1 
ATOM   1866 O  O     . GLN   B 1 73  ? 26.917  4.961   -18.066 1.00 25.64 ? 70  GLN   B O     1 
ATOM   1867 C  CB    . GLN   B 1 73  ? 26.560  7.615   -20.032 1.00 26.92 ? 70  GLN   B CB    1 
ATOM   1868 C  CG    . GLN   B 1 73  ? 27.334  8.136   -18.825 1.00 26.96 ? 70  GLN   B CG    1 
ATOM   1869 C  CD    . GLN   B 1 73  ? 28.777  7.687   -18.847 1.00 27.04 ? 70  GLN   B CD    1 
ATOM   1870 O  OE1   . GLN   B 1 73  ? 29.543  8.045   -19.735 1.00 27.65 ? 70  GLN   B OE1   1 
ATOM   1871 N  NE2   . GLN   B 1 73  ? 29.156  6.867   -17.881 1.00 26.78 ? 70  GLN   B NE2   1 
ATOM   1872 N  N     . TYR   B 1 74  ? 24.786  5.470   -18.606 1.00 25.63 ? 71  TYR   B N     1 
ATOM   1873 C  CA    . TYR   B 1 74  ? 24.280  4.928   -17.333 1.00 25.29 ? 71  TYR   B CA    1 
ATOM   1874 C  C     . TYR   B 1 74  ? 24.364  3.404   -17.319 1.00 25.06 ? 71  TYR   B C     1 
ATOM   1875 O  O     . TYR   B 1 74  ? 24.447  2.785   -16.245 1.00 24.59 ? 71  TYR   B O     1 
ATOM   1876 C  CB    . TYR   B 1 74  ? 22.912  5.494   -16.934 1.00 25.32 ? 71  TYR   B CB    1 
ATOM   1877 C  CG    . TYR   B 1 74  ? 21.687  5.247   -17.782 1.00 25.35 ? 71  TYR   B CG    1 
ATOM   1878 C  CD1   . TYR   B 1 74  ? 21.202  3.974   -18.053 1.00 24.97 ? 71  TYR   B CD1   1 
ATOM   1879 C  CD2   . TYR   B 1 74  ? 20.915  6.329   -18.175 1.00 25.80 ? 71  TYR   B CD2   1 
ATOM   1880 C  CE1   . TYR   B 1 74  ? 20.029  3.795   -18.769 1.00 25.20 ? 71  TYR   B CE1   1 
ATOM   1881 C  CE2   . TYR   B 1 74  ? 19.740  6.170   -18.889 1.00 25.86 ? 71  TYR   B CE2   1 
ATOM   1882 C  CZ    . TYR   B 1 74  ? 19.301  4.898   -19.192 1.00 25.57 ? 71  TYR   B CZ    1 
ATOM   1883 O  OH    . TYR   B 1 74  ? 18.147  4.766   -19.898 1.00 25.80 ? 71  TYR   B OH    1 
ATOM   1884 N  N     . MET   B 1 75  ? 24.458  2.819   -18.516 1.00 25.10 ? 72  MET   B N     1 
ATOM   1885 C  CA    . MET   B 1 75  ? 24.645  1.359   -18.648 1.00 24.89 ? 72  MET   B CA    1 
ATOM   1886 C  C     . MET   B 1 75  ? 26.102  1.024   -18.343 1.00 25.06 ? 72  MET   B C     1 
ATOM   1887 O  O     . MET   B 1 75  ? 26.349  -0.038  -17.851 1.00 24.99 ? 72  MET   B O     1 
ATOM   1888 C  CB    . MET   B 1 75  ? 24.223  0.859   -20.026 1.00 25.07 ? 72  MET   B CB    1 
ATOM   1889 C  CG    . MET   B 1 75  ? 22.740  0.745   -20.141 1.00 24.93 ? 72  MET   B CG    1 
ATOM   1890 S  SD    . MET   B 1 75  ? 22.078  0.076   -21.644 1.00 25.38 ? 72  MET   B SD    1 
ATOM   1891 C  CE    . MET   B 1 75  ? 20.404  0.663   -21.501 1.00 25.16 ? 72  MET   B CE    1 
ATOM   1892 N  N     . ARG   B 1 76  ? 27.022  1.913   -18.695 1.00 25.33 ? 73  ARG   B N     1 
ATOM   1893 C  CA    . ARG   B 1 76  ? 28.431  1.685   -18.343 1.00 25.51 ? 73  ARG   B CA    1 
ATOM   1894 C  C     . ARG   B 1 76  ? 28.491  1.853   -16.822 1.00 25.45 ? 73  ARG   B C     1 
ATOM   1895 O  O     . ARG   B 1 76  ? 29.050  1.043   -16.179 1.00 25.47 ? 73  ARG   B O     1 
ATOM   1896 C  CB    . ARG   B 1 76  ? 29.321  2.658   -19.111 1.00 25.87 ? 73  ARG   B CB    1 
ATOM   1897 C  CG    . ARG   B 1 76  ? 29.424  2.339   -20.593 1.00 26.23 ? 73  ARG   B CG    1 
ATOM   1898 C  CD    . ARG   B 1 76  ? 30.536  3.085   -21.284 1.00 26.81 ? 73  ARG   B CD    1 
ATOM   1899 N  NE    . ARG   B 1 76  ? 30.351  4.506   -21.186 1.00 27.12 ? 73  ARG   B NE    1 
ATOM   1900 C  CZ    . ARG   B 1 76  ? 29.769  5.236   -22.087 1.00 27.33 ? 73  ARG   B CZ    1 
ATOM   1901 N  NH1   . ARG   B 1 76  ? 29.355  4.668   -23.198 1.00 27.54 ? 73  ARG   B NH1   1 
ATOM   1902 N  NH2   . ARG   B 1 76  ? 29.647  6.527   -21.883 1.00 27.70 ? 73  ARG   B NH2   1 
ATOM   1903 N  N     . THR   B 1 77  ? 27.831  2.886   -16.320 1.00 25.60 ? 74  THR   B N     1 
ATOM   1904 C  CA    . THR   B 1 77  ? 27.842  3.312   -14.901 1.00 25.56 ? 74  THR   B CA    1 
ATOM   1905 C  C     . THR   B 1 77  ? 27.074  2.359   -13.970 1.00 25.19 ? 74  THR   B C     1 
ATOM   1906 O  O     . THR   B 1 77  ? 27.624  2.038   -12.949 1.00 25.44 ? 74  THR   B O     1 
ATOM   1907 C  CB    . THR   B 1 77  ? 27.568  4.824   -14.829 1.00 25.82 ? 74  THR   B CB    1 
ATOM   1908 O  OG1   . THR   B 1 77  ? 28.618  5.470   -15.542 1.00 26.16 ? 74  THR   B OG1   1 
ATOM   1909 C  CG2   . THR   B 1 77  ? 27.535  5.351   -13.414 1.00 25.90 ? 74  THR   B CG2   1 
ATOM   1910 N  N     . GLY   B 1 78  ? 25.904  1.896   -14.366 1.00 25.05 ? 75  GLY   B N     1 
ATOM   1911 C  CA    . GLY   B 1 78  ? 25.044  1.050   -13.531 1.00 24.89 ? 75  GLY   B CA    1 
ATOM   1912 C  C     . GLY   B 1 78  ? 25.710  -0.252  -13.104 1.00 25.00 ? 75  GLY   B C     1 
ATOM   1913 O  O     . GLY   B 1 78  ? 26.259  -0.940  -13.946 1.00 24.95 ? 75  GLY   B O     1 
ATOM   1914 N  N     . GLU   B 1 79  ? 25.621  -0.572  -11.815 1.00 25.20 ? 76  GLU   B N     1 
ATOM   1915 C  CA    . GLU   B 1 79  ? 26.162  -1.864  -11.326 1.00 25.42 ? 76  GLU   B CA    1 
ATOM   1916 C  C     . GLU   B 1 79  ? 25.096  -2.959  -11.368 1.00 25.36 ? 76  GLU   B C     1 
ATOM   1917 O  O     . GLU   B 1 79  ? 25.481  -4.079  -11.570 1.00 25.29 ? 76  GLU   B O     1 
ATOM   1918 C  CB    . GLU   B 1 79  ? 26.749  -1.663  -9.949  1.00 25.80 ? 76  GLU   B CB    1 
ATOM   1919 C  CG    . GLU   B 1 79  ? 28.079  -0.988  -10.082 1.00 26.55 ? 76  GLU   B CG    1 
ATOM   1920 C  CD    . GLU   B 1 79  ? 28.595  -0.279  -8.864  1.00 27.17 ? 76  GLU   B CD    1 
ATOM   1921 O  OE1   . GLU   B 1 79  ? 28.174  -0.606  -7.790  1.00 27.22 ? 76  GLU   B OE1   1 
ATOM   1922 O  OE2   . GLU   B 1 79  ? 29.423  0.612   -9.057  1.00 28.30 ? 76  GLU   B OE2   1 
ATOM   1923 N  N     . GLY   B 1 80  ? 23.848  -2.603  -11.125 1.00 25.14 ? 77  GLY   B N     1 
ATOM   1924 C  CA    . GLY   B 1 80  ? 22.695  -3.505  -11.087 1.00 24.95 ? 77  GLY   B CA    1 
ATOM   1925 C  C     . GLY   B 1 80  ? 21.505  -2.858  -11.738 1.00 24.74 ? 77  GLY   B C     1 
ATOM   1926 O  O     . GLY   B 1 80  ? 21.328  -1.687  -11.577 1.00 24.85 ? 77  GLY   B O     1 
ATOM   1927 N  N     . PHE   B 1 81  ? 20.686  -3.650  -12.405 1.00 24.53 ? 78  PHE   B N     1 
ATOM   1928 C  CA    . PHE   B 1 81  ? 19.545  -3.123  -13.182 1.00 24.46 ? 78  PHE   B CA    1 
ATOM   1929 C  C     . PHE   B 1 81  ? 18.199  -3.739  -12.781 1.00 24.38 ? 78  PHE   B C     1 
ATOM   1930 O  O     . PHE   B 1 81  ? 18.088  -4.934  -12.741 1.00 24.80 ? 78  PHE   B O     1 
ATOM   1931 C  CB    . PHE   B 1 81  ? 19.883  -3.338  -14.660 1.00 24.48 ? 78  PHE   B CB    1 
ATOM   1932 C  CG    . PHE   B 1 81  ? 21.095  -2.592  -15.148 1.00 24.40 ? 78  PHE   B CG    1 
ATOM   1933 C  CD1   . PHE   B 1 81  ? 22.381  -3.090  -15.012 1.00 24.75 ? 78  PHE   B CD1   1 
ATOM   1934 C  CD2   . PHE   B 1 81  ? 20.955  -1.347  -15.711 1.00 24.45 ? 78  PHE   B CD2   1 
ATOM   1935 C  CE1   . PHE   B 1 81  ? 23.478  -2.376  -15.468 1.00 24.89 ? 78  PHE   B CE1   1 
ATOM   1936 C  CE2   . PHE   B 1 81  ? 22.045  -0.621  -16.133 1.00 24.68 ? 78  PHE   B CE2   1 
ATOM   1937 C  CZ    . PHE   B 1 81  ? 23.302  -1.145  -16.041 1.00 24.77 ? 78  PHE   B CZ    1 
ATOM   1938 N  N     . LEU   B 1 82  ? 17.221  -2.894  -12.470 1.00 24.57 ? 79  LEU   B N     1 
ATOM   1939 C  CA    . LEU   B 1 82  ? 15.821  -3.306  -12.221 1.00 24.45 ? 79  LEU   B CA    1 
ATOM   1940 C  C     . LEU   B 1 82  ? 15.093  -3.219  -13.564 1.00 24.62 ? 79  LEU   B C     1 
ATOM   1941 O  O     . LEU   B 1 82  ? 14.859  -2.116  -13.993 1.00 24.47 ? 79  LEU   B O     1 
ATOM   1942 C  CB    . LEU   B 1 82  ? 15.107  -2.349  -11.257 1.00 24.74 ? 79  LEU   B CB    1 
ATOM   1943 C  CG    . LEU   B 1 82  ? 15.225  -2.574  -9.756  1.00 24.96 ? 79  LEU   B CG    1 
ATOM   1944 C  CD1   . LEU   B 1 82  ? 14.262  -1.697  -9.015  1.00 25.11 ? 79  LEU   B CD1   1 
ATOM   1945 C  CD2   . LEU   B 1 82  ? 14.967  -4.011  -9.368  1.00 25.09 ? 79  LEU   B CD2   1 
ATOM   1946 N  N     . CYS   B 1 83  ? 14.768  -4.354  -14.175 1.00 24.63 ? 80  CYS   B N     1 
ATOM   1947 C  CA    . CYS   B 1 83  ? 13.982  -4.387  -15.434 1.00 24.87 ? 80  CYS   B CA    1 
ATOM   1948 C  C     . CYS   B 1 83  ? 12.505  -4.537  -15.104 1.00 24.43 ? 80  CYS   B C     1 
ATOM   1949 O  O     . CYS   B 1 83  ? 12.083  -5.635  -14.789 1.00 24.53 ? 80  CYS   B O     1 
ATOM   1950 C  CB    . CYS   B 1 83  ? 14.493  -5.478  -16.349 1.00 25.34 ? 80  CYS   B CB    1 
ATOM   1951 S  SG    . CYS   B 1 83  ? 16.216  -5.189  -16.764 1.00 26.69 ? 80  CYS   B SG    1 
ATOM   1952 N  N     . VAL   B 1 84  ? 11.760  -3.432  -15.199 1.00 24.05 ? 81  VAL   B N     1 
ATOM   1953 C  CA    . VAL   B 1 84  ? 10.347  -3.322  -14.768 1.00 23.86 ? 81  VAL   B CA    1 
ATOM   1954 C  C     . VAL   B 1 84  ? 9.380   -3.404  -15.940 1.00 23.73 ? 81  VAL   B C     1 
ATOM   1955 O  O     . VAL   B 1 84  ? 9.557   -2.737  -16.912 1.00 24.01 ? 81  VAL   B O     1 
ATOM   1956 C  CB    . VAL   B 1 84  ? 10.104  -2.011  -13.984 1.00 23.86 ? 81  VAL   B CB    1 
ATOM   1957 C  CG1   . VAL   B 1 84  ? 8.697   -1.886  -13.448 1.00 24.13 ? 81  VAL   B CG1   1 
ATOM   1958 C  CG2   . VAL   B 1 84  ? 11.098  -1.809  -12.866 1.00 23.99 ? 81  VAL   B CG2   1 
ATOM   1959 N  N     . PHE   B 1 85  ? 8.374   -4.219  -15.773 1.00 23.64 ? 82  PHE   B N     1 
ATOM   1960 C  CA    . PHE   B 1 85  ? 7.225   -4.266  -16.696 1.00 23.70 ? 82  PHE   B CA    1 
ATOM   1961 C  C     . PHE   B 1 85  ? 5.952   -4.141  -15.839 1.00 23.70 ? 82  PHE   B C     1 
ATOM   1962 O  O     . PHE   B 1 85  ? 6.031   -4.265  -14.645 1.00 23.71 ? 82  PHE   B O     1 
ATOM   1963 C  CB    . PHE   B 1 85  ? 7.287   -5.519  -17.574 1.00 23.79 ? 82  PHE   B CB    1 
ATOM   1964 C  CG    . PHE   B 1 85  ? 6.932   -6.779  -16.824 1.00 23.56 ? 82  PHE   B CG    1 
ATOM   1965 C  CD1   . PHE   B 1 85  ? 5.621   -7.157  -16.645 1.00 23.55 ? 82  PHE   B CD1   1 
ATOM   1966 C  CD2   . PHE   B 1 85  ? 7.915   -7.534  -16.235 1.00 23.47 ? 82  PHE   B CD2   1 
ATOM   1967 C  CE1   . PHE   B 1 85  ? 5.300   -8.292  -15.919 1.00 23.60 ? 82  PHE   B CE1   1 
ATOM   1968 C  CE2   . PHE   B 1 85  ? 7.595   -8.673  -15.523 1.00 23.51 ? 82  PHE   B CE2   1 
ATOM   1969 C  CZ    . PHE   B 1 85  ? 6.295   -9.043  -15.370 1.00 23.59 ? 82  PHE   B CZ    1 
ATOM   1970 N  N     . ALA   B 1 86  ? 4.819   -3.808  -16.423 1.00 23.84 ? 83  ALA   B N     1 
ATOM   1971 C  CA    . ALA   B 1 86  ? 3.550   -3.766  -15.689 1.00 23.98 ? 83  ALA   B CA    1 
ATOM   1972 C  C     . ALA   B 1 86  ? 2.769   -5.040  -16.008 1.00 24.07 ? 83  ALA   B C     1 
ATOM   1973 O  O     . ALA   B 1 86  ? 2.762   -5.445  -17.180 1.00 24.45 ? 83  ALA   B O     1 
ATOM   1974 C  CB    . ALA   B 1 86  ? 2.772   -2.521  -16.062 1.00 24.15 ? 83  ALA   B CB    1 
ATOM   1975 N  N     . ILE   B 1 87  ? 2.145   -5.667  -14.993 1.00 24.10 ? 84  ILE   B N     1 
ATOM   1976 C  CA    . ILE   B 1 87  ? 1.445   -6.956  -15.170 1.00 24.37 ? 84  ILE   B CA    1 
ATOM   1977 C  C     . ILE   B 1 87  ? 0.168   -6.805  -16.004 1.00 24.68 ? 84  ILE   B C     1 
ATOM   1978 O  O     . ILE   B 1 87  ? -0.334  -7.804  -16.494 1.00 24.94 ? 84  ILE   B O     1 
ATOM   1979 C  CB    . ILE   B 1 87  ? 1.098   -7.670  -13.841 1.00 24.37 ? 84  ILE   B CB    1 
ATOM   1980 C  CG1   . ILE   B 1 87  ? 0.222   -6.816  -12.925 1.00 24.47 ? 84  ILE   B CG1   1 
ATOM   1981 C  CG2   . ILE   B 1 87  ? 2.345   -8.168  -13.131 1.00 24.26 ? 84  ILE   B CG2   1 
ATOM   1982 C  CD1   . ILE   B 1 87  ? -0.897  -7.598  -12.276 1.00 24.77 ? 84  ILE   B CD1   1 
ATOM   1983 N  N     . ASN   B 1 88  ? -0.355  -5.581  -16.143 1.00 24.81 ? 85  ASN   B N     1 
ATOM   1984 C  CA    . ASN   B 1 88  ? -1.544  -5.308  -16.952 1.00 25.06 ? 85  ASN   B CA    1 
ATOM   1985 C  C     . ASN   B 1 88  ? -1.160  -4.754  -18.328 1.00 25.24 ? 85  ASN   B C     1 
ATOM   1986 O  O     . ASN   B 1 88  ? -2.014  -4.238  -19.026 1.00 25.72 ? 85  ASN   B O     1 
ATOM   1987 C  CB    . ASN   B 1 88  ? -2.486  -4.327  -16.252 1.00 24.99 ? 85  ASN   B CB    1 
ATOM   1988 C  CG    . ASN   B 1 88  ? -1.878  -2.949  -16.159 1.00 24.82 ? 85  ASN   B CG    1 
ATOM   1989 O  OD1   . ASN   B 1 88  ? -0.659  -2.834  -16.055 1.00 24.28 ? 85  ASN   B OD1   1 
ATOM   1990 N  ND2   . ASN   B 1 88  ? -2.707  -1.918  -16.205 1.00 24.98 ? 85  ASN   B ND2   1 
ATOM   1991 N  N     . ASN   B 1 89  ? 0.107   -4.899  -18.689 1.00 25.22 ? 86  ASN   B N     1 
ATOM   1992 C  CA    . ASN   B 1 89  ? 0.597   -4.452  -20.020 1.00 25.55 ? 86  ASN   B CA    1 
ATOM   1993 C  C     . ASN   B 1 89  ? 1.564   -5.459  -20.657 1.00 25.54 ? 86  ASN   B C     1 
ATOM   1994 O  O     . ASN   B 1 89  ? 2.732   -5.515  -20.290 1.00 25.09 ? 86  ASN   B O     1 
ATOM   1995 C  CB    . ASN   B 1 89  ? 1.129   -3.024  -20.083 1.00 25.78 ? 86  ASN   B CB    1 
ATOM   1996 C  CG    . ASN   B 1 89  ? 1.409   -2.645  -21.519 1.00 26.14 ? 86  ASN   B CG    1 
ATOM   1997 O  OD1   . ASN   B 1 89  ? 2.505   -2.823  -22.019 1.00 26.16 ? 86  ASN   B OD1   1 
ATOM   1998 N  ND2   . ASN   B 1 89  ? 0.402   -2.190  -22.207 1.00 26.75 ? 86  ASN   B ND2   1 
ATOM   1999 N  N     . THR   B 1 90  ? 1.056   -6.185  -21.636 1.00 25.89 ? 87  THR   B N     1 
ATOM   2000 C  CA    . THR   B 1 90  ? 1.828   -7.216  -22.349 1.00 26.08 ? 87  THR   B CA    1 
ATOM   2001 C  C     . THR   B 1 90  ? 3.010   -6.623  -23.116 1.00 26.02 ? 87  THR   B C     1 
ATOM   2002 O  O     . THR   B 1 90  ? 4.023   -7.215  -23.121 1.00 26.10 ? 87  THR   B O     1 
ATOM   2003 C  CB    . THR   B 1 90  ? 0.920   -8.197  -23.088 1.00 26.53 ? 87  THR   B CB    1 
ATOM   2004 O  OG1   . THR   B 1 90  ? 0.271   -8.889  -22.038 1.00 26.52 ? 87  THR   B OG1   1 
ATOM   2005 C  CG2   . THR   B 1 90  ? 1.698   -9.210  -23.890 1.00 26.78 ? 87  THR   B CG2   1 
ATOM   2006 N  N     . LYS   B 1 91  ? 2.856   -5.468  -23.730 1.00 26.27 ? 88  LYS   B N     1 
ATOM   2007 C  CA    . LYS   B 1 91  ? 3.968   -4.902  -24.521 1.00 26.30 ? 88  LYS   B CA    1 
ATOM   2008 C  C     . LYS   B 1 91  ? 5.155   -4.558  -23.621 1.00 25.69 ? 88  LYS   B C     1 
ATOM   2009 O  O     . LYS   B 1 91  ? 6.282   -4.762  -24.015 1.00 25.63 ? 88  LYS   B O     1 
ATOM   2010 C  CB    . LYS   B 1 91  ? 3.448   -3.690  -25.289 1.00 26.92 ? 88  LYS   B CB    1 
ATOM   2011 C  CG    . LYS   B 1 91  ? 4.491   -2.968  -26.102 1.00 27.39 ? 88  LYS   B CG    1 
ATOM   2012 C  CD    . LYS   B 1 91  ? 5.161   -3.842  -27.125 1.00 28.00 ? 88  LYS   B CD    1 
ATOM   2013 C  CE    . LYS   B 1 91  ? 5.981   -3.074  -28.142 1.00 28.54 ? 88  LYS   B CE    1 
ATOM   2014 N  NZ    . LYS   B 1 91  ? 7.147   -2.384  -27.554 1.00 28.35 ? 88  LYS   B NZ    1 
ATOM   2015 N  N     . SER   B 1 92  ? 4.876   -4.099  -22.407 1.00 25.02 ? 89  SER   B N     1 
ATOM   2016 C  CA    . SER   B 1 92  ? 5.953   -3.756  -21.516 1.00 24.58 ? 89  SER   B CA    1 
ATOM   2017 C  C     . SER   B 1 92  ? 6.763   -5.023  -21.194 1.00 24.53 ? 89  SER   B C     1 
ATOM   2018 O  O     . SER   B 1 92  ? 7.973   -4.958  -21.068 1.00 24.31 ? 89  SER   B O     1 
ATOM   2019 C  CB    . SER   B 1 92  ? 5.458   -3.024  -20.274 1.00 24.19 ? 89  SER   B CB    1 
ATOM   2020 O  OG    . SER   B 1 92  ? 4.714   -3.862  -19.413 1.00 24.09 ? 89  SER   B OG    1 
ATOM   2021 N  N     . PHE   B 1 93  ? 6.084   -6.172  -21.115 1.00 24.86 ? 90  PHE   B N     1 
ATOM   2022 C  CA    . PHE   B 1 93  ? 6.729   -7.444  -20.804 1.00 25.29 ? 90  PHE   B CA    1 
ATOM   2023 C  C     . PHE   B 1 93  ? 7.552   -7.889  -22.016 1.00 26.02 ? 90  PHE   B C     1 
ATOM   2024 O  O     . PHE   B 1 93  ? 8.722   -8.281  -21.897 1.00 26.27 ? 90  PHE   B O     1 
ATOM   2025 C  CB    . PHE   B 1 93  ? 5.705   -8.505  -20.389 1.00 25.30 ? 90  PHE   B CB    1 
ATOM   2026 C  CG    . PHE   B 1 93  ? 6.296   -9.869  -20.113 1.00 25.54 ? 90  PHE   B CG    1 
ATOM   2027 C  CD1   . PHE   B 1 93  ? 7.146   -10.073 -19.030 1.00 25.34 ? 90  PHE   B CD1   1 
ATOM   2028 C  CD2   . PHE   B 1 93  ? 6.030   -10.944 -20.951 1.00 25.94 ? 90  PHE   B CD2   1 
ATOM   2029 C  CE1   . PHE   B 1 93  ? 7.714   -11.321 -18.799 1.00 25.58 ? 90  PHE   B CE1   1 
ATOM   2030 C  CE2   . PHE   B 1 93  ? 6.588   -12.196 -20.711 1.00 26.19 ? 90  PHE   B CE2   1 
ATOM   2031 C  CZ    . PHE   B 1 93  ? 7.422   -12.383 -19.632 1.00 26.10 ? 90  PHE   B CZ    1 
ATOM   2032 N  N     . GLU   B 1 94  ? 6.930   -7.783  -23.191 1.00 27.06 ? 91  GLU   B N     1 
ATOM   2033 C  CA    . GLU   B 1 94  ? 7.537   -8.215  -24.424 1.00 27.96 ? 91  GLU   B CA    1 
ATOM   2034 C  C     . GLU   B 1 94  ? 8.787   -7.385  -24.720 1.00 27.82 ? 91  GLU   B C     1 
ATOM   2035 O  O     . GLU   B 1 94  ? 9.663   -7.893  -25.390 1.00 28.39 ? 91  GLU   B O     1 
ATOM   2036 C  CB    . GLU   B 1 94  ? 6.521   -8.216  -25.569 1.00 28.91 ? 91  GLU   B CB    1 
ATOM   2037 C  CG    . GLU   B 1 94  ? 5.540   -9.378  -25.445 1.00 29.61 ? 91  GLU   B CG    1 
ATOM   2038 C  CD    . GLU   B 1 94  ? 4.489   -9.470  -26.534 1.00 30.97 ? 91  GLU   B CD    1 
ATOM   2039 O  OE1   . GLU   B 1 94  ? 4.087   -8.407  -27.067 1.00 31.44 ? 91  GLU   B OE1   1 
ATOM   2040 O  OE2   . GLU   B 1 94  ? 4.071   -10.603 -26.857 1.00 32.10 ? 91  GLU   B OE2   1 
ATOM   2041 N  N     . ASP   B 1 95  ? 8.884   -6.195  -24.127 1.00 27.42 ? 92  ASP   B N     1 
ATOM   2042 C  CA    . ASP   B 1 95  ? 9.991   -5.230  -24.326 1.00 27.15 ? 92  ASP   B CA    1 
ATOM   2043 C  C     . ASP   B 1 95  ? 11.239  -5.547  -23.501 1.00 26.84 ? 92  ASP   B C     1 
ATOM   2044 O  O     . ASP   B 1 95  ? 12.246  -5.031  -23.806 1.00 27.00 ? 92  ASP   B O     1 
ATOM   2045 C  CB    . ASP   B 1 95  ? 9.588   -3.880  -23.764 1.00 27.16 ? 92  ASP   B CB    1 
ATOM   2046 C  CG    . ASP   B 1 95  ? 9.040   -2.938  -24.797 1.00 27.77 ? 92  ASP   B CG    1 
ATOM   2047 O  OD1   . ASP   B 1 95  ? 8.868   -3.375  -25.913 1.00 28.26 ? 92  ASP   B OD1   1 
ATOM   2048 O  OD2   . ASP   B 1 95  ? 8.775   -1.803  -24.441 1.00 28.09 ? 92  ASP   B OD2   1 
ATOM   2049 N  N     . ILE   B 1 96  ? 11.099  -6.345  -22.463 1.00 26.37 ? 93  ILE   B N     1 
ATOM   2050 C  CA    . ILE   B 1 96  ? 12.147  -6.591  -21.456 1.00 25.97 ? 93  ILE   B CA    1 
ATOM   2051 C  C     . ILE   B 1 96  ? 13.434  -7.077  -22.148 1.00 26.31 ? 93  ILE   B C     1 
ATOM   2052 O  O     . ILE   B 1 96  ? 14.504  -6.570  -21.905 1.00 26.07 ? 93  ILE   B O     1 
ATOM   2053 C  CB    . ILE   B 1 96  ? 11.650  -7.597  -20.391 1.00 25.67 ? 93  ILE   B CB    1 
ATOM   2054 C  CG1   . ILE   B 1 96  ? 10.560  -6.984  -19.507 1.00 25.43 ? 93  ILE   B CG1   1 
ATOM   2055 C  CG2   . ILE   B 1 96  ? 12.797  -8.156  -19.556 1.00 25.48 ? 93  ILE   B CG2   1 
ATOM   2056 C  CD1   . ILE   B 1 96  ? 11.029  -5.869  -18.606 1.00 25.18 ? 93  ILE   B CD1   1 
ATOM   2057 N  N     . HIS   B 1 97  ? 13.320  -8.067  -23.026 1.00 26.98 ? 94  HIS   B N     1 
ATOM   2058 C  CA    . HIS   B 1 97  ? 14.505  -8.657  -23.655 1.00 27.64 ? 94  HIS   B CA    1 
ATOM   2059 C  C     . HIS   B 1 97  ? 15.366  -7.593  -24.369 1.00 27.62 ? 94  HIS   B C     1 
ATOM   2060 O  O     . HIS   B 1 97  ? 16.588  -7.733  -24.401 1.00 27.62 ? 94  HIS   B O     1 
ATOM   2061 C  CB    . HIS   B 1 97  ? 14.106  -9.814  -24.587 1.00 28.39 ? 94  HIS   B CB    1 
ATOM   2062 C  CG    . HIS   B 1 97  ? 13.614  -9.392  -25.928 1.00 29.16 ? 94  HIS   B CG    1 
ATOM   2063 N  ND1   . HIS   B 1 97  ? 12.293  -9.010  -26.152 1.00 29.30 ? 94  HIS   B ND1   1 
ATOM   2064 C  CD2   . HIS   B 1 97  ? 14.250  -9.294  -27.118 1.00 29.77 ? 94  HIS   B CD2   1 
ATOM   2065 C  CE1   . HIS   B 1 97  ? 12.136  -8.702  -27.428 1.00 29.82 ? 94  HIS   B CE1   1 
ATOM   2066 N  NE2   . HIS   B 1 97  ? 13.314  -8.880  -28.044 1.00 30.32 ? 94  HIS   B NE2   1 
ATOM   2067 N  N     . HIS   B 1 98  ? 14.739  -6.549  -24.937 1.00 27.81 ? 95  HIS   B N     1 
ATOM   2068 C  CA    . HIS   B 1 98  ? 15.481  -5.441  -25.584 1.00 28.16 ? 95  HIS   B CA    1 
ATOM   2069 C  C     . HIS   B 1 98  ? 16.388  -4.732  -24.564 1.00 27.79 ? 95  HIS   B C     1 
ATOM   2070 O  O     . HIS   B 1 98  ? 17.550  -4.470  -24.868 1.00 27.98 ? 95  HIS   B O     1 
ATOM   2071 C  CB    . HIS   B 1 98  ? 14.558  -4.409  -26.242 1.00 28.47 ? 95  HIS   B CB    1 
ATOM   2072 C  CG    . HIS   B 1 98  ? 13.671  -4.938  -27.321 1.00 29.12 ? 95  HIS   B CG    1 
ATOM   2073 N  ND1   . HIS   B 1 98  ? 14.155  -5.531  -28.468 1.00 29.95 ? 95  HIS   B ND1   1 
ATOM   2074 C  CD2   . HIS   B 1 98  ? 12.324  -4.917  -27.445 1.00 29.42 ? 95  HIS   B CD2   1 
ATOM   2075 C  CE1   . HIS   B 1 98  ? 13.142  -5.871  -29.248 1.00 30.43 ? 95  HIS   B CE1   1 
ATOM   2076 N  NE2   . HIS   B 1 98  ? 12.002  -5.509  -28.633 1.00 30.17 ? 95  HIS   B NE2   1 
ATOM   2077 N  N     . TYR   B 1 99  ? 15.856  -4.432  -23.368 1.00 27.60 ? 96  TYR   B N     1 
ATOM   2078 C  CA    . TYR   B 1 99  ? 16.638  -3.846  -22.263 1.00 27.39 ? 96  TYR   B CA    1 
ATOM   2079 C  C     . TYR   B 1 99  ? 17.803  -4.758  -21.870 1.00 27.57 ? 96  TYR   B C     1 
ATOM   2080 O  O     . TYR   B 1 99  ? 18.924  -4.280  -21.738 1.00 27.76 ? 96  TYR   B O     1 
ATOM   2081 C  CB    . TYR   B 1 99  ? 15.757  -3.523  -21.050 1.00 27.24 ? 96  TYR   B CB    1 
ATOM   2082 C  CG    . TYR   B 1 99  ? 14.797  -2.397  -21.312 1.00 27.37 ? 96  TYR   B CG    1 
ATOM   2083 C  CD1   . TYR   B 1 99  ? 15.259  -1.107  -21.511 1.00 27.71 ? 96  TYR   B CD1   1 
ATOM   2084 C  CD2   . TYR   B 1 99  ? 13.431  -2.623  -21.402 1.00 27.55 ? 96  TYR   B CD2   1 
ATOM   2085 C  CE1   . TYR   B 1 99  ? 14.390  -0.064  -21.792 1.00 27.90 ? 96  TYR   B CE1   1 
ATOM   2086 C  CE2   . TYR   B 1 99  ? 12.546  -1.589  -21.676 1.00 27.90 ? 96  TYR   B CE2   1 
ATOM   2087 C  CZ    . TYR   B 1 99  ? 13.029  -0.304  -21.868 1.00 27.97 ? 96  TYR   B CZ    1 
ATOM   2088 O  OH    . TYR   B 1 99  ? 12.166  0.711   -22.161 1.00 28.54 ? 96  TYR   B OH    1 
ATOM   2089 N  N     . ARG   B 1 100 ? 17.551  -6.061  -21.701 1.00 27.63 ? 97  ARG   B N     1 
ATOM   2090 C  CA    . ARG   B 1 100 ? 18.621  -6.986  -21.320 1.00 28.15 ? 97  ARG   B CA    1 
ATOM   2091 C  C     . ARG   B 1 100 ? 19.672  -7.063  -22.434 1.00 28.24 ? 97  ARG   B C     1 
ATOM   2092 O  O     . ARG   B 1 100 ? 20.856  -7.139  -22.154 1.00 28.24 ? 97  ARG   B O     1 
ATOM   2093 C  CB    . ARG   B 1 100 ? 18.094  -8.386  -20.978 1.00 28.71 ? 97  ARG   B CB    1 
ATOM   2094 C  CG    . ARG   B 1 100 ? 19.188  -9.311  -20.458 1.00 29.34 ? 97  ARG   B CG    1 
ATOM   2095 C  CD    . ARG   B 1 100 ? 18.794  -10.768 -20.312 1.00 30.36 ? 97  ARG   B CD    1 
ATOM   2096 N  NE    . ARG   B 1 100 ? 19.955  -11.588 -19.961 1.00 31.13 ? 97  ARG   B NE    1 
ATOM   2097 C  CZ    . ARG   B 1 100 ? 20.552  -11.577 -18.771 1.00 31.29 ? 97  ARG   B CZ    1 
ATOM   2098 N  NH1   . ARG   B 1 100 ? 20.033  -10.891 -17.766 1.00 31.03 ? 97  ARG   B NH1   1 
ATOM   2099 N  NH2   . ARG   B 1 100 ? 21.674  -12.253 -18.595 1.00 32.07 ? 97  ARG   B NH2   1 
ATOM   2100 N  N     . GLU   B 1 101 ? 19.238  -7.044  -23.695 1.00 28.74 ? 98  GLU   B N     1 
ATOM   2101 C  CA    . GLU   B 1 101 ? 20.180  -7.069  -24.824 1.00 29.67 ? 98  GLU   B CA    1 
ATOM   2102 C  C     . GLU   B 1 101 ? 21.069  -5.814  -24.847 1.00 29.09 ? 98  GLU   B C     1 
ATOM   2103 O  O     . GLU   B 1 101 ? 22.288  -5.918  -25.009 1.00 29.31 ? 98  GLU   B O     1 
ATOM   2104 C  CB    . GLU   B 1 101 ? 19.425  -7.288  -26.139 1.00 30.73 ? 98  GLU   B CB    1 
ATOM   2105 C  CG    . GLU   B 1 101 ? 19.027  -8.735  -26.313 1.00 31.64 ? 98  GLU   B CG    1 
ATOM   2106 C  CD    . GLU   B 1 101 ? 20.222  -9.666  -26.179 1.00 32.69 ? 98  GLU   B CD    1 
ATOM   2107 O  OE1   . GLU   B 1 101 ? 21.137  -9.564  -27.019 1.00 33.88 ? 98  GLU   B OE1   1 
ATOM   2108 O  OE2   . GLU   B 1 101 ? 20.254  -10.484 -25.231 1.00 33.44 ? 98  GLU   B OE2   1 
ATOM   2109 N  N     . GLN   B 1 102 ? 20.469  -4.637  -24.658 1.00 28.70 ? 99  GLN   B N     1 
ATOM   2110 C  CA    . GLN   B 1 102 ? 21.218  -3.369  -24.654 1.00 28.56 ? 99  GLN   B CA    1 
ATOM   2111 C  C     . GLN   B 1 102 ? 22.273  -3.381  -23.544 1.00 27.92 ? 99  GLN   B C     1 
ATOM   2112 O  O     . GLN   B 1 102 ? 23.420  -3.011  -23.793 1.00 28.40 ? 99  GLN   B O     1 
ATOM   2113 C  CB    . GLN   B 1 102 ? 20.286  -2.171  -24.472 1.00 28.75 ? 99  GLN   B CB    1 
ATOM   2114 C  CG    . GLN   B 1 102 ? 19.426  -1.911  -25.696 1.00 29.32 ? 99  GLN   B CG    1 
ATOM   2115 C  CD    . GLN   B 1 102 ? 18.446  -0.774  -25.521 1.00 29.60 ? 99  GLN   B CD    1 
ATOM   2116 O  OE1   . GLN   B 1 102 ? 17.985  -0.471  -24.417 1.00 29.53 ? 99  GLN   B OE1   1 
ATOM   2117 N  NE2   . GLN   B 1 102 ? 18.117  -0.133  -26.629 1.00 30.10 ? 99  GLN   B NE2   1 
ATOM   2118 N  N     . ILE   B 1 103 ? 21.896  -3.832  -22.338 1.00 26.96 ? 100 ILE   B N     1 
ATOM   2119 C  CA    . ILE   B 1 103 ? 22.807  -3.799  -21.189 1.00 26.26 ? 100 ILE   B CA    1 
ATOM   2120 C  C     . ILE   B 1 103 ? 23.947  -4.800  -21.403 1.00 26.47 ? 100 ILE   B C     1 
ATOM   2121 O  O     . ILE   B 1 103 ? 25.106  -4.470  -21.195 1.00 26.10 ? 100 ILE   B O     1 
ATOM   2122 C  CB    . ILE   B 1 103 ? 22.062  -4.060  -19.871 1.00 25.74 ? 100 ILE   B CB    1 
ATOM   2123 C  CG1   . ILE   B 1 103 ? 20.944  -3.042  -19.644 1.00 25.43 ? 100 ILE   B CG1   1 
ATOM   2124 C  CG2   . ILE   B 1 103 ? 23.051  -4.053  -18.710 1.00 25.62 ? 100 ILE   B CG2   1 
ATOM   2125 C  CD1   . ILE   B 1 103 ? 19.925  -3.458  -18.606 1.00 25.20 ? 100 ILE   B CD1   1 
ATOM   2126 N  N     . LYS   B 1 104 ? 23.596  -6.029  -21.791 1.00 26.79 ? 101 LYS   B N     1 
ATOM   2127 C  CA    . LYS   B 1 104 ? 24.580  -7.042  -22.149 1.00 27.59 ? 101 LYS   B CA    1 
ATOM   2128 C  C     . LYS   B 1 104 ? 25.570  -6.463  -23.173 1.00 28.00 ? 101 LYS   B C     1 
ATOM   2129 O  O     . LYS   B 1 104 ? 26.765  -6.681  -23.056 1.00 28.17 ? 101 LYS   B O     1 
ATOM   2130 C  CB    . LYS   B 1 104 ? 23.912  -8.321  -22.677 1.00 28.15 ? 101 LYS   B CB    1 
ATOM   2131 C  CG    . LYS   B 1 104 ? 23.523  -9.354  -21.617 1.00 28.40 ? 101 LYS   B CG    1 
ATOM   2132 C  CD    . LYS   B 1 104 ? 22.875  -10.656 -22.149 1.00 29.00 ? 101 LYS   B CD    1 
ATOM   2133 C  CE    . LYS   B 1 104 ? 23.105  -10.915 -23.628 1.00 29.86 ? 101 LYS   B CE    1 
ATOM   2134 N  NZ    . LYS   B 1 104 ? 22.647  -12.255 -24.087 1.00 30.61 ? 101 LYS   B NZ    1 
ATOM   2135 N  N     . ARG   B 1 105 ? 25.069  -5.720  -24.170 1.00 28.19 ? 102 ARG   B N     1 
ATOM   2136 C  CA    . ARG   B 1 105 ? 25.942  -5.144  -25.207 1.00 28.78 ? 102 ARG   B CA    1 
ATOM   2137 C  C     . ARG   B 1 105 ? 26.929  -4.148  -24.583 1.00 28.05 ? 102 ARG   B C     1 
ATOM   2138 O  O     . ARG   B 1 105 ? 28.131  -4.282  -24.766 1.00 28.35 ? 102 ARG   B O     1 
ATOM   2139 C  CB    . ARG   B 1 105 ? 25.140  -4.478  -26.332 1.00 29.57 ? 102 ARG   B CB    1 
ATOM   2140 C  CG    . ARG   B 1 105 ? 26.023  -3.881  -27.421 1.00 30.63 ? 102 ARG   B CG    1 
ATOM   2141 C  CD    . ARG   B 1 105 ? 25.340  -3.702  -28.772 1.00 31.76 ? 102 ARG   B CD    1 
ATOM   2142 N  NE    . ARG   B 1 105 ? 25.032  -2.298  -29.067 1.00 32.33 ? 102 ARG   B NE    1 
ATOM   2143 C  CZ    . ARG   B 1 105 ? 24.703  -1.815  -30.275 1.00 33.30 ? 102 ARG   B CZ    1 
ATOM   2144 N  NH1   . ARG   B 1 105 ? 24.530  -0.506  -30.441 1.00 33.35 ? 102 ARG   B NH1   1 
ATOM   2145 N  NH2   . ARG   B 1 105 ? 24.554  -2.633  -31.310 1.00 34.15 ? 102 ARG   B NH2   1 
ATOM   2146 N  N     . VAL   B 1 106 ? 26.409  -3.169  -23.837 1.00 27.21 ? 103 VAL   B N     1 
ATOM   2147 C  CA    . VAL   B 1 106 ? 27.228  -2.133  -23.187 1.00 26.84 ? 103 VAL   B CA    1 
ATOM   2148 C  C     . VAL   B 1 106 ? 28.249  -2.791  -22.240 1.00 26.61 ? 103 VAL   B C     1 
ATOM   2149 O  O     . VAL   B 1 106 ? 29.439  -2.446  -22.273 1.00 26.71 ? 103 VAL   B O     1 
ATOM   2150 C  CB    . VAL   B 1 106 ? 26.341  -1.082  -22.478 1.00 26.43 ? 103 VAL   B CB    1 
ATOM   2151 C  CG1   . VAL   B 1 106 ? 27.148  -0.129  -21.598 1.00 26.31 ? 103 VAL   B CG1   1 
ATOM   2152 C  CG2   . VAL   B 1 106 ? 25.509  -0.296  -23.483 1.00 26.58 ? 103 VAL   B CG2   1 
ATOM   2153 N  N     . LYS   B 1 107 ? 27.795  -3.761  -21.437 1.00 26.40 ? 104 LYS   B N     1 
ATOM   2154 C  CA    . LYS   B 1 107 ? 28.654  -4.448  -20.475 1.00 26.60 ? 104 LYS   B CA    1 
ATOM   2155 C  C     . LYS   B 1 107 ? 29.611  -5.414  -21.183 1.00 27.57 ? 104 LYS   B C     1 
ATOM   2156 O  O     . LYS   B 1 107 ? 30.703  -5.693  -20.658 1.00 27.74 ? 104 LYS   B O     1 
ATOM   2157 C  CB    . LYS   B 1 107 ? 27.824  -5.209  -19.438 1.00 26.19 ? 104 LYS   B CB    1 
ATOM   2158 C  CG    . LYS   B 1 107 ? 26.949  -4.343  -18.550 1.00 25.59 ? 104 LYS   B CG    1 
ATOM   2159 C  CD    . LYS   B 1 107 ? 27.755  -3.392  -17.693 1.00 25.55 ? 104 LYS   B CD    1 
ATOM   2160 C  CE    . LYS   B 1 107 ? 26.893  -2.738  -16.642 1.00 25.16 ? 104 LYS   B CE    1 
ATOM   2161 N  NZ    . LYS   B 1 107 ? 27.545  -1.546  -16.066 1.00 25.27 ? 104 LYS   B NZ    1 
ATOM   2162 N  N     . ASP   B 1 108 ? 29.208  -5.918  -22.360 1.00 28.37 ? 105 ASP   B N     1 
ATOM   2163 C  CA    . ASP   B 1 108 ? 29.968  -6.932  -23.090 1.00 29.27 ? 105 ASP   B CA    1 
ATOM   2164 C  C     . ASP   B 1 108 ? 30.181  -8.141  -22.177 1.00 29.51 ? 105 ASP   B C     1 
ATOM   2165 O  O     . ASP   B 1 108 ? 31.257  -8.722  -22.180 1.00 29.83 ? 105 ASP   B O     1 
ATOM   2166 C  CB    . ASP   B 1 108 ? 31.320  -6.398  -23.576 1.00 29.93 ? 105 ASP   B CB    1 
ATOM   2167 C  CG    . ASP   B 1 108 ? 32.124  -7.390  -24.415 1.00 30.91 ? 105 ASP   B CG    1 
ATOM   2168 O  OD1   . ASP   B 1 108 ? 31.495  -8.239  -25.079 1.00 31.22 ? 105 ASP   B OD1   1 
ATOM   2169 O  OD2   . ASP   B 1 108 ? 33.377  -7.317  -24.386 1.00 31.49 ? 105 ASP   B OD2   1 
ATOM   2170 N  N     . SER   B 1 109 ? 29.143  -8.498  -21.411 1.00 29.55 ? 106 SER   B N     1 
ATOM   2171 C  CA    . SER   B 1 109 ? 29.212  -9.571  -20.410 1.00 29.91 ? 106 SER   B CA    1 
ATOM   2172 C  C     . SER   B 1 109 ? 27.833  -10.199 -20.202 1.00 29.75 ? 106 SER   B C     1 
ATOM   2173 O  O     . SER   B 1 109 ? 26.819  -9.518  -20.353 1.00 29.43 ? 106 SER   B O     1 
ATOM   2174 C  CB    . SER   B 1 109 ? 29.749  -9.023  -19.112 1.00 29.84 ? 106 SER   B CB    1 
ATOM   2175 O  OG    . SER   B 1 109 ? 29.811  -10.024 -18.109 1.00 30.23 ? 106 SER   B OG    1 
ATOM   2176 N  N     . GLU   B 1 110 ? 27.809  -11.488 -19.835 1.00 30.30 ? 107 GLU   B N     1 
ATOM   2177 C  CA    . GLU   B 1 110 ? 26.578  -12.138 -19.385 1.00 30.30 ? 107 GLU   B CA    1 
ATOM   2178 C  C     . GLU   B 1 110 ? 26.393  -11.947 -17.880 1.00 29.62 ? 107 GLU   B C     1 
ATOM   2179 O  O     . GLU   B 1 110 ? 25.313  -12.203 -17.384 1.00 29.43 ? 107 GLU   B O     1 
ATOM   2180 C  CB    . GLU   B 1 110 ? 26.531  -13.634 -19.707 1.00 31.60 ? 107 GLU   B CB    1 
ATOM   2181 C  CG    . GLU   B 1 110 ? 25.580  -13.971 -20.846 1.00 32.24 ? 107 GLU   B CG    1 
ATOM   2182 C  CD    . GLU   B 1 110 ? 26.065  -13.445 -22.176 1.00 33.10 ? 107 GLU   B CD    1 
ATOM   2183 O  OE1   . GLU   B 1 110 ? 27.300  -13.400 -22.360 1.00 34.29 ? 107 GLU   B OE1   1 
ATOM   2184 O  OE2   . GLU   B 1 110 ? 25.223  -13.086 -23.029 1.00 33.70 ? 107 GLU   B OE2   1 
ATOM   2185 N  N     . ASP   B 1 111 ? 27.435  -11.497 -17.171 1.00 29.40 ? 108 ASP   B N     1 
ATOM   2186 C  CA    . ASP   B 1 111 ? 27.370  -11.304 -15.712 1.00 28.80 ? 108 ASP   B CA    1 
ATOM   2187 C  C     . ASP   B 1 111 ? 26.759  -9.942  -15.392 1.00 28.05 ? 108 ASP   B C     1 
ATOM   2188 O  O     . ASP   B 1 111 ? 27.449  -9.042  -14.941 1.00 28.17 ? 108 ASP   B O     1 
ATOM   2189 C  CB    . ASP   B 1 111 ? 28.757  -11.386 -15.071 1.00 29.19 ? 108 ASP   B CB    1 
ATOM   2190 C  CG    . ASP   B 1 111 ? 29.324  -12.792 -15.026 1.00 30.08 ? 108 ASP   B CG    1 
ATOM   2191 O  OD1   . ASP   B 1 111 ? 28.589  -13.736 -15.409 1.00 30.64 ? 108 ASP   B OD1   1 
ATOM   2192 O  OD2   . ASP   B 1 111 ? 30.497  -12.940 -14.597 1.00 30.35 ? 108 ASP   B OD2   1 
ATOM   2193 N  N     . VAL   B 1 112 ? 25.453  -9.795  -15.614 1.00 27.36 ? 109 VAL   B N     1 
ATOM   2194 C  CA    . VAL   B 1 112 ? 24.794  -8.534  -15.342 1.00 26.59 ? 109 VAL   B CA    1 
ATOM   2195 C  C     . VAL   B 1 112 ? 23.876  -8.691  -14.140 1.00 26.26 ? 109 VAL   B C     1 
ATOM   2196 O  O     . VAL   B 1 112 ? 22.872  -9.393  -14.259 1.00 26.39 ? 109 VAL   B O     1 
ATOM   2197 C  CB    . VAL   B 1 112 ? 23.995  -8.068  -16.564 1.00 26.42 ? 109 VAL   B CB    1 
ATOM   2198 C  CG1   . VAL   B 1 112 ? 23.433  -6.674  -16.337 1.00 26.04 ? 109 VAL   B CG1   1 
ATOM   2199 C  CG2   . VAL   B 1 112 ? 24.843  -8.124  -17.820 1.00 26.69 ? 109 VAL   B CG2   1 
ATOM   2200 N  N     . PRO   B 1 113 ? 24.173  -8.040  -12.986 1.00 25.91 ? 110 PRO   B N     1 
ATOM   2201 C  CA    . PRO   B 1 113 ? 23.252  -8.054  -11.849 1.00 25.83 ? 110 PRO   B CA    1 
ATOM   2202 C  C     . PRO   B 1 113 ? 21.915  -7.451  -12.300 1.00 25.50 ? 110 PRO   B C     1 
ATOM   2203 O  O     . PRO   B 1 113 ? 21.865  -6.309  -12.772 1.00 25.13 ? 110 PRO   B O     1 
ATOM   2204 C  CB    . PRO   B 1 113 ? 23.963  -7.237  -10.763 1.00 25.65 ? 110 PRO   B CB    1 
ATOM   2205 C  CG    . PRO   B 1 113 ? 25.410  -7.308  -11.154 1.00 25.98 ? 110 PRO   B CG    1 
ATOM   2206 C  CD    . PRO   B 1 113 ? 25.402  -7.297  -12.670 1.00 26.02 ? 110 PRO   B CD    1 
ATOM   2207 N  N     . MET   B 1 114 ? 20.883  -8.265  -12.184 1.00 25.71 ? 111 MET   B N     1 
ATOM   2208 C  CA    . MET   B 1 114 ? 19.594  -7.879  -12.747 1.00 25.55 ? 111 MET   B CA    1 
ATOM   2209 C  C     . MET   B 1 114 ? 18.464  -8.621  -12.031 1.00 25.28 ? 111 MET   B C     1 
ATOM   2210 O  O     . MET   B 1 114 ? 18.688  -9.735  -11.619 1.00 25.49 ? 111 MET   B O     1 
ATOM   2211 C  CB    . MET   B 1 114 ? 19.636  -8.281  -14.222 1.00 26.40 ? 111 MET   B CB    1 
ATOM   2212 C  CG    . MET   B 1 114 ? 18.525  -7.758  -15.048 1.00 26.67 ? 111 MET   B CG    1 
ATOM   2213 S  SD    . MET   B 1 114 ? 18.829  -8.017  -16.832 1.00 27.81 ? 111 MET   B SD    1 
ATOM   2214 C  CE    . MET   B 1 114 ? 20.294  -7.047  -17.099 1.00 27.82 ? 111 MET   B CE    1 
ATOM   2215 N  N     . VAL   B 1 115 ? 17.333  -7.945  -11.853 1.00 24.55 ? 112 VAL   B N     1 
ATOM   2216 C  CA    . VAL   B 1 115 ? 16.109  -8.461  -11.275 1.00 24.31 ? 112 VAL   B CA    1 
ATOM   2217 C  C     . VAL   B 1 115 ? 14.955  -8.051  -12.194 1.00 23.91 ? 112 VAL   B C     1 
ATOM   2218 O  O     . VAL   B 1 115 ? 14.851  -6.902  -12.558 1.00 23.84 ? 112 VAL   B O     1 
ATOM   2219 C  CB    . VAL   B 1 115 ? 15.894  -7.928  -9.846  1.00 24.23 ? 112 VAL   B CB    1 
ATOM   2220 C  CG1   . VAL   B 1 115 ? 14.591  -8.441  -9.264  1.00 24.29 ? 112 VAL   B CG1   1 
ATOM   2221 C  CG2   . VAL   B 1 115 ? 17.071  -8.258  -8.934  1.00 24.44 ? 112 VAL   B CG2   1 
ATOM   2222 N  N     . LEU   B 1 116 ? 14.097  -9.017  -12.541 1.00 23.87 ? 113 LEU   B N     1 
ATOM   2223 C  CA    . LEU   B 1 116 ? 12.864  -8.774  -13.290 1.00 23.67 ? 113 LEU   B CA    1 
ATOM   2224 C  C     . LEU   B 1 116 ? 11.736  -8.408  -12.331 1.00 23.40 ? 113 LEU   B C     1 
ATOM   2225 O  O     . LEU   B 1 116 ? 11.495  -9.151  -11.376 1.00 23.67 ? 113 LEU   B O     1 
ATOM   2226 C  CB    . LEU   B 1 116 ? 12.476  -10.040 -14.061 1.00 24.03 ? 113 LEU   B CB    1 
ATOM   2227 C  CG    . LEU   B 1 116 ? 11.308  -9.890  -15.034 1.00 24.03 ? 113 LEU   B CG    1 
ATOM   2228 C  CD1   . LEU   B 1 116 ? 11.623  -8.851  -16.111 1.00 23.93 ? 113 LEU   B CD1   1 
ATOM   2229 C  CD2   . LEU   B 1 116 ? 10.940  -11.219 -15.667 1.00 24.47 ? 113 LEU   B CD2   1 
ATOM   2230 N  N     . VAL   B 1 117 ? 11.031  -7.307  -12.618 1.00 23.15 ? 114 VAL   B N     1 
ATOM   2231 C  CA    . VAL   B 1 117 ? 10.001  -6.778  -11.721 1.00 23.26 ? 114 VAL   B CA    1 
ATOM   2232 C  C     . VAL   B 1 117 ? 8.696   -6.598  -12.488 1.00 23.32 ? 114 VAL   B C     1 
ATOM   2233 O  O     . VAL   B 1 117 ? 8.645   -5.866  -13.473 1.00 23.46 ? 114 VAL   B O     1 
ATOM   2234 C  CB    . VAL   B 1 117 ? 10.434  -5.461  -11.054 1.00 23.15 ? 114 VAL   B CB    1 
ATOM   2235 C  CG1   . VAL   B 1 117 ? 9.301   -4.838  -10.263 1.00 23.30 ? 114 VAL   B CG1   1 
ATOM   2236 C  CG2   . VAL   B 1 117 ? 11.647  -5.668  -10.157 1.00 23.25 ? 114 VAL   B CG2   1 
ATOM   2237 N  N     . GLY   B 1 118 ? 7.660   -7.307  -12.025 1.00 23.45 ? 115 GLY   B N     1 
ATOM   2238 C  CA    . GLY   B 1 118 ? 6.308   -7.146  -12.501 1.00 23.54 ? 115 GLY   B CA    1 
ATOM   2239 C  C     . GLY   B 1 118 ? 5.558   -6.214  -11.578 1.00 23.64 ? 115 GLY   B C     1 
ATOM   2240 O  O     . GLY   B 1 118 ? 5.132   -6.617  -10.498 1.00 23.85 ? 115 GLY   B O     1 
ATOM   2241 N  N     . ASN   B 1 119 ? 5.515   -4.941  -11.965 1.00 23.55 ? 116 ASN   B N     1 
ATOM   2242 C  CA    . ASN   B 1 119 ? 4.867   -3.886  -11.133 1.00 23.75 ? 116 ASN   B CA    1 
ATOM   2243 C  C     . ASN   B 1 119 ? 3.353   -3.878  -11.400 1.00 23.89 ? 116 ASN   B C     1 
ATOM   2244 O  O     . ASN   B 1 119 ? 2.957   -4.480  -12.354 1.00 24.06 ? 116 ASN   B O     1 
ATOM   2245 C  CB    . ASN   B 1 119 ? 5.658   -2.556  -11.165 1.00 23.76 ? 116 ASN   B CB    1 
ATOM   2246 C  CG    . ASN   B 1 119 ? 5.215   -1.521  -10.137 1.00 24.08 ? 116 ASN   B CG    1 
ATOM   2247 O  OD1   . ASN   B 1 119 ? 5.086   -1.821  -8.967  1.00 23.93 ? 116 ASN   B OD1   1 
ATOM   2248 N  ND2   . ASN   B 1 119 ? 4.771   -0.374  -10.620 1.00 24.15 ? 116 ASN   B ND2   1 
ATOM   2249 N  N     . LYS   B 1 120 ? 2.560   -3.188  -10.560 1.00 24.19 ? 117 LYS   B N     1 
ATOM   2250 C  CA    . LYS   B 1 120 ? 1.095   -3.016  -10.574 1.00 24.52 ? 117 LYS   B CA    1 
ATOM   2251 C  C     . LYS   B 1 120 ? 0.433   -4.317  -10.120 1.00 24.65 ? 117 LYS   B C     1 
ATOM   2252 O  O     . LYS   B 1 120 ? -0.581  -4.637  -10.624 1.00 24.80 ? 117 LYS   B O     1 
ATOM   2253 C  CB    . LYS   B 1 120 ? 0.562   -2.395  -11.880 1.00 24.54 ? 117 LYS   B CB    1 
ATOM   2254 C  CG    . LYS   B 1 120 ? 1.384   -1.279  -12.507 1.00 24.57 ? 117 LYS   B CG    1 
ATOM   2255 C  CD    . LYS   B 1 120 ? 0.601   -0.297  -13.373 1.00 24.88 ? 117 LYS   B CD    1 
ATOM   2256 C  CE    . LYS   B 1 120 ? 1.517   0.786   -13.914 1.00 25.06 ? 117 LYS   B CE    1 
ATOM   2257 N  NZ    . LYS   B 1 120 ? 0.957   1.513   -15.061 1.00 25.40 ? 117 LYS   B NZ    1 
ATOM   2258 N  N     . SER   B 1 121 ? 1.066   -5.038  -9.194  1.00 24.84 ? 118 SER   B N     1 
ATOM   2259 C  CA    . SER   B 1 121 ? 0.463   -6.301  -8.695  1.00 25.06 ? 118 SER   B CA    1 
ATOM   2260 C  C     . SER   B 1 121 ? -0.935  -6.084  -8.106  1.00 25.44 ? 118 SER   B C     1 
ATOM   2261 O  O     . SER   B 1 121 ? -1.676  -7.048  -8.007  1.00 25.70 ? 118 SER   B O     1 
ATOM   2262 C  CB    . SER   B 1 121 ? 1.375   -7.009  -7.730  1.00 25.10 ? 118 SER   B CB    1 
ATOM   2263 O  OG    . SER   B 1 121 ? 1.461   -6.342  -6.499  1.00 25.21 ? 118 SER   B OG    1 
ATOM   2264 N  N     . ASP   B 1 122 ? -1.279  -4.854  -7.734  1.00 25.45 ? 119 ASP   B N     1 
ATOM   2265 C  CA    . ASP   B 1 122 ? -2.552  -4.515  -7.132  1.00 25.79 ? 119 ASP   B CA    1 
ATOM   2266 C  C     . ASP   B 1 122 ? -3.668  -4.415  -8.170  1.00 25.86 ? 119 ASP   B C     1 
ATOM   2267 O  O     . ASP   B 1 122 ? -4.829  -4.296  -7.806  1.00 26.22 ? 119 ASP   B O     1 
ATOM   2268 C  CB    . ASP   B 1 122 ? -2.488  -3.186  -6.385  1.00 25.92 ? 119 ASP   B CB    1 
ATOM   2269 C  CG    . ASP   B 1 122 ? -2.137  -2.036  -7.306  1.00 25.92 ? 119 ASP   B CG    1 
ATOM   2270 O  OD1   . ASP   B 1 122 ? -0.942  -1.902  -7.621  1.00 25.65 ? 119 ASP   B OD1   1 
ATOM   2271 O  OD2   . ASP   B 1 122 ? -3.063  -1.313  -7.735  1.00 26.20 ? 119 ASP   B OD2   1 
ATOM   2272 N  N     . LEU   B 1 123 ? -3.333  -4.429  -9.455  1.00 25.74 ? 120 LEU   B N     1 
ATOM   2273 C  CA    . LEU   B 1 123 ? -4.383  -4.328  -10.450 1.00 25.93 ? 120 LEU   B CA    1 
ATOM   2274 C  C     . LEU   B 1 123 ? -4.940  -5.714  -10.735 1.00 25.77 ? 120 LEU   B C     1 
ATOM   2275 O  O     . LEU   B 1 123 ? -4.183  -6.647  -11.013 1.00 25.63 ? 120 LEU   B O     1 
ATOM   2276 C  CB    . LEU   B 1 123 ? -3.841  -3.706  -11.730 1.00 26.01 ? 120 LEU   B CB    1 
ATOM   2277 C  CG    . LEU   B 1 123 ? -3.496  -2.225  -11.651 1.00 26.19 ? 120 LEU   B CG    1 
ATOM   2278 C  CD1   . LEU   B 1 123 ? -2.888  -1.797  -12.970 1.00 26.10 ? 120 LEU   B CD1   1 
ATOM   2279 C  CD2   . LEU   B 1 123 ? -4.724  -1.390  -11.325 1.00 26.65 ? 120 LEU   B CD2   1 
ATOM   2280 N  N     . PRO   B 1 124 ? -6.274  -5.877  -10.709 1.00 25.79 ? 121 PRO   B N     1 
ATOM   2281 C  CA    . PRO   B 1 124 ? -6.873  -7.192  -10.914 1.00 26.00 ? 121 PRO   B CA    1 
ATOM   2282 C  C     . PRO   B 1 124 ? -6.985  -7.692  -12.367 1.00 26.00 ? 121 PRO   B C     1 
ATOM   2283 O  O     . PRO   B 1 124 ? -7.227  -8.875  -12.565 1.00 26.23 ? 121 PRO   B O     1 
ATOM   2284 C  CB    . PRO   B 1 124 ? -8.260  -6.985  -10.290 1.00 26.30 ? 121 PRO   B CB    1 
ATOM   2285 C  CG    . PRO   B 1 124 ? -8.580  -5.562  -10.639 1.00 26.43 ? 121 PRO   B CG    1 
ATOM   2286 C  CD    . PRO   B 1 124 ? -7.274  -4.832  -10.441 1.00 26.16 ? 121 PRO   B CD    1 
ATOM   2287 N  N     . SER   B 1 125 ? -6.835  -6.815  -13.368 1.00 25.80 ? 122 SER   B N     1 
ATOM   2288 C  CA    . SER   B 1 125 ? -6.972  -7.244  -14.764 1.00 26.03 ? 122 SER   B CA    1 
ATOM   2289 C  C     . SER   B 1 125 ? -5.596  -7.535  -15.363 1.00 25.77 ? 122 SER   B C     1 
ATOM   2290 O  O     . SER   B 1 125 ? -5.114  -6.785  -16.213 1.00 25.64 ? 122 SER   B O     1 
ATOM   2291 C  CB    . SER   B 1 125 ? -7.731  -6.237  -15.583 1.00 26.21 ? 122 SER   B CB    1 
ATOM   2292 O  OG    . SER   B 1 125 ? -9.102  -6.249  -15.236 1.00 26.63 ? 122 SER   B OG    1 
ATOM   2293 N  N     . ARG   B 1 126 ? -4.979  -8.633  -14.917 1.00 25.80 ? 123 ARG   B N     1 
ATOM   2294 C  CA    . ARG   B 1 126 ? -3.607  -8.962  -15.351 1.00 25.77 ? 123 ARG   B CA    1 
ATOM   2295 C  C     . ARG   B 1 126 ? -3.629  -9.516  -16.784 1.00 25.84 ? 123 ARG   B C     1 
ATOM   2296 O  O     . ARG   B 1 126 ? -4.607  -10.130 -17.222 1.00 26.17 ? 123 ARG   B O     1 
ATOM   2297 C  CB    . ARG   B 1 126 ? -2.871  -9.866  -14.352 1.00 25.93 ? 123 ARG   B CB    1 
ATOM   2298 C  CG    . ARG   B 1 126 ? -3.168  -11.355 -14.362 1.00 26.46 ? 123 ARG   B CG    1 
ATOM   2299 C  CD    . ARG   B 1 126 ? -2.503  -11.981 -13.132 1.00 26.65 ? 123 ARG   B CD    1 
ATOM   2300 N  NE    . ARG   B 1 126 ? -1.057  -11.854 -13.246 1.00 26.49 ? 123 ARG   B NE    1 
ATOM   2301 C  CZ    . ARG   B 1 126 ? -0.201  -11.556 -12.267 1.00 26.30 ? 123 ARG   B CZ    1 
ATOM   2302 N  NH1   . ARG   B 1 126 ? 1.085   -11.470 -12.572 1.00 26.28 ? 123 ARG   B NH1   1 
ATOM   2303 N  NH2   . ARG   B 1 126 ? -0.599  -11.351 -11.021 1.00 26.32 ? 123 ARG   B NH2   1 
ATOM   2304 N  N     . THR   B 1 127 ? -2.550  -9.208  -17.506 1.00 25.66 ? 124 THR   B N     1 
ATOM   2305 C  CA    . THR   B 1 127 ? -2.325  -9.641  -18.885 1.00 25.76 ? 124 THR   B CA    1 
ATOM   2306 C  C     . THR   B 1 127 ? -1.045  -10.473 -18.994 1.00 26.08 ? 124 THR   B C     1 
ATOM   2307 O  O     . THR   B 1 127 ? -0.918  -11.268 -19.908 1.00 26.64 ? 124 THR   B O     1 
ATOM   2308 C  CB    . THR   B 1 127 ? -2.242  -8.453  -19.854 1.00 25.64 ? 124 THR   B CB    1 
ATOM   2309 O  OG1   . THR   B 1 127 ? -1.059  -7.693  -19.603 1.00 25.30 ? 124 THR   B OG1   1 
ATOM   2310 C  CG2   . THR   B 1 127 ? -3.450  -7.552  -19.774 1.00 25.69 ? 124 THR   B CG2   1 
ATOM   2311 N  N     . VAL   B 1 128 ? -0.109  -10.264 -18.062 1.00 26.04 ? 125 VAL   B N     1 
ATOM   2312 C  CA    . VAL   B 1 128 ? 1.152   -11.056 -17.984 1.00 26.26 ? 125 VAL   B CA    1 
ATOM   2313 C  C     . VAL   B 1 128 ? 1.038   -12.038 -16.815 1.00 26.76 ? 125 VAL   B C     1 
ATOM   2314 O  O     . VAL   B 1 128 ? 1.123   -11.662 -15.663 1.00 26.41 ? 125 VAL   B O     1 
ATOM   2315 C  CB    . VAL   B 1 128 ? 2.414   -10.189 -17.909 1.00 25.93 ? 125 VAL   B CB    1 
ATOM   2316 C  CG1   . VAL   B 1 128 ? 3.661   -11.026 -18.041 1.00 25.98 ? 125 VAL   B CG1   1 
ATOM   2317 C  CG2   . VAL   B 1 128 ? 2.375   -9.100  -18.958 1.00 25.96 ? 125 VAL   B CG2   1 
ATOM   2318 N  N     . ASP   B 1 129 ? 0.781   -13.308 -17.151 1.00 27.94 ? 126 ASP   B N     1 
ATOM   2319 C  CA    . ASP   B 1 129 ? 0.641   -14.426 -16.180 1.00 28.67 ? 126 ASP   B CA    1 
ATOM   2320 C  C     . ASP   B 1 129 ? 1.963   -14.646 -15.468 1.00 28.62 ? 126 ASP   B C     1 
ATOM   2321 O  O     . ASP   B 1 129 ? 2.967   -14.690 -16.157 1.00 28.54 ? 126 ASP   B O     1 
ATOM   2322 C  CB    . ASP   B 1 129 ? 0.309   -15.747 -16.881 1.00 29.98 ? 126 ASP   B CB    1 
ATOM   2323 C  CG    . ASP   B 1 129 ? -0.868  -15.555 -17.793 1.00 30.84 ? 126 ASP   B CG    1 
ATOM   2324 O  OD1   . ASP   B 1 129 ? -1.984  -15.423 -17.278 1.00 31.76 ? 126 ASP   B OD1   1 
ATOM   2325 O  OD2   . ASP   B 1 129 ? -0.656  -15.473 -18.975 1.00 31.75 ? 126 ASP   B OD2   1 
ATOM   2326 N  N     . THR   B 1 130 ? 1.916   -14.791 -14.134 1.00 28.84 ? 127 THR   B N     1 
ATOM   2327 C  CA    . THR   B 1 130 ? 3.132   -15.020 -13.334 1.00 28.87 ? 127 THR   B CA    1 
ATOM   2328 C  C     . THR   B 1 130 ? 3.998   -16.114 -13.958 1.00 29.15 ? 127 THR   B C     1 
ATOM   2329 O  O     . THR   B 1 130 ? 5.163   -15.898 -14.057 1.00 29.09 ? 127 THR   B O     1 
ATOM   2330 C  CB    . THR   B 1 130 ? 2.769   -15.113 -11.847 1.00 29.12 ? 127 THR   B CB    1 
ATOM   2331 O  OG1   . THR   B 1 130 ? 1.835   -14.067 -11.605 1.00 29.13 ? 127 THR   B OG1   1 
ATOM   2332 C  CG2   . THR   B 1 130 ? 3.961   -14.899 -10.951 1.00 29.10 ? 127 THR   B CG2   1 
ATOM   2333 N  N     . LYS   B 1 131 ? 3.423   -17.223 -14.390 1.00 29.67 ? 128 LYS   B N     1 
ATOM   2334 C  CA    . LYS   B 1 131 ? 4.256   -18.303 -14.964 1.00 30.16 ? 128 LYS   B CA    1 
ATOM   2335 C  C     . LYS   B 1 131 ? 5.059   -17.827 -16.174 1.00 30.05 ? 128 LYS   B C     1 
ATOM   2336 O  O     . LYS   B 1 131 ? 6.167   -18.286 -16.292 1.00 30.58 ? 128 LYS   B O     1 
ATOM   2337 C  CB    . LYS   B 1 131 ? 3.498   -19.587 -15.302 1.00 30.90 ? 128 LYS   B CB    1 
ATOM   2338 C  CG    . LYS   B 1 131 ? 4.322   -20.585 -16.103 1.00 31.38 ? 128 LYS   B CG    1 
ATOM   2339 C  CD    . LYS   B 1 131 ? 3.642   -21.927 -16.273 0.00 66.08 ? 128 LYS   B CD    1 
ATOM   2340 C  CE    . LYS   B 1 131 ? 4.562   -22.994 -16.829 0.00 66.83 ? 128 LYS   B CE    1 
ATOM   2341 N  NZ    . LYS   B 1 131 ? 5.113   -22.612 -18.150 0.00 66.80 ? 128 LYS   B NZ    1 
ATOM   2342 N  N     . GLN   B 1 132 ? 4.508   -16.984 -17.042 1.00 29.61 ? 129 GLN   B N     1 
ATOM   2343 C  CA    . GLN   B 1 132 ? 5.273   -16.518 -18.229 1.00 29.37 ? 129 GLN   B CA    1 
ATOM   2344 C  C     . GLN   B 1 132 ? 6.492   -15.713 -17.792 1.00 28.43 ? 129 GLN   B C     1 
ATOM   2345 O  O     . GLN   B 1 132 ? 7.518   -15.814 -18.445 1.00 28.46 ? 129 GLN   B O     1 
ATOM   2346 C  CB    . GLN   B 1 132 ? 4.516   -15.518 -19.097 1.00 29.64 ? 129 GLN   B CB    1 
ATOM   2347 C  CG    . GLN   B 1 132 ? 3.186   -15.958 -19.684 1.00 30.51 ? 129 GLN   B CG    1 
ATOM   2348 C  CD    . GLN   B 1 132 ? 2.626   -14.898 -20.610 1.00 30.90 ? 129 GLN   B CD    1 
ATOM   2349 O  OE1   . GLN   B 1 132 ? 3.222   -14.606 -21.630 1.00 31.50 ? 129 GLN   B OE1   1 
ATOM   2350 N  NE2   . GLN   B 1 132 ? 1.472   -14.317 -20.274 1.00 30.77 ? 129 GLN   B NE2   1 
ATOM   2351 N  N     . ALA   B 1 133 ? 6.329   -14.901 -16.753 1.00 27.44 ? 130 ALA   B N     1 
ATOM   2352 C  CA    . ALA   B 1 133 ? 7.380   -14.028 -16.206 1.00 26.65 ? 130 ALA   B CA    1 
ATOM   2353 C  C     . ALA   B 1 133 ? 8.444   -14.882 -15.512 1.00 26.56 ? 130 ALA   B C     1 
ATOM   2354 O  O     . ALA   B 1 133 ? 9.613   -14.689 -15.729 1.00 26.22 ? 130 ALA   B O     1 
ATOM   2355 C  CB    . ALA   B 1 133 ? 6.733   -13.050 -15.264 1.00 26.23 ? 130 ALA   B CB    1 
ATOM   2356 N  N     . GLN   B 1 134 ? 7.973   -15.838 -14.717 1.00 26.76 ? 131 GLN   B N     1 
ATOM   2357 C  CA    . GLN   B 1 134 ? 8.865   -16.763 -14.026 1.00 26.91 ? 131 GLN   B CA    1 
ATOM   2358 C  C     . GLN   B 1 134 ? 9.755   -17.473 -15.049 1.00 27.36 ? 131 GLN   B C     1 
ATOM   2359 O  O     . GLN   B 1 134 ? 10.950  -17.589 -14.847 1.00 27.67 ? 131 GLN   B O     1 
ATOM   2360 C  CB    . GLN   B 1 134 ? 8.066   -17.778 -13.197 1.00 27.22 ? 131 GLN   B CB    1 
ATOM   2361 C  CG    . GLN   B 1 134 ? 7.465   -17.195 -11.929 1.00 26.91 ? 131 GLN   B CG    1 
ATOM   2362 C  CD    . GLN   B 1 134 ? 6.864   -18.255 -11.046 1.00 27.58 ? 131 GLN   B CD    1 
ATOM   2363 O  OE1   . GLN   B 1 134 ? 6.393   -19.282 -11.531 1.00 28.11 ? 131 GLN   B OE1   1 
ATOM   2364 N  NE2   . GLN   B 1 134 ? 6.900   -18.028 -9.737  1.00 27.50 ? 131 GLN   B NE2   1 
ATOM   2365 N  N     . ASP   B 1 135 ? 9.161   -17.929 -16.157 1.00 27.84 ? 132 ASP   B N     1 
ATOM   2366 C  CA    . ASP   B 1 135 ? 9.873   -18.704 -17.185 1.00 28.51 ? 132 ASP   B CA    1 
ATOM   2367 C  C     . ASP   B 1 135 ? 10.952  -17.840 -17.836 1.00 28.09 ? 132 ASP   B C     1 
ATOM   2368 O  O     . ASP   B 1 135 ? 12.045  -18.304 -18.099 1.00 28.20 ? 132 ASP   B O     1 
ATOM   2369 C  CB    . ASP   B 1 135 ? 8.916   -19.270 -18.240 1.00 29.14 ? 132 ASP   B CB    1 
ATOM   2370 C  CG    . ASP   B 1 135 ? 8.021   -20.391 -17.734 1.00 29.92 ? 132 ASP   B CG    1 
ATOM   2371 O  OD1   . ASP   B 1 135 ? 8.260   -20.896 -16.601 1.00 30.18 ? 132 ASP   B OD1   1 
ATOM   2372 O  OD2   . ASP   B 1 135 ? 7.067   -20.744 -18.470 1.00 30.50 ? 132 ASP   B OD2   1 
ATOM   2373 N  N     . LEU   B 1 136 ? 10.634  -16.568 -18.063 1.00 27.59 ? 133 LEU   B N     1 
ATOM   2374 C  CA    . LEU   B 1 136 ? 11.578  -15.644 -18.660 1.00 27.27 ? 133 LEU   B CA    1 
ATOM   2375 C  C     . LEU   B 1 136 ? 12.771  -15.427 -17.717 1.00 27.08 ? 133 LEU   B C     1 
ATOM   2376 O  O     . LEU   B 1 136 ? 13.926  -15.515 -18.146 1.00 27.22 ? 133 LEU   B O     1 
ATOM   2377 C  CB    . LEU   B 1 136 ? 10.851  -14.334 -18.980 1.00 26.94 ? 133 LEU   B CB    1 
ATOM   2378 C  CG    . LEU   B 1 136 ? 11.651  -13.298 -19.772 1.00 26.84 ? 133 LEU   B CG    1 
ATOM   2379 C  CD1   . LEU   B 1 136 ? 12.088  -13.833 -21.132 1.00 27.48 ? 133 LEU   B CD1   1 
ATOM   2380 C  CD2   . LEU   B 1 136 ? 10.838  -12.030 -19.948 1.00 26.43 ? 133 LEU   B CD2   1 
ATOM   2381 N  N     . ALA   B 1 137 ? 12.501  -15.180 -16.430 1.00 26.85 ? 134 ALA   B N     1 
ATOM   2382 C  CA    . ALA   B 1 137 ? 13.558  -14.932 -15.439 1.00 26.70 ? 134 ALA   B CA    1 
ATOM   2383 C  C     . ALA   B 1 137 ? 14.452  -16.168 -15.287 1.00 27.44 ? 134 ALA   B C     1 
ATOM   2384 O  O     . ALA   B 1 137 ? 15.655  -16.056 -15.162 1.00 27.30 ? 134 ALA   B O     1 
ATOM   2385 C  CB    . ALA   B 1 137 ? 12.952  -14.517 -14.126 1.00 26.41 ? 134 ALA   B CB    1 
ATOM   2386 N  N     . ARG   B 1 138 ? 13.841  -17.351 -15.356 1.00 28.21 ? 135 ARG   B N     1 
ATOM   2387 C  CA    . ARG   B 1 138 ? 14.545  -18.613 -15.310 1.00 29.38 ? 135 ARG   B CA    1 
ATOM   2388 C  C     . ARG   B 1 138 ? 15.514  -18.711 -16.495 1.00 29.45 ? 135 ARG   B C     1 
ATOM   2389 O  O     . ARG   B 1 138 ? 16.621  -19.166 -16.314 1.00 29.85 ? 135 ARG   B O     1 
ATOM   2390 C  CB    . ARG   B 1 138 ? 13.532  -19.764 -15.312 1.00 30.37 ? 135 ARG   B CB    1 
ATOM   2391 C  CG    . ARG   B 1 138 ? 14.099  -21.135 -14.973 1.00 31.75 ? 135 ARG   B CG    1 
ATOM   2392 C  CD    . ARG   B 1 138 ? 13.040  -22.243 -14.927 1.00 32.94 ? 135 ARG   B CD    1 
ATOM   2393 N  NE    . ARG   B 1 138 ? 11.880  -21.900 -14.094 1.00 33.00 ? 135 ARG   B NE    1 
ATOM   2394 C  CZ    . ARG   B 1 138 ? 10.630  -21.707 -14.536 1.00 33.28 ? 135 ARG   B CZ    1 
ATOM   2395 N  NH1   . ARG   B 1 138 ? 10.278  -22.076 -15.760 1.00 33.81 ? 135 ARG   B NH1   1 
ATOM   2396 N  NH2   . ARG   B 1 138 ? 9.730   -21.151 -13.735 1.00 32.88 ? 135 ARG   B NH2   1 
ATOM   2397 N  N     . SER   B 1 139 ? 15.095  -18.270 -17.690 1.00 29.47 ? 136 SER   B N     1 
ATOM   2398 C  CA    . SER   B 1 139 ? 15.938  -18.357 -18.909 1.00 30.02 ? 136 SER   B CA    1 
ATOM   2399 C  C     . SER   B 1 139 ? 17.135  -17.408 -18.809 1.00 29.71 ? 136 SER   B C     1 
ATOM   2400 O  O     . SER   B 1 139 ? 18.177  -17.683 -19.376 1.00 30.42 ? 136 SER   B O     1 
ATOM   2401 C  CB    . SER   B 1 139 ? 15.146  -18.107 -20.181 1.00 30.08 ? 136 SER   B CB    1 
ATOM   2402 O  OG    . SER   B 1 139 ? 14.703  -16.755 -20.233 1.00 29.24 ? 136 SER   B OG    1 
ATOM   2403 N  N     . TYR   B 1 140 ? 16.996  -16.321 -18.052 1.00 28.95 ? 137 TYR   B N     1 
ATOM   2404 C  CA    . TYR   B 1 140 ? 18.092  -15.371 -17.852 1.00 28.59 ? 137 TYR   B CA    1 
ATOM   2405 C  C     . TYR   B 1 140 ? 18.937  -15.717 -16.623 1.00 28.46 ? 137 TYR   B C     1 
ATOM   2406 O  O     . TYR   B 1 140 ? 20.060  -15.199 -16.487 1.00 28.62 ? 137 TYR   B O     1 
ATOM   2407 C  CB    . TYR   B 1 140 ? 17.566  -13.946 -17.675 1.00 28.24 ? 137 TYR   B CB    1 
ATOM   2408 C  CG    . TYR   B 1 140 ? 16.859  -13.339 -18.862 1.00 28.37 ? 137 TYR   B CG    1 
ATOM   2409 C  CD1   . TYR   B 1 140 ? 17.156  -13.706 -20.164 1.00 28.91 ? 137 TYR   B CD1   1 
ATOM   2410 C  CD2   . TYR   B 1 140 ? 15.916  -12.340 -18.670 1.00 28.10 ? 137 TYR   B CD2   1 
ATOM   2411 C  CE1   . TYR   B 1 140 ? 16.503  -13.135 -21.243 1.00 29.05 ? 137 TYR   B CE1   1 
ATOM   2412 C  CE2   . TYR   B 1 140 ? 15.267  -11.743 -19.741 1.00 28.26 ? 137 TYR   B CE2   1 
ATOM   2413 C  CZ    . TYR   B 1 140 ? 15.569  -12.138 -21.032 1.00 28.67 ? 137 TYR   B CZ    1 
ATOM   2414 O  OH    . TYR   B 1 140 ? 14.911  -11.555 -22.075 1.00 28.91 ? 137 TYR   B OH    1 
ATOM   2415 N  N     . GLY   B 1 141 ? 18.399  -16.556 -15.734 1.00 28.24 ? 138 GLY   B N     1 
ATOM   2416 C  CA    . GLY   B 1 141 ? 19.035  -16.887 -14.464 1.00 28.22 ? 138 GLY   B CA    1 
ATOM   2417 C  C     . GLY   B 1 141 ? 18.992  -15.729 -13.478 1.00 27.47 ? 138 GLY   B C     1 
ATOM   2418 O  O     . GLY   B 1 141 ? 19.953  -15.487 -12.744 1.00 27.62 ? 138 GLY   B O     1 
ATOM   2419 N  N     . ILE   B 1 142 ? 17.875  -15.005 -13.448 1.00 26.56 ? 139 ILE   B N     1 
ATOM   2420 C  CA    . ILE   B 1 142 ? 17.759  -13.851 -12.572 1.00 26.00 ? 139 ILE   B CA    1 
ATOM   2421 C  C     . ILE   B 1 142 ? 16.535  -14.016 -11.681 1.00 25.64 ? 139 ILE   B C     1 
ATOM   2422 O  O     . ILE   B 1 142 ? 15.628  -14.781 -12.009 1.00 25.68 ? 139 ILE   B O     1 
ATOM   2423 C  CB    . ILE   B 1 142 ? 17.691  -12.538 -13.374 1.00 25.65 ? 139 ILE   B CB    1 
ATOM   2424 C  CG1   . ILE   B 1 142 ? 16.398  -12.428 -14.187 1.00 25.54 ? 139 ILE   B CG1   1 
ATOM   2425 C  CG2   . ILE   B 1 142 ? 18.923  -12.398 -14.252 1.00 25.79 ? 139 ILE   B CG2   1 
ATOM   2426 C  CD1   . ILE   B 1 142 ? 16.192  -11.081 -14.844 1.00 25.18 ? 139 ILE   B CD1   1 
ATOM   2427 N  N     . PRO   B 1 143 ? 16.469  -13.298 -10.538 1.00 25.05 ? 140 PRO   B N     1 
ATOM   2428 C  CA    . PRO   B 1 143 ? 15.260  -13.312 -9.725  1.00 24.85 ? 140 PRO   B CA    1 
ATOM   2429 C  C     . PRO   B 1 143 ? 14.108  -12.573 -10.417 1.00 24.26 ? 140 PRO   B C     1 
ATOM   2430 O  O     . PRO   B 1 143 ? 14.330  -11.636 -11.180 1.00 24.00 ? 140 PRO   B O     1 
ATOM   2431 C  CB    . PRO   B 1 143 ? 15.679  -12.617 -8.412  1.00 24.76 ? 140 PRO   B CB    1 
ATOM   2432 C  CG    . PRO   B 1 143 ? 17.187  -12.561 -8.453  1.00 24.92 ? 140 PRO   B CG    1 
ATOM   2433 C  CD    . PRO   B 1 143 ? 17.533  -12.489 -9.924  1.00 24.85 ? 140 PRO   B CD    1 
ATOM   2434 N  N     . PHE   B 1 144 ? 12.887  -13.030 -10.140 1.00 24.23 ? 141 PHE   B N     1 
ATOM   2435 C  CA    . PHE   B 1 144 ? 11.645  -12.355 -10.508 1.00 23.89 ? 141 PHE   B CA    1 
ATOM   2436 C  C     . PHE   B 1 144 ? 10.860  -11.999 -9.237  1.00 24.09 ? 141 PHE   B C     1 
ATOM   2437 O  O     . PHE   B 1 144 ? 10.684  -12.872 -8.353  1.00 24.39 ? 141 PHE   B O     1 
ATOM   2438 C  CB    . PHE   B 1 144 ? 10.797  -13.266 -11.397 1.00 24.00 ? 141 PHE   B CB    1 
ATOM   2439 C  CG    . PHE   B 1 144 ? 9.392   -12.781 -11.637 1.00 23.71 ? 141 PHE   B CG    1 
ATOM   2440 C  CD1   . PHE   B 1 144 ? 9.166   -11.543 -12.216 1.00 23.33 ? 141 PHE   B CD1   1 
ATOM   2441 C  CD2   . PHE   B 1 144 ? 8.301   -13.569 -11.322 1.00 23.91 ? 141 PHE   B CD2   1 
ATOM   2442 C  CE1   . PHE   B 1 144 ? 7.878   -11.084 -12.437 1.00 23.23 ? 141 PHE   B CE1   1 
ATOM   2443 C  CE2   . PHE   B 1 144 ? 7.013   -13.115 -11.554 1.00 23.81 ? 141 PHE   B CE2   1 
ATOM   2444 C  CZ    . PHE   B 1 144 ? 6.801   -11.877 -12.114 1.00 23.46 ? 141 PHE   B CZ    1 
ATOM   2445 N  N     . ILE   B 1 145 ? 10.347  -10.757 -9.187  1.00 23.95 ? 142 ILE   B N     1 
ATOM   2446 C  CA    . ILE   B 1 145 ? 9.524   -10.246 -8.075  1.00 24.27 ? 142 ILE   B CA    1 
ATOM   2447 C  C     . ILE   B 1 145 ? 8.347   -9.432  -8.631  1.00 24.38 ? 142 ILE   B C     1 
ATOM   2448 O  O     . ILE   B 1 145 ? 8.536   -8.590  -9.493  1.00 24.24 ? 142 ILE   B O     1 
ATOM   2449 C  CB    . ILE   B 1 145 ? 10.386  -9.395  -7.114  1.00 24.20 ? 142 ILE   B CB    1 
ATOM   2450 C  CG1   . ILE   B 1 145 ? 11.439  -10.254 -6.410  1.00 24.46 ? 142 ILE   B CG1   1 
ATOM   2451 C  CG2   . ILE   B 1 145 ? 9.522   -8.628  -6.119  1.00 24.21 ? 142 ILE   B CG2   1 
ATOM   2452 C  CD1   . ILE   B 1 145 ? 12.422  -9.479  -5.570  1.00 24.46 ? 142 ILE   B CD1   1 
ATOM   2453 N  N     . GLU   B 1 146 ? 7.175   -9.673  -8.093  1.00 25.07 ? 143 GLU   B N     1 
ATOM   2454 C  CA    . GLU   B 1 146 ? 5.988   -8.851  -8.410  1.00 25.33 ? 143 GLU   B CA    1 
ATOM   2455 C  C     . GLU   B 1 146 ? 5.904   -7.764  -7.332  1.00 25.58 ? 143 GLU   B C     1 
ATOM   2456 O  O     . GLU   B 1 146 ? 6.106   -8.073  -6.167  1.00 26.08 ? 143 GLU   B O     1 
ATOM   2457 C  CB    . GLU   B 1 146 ? 4.763   -9.715  -8.630  1.00 25.86 ? 143 GLU   B CB    1 
ATOM   2458 C  CG    . GLU   B 1 146 ? 4.693   -10.296 -10.027 1.00 26.17 ? 143 GLU   B CG    1 
ATOM   2459 C  CD    . GLU   B 1 146 ? 3.371   -10.864 -10.504 1.00 26.62 ? 143 GLU   B CD    1 
ATOM   2460 O  OE1   . GLU   B 1 146 ? 2.392   -10.723 -9.822  1.00 27.07 ? 143 GLU   B OE1   1 
ATOM   2461 O  OE2   . GLU   B 1 146 ? 3.358   -11.479 -11.542 1.00 27.06 ? 143 GLU   B OE2   1 
ATOM   2462 N  N     . THR   B 1 147 ? 5.692   -6.519  -7.736  1.00 25.64 ? 144 THR   B N     1 
ATOM   2463 C  CA    . THR   B 1 147 ? 5.649   -5.388  -6.772  1.00 25.79 ? 144 THR   B CA    1 
ATOM   2464 C  C     . THR   B 1 147 ? 4.404   -4.532  -6.993  1.00 26.00 ? 144 THR   B C     1 
ATOM   2465 O  O     . THR   B 1 147 ? 3.701   -4.731  -7.966  1.00 26.01 ? 144 THR   B O     1 
ATOM   2466 C  CB    . THR   B 1 147 ? 6.891   -4.490  -6.856  1.00 25.52 ? 144 THR   B CB    1 
ATOM   2467 O  OG1   . THR   B 1 147 ? 6.999   -3.945  -8.163  1.00 25.53 ? 144 THR   B OG1   1 
ATOM   2468 C  CG2   . THR   B 1 147 ? 8.185   -5.151  -6.458  1.00 25.58 ? 144 THR   B CG2   1 
ATOM   2469 N  N     . SER   B 1 148 ? 4.125   -3.677  -6.018  1.00 26.36 ? 145 SER   B N     1 
ATOM   2470 C  CA    . SER   B 1 148 ? 3.055   -2.668  -6.098  1.00 26.75 ? 145 SER   B CA    1 
ATOM   2471 C  C     . SER   B 1 148 ? 3.577   -1.392  -5.436  1.00 27.17 ? 145 SER   B C     1 
ATOM   2472 O  O     . SER   B 1 148 ? 3.908   -1.390  -4.258  1.00 27.61 ? 145 SER   B O     1 
ATOM   2473 C  CB    . SER   B 1 148 ? 1.794   -3.088  -5.478  1.00 27.17 ? 145 SER   B CB    1 
ATOM   2474 O  OG    . SER   B 1 148 ? 0.881   -2.016  -5.523  1.00 27.49 ? 145 SER   B OG    1 
ATOM   2475 N  N     . ALA   B 1 149 ? 3.813   -0.394  -6.252  1.00 27.27 ? 146 ALA   B N     1 
ATOM   2476 C  CA    . ALA   B 1 149 ? 4.232   0.901   -5.744  1.00 27.34 ? 146 ALA   B CA    1 
ATOM   2477 C  C     . ALA   B 1 149 ? 3.068   1.556   -5.002  1.00 27.85 ? 146 ALA   B C     1 
ATOM   2478 O  O     . ALA   B 1 149 ? 3.293   2.429   -4.189  1.00 28.68 ? 146 ALA   B O     1 
ATOM   2479 C  CB    . ALA   B 1 149 ? 4.735   1.769   -6.867  1.00 27.13 ? 146 ALA   B CB    1 
ATOM   2480 N  N     . LYS   B 1 150 ? 1.843   1.097   -5.274  1.00 27.82 ? 147 LYS   B N     1 
ATOM   2481 C  CA    . LYS   B 1 150 ? 0.636   1.615   -4.650  1.00 28.31 ? 147 LYS   B CA    1 
ATOM   2482 C  C     . LYS   B 1 150 ? 0.461   1.113   -3.208  1.00 28.83 ? 147 LYS   B C     1 
ATOM   2483 O  O     . LYS   B 1 150 ? 0.044   1.875   -2.357  1.00 29.36 ? 147 LYS   B O     1 
ATOM   2484 C  CB    . LYS   B 1 150 ? -0.563  1.218   -5.505  1.00 28.30 ? 147 LYS   B CB    1 
ATOM   2485 C  CG    . LYS   B 1 150 ? -1.877  1.910   -5.182  1.00 28.72 ? 147 LYS   B CG    1 
ATOM   2486 C  CD    . LYS   B 1 150 ? -2.728  2.056   -6.431  1.00 28.89 ? 147 LYS   B CD    1 
ATOM   2487 C  CE    . LYS   B 1 150 ? -4.224  1.971   -6.187  1.00 29.22 ? 147 LYS   B CE    1 
ATOM   2488 N  NZ    . LYS   B 1 150 ? -4.753  3.119   -5.422  1.00 30.08 ? 147 LYS   B NZ    1 
ATOM   2489 N  N     . THR   B 1 151 ? 0.728   -0.172  -2.954  1.00 28.73 ? 148 THR   B N     1 
ATOM   2490 C  CA    . THR   B 1 151 ? 0.519   -0.784  -1.638  1.00 29.07 ? 148 THR   B CA    1 
ATOM   2491 C  C     . THR   B 1 151 ? 1.853   -0.992  -0.915  1.00 29.32 ? 148 THR   B C     1 
ATOM   2492 O  O     . THR   B 1 151 ? 1.865   -1.338  0.267   1.00 29.91 ? 148 THR   B O     1 
ATOM   2493 C  CB    . THR   B 1 151 ? -0.249  -2.112  -1.731  1.00 28.87 ? 148 THR   B CB    1 
ATOM   2494 O  OG1   . THR   B 1 151 ? 0.565   -3.111  -2.343  1.00 28.28 ? 148 THR   B OG1   1 
ATOM   2495 C  CG2   . THR   B 1 151 ? -1.546  -1.994  -2.503  1.00 28.83 ? 148 THR   B CG2   1 
ATOM   2496 N  N     . ARG   B 1 152 ? 2.969   -0.765  -1.615  1.00 29.08 ? 149 ARG   B N     1 
ATOM   2497 C  CA    . ARG   B 1 152 ? 4.386   -0.921  -1.168  1.00 29.26 ? 149 ARG   B CA    1 
ATOM   2498 C  C     . ARG   B 1 152 ? 4.778   -2.415  -1.159  1.00 28.78 ? 149 ARG   B C     1 
ATOM   2499 O  O     . ARG   B 1 152 ? 5.848   -2.715  -0.753  1.00 29.26 ? 149 ARG   B O     1 
ATOM   2500 C  CB    . ARG   B 1 152 ? 4.686   0.019   0.019   1.00 30.05 ? 149 ARG   B CB    1 
ATOM   2501 C  CG    . ARG   B 1 152 ? 6.088   0.093   0.579   1.00 30.40 ? 149 ARG   B CG    1 
ATOM   2502 C  CD    . ARG   B 1 152 ? 6.010   1.048   1.757   1.00 31.30 ? 149 ARG   B CD    1 
ATOM   2503 N  NE    . ARG   B 1 152 ? 7.055   1.978   1.505   1.00 31.58 ? 149 ARG   B NE    1 
ATOM   2504 C  CZ    . ARG   B 1 152 ? 8.303   1.685   1.708   1.00 31.68 ? 149 ARG   B CZ    1 
ATOM   2505 N  NH1   . ARG   B 1 152 ? 8.621   0.498   2.175   1.00 31.81 ? 149 ARG   B NH1   1 
ATOM   2506 N  NH2   . ARG   B 1 152 ? 9.241   2.556   1.415   1.00 31.80 ? 149 ARG   B NH2   1 
ATOM   2507 N  N     . GLN   B 1 153 ? 3.932   -3.293  -1.714  1.00 28.41 ? 150 GLN   B N     1 
ATOM   2508 C  CA    . GLN   B 1 153 ? 4.175   -4.762  -1.794  1.00 27.75 ? 150 GLN   B CA    1 
ATOM   2509 C  C     . GLN   B 1 153 ? 5.487   -5.090  -2.521  1.00 27.01 ? 150 GLN   B C     1 
ATOM   2510 O  O     . GLN   B 1 153 ? 5.590   -4.782  -3.696  1.00 26.53 ? 150 GLN   B O     1 
ATOM   2511 C  CB    . GLN   B 1 153 ? 2.942   -5.383  -2.456  1.00 27.99 ? 150 GLN   B CB    1 
ATOM   2512 C  CG    . GLN   B 1 153 ? 2.573   -6.790  -2.019  1.00 28.37 ? 150 GLN   B CG    1 
ATOM   2513 C  CD    . GLN   B 1 153 ? 2.133   -6.863  -0.579  1.00 28.83 ? 150 GLN   B CD    1 
ATOM   2514 O  OE1   . GLN   B 1 153 ? 2.913   -7.169  0.303   1.00 29.22 ? 150 GLN   B OE1   1 
ATOM   2515 N  NE2   . GLN   B 1 153 ? 0.854   -6.621  -0.343  1.00 29.24 ? 150 GLN   B NE2   1 
ATOM   2516 N  N     . ARG   B 1 154 ? 6.459   -5.628  -1.784  1.00 26.37 ? 151 ARG   B N     1 
ATOM   2517 C  CA    . ARG   B 1 154 ? 7.786   -6.100  -2.249  1.00 25.85 ? 151 ARG   B CA    1 
ATOM   2518 C  C     . ARG   B 1 154 ? 8.658   -4.974  -2.831  1.00 25.50 ? 151 ARG   B C     1 
ATOM   2519 O  O     . ARG   B 1 154 ? 9.587   -5.268  -3.517  1.00 25.23 ? 151 ARG   B O     1 
ATOM   2520 C  CB    . ARG   B 1 154 ? 7.617   -7.296  -3.193  1.00 25.55 ? 151 ARG   B CB    1 
ATOM   2521 C  CG    . ARG   B 1 154 ? 6.809   -8.457  -2.636  1.00 25.79 ? 151 ARG   B CG    1 
ATOM   2522 C  CD    . ARG   B 1 154 ? 7.095   -9.760  -3.346  1.00 25.76 ? 151 ARG   B CD    1 
ATOM   2523 N  NE    . ARG   B 1 154 ? 8.380   -10.210 -2.868  1.00 26.14 ? 151 ARG   B NE    1 
ATOM   2524 C  CZ    . ARG   B 1 154 ? 9.132   -11.174 -3.377  1.00 26.25 ? 151 ARG   B CZ    1 
ATOM   2525 N  NH1   . ARG   B 1 154 ? 8.758   -11.844 -4.444  1.00 26.23 ? 151 ARG   B NH1   1 
ATOM   2526 N  NH2   . ARG   B 1 154 ? 10.291  -11.431 -2.832  1.00 26.44 ? 151 ARG   B NH2   1 
ATOM   2527 N  N     . VAL   B 1 155 ? 8.441   -3.729  -2.439  1.00 25.50 ? 152 VAL   B N     1 
ATOM   2528 C  CA    . VAL   B 1 155 ? 9.264   -2.641  -3.030  1.00 25.35 ? 152 VAL   B CA    1 
ATOM   2529 C  C     . VAL   B 1 155 ? 10.704  -2.690  -2.539  1.00 25.58 ? 152 VAL   B C     1 
ATOM   2530 O  O     . VAL   B 1 155 ? 11.572  -2.686  -3.345  1.00 25.18 ? 152 VAL   B O     1 
ATOM   2531 C  CB    . VAL   B 1 155 ? 8.629   -1.262  -2.850  1.00 25.43 ? 152 VAL   B CB    1 
ATOM   2532 C  CG1   . VAL   B 1 155 ? 9.588   -0.206  -3.331  1.00 25.41 ? 152 VAL   B CG1   1 
ATOM   2533 C  CG2   . VAL   B 1 155 ? 7.315   -1.178  -3.591  1.00 25.33 ? 152 VAL   B CG2   1 
ATOM   2534 N  N     . GLU   B 1 156 ? 10.896  -2.684  -1.226  1.00 26.28 ? 153 GLU   B N     1 
ATOM   2535 C  CA    . GLU   B 1 156 ? 12.235  -2.819  -0.641  1.00 26.70 ? 153 GLU   B CA    1 
ATOM   2536 C  C     . GLU   B 1 156 ? 12.849  -4.138  -1.121  1.00 26.61 ? 153 GLU   B C     1 
ATOM   2537 O  O     . GLU   B 1 156 ? 14.008  -4.218  -1.527  1.00 26.52 ? 153 GLU   B O     1 
ATOM   2538 C  CB    . GLU   B 1 156 ? 12.129  -2.734  0.879   1.00 27.64 ? 153 GLU   B CB    1 
ATOM   2539 C  CG    . GLU   B 1 156 ? 11.619  -1.381  1.319   1.00 28.14 ? 153 GLU   B CG    1 
ATOM   2540 C  CD    . GLU   B 1 156 ? 11.888  -1.065  2.764   1.00 29.31 ? 153 GLU   B CD    1 
ATOM   2541 O  OE1   . GLU   B 1 156 ? 11.569  -1.921  3.620   1.00 29.81 ? 153 GLU   B OE1   1 
ATOM   2542 O  OE2   . GLU   B 1 156 ? 12.411  0.041   3.019   1.00 29.94 ? 153 GLU   B OE2   1 
ATOM   2543 N  N     . ASP   B 1 157 ? 12.007  -5.165  -1.121  1.00 26.65 ? 154 ASP   B N     1 
ATOM   2544 C  CA    . ASP   B 1 157 ? 12.349  -6.471  -1.541  1.00 26.69 ? 154 ASP   B CA    1 
ATOM   2545 C  C     . ASP   B 1 157 ? 13.018  -6.432  -2.939  1.00 25.74 ? 154 ASP   B C     1 
ATOM   2546 O  O     . ASP   B 1 157 ? 14.078  -7.028  -3.152  1.00 25.57 ? 154 ASP   B O     1 
ATOM   2547 C  CB    . ASP   B 1 157 ? 11.076  -7.323  -1.470  1.00 27.35 ? 154 ASP   B CB    1 
ATOM   2548 C  CG    . ASP   B 1 157 ? 11.359  -8.767  -1.185  1.00 28.05 ? 154 ASP   B CG    1 
ATOM   2549 O  OD1   . ASP   B 1 157 ? 12.331  -9.264  -1.774  1.00 28.31 ? 154 ASP   B OD1   1 
ATOM   2550 O  OD2   . ASP   B 1 157 ? 10.610  -9.367  -0.373  1.00 28.78 ? 154 ASP   B OD2   1 
ATOM   2551 N  N     . ALA   B 1 158 ? 12.411  -5.727  -3.896  1.00 25.03 ? 155 ALA   B N     1 
ATOM   2552 C  CA    . ALA   B 1 158 ? 12.926  -5.702  -5.269  1.00 24.52 ? 155 ALA   B CA    1 
ATOM   2553 C  C     . ALA   B 1 158 ? 14.347  -5.115  -5.305  1.00 24.39 ? 155 ALA   B C     1 
ATOM   2554 O  O     . ALA   B 1 158 ? 15.278  -5.733  -5.833  1.00 24.37 ? 155 ALA   B O     1 
ATOM   2555 C  CB    . ALA   B 1 158 ? 11.991  -4.918  -6.155  1.00 24.28 ? 155 ALA   B CB    1 
ATOM   2556 N  N     . PHE   B 1 159 ? 14.504  -3.934  -4.705  1.00 24.47 ? 156 PHE   B N     1 
ATOM   2557 C  CA    . PHE   B 1 159 ? 15.780  -3.232  -4.647  1.00 24.43 ? 156 PHE   B CA    1 
ATOM   2558 C  C     . PHE   B 1 159 ? 16.833  -4.019  -3.841  1.00 24.58 ? 156 PHE   B C     1 
ATOM   2559 O  O     . PHE   B 1 159 ? 17.977  -4.139  -4.270  1.00 24.45 ? 156 PHE   B O     1 
ATOM   2560 C  CB    . PHE   B 1 159 ? 15.570  -1.832  -4.069  1.00 24.67 ? 156 PHE   B CB    1 
ATOM   2561 C  CG    . PHE   B 1 159 ? 14.884  -0.870  -5.005  1.00 24.64 ? 156 PHE   B CG    1 
ATOM   2562 C  CD1   . PHE   B 1 159 ? 15.584  -0.249  -6.036  1.00 24.61 ? 156 PHE   B CD1   1 
ATOM   2563 C  CD2   . PHE   B 1 159 ? 13.541  -0.566  -4.848  1.00 24.76 ? 156 PHE   B CD2   1 
ATOM   2564 C  CE1   . PHE   B 1 159 ? 14.946  0.651   -6.884  1.00 24.45 ? 156 PHE   B CE1   1 
ATOM   2565 C  CE2   . PHE   B 1 159 ? 12.906  0.328   -5.702  1.00 24.74 ? 156 PHE   B CE2   1 
ATOM   2566 C  CZ    . PHE   B 1 159 ? 13.609  0.939   -6.715  1.00 24.49 ? 156 PHE   B CZ    1 
ATOM   2567 N  N     . TYR   B 1 160 ? 16.450  -4.541  -2.669  1.00 24.98 ? 157 TYR   B N     1 
ATOM   2568 C  CA    . TYR   B 1 160 ? 17.396  -5.205  -1.766  1.00 25.31 ? 157 TYR   B CA    1 
ATOM   2569 C  C     . TYR   B 1 160 ? 17.943  -6.472  -2.435  1.00 24.93 ? 157 TYR   B C     1 
ATOM   2570 O  O     . TYR   B 1 160 ? 19.117  -6.800  -2.285  1.00 25.18 ? 157 TYR   B O     1 
ATOM   2571 C  CB    . TYR   B 1 160 ? 16.725  -5.494  -0.424  1.00 26.15 ? 157 TYR   B CB    1 
ATOM   2572 C  CG    . TYR   B 1 160 ? 16.469  -4.295  0.463   1.00 27.01 ? 157 TYR   B CG    1 
ATOM   2573 C  CD1   . TYR   B 1 160 ? 16.346  -3.000  -0.045  1.00 27.13 ? 157 TYR   B CD1   1 
ATOM   2574 C  CD2   . TYR   B 1 160 ? 16.315  -4.472  1.828   1.00 27.91 ? 157 TYR   B CD2   1 
ATOM   2575 C  CE1   . TYR   B 1 160 ? 16.078  -1.920  0.786   1.00 27.80 ? 157 TYR   B CE1   1 
ATOM   2576 C  CE2   . TYR   B 1 160 ? 16.079  -3.401  2.670   1.00 28.58 ? 157 TYR   B CE2   1 
ATOM   2577 C  CZ    . TYR   B 1 160 ? 15.942  -2.128  2.147   1.00 28.41 ? 157 TYR   B CZ    1 
ATOM   2578 O  OH    . TYR   B 1 160 ? 15.710  -1.103  3.013   1.00 29.35 ? 157 TYR   B OH    1 
ATOM   2579 N  N     . THR   B 1 161 ? 17.084  -7.156  -3.192  1.00 24.41 ? 158 THR   B N     1 
ATOM   2580 C  CA    . THR   B 1 161 ? 17.463  -8.345  -3.977  1.00 24.27 ? 158 THR   B CA    1 
ATOM   2581 C  C     . THR   B 1 161 ? 18.533  -8.003  -5.019  1.00 23.88 ? 158 THR   B C     1 
ATOM   2582 O  O     . THR   B 1 161 ? 19.435  -8.793  -5.236  1.00 24.04 ? 158 THR   B O     1 
ATOM   2583 C  CB    . THR   B 1 161 ? 16.254  -8.974  -4.679  1.00 24.09 ? 158 THR   B CB    1 
ATOM   2584 O  OG1   . THR   B 1 161 ? 15.362  -9.357  -3.633  1.00 24.37 ? 158 THR   B OG1   1 
ATOM   2585 C  CG2   . THR   B 1 161 ? 16.621  -10.168 -5.543  1.00 24.13 ? 158 THR   B CG2   1 
ATOM   2586 N  N     . LEU   B 1 162 ? 18.411  -6.843  -5.664  1.00 23.54 ? 159 LEU   B N     1 
ATOM   2587 C  CA    . LEU   B 1 162 ? 19.362  -6.426  -6.697  1.00 23.42 ? 159 LEU   B CA    1 
ATOM   2588 C  C     . LEU   B 1 162 ? 20.721  -6.141  -6.048  1.00 23.81 ? 159 LEU   B C     1 
ATOM   2589 O  O     . LEU   B 1 162 ? 21.737  -6.508  -6.594  1.00 23.86 ? 159 LEU   B O     1 
ATOM   2590 C  CB    . LEU   B 1 162 ? 18.799  -5.206  -7.436  1.00 23.15 ? 159 LEU   B CB    1 
ATOM   2591 C  CG    . LEU   B 1 162 ? 19.627  -4.626  -8.583  1.00 23.04 ? 159 LEU   B CG    1 
ATOM   2592 C  CD1   . LEU   B 1 162 ? 19.984  -5.674  -9.637  1.00 23.06 ? 159 LEU   B CD1   1 
ATOM   2593 C  CD2   . LEU   B 1 162 ? 18.858  -3.477  -9.225  1.00 22.96 ? 159 LEU   B CD2   1 
ATOM   2594 N  N     . VAL   B 1 163 ? 20.711  -5.544  -4.847  1.00 24.17 ? 160 VAL   B N     1 
ATOM   2595 C  CA    . VAL   B 1 163 ? 21.930  -5.338  -4.076  1.00 24.72 ? 160 VAL   B CA    1 
ATOM   2596 C  C     . VAL   B 1 163 ? 22.594  -6.700  -3.825  1.00 25.08 ? 160 VAL   B C     1 
ATOM   2597 O  O     . VAL   B 1 163 ? 23.798  -6.843  -4.016  1.00 25.17 ? 160 VAL   B O     1 
ATOM   2598 C  CB    . VAL   B 1 163 ? 21.661  -4.563  -2.767  1.00 25.05 ? 160 VAL   B CB    1 
ATOM   2599 C  CG1   . VAL   B 1 163 ? 22.854  -4.592  -1.825  1.00 25.47 ? 160 VAL   B CG1   1 
ATOM   2600 C  CG2   . VAL   B 1 163 ? 21.252  -3.128  -3.046  1.00 24.89 ? 160 VAL   B CG2   1 
ATOM   2601 N  N     . ARG   B 1 164 ? 21.802  -7.706  -3.429  1.00 25.54 ? 161 ARG   B N     1 
ATOM   2602 C  CA    . ARG   B 1 164 ? 22.336  -9.041  -3.151  1.00 26.13 ? 161 ARG   B CA    1 
ATOM   2603 C  C     . ARG   B 1 164 ? 22.951  -9.630  -4.422  1.00 26.02 ? 161 ARG   B C     1 
ATOM   2604 O  O     . ARG   B 1 164 ? 24.002  -10.247 -4.364  1.00 26.23 ? 161 ARG   B O     1 
ATOM   2605 C  CB    . ARG   B 1 164 ? 21.260  -9.973  -2.597  1.00 26.65 ? 161 ARG   B CB    1 
ATOM   2606 C  CG    . ARG   B 1 164 ? 20.976  -9.742  -1.119  1.00 27.35 ? 161 ARG   B CG    1 
ATOM   2607 C  CD    . ARG   B 1 164 ? 19.582  -10.158 -0.668  1.00 27.84 ? 161 ARG   B CD    1 
ATOM   2608 N  NE    . ARG   B 1 164 ? 19.433  -10.179 0.817   1.00 28.62 ? 161 ARG   B NE    1 
ATOM   2609 C  CZ    . ARG   B 1 164 ? 18.357  -10.628 1.466   1.00 28.91 ? 161 ARG   B CZ    1 
ATOM   2610 N  NH1   . ARG   B 1 164 ? 17.269  -10.966 0.792   1.00 28.78 ? 161 ARG   B NH1   1 
ATOM   2611 N  NH2   . ARG   B 1 164 ? 18.372  -10.759 2.785   1.00 29.57 ? 161 ARG   B NH2   1 
ATOM   2612 N  N     . GLU   B 1 165 ? 22.273  -9.430  -5.550  1.00 25.85 ? 162 GLU   B N     1 
ATOM   2613 C  CA    . GLU   B 1 165 ? 22.747  -9.939  -6.840  1.00 25.99 ? 162 GLU   B CA    1 
ATOM   2614 C  C     . GLU   B 1 165 ? 24.105  -9.323  -7.179  1.00 26.03 ? 162 GLU   B C     1 
ATOM   2615 O  O     . GLU   B 1 165 ? 24.981  -10.015 -7.694  1.00 26.09 ? 162 GLU   B O     1 
ATOM   2616 C  CB    . GLU   B 1 165 ? 21.738  -9.662  -7.955  1.00 25.75 ? 162 GLU   B CB    1 
ATOM   2617 C  CG    . GLU   B 1 165 ? 20.476  -10.499 -7.858  1.00 26.01 ? 162 GLU   B CG    1 
ATOM   2618 C  CD    . GLU   B 1 165 ? 20.666  -11.991 -8.083  1.00 26.51 ? 162 GLU   B CD    1 
ATOM   2619 O  OE1   . GLU   B 1 165 ? 20.987  -12.380 -9.216  1.00 26.52 ? 162 GLU   B OE1   1 
ATOM   2620 O  OE2   . GLU   B 1 165 ? 20.500  -12.754 -7.114  1.00 26.96 ? 162 GLU   B OE2   1 
ATOM   2621 N  N     . ILE   B 1 166 ? 24.269  -8.023  -6.892  1.00 25.99 ? 163 ILE   B N     1 
ATOM   2622 C  CA    . ILE   B 1 166 ? 25.520  -7.334  -7.230  1.00 26.15 ? 163 ILE   B CA    1 
ATOM   2623 C  C     . ILE   B 1 166 ? 26.625  -7.909  -6.347  1.00 26.67 ? 163 ILE   B C     1 
ATOM   2624 O  O     . ILE   B 1 166 ? 27.705  -8.289  -6.813  1.00 26.97 ? 163 ILE   B O     1 
ATOM   2625 C  CB    . ILE   B 1 166 ? 25.404  -5.806  -7.071  1.00 25.79 ? 163 ILE   B CB    1 
ATOM   2626 C  CG1   . ILE   B 1 166 ? 24.327  -5.220  -7.982  1.00 25.50 ? 163 ILE   B CG1   1 
ATOM   2627 C  CG2   . ILE   B 1 166 ? 26.742  -5.141  -7.333  1.00 25.99 ? 163 ILE   B CG2   1 
ATOM   2628 C  CD1   . ILE   B 1 166 ? 23.961  -3.795  -7.648  1.00 25.34 ? 163 ILE   B CD1   1 
ATOM   2629 N  N     . ARG   B 1 167 ? 26.311  -7.982  -5.061  1.00 27.22 ? 164 ARG   B N     1 
ATOM   2630 C  CA    . ARG   B 1 167 ? 27.214  -8.459  -4.057  1.00 28.00 ? 164 ARG   B CA    1 
ATOM   2631 C  C     . ARG   B 1 167 ? 27.730  -9.852  -4.439  1.00 28.63 ? 164 ARG   B C     1 
ATOM   2632 O  O     . ARG   B 1 167 ? 28.899  -10.119 -4.265  1.00 29.36 ? 164 ARG   B O     1 
ATOM   2633 C  CB    . ARG   B 1 167 ? 26.517  -8.421  -2.694  1.00 28.20 ? 164 ARG   B CB    1 
ATOM   2634 C  CG    . ARG   B 1 167 ? 27.431  -8.737  -1.525  1.00 28.99 ? 164 ARG   B CG    1 
ATOM   2635 C  CD    . ARG   B 1 167 ? 26.615  -9.011  -0.274  1.00 29.38 ? 164 ARG   B CD    1 
ATOM   2636 N  NE    . ARG   B 1 167 ? 25.985  -7.790  0.204   1.00 29.16 ? 164 ARG   B NE    1 
ATOM   2637 C  CZ    . ARG   B 1 167 ? 24.810  -7.729  0.817   1.00 29.35 ? 164 ARG   B CZ    1 
ATOM   2638 N  NH1   . ARG   B 1 167 ? 24.022  -8.795  0.863   1.00 29.39 ? 164 ARG   B NH1   1 
ATOM   2639 N  NH2   . ARG   B 1 167 ? 24.424  -6.590  1.376   1.00 29.44 ? 164 ARG   B NH2   1 
ATOM   2640 N  N     . GLN   B 1 168 ? 26.870  -10.721 -4.976  1.00 28.97 ? 165 GLN   B N     1 
ATOM   2641 C  CA    . GLN   B 1 168 ? 27.269  -12.101 -5.320  1.00 29.81 ? 165 GLN   B CA    1 
ATOM   2642 C  C     . GLN   B 1 168 ? 28.132  -12.116 -6.591  1.00 29.62 ? 165 GLN   B C     1 
ATOM   2643 O  O     . GLN   B 1 168 ? 29.128  -12.843 -6.657  1.00 30.25 ? 165 GLN   B O     1 
ATOM   2644 C  CB    . GLN   B 1 168 ? 26.040  -13.008 -5.436  1.00 30.30 ? 165 GLN   B CB    1 
ATOM   2645 C  CG    . GLN   B 1 168 ? 25.416  -13.296 -4.076  1.00 31.07 ? 165 GLN   B CG    1 
ATOM   2646 C  CD    . GLN   B 1 168 ? 24.043  -13.920 -4.169  1.00 31.45 ? 165 GLN   B CD    1 
ATOM   2647 O  OE1   . GLN   B 1 168 ? 23.065  -13.398 -3.625  1.00 31.65 ? 165 GLN   B OE1   1 
ATOM   2648 N  NE2   . GLN   B 1 168 ? 23.968  -15.051 -4.856  1.00 32.14 ? 165 GLN   B NE2   1 
ATOM   2649 N  N     . TYR   B 1 169 ? 27.774  -11.296 -7.581  1.00 28.94 ? 166 TYR   B N     1 
ATOM   2650 C  CA    . TYR   B 1 169 ? 28.572  -11.189 -8.805  1.00 28.92 ? 166 TYR   B CA    1 
ATOM   2651 C  C     . TYR   B 1 169 ? 29.961  -10.614 -8.506  1.00 29.04 ? 166 TYR   B C     1 
ATOM   2652 O  O     . TYR   B 1 169 ? 30.885  -10.875 -9.249  1.00 29.40 ? 166 TYR   B O     1 
ATOM   2653 C  CB    . TYR   B 1 169 ? 27.848  -10.357 -9.864  1.00 28.48 ? 166 TYR   B CB    1 
ATOM   2654 C  CG    . TYR   B 1 169 ? 26.930  -11.159 -10.750 1.00 28.68 ? 166 TYR   B CG    1 
ATOM   2655 C  CD1   . TYR   B 1 169 ? 27.450  -12.080 -11.644 1.00 29.30 ? 166 TYR   B CD1   1 
ATOM   2656 C  CD2   . TYR   B 1 169 ? 25.550  -11.005 -10.700 1.00 28.33 ? 166 TYR   B CD2   1 
ATOM   2657 C  CE1   . TYR   B 1 169 ? 26.627  -12.842 -12.457 1.00 29.43 ? 166 TYR   B CE1   1 
ATOM   2658 C  CE2   . TYR   B 1 169 ? 24.715  -11.747 -11.517 1.00 28.49 ? 166 TYR   B CE2   1 
ATOM   2659 C  CZ    . TYR   B 1 169 ? 25.257  -12.668 -12.401 1.00 29.13 ? 166 TYR   B CZ    1 
ATOM   2660 O  OH    . TYR   B 1 169 ? 24.465  -13.435 -13.214 1.00 29.45 ? 166 TYR   B OH    1 
ATOM   2661 N  N     . ARG   B 1 170 ? 30.114  -9.853  -7.415  1.00 29.07 ? 167 ARG   B N     1 
ATOM   2662 C  CA    . ARG   B 1 170 ? 31.433  -9.325  -7.028  1.00 29.32 ? 167 ARG   B CA    1 
ATOM   2663 C  C     . ARG   B 1 170 ? 32.401  -10.458 -6.635  1.00 30.22 ? 167 ARG   B C     1 
ATOM   2664 O  O     . ARG   B 1 170 ? 33.610  -10.296 -6.797  1.00 30.66 ? 167 ARG   B O     1 
ATOM   2665 C  CB    . ARG   B 1 170 ? 31.324  -8.289  -5.900  1.00 29.13 ? 167 ARG   B CB    1 
ATOM   2666 C  CG    . ARG   B 1 170 ? 30.876  -6.901  -6.339  1.00 28.84 ? 167 ARG   B CG    1 
ATOM   2667 C  CD    . ARG   B 1 170 ? 30.726  -5.897  -5.191  1.00 28.83 ? 167 ARG   B CD    1 
ATOM   2668 N  NE    . ARG   B 1 170 ? 30.472  -4.542  -5.686  1.00 28.63 ? 167 ARG   B NE    1 
ATOM   2669 C  CZ    . ARG   B 1 170 ? 29.726  -3.617  -5.084  1.00 28.69 ? 167 ARG   B CZ    1 
ATOM   2670 N  NH1   . ARG   B 1 170 ? 29.158  -3.864  -3.914  1.00 28.99 ? 167 ARG   B NH1   1 
ATOM   2671 N  NH2   . ARG   B 1 170 ? 29.521  -2.449  -5.671  1.00 28.66 ? 167 ARG   B NH2   1 
ATOM   2672 N  N     . LEU   B 1 171 ? 31.895  -11.585 -6.109  1.00 31.03 ? 168 LEU   B N     1 
ATOM   2673 C  CA    . LEU   B 1 171 ? 32.769  -12.713 -5.657  1.00 32.07 ? 168 LEU   B CA    1 
ATOM   2674 C  C     . LEU   B 1 171 ? 33.019  -13.711 -6.790  1.00 32.82 ? 168 LEU   B C     1 
ATOM   2675 O  O     . LEU   B 1 171 ? 33.794  -14.662 -6.632  1.00 33.88 ? 168 LEU   B O     1 
ATOM   2676 C  CB    . LEU   B 1 171 ? 32.125  -13.464 -4.492  1.00 32.50 ? 168 LEU   B CB    1 
ATOM   2677 C  CG    . LEU   B 1 171 ? 31.810  -12.653 -3.244  1.00 32.28 ? 168 LEU   B CG    1 
ATOM   2678 C  CD1   . LEU   B 1 171 ? 31.276  -13.590 -2.176  1.00 32.95 ? 168 LEU   B CD1   1 
ATOM   2679 C  CD2   . LEU   B 1 171 ? 33.034  -11.894 -2.748  1.00 32.39 ? 168 LEU   B CD2   1 
ATOM   2680 N  N     . LYS   B 1 172 ? 32.343  -13.502 -7.916  1.00 32.72 ? 169 LYS   B N     1 
ATOM   2681 C  CA    . LYS   B 1 172 ? 32.431  -14.372 -9.051  1.00 33.42 ? 169 LYS   B CA    1 
ATOM   2682 C  C     . LYS   B 1 172 ? 33.282  -13.678 -10.116 1.00 33.76 ? 169 LYS   B C     1 
ATOM   2683 O  O     . LYS   B 1 172 ? 33.220  -12.446 -10.281 1.00 33.81 ? 169 LYS   B O     1 
ATOM   2684 C  CB    . LYS   B 1 172 ? 31.020  -14.679 -9.561  1.00 33.01 ? 169 LYS   B CB    1 
ATOM   2685 C  CG    . LYS   B 1 172 ? 30.965  -15.659 -10.716 1.00 33.58 ? 169 LYS   B CG    1 
ATOM   2686 C  CD    . LYS   B 1 172 ? 29.656  -15.617 -11.483 1.00 33.35 ? 169 LYS   B CD    1 
ATOM   2687 C  CE    . LYS   B 1 172 ? 29.752  -16.271 -12.845 1.00 33.70 ? 169 LYS   B CE    1 
ATOM   2688 N  NZ    . LYS   B 1 172 ? 30.695  -15.511 -13.699 1.00 33.90 ? 169 LYS   B NZ    1 
ATOM   2689 O  OXT   . LYS   B 1 172 ? 34.033  -14.346 -10.825 1.00 34.69 ? 169 LYS   B OXT   1 
HETATM 2690 P  PB    . GDP   C 2 .   ? 21.447  7.917   40.524  1.00 14.31 ? 201 GDP   A PB    1 
HETATM 2691 O  O1B   . GDP   C 2 .   ? 20.911  8.175   41.737  1.00 13.69 ? 201 GDP   A O1B   1 
HETATM 2692 O  O2B   . GDP   C 2 .   ? 20.709  7.245   39.525  1.00 14.00 ? 201 GDP   A O2B   1 
HETATM 2693 O  O3B   . GDP   C 2 .   ? 22.762  7.215   40.581  1.00 14.75 ? 201 GDP   A O3B   1 
HETATM 2694 O  O3A   . GDP   C 2 .   ? 21.591  9.308   39.787  1.00 14.63 ? 201 GDP   A O3A   1 
HETATM 2695 P  PA    . GDP   C 2 .   ? 21.893  10.659  40.400  1.00 15.11 ? 201 GDP   A PA    1 
HETATM 2696 O  O1A   . GDP   C 2 .   ? 20.686  11.340  40.903  1.00 14.39 ? 201 GDP   A O1A   1 
HETATM 2697 O  O2A   . GDP   C 2 .   ? 22.933  10.546  41.381  1.00 15.26 ? 201 GDP   A O2A   1 
HETATM 2698 O  "O5'" . GDP   C 2 .   ? 22.256  11.486  39.156  1.00 15.74 ? 201 GDP   A "O5'" 1 
HETATM 2699 C  "C5'" . GDP   C 2 .   ? 23.445  11.257  38.397  1.00 16.55 ? 201 GDP   A "C5'" 1 
HETATM 2700 C  "C4'" . GDP   C 2 .   ? 23.904  12.472  37.613  1.00 17.40 ? 201 GDP   A "C4'" 1 
HETATM 2701 O  "O4'" . GDP   C 2 .   ? 22.944  12.915  36.693  1.00 17.28 ? 201 GDP   A "O4'" 1 
HETATM 2702 C  "C3'" . GDP   C 2 .   ? 24.146  13.637  38.548  1.00 17.70 ? 201 GDP   A "C3'" 1 
HETATM 2703 O  "O3'" . GDP   C 2 .   ? 25.187  14.464  38.078  1.00 18.77 ? 201 GDP   A "O3'" 1 
HETATM 2704 C  "C2'" . GDP   C 2 .   ? 22.852  14.432  38.400  1.00 17.18 ? 201 GDP   A "C2'" 1 
HETATM 2705 O  "O2'" . GDP   C 2 .   ? 22.987  15.789  38.683  1.00 17.90 ? 201 GDP   A "O2'" 1 
HETATM 2706 C  "C1'" . GDP   C 2 .   ? 22.501  14.191  36.981  1.00 17.30 ? 201 GDP   A "C1'" 1 
HETATM 2707 N  N9    . GDP   C 2 .   ? 21.020  14.287  36.700  1.00 16.64 ? 201 GDP   A N9    1 
HETATM 2708 C  C8    . GDP   C 2 .   ? 20.101  13.626  37.321  1.00 15.75 ? 201 GDP   A C8    1 
HETATM 2709 N  N7    . GDP   C 2 .   ? 18.874  13.905  36.844  1.00 15.52 ? 201 GDP   A N7    1 
HETATM 2710 C  C5    . GDP   C 2 .   ? 19.066  14.778  35.857  1.00 16.28 ? 201 GDP   A C5    1 
HETATM 2711 C  C6    . GDP   C 2 .   ? 18.233  15.501  34.859  1.00 16.69 ? 201 GDP   A C6    1 
HETATM 2712 O  O6    . GDP   C 2 .   ? 17.002  15.375  34.813  1.00 16.16 ? 201 GDP   A O6    1 
HETATM 2713 N  N1    . GDP   C 2 .   ? 18.847  16.304  34.001  1.00 17.70 ? 201 GDP   A N1    1 
HETATM 2714 C  C2    . GDP   C 2 .   ? 20.179  16.455  34.037  1.00 18.31 ? 201 GDP   A C2    1 
HETATM 2715 N  N2    . GDP   C 2 .   ? 20.773  17.228  33.172  1.00 19.39 ? 201 GDP   A N2    1 
HETATM 2716 N  N3    . GDP   C 2 .   ? 20.960  15.812  34.874  1.00 17.98 ? 201 GDP   A N3    1 
HETATM 2717 C  C4    . GDP   C 2 .   ? 20.517  15.007  35.798  1.00 17.00 ? 201 GDP   A C4    1 
HETATM 2718 MG MG    . MG    D 3 .   ? 21.522  7.530   43.723  1.00 13.68 ? 202 MG    A MG    1 
HETATM 2719 O  OBB   . A1ILA E 4 .   ? 19.314  -1.553  54.909  1.00 16.46 ? 203 A1ILA A OBB   1 
HETATM 2720 C  CAS   . A1ILA E 4 .   ? 18.557  -1.031  54.088  1.00 16.52 ? 203 A1ILA A CAS   1 
HETATM 2721 C  CAT   . A1ILA E 4 .   ? 17.721  -1.842  53.318  1.00 16.59 ? 203 A1ILA A CAT   1 
HETATM 2722 C  CAZ   . A1ILA E 4 .   ? 16.522  -2.379  53.833  1.00 16.60 ? 203 A1ILA A CAZ   1 
HETATM 2723 C  CAU   . A1ILA E 4 .   ? 18.049  -2.100  51.999  1.00 16.68 ? 203 A1ILA A CAU   1 
HETATM 2724 O  OBA   . A1ILA E 4 .   ? 19.169  -1.535  51.509  1.00 16.71 ? 203 A1ILA A OBA   1 
HETATM 2725 C  CAV   . A1ILA E 4 .   ? 17.229  -2.878  51.191  1.00 16.77 ? 203 A1ILA A CAV   1 
HETATM 2726 C  CAW   . A1ILA E 4 .   ? 16.059  -3.421  51.707  1.00 16.78 ? 203 A1ILA A CAW   1 
HETATM 2727 C  CAX   . A1ILA E 4 .   ? 15.745  -3.163  53.023  1.00 16.70 ? 203 A1ILA A CAX   1 
HETATM 2728 S  SAI   . A1ILA E 4 .   ? 14.168  -3.782  53.704  1.00 16.75 ? 203 A1ILA A SAI   1 
HETATM 2729 O  OAH   . A1ILA E 4 .   ? 14.401  -4.467  54.991  1.00 16.68 ? 203 A1ILA A OAH   1 
HETATM 2730 O  OAY   . A1ILA E 4 .   ? 13.604  -4.651  52.640  1.00 16.88 ? 203 A1ILA A OAY   1 
HETATM 2731 N  NAJ   . A1ILA E 4 .   ? 13.443  -2.418  53.997  1.00 16.75 ? 203 A1ILA A NAJ   1 
HETATM 2732 C  CAK   . A1ILA E 4 .   ? 12.697  -1.828  53.074  1.00 16.85 ? 203 A1ILA A CAK   1 
HETATM 2733 S  SBK   . A1ILA E 4 .   ? 12.063  -2.471  51.579  1.00 17.01 ? 203 A1ILA A SBK   1 
HETATM 2734 C  CAF   . A1ILA E 4 .   ? 11.281  -0.942  51.265  1.00 17.09 ? 203 A1ILA A CAF   1 
HETATM 2735 C  CAE   . A1ILA E 4 .   ? 10.545  -0.648  50.205  1.00 17.23 ? 203 A1ILA A CAE   1 
HETATM 2736 CL CLBI  . A1ILA E 4 .   ? 10.323  -1.859  49.003  1.00 17.34 ? 203 A1ILA A CLBI  1 
HETATM 2737 C  CAD   . A1ILA E 4 .   ? 9.976   0.612   50.046  1.00 17.31 ? 203 A1ILA A CAD   1 
HETATM 2738 C  CAC   . A1ILA E 4 .   ? 10.179  1.554   51.036  1.00 17.25 ? 203 A1ILA A CAC   1 
HETATM 2739 C  CAB   . A1ILA E 4 .   ? 10.963  1.192   52.136  1.00 17.09 ? 203 A1ILA A CAB   1 
HETATM 2740 O  OAA   . A1ILA E 4 .   ? 11.163  2.097   53.117  1.00 17.03 ? 203 A1ILA A OAA   1 
HETATM 2741 C  CAG   . A1ILA E 4 .   ? 11.517  -0.038  52.257  1.00 17.01 ? 203 A1ILA A CAG   1 
HETATM 2742 N  NAL   . A1ILA E 4 .   ? 12.277  -0.545  53.256  1.00 16.87 ? 203 A1ILA A NAL   1 
HETATM 2743 C  CAM   . A1ILA E 4 .   ? 12.753  0.164   54.475  1.00 16.76 ? 203 A1ILA A CAM   1 
HETATM 2744 C  CAN   . A1ILA E 4 .   ? 13.947  1.165   54.070  1.00 16.72 ? 203 A1ILA A CAN   1 
HETATM 2745 C  CAO   . A1ILA E 4 .   ? 15.341  0.443   53.908  1.00 16.64 ? 203 A1ILA A CAO   1 
HETATM 2746 C  CAP   . A1ILA E 4 .   ? 16.384  1.505   53.544  1.00 16.64 ? 203 A1ILA A CAP   1 
HETATM 2747 C  CAQ   . A1ILA E 4 .   ? 17.650  0.942   52.912  1.00 16.64 ? 203 A1ILA A CAQ   1 
HETATM 2748 N  NAR   . A1ILA E 4 .   ? 18.539  0.307   53.940  1.00 16.54 ? 203 A1ILA A NAR   1 
HETATM 2749 C  CBC   . A1ILA E 4 .   ? 19.508  1.137   54.739  1.00 16.50 ? 203 A1ILA A CBC   1 
HETATM 2750 C  CBD   . A1ILA E 4 .   ? 19.030  2.507   55.102  1.00 16.51 ? 203 A1ILA A CBD   1 
HETATM 2751 C  CBE   . A1ILA E 4 .   ? 20.125  3.274   55.862  1.00 16.49 ? 203 A1ILA A CBE   1 
HETATM 2752 C  CBF   . A1ILA E 4 .   ? 21.421  3.344   55.057  1.00 16.57 ? 203 A1ILA A CBF   1 
HETATM 2753 N  NBJ   . A1ILA E 4 .   ? 21.398  4.182   53.842  1.00 16.70 ? 203 A1ILA A NBJ   1 
HETATM 2754 C  CBG   . A1ILA E 4 .   ? 21.867  1.942   54.701  1.00 16.55 ? 203 A1ILA A CBG   1 
HETATM 2755 C  CBH   . A1ILA E 4 .   ? 20.787  1.193   53.910  1.00 16.57 ? 203 A1ILA A CBH   1 
HETATM 2756 C  C1    . EDO   F 5 .   ? -10.599 15.224  49.920  1.00 23.44 ? 204 EDO   A C1    1 
HETATM 2757 O  O1    . EDO   F 5 .   ? -9.256  15.601  49.516  1.00 23.07 ? 204 EDO   A O1    1 
HETATM 2758 C  C2    . EDO   F 5 .   ? -11.214 14.492  48.737  1.00 23.60 ? 204 EDO   A C2    1 
HETATM 2759 O  O2    . EDO   F 5 .   ? -10.991 13.102  48.893  1.00 23.28 ? 204 EDO   A O2    1 
HETATM 2760 P  PB    . GDP   G 2 .   ? 7.076   5.345   -15.258 1.00 27.19 ? 201 GDP   B PB    1 
HETATM 2761 O  O1B   . GDP   G 2 .   ? 8.085   6.059   -14.540 1.00 27.27 ? 201 GDP   B O1B   1 
HETATM 2762 O  O2B   . GDP   G 2 .   ? 7.633   4.024   -15.508 1.00 26.72 ? 201 GDP   B O2B   1 
HETATM 2763 O  O3B   . GDP   G 2 .   ? 6.455   5.968   -16.398 1.00 27.80 ? 201 GDP   B O3B   1 
HETATM 2764 O  O3A   . GDP   G 2 .   ? 5.931   5.131   -14.376 1.00 27.08 ? 201 GDP   B O3A   1 
HETATM 2765 P  PA    . GDP   G 2 .   ? 5.415   6.088   -13.280 1.00 27.62 ? 201 GDP   B PA    1 
HETATM 2766 O  O1A   . GDP   G 2 .   ? 6.003   5.705   -12.055 1.00 27.00 ? 201 GDP   B O1A   1 
HETATM 2767 O  O2A   . GDP   G 2 .   ? 5.566   7.467   -13.764 1.00 28.34 ? 201 GDP   B O2A   1 
HETATM 2768 O  "O5'" . GDP   G 2 .   ? 3.996   5.610   -13.228 1.00 27.12 ? 201 GDP   B "O5'" 1 
HETATM 2769 C  "C5'" . GDP   G 2 .   ? 3.085   5.555   -14.273 1.00 27.08 ? 201 GDP   B "C5'" 1 
HETATM 2770 C  "C4'" . GDP   G 2 .   ? 1.649   5.494   -13.859 1.00 27.14 ? 201 GDP   B "C4'" 1 
HETATM 2771 O  "O4'" . GDP   G 2 .   ? 1.227   4.254   -13.335 1.00 26.69 ? 201 GDP   B "O4'" 1 
HETATM 2772 C  "C3'" . GDP   G 2 .   ? 1.311   6.463   -12.755 1.00 27.59 ? 201 GDP   B "C3'" 1 
HETATM 2773 O  "O3'" . GDP   G 2 .   ? -0.007  6.875   -12.992 1.00 27.86 ? 201 GDP   B "O3'" 1 
HETATM 2774 C  "C2'" . GDP   G 2 .   ? 1.326   5.660   -11.494 1.00 27.22 ? 201 GDP   B "C2'" 1 
HETATM 2775 O  "O2'" . GDP   G 2 .   ? 0.460   6.171   -10.502 1.00 27.83 ? 201 GDP   B "O2'" 1 
HETATM 2776 C  "C1'" . GDP   G 2 .   ? 0.772   4.374   -12.007 1.00 26.74 ? 201 GDP   B "C1'" 1 
HETATM 2777 N  N9    . GDP   G 2 .   ? 1.277   3.280   -11.161 1.00 26.05 ? 201 GDP   B N9    1 
HETATM 2778 C  C8    . GDP   G 2 .   ? 2.492   3.109   -10.914 1.00 25.73 ? 201 GDP   B C8    1 
HETATM 2779 N  N7    . GDP   G 2 .   ? 2.699   2.083   -10.157 1.00 25.35 ? 201 GDP   B N7    1 
HETATM 2780 C  C5    . GDP   G 2 .   ? 1.625   1.533   -9.886  1.00 25.40 ? 201 GDP   B C5    1 
HETATM 2781 C  C6    . GDP   G 2 .   ? 1.214   0.361   -9.106  1.00 25.46 ? 201 GDP   B C6    1 
HETATM 2782 O  O6    . GDP   G 2 .   ? 2.052   -0.343  -8.540  1.00 25.42 ? 201 GDP   B O6    1 
HETATM 2783 N  N1    . GDP   G 2 .   ? -0.050  0.116   -9.148  1.00 25.63 ? 201 GDP   B N1    1 
HETATM 2784 C  C2    . GDP   G 2 .   ? -0.939  0.898   -9.748  1.00 25.84 ? 201 GDP   B C2    1 
HETATM 2785 N  N2    . GDP   G 2 .   ? -2.217  0.585   -9.677  1.00 26.03 ? 201 GDP   B N2    1 
HETATM 2786 N  N3    . GDP   G 2 .   ? -0.608  1.961   -10.458 1.00 25.92 ? 201 GDP   B N3    1 
HETATM 2787 C  C4    . GDP   G 2 .   ? 0.633   2.320   -10.569 1.00 25.77 ? 201 GDP   B C4    1 
HETATM 2788 MG MG    . MG    H 3 .   ? 9.226   7.826   -14.588 1.00 28.21 ? 202 MG    B MG    1 
HETATM 2789 O  OBB   . A1ILA I 4 .   ? 22.141  14.554  -16.437 1.00 30.47 ? 203 A1ILA B OBB   1 
HETATM 2790 C  CAS   . A1ILA I 4 .   ? 21.742  13.537  -15.852 1.00 30.18 ? 203 A1ILA B CAS   1 
HETATM 2791 C  CAT   . A1ILA I 4 .   ? 22.241  12.276  -16.228 1.00 29.87 ? 203 A1ILA B CAT   1 
HETATM 2792 C  CAZ   . A1ILA I 4 .   ? 23.551  11.933  -15.901 1.00 30.04 ? 203 A1ILA B CAZ   1 
HETATM 2793 C  CAU   . A1ILA I 4 .   ? 21.473  11.332  -16.913 1.00 29.78 ? 203 A1ILA B CAU   1 
HETATM 2794 O  OBA   . A1ILA I 4 .   ? 20.208  11.674  -17.216 1.00 29.71 ? 203 A1ILA B OBA   1 
HETATM 2795 C  CAV   . A1ILA I 4 .   ? 21.983  10.077  -17.244 1.00 29.79 ? 203 A1ILA B CAV   1 
HETATM 2796 C  CAW   . A1ILA I 4 .   ? 23.289  9.738   -16.906 1.00 29.83 ? 203 A1ILA B CAW   1 
HETATM 2797 C  CAX   . A1ILA I 4 .   ? 24.058  10.681  -16.247 1.00 29.97 ? 203 A1ILA B CAX   1 
HETATM 2798 S  SAI   . A1ILA I 4 .   ? 25.554  10.321  -15.782 1.00 30.38 ? 203 A1ILA B SAI   1 
HETATM 2799 O  OAH   . A1ILA I 4 .   ? 26.598  11.349  -16.244 1.00 30.78 ? 203 A1ILA B OAH   1 
HETATM 2800 O  OAY   . A1ILA I 4 .   ? 25.999  8.960   -16.288 1.00 30.50 ? 203 A1ILA B OAY   1 
HETATM 2801 N  NAJ   . A1ILA I 4 .   ? 25.378  10.290  -14.159 1.00 29.75 ? 203 A1ILA B NAJ   1 
HETATM 2802 C  CAK   . A1ILA I 4 .   ? 24.955  9.195   -13.530 1.00 29.18 ? 203 A1ILA B CAK   1 
HETATM 2803 S  SBK   . A1ILA I 4 .   ? 24.856  7.598   -14.026 1.00 29.06 ? 203 A1ILA B SBK   1 
HETATM 2804 C  CAF   . A1ILA I 4 .   ? 24.251  7.019   -12.558 1.00 28.45 ? 203 A1ILA B CAF   1 
HETATM 2805 C  CAE   . A1ILA I 4 .   ? 23.922  5.763   -12.226 1.00 28.10 ? 203 A1ILA B CAE   1 
HETATM 2806 CL CLBI  . A1ILA I 4 .   ? 24.141  4.462   -13.364 1.00 28.09 ? 203 A1ILA B CLBI  1 
HETATM 2807 C  CAD   . A1ILA I 4 .   ? 23.424  5.483   -10.965 1.00 27.75 ? 203 A1ILA B CAD   1 
HETATM 2808 C  CAC   . A1ILA I 4 .   ? 23.252  6.525   -10.077 1.00 27.75 ? 203 A1ILA B CAC   1 
HETATM 2809 C  CAB   . A1ILA I 4 .   ? 23.605  7.811   -10.467 1.00 28.06 ? 203 A1ILA B CAB   1 
HETATM 2810 O  OAA   . A1ILA I 4 .   ? 23.444  8.832   -9.570  1.00 27.89 ? 203 A1ILA B OAA   1 
HETATM 2811 C  CAG   . A1ILA I 4 .   ? 24.099  8.079   -11.706 1.00 28.39 ? 203 A1ILA B CAG   1 
HETATM 2812 N  NAL   . A1ILA I 4 .   ? 24.511  9.271   -12.263 1.00 28.77 ? 203 A1ILA B NAL   1 
HETATM 2813 C  CAM   . A1ILA I 4 .   ? 24.440  10.644  -11.589 1.00 28.76 ? 203 A1ILA B CAM   1 
HETATM 2814 C  CAN   . A1ILA I 4 .   ? 22.955  11.011  -11.443 1.00 28.56 ? 203 A1ILA B CAN   1 
HETATM 2815 C  CAO   . A1ILA I 4 .   ? 22.466  12.134  -12.393 1.00 29.03 ? 203 A1ILA B CAO   1 
HETATM 2816 C  CAP   . A1ILA I 4 .   ? 21.400  11.562  -13.320 1.00 29.12 ? 203 A1ILA B CAP   1 
HETATM 2817 C  CAQ   . A1ILA I 4 .   ? 20.389  12.563  -13.956 1.00 29.43 ? 203 A1ILA B CAQ   1 
HETATM 2818 N  NAR   . A1ILA I 4 .   ? 20.934  13.699  -14.761 1.00 29.98 ? 203 A1ILA B NAR   1 
HETATM 2819 C  CBC   . A1ILA I 4 .   ? 20.500  15.083  -14.447 1.00 30.38 ? 203 A1ILA B CBC   1 
HETATM 2820 C  CBD   . A1ILA I 4 .   ? 20.307  15.303  -12.980 1.00 30.12 ? 203 A1ILA B CBD   1 
HETATM 2821 C  CBE   . A1ILA I 4 .   ? 19.640  16.676  -12.795 1.00 30.44 ? 203 A1ILA B CBE   1 
HETATM 2822 C  CBF   . A1ILA I 4 .   ? 18.322  16.753  -13.569 1.00 30.61 ? 203 A1ILA B CBF   1 
HETATM 2823 N  NBJ   . A1ILA I 4 .   ? 17.334  15.725  -13.149 1.00 30.35 ? 203 A1ILA B NBJ   1 
HETATM 2824 C  CBG   . A1ILA I 4 .   ? 18.626  16.701  -15.048 1.00 30.83 ? 203 A1ILA B CBG   1 
HETATM 2825 C  CBH   . A1ILA I 4 .   ? 19.271  15.362  -15.353 1.00 30.75 ? 203 A1ILA B CBH   1 
HETATM 2826 C  C1    . EDO   J 5 .   ? 18.020  -8.751  6.032   1.00 29.81 ? 204 EDO   B C1    1 
HETATM 2827 O  O1    . EDO   J 5 .   ? 19.072  -8.038  5.396   1.00 30.13 ? 204 EDO   B O1    1 
HETATM 2828 C  C2    . EDO   J 5 .   ? 18.665  -9.947  6.739   1.00 29.99 ? 204 EDO   B C2    1 
HETATM 2829 O  O2    . EDO   J 5 .   ? 19.914  -9.517  7.379   1.00 30.23 ? 204 EDO   B O2    1 
HETATM 2830 O  O     . HOH   K 6 .   ? 23.158  10.366  31.374  1.00 19.38 ? 301 HOH   A O     1 
HETATM 2831 O  O     . HOH   K 6 .   ? 22.972  9.219   43.579  1.00 18.02 ? 302 HOH   A O     1 
HETATM 2832 O  O     . HOH   K 6 .   ? -7.398  17.348  49.850  1.00 25.27 ? 303 HOH   A O     1 
HETATM 2833 O  O     . HOH   K 6 .   ? 8.003   -6.999  53.322  1.00 22.71 ? 304 HOH   A O     1 
HETATM 2834 O  O     . HOH   K 6 .   ? 22.599  -1.281  35.392  1.00 26.06 ? 305 HOH   A O     1 
HETATM 2835 O  O     . HOH   K 6 .   ? 5.763   -2.372  21.287  1.00 26.23 ? 306 HOH   A O     1 
HETATM 2836 O  O     . HOH   K 6 .   ? 4.170   16.070  45.429  1.00 28.40 ? 307 HOH   A O     1 
HETATM 2837 O  O     . HOH   K 6 .   ? 19.086  7.230   48.235  1.00 17.32 ? 308 HOH   A O     1 
HETATM 2838 O  O     . HOH   K 6 .   ? 2.059   -0.574  35.525  1.00 19.49 ? 309 HOH   A O     1 
HETATM 2839 O  O     . HOH   K 6 .   ? 17.226  -2.678  41.494  1.00 17.51 ? 310 HOH   A O     1 
HETATM 2840 O  O     . HOH   K 6 .   ? -8.677  16.947  47.319  1.00 30.95 ? 311 HOH   A O     1 
HETATM 2841 O  O     . HOH   K 6 .   ? 13.998  9.611   54.837  1.00 17.24 ? 312 HOH   A O     1 
HETATM 2842 O  O     . HOH   K 6 .   ? 20.102  6.116   43.964  1.00 17.59 ? 313 HOH   A O     1 
HETATM 2843 O  O     . HOH   K 6 .   ? 22.859  6.076   42.977  1.00 17.77 ? 314 HOH   A O     1 
HETATM 2844 O  O     . HOH   K 6 .   ? 17.095  16.520  43.099  1.00 19.07 ? 315 HOH   A O     1 
HETATM 2845 O  O     . HOH   K 6 .   ? 20.917  8.532   53.918  1.00 17.72 ? 316 HOH   A O     1 
HETATM 2846 O  O     . HOH   K 6 .   ? 10.752  9.209   18.740  1.00 23.71 ? 317 HOH   A O     1 
HETATM 2847 O  O     . HOH   K 6 .   ? 3.858   8.438   27.143  1.00 22.76 ? 318 HOH   A O     1 
HETATM 2848 O  O     . HOH   K 6 .   ? 8.276   14.682  53.224  1.00 23.86 ? 319 HOH   A O     1 
HETATM 2849 O  O     . HOH   K 6 .   ? 18.540  1.964   33.561  1.00 18.28 ? 320 HOH   A O     1 
HETATM 2850 O  O     . HOH   K 6 .   ? -1.222  9.550   35.624  1.00 25.45 ? 321 HOH   A O     1 
HETATM 2851 O  O     . HOH   K 6 .   ? 21.377  22.384  42.056  1.00 32.75 ? 322 HOH   A O     1 
HETATM 2852 O  O     . HOH   K 6 .   ? 2.176   -5.359  32.541  1.00 28.58 ? 323 HOH   A O     1 
HETATM 2853 O  O     . HOH   K 6 .   ? 24.017  4.567   53.247  1.00 17.54 ? 324 HOH   A O     1 
HETATM 2854 O  O     . HOH   K 6 .   ? -5.201  6.833   51.882  1.00 26.52 ? 325 HOH   A O     1 
HETATM 2855 O  O     . HOH   K 6 .   ? 1.956   2.464   27.365  1.00 25.29 ? 326 HOH   A O     1 
HETATM 2856 O  O     . HOH   K 6 .   ? 29.070  6.322   51.164  1.00 27.39 ? 327 HOH   A O     1 
HETATM 2857 O  O     . HOH   K 6 .   ? 4.731   -4.557  51.065  1.00 18.03 ? 328 HOH   A O     1 
HETATM 2858 O  O     . HOH   K 6 .   ? -0.485  16.527  45.502  1.00 31.18 ? 329 HOH   A O     1 
HETATM 2859 O  O     . HOH   K 6 .   ? 22.042  3.423   41.753  1.00 19.39 ? 330 HOH   A O     1 
HETATM 2860 O  O     . HOH   K 6 .   ? 0.115   -1.836  25.866  1.00 22.78 ? 331 HOH   A O     1 
HETATM 2861 O  O     . HOH   K 6 .   ? 9.872   15.733  30.056  1.00 26.08 ? 332 HOH   A O     1 
HETATM 2862 O  O     . HOH   K 6 .   ? -0.603  0.157   49.729  1.00 22.28 ? 333 HOH   A O     1 
HETATM 2863 O  O     . HOH   K 6 .   ? 11.245  -0.520  21.552  1.00 21.14 ? 334 HOH   A O     1 
HETATM 2864 O  O     . HOH   K 6 .   ? 18.008  -5.018  26.351  1.00 29.41 ? 335 HOH   A O     1 
HETATM 2865 O  O     . HOH   K 6 .   ? 25.303  8.261   40.324  1.00 18.38 ? 336 HOH   A O     1 
HETATM 2866 O  O     . HOH   K 6 .   ? 5.735   18.950  34.542  1.00 22.90 ? 337 HOH   A O     1 
HETATM 2867 O  O     . HOH   K 6 .   ? 25.791  14.791  35.398  1.00 25.77 ? 338 HOH   A O     1 
HETATM 2868 O  O     . HOH   K 6 .   ? 22.346  7.223   45.682  1.00 17.61 ? 339 HOH   A O     1 
HETATM 2869 O  O     . HOH   K 6 .   ? -4.882  1.614   47.345  1.00 21.18 ? 340 HOH   A O     1 
HETATM 2870 O  O     . HOH   K 6 .   ? 5.597   2.176   53.878  1.00 33.60 ? 341 HOH   A O     1 
HETATM 2871 O  O     . HOH   K 6 .   ? 5.447   14.725  54.025  1.00 21.03 ? 342 HOH   A O     1 
HETATM 2872 O  O     . HOH   K 6 .   ? 2.065   -4.441  50.810  1.00 19.87 ? 343 HOH   A O     1 
HETATM 2873 O  O     . HOH   K 6 .   ? 28.916  10.523  51.521  1.00 17.96 ? 344 HOH   A O     1 
HETATM 2874 O  O     . HOH   K 6 .   ? 15.717  -2.690  27.781  1.00 20.64 ? 345 HOH   A O     1 
HETATM 2875 O  O     . HOH   K 6 .   ? 25.607  11.694  42.085  1.00 27.97 ? 346 HOH   A O     1 
HETATM 2876 O  O     . HOH   K 6 .   ? 6.591   17.711  38.500  1.00 20.51 ? 347 HOH   A O     1 
HETATM 2877 O  O     . HOH   K 6 .   ? -6.714  9.313   53.613  1.00 28.38 ? 348 HOH   A O     1 
HETATM 2878 O  O     . HOH   K 6 .   ? 11.487  21.381  50.594  1.00 28.09 ? 349 HOH   A O     1 
HETATM 2879 O  O     . HOH   K 6 .   ? 13.352  20.846  53.688  1.00 32.73 ? 350 HOH   A O     1 
HETATM 2880 O  O     . HOH   K 6 .   ? 5.470   20.029  40.146  1.00 35.77 ? 351 HOH   A O     1 
HETATM 2881 O  O     . HOH   K 6 .   ? 16.547  23.089  42.222  1.00 20.64 ? 352 HOH   A O     1 
HETATM 2882 O  O     . HOH   K 6 .   ? 22.063  -7.986  50.237  1.00 19.98 ? 353 HOH   A O     1 
HETATM 2883 O  O     . HOH   K 6 .   ? 23.290  2.859   51.290  1.00 17.33 ? 354 HOH   A O     1 
HETATM 2884 O  O     . HOH   K 6 .   ? 10.096  2.976   56.137  1.00 34.44 ? 355 HOH   A O     1 
HETATM 2885 O  O     . HOH   K 6 .   ? -4.168  14.932  42.000  1.00 25.79 ? 356 HOH   A O     1 
HETATM 2886 O  O     . HOH   K 6 .   ? 23.987  17.617  47.408  1.00 19.04 ? 357 HOH   A O     1 
HETATM 2887 O  O     . HOH   K 6 .   ? 21.079  -5.903  27.729  1.00 33.45 ? 358 HOH   A O     1 
HETATM 2888 O  O     . HOH   K 6 .   ? -0.975  1.045   53.708  1.00 26.24 ? 359 HOH   A O     1 
HETATM 2889 O  O     . HOH   K 6 .   ? 24.434  13.634  31.281  1.00 22.95 ? 360 HOH   A O     1 
HETATM 2890 O  O     . HOH   K 6 .   ? 18.273  -0.116  40.703  1.00 17.57 ? 361 HOH   A O     1 
HETATM 2891 O  O     . HOH   K 6 .   ? 5.874   -10.171 48.662  1.00 18.36 ? 362 HOH   A O     1 
HETATM 2892 O  O     . HOH   K 6 .   ? 4.568   16.600  37.174  1.00 20.69 ? 363 HOH   A O     1 
HETATM 2893 O  O     . HOH   K 6 .   ? 24.830  3.857   41.882  1.00 24.36 ? 364 HOH   A O     1 
HETATM 2894 O  O     . HOH   K 6 .   ? 10.859  -14.427 46.054  1.00 21.00 ? 365 HOH   A O     1 
HETATM 2895 O  O     . HOH   K 6 .   ? 2.500   5.906   28.240  1.00 20.32 ? 366 HOH   A O     1 
HETATM 2896 O  O     . HOH   K 6 .   ? 0.058   16.823  48.033  1.00 21.28 ? 367 HOH   A O     1 
HETATM 2897 O  O     . HOH   K 6 .   ? 24.561  0.371   37.033  1.00 22.93 ? 368 HOH   A O     1 
HETATM 2898 O  O     . HOH   K 6 .   ? 25.651  9.998   34.909  1.00 29.40 ? 369 HOH   A O     1 
HETATM 2899 O  O     . HOH   K 6 .   ? 23.554  14.511  33.774  1.00 20.81 ? 370 HOH   A O     1 
HETATM 2900 O  O     . HOH   K 6 .   ? 14.104  22.475  40.042  1.00 24.30 ? 371 HOH   A O     1 
HETATM 2901 O  O     . HOH   K 6 .   ? 25.568  9.335   30.454  1.00 31.99 ? 372 HOH   A O     1 
HETATM 2902 O  O     . HOH   K 6 .   ? 9.240   -1.139  54.391  1.00 22.29 ? 373 HOH   A O     1 
HETATM 2903 O  O     . HOH   K 6 .   ? 1.271   -3.233  34.362  1.00 31.26 ? 374 HOH   A O     1 
HETATM 2904 O  O     . HOH   K 6 .   ? -10.620 18.684  47.882  1.00 32.36 ? 375 HOH   A O     1 
HETATM 2905 O  O     . HOH   K 6 .   ? 15.168  -3.075  25.147  1.00 27.33 ? 376 HOH   A O     1 
HETATM 2906 O  O     . HOH   L 6 .   ? 23.324  5.507   -25.593 1.00 30.34 ? 301 HOH   B O     1 
HETATM 2907 O  O     . HOH   L 6 .   ? -0.396  -5.512  -2.206  1.00 29.18 ? 302 HOH   B O     1 
HETATM 2908 O  O     . HOH   L 6 .   ? 11.143  7.181   -14.620 1.00 29.33 ? 303 HOH   B O     1 
HETATM 2909 O  O     . HOH   L 6 .   ? -5.540  -0.747  -7.263  1.00 34.02 ? 304 HOH   B O     1 
HETATM 2910 O  O     . HOH   L 6 .   ? 18.206  -20.012 -20.501 1.00 43.00 ? 305 HOH   B O     1 
HETATM 2911 O  O     . HOH   L 6 .   ? 0.859   -17.727 -14.378 1.00 37.38 ? 306 HOH   B O     1 
HETATM 2912 O  O     . HOH   L 6 .   ? 3.163   -7.866  -5.227  1.00 26.24 ? 307 HOH   B O     1 
HETATM 2913 O  O     . HOH   L 6 .   ? 28.585  -4.423  8.718   1.00 30.14 ? 308 HOH   B O     1 
HETATM 2914 O  O     . HOH   L 6 .   ? 28.243  6.907   -24.072 1.00 32.94 ? 309 HOH   B O     1 
HETATM 2915 O  O     . HOH   L 6 .   ? 12.814  10.701  -12.118 1.00 35.32 ? 310 HOH   B O     1 
HETATM 2916 O  O     . HOH   L 6 .   ? -10.394 -4.430  -13.795 1.00 30.63 ? 311 HOH   B O     1 
HETATM 2917 O  O     . HOH   L 6 .   ? 16.642  2.750   -20.816 1.00 35.50 ? 312 HOH   B O     1 
HETATM 2918 O  O     . HOH   L 6 .   ? 17.374  9.232   0.962   1.00 33.35 ? 313 HOH   B O     1 
HETATM 2919 O  O     . HOH   L 6 .   ? 0.820   10.883  -2.960  1.00 26.82 ? 314 HOH   B O     1 
HETATM 2920 O  O     . HOH   L 6 .   ? 9.845   5.810   -19.132 1.00 30.90 ? 315 HOH   B O     1 
HETATM 2921 O  O     . HOH   L 6 .   ? 23.062  0.535   -26.607 1.00 36.28 ? 316 HOH   B O     1 
HETATM 2922 O  O     . HOH   L 6 .   ? 21.991  -11.386 -15.965 1.00 28.11 ? 317 HOH   B O     1 
HETATM 2923 O  O     . HOH   L 6 .   ? -6.310  -11.399 -12.216 1.00 27.56 ? 318 HOH   B O     1 
HETATM 2924 O  O     . HOH   L 6 .   ? 0.164   -0.361  -16.854 1.00 26.50 ? 319 HOH   B O     1 
HETATM 2925 O  O     . HOH   L 6 .   ? 31.368  -4.934  -18.133 1.00 27.28 ? 320 HOH   B O     1 
HETATM 2926 O  O     . HOH   L 6 .   ? 25.522  6.248   -27.307 1.00 33.17 ? 321 HOH   B O     1 
HETATM 2927 O  O     . HOH   L 6 .   ? 2.510   9.407   -14.725 1.00 34.15 ? 322 HOH   B O     1 
HETATM 2928 O  O     . HOH   L 6 .   ? 16.510  7.023   -20.405 1.00 30.51 ? 323 HOH   B O     1 
HETATM 2929 O  O     . HOH   L 6 .   ? 7.710   8.973   -14.622 1.00 27.87 ? 324 HOH   B O     1 
HETATM 2930 O  O     . HOH   L 6 .   ? -1.618  -5.869  -22.355 1.00 32.77 ? 325 HOH   B O     1 
HETATM 2931 O  O     . HOH   L 6 .   ? 12.657  -15.180 -8.372  1.00 28.17 ? 326 HOH   B O     1 
HETATM 2932 O  O     . HOH   L 6 .   ? 8.744   -2.815  0.589   1.00 23.97 ? 327 HOH   B O     1 
HETATM 2933 O  O     . HOH   L 6 .   ? 8.760   7.796   -16.665 1.00 26.54 ? 328 HOH   B O     1 
HETATM 2934 O  O     . HOH   L 6 .   ? 16.976  -11.410 -1.983  1.00 29.87 ? 329 HOH   B O     1 
HETATM 2935 O  O     . HOH   L 6 .   ? 12.241  3.941   -20.865 1.00 34.46 ? 330 HOH   B O     1 
HETATM 2936 O  O     . HOH   L 6 .   ? 9.908   9.764   -14.890 1.00 32.32 ? 331 HOH   B O     1 
HETATM 2937 O  O     . HOH   L 6 .   ? 9.437   -2.744  -19.776 1.00 25.04 ? 332 HOH   B O     1 
HETATM 2938 O  O     . HOH   L 6 .   ? 10.067  -14.051 -5.729  1.00 26.90 ? 333 HOH   B O     1 
HETATM 2939 O  O     . HOH   L 6 .   ? 4.229   7.528   -17.324 1.00 27.32 ? 334 HOH   B O     1 
HETATM 2940 O  O     . HOH   L 6 .   ? 20.034  7.359   4.469   1.00 27.18 ? 335 HOH   B O     1 
HETATM 2941 O  O     . HOH   L 6 .   ? 3.854   -11.309 -14.394 1.00 34.21 ? 336 HOH   B O     1 
HETATM 2942 O  O     . HOH   L 6 .   ? 18.167  -20.888 -14.529 1.00 31.63 ? 337 HOH   B O     1 
HETATM 2943 O  O     . HOH   L 6 .   ? 1.024   -11.950 -22.056 1.00 34.27 ? 338 HOH   B O     1 
HETATM 2944 O  O     . HOH   L 6 .   ? 20.525  -6.562  8.090   1.00 27.72 ? 339 HOH   B O     1 
HETATM 2945 O  O     . HOH   L 6 .   ? 28.652  -2.025  7.044   1.00 25.02 ? 340 HOH   B O     1 
HETATM 2946 O  O     . HOH   L 6 .   ? 14.034  2.644   -19.359 1.00 26.41 ? 341 HOH   B O     1 
HETATM 2947 O  O     . HOH   L 6 .   ? 30.558  -8.524  -2.326  1.00 35.16 ? 342 HOH   B O     1 
HETATM 2948 O  O     . HOH   L 6 .   ? 10.899  -9.904  -23.201 1.00 28.41 ? 343 HOH   B O     1 
HETATM 2949 O  O     . HOH   L 6 .   ? 15.184  8.112   1.974   1.00 33.64 ? 344 HOH   B O     1 
HETATM 2950 O  O     . HOH   L 6 .   ? 9.567   -5.350  0.660   1.00 22.59 ? 345 HOH   B O     1 
HETATM 2951 O  O     . HOH   L 6 .   ? -3.975  -9.670  -10.922 1.00 27.24 ? 346 HOH   B O     1 
HETATM 2952 O  O     . HOH   L 6 .   ? 27.796  6.757   -5.761  1.00 40.98 ? 347 HOH   B O     1 
HETATM 2953 O  O     . HOH   L 6 .   ? 17.975  11.426  -2.715  1.00 29.09 ? 348 HOH   B O     1 
HETATM 2954 O  O     . HOH   L 6 .   ? 32.534  -11.129 -24.681 1.00 40.07 ? 349 HOH   B O     1 
HETATM 2955 O  O     . HOH   L 6 .   ? 16.689  12.922  -4.778  1.00 35.23 ? 350 HOH   B O     1 
HETATM 2956 O  O     . HOH   L 6 .   ? -0.062  11.990  -6.171  1.00 34.25 ? 351 HOH   B O     1 
HETATM 2957 O  O     . HOH   L 6 .   ? 30.040  -12.019 -23.331 1.00 38.11 ? 352 HOH   B O     1 
HETATM 2958 O  O     . HOH   L 6 .   ? 16.843  11.479  -0.418  1.00 34.03 ? 353 HOH   B O     1 
HETATM 2959 O  O     . HOH   L 6 .   ? 12.769  -13.781 -5.260  1.00 33.59 ? 354 HOH   B O     1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N  N     . SER   A 3   ? 0.1131 0.6024 0.4311 0.0072  0.0792  -0.0133 0   SER   A N     
2    C  CA    . SER   A 3   ? 0.1090 0.5650 0.4097 0.0017  0.0749  -0.0071 0   SER   A CA    
3    C  C     . SER   A 3   ? 0.0945 0.5329 0.3999 0.0013  0.0643  -0.0074 0   SER   A C     
4    O  O     . SER   A 3   ? 0.0905 0.5415 0.4115 -0.0019 0.0613  -0.0085 0   SER   A O     
5    C  CB    . SER   A 3   ? 0.1190 0.5727 0.4124 -0.0130 0.0818  0.0030  0   SER   A CB    
6    O  OG    . SER   A 3   ? 0.1298 0.5557 0.4034 -0.0132 0.0795  0.0074  0   SER   A OG    
7    N  N     . MET   A 4   ? 0.0784 0.4894 0.3700 0.0059  0.0583  -0.0075 1   MET   A N     
8    C  CA    . MET   A 4   ? 0.0671 0.4593 0.3596 0.0075  0.0485  -0.0085 1   MET   A CA    
9    C  C     . MET   A 4   ? 0.0589 0.4328 0.3458 -0.0040 0.0466  -0.0010 1   MET   A C     
10   O  O     . MET   A 4   ? 0.0619 0.4255 0.3373 -0.0080 0.0500  0.0040  1   MET   A O     
11   C  CB    . MET   A 4   ? 0.0679 0.4391 0.3473 0.0171  0.0438  -0.0119 1   MET   A CB    
12   C  CG    . MET   A 4   ? 0.0718 0.4479 0.3537 0.0300  0.0412  -0.0202 1   MET   A CG    
13   S  SD    . MET   A 4   ? 0.0769 0.4215 0.3418 0.0357  0.0345  -0.0219 1   MET   A SD    
14   C  CE    . MET   A 4   ? 0.0876 0.4385 0.3418 0.0394  0.0414  -0.0245 1   MET   A CE    
15   N  N     . THR   A 5   ? 0.0480 0.4189 0.3429 -0.0074 0.0408  -0.0012 2   THR   A N     
16   C  CA    . THR   A 5   ? 0.0443 0.3964 0.3339 -0.0169 0.0379  0.0043  2   THR   A CA    
17   C  C     . THR   A 5   ? 0.0410 0.3681 0.3165 -0.0108 0.0338  0.0043  2   THR   A C     
18   O  O     . THR   A 5   ? 0.0364 0.3611 0.3115 -0.0017 0.0298  -0.0006 2   THR   A O     
19   C  CB    . THR   A 5   ? 0.0415 0.3988 0.3429 -0.0205 0.0319  0.0022  2   THR   A CB    
20   O  OG1   . THR   A 5   ? 0.0443 0.4278 0.3605 -0.0274 0.0361  0.0023  2   THR   A OG1   
21   C  CG2   . THR   A 5   ? 0.0472 0.3831 0.3419 -0.0288 0.0282  0.0062  2   THR   A CG2   
22   N  N     . GLU   A 6   ? 0.0447 0.3554 0.3095 -0.0160 0.0351  0.0099  3   GLU   A N     
23   C  CA    . GLU   A 6   ? 0.0407 0.3305 0.2942 -0.0111 0.0312  0.0101  3   GLU   A CA    
24   C  C     . GLU   A 6   ? 0.0369 0.3118 0.2894 -0.0157 0.0267  0.0118  3   GLU   A C     
25   O  O     . GLU   A 6   ? 0.0465 0.3187 0.2993 -0.0240 0.0283  0.0157  3   GLU   A O     
26   C  CB    . GLU   A 6   ? 0.0528 0.3347 0.2945 -0.0114 0.0349  0.0146  3   GLU   A CB    
27   C  CG    . GLU   A 6   ? 0.0598 0.3556 0.2996 -0.0073 0.0396  0.0128  3   GLU   A CG    
28   C  CD    . GLU   A 6   ? 0.0711 0.3598 0.2977 -0.0060 0.0418  0.0163  3   GLU   A CD    
29   O  OE1   . GLU   A 6   ? 0.0761 0.3485 0.2953 -0.0074 0.0393  0.0205  3   GLU   A OE1   
30   O  OE2   . GLU   A 6   ? 0.0762 0.3756 0.2995 -0.0025 0.0454  0.0143  3   GLU   A OE2   
31   N  N     . TYR   A 7   ? 0.0243 0.2891 0.2745 -0.0105 0.0215  0.0088  4   TYR   A N     
32   C  CA    . TYR   A 7   ? 0.0215 0.2720 0.2688 -0.0140 0.0177  0.0098  4   TYR   A CA    
33   C  C     . TYR   A 7   ? 0.0220 0.2558 0.2583 -0.0116 0.0178  0.0122  4   TYR   A C     
34   O  O     . TYR   A 7   ? 0.0186 0.2511 0.2521 -0.0059 0.0169  0.0103  4   TYR   A O     
35   C  CB    . TYR   A 7   ? 0.0151 0.2660 0.2662 -0.0103 0.0119  0.0054  4   TYR   A CB    
36   C  CG    . TYR   A 7   ? 0.0144 0.2826 0.2776 -0.0128 0.0105  0.0031  4   TYR   A CG    
37   C  CD1   . TYR   A 7   ? 0.0191 0.2882 0.2863 -0.0214 0.0092  0.0042  4   TYR   A CD1   
38   C  CD2   . TYR   A 7   ? 0.0112 0.2958 0.2823 -0.0065 0.0106  -0.0006 4   TYR   A CD2   
39   C  CE1   . TYR   A 7   ? 0.0194 0.3075 0.2997 -0.0247 0.0076  0.0019  4   TYR   A CE1   
40   C  CE2   . TYR   A 7   ? 0.0113 0.3157 0.2957 -0.0081 0.0094  -0.0029 4   TYR   A CE2   
41   C  CZ    . TYR   A 7   ? 0.0147 0.3220 0.3045 -0.0176 0.0077  -0.0016 4   TYR   A CZ    
42   O  OH    . TYR   A 7   ? 0.0150 0.3445 0.3197 -0.0202 0.0061  -0.0041 4   TYR   A OH    
43   N  N     . LYS   A 8   ? 0.0298 0.2525 0.2609 -0.0164 0.0189  0.0161  5   LYS   A N     
44   C  CA    . LYS   A 8   ? 0.0339 0.2425 0.2559 -0.0132 0.0188  0.0182  5   LYS   A CA    
45   C  C     . LYS   A 8   ? 0.0299 0.2275 0.2493 -0.0119 0.0151  0.0158  5   LYS   A C     
46   O  O     . LYS   A 8   ? 0.0363 0.2256 0.2541 -0.0162 0.0139  0.0160  5   LYS   A O     
47   C  CB    . LYS   A 8   ? 0.0498 0.2498 0.2658 -0.0172 0.0216  0.0237  5   LYS   A CB    
48   C  CG    . LYS   A 8   ? 0.0590 0.2674 0.2734 -0.0176 0.0257  0.0273  5   LYS   A CG    
49   C  CD    . LYS   A 8   ? 0.0805 0.2804 0.2893 -0.0242 0.0285  0.0336  5   LYS   A CD    
50   C  CE    . LYS   A 8   ? 0.0905 0.3002 0.2970 -0.0263 0.0333  0.0377  5   LYS   A CE    
51   N  NZ    . LYS   A 8   ? 0.0890 0.3184 0.3059 -0.0304 0.0360  0.0350  5   LYS   A NZ    
52   N  N     . LEU   A 9   ? 0.0223 0.2192 0.2402 -0.0067 0.0135  0.0134  6   LEU   A N     
53   C  CA    . LEU   A 9   ? 0.0229 0.2111 0.2373 -0.0053 0.0109  0.0114  6   LEU   A CA    
54   C  C     . LEU   A 9   ? 0.0241 0.2051 0.2327 -0.0019 0.0124  0.0128  6   LEU   A C     
55   O  O     . LEU   A 9   ? 0.0208 0.2063 0.2297 0.0006  0.0138  0.0139  6   LEU   A O     
56   C  CB    . LEU   A 9   ? 0.0180 0.2111 0.2348 -0.0026 0.0081  0.0083  6   LEU   A CB    
57   C  CG    . LEU   A 9   ? 0.0161 0.2207 0.2406 -0.0033 0.0066  0.0065  6   LEU   A CG    
58   C  CD1   . LEU   A 9   ? 0.0142 0.2211 0.2396 0.0014  0.0033  0.0035  6   LEU   A CD1   
59   C  CD2   . LEU   A 9   ? 0.0208 0.2255 0.2480 -0.0085 0.0047  0.0062  6   LEU   A CD2   
60   N  N     . VAL   A 10  ? 0.0296 0.2008 0.2333 -0.0016 0.0119  0.0120  7   VAL   A N     
61   C  CA    . VAL   A 10  ? 0.0315 0.1985 0.2311 0.0024  0.0137  0.0128  7   VAL   A CA    
62   C  C     . VAL   A 10  ? 0.0320 0.1962 0.2283 0.0036  0.0131  0.0103  7   VAL   A C     
63   O  O     . VAL   A 10  ? 0.0373 0.1954 0.2300 0.0018  0.0114  0.0085  7   VAL   A O     
64   C  CB    . VAL   A 10  ? 0.0419 0.1985 0.2368 0.0030  0.0149  0.0146  7   VAL   A CB    
65   C  CG1   . VAL   A 10  ? 0.0444 0.1991 0.2365 0.0091  0.0168  0.0150  7   VAL   A CG1   
66   C  CG2   . VAL   A 10  ? 0.0445 0.2021 0.2408 0.0004  0.0158  0.0182  7   VAL   A CG2   
67   N  N     . VAL   A 11  ? 0.0282 0.1971 0.2251 0.0060  0.0145  0.0104  8   VAL   A N     
68   C  CA    . VAL   A 11  ? 0.0305 0.1973 0.2234 0.0061  0.0149  0.0090  8   VAL   A CA    
69   C  C     . VAL   A 11  ? 0.0355 0.2010 0.2257 0.0097  0.0183  0.0089  8   VAL   A C     
70   O  O     . VAL   A 11  ? 0.0323 0.2050 0.2268 0.0123  0.0200  0.0102  8   VAL   A O     
71   C  CB    . VAL   A 11  ? 0.0270 0.1998 0.2223 0.0049  0.0144  0.0091  8   VAL   A CB    
72   C  CG1   . VAL   A 11  ? 0.0332 0.2016 0.2224 0.0035  0.0148  0.0086  8   VAL   A CG1   
73   C  CG2   . VAL   A 11  ? 0.0235 0.1986 0.2222 0.0037  0.0114  0.0087  8   VAL   A CG2   
74   N  N     . VAL   A 12  ? 0.0444 0.2015 0.2275 0.0104  0.0189  0.0070  9   VAL   A N     
75   C  CA    . VAL   A 12  ? 0.0525 0.2068 0.2316 0.0152  0.0224  0.0058  9   VAL   A CA    
76   C  C     . VAL   A 12  ? 0.0574 0.2122 0.2304 0.0150  0.0248  0.0041  9   VAL   A C     
77   O  O     . VAL   A 12  ? 0.0582 0.2105 0.2272 0.0112  0.0229  0.0039  9   VAL   A O     
78   C  CB    . VAL   A 12  ? 0.0646 0.2058 0.2380 0.0171  0.0215  0.0043  9   VAL   A CB    
79   C  CG1   . VAL   A 12  ? 0.0639 0.2035 0.2416 0.0167  0.0199  0.0072  9   VAL   A CG1   
80   C  CG2   . VAL   A 12  ? 0.0734 0.2039 0.2389 0.0134  0.0187  0.0015  9   VAL   A CG2   
81   N  N     . GLY   A 13  ? 0.0624 0.2211 0.2345 0.0199  0.0293  0.0029  10  GLY   A N     
82   C  CA    . GLY   A 13  ? 0.0693 0.2303 0.2350 0.0200  0.0334  0.0015  10  GLY   A CA    
83   C  C     . GLY   A 13  ? 0.0668 0.2432 0.2397 0.0234  0.0386  0.0020  10  GLY   A C     
84   O  O     . GLY   A 13  ? 0.0581 0.2436 0.2411 0.0244  0.0377  0.0038  10  GLY   A O     
85   N  N     . ALA   A 14  ? 0.0751 0.2558 0.2427 0.0246  0.0440  0.0003  11  ALA   A N     
86   C  CA    . ALA   A 14  ? 0.0749 0.2735 0.2501 0.0283  0.0501  0.0000  11  ALA   A CA    
87   C  C     . ALA   A 14  ? 0.0632 0.2764 0.2499 0.0217  0.0496  0.0036  11  ALA   A C     
88   O  O     . ALA   A 14  ? 0.0601 0.2682 0.2444 0.0141  0.0468  0.0059  11  ALA   A O     
89   C  CB    . ALA   A 14  ? 0.0872 0.2881 0.2532 0.0290  0.0565  -0.0021 11  ALA   A CB    
90   N  N     . GLY   A 15  ? 0.0587 0.2901 0.2575 0.0250  0.0521  0.0036  12  GLY   A N     
91   C  CA    . GLY   A 15  ? 0.0500 0.2959 0.2594 0.0177  0.0514  0.0062  12  GLY   A CA    
92   C  C     . GLY   A 15  ? 0.0550 0.3015 0.2591 0.0081  0.0549  0.0080  12  GLY   A C     
93   O  O     . GLY   A 15  ? 0.0649 0.3115 0.2613 0.0089  0.0605  0.0071  12  GLY   A O     
94   N  N     . GLY   A 16  ? 0.0507 0.2946 0.2565 -0.0007 0.0512  0.0106  13  GLY   A N     
95   C  CA    . GLY   A 16  ? 0.0577 0.3009 0.2588 -0.0110 0.0538  0.0133  13  GLY   A CA    
96   C  C     . GLY   A 16  ? 0.0666 0.2884 0.2514 -0.0138 0.0519  0.0149  13  GLY   A C     
97   O  O     . GLY   A 16  ? 0.0762 0.2951 0.2541 -0.0215 0.0545  0.0178  13  GLY   A O     
98   N  N     . VAL   A 17  ? 0.0645 0.2719 0.2434 -0.0084 0.0469  0.0133  14  VAL   A N     
99   C  CA    . VAL   A 17  ? 0.0732 0.2624 0.2378 -0.0103 0.0438  0.0144  14  VAL   A CA    
100  C  C     . VAL   A 17  ? 0.0703 0.2501 0.2352 -0.0147 0.0373  0.0164  14  VAL   A C     
101  O  O     . VAL   A 17  ? 0.0793 0.2456 0.2333 -0.0172 0.0344  0.0182  14  VAL   A O     
102  C  CB    . VAL   A 17  ? 0.0749 0.2542 0.2329 -0.0033 0.0414  0.0113  14  VAL   A CB    
103  C  CG1   . VAL   A 17  ? 0.0823 0.2667 0.2365 0.0021  0.0475  0.0085  14  VAL   A CG1   
104  C  CG2   . VAL   A 17  ? 0.0635 0.2418 0.2303 0.0005  0.0363  0.0098  14  VAL   A CG2   
105  N  N     . GLY   A 18  ? 0.0595 0.2462 0.2360 -0.0146 0.0347  0.0156  15  GLY   A N     
106  C  CA    . GLY   A 18  ? 0.0577 0.2376 0.2356 -0.0181 0.0293  0.0164  15  GLY   A CA    
107  C  C     . GLY   A 18  ? 0.0486 0.2253 0.2304 -0.0126 0.0242  0.0142  15  GLY   A C     
108  O  O     . GLY   A 18  ? 0.0500 0.2176 0.2291 -0.0131 0.0195  0.0141  15  GLY   A O     
109  N  N     . LYS   A 19  ? 0.0409 0.2256 0.2291 -0.0075 0.0254  0.0125  16  LYS   A N     
110  C  CA    . LYS   A 19  ? 0.0337 0.2168 0.2255 -0.0034 0.0217  0.0112  16  LYS   A CA    
111  C  C     . LYS   A 19  ? 0.0290 0.2154 0.2264 -0.0055 0.0187  0.0109  16  LYS   A C     
112  O  O     . LYS   A 19  ? 0.0280 0.2087 0.2243 -0.0047 0.0150  0.0101  16  LYS   A O     
113  C  CB    . LYS   A 19  ? 0.0303 0.2193 0.2262 0.0019  0.0238  0.0104  16  LYS   A CB    
114  C  CG    . LYS   A 19  ? 0.0375 0.2206 0.2265 0.0049  0.0263  0.0095  16  LYS   A CG    
115  C  CD    . LYS   A 19  ? 0.0380 0.2220 0.2289 0.0110  0.0276  0.0085  16  LYS   A CD    
116  C  CE    . LYS   A 19  ? 0.0355 0.2329 0.2342 0.0146  0.0304  0.0088  16  LYS   A CE    
117  N  NZ    . LYS   A 19  ? 0.0396 0.2455 0.2383 0.0136  0.0353  0.0083  16  LYS   A NZ    
118  N  N     . SER   A 20  ? 0.0277 0.2241 0.2308 -0.0082 0.0201  0.0110  17  SER   A N     
119  C  CA    . SER   A 20  ? 0.0255 0.2250 0.2327 -0.0105 0.0169  0.0098  17  SER   A CA    
120  C  C     . SER   A 20  ? 0.0337 0.2207 0.2346 -0.0151 0.0142  0.0097  17  SER   A C     
121  O  O     . SER   A 20  ? 0.0340 0.2157 0.2339 -0.0138 0.0104  0.0078  17  SER   A O     
122  C  CB    . SER   A 20  ? 0.0235 0.2382 0.2389 -0.0128 0.0184  0.0096  17  SER   A CB    
123  O  OG    . SER   A 20  ? 0.0180 0.2428 0.2385 -0.0065 0.0199  0.0098  17  SER   A OG    
124  N  N     . ALA   A 21  ? 0.0426 0.2239 0.2379 -0.0199 0.0162  0.0118  18  ALA   A N     
125  C  CA    . ALA   A 21  ? 0.0543 0.2204 0.2414 -0.0240 0.0131  0.0125  18  ALA   A CA    
126  C  C     . ALA   A 21  ? 0.0551 0.2099 0.2370 -0.0180 0.0089  0.0116  18  ALA   A C     
127  O  O     . ALA   A 21  ? 0.0608 0.2064 0.2399 -0.0174 0.0048  0.0101  18  ALA   A O     
128  C  CB    . ALA   A 21  ? 0.0657 0.2268 0.2457 -0.0301 0.0165  0.0161  18  ALA   A CB    
129  N  N     . LEU   A 22  ? 0.0512 0.2070 0.2318 -0.0137 0.0099  0.0121  19  LEU   A N     
130  C  CA    . LEU   A 22  ? 0.0516 0.2005 0.2293 -0.0085 0.0058  0.0110  19  LEU   A CA    
131  C  C     . LEU   A 22  ? 0.0441 0.1984 0.2290 -0.0047 0.0034  0.0079  19  LEU   A C     
132  O  O     . LEU   A 22  ? 0.0492 0.1981 0.2327 -0.0013 -0.0005 0.0063  19  LEU   A O     
133  C  CB    . LEU   A 22  ? 0.0499 0.2010 0.2262 -0.0059 0.0072  0.0113  19  LEU   A CB    
134  C  CG    . LEU   A 22  ? 0.0627 0.2059 0.2284 -0.0078 0.0083  0.0136  19  LEU   A CG    
135  C  CD1   . LEU   A 22  ? 0.0616 0.2082 0.2263 -0.0055 0.0105  0.0127  19  LEU   A CD1   
136  C  CD2   . LEU   A 22  ? 0.0742 0.2045 0.2310 -0.0065 0.0028  0.0147  19  LEU   A CD2   
137  N  N     . THR   A 23  ? 0.0347 0.2004 0.2267 -0.0043 0.0060  0.0072  20  THR   A N     
138  C  CA    . THR   A 23  ? 0.0282 0.2005 0.2256 -0.0010 0.0049  0.0050  20  THR   A CA    
139  C  C     . THR   A 23  ? 0.0339 0.2031 0.2303 -0.0019 0.0024  0.0026  20  THR   A C     
140  O  O     . THR   A 23  ? 0.0362 0.2034 0.2324 0.0017  -0.0001 0.0000  20  THR   A O     
141  C  CB    . THR   A 23  ? 0.0208 0.2038 0.2235 -0.0004 0.0079  0.0059  20  THR   A CB    
142  O  OG1   . THR   A 23  ? 0.0191 0.2013 0.2209 0.0008  0.0098  0.0075  20  THR   A OG1   
143  C  CG2   . THR   A 23  ? 0.0168 0.2065 0.2230 0.0023  0.0073  0.0045  20  THR   A CG2   
144  N  N     . ILE   A 24  ? 0.0371 0.2059 0.2329 -0.0070 0.0030  0.0030  21  ILE   A N     
145  C  CA    . ILE   A 24  ? 0.0461 0.2096 0.2396 -0.0094 0.0001  0.0002  21  ILE   A CA    
146  C  C     . ILE   A 24  ? 0.0594 0.2059 0.2450 -0.0081 -0.0035 -0.0005 21  ILE   A C     
147  O  O     . ILE   A 24  ? 0.0660 0.2061 0.2490 -0.0059 -0.0067 -0.0042 21  ILE   A O     
148  C  CB    . ILE   A 24  ? 0.0486 0.2169 0.2444 -0.0168 0.0013  0.0010  21  ILE   A CB    
149  C  CG1   . ILE   A 24  ? 0.0373 0.2231 0.2412 -0.0154 0.0034  0.0010  21  ILE   A CG1   
150  C  CG2   . ILE   A 24  ? 0.0611 0.2202 0.2529 -0.0211 -0.0025 -0.0023 21  ILE   A CG2   
151  C  CD1   . ILE   A 24  ? 0.0367 0.2332 0.2460 -0.0214 0.0054  0.0024  21  ILE   A CD1   
152  N  N     . GLN   A 25  ? 0.0656 0.2042 0.2462 -0.0090 -0.0032 0.0029  22  GLN   A N     
153  C  CA    . GLN   A 25  ? 0.0826 0.2042 0.2544 -0.0065 -0.0073 0.0030  22  GLN   A CA    
154  C  C     . GLN   A 25  ? 0.0808 0.2050 0.2556 0.0025  -0.0102 -0.0005 22  GLN   A C     
155  O  O     . GLN   A 25  ? 0.0922 0.2059 0.2627 0.0068  -0.0142 -0.0033 22  GLN   A O     
156  C  CB    . GLN   A 25  ? 0.0895 0.2037 0.2542 -0.0086 -0.0065 0.0077  22  GLN   A CB    
157  C  CG    . GLN   A 25  ? 0.1086 0.2039 0.2624 -0.0056 -0.0116 0.0090  22  GLN   A CG    
158  C  CD    . GLN   A 25  ? 0.1267 0.2044 0.2727 -0.0089 -0.0145 0.0086  22  GLN   A CD    
159  O  OE1   . GLN   A 25  ? 0.1329 0.2034 0.2779 -0.0029 -0.0188 0.0047  22  GLN   A OE1   
160  N  NE2   . GLN   A 25  ? 0.1359 0.2064 0.2761 -0.0187 -0.0122 0.0123  22  GLN   A NE2   
161  N  N     . LEU   A 26  ? 0.0695 0.2074 0.2514 0.0052  -0.0080 -0.0003 23  LEU   A N     
162  C  CA    . LEU   A 26  ? 0.0681 0.2129 0.2549 0.0126  -0.0097 -0.0034 23  LEU   A CA    
163  C  C     . LEU   A 26  ? 0.0694 0.2191 0.2590 0.0151  -0.0095 -0.0078 23  LEU   A C     
164  O  O     . LEU   A 26  ? 0.0748 0.2226 0.2641 0.0213  -0.0120 -0.0113 23  LEU   A O     
165  C  CB    . LEU   A 26  ? 0.0564 0.2144 0.2502 0.0129  -0.0071 -0.0020 23  LEU   A CB    
166  C  CG    . LEU   A 26  ? 0.0546 0.2223 0.2549 0.0187  -0.0083 -0.0047 23  LEU   A CG    
167  C  CD1   . LEU   A 26  ? 0.0603 0.2228 0.2585 0.0224  -0.0129 -0.0044 23  LEU   A CD1   
168  C  CD2   . LEU   A 26  ? 0.0453 0.2260 0.2525 0.0165  -0.0046 -0.0034 23  LEU   A CD2   
169  N  N     . ILE   A 27  ? 0.0645 0.2217 0.2566 0.0111  -0.0066 -0.0079 24  ILE   A N     
170  C  CA    . ILE   A 27  ? 0.0680 0.2303 0.2608 0.0132  -0.0065 -0.0123 24  ILE   A CA    
171  C  C     . ILE   A 27  ? 0.0835 0.2316 0.2690 0.0131  -0.0102 -0.0162 24  ILE   A C     
172  O  O     . ILE   A 27  ? 0.0890 0.2366 0.2729 0.0189  -0.0116 -0.0212 24  ILE   A O     
173  C  CB    . ILE   A 27  ? 0.0645 0.2377 0.2606 0.0090  -0.0036 -0.0107 24  ILE   A CB    
174  C  CG1   . ILE   A 27  ? 0.0549 0.2382 0.2563 0.0089  -0.0002 -0.0066 24  ILE   A CG1   
175  C  CG2   . ILE   A 27  ? 0.0684 0.2467 0.2631 0.0109  -0.0040 -0.0151 24  ILE   A CG2   
176  C  CD1   . ILE   A 27  ? 0.0517 0.2427 0.2567 0.0134  0.0011  -0.0074 24  ILE   A CD1   
177  N  N     . GLN   A 28  ? 0.0896 0.2270 0.2707 0.0062  -0.0114 -0.0141 25  GLN   A N     
178  C  CA    . GLN   A 28  ? 0.1066 0.2298 0.2805 0.0033  -0.0149 -0.0178 25  GLN   A CA    
179  C  C     . GLN   A 28  ? 0.1239 0.2250 0.2886 0.0034  -0.0186 -0.0168 25  GLN   A C     
180  O  O     . GLN   A 28  ? 0.1383 0.2248 0.2959 0.0011  -0.0218 -0.0200 25  GLN   A O     
181  C  CB    . GLN   A 28  ? 0.1051 0.2326 0.2807 -0.0068 -0.0138 -0.0162 25  GLN   A CB    
182  C  CG    . GLN   A 28  ? 0.0950 0.2419 0.2776 -0.0067 -0.0117 -0.0174 25  GLN   A CG    
183  C  CD    . GLN   A 28  ? 0.1039 0.2502 0.2827 -0.0032 -0.0142 -0.0241 25  GLN   A CD    
184  O  OE1   . GLN   A 28  ? 0.1201 0.2531 0.2923 0.0012  -0.0170 -0.0283 25  GLN   A OE1   
185  N  NE2   . GLN   A 28  ? 0.0962 0.2568 0.2782 -0.0040 -0.0135 -0.0252 25  GLN   A NE2   
186  N  N     . ASN   A 29  ? 0.1277 0.2262 0.2918 0.0055  -0.0183 -0.0123 26  ASN   A N     
187  C  CA    . ASN   A 29  ? 0.1483 0.2243 0.3015 0.0054  -0.0222 -0.0098 26  ASN   A CA    
188  C  C     . ASN   A 29  ? 0.1616 0.2256 0.3085 -0.0065 -0.0218 -0.0069 26  ASN   A C     
189  O  O     . ASN   A 29  ? 0.1816 0.2229 0.3175 -0.0083 -0.0257 -0.0071 26  ASN   A O     
190  C  CB    . ASN   A 29  ? 0.1697 0.2304 0.3163 0.0148  -0.0275 -0.0147 26  ASN   A CB    
191  C  CG    . ASN   A 29  ? 0.1669 0.2370 0.3186 0.0262  -0.0286 -0.0156 26  ASN   A CG    
192  O  OD1   . ASN   A 29  ? 0.1860 0.2448 0.3321 0.0308  -0.0323 -0.0131 26  ASN   A OD1   
193  N  ND2   . ASN   A 29  ? 0.1507 0.2425 0.3132 0.0297  -0.0253 -0.0187 26  ASN   A ND2   
194  N  N     . HIS   A 30  ? 0.1484 0.2279 0.3024 -0.0144 -0.0171 -0.0043 27  HIS   A N     
195  C  CA    . HIS   A 30  ? 0.1584 0.2335 0.3100 -0.0268 -0.0157 -0.0019 27  HIS   A CA    
196  C  C     . HIS   A 30  ? 0.1441 0.2347 0.3016 -0.0317 -0.0100 0.0034  27  HIS   A C     
197  O  O     . HIS   A 30  ? 0.1224 0.2312 0.2887 -0.0274 -0.0071 0.0031  27  HIS   A O     
198  C  CB    . HIS   A 30  ? 0.1585 0.2397 0.3145 -0.0307 -0.0170 -0.0073 27  HIS   A CB    
199  C  CG    . HIS   A 30  ? 0.1658 0.2508 0.3241 -0.0442 -0.0154 -0.0055 27  HIS   A CG    
200  N  ND1   . HIS   A 30  ? 0.1881 0.2535 0.3373 -0.0542 -0.0170 -0.0033 27  HIS   A ND1   
201  C  CD2   . HIS   A 30  ? 0.1521 0.2592 0.3214 -0.0493 -0.0126 -0.0058 27  HIS   A CD2   
202  C  CE1   . HIS   A 30  ? 0.1877 0.2650 0.3435 -0.0660 -0.0148 -0.0024 27  HIS   A CE1   
203  N  NE2   . HIS   A 30  ? 0.1651 0.2690 0.3338 -0.0624 -0.0123 -0.0042 27  HIS   A NE2   
204  N  N     . PHE   A 31  ? 0.1608 0.2425 0.3120 -0.0410 -0.0082 0.0083  28  PHE   A N     
205  C  CA    . PHE   A 31  ? 0.1535 0.2500 0.3094 -0.0467 -0.0020 0.0127  28  PHE   A CA    
206  C  C     . PHE   A 31  ? 0.1546 0.2673 0.3207 -0.0555 0.0004  0.0112  28  PHE   A C     
207  O  O     . PHE   A 31  ? 0.1661 0.2699 0.3290 -0.0652 -0.0011 0.0111  28  PHE   A O     
208  C  CB    . PHE   A 31  ? 0.1705 0.2513 0.3140 -0.0528 -0.0005 0.0189  28  PHE   A CB    
209  C  CG    . PHE   A 31  ? 0.1643 0.2606 0.3112 -0.0583 0.0068  0.0231  28  PHE   A CG    
210  C  CD1   . PHE   A 31  ? 0.1483 0.2603 0.3012 -0.0510 0.0100  0.0226  28  PHE   A CD1   
211  C  CD2   . PHE   A 31  ? 0.1775 0.2717 0.3208 -0.0710 0.0107  0.0274  28  PHE   A CD2   
212  C  CE1   . PHE   A 31  ? 0.1457 0.2706 0.3003 -0.0545 0.0169  0.0256  28  PHE   A CE1   
213  C  CE2   . PHE   A 31  ? 0.1749 0.2854 0.3214 -0.0751 0.0183  0.0307  28  PHE   A CE2   
214  C  CZ    . PHE   A 31  ? 0.1582 0.2837 0.3100 -0.0660 0.0214  0.0295  28  PHE   A CZ    
215  N  N     . VAL   A 32  ? 0.1440 0.2799 0.3217 -0.0524 0.0041  0.0104  29  VAL   A N     
216  C  CA    . VAL   A 32  ? 0.1432 0.2992 0.3322 -0.0597 0.0067  0.0097  29  VAL   A CA    
217  C  C     . VAL   A 32  ? 0.1511 0.3162 0.3416 -0.0659 0.0134  0.0146  29  VAL   A C     
218  O  O     . VAL   A 32  ? 0.1540 0.3228 0.3431 -0.0598 0.0171  0.0168  29  VAL   A O     
219  C  CB    . VAL   A 32  ? 0.1254 0.3010 0.3254 -0.0519 0.0063  0.0063  29  VAL   A CB    
220  C  CG1   . VAL   A 32  ? 0.1248 0.2938 0.3230 -0.0483 0.0005  0.0012  29  VAL   A CG1   
221  C  CG2   . VAL   A 32  ? 0.1160 0.2969 0.3169 -0.0420 0.0093  0.0079  29  VAL   A CG2   
222  N  N     . ASP   A 33  ? 0.1646 0.3331 0.3572 -0.0784 0.0151  0.0161  30  ASP   A N     
223  C  CA    . ASP   A 33  ? 0.1728 0.3541 0.3683 -0.0861 0.0226  0.0206  30  ASP   A CA    
224  C  C     . ASP   A 33  ? 0.1454 0.3565 0.3563 -0.0803 0.0266  0.0187  30  ASP   A C     
225  O  O     . ASP   A 33  ? 0.1458 0.3667 0.3575 -0.0780 0.0329  0.0211  30  ASP   A O     
226  C  CB    . ASP   A 33  ? 0.1967 0.3763 0.3925 -0.1025 0.0232  0.0223  30  ASP   A CB    
227  C  CG    . ASP   A 33  ? 0.2311 0.3806 0.4087 -0.1094 0.0224  0.0272  30  ASP   A CG    
228  O  OD1   . ASP   A 33  ? 0.2450 0.3925 0.4154 -0.1122 0.0282  0.0326  30  ASP   A OD1   
229  O  OD2   . ASP   A 33  ? 0.2529 0.3805 0.4225 -0.1108 0.0158  0.0253  30  ASP   A OD2   
230  N  N     . GLU   A 34  ? 0.1241 0.3470 0.3450 -0.0770 0.0223  0.0143  31  GLU   A N     
231  C  CA    . GLU   A 34  ? 0.1004 0.3489 0.3346 -0.0692 0.0247  0.0127  31  GLU   A CA    
232  C  C     . GLU   A 34  ? 0.0812 0.3285 0.3169 -0.0594 0.0187  0.0089  31  GLU   A C     
233  O  O     . GLU   A 34  ? 0.0827 0.3201 0.3151 -0.0620 0.0130  0.0062  31  GLU   A O     
234  C  CB    . GLU   A 34  ? 0.1035 0.3778 0.3523 -0.0780 0.0269  0.0122  31  GLU   A CB    
235  C  CG    . GLU   A 34  ? 0.1190 0.3875 0.3676 -0.0925 0.0232  0.0114  31  GLU   A CG    
236  C  CD    . GLU   A 34  ? 0.1245 0.4212 0.3884 -0.1034 0.0271  0.0119  31  GLU   A CD    
237  O  OE1   . GLU   A 34  ? 0.1226 0.4307 0.3892 -0.1053 0.0351  0.0153  31  GLU   A OE1   
238  O  OE2   . GLU   A 34  ? 0.1259 0.4343 0.3991 -0.1091 0.0220  0.0084  31  GLU   A OE2   
239  N  N     . TYR   A 35  ? 0.0572 0.3140 0.2968 -0.0487 0.0205  0.0088  32  TYR   A N     
240  C  CA    . TYR   A 35  ? 0.0423 0.3024 0.2843 -0.0397 0.0160  0.0063  32  TYR   A CA    
241  C  C     . TYR   A 35  ? 0.0297 0.3095 0.2811 -0.0322 0.0194  0.0070  32  TYR   A C     
242  O  O     . TYR   A 35  ? 0.0281 0.3062 0.2769 -0.0284 0.0244  0.0089  32  TYR   A O     
243  C  CB    . TYR   A 35  ? 0.0384 0.2794 0.2700 -0.0326 0.0145  0.0064  32  TYR   A CB    
244  C  CG    . TYR   A 35  ? 0.0319 0.2728 0.2633 -0.0261 0.0101  0.0041  32  TYR   A CG    
245  C  CD1   . TYR   A 35  ? 0.0348 0.2735 0.2651 -0.0295 0.0051  0.0009  32  TYR   A CD1   
246  C  CD2   . TYR   A 35  ? 0.0248 0.2662 0.2555 -0.0169 0.0110  0.0052  32  TYR   A CD2   
247  C  CE1   . TYR   A 35  ? 0.0325 0.2718 0.2611 -0.0235 0.0018  -0.0011 32  TYR   A CE1   
248  C  CE2   . TYR   A 35  ? 0.0211 0.2625 0.2505 -0.0119 0.0078  0.0040  32  TYR   A CE2   
249  C  CZ    . TYR   A 35  ? 0.0255 0.2663 0.2534 -0.0149 0.0035  0.0008  32  TYR   A CZ    
250  O  OH    . TYR   A 35  ? 0.0235 0.2646 0.2484 -0.0099 0.0010  -0.0004 32  TYR   A OH    
251  N  N     . ASP   A 36  ? 0.0216 0.3179 0.2819 -0.0298 0.0159  0.0052  33  ASP   A N     
252  C  CA    . ASP   A 36  ? 0.0161 0.3322 0.2861 -0.0215 0.0176  0.0056  33  ASP   A CA    
253  C  C     . ASP   A 36  ? 0.0138 0.3208 0.2779 -0.0114 0.0217  0.0075  33  ASP   A C     
254  O  O     . ASP   A 36  ? 0.0121 0.3042 0.2681 -0.0059 0.0196  0.0079  33  ASP   A O     
255  C  CB    . ASP   A 36  ? 0.0134 0.3384 0.2872 -0.0169 0.0111  0.0040  33  ASP   A CB    
256  C  CG    . ASP   A 36  ? 0.0102 0.3537 0.2927 -0.0063 0.0111  0.0047  33  ASP   A CG    
257  O  OD1   . ASP   A 36  ? 0.0096 0.3552 0.2933 0.0001  0.0165  0.0061  33  ASP   A OD1   
258  O  OD2   . ASP   A 36  ? 0.0102 0.3659 0.2975 -0.0041 0.0054  0.0036  33  ASP   A OD2   
259  N  N     . PRO   A 37  ? 0.0151 0.3316 0.2831 -0.0088 0.0277  0.0082  34  PRO   A N     
260  C  CA    . PRO   A 37  ? 0.0162 0.3201 0.2760 -0.0006 0.0313  0.0090  34  PRO   A CA    
261  C  C     . PRO   A 37  ? 0.0145 0.3169 0.2738 0.0117  0.0289  0.0091  34  PRO   A C     
262  O  O     . PRO   A 37  ? 0.0170 0.3036 0.2674 0.0169  0.0303  0.0096  34  PRO   A O     
263  C  CB    . PRO   A 37  ? 0.0207 0.3356 0.2836 -0.0015 0.0386  0.0090  34  PRO   A CB    
264  C  CG    . PRO   A 37  ? 0.0221 0.3528 0.2939 -0.0132 0.0394  0.0091  34  PRO   A CG    
265  C  CD    . PRO   A 37  ? 0.0174 0.3560 0.2966 -0.0141 0.0320  0.0079  34  PRO   A CD    
266  N  N     . THR   A 38  ? 0.0122 0.3277 0.2790 0.0151  0.0245  0.0089  35  THR   A N     
267  C  CA    . THR   A 38  ? 0.0139 0.3273 0.2791 0.0269  0.0219  0.0100  35  THR   A CA    
268  C  C     . THR   A 38  ? 0.0155 0.3128 0.2716 0.0267  0.0171  0.0115  35  THR   A C     
269  O  O     . THR   A 38  ? 0.0185 0.3116 0.2713 0.0348  0.0149  0.0133  35  THR   A O     
270  C  CB    . THR   A 38  ? 0.0141 0.3521 0.2918 0.0320  0.0190  0.0095  35  THR   A CB    
271  O  OG1   . THR   A 38  ? 0.0112 0.3561 0.2919 0.0254  0.0132  0.0089  35  THR   A OG1   
272  C  CG2   . THR   A 38  ? 0.0143 0.3739 0.3039 0.0313  0.0241  0.0077  35  THR   A CG2   
273  N  N     . ILE   A 39  ? 0.0144 0.3041 0.2668 0.0177  0.0157  0.0106  36  ILE   A N     
274  C  CA    . ILE   A 39  ? 0.0170 0.2954 0.2620 0.0175  0.0118  0.0113  36  ILE   A CA    
275  C  C     . ILE   A 39  ? 0.0173 0.2763 0.2529 0.0191  0.0140  0.0127  36  ILE   A C     
276  O  O     . ILE   A 39  ? 0.0145 0.2657 0.2475 0.0144  0.0161  0.0118  36  ILE   A O     
277  C  CB    . ILE   A 39  ? 0.0198 0.2985 0.2647 0.0086  0.0090  0.0089  36  ILE   A CB    
278  C  CG1   . ILE   A 39  ? 0.0226 0.3202 0.2761 0.0064  0.0052  0.0072  36  ILE   A CG1   
279  C  CG2   . ILE   A 39  ? 0.0200 0.2871 0.2565 0.0094  0.0064  0.0089  36  ILE   A CG2   
280  C  CD1   . ILE   A 39  ? 0.0279 0.3242 0.2809 -0.0032 0.0024  0.0041  36  ILE   A CD1   
281  N  N     . GLU   A 40  ? 0.0218 0.2747 0.2528 0.0251  0.0128  0.0151  37  GLU   A N     
282  C  CA    . GLU   A 40  ? 0.0251 0.2611 0.2478 0.0257  0.0140  0.0167  37  GLU   A CA    
283  C  C     . GLU   A 40  ? 0.0251 0.2596 0.2440 0.0238  0.0113  0.0175  37  GLU   A C     
284  O  O     . GLU   A 40  ? 0.0290 0.2694 0.2472 0.0272  0.0088  0.0192  37  GLU   A O     
285  C  CB    . GLU   A 40  ? 0.0325 0.2618 0.2522 0.0332  0.0153  0.0190  37  GLU   A CB    
286  C  CG    . GLU   A 40  ? 0.0374 0.2502 0.2487 0.0331  0.0156  0.0214  37  GLU   A CG    
287  C  CD    . GLU   A 40  ? 0.0474 0.2491 0.2545 0.0389  0.0172  0.0223  37  GLU   A CD    
288  O  OE1   . GLU   A 40  ? 0.0475 0.2485 0.2557 0.0394  0.0196  0.0195  37  GLU   A OE1   
289  O  OE2   . GLU   A 40  ? 0.0558 0.2497 0.2579 0.0430  0.0161  0.0255  37  GLU   A OE2   
290  N  N     . ASP   A 41  ? 0.0233 0.2510 0.2395 0.0189  0.0117  0.0161  38  ASP   A N     
291  C  CA    . ASP   A 41  ? 0.0231 0.2517 0.2359 0.0176  0.0099  0.0159  38  ASP   A CA    
292  C  C     . ASP   A 41  ? 0.0211 0.2413 0.2312 0.0145  0.0114  0.0150  38  ASP   A C     
293  O  O     . ASP   A 41  ? 0.0198 0.2337 0.2309 0.0127  0.0127  0.0142  38  ASP   A O     
294  C  CB    . ASP   A 41  ? 0.0221 0.2600 0.2375 0.0149  0.0070  0.0125  38  ASP   A CB    
295  C  CG    . ASP   A 41  ? 0.0270 0.2709 0.2385 0.0170  0.0042  0.0129  38  ASP   A CG    
296  O  OD1   . ASP   A 41  ? 0.0296 0.2690 0.2352 0.0184  0.0054  0.0149  38  ASP   A OD1   
297  O  OD2   . ASP   A 41  ? 0.0285 0.2824 0.2427 0.0171  0.0009  0.0114  38  ASP   A OD2   
298  N  N     . SER   A 42  ? 0.0225 0.2443 0.2295 0.0142  0.0111  0.0150  39  SER   A N     
299  C  CA    . SER   A 42  ? 0.0218 0.2402 0.2280 0.0122  0.0125  0.0139  39  SER   A CA    
300  C  C     . SER   A 42  ? 0.0194 0.2400 0.2263 0.0110  0.0107  0.0089  39  SER   A C     
301  O  O     . SER   A 42  ? 0.0186 0.2439 0.2239 0.0114  0.0087  0.0069  39  SER   A O     
302  C  CB    . SER   A 42  ? 0.0283 0.2478 0.2303 0.0126  0.0144  0.0171  39  SER   A CB    
303  O  OG    . SER   A 42  ? 0.0338 0.2601 0.2318 0.0144  0.0133  0.0168  39  SER   A OG    
304  N  N     . TYR   A 43  ? 0.0153 0.2317 0.2237 0.0099  0.0109  0.0069  40  TYR   A N     
305  C  CA    . TYR   A 43  ? 0.0170 0.2317 0.2250 0.0100  0.0089  0.0022  40  TYR   A CA    
306  C  C     . TYR   A 43  ? 0.0211 0.2374 0.2305 0.0116  0.0100  0.0009  40  TYR   A C     
307  O  O     . TYR   A 43  ? 0.0169 0.2312 0.2291 0.0106  0.0107  0.0026  40  TYR   A O     
308  C  CB    . TYR   A 43  ? 0.0158 0.2229 0.2244 0.0078  0.0072  0.0014  40  TYR   A CB    
309  C  CG    . TYR   A 43  ? 0.0143 0.2235 0.2238 0.0056  0.0069  0.0027  40  TYR   A CG    
310  C  CD1   . TYR   A 43  ? 0.0114 0.2227 0.2227 0.0061  0.0089  0.0061  40  TYR   A CD1   
311  C  CD2   . TYR   A 43  ? 0.0182 0.2284 0.2269 0.0033  0.0045  -0.0001 40  TYR   A CD2   
312  C  CE1   . TYR   A 43  ? 0.0117 0.2286 0.2256 0.0053  0.0089  0.0069  40  TYR   A CE1   
313  C  CE2   . TYR   A 43  ? 0.0182 0.2343 0.2300 0.0007  0.0042  0.0009  40  TYR   A CE2   
314  C  CZ    . TYR   A 43  ? 0.0138 0.2347 0.2289 0.0023  0.0066  0.0044  40  TYR   A CZ    
315  O  OH    . TYR   A 43  ? 0.0144 0.2445 0.2342 0.0010  0.0066  0.0051  40  TYR   A OH    
316  N  N     . ARG   A 44  ? 0.0309 0.2520 0.2385 0.0141  0.0101  -0.0025 41  ARG   A N     
317  C  CA    . ARG   A 44  ? 0.0377 0.2651 0.2483 0.0164  0.0120  -0.0042 41  ARG   A CA    
318  C  C     . ARG   A 44  ? 0.0393 0.2632 0.2503 0.0204  0.0093  -0.0096 41  ARG   A C     
319  O  O     . ARG   A 44  ? 0.0435 0.2612 0.2496 0.0217  0.0068  -0.0134 41  ARG   A O     
320  C  CB    . ARG   A 44  ? 0.0512 0.2885 0.2587 0.0178  0.0153  -0.0043 41  ARG   A CB    
321  C  CG    . ARG   A 44  ? 0.0626 0.3021 0.2679 0.0147  0.0179  0.0019  41  ARG   A CG    
322  C  CD    . ARG   A 44  ? 0.0810 0.3301 0.2817 0.0155  0.0217  0.0028  41  ARG   A CD    
323  N  NE    . ARG   A 44  ? 0.0966 0.3470 0.2983 0.0114  0.0253  0.0093  41  ARG   A NE    
324  C  CZ    . ARG   A 44  ? 0.1082 0.3676 0.3128 0.0093  0.0298  0.0105  41  ARG   A CZ    
325  N  NH1   . ARG   A 44  ? 0.1177 0.3756 0.3223 0.0040  0.0326  0.0168  41  ARG   A NH1   
326  N  NH2   . ARG   A 44  ? 0.1192 0.3891 0.3267 0.0125  0.0315  0.0052  41  ARG   A NH2   
327  N  N     . LYS   A 45  ? 0.0357 0.2633 0.2522 0.0222  0.0094  -0.0102 42  LYS   A N     
328  C  CA    . LYS   A 45  ? 0.0387 0.2638 0.2556 0.0279  0.0066  -0.0153 42  LYS   A CA    
329  C  C     . LYS   A 45  ? 0.0336 0.2729 0.2586 0.0312  0.0086  -0.0167 42  LYS   A C     
330  O  O     . LYS   A 45  ? 0.0259 0.2708 0.2568 0.0272  0.0097  -0.0130 42  LYS   A O     
331  C  CB    . LYS   A 45  ? 0.0428 0.2543 0.2581 0.0275  0.0021  -0.0147 42  LYS   A CB    
332  C  CG    . LYS   A 45  ? 0.0574 0.2592 0.2684 0.0335  -0.0020 -0.0196 42  LYS   A CG    
333  C  CD    . LYS   A 45  ? 0.0642 0.2515 0.2717 0.0326  -0.0063 -0.0177 42  LYS   A CD    
334  C  CE    . LYS   A 45  ? 0.0814 0.2560 0.2834 0.0393  -0.0109 -0.0220 42  LYS   A CE    
335  N  NZ    . LYS   A 45  ? 0.0898 0.2524 0.2884 0.0392  -0.0151 -0.0189 42  LYS   A NZ    
336  N  N     . GLN   A 46  ? 0.0373 0.2823 0.2622 0.0382  0.0090  -0.0223 43  GLN   A N     
337  C  CA    . GLN   A 46  ? 0.0374 0.2982 0.2714 0.0434  0.0105  -0.0251 43  GLN   A CA    
338  C  C     . GLN   A 46  ? 0.0390 0.2926 0.2755 0.0493  0.0044  -0.0276 43  GLN   A C     
339  O  O     . GLN   A 46  ? 0.0475 0.2858 0.2765 0.0543  0.0002  -0.0309 43  GLN   A O     
340  C  CB    . GLN   A 46  ? 0.0447 0.3154 0.2765 0.0495  0.0143  -0.0306 43  GLN   A CB    
341  C  CG    . GLN   A 46  ? 0.0465 0.3392 0.2895 0.0544  0.0177  -0.0333 43  GLN   A CG    
342  C  CD    . GLN   A 46  ? 0.0546 0.3595 0.2941 0.0589  0.0235  -0.0378 43  GLN   A CD    
343  O  OE1   . GLN   A 46  ? 0.0557 0.3616 0.2882 0.0537  0.0276  -0.0350 43  GLN   A OE1   
344  N  NE2   . GLN   A 46  ? 0.0623 0.3769 0.3059 0.0695  0.0238  -0.0448 43  GLN   A NE2   
345  N  N     . VAL   A 47  ? 0.0328 0.2965 0.2790 0.0482  0.0033  -0.0257 44  VAL   A N     
346  C  CA    . VAL   A 47  ? 0.0353 0.2925 0.2832 0.0529  -0.0033 -0.0266 44  VAL   A CA    
347  C  C     . VAL   A 47  ? 0.0336 0.3136 0.2956 0.0571  -0.0033 -0.0288 44  VAL   A C     
348  O  O     . VAL   A 47  ? 0.0280 0.3272 0.2980 0.0534  0.0026  -0.0284 44  VAL   A O     
349  C  CB    . VAL   A 47  ? 0.0336 0.2777 0.2774 0.0454  -0.0064 -0.0212 44  VAL   A CB    
350  C  CG1   . VAL   A 47  ? 0.0363 0.2611 0.2681 0.0417  -0.0062 -0.0193 44  VAL   A CG1   
351  C  CG2   . VAL   A 47  ? 0.0239 0.2797 0.2747 0.0365  -0.0030 -0.0171 44  VAL   A CG2   
352  N  N     . VAL   A 48  ? 0.0399 0.3171 0.3041 0.0644  -0.0101 -0.0307 45  VAL   A N     
353  C  CA    . VAL   A 48  ? 0.0385 0.3382 0.3176 0.0682  -0.0123 -0.0326 45  VAL   A CA    
354  C  C     . VAL   A 48  ? 0.0388 0.3293 0.3163 0.0646  -0.0193 -0.0290 45  VAL   A C     
355  O  O     . VAL   A 48  ? 0.0480 0.3177 0.3148 0.0693  -0.0254 -0.0284 45  VAL   A O     
356  C  CB    . VAL   A 48  ? 0.0491 0.3560 0.3323 0.0834  -0.0151 -0.0392 45  VAL   A CB    
357  C  CG1   . VAL   A 48  ? 0.0460 0.3825 0.3477 0.0866  -0.0163 -0.0413 45  VAL   A CG1   
358  C  CG2   . VAL   A 48  ? 0.0536 0.3628 0.3331 0.0888  -0.0090 -0.0440 45  VAL   A CG2   
359  N  N     . ILE   A 49  ? 0.0308 0.3345 0.3170 0.0555  -0.0184 -0.0263 46  ILE   A N     
360  C  CA    . ILE   A 49  ? 0.0322 0.3289 0.3164 0.0516  -0.0250 -0.0237 46  ILE   A CA    
361  C  C     . ILE   A 49  ? 0.0318 0.3543 0.3327 0.0536  -0.0289 -0.0263 46  ILE   A C     
362  O  O     . ILE   A 49  ? 0.0251 0.3688 0.3385 0.0469  -0.0241 -0.0265 46  ILE   A O     
363  C  CB    . ILE   A 49  ? 0.0261 0.3125 0.3040 0.0385  -0.0215 -0.0188 46  ILE   A CB    
364  C  CG1   . ILE   A 49  ? 0.0261 0.2923 0.2904 0.0374  -0.0175 -0.0168 46  ILE   A CG1   
365  C  CG2   . ILE   A 49  ? 0.0300 0.3081 0.3038 0.0350  -0.0283 -0.0170 46  ILE   A CG2   
366  C  CD1   . ILE   A 49  ? 0.0205 0.2793 0.2800 0.0267  -0.0131 -0.0126 46  ILE   A CD1   
367  N  N     . ASP   A 50  ? 0.0407 0.3612 0.3413 0.0630  -0.0377 -0.0281 47  ASP   A N     
368  C  CA    . ASP   A 50  ? 0.0418 0.3881 0.3588 0.0665  -0.0432 -0.0310 47  ASP   A CA    
369  C  C     . ASP   A 50  ? 0.0371 0.4139 0.3720 0.0706  -0.0372 -0.0353 47  ASP   A C     
370  O  O     . ASP   A 50  ? 0.0330 0.4382 0.3856 0.0665  -0.0374 -0.0368 47  ASP   A O     
371  C  CB    . ASP   A 50  ? 0.0371 0.3904 0.3589 0.0532  -0.0451 -0.0286 47  ASP   A CB    
372  C  CG    . ASP   A 50  ? 0.0422 0.3679 0.3462 0.0484  -0.0498 -0.0248 47  ASP   A CG    
373  O  OD1   . ASP   A 50  ? 0.0525 0.3607 0.3445 0.0573  -0.0562 -0.0243 47  ASP   A OD1   
374  O  OD2   . ASP   A 50  ? 0.0377 0.3580 0.3385 0.0360  -0.0464 -0.0223 47  ASP   A OD2   
375  N  N     . GLY   A 51  ? 0.0392 0.4102 0.3689 0.0779  -0.0317 -0.0375 48  GLY   A N     
376  C  CA    . GLY   A 51  ? 0.0373 0.4343 0.3802 0.0833  -0.0250 -0.0420 48  GLY   A CA    
377  C  C     . GLY   A 51  ? 0.0277 0.4349 0.3735 0.0704  -0.0139 -0.0395 48  GLY   A C     
378  O  O     . GLY   A 51  ? 0.0267 0.4566 0.3822 0.0732  -0.0067 -0.0427 48  GLY   A O     
379  N  N     . GLU   A 52  ? 0.0223 0.4135 0.3594 0.0567  -0.0123 -0.0338 49  GLU   A N     
380  C  CA    . GLU   A 52  ? 0.0163 0.4116 0.3527 0.0451  -0.0026 -0.0304 49  GLU   A CA    
381  C  C     . GLU   A 52  ? 0.0183 0.3932 0.3386 0.0487  0.0016  -0.0301 49  GLU   A C     
382  O  O     . GLU   A 52  ? 0.0197 0.3671 0.3255 0.0481  -0.0021 -0.0278 49  GLU   A O     
383  C  CB    . GLU   A 52  ? 0.0125 0.3986 0.3461 0.0300  -0.0033 -0.0247 49  GLU   A CB    
384  C  CG    . GLU   A 52  ? 0.0097 0.3969 0.3407 0.0188  0.0061  -0.0204 49  GLU   A CG    
385  C  CD    . GLU   A 52  ? 0.0092 0.3818 0.3343 0.0046  0.0062  -0.0147 49  GLU   A CD    
386  O  OE1   . GLU   A 52  ? 0.0104 0.3682 0.3305 0.0033  -0.0009 -0.0143 49  GLU   A OE1   
387  O  OE2   . GLU   A 52  ? 0.0097 0.3863 0.3346 -0.0046 0.0135  -0.0109 49  GLU   A OE2   
388  N  N     . THR   A 53  ? 0.0194 0.4078 0.3418 0.0517  0.0094  -0.0325 50  THR   A N     
389  C  CA    . THR   A 53  ? 0.0217 0.3920 0.3286 0.0527  0.0133  -0.0321 50  THR   A CA    
390  C  C     . THR   A 53  ? 0.0166 0.3803 0.3177 0.0388  0.0183  -0.0252 50  THR   A C     
391  O  O     . THR   A 53  ? 0.0149 0.3956 0.3229 0.0310  0.0246  -0.0226 50  THR   A O     
392  C  CB    . THR   A 53  ? 0.0278 0.4113 0.3350 0.0620  0.0190  -0.0378 50  THR   A CB    
393  O  OG1   . THR   A 53  ? 0.0353 0.4185 0.3453 0.0763  0.0130  -0.0442 50  THR   A OG1   
394  C  CG2   . THR   A 53  ? 0.0314 0.3960 0.3217 0.0616  0.0221  -0.0375 50  THR   A CG2   
395  N  N     . CYS   A 54  ? 0.0160 0.3539 0.3036 0.0360  0.0154  -0.0222 51  CYS   A N     
396  C  CA    . CYS   A 54  ? 0.0128 0.3420 0.2941 0.0247  0.0190  -0.0158 51  CYS   A CA    
397  C  C     . CYS   A 54  ? 0.0143 0.3211 0.2805 0.0260  0.0182  -0.0147 51  CYS   A C     
398  O  O     . CYS   A 54  ? 0.0177 0.3159 0.2790 0.0338  0.0149  -0.0187 51  CYS   A O     
399  C  CB    . CYS   A 54  ? 0.0100 0.3339 0.2946 0.0166  0.0152  -0.0121 51  CYS   A CB    
400  S  SG    . CYS   A 54  ? 0.0121 0.3169 0.2913 0.0219  0.0057  -0.0138 51  CYS   A SG    
401  N  N     . LEU   A 55  ? 0.0172 0.3171 0.2775 0.0181  0.0212  -0.0093 52  LEU   A N     
402  C  CA    . LEU   A 55  ? 0.0216 0.3045 0.2696 0.0181  0.0208  -0.0076 52  LEU   A CA    
403  C  C     . LEU   A 55  ? 0.0196 0.2881 0.2646 0.0122  0.0180  -0.0032 52  LEU   A C     
404  O  O     . LEU   A 55  ? 0.0149 0.2863 0.2633 0.0059  0.0196  0.0003  52  LEU   A O     
405  C  CB    . LEU   A 55  ? 0.0295 0.3198 0.2732 0.0154  0.0272  -0.0050 52  LEU   A CB    
406  C  CG    . LEU   A 55  ? 0.0396 0.3198 0.2717 0.0176  0.0270  -0.0051 52  LEU   A CG    
407  C  CD1   . LEU   A 55  ? 0.0394 0.3040 0.2670 0.0136  0.0240  -0.0008 52  LEU   A CD1   
408  C  CD2   . LEU   A 55  ? 0.0442 0.3207 0.2733 0.0257  0.0238  -0.0120 52  LEU   A CD2   
409  N  N     . LEU   A 56  ? 0.0194 0.2727 0.2578 0.0145  0.0141  -0.0038 53  LEU   A N     
410  C  CA    . LEU   A 56  ? 0.0192 0.2593 0.2534 0.0102  0.0123  -0.0003 53  LEU   A CA    
411  C  C     . LEU   A 56  ? 0.0219 0.2561 0.2489 0.0091  0.0145  0.0024  53  LEU   A C     
412  O  O     . LEU   A 56  ? 0.0199 0.2546 0.2437 0.0124  0.0144  0.0001  53  LEU   A O     
413  C  CB    . LEU   A 56  ? 0.0204 0.2499 0.2521 0.0132  0.0072  -0.0025 53  LEU   A CB    
414  C  CG    . LEU   A 56  ? 0.0228 0.2574 0.2602 0.0167  0.0035  -0.0055 53  LEU   A CG    
415  C  CD1   . LEU   A 56  ? 0.0279 0.2487 0.2595 0.0187  -0.0016 -0.0058 53  LEU   A CD1   
416  C  CD2   . LEU   A 56  ? 0.0195 0.2640 0.2645 0.0119  0.0041  -0.0040 53  LEU   A CD2   
417  N  N     . ASP   A 57  ? 0.0234 0.2545 0.2487 0.0047  0.0166  0.0069  54  ASP   A N     
418  C  CA    . ASP   A 57  ? 0.0255 0.2516 0.2444 0.0045  0.0180  0.0101  54  ASP   A CA    
419  C  C     . ASP   A 57  ? 0.0222 0.2370 0.2391 0.0035  0.0160  0.0114  54  ASP   A C     
420  O  O     . ASP   A 57  ? 0.0203 0.2307 0.2372 0.0004  0.0166  0.0137  54  ASP   A O     
421  C  CB    . ASP   A 57  ? 0.0332 0.2641 0.2501 0.0017  0.0221  0.0144  54  ASP   A CB    
422  C  CG    . ASP   A 57  ? 0.0414 0.2675 0.2507 0.0031  0.0225  0.0179  54  ASP   A CG    
423  O  OD1   . ASP   A 57  ? 0.0405 0.2613 0.2483 0.0056  0.0199  0.0168  54  ASP   A OD1   
424  O  OD2   . ASP   A 57  ? 0.0529 0.2813 0.2580 0.0016  0.0254  0.0219  54  ASP   A OD2   
425  N  N     . ILE   A 58  ? 0.0165 0.2274 0.2315 0.0058  0.0140  0.0095  55  ILE   A N     
426  C  CA    . ILE   A 58  ? 0.0168 0.2191 0.2300 0.0053  0.0127  0.0099  55  ILE   A CA    
427  C  C     . ILE   A 58  ? 0.0188 0.2196 0.2293 0.0066  0.0137  0.0121  55  ILE   A C     
428  O  O     . ILE   A 58  ? 0.0157 0.2210 0.2260 0.0079  0.0132  0.0113  55  ILE   A O     
429  C  CB    . ILE   A 58  ? 0.0163 0.2156 0.2291 0.0062  0.0100  0.0068  55  ILE   A CB    
430  C  CG1   . ILE   A 58  ? 0.0188 0.2197 0.2343 0.0071  0.0078  0.0044  55  ILE   A CG1   
431  C  CG2   . ILE   A 58  ? 0.0197 0.2116 0.2294 0.0053  0.0097  0.0076  55  ILE   A CG2   
432  C  CD1   . ILE   A 58  ? 0.0203 0.2177 0.2340 0.0095  0.0050  0.0015  55  ILE   A CD1   
433  N  N     . LEU   A 59  ? 0.0228 0.2175 0.2313 0.0065  0.0147  0.0144  56  LEU   A N     
434  C  CA    . LEU   A 59  ? 0.0259 0.2200 0.2327 0.0095  0.0155  0.0161  56  LEU   A CA    
435  C  C     . LEU   A 59  ? 0.0247 0.2164 0.2316 0.0099  0.0155  0.0143  56  LEU   A C     
436  O  O     . LEU   A 59  ? 0.0247 0.2093 0.2292 0.0090  0.0158  0.0136  56  LEU   A O     
437  C  CB    . LEU   A 59  ? 0.0370 0.2239 0.2403 0.0105  0.0167  0.0195  56  LEU   A CB    
438  C  CG    . LEU   A 59  ? 0.0439 0.2306 0.2454 0.0158  0.0169  0.0215  56  LEU   A CG    
439  C  CD1   . LEU   A 59  ? 0.0441 0.2405 0.2463 0.0177  0.0159  0.0228  56  LEU   A CD1   
440  C  CD2   . LEU   A 59  ? 0.0561 0.2306 0.2522 0.0175  0.0177  0.0244  56  LEU   A CD2   
441  N  N     . ASP   A 60  ? 0.0210 0.2194 0.2301 0.0104  0.0152  0.0133  57  ASP   A N     
442  C  CA    . ASP   A 60  ? 0.0233 0.2221 0.2328 0.0098  0.0163  0.0122  57  ASP   A CA    
443  C  C     . ASP   A 60  ? 0.0251 0.2289 0.2363 0.0143  0.0180  0.0135  57  ASP   A C     
444  O  O     . ASP   A 60  ? 0.0230 0.2338 0.2368 0.0164  0.0168  0.0146  57  ASP   A O     
445  C  CB    . ASP   A 60  ? 0.0212 0.2249 0.2328 0.0065  0.0150  0.0106  57  ASP   A CB    
446  C  CG    . ASP   A 60  ? 0.0243 0.2309 0.2368 0.0044  0.0169  0.0104  57  ASP   A CG    
447  O  OD1   . ASP   A 60  ? 0.0256 0.2278 0.2350 0.0051  0.0191  0.0107  57  ASP   A OD1   
448  O  OD2   . ASP   A 60  ? 0.0257 0.2385 0.2412 0.0013  0.0160  0.0096  57  ASP   A OD2   
449  N  N     . THR   A 61  ? 0.0307 0.2296 0.2394 0.0164  0.0202  0.0132  58  THR   A N     
450  C  CA    . THR   A 61  ? 0.0403 0.2407 0.2493 0.0229  0.0218  0.0140  58  THR   A CA    
451  C  C     . THR   A 61  ? 0.0464 0.2590 0.2604 0.0250  0.0244  0.0127  58  THR   A C     
452  O  O     . THR   A 61  ? 0.0435 0.2590 0.2581 0.0205  0.0258  0.0115  58  THR   A O     
453  C  CB    . THR   A 61  ? 0.0455 0.2314 0.2474 0.0247  0.0227  0.0135  58  THR   A CB    
454  O  OG1   . THR   A 61  ? 0.0449 0.2279 0.2437 0.0221  0.0244  0.0111  58  THR   A OG1   
455  C  CG2   . THR   A 61  ? 0.0464 0.2228 0.2451 0.0215  0.0205  0.0150  58  THR   A CG2   
456  N  N     . ALA   A 62  ? 0.0625 0.2809 0.2793 0.0324  0.0249  0.0134  59  ALA   A N     
457  C  CA    . ALA   A 62  ? 0.0770 0.3114 0.3010 0.0357  0.0276  0.0120  59  ALA   A CA    
458  C  C     . ALA   A 62  ? 0.1053 0.3347 0.3256 0.0440  0.0310  0.0104  59  ALA   A C     
459  O  O     . ALA   A 62  ? 0.1268 0.3398 0.3393 0.0479  0.0301  0.0108  59  ALA   A O     
460  C  CB    . ALA   A 62  ? 0.0735 0.3228 0.3055 0.0388  0.0246  0.0132  59  ALA   A CB    
461  N  N     . GLY   A 63  ? 0.1232 0.3669 0.3491 0.0465  0.0352  0.0084  60  GLY   A N     
462  C  CA    . GLY   A 63  ? 0.1411 0.3803 0.3628 0.0561  0.0387  0.0059  60  GLY   A CA    
463  C  C     . GLY   A 63  ? 0.1630 0.3983 0.3847 0.0672  0.0357  0.0071  60  GLY   A C     
464  O  O     . GLY   A 63  ? 0.1745 0.4230 0.4044 0.0693  0.0326  0.0092  60  GLY   A O     
465  N  N     . GLN   A 64  ? 0.1811 0.3968 0.3926 0.0739  0.0358  0.0060  61  GLN   A N     
466  C  CA    . GLN   A 64  ? 0.1989 0.4105 0.4098 0.0861  0.0331  0.0074  61  GLN   A CA    
467  C  C     . GLN   A 64  ? 0.2087 0.4121 0.4135 0.0971  0.0370  0.0028  61  GLN   A C     
468  O  O     . GLN   A 64  ? 0.2166 0.3971 0.4092 0.0967  0.0370  0.0013  61  GLN   A O     
469  C  CB    . GLN   A 64  ? 0.2094 0.3989 0.4109 0.0829  0.0284  0.0115  61  GLN   A CB    
470  C  CG    . GLN   A 64  ? 0.2059 0.4059 0.4133 0.0763  0.0248  0.0155  61  GLN   A CG    
471  C  CD    . GLN   A 64  ? 0.2054 0.3852 0.4033 0.0702  0.0222  0.0189  61  GLN   A CD    
472  O  OE1   . GLN   A 64  ? 0.2280 0.3946 0.4199 0.0640  0.0235  0.0173  61  GLN   A OE1   
473  N  NE2   . GLN   A 64  ? 0.2243 0.4033 0.4210 0.0718  0.0186  0.0235  61  GLN   A NE2   
474  N  N     . GLU   A 65  ? 0.2116 0.4347 0.4250 0.1072  0.0402  0.0001  62  GLU   A N     
475  C  CA    . GLU   A 65  ? 0.2270 0.4431 0.4336 0.1174  0.0452  -0.0057 62  GLU   A CA    
476  C  C     . GLU   A 65  ? 0.2478 0.4340 0.4405 0.1278  0.0420  -0.0063 62  GLU   A C     
477  O  O     . GLU   A 65  ? 0.2680 0.4348 0.4482 0.1289  0.0443  -0.0106 62  GLU   A O     
478  C  CB    . GLU   A 65  ? 0.2288 0.4755 0.4487 0.1265  0.0506  -0.0091 62  GLU   A CB    
479  C  CG    . GLU   A 65  ? 0.2218 0.4882 0.4477 0.1151  0.0568  -0.0106 62  GLU   A CG    
480  C  CD    . GLU   A 65  ? 0.2344 0.4847 0.4461 0.1096  0.0614  -0.0140 62  GLU   A CD    
481  O  OE1   . GLU   A 65  ? 0.2221 0.4855 0.4362 0.0999  0.0661  -0.0142 62  GLU   A OE1   
482  O  OE2   . GLU   A 65  ? 0.2591 0.4829 0.4561 0.1148  0.0601  -0.0166 62  GLU   A OE2   
483  N  N     . GLU   A 66  ? 0.2486 0.4297 0.4421 0.1346  0.0366  -0.0019 63  GLU   A N     
484  C  CA    . GLU   A 66  ? 0.2687 0.4194 0.4480 0.1453  0.0335  -0.0019 63  GLU   A CA    
485  C  C     . GLU   A 66  ? 0.2622 0.3854 0.4298 0.1339  0.0289  0.0030  63  GLU   A C     
486  O  O     . GLU   A 66  ? 0.2486 0.3777 0.4193 0.1189  0.0292  0.0046  63  GLU   A O     
487  C  CB    . GLU   A 66  ? 0.2822 0.4432 0.4681 0.1616  0.0302  0.0003  63  GLU   A CB    
488  C  CG    . GLU   A 66  ? 0.2943 0.4774 0.4892 0.1757  0.0354  -0.0062 63  GLU   A CG    
489  C  CD    . GLU   A 66  ? 0.3055 0.5092 0.5123 0.1910  0.0319  -0.0043 63  GLU   A CD    
490  O  OE1   . GLU   A 66  ? 0.3111 0.5153 0.5197 0.1884  0.0255  0.0024  63  GLU   A OE1   
491  O  OE2   . GLU   A 66  ? 0.3222 0.5424 0.5360 0.2061  0.0356  -0.0098 63  GLU   A OE2   
492  N  N     . TYR   A 67  ? 0.2718 0.3656 0.4261 0.1408  0.0253  0.0049  64  TYR   A N     
493  C  CA    . TYR   A 67  ? 0.2650 0.3343 0.4090 0.1307  0.0211  0.0107  64  TYR   A CA    
494  C  C     . TYR   A 67  ? 0.2312 0.3187 0.3845 0.1241  0.0183  0.0177  64  TYR   A C     
495  O  O     . TYR   A 67  ? 0.2224 0.3291 0.3845 0.1332  0.0167  0.0199  64  TYR   A O     
496  C  CB    . TYR   A 67  ? 0.3074 0.3436 0.4361 0.1407  0.0175  0.0127  64  TYR   A CB    
497  C  CG    . TYR   A 67  ? 0.3202 0.3343 0.4393 0.1300  0.0135  0.0204  64  TYR   A CG    
498  C  CD1   . TYR   A 67  ? 0.3211 0.3254 0.4365 0.1129  0.0142  0.0202  64  TYR   A CD1   
499  C  CD2   . TYR   A 67  ? 0.3386 0.3440 0.4528 0.1364  0.0091  0.0283  64  TYR   A CD2   
500  C  CE1   . TYR   A 67  ? 0.3301 0.3180 0.4384 0.1020  0.0116  0.0273  64  TYR   A CE1   
501  C  CE2   . TYR   A 67  ? 0.3519 0.3383 0.4567 0.1254  0.0065  0.0360  64  TYR   A CE2   
502  C  CZ    . TYR   A 67  ? 0.3470 0.3254 0.4494 0.1078  0.0082  0.0353  64  TYR   A CZ    
503  O  OH    . TYR   A 67  ? 0.3645 0.3273 0.4590 0.0960  0.0067  0.0427  64  TYR   A OH    
504  N  N     . SER   A 68  ? 0.2047 0.2873 0.3562 0.1086  0.0177  0.0208  65  SER   A N     
505  C  CA    . SER   A 68  ? 0.1816 0.2792 0.3397 0.1015  0.0156  0.0266  65  SER   A CA    
506  C  C     . SER   A 68  ? 0.1847 0.2601 0.3321 0.0912  0.0137  0.0320  65  SER   A C     
507  O  O     . SER   A 68  ? 0.1799 0.2482 0.3254 0.0797  0.0152  0.0300  65  SER   A O     
508  C  CB    . SER   A 68  ? 0.1535 0.2768 0.3241 0.0925  0.0181  0.0236  65  SER   A CB    
509  O  OG    . SER   A 68  ? 0.1377 0.2738 0.3135 0.0856  0.0160  0.0281  65  SER   A OG    
510  N  N     . ALA   A 69  ? 0.1942 0.2598 0.3348 0.0954  0.0103  0.0389  66  ALA   A N     
511  C  CA    . ALA   A 69  ? 0.2030 0.2512 0.3339 0.0851  0.0091  0.0456  66  ALA   A CA    
512  C  C     . ALA   A 69  ? 0.1771 0.2439 0.3165 0.0711  0.0110  0.0456  66  ALA   A C     
513  O  O     . ALA   A 69  ? 0.1750 0.2323 0.3109 0.0588  0.0122  0.0469  66  ALA   A O     
514  C  CB    . ALA   A 69  ? 0.2201 0.2609 0.3430 0.0930  0.0054  0.0536  66  ALA   A CB    
515  N  N     . MET   A 70  ? 0.1563 0.2505 0.3075 0.0729  0.0110  0.0440  67  MET   A N     
516  C  CA    . MET   A 70  ? 0.1366 0.2472 0.2948 0.0614  0.0122  0.0437  67  MET   A CA    
517  C  C     . MET   A 70  ? 0.1259 0.2385 0.2891 0.0530  0.0149  0.0378  67  MET   A C     
518  O  O     . MET   A 70  ? 0.1154 0.2302 0.2800 0.0425  0.0158  0.0382  67  MET   A O     
519  C  CB    . MET   A 70  ? 0.1216 0.2576 0.2890 0.0650  0.0106  0.0435  67  MET   A CB    
520  C  CG    . MET   A 70  ? 0.1352 0.2689 0.2957 0.0721  0.0070  0.0500  67  MET   A CG    
521  S  SD    . MET   A 70  ? 0.1200 0.2809 0.2876 0.0720  0.0040  0.0507  67  MET   A SD    
522  C  CE    . MET   A 70  ? 0.1142 0.2728 0.2775 0.0580  0.0066  0.0525  67  MET   A CE    
523  N  N     . ARG   A 71  ? 0.1304 0.2410 0.2950 0.0577  0.0162  0.0325  68  ARG   A N     
524  C  CA    . ARG   A 71  ? 0.1226 0.2327 0.2891 0.0505  0.0182  0.0272  68  ARG   A CA    
525  C  C     . ARG   A 71  ? 0.1335 0.2213 0.2909 0.0431  0.0175  0.0282  68  ARG   A C     
526  O  O     . ARG   A 71  ? 0.1215 0.2126 0.2817 0.0333  0.0177  0.0273  68  ARG   A O     
527  C  CB    . ARG   A 71  ? 0.1318 0.2440 0.2993 0.0580  0.0201  0.0215  68  ARG   A CB    
528  C  CG    . ARG   A 71  ? 0.1323 0.2434 0.2994 0.0513  0.0218  0.0164  68  ARG   A CG    
529  C  CD    . ARG   A 71  ? 0.1416 0.2585 0.3093 0.0569  0.0249  0.0109  68  ARG   A CD    
530  N  NE    . ARG   A 71  ? 0.1708 0.2711 0.3298 0.0664  0.0252  0.0088  68  ARG   A NE    
531  C  CZ    . ARG   A 71  ? 0.1831 0.2901 0.3440 0.0783  0.0273  0.0067  68  ARG   A CZ    
532  N  NH1   . ARG   A 71  ? 0.1759 0.3083 0.3481 0.0809  0.0297  0.0061  68  ARG   A NH1   
533  N  NH2   . ARG   A 71  ? 0.2100 0.2977 0.3611 0.0874  0.0271  0.0045  68  ARG   A NH2   
534  N  N     . ASP   A 72  ? 0.1526 0.2189 0.2998 0.0482  0.0164  0.0303  69  ASP   A N     
535  C  CA    . ASP   A 72  ? 0.1701 0.2131 0.3079 0.0401  0.0154  0.0318  69  ASP   A CA    
536  C  C     . ASP   A 72  ? 0.1605 0.2105 0.3014 0.0285  0.0157  0.0370  69  ASP   A C     
537  O  O     . ASP   A 72  ? 0.1623 0.2089 0.3039 0.0175  0.0157  0.0357  69  ASP   A O     
538  C  CB    . ASP   A 72  ? 0.1985 0.2150 0.3233 0.0475  0.0138  0.0348  69  ASP   A CB    
539  C  CG    . ASP   A 72  ? 0.2119 0.2167 0.3314 0.0580  0.0139  0.0283  69  ASP   A CG    
540  O  OD1   . ASP   A 72  ? 0.1969 0.2168 0.3231 0.0601  0.0158  0.0220  69  ASP   A OD1   
541  O  OD2   . ASP   A 72  ? 0.2401 0.2196 0.3476 0.0641  0.0122  0.0295  69  ASP   A OD2   
542  N  N     . GLN   A 73  ? 0.1543 0.2158 0.2974 0.0312  0.0157  0.0422  70  GLN   A N     
543  C  CA    . GLN   A 73  ? 0.1499 0.2181 0.2943 0.0217  0.0167  0.0471  70  GLN   A CA    
544  C  C     . GLN   A 73  ? 0.1268 0.2155 0.2826 0.0144  0.0180  0.0428  70  GLN   A C     
545  O  O     . GLN   A 73  ? 0.1256 0.2166 0.2832 0.0043  0.0192  0.0442  70  GLN   A O     
546  C  CB    . GLN   A 73  ? 0.1511 0.2269 0.2931 0.0272  0.0162  0.0532  70  GLN   A CB    
547  C  CG    . GLN   A 73  ? 0.1498 0.2321 0.2908 0.0178  0.0181  0.0583  70  GLN   A CG    
548  C  CD    . GLN   A 73  ? 0.1664 0.2316 0.3010 0.0067  0.0197  0.0619  70  GLN   A CD    
549  O  OE1   . GLN   A 73  ? 0.1831 0.2268 0.3113 0.0060  0.0185  0.0613  70  GLN   A OE1   
550  N  NE2   . GLN   A 73  ? 0.1640 0.2392 0.3001 -0.0025 0.0225  0.0654  70  GLN   A NE2   
551  N  N     . TYR   A 74  ? 0.1104 0.2139 0.2737 0.0194  0.0178  0.0378  71  TYR   A N     
552  C  CA    . TYR   A 74  ? 0.0916 0.2112 0.2642 0.0133  0.0184  0.0338  71  TYR   A CA    
553  C  C     . TYR   A 74  ? 0.0952 0.2059 0.2672 0.0069  0.0179  0.0300  71  TYR   A C     
554  O  O     . TYR   A 74  ? 0.0858 0.2058 0.2637 0.0002  0.0177  0.0284  71  TYR   A O     
555  C  CB    . TYR   A 74  ? 0.0751 0.2122 0.2549 0.0182  0.0183  0.0306  71  TYR   A CB    
556  C  CG    . TYR   A 74  ? 0.0726 0.2104 0.2539 0.0233  0.0185  0.0261  71  TYR   A CG    
557  C  CD1   . TYR   A 74  ? 0.0728 0.2053 0.2533 0.0205  0.0186  0.0218  71  TYR   A CD1   
558  C  CD2   . TYR   A 74  ? 0.0695 0.2168 0.2537 0.0309  0.0185  0.0260  71  TYR   A CD2   
559  C  CE1   . TYR   A 74  ? 0.0711 0.2064 0.2520 0.0249  0.0197  0.0180  71  TYR   A CE1   
560  C  CE2   . TYR   A 74  ? 0.0670 0.2187 0.2537 0.0350  0.0198  0.0220  71  TYR   A CE2   
561  C  CZ    . TYR   A 74  ? 0.0692 0.2144 0.2535 0.0322  0.0208  0.0182  71  TYR   A CZ    
562  O  OH    . TYR   A 74  ? 0.0672 0.2182 0.2530 0.0362  0.0229  0.0148  71  TYR   A OH    
563  N  N     . MET   A 75  ? 0.1089 0.2032 0.2741 0.0101  0.0171  0.0280  72  MET   A N     
564  C  CA    . MET   A 75  ? 0.1160 0.2004 0.2788 0.0039  0.0157  0.0238  72  MET   A CA    
565  C  C     . MET   A 75  ? 0.1270 0.2025 0.2878 -0.0066 0.0152  0.0272  72  MET   A C     
566  O  O     . MET   A 75  ? 0.1241 0.2037 0.2890 -0.0143 0.0139  0.0246  72  MET   A O     
567  C  CB    . MET   A 75  ? 0.1300 0.1985 0.2844 0.0105  0.0153  0.0198  72  MET   A CB    
568  C  CG    . MET   A 75  ? 0.1168 0.1991 0.2754 0.0178  0.0167  0.0160  72  MET   A CG    
569  S  SD    . MET   A 75  ? 0.1344 0.2024 0.2835 0.0256  0.0173  0.0102  72  MET   A SD    
570  C  CE    . MET   A 75  ? 0.1152 0.2053 0.2715 0.0290  0.0198  0.0070  72  MET   A CE    
571  N  N     . ARG   A 76  ? 0.1412 0.2054 0.2956 -0.0062 0.0160  0.0331  73  ARG   A N     
572  C  CA    . ARG   A 76  ? 0.1539 0.2111 0.3063 -0.0176 0.0166  0.0378  73  ARG   A CA    
573  C  C     . ARG   A 76  ? 0.1346 0.2164 0.2983 -0.0239 0.0186  0.0391  73  ARG   A C     
574  O  O     . ARG   A 76  ? 0.1359 0.2216 0.3042 -0.0344 0.0186  0.0387  73  ARG   A O     
575  C  CB    . ARG   A 76  ? 0.1755 0.2168 0.3173 -0.0147 0.0175  0.0454  73  ARG   A CB    
576  C  CG    . ARG   A 76  ? 0.2033 0.2154 0.3321 -0.0097 0.0154  0.0450  73  ARG   A CG    
577  C  CD    . ARG   A 76  ? 0.2288 0.2219 0.3455 -0.0080 0.0156  0.0536  73  ARG   A CD    
578  N  NE    . ARG   A 76  ? 0.2509 0.2205 0.3565 0.0033  0.0132  0.0521  73  ARG   A NE    
579  C  CZ    . ARG   A 76  ? 0.2536 0.2235 0.3562 0.0179  0.0125  0.0536  73  ARG   A CZ    
580  N  NH1   . ARG   A 76  ? 0.2372 0.2282 0.3456 0.0221  0.0135  0.0575  73  ARG   A NH1   
581  N  NH2   . ARG   A 76  ? 0.2741 0.2226 0.3673 0.0283  0.0105  0.0510  73  ARG   A NH2   
582  N  N     . THR   A 77  ? 0.1187 0.2171 0.2870 -0.0171 0.0198  0.0396  74  THR   A N     
583  C  CA    . THR   A 77  ? 0.1054 0.2245 0.2818 -0.0212 0.0220  0.0408  74  THR   A CA    
584  C  C     . THR   A 77  ? 0.0886 0.2234 0.2758 -0.0233 0.0207  0.0344  74  THR   A C     
585  O  O     . THR   A 77  ? 0.0833 0.2317 0.2780 -0.0296 0.0219  0.0342  74  THR   A O     
586  C  CB    . THR   A 77  ? 0.0990 0.2273 0.2739 -0.0134 0.0232  0.0436  74  THR   A CB    
587  O  OG1   . THR   A 77  ? 0.1175 0.2314 0.2815 -0.0121 0.0239  0.0505  74  THR   A OG1   
588  C  CG2   . THR   A 77  ? 0.0864 0.2356 0.2683 -0.0159 0.0254  0.0434  74  THR   A CG2   
589  N  N     . GLY   A 78  ? 0.0815 0.2152 0.2694 -0.0175 0.0183  0.0294  75  GLY   A N     
590  C  CA    . GLY   A 78  ? 0.0674 0.2142 0.2631 -0.0176 0.0166  0.0243  75  GLY   A CA    
591  C  C     . GLY   A 78  ? 0.0711 0.2185 0.2709 -0.0259 0.0145  0.0219  75  GLY   A C     
592  O  O     . GLY   A 78  ? 0.0854 0.2183 0.2800 -0.0306 0.0132  0.0218  75  GLY   A O     
593  N  N     . GLU   A 79  ? 0.0608 0.2256 0.2702 -0.0277 0.0137  0.0196  76  GLU   A N     
594  C  CA    . GLU   A 79  ? 0.0634 0.2341 0.2794 -0.0354 0.0111  0.0171  76  GLU   A CA    
595  C  C     . GLU   A 79  ? 0.0600 0.2285 0.2752 -0.0328 0.0062  0.0119  76  GLU   A C     
596  O  O     . GLU   A 79  ? 0.0680 0.2327 0.2833 -0.0385 0.0025  0.0093  76  GLU   A O     
597  C  CB    . GLU   A 79  ? 0.0578 0.2503 0.2850 -0.0377 0.0130  0.0176  76  GLU   A CB    
598  C  CG    . GLU   A 79  ? 0.0649 0.2599 0.2908 -0.0407 0.0185  0.0232  76  GLU   A CG    
599  C  CD    . GLU   A 79  ? 0.0607 0.2786 0.2966 -0.0414 0.0215  0.0230  76  GLU   A CD    
600  O  OE1   . GLU   A 79  ? 0.0503 0.2796 0.2914 -0.0346 0.0200  0.0189  76  GLU   A OE1   
601  O  OE2   . GLU   A 79  ? 0.0712 0.2953 0.3095 -0.0491 0.0255  0.0267  76  GLU   A OE2   
602  N  N     . GLY   A 80  ? 0.0513 0.2210 0.2642 -0.0246 0.0060  0.0105  77  GLY   A N     
603  C  CA    . GLY   A 80  ? 0.0506 0.2170 0.2601 -0.0214 0.0020  0.0066  77  GLY   A CA    
604  C  C     . GLY   A 80  ? 0.0489 0.2075 0.2507 -0.0145 0.0039  0.0067  77  GLY   A C     
605  O  O     . GLY   A 80  ? 0.0430 0.2054 0.2461 -0.0113 0.0068  0.0089  77  GLY   A O     
606  N  N     . PHE   A 81  ? 0.0550 0.2047 0.2493 -0.0131 0.0018  0.0040  78  PHE   A N     
607  C  CA    . PHE   A 81  ? 0.0549 0.1991 0.2424 -0.0072 0.0045  0.0041  78  PHE   A CA    
608  C  C     . PHE   A 81  ? 0.0548 0.1997 0.2381 -0.0053 0.0023  0.0021  78  PHE   A C     
609  O  O     . PHE   A 81  ? 0.0624 0.2026 0.2410 -0.0072 -0.0013 -0.0004 78  PHE   A O     
610  C  CB    . PHE   A 81  ? 0.0678 0.1976 0.2467 -0.0064 0.0059  0.0031  78  PHE   A CB    
611  C  CG    . PHE   A 81  ? 0.0723 0.1973 0.2524 -0.0076 0.0079  0.0060  78  PHE   A CG    
612  C  CD1   . PHE   A 81  ? 0.0798 0.2006 0.2614 -0.0146 0.0060  0.0065  78  PHE   A CD1   
613  C  CD2   . PHE   A 81  ? 0.0712 0.1956 0.2505 -0.0021 0.0114  0.0086  78  PHE   A CD2   
614  C  CE1   . PHE   A 81  ? 0.0864 0.2014 0.2675 -0.0165 0.0082  0.0104  78  PHE   A CE1   
615  C  CE2   . PHE   A 81  ? 0.0776 0.1964 0.2563 -0.0026 0.0127  0.0122  78  PHE   A CE2   
616  C  CZ    . PHE   A 81  ? 0.0863 0.1988 0.2647 -0.0100 0.0113  0.0134  78  PHE   A CZ    
617  N  N     . LEU   A 82  ? 0.0502 0.2000 0.2343 -0.0020 0.0043  0.0035  79  LEU   A N     
618  C  CA    . LEU   A 82  ? 0.0572 0.2046 0.2346 -0.0005 0.0033  0.0028  79  LEU   A CA    
619  C  C     . LEU   A 82  ? 0.0646 0.2060 0.2345 0.0017  0.0076  0.0023  79  LEU   A C     
620  O  O     . LEU   A 82  ? 0.0588 0.2043 0.2326 0.0038  0.0114  0.0039  79  LEU   A O     
621  C  CB    . LEU   A 82  ? 0.0532 0.2068 0.2344 0.0008  0.0040  0.0046  79  LEU   A CB    
622  C  CG    . LEU   A 82  ? 0.0538 0.2123 0.2400 0.0009  -0.0003 0.0044  79  LEU   A CG    
623  C  CD1   . LEU   A 82  ? 0.0533 0.2119 0.2386 0.0022  0.0002  0.0056  79  LEU   A CD1   
624  C  CD2   . LEU   A 82  ? 0.0626 0.2176 0.2443 0.0004  -0.0056 0.0027  79  LEU   A CD2   
625  N  N     . CYS   A 83  ? 0.0776 0.2108 0.2375 0.0017  0.0067  -0.0001 80  CYS   A N     
626  C  CA    . CYS   A 83  ? 0.0879 0.2161 0.2393 0.0049  0.0113  -0.0015 80  CYS   A CA    
627  C  C     . CYS   A 83  ? 0.0878 0.2184 0.2334 0.0048  0.0130  -0.0001 80  CYS   A C     
628  O  O     . CYS   A 83  ? 0.0932 0.2187 0.2303 0.0034  0.0096  -0.0009 80  CYS   A O     
629  C  CB    . CYS   A 83  ? 0.1055 0.2220 0.2472 0.0048  0.0094  -0.0056 80  CYS   A CB    
630  S  SG    . CYS   A 83  ? 0.1171 0.2272 0.2638 0.0036  0.0082  -0.0063 80  CYS   A SG    
631  N  N     . VAL   A 84  ? 0.0791 0.2176 0.2293 0.0059  0.0177  0.0021  81  VAL   A N     
632  C  CA    . VAL   A 84  ? 0.0800 0.2210 0.2262 0.0037  0.0195  0.0045  81  VAL   A CA    
633  C  C     . VAL   A 84  ? 0.0886 0.2318 0.2278 0.0051  0.0262  0.0040  81  VAL   A C     
634  O  O     . VAL   A 84  ? 0.0837 0.2324 0.2274 0.0087  0.0303  0.0026  81  VAL   A O     
635  C  CB    . VAL   A 84  ? 0.0687 0.2182 0.2256 0.0018  0.0199  0.0073  81  VAL   A CB    
636  C  CG1   . VAL   A 84  ? 0.0732 0.2224 0.2255 -0.0020 0.0210  0.0101  81  VAL   A CG1   
637  C  CG2   . VAL   A 84  ? 0.0596 0.2098 0.2244 0.0016  0.0149  0.0073  81  VAL   A CG2   
638  N  N     . PHE   A 85  ? 0.0984 0.2368 0.2257 0.0029  0.0266  0.0050  82  PHE   A N     
639  C  CA    . PHE   A 85  ? 0.1087 0.2517 0.2290 0.0028  0.0341  0.0055  82  PHE   A CA    
640  C  C     . PHE   A 85  ? 0.1131 0.2560 0.2296 -0.0033 0.0346  0.0105  82  PHE   A C     
641  O  O     . PHE   A 85  ? 0.1097 0.2468 0.2274 -0.0057 0.0287  0.0127  82  PHE   A O     
642  C  CB    . PHE   A 85  ? 0.1240 0.2593 0.2294 0.0060  0.0356  0.0017  82  PHE   A CB    
643  C  CG    . PHE   A 85  ? 0.1348 0.2585 0.2257 0.0034  0.0302  0.0026  82  PHE   A CG    
644  C  CD1   . PHE   A 85  ? 0.1339 0.2497 0.2249 0.0035  0.0216  0.0009  82  PHE   A CD1   
645  C  CD2   . PHE   A 85  ? 0.1483 0.2701 0.2257 0.0005  0.0335  0.0056  82  PHE   A CD2   
646  C  CE1   . PHE   A 85  ? 0.1453 0.2523 0.2237 0.0019  0.0157  0.0017  82  PHE   A CE1   
647  C  CE2   . PHE   A 85  ? 0.1628 0.2732 0.2252 -0.0011 0.0278  0.0070  82  PHE   A CE2   
648  C  CZ    . PHE   A 85  ? 0.1593 0.2628 0.2228 0.0001  0.0183  0.0048  82  PHE   A CZ    
649  N  N     . ALA   A 86  ? 0.1210 0.2709 0.2338 -0.0057 0.0420  0.0122  83  ALA   A N     
650  C  CA    . ALA   A 86  ? 0.1312 0.2790 0.2381 -0.0130 0.0435  0.0176  83  ALA   A CA    
651  C  C     . ALA   A 86  ? 0.1536 0.2930 0.2402 -0.0138 0.0458  0.0187  83  ALA   A C     
652  O  O     . ALA   A 86  ? 0.1605 0.3048 0.2415 -0.0102 0.0517  0.0155  83  ALA   A O     
653  C  CB    . ALA   A 86  ? 0.1266 0.2904 0.2451 -0.0172 0.0502  0.0195  83  ALA   A CB    
654  N  N     . ILE   A 87  ? 0.1661 0.2921 0.2403 -0.0178 0.0412  0.0232  84  ILE   A N     
655  C  CA    . ILE   A 87  ? 0.1899 0.3052 0.2419 -0.0181 0.0414  0.0249  84  ILE   A CA    
656  C  C     . ILE   A 87  ? 0.2022 0.3251 0.2456 -0.0228 0.0525  0.0278  84  ILE   A C     
657  O  O     . ILE   A 87  ? 0.2198 0.3365 0.2435 -0.0228 0.0550  0.0287  84  ILE   A O     
658  C  CB    . ILE   A 87  ? 0.2035 0.3019 0.2445 -0.0201 0.0327  0.0297  84  ILE   A CB    
659  C  CG1   . ILE   A 87  ? 0.2111 0.3059 0.2530 -0.0278 0.0343  0.0364  84  ILE   A CG1   
660  C  CG2   . ILE   A 87  ? 0.1906 0.2852 0.2409 -0.0149 0.0225  0.0261  84  ILE   A CG2   
661  C  CD1   . ILE   A 87  ? 0.2316 0.3066 0.2570 -0.0289 0.0267  0.0419  84  ILE   A CD1   
662  N  N     . ASN   A 88  ? 0.1928 0.3303 0.2507 -0.0274 0.0591  0.0294  85  ASN   A N     
663  C  CA    . ASN   A 88  ? 0.2049 0.3552 0.2590 -0.0325 0.0707  0.0318  85  ASN   A CA    
664  C  C     . ASN   A 88  ? 0.1955 0.3667 0.2630 -0.0264 0.0783  0.0257  85  ASN   A C     
665  O  O     . ASN   A 88  ? 0.1999 0.3886 0.2717 -0.0301 0.0883  0.0269  85  ASN   A O     
666  C  CB    . ASN   A 88  ? 0.2072 0.3602 0.2671 -0.0437 0.0731  0.0385  85  ASN   A CB    
667  C  CG    . ASN   A 88  ? 0.1853 0.3518 0.2696 -0.0444 0.0717  0.0363  85  ASN   A CG    
668  O  OD1   . ASN   A 88  ? 0.1665 0.3355 0.2621 -0.0364 0.0668  0.0310  85  ASN   A OD1   
669  N  ND2   . ASN   A 88  ? 0.1873 0.3620 0.2788 -0.0547 0.0758  0.0405  85  ASN   A ND2   
670  N  N     . ASN   A 89  ? 0.1854 0.3555 0.2595 -0.0169 0.0737  0.0192  86  ASN   A N     
671  C  CA    . ASN   A 89  ? 0.1807 0.3675 0.2669 -0.0094 0.0796  0.0134  86  ASN   A CA    
672  C  C     . ASN   A 89  ? 0.1873 0.3635 0.2644 0.0004  0.0766  0.0066  86  ASN   A C     
673  O  O     . ASN   A 89  ? 0.1770 0.3454 0.2608 0.0046  0.0689  0.0038  86  ASN   A O     
674  C  CB    . ASN   A 89  ? 0.1593 0.3584 0.2690 -0.0092 0.0774  0.0132  86  ASN   A CB    
675  C  CG    . ASN   A 89  ? 0.1544 0.3727 0.2766 -0.0013 0.0838  0.0085  86  ASN   A CG    
676  O  OD1   . ASN   A 89  ? 0.1507 0.3642 0.2731 0.0083  0.0815  0.0032  86  ASN   A OD1   
677  N  ND2   . ASN   A 89  ? 0.1552 0.3954 0.2872 -0.0053 0.0921  0.0102  86  ASN   A ND2   
678  N  N     . THR   A 90  ? 0.2064 0.3829 0.2679 0.0037  0.0831  0.0038  87  THR   A N     
679  C  CA    . THR   A 90  ? 0.2198 0.3847 0.2687 0.0124  0.0810  -0.0035 87  THR   A CA    
680  C  C     . THR   A 90  ? 0.2090 0.3767 0.2722 0.0214  0.0794  -0.0095 87  THR   A C     
681  O  O     . THR   A 90  ? 0.2117 0.3638 0.2703 0.0254  0.0721  -0.0138 87  THR   A O     
682  C  CB    . THR   A 90  ? 0.2464 0.4156 0.2776 0.0150  0.0907  -0.0062 87  THR   A CB    
683  O  OG1   . THR   A 90  ? 0.2621 0.4238 0.2769 0.0063  0.0904  0.0003  87  THR   A OG1   
684  C  CG2   . THR   A 90  ? 0.2619 0.4182 0.2790 0.0245  0.0888  -0.0151 87  THR   A CG2   
685  N  N     . LYS   A 91  ? 0.1999 0.3873 0.2800 0.0245  0.0858  -0.0097 88  LYS   A N     
686  C  CA    . LYS   A 91  ? 0.1936 0.3831 0.2858 0.0344  0.0845  -0.0147 88  LYS   A CA    
687  C  C     . LYS   A 91  ? 0.1735 0.3509 0.2742 0.0325  0.0739  -0.0131 88  LYS   A C     
688  O  O     . LYS   A 91  ? 0.1755 0.3411 0.2751 0.0390  0.0697  -0.0175 88  LYS   A O     
689  C  CB    . LYS   A 91  ? 0.1907 0.4064 0.3009 0.0378  0.0923  -0.0143 88  LYS   A CB    
690  C  CG    . LYS   A 91  ? 0.1899 0.4083 0.3124 0.0491  0.0905  -0.0185 88  LYS   A CG    
691  C  CD    . LYS   A 91  ? 0.2137 0.4201 0.3231 0.0612  0.0925  -0.0265 88  LYS   A CD    
692  C  CE    . LYS   A 91  ? 0.2158 0.4283 0.3370 0.0741  0.0930  -0.0303 88  LYS   A CE    
693  N  NZ    . LYS   A 91  ? 0.2021 0.4092 0.3360 0.0720  0.0844  -0.0264 88  LYS   A NZ    
694  N  N     . SER   A 92  ? 0.1569 0.3367 0.2652 0.0236  0.0700  -0.0070 89  SER   A N     
695  C  CA    . SER   A 92  ? 0.1404 0.3113 0.2567 0.0213  0.0609  -0.0053 89  SER   A CA    
696  C  C     . SER   A 92  ? 0.1470 0.2975 0.2500 0.0210  0.0536  -0.0076 89  SER   A C     
697  O  O     . SER   A 92  ? 0.1380 0.2808 0.2461 0.0223  0.0476  -0.0088 89  SER   A O     
698  C  CB    . SER   A 92  ? 0.1283 0.3050 0.2532 0.0127  0.0586  0.0008  89  SER   A CB    
699  O  OG    . SER   A 92  ? 0.1343 0.3003 0.2459 0.0063  0.0561  0.0038  89  SER   A OG    
700  N  N     . PHE   A 93  ? 0.1615 0.3047 0.2475 0.0184  0.0542  -0.0078 90  PHE   A N     
701  C  CA    . PHE   A 93  ? 0.1723 0.2980 0.2447 0.0185  0.0470  -0.0110 90  PHE   A CA    
702  C  C     . PHE   A 93  ? 0.1851 0.3027 0.2523 0.0261  0.0476  -0.0185 90  PHE   A C     
703  O  O     . PHE   A 93  ? 0.1860 0.2918 0.2528 0.0263  0.0408  -0.0213 90  PHE   A O     
704  C  CB    . PHE   A 93  ? 0.1879 0.3079 0.2413 0.0149  0.0473  -0.0095 90  PHE   A CB    
705  C  CG    . PHE   A 93  ? 0.1992 0.3032 0.2387 0.0148  0.0388  -0.0131 90  PHE   A CG    
706  C  CD1   . PHE   A 93  ? 0.1903 0.2888 0.2354 0.0110  0.0290  -0.0110 90  PHE   A CD1   
707  C  CD2   . PHE   A 93  ? 0.2192 0.3146 0.2408 0.0187  0.0402  -0.0193 90  PHE   A CD2   
708  C  CE1   . PHE   A 93  ? 0.2005 0.2873 0.2352 0.0105  0.0206  -0.0147 90  PHE   A CE1   
709  C  CE2   . PHE   A 93  ? 0.2315 0.3128 0.2408 0.0179  0.0313  -0.0232 90  PHE   A CE2   
710  C  CZ    . PHE   A 93  ? 0.2213 0.2994 0.2381 0.0134  0.0213  -0.0207 90  PHE   A CZ    
711  N  N     . GLU   A 94  ? 0.1985 0.3229 0.2621 0.0325  0.0562  -0.0218 91  GLU   A N     
712  C  CA    . GLU   A 94  ? 0.2165 0.3307 0.2729 0.0410  0.0570  -0.0295 91  GLU   A CA    
713  C  C     . GLU   A 94  ? 0.2065 0.3175 0.2772 0.0448  0.0535  -0.0301 91  GLU   A C     
714  O  O     . GLU   A 94  ? 0.2214 0.3161 0.2851 0.0493  0.0503  -0.0355 91  GLU   A O     
715  C  CB    . GLU   A 94  ? 0.2338 0.3590 0.2852 0.0486  0.0678  -0.0330 91  GLU   A CB    
716  C  CG    . GLU   A 94  ? 0.2556 0.3801 0.2875 0.0460  0.0718  -0.0337 91  GLU   A CG    
717  C  CD    . GLU   A 94  ? 0.2679 0.4098 0.2985 0.0520  0.0843  -0.0357 91  GLU   A CD    
718  O  OE1   . GLU   A 94  ? 0.2667 0.4214 0.3129 0.0588  0.0886  -0.0368 91  GLU   A OE1   
719  O  OE2   . GLU   A 94  ? 0.2875 0.4312 0.3016 0.0501  0.0896  -0.0359 91  GLU   A OE2   
720  N  N     . ASP   A 95  ? 0.1848 0.3100 0.2735 0.0429  0.0542  -0.0245 92  ASP   A N     
721  C  CA    . ASP   A 95  ? 0.1757 0.2993 0.2773 0.0462  0.0511  -0.0236 92  ASP   A CA    
722  C  C     . ASP   A 95  ? 0.1710 0.2804 0.2729 0.0399  0.0420  -0.0224 92  ASP   A C     
723  O  O     . ASP   A 95  ? 0.1682 0.2696 0.2747 0.0423  0.0390  -0.0227 92  ASP   A O     
724  C  CB    . ASP   A 95  ? 0.1560 0.2995 0.2756 0.0450  0.0534  -0.0181 92  ASP   A CB    
725  C  CG    . ASP   A 95  ? 0.1598 0.3218 0.2851 0.0519  0.0620  -0.0192 92  ASP   A CG    
726  O  OD1   . ASP   A 95  ? 0.1739 0.3332 0.2898 0.0598  0.0669  -0.0247 92  ASP   A OD1   
727  O  OD2   . ASP   A 95  ? 0.1481 0.3279 0.2873 0.0490  0.0637  -0.0150 92  ASP   A OD2   
728  N  N     . ILE   A 96  ? 0.1709 0.2779 0.2678 0.0320  0.0378  -0.0206 93  ILE   A N     
729  C  CA    . ILE   A 96  ? 0.1658 0.2650 0.2663 0.0256  0.0295  -0.0190 93  ILE   A CA    
730  C  C     . ILE   A 96  ? 0.1814 0.2633 0.2762 0.0270  0.0255  -0.0237 93  ILE   A C     
731  O  O     . ILE   A 96  ? 0.1763 0.2547 0.2795 0.0243  0.0216  -0.0218 93  ILE   A O     
732  C  CB    . ILE   A 96  ? 0.1681 0.2660 0.2612 0.0192  0.0251  -0.0178 93  ILE   A CB    
733  C  CG1   . ILE   A 96  ? 0.1557 0.2669 0.2560 0.0160  0.0271  -0.0119 93  ILE   A CG1   
734  C  CG2   . ILE   A 96  ? 0.1661 0.2562 0.2614 0.0140  0.0163  -0.0185 93  ILE   A CG2   
735  C  CD1   . ILE   A 96  ? 0.1383 0.2565 0.2548 0.0133  0.0243  -0.0078 93  ILE   A CD1   
736  N  N     . HIS   A 97  ? 0.2057 0.2757 0.2849 0.0305  0.0263  -0.0300 94  HIS   A N     
737  C  CA    . HIS   A 97  ? 0.2272 0.2774 0.2984 0.0311  0.0221  -0.0353 94  HIS   A CA    
738  C  C     . HIS   A 97  ? 0.2268 0.2722 0.3062 0.0361  0.0237  -0.0341 94  HIS   A C     
739  O  O     . HIS   A 97  ? 0.2322 0.2626 0.3105 0.0330  0.0190  -0.0350 94  HIS   A O     
740  C  CB    . HIS   A 97  ? 0.2588 0.2971 0.3103 0.0357  0.0238  -0.0430 94  HIS   A CB    
741  C  CG    . HIS   A 97  ? 0.2867 0.3019 0.3283 0.0371  0.0199  -0.0495 94  HIS   A CG    
742  N  ND1   . HIS   A 97  ? 0.3072 0.3117 0.3422 0.0475  0.0245  -0.0543 94  HIS   A ND1   
743  C  CD2   . HIS   A 97  ? 0.3004 0.3006 0.3379 0.0291  0.0116  -0.0520 94  HIS   A CD2   
744  C  CE1   . HIS   A 97  ? 0.3302 0.3109 0.3559 0.0458  0.0190  -0.0594 94  HIS   A CE1   
745  N  NE2   . HIS   A 97  ? 0.3253 0.3036 0.3528 0.0337  0.0111  -0.0580 94  HIS   A NE2   
746  N  N     . HIS   A 98  ? 0.2221 0.2800 0.3085 0.0440  0.0303  -0.0321 95  HIS   A N     
747  C  CA    . HIS   A 98  ? 0.2278 0.2822 0.3210 0.0507  0.0315  -0.0305 95  HIS   A CA    
748  C  C     . HIS   A 98  ? 0.2061 0.2652 0.3127 0.0441  0.0276  -0.0236 95  HIS   A C     
749  O  O     . HIS   A 98  ? 0.2147 0.2608 0.3213 0.0450  0.0251  -0.0225 95  HIS   A O     
750  C  CB    . HIS   A 98  ? 0.2308 0.3009 0.3291 0.0613  0.0390  -0.0307 95  HIS   A CB    
751  C  CG    . HIS   A 98  ? 0.2609 0.3250 0.3455 0.0697  0.0437  -0.0381 95  HIS   A CG    
752  N  ND1   . HIS   A 98  ? 0.2906 0.3321 0.3630 0.0773  0.0424  -0.0442 95  HIS   A ND1   
753  C  CD2   . HIS   A 98  ? 0.2679 0.3447 0.3476 0.0719  0.0498  -0.0406 95  HIS   A CD2   
754  C  CE1   . HIS   A 98  ? 0.3090 0.3508 0.3702 0.0850  0.0479  -0.0509 95  HIS   A CE1   
755  N  NE2   . HIS   A 98  ? 0.2961 0.3604 0.3615 0.0815  0.0528  -0.0486 95  HIS   A NE2   
756  N  N     . TYR   A 99  ? 0.1831 0.2592 0.2994 0.0377  0.0272  -0.0191 96  TYR   A N     
757  C  CA    . TYR   A 99  ? 0.1660 0.2478 0.2941 0.0317  0.0239  -0.0134 96  TYR   A CA    
758  C  C     . TYR   A 99  ? 0.1741 0.2419 0.2986 0.0236  0.0179  -0.0142 96  TYR   A C     
759  O  O     . TYR   A 99  ? 0.1678 0.2306 0.2967 0.0210  0.0160  -0.0110 96  TYR   A O     
760  C  CB    . TYR   A 99  ? 0.1467 0.2475 0.2841 0.0274  0.0246  -0.0096 96  TYR   A CB    
761  C  CG    . TYR   A 99  ? 0.1383 0.2552 0.2826 0.0329  0.0300  -0.0080 96  TYR   A CG    
762  C  CD1   . TYR   A 99  ? 0.1321 0.2565 0.2860 0.0367  0.0308  -0.0047 96  TYR   A CD1   
763  C  CD2   . TYR   A 99  ? 0.1416 0.2666 0.2821 0.0340  0.0342  -0.0096 96  TYR   A CD2   
764  C  CE1   . TYR   A 99  ? 0.1258 0.2669 0.2871 0.0415  0.0351  -0.0038 96  TYR   A CE1   
765  C  CE2   . TYR   A 99  ? 0.1366 0.2781 0.2844 0.0382  0.0396  -0.0084 96  TYR   A CE2   
766  C  CZ    . TYR   A 99  ? 0.1261 0.2767 0.2855 0.0416  0.0396  -0.0056 96  TYR   A CZ    
767  O  OH    . TYR   A 99  ? 0.1228 0.2922 0.2911 0.0450  0.0441  -0.0047 96  TYR   A OH    
768  N  N     . ARG   A 100 ? 0.1846 0.2474 0.3010 0.0192  0.0150  -0.0181 97  ARG   A N     
769  C  CA    . ARG   A 100 ? 0.1959 0.2484 0.3102 0.0107  0.0088  -0.0195 97  ARG   A CA    
770  C  C     . ARG   A 100 ? 0.2176 0.2486 0.3243 0.0115  0.0076  -0.0220 97  ARG   A C     
771  O  O     . ARG   A 100 ? 0.2213 0.2458 0.3315 0.0040  0.0041  -0.0200 97  ARG   A O     
772  C  CB    . ARG   A 100 ? 0.2043 0.2559 0.3102 0.0067  0.0048  -0.0238 97  ARG   A CB    
773  C  CG    . ARG   A 100 ? 0.2184 0.2602 0.3224 -0.0022 -0.0023 -0.0264 97  ARG   A CG    
774  C  CD    . ARG   A 100 ? 0.2244 0.2700 0.3230 -0.0064 -0.0077 -0.0296 97  ARG   A CD    
775  N  NE    . ARG   A 100 ? 0.2419 0.2780 0.3382 -0.0149 -0.0150 -0.0334 97  ARG   A NE    
776  C  CZ    . ARG   A 100 ? 0.2353 0.2807 0.3442 -0.0233 -0.0195 -0.0309 97  ARG   A CZ    
777  N  NH1   . ARG   A 100 ? 0.2170 0.2800 0.3405 -0.0230 -0.0174 -0.0250 97  ARG   A NH1   
778  N  NH2   . ARG   A 100 ? 0.2523 0.2903 0.3595 -0.0321 -0.0261 -0.0348 97  ARG   A NH2   
779  N  N     . GLU   A 101 ? 0.2343 0.2537 0.3301 0.0203  0.0107  -0.0264 98  GLU   A N     
780  C  CA    . GLU   A 101 ? 0.2616 0.2559 0.3475 0.0221  0.0091  -0.0293 98  GLU   A CA    
781  C  C     . GLU   A 101 ? 0.2542 0.2467 0.3480 0.0238  0.0103  -0.0227 98  GLU   A C     
782  O  O     . GLU   A 101 ? 0.2630 0.2384 0.3536 0.0183  0.0071  -0.0215 98  GLU   A O     
783  C  CB    . GLU   A 101 ? 0.2892 0.2728 0.3614 0.0332  0.0125  -0.0363 98  GLU   A CB    
784  C  CG    . GLU   A 101 ? 0.3121 0.2875 0.3708 0.0294  0.0094  -0.0437 98  GLU   A CG    
785  C  CD    . GLU   A 101 ? 0.3407 0.2943 0.3921 0.0196  0.0021  -0.0470 98  GLU   A CD    
786  O  OE1   . GLU   A 101 ? 0.3622 0.2971 0.4108 0.0202  0.0012  -0.0464 98  GLU   A OE1   
787  O  OE2   . GLU   A 101 ? 0.3513 0.3072 0.4001 0.0107  -0.0031 -0.0496 98  GLU   A OE2   
788  N  N     . GLN   A 102 ? 0.2345 0.2447 0.3376 0.0309  0.0147  -0.0186 99  GLN   A N     
789  C  CA    . GLN   A 102 ? 0.2321 0.2429 0.3420 0.0337  0.0155  -0.0121 99  GLN   A CA    
790  C  C     . GLN   A 102 ? 0.2141 0.2285 0.3317 0.0217  0.0124  -0.0065 99  GLN   A C     
791  O  O     . GLN   A 102 ? 0.2241 0.2257 0.3396 0.0197  0.0113  -0.0027 99  GLN   A O     
792  C  CB    . GLN   A 102 ? 0.2206 0.2555 0.3410 0.0409  0.0198  -0.0094 99  GLN   A CB    
793  C  CG    . GLN   A 102 ? 0.2240 0.2626 0.3506 0.0459  0.0204  -0.0033 99  GLN   A CG    
794  C  CD    . GLN   A 102 ? 0.2226 0.2805 0.3560 0.0561  0.0246  -0.0038 99  GLN   A CD    
795  O  OE1   . GLN   A 102 ? 0.2363 0.2971 0.3730 0.0641  0.0251  -0.0007 99  GLN   A OE1   
796  N  NE2   . GLN   A 102 ? 0.2132 0.2844 0.3483 0.0553  0.0273  -0.0074 99  GLN   A NE2   
797  N  N     . ILE   A 103 ? 0.1880 0.2201 0.3139 0.0147  0.0116  -0.0061 100 ILE   A N     
798  C  CA    . ILE   A 103 ? 0.1763 0.2150 0.3106 0.0042  0.0092  -0.0015 100 ILE   A CA    
799  C  C     . ILE   A 103 ? 0.1957 0.2143 0.3230 -0.0046 0.0054  -0.0030 100 ILE   A C     
800  O  O     . ILE   A 103 ? 0.2014 0.2132 0.3297 -0.0093 0.0053  0.0018  100 ILE   A O     
801  C  CB    . ILE   A 103 ? 0.1530 0.2124 0.2963 -0.0001 0.0083  -0.0020 100 ILE   A CB    
802  C  CG1   . ILE   A 103 ? 0.1337 0.2106 0.2838 0.0067  0.0119  0.0003  100 ILE   A CG1   
803  C  CG2   . ILE   A 103 ? 0.1457 0.2123 0.2974 -0.0104 0.0058  0.0010  100 ILE   A CG2   
804  C  CD1   . ILE   A 103 ? 0.1218 0.2116 0.2747 0.0056  0.0114  -0.0017 100 ILE   A CD1   
805  N  N     . LYS   A 104 ? 0.2098 0.2178 0.3285 -0.0063 0.0026  -0.0096 101 LYS   A N     
806  C  CA    . LYS   A 104 ? 0.2347 0.2237 0.3467 -0.0163 -0.0019 -0.0122 101 LYS   A CA    
807  C  C     . LYS   A 104 ? 0.2605 0.2236 0.3628 -0.0143 -0.0013 -0.0099 101 LYS   A C     
808  O  O     . LYS   A 104 ? 0.2710 0.2224 0.3726 -0.0250 -0.0036 -0.0072 101 LYS   A O     
809  C  CB    . LYS   A 104 ? 0.2500 0.2304 0.3515 -0.0169 -0.0055 -0.0208 101 LYS   A CB    
810  C  CG    . LYS   A 104 ? 0.2342 0.2360 0.3430 -0.0208 -0.0081 -0.0225 101 LYS   A CG    
811  C  CD    . LYS   A 104 ? 0.2504 0.2457 0.3464 -0.0174 -0.0102 -0.0302 101 LYS   A CD    
812  C  CE    . LYS   A 104 ? 0.2796 0.2535 0.3639 -0.0248 -0.0162 -0.0368 101 LYS   A CE    
813  N  NZ    . LYS   A 104 ? 0.2996 0.2613 0.3665 -0.0174 -0.0164 -0.0448 101 LYS   A NZ    
814  N  N     . ARG   A 105 ? 0.2708 0.2246 0.3654 -0.0007 0.0018  -0.0112 102 ARG   A N     
815  C  CA    . ARG   A 105 ? 0.3014 0.2280 0.3849 0.0044  0.0019  -0.0094 102 ARG   A CA    
816  C  C     . ARG   A 105 ? 0.2916 0.2223 0.3820 0.0013  0.0033  0.0006  102 ARG   A C     
817  O  O     . ARG   A 105 ? 0.3123 0.2194 0.3945 -0.0039 0.0016  0.0041  102 ARG   A O     
818  C  CB    . ARG   A 105 ? 0.3144 0.2375 0.3913 0.0219  0.0052  -0.0131 102 ARG   A CB    
819  C  CG    . ARG   A 105 ? 0.3495 0.2465 0.4154 0.0315  0.0053  -0.0112 102 ARG   A CG    
820  C  CD    . ARG   A 105 ? 0.3628 0.2629 0.4257 0.0506  0.0089  -0.0151 102 ARG   A CD    
821  N  NE    . ARG   A 105 ? 0.3395 0.2734 0.4175 0.0558  0.0129  -0.0120 102 ARG   A NE    
822  C  CZ    . ARG   A 105 ? 0.3338 0.2874 0.4160 0.0607  0.0163  -0.0170 102 ARG   A CZ    
823  N  NH1   . ARG   A 105 ? 0.3102 0.2927 0.4062 0.0637  0.0195  -0.0135 102 ARG   A NH1   
824  N  NH2   . ARG   A 105 ? 0.3521 0.2957 0.4237 0.0619  0.0164  -0.0254 102 ARG   A NH2   
825  N  N     . VAL   A 106 ? 0.2619 0.2204 0.3655 0.0037  0.0062  0.0050  103 VAL   A N     
826  C  CA    . VAL   A 106 ? 0.2561 0.2213 0.3653 0.0019  0.0078  0.0141  103 VAL   A CA    
827  C  C     . VAL   A 106 ? 0.2579 0.2241 0.3713 -0.0144 0.0065  0.0179  103 VAL   A C     
828  O  O     . VAL   A 106 ? 0.2705 0.2237 0.3792 -0.0189 0.0067  0.0242  103 VAL   A O     
829  C  CB    . VAL   A 106 ? 0.2272 0.2215 0.3486 0.0087  0.0107  0.0164  103 VAL   A CB    
830  C  CG1   . VAL   A 106 ? 0.2207 0.2229 0.3466 0.0057  0.0120  0.0249  103 VAL   A CG1   
831  C  CG2   . VAL   A 106 ? 0.2290 0.2234 0.3472 0.0241  0.0124  0.0136  103 VAL   A CG2   
832  N  N     . LYS   A 107 ? 0.2477 0.2298 0.3695 -0.0225 0.0050  0.0138  104 LYS   A N     
833  C  CA    . LYS   A 107 ? 0.2500 0.2386 0.3789 -0.0382 0.0036  0.0158  104 LYS   A CA    
834  C  C     . LYS   A 107 ? 0.2872 0.2485 0.4055 -0.0480 0.0000  0.0135  104 LYS   A C     
835  O  O     . LYS   A 107 ? 0.2910 0.2538 0.4137 -0.0617 -0.0006 0.0168  104 LYS   A O     
836  C  CB    . LYS   A 107 ? 0.2276 0.2409 0.3682 -0.0417 0.0019  0.0111  104 LYS   A CB    
837  C  CG    . LYS   A 107 ? 0.1982 0.2379 0.3495 -0.0346 0.0047  0.0126  104 LYS   A CG    
838  C  CD    . LYS   A 107 ? 0.1871 0.2446 0.3493 -0.0411 0.0068  0.0182  104 LYS   A CD    
839  C  CE    . LYS   A 107 ? 0.1572 0.2405 0.3303 -0.0364 0.0083  0.0181  104 LYS   A CE    
840  N  NZ    . LYS   A 107 ? 0.1510 0.2435 0.3279 -0.0367 0.0122  0.0245  104 LYS   A NZ    
841  N  N     . ASP   A 108 ? 0.3137 0.2523 0.4189 -0.0415 -0.0023 0.0074  105 ASP   A N     
842  C  CA    . ASP   A 108 ? 0.3482 0.2594 0.4421 -0.0512 -0.0068 0.0030  105 ASP   A CA    
843  C  C     . ASP   A 108 ? 0.3445 0.2735 0.4491 -0.0653 -0.0106 -0.0008 105 ASP   A C     
844  O  O     . ASP   A 108 ? 0.3578 0.2820 0.4649 -0.0806 -0.0124 0.0017  105 ASP   A O     
845  C  CB    . ASP   A 108 ? 0.3771 0.2602 0.4606 -0.0561 -0.0065 0.0095  105 ASP   A CB    
846  C  CG    . ASP   A 108 ? 0.4132 0.2649 0.4837 -0.0663 -0.0116 0.0044  105 ASP   A CG    
847  O  OD1   . ASP   A 108 ? 0.4270 0.2665 0.4882 -0.0602 -0.0145 -0.0048 105 ASP   A OD1   
848  O  OD2   . ASP   A 108 ? 0.4305 0.2712 0.5000 -0.0806 -0.0123 0.0096  105 ASP   A OD2   
849  N  N     . SER   A 109 ? 0.3342 0.2835 0.4449 -0.0603 -0.0117 -0.0062 106 SER   A N     
850  C  CA    . SER   A 109 ? 0.3336 0.3031 0.4553 -0.0709 -0.0159 -0.0096 106 SER   A CA    
851  C  C     . SER   A 109 ? 0.3326 0.3104 0.4515 -0.0628 -0.0184 -0.0170 106 SER   A C     
852  O  O     . SER   A 109 ? 0.3254 0.3110 0.4437 -0.0501 -0.0145 -0.0164 106 SER   A O     
853  C  CB    . SER   A 109 ? 0.3102 0.3093 0.4499 -0.0752 -0.0130 -0.0032 106 SER   A CB    
854  O  OG    . SER   A 109 ? 0.3052 0.3250 0.4561 -0.0833 -0.0176 -0.0070 106 SER   A OG    
855  N  N     . GLU   A 110 ? 0.3545 0.3307 0.4710 -0.0710 -0.0250 -0.0237 107 GLU   A N     
856  C  CA    . GLU   A 110 ? 0.3539 0.3362 0.4648 -0.0637 -0.0278 -0.0304 107 GLU   A CA    
857  C  C     . GLU   A 110 ? 0.3231 0.3373 0.4498 -0.0647 -0.0291 -0.0284 107 GLU   A C     
858  O  O     . GLU   A 110 ? 0.3207 0.3425 0.4437 -0.0568 -0.0297 -0.0312 107 GLU   A O     
859  C  CB    . GLU   A 110 ? 0.3943 0.3550 0.4897 -0.0680 -0.0343 -0.0396 107 GLU   A CB    
860  C  CG    . GLU   A 110 ? 0.4203 0.3588 0.4969 -0.0551 -0.0313 -0.0442 107 GLU   A CG    
861  C  CD    . GLU   A 110 ? 0.4670 0.3770 0.5247 -0.0583 -0.0368 -0.0536 107 GLU   A CD    
862  O  OE1   . GLU   A 110 ? 0.4829 0.3972 0.5357 -0.0616 -0.0428 -0.0603 107 GLU   A OE1   
863  O  OE2   . GLU   A 110 ? 0.5043 0.3865 0.5510 -0.0568 -0.0354 -0.0544 107 GLU   A OE2   
864  N  N     . ASP   A 111 ? 0.3093 0.3406 0.4521 -0.0737 -0.0290 -0.0235 108 ASP   A N     
865  C  CA    . ASP   A 111 ? 0.2773 0.3393 0.4359 -0.0728 -0.0299 -0.0217 108 ASP   A CA    
866  C  C     . ASP   A 111 ? 0.2399 0.3146 0.4085 -0.0682 -0.0226 -0.0141 108 ASP   A C     
867  O  O     . ASP   A 111 ? 0.2463 0.3243 0.4225 -0.0756 -0.0200 -0.0095 108 ASP   A O     
868  C  CB    . ASP   A 111 ? 0.2928 0.3712 0.4635 -0.0850 -0.0367 -0.0241 108 ASP   A CB    
869  C  CG    . ASP   A 111 ? 0.3183 0.3954 0.4816 -0.0853 -0.0453 -0.0318 108 ASP   A CG    
870  O  OD1   . ASP   A 111 ? 0.3459 0.4005 0.4915 -0.0819 -0.0466 -0.0365 108 ASP   A OD1   
871  O  OD2   . ASP   A 111 ? 0.3203 0.4197 0.4950 -0.0878 -0.0507 -0.0331 108 ASP   A OD2   
872  N  N     . VAL   A 112 ? 0.1986 0.2810 0.3667 -0.0568 -0.0196 -0.0130 109 VAL   A N     
873  C  CA    . VAL   A 112 ? 0.1692 0.2644 0.3459 -0.0516 -0.0135 -0.0068 109 VAL   A CA    
874  C  C     . VAL   A 112 ? 0.1442 0.2581 0.3272 -0.0459 -0.0151 -0.0078 109 VAL   A C     
875  O  O     . VAL   A 112 ? 0.1448 0.2540 0.3195 -0.0408 -0.0174 -0.0113 109 VAL   A O     
876  C  CB    . VAL   A 112 ? 0.1662 0.2483 0.3334 -0.0418 -0.0082 -0.0047 109 VAL   A CB    
877  C  CG1   . VAL   A 112 ? 0.1454 0.2434 0.3212 -0.0361 -0.0035 0.0004  109 VAL   A CG1   
878  C  CG2   . VAL   A 112 ? 0.1879 0.2465 0.3454 -0.0443 -0.0070 -0.0037 109 VAL   A CG2   
879  N  N     . PRO   A 113 ? 0.1188 0.2556 0.3163 -0.0453 -0.0139 -0.0049 110 PRO   A N     
880  C  CA    . PRO   A 113 ? 0.1015 0.2529 0.3037 -0.0386 -0.0155 -0.0055 110 PRO   A CA    
881  C  C     . PRO   A 113 ? 0.0975 0.2406 0.2901 -0.0293 -0.0124 -0.0049 110 PRO   A C     
882  O  O     . PRO   A 113 ? 0.0901 0.2291 0.2812 -0.0263 -0.0071 -0.0018 110 PRO   A O     
883  C  CB    . PRO   A 113 ? 0.0892 0.2586 0.3048 -0.0389 -0.0120 -0.0020 110 PRO   A CB    
884  C  CG    . PRO   A 113 ? 0.0989 0.2695 0.3200 -0.0496 -0.0113 -0.0008 110 PRO   A CG    
885  C  CD    . PRO   A 113 ? 0.1166 0.2625 0.3241 -0.0517 -0.0105 -0.0007 110 PRO   A CD    
886  N  N     . MET   A 114 ? 0.0985 0.2398 0.2844 -0.0256 -0.0160 -0.0076 111 MET   A N     
887  C  CA    . MET   A 114 ? 0.0988 0.2329 0.2750 -0.0185 -0.0129 -0.0071 111 MET   A CA    
888  C  C     . MET   A 114 ? 0.0924 0.2308 0.2652 -0.0154 -0.0172 -0.0082 111 MET   A C     
889  O  O     . MET   A 114 ? 0.0958 0.2362 0.2680 -0.0180 -0.0236 -0.0109 111 MET   A O     
890  C  CB    . MET   A 114 ? 0.1205 0.2373 0.2834 -0.0180 -0.0117 -0.0098 111 MET   A CB    
891  C  CG    . MET   A 114 ? 0.1300 0.2384 0.2924 -0.0175 -0.0067 -0.0080 111 MET   A CG    
892  S  SD    . MET   A 114 ? 0.1589 0.2461 0.3049 -0.0139 -0.0050 -0.0121 111 MET   A SD    
893  C  CE    . MET   A 114 ? 0.1574 0.2472 0.2940 -0.0087 -0.0051 -0.0145 111 MET   A CE    
894  N  N     . VAL   A 115 ? 0.0809 0.2200 0.2509 -0.0101 -0.0141 -0.0059 112 VAL   A N     
895  C  CA    . VAL   A 115 ? 0.0826 0.2204 0.2449 -0.0069 -0.0172 -0.0058 112 VAL   A CA    
896  C  C     . VAL   A 115 ? 0.0873 0.2162 0.2381 -0.0041 -0.0117 -0.0049 112 VAL   A C     
897  O  O     . VAL   A 115 ? 0.0792 0.2096 0.2337 -0.0027 -0.0058 -0.0030 112 VAL   A O     
898  C  CB    . VAL   A 115 ? 0.0726 0.2201 0.2431 -0.0041 -0.0188 -0.0035 112 VAL   A CB    
899  C  CG1   . VAL   A 115 ? 0.0795 0.2215 0.2396 -0.0007 -0.0216 -0.0022 112 VAL   A CG1   
900  C  CG2   . VAL   A 115 ? 0.0682 0.2280 0.2512 -0.0058 -0.0235 -0.0049 112 VAL   A CG2   
901  N  N     . LEU   A 116 ? 0.0994 0.2206 0.2365 -0.0034 -0.0138 -0.0063 113 LEU   A N     
902  C  CA    . LEU   A 116 ? 0.1073 0.2228 0.2329 -0.0010 -0.0082 -0.0052 113 LEU   A CA    
903  C  C     . LEU   A 116 ? 0.1041 0.2224 0.2293 0.0001  -0.0078 -0.0009 113 LEU   A C     
904  O  O     . LEU   A 116 ? 0.1076 0.2251 0.2299 0.0005  -0.0139 0.0000  113 LEU   A O     
905  C  CB    . LEU   A 116 ? 0.1246 0.2304 0.2337 -0.0009 -0.0103 -0.0087 113 LEU   A CB    
906  C  CG    . LEU   A 116 ? 0.1336 0.2351 0.2296 0.0014  -0.0037 -0.0077 113 LEU   A CG    
907  C  CD1   . LEU   A 116 ? 0.1289 0.2322 0.2295 0.0036  0.0044  -0.0086 113 LEU   A CD1   
908  C  CD2   . LEU   A 116 ? 0.1538 0.2459 0.2310 0.0017  -0.0066 -0.0112 113 LEU   A CD2   
909  N  N     . VAL   A 117 ? 0.0982 0.2190 0.2254 0.0007  -0.0011 0.0016  114 VAL   A N     
910  C  CA    . VAL   A 117 ? 0.0983 0.2196 0.2247 0.0002  -0.0008 0.0056  114 VAL   A CA    
911  C  C     . VAL   A 117 ? 0.1079 0.2262 0.2233 -0.0008 0.0055  0.0076  114 VAL   A C     
912  O  O     . VAL   A 117 ? 0.1037 0.2271 0.2225 -0.0005 0.0121  0.0069  114 VAL   A O     
913  C  CB    . VAL   A 117 ? 0.0847 0.2139 0.2255 0.0002  0.0007  0.0069  114 VAL   A CB    
914  C  CG1   . VAL   A 117 ? 0.0884 0.2154 0.2270 -0.0011 0.0013  0.0105  114 VAL   A CG1   
915  C  CG2   . VAL   A 117 ? 0.0778 0.2120 0.2291 0.0010  -0.0042 0.0052  114 VAL   A CG2   
916  N  N     . GLY   A 118 ? 0.1215 0.2322 0.2240 -0.0018 0.0033  0.0104  115 GLY   A N     
917  C  CA    . GLY   A 118 ? 0.1324 0.2406 0.2239 -0.0044 0.0096  0.0137  115 GLY   A CA    
918  C  C     . GLY   A 118 ? 0.1302 0.2376 0.2254 -0.0077 0.0101  0.0185  115 GLY   A C     
919  O  O     . GLY   A 118 ? 0.1365 0.2345 0.2252 -0.0078 0.0043  0.0213  115 GLY   A O     
920  N  N     . ASN   A 119 ? 0.1192 0.2362 0.2250 -0.0100 0.0164  0.0188  116 ASN   A N     
921  C  CA    . ASN   A 119 ? 0.1170 0.2343 0.2283 -0.0142 0.0170  0.0221  116 ASN   A CA    
922  C  C     . ASN   A 119 ? 0.1336 0.2471 0.2337 -0.0206 0.0225  0.0270  116 ASN   A C     
923  O  O     . ASN   A 119 ? 0.1416 0.2578 0.2333 -0.0209 0.0278  0.0269  116 ASN   A O     
924  C  CB    . ASN   A 119 ? 0.0987 0.2287 0.2275 -0.0136 0.0191  0.0196  116 ASN   A CB    
925  C  CG    . ASN   A 119 ? 0.0955 0.2253 0.2310 -0.0171 0.0177  0.0213  116 ASN   A CG    
926  O  OD1   . ASN   A 119 ? 0.1012 0.2196 0.2314 -0.0173 0.0124  0.0228  116 ASN   A OD1   
927  N  ND2   . ASN   A 119 ? 0.0886 0.2295 0.2330 -0.0205 0.0225  0.0213  116 ASN   A ND2   
928  N  N     . LYS   A 120 ? 0.1395 0.2473 0.2401 -0.0258 0.0214  0.0305  117 LYS   A N     
929  C  CA    . LYS   A 120 ? 0.1571 0.2595 0.2486 -0.0345 0.0260  0.0361  117 LYS   A CA    
930  C  C     . LYS   A 120 ? 0.1814 0.2660 0.2515 -0.0349 0.0230  0.0408  117 LYS   A C     
931  O  O     . LYS   A 120 ? 0.1950 0.2781 0.2539 -0.0406 0.0290  0.0449  117 LYS   A O     
932  C  CB    . LYS   A 120 ? 0.1545 0.2744 0.2519 -0.0389 0.0360  0.0359  117 LYS   A CB    
933  C  CG    . LYS   A 120 ? 0.1334 0.2718 0.2507 -0.0361 0.0381  0.0311  117 LYS   A CG    
934  C  CD    . LYS   A 120 ? 0.1308 0.2880 0.2561 -0.0407 0.0472  0.0314  117 LYS   A CD    
935  C  CE    . LYS   A 120 ? 0.1122 0.2863 0.2567 -0.0370 0.0473  0.0271  117 LYS   A CE    
936  N  NZ    . LYS   A 120 ? 0.1109 0.3062 0.2643 -0.0398 0.0557  0.0269  117 LYS   A NZ    
937  N  N     . SER   A 121 ? 0.1848 0.2586 0.2504 -0.0280 0.0139  0.0396  118 SER   A N     
938  C  CA    . SER   A 121 ? 0.2098 0.2659 0.2548 -0.0265 0.0087  0.0439  118 SER   A CA    
939  C  C     . SER   A 121 ? 0.2339 0.2730 0.2660 -0.0336 0.0090  0.0514  118 SER   A C     
940  O  O     . SER   A 121 ? 0.2545 0.2787 0.2671 -0.0333 0.0062  0.0562  118 SER   A O     
941  C  CB    . SER   A 121 ? 0.2059 0.2569 0.2524 -0.0176 -0.0018 0.0410  118 SER   A CB    
942  O  OG    . SER   A 121 ? 0.2001 0.2470 0.2562 -0.0161 -0.0064 0.0405  118 SER   A OG    
943  N  N     . ASP   A 122 ? 0.2310 0.2702 0.2732 -0.0389 0.0105  0.0518  119 ASP   A N     
944  C  CA    . ASP   A 122 ? 0.2579 0.2800 0.2884 -0.0480 0.0116  0.0588  119 ASP   A CA    
945  C  C     . ASP   A 122 ? 0.2760 0.3024 0.2966 -0.0584 0.0219  0.0641  119 ASP   A C     
946  O  O     . ASP   A 122 ? 0.3019 0.3115 0.3074 -0.0666 0.0230  0.0714  119 ASP   A O     
947  C  CB    . ASP   A 122 ? 0.2485 0.2725 0.2936 -0.0529 0.0115  0.0567  119 ASP   A CB    
948  C  CG    . ASP   A 122 ? 0.2245 0.2751 0.2891 -0.0564 0.0193  0.0522  119 ASP   A CG    
949  O  OD1   . ASP   A 122 ? 0.2024 0.2674 0.2797 -0.0483 0.0181  0.0462  119 ASP   A OD1   
950  O  OD2   . ASP   A 122 ? 0.2289 0.2862 0.2956 -0.0672 0.0264  0.0550  119 ASP   A OD2   
951  N  N     . LEU   A 123 ? 0.2676 0.3163 0.2966 -0.0582 0.0298  0.0606  120 LEU   A N     
952  C  CA    . LEU   A 123 ? 0.2862 0.3448 0.3102 -0.0678 0.0411  0.0644  120 LEU   A CA    
953  C  C     . LEU   A 123 ? 0.3157 0.3632 0.3149 -0.0674 0.0427  0.0694  120 LEU   A C     
954  O  O     . LEU   A 123 ? 0.3161 0.3651 0.3102 -0.0582 0.0398  0.0656  120 LEU   A O     
955  C  CB    . LEU   A 123 ? 0.2660 0.3530 0.3084 -0.0654 0.0486  0.0580  120 LEU   A CB    
956  C  CG    . LEU   A 123 ? 0.2470 0.3492 0.3134 -0.0673 0.0489  0.0539  120 LEU   A CG    
957  C  CD1   . LEU   A 123 ? 0.2298 0.3591 0.3111 -0.0641 0.0567  0.0487  120 LEU   A CD1   
958  C  CD2   . LEU   A 123 ? 0.2608 0.3587 0.3280 -0.0807 0.0512  0.0590  120 LEU   A CD2   
959  N  N     . PRO   A 124 ? 0.3482 0.3853 0.3308 -0.0782 0.0481  0.0779  121 PRO   A N     
960  C  CA    . PRO   A 124 ? 0.3782 0.4028 0.3338 -0.0779 0.0493  0.0834  121 PRO   A CA    
961  C  C     . PRO   A 124 ? 0.3772 0.4220 0.3305 -0.0750 0.0586  0.0795  121 PRO   A C     
962  O  O     . PRO   A 124 ? 0.3991 0.4355 0.3328 -0.0696 0.0565  0.0801  121 PRO   A O     
963  C  CB    . PRO   A 124 ? 0.4058 0.4157 0.3468 -0.0923 0.0541  0.0939  121 PRO   A CB    
964  C  CG    . PRO   A 124 ? 0.3900 0.4194 0.3544 -0.1020 0.0614  0.0918  121 PRO   A CG    
965  C  CD    . PRO   A 124 ? 0.3582 0.3968 0.3465 -0.0923 0.0540  0.0826  121 PRO   A CD    
966  N  N     . SER   A 125 ? 0.3582 0.4290 0.3310 -0.0772 0.0679  0.0747  122 SER   A N     
967  C  CA    . SER   A 125 ? 0.3578 0.4472 0.3273 -0.0738 0.0777  0.0707  122 SER   A CA    
968  C  C     . SER   A 125 ? 0.3348 0.4341 0.3153 -0.0603 0.0739  0.0603  122 SER   A C     
969  O  O     . SER   A 125 ? 0.3208 0.4418 0.3198 -0.0580 0.0801  0.0547  122 SER   A O     
970  C  CB    . SER   A 125 ? 0.3539 0.4681 0.3374 -0.0830 0.0910  0.0715  122 SER   A CB    
971  O  OG    . SER   A 125 ? 0.3780 0.4843 0.3523 -0.0978 0.0956  0.0812  122 SER   A OG    
972  N  N     . ARG   A 126 ? 0.3374 0.4222 0.3051 -0.0519 0.0649  0.0580  123 ARG   A N     
973  C  CA    . ARG   A 126 ? 0.3156 0.4076 0.2933 -0.0407 0.0606  0.0482  123 ARG   A CA    
974  C  C     . ARG   A 126 ? 0.3144 0.4189 0.2851 -0.0366 0.0698  0.0430  123 ARG   A C     
975  O  O     . ARG   A 126 ? 0.3359 0.4363 0.2851 -0.0394 0.0751  0.0465  123 ARG   A O     
976  C  CB    . ARG   A 126 ? 0.3278 0.4012 0.2922 -0.0343 0.0480  0.0473  123 ARG   A CB    
977  C  CG    . ARG   A 126 ? 0.3378 0.3942 0.3005 -0.0364 0.0382  0.0532  123 ARG   A CG    
978  C  CD    . ARG   A 126 ? 0.3477 0.3903 0.2990 -0.0288 0.0257  0.0516  123 ARG   A CD    
979  N  NE    . ARG   A 126 ? 0.3326 0.3857 0.2960 -0.0216 0.0230  0.0422  123 ARG   A NE    
980  C  CZ    . ARG   A 126 ? 0.3188 0.3720 0.2961 -0.0165 0.0136  0.0382  123 ARG   A CZ    
981  N  NH1   . ARG   A 126 ? 0.3056 0.3674 0.2927 -0.0118 0.0122  0.0304  123 ARG   A NH1   
982  N  NH2   . ARG   A 126 ? 0.3179 0.3625 0.2994 -0.0164 0.0063  0.0420  123 ARG   A NH2   
983  N  N     . THR   A 127 ? 0.2894 0.4064 0.2760 -0.0292 0.0707  0.0345  124 THR   A N     
984  C  CA    . THR   A 127 ? 0.2933 0.4195 0.2733 -0.0227 0.0780  0.0277  124 THR   A CA    
985  C  C     . THR   A 127 ? 0.2874 0.4033 0.2634 -0.0136 0.0690  0.0199  124 THR   A C     
986  O  O     . THR   A 127 ? 0.2988 0.4147 0.2619 -0.0083 0.0726  0.0143  124 THR   A O     
987  C  CB    . THR   A 127 ? 0.2811 0.4312 0.2812 -0.0216 0.0885  0.0245  124 THR   A CB    
988  O  OG1   . THR   A 127 ? 0.2564 0.4099 0.2794 -0.0185 0.0821  0.0216  124 THR   A OG1   
989  C  CG2   . THR   A 127 ? 0.2885 0.4509 0.2909 -0.0322 0.0982  0.0318  124 THR   A CG2   
990  N  N     . VAL   A 128 ? 0.2684 0.3767 0.2558 -0.0123 0.0580  0.0194  125 VAL   A N     
991  C  CA    . VAL   A 128 ? 0.2656 0.3647 0.2511 -0.0057 0.0486  0.0125  125 VAL   A CA    
992  C  C     . VAL   A 128 ? 0.2795 0.3625 0.2501 -0.0072 0.0377  0.0162  125 VAL   A C     
993  O  O     . VAL   A 128 ? 0.2701 0.3494 0.2484 -0.0102 0.0321  0.0213  125 VAL   A O     
994  C  CB    . VAL   A 128 ? 0.2387 0.3434 0.2487 -0.0029 0.0443  0.0090  125 VAL   A CB    
995  C  CG1   . VAL   A 128 ? 0.2370 0.3328 0.2453 0.0018  0.0354  0.0025  125 VAL   A CG1   
996  C  CG2   . VAL   A 128 ? 0.2269 0.3475 0.2514 -0.0005 0.0540  0.0062  125 VAL   A CG2   
997  N  N     . ASP   A 129 ? 0.3032 0.3771 0.2524 -0.0045 0.0346  0.0131  126 ASP   A N     
998  C  CA    . ASP   A 129 ? 0.3235 0.3827 0.2555 -0.0044 0.0232  0.0157  126 ASP   A CA    
999  C  C     . ASP   A 129 ? 0.3015 0.3594 0.2506 -0.0021 0.0112  0.0128  126 ASP   A C     
1000 O  O     . ASP   A 129 ? 0.2872 0.3506 0.2495 0.0005  0.0110  0.0059  126 ASP   A O     
1001 C  CB    . ASP   A 129 ? 0.3549 0.4075 0.2631 -0.0009 0.0221  0.0099  126 ASP   A CB    
1002 C  CG    . ASP   A 129 ? 0.3918 0.4318 0.2708 -0.0020 0.0177  0.0148  126 ASP   A CG    
1003 O  OD1   . ASP   A 129 ? 0.4042 0.4371 0.2802 -0.0045 0.0121  0.0228  126 ASP   A OD1   
1004 O  OD2   . ASP   A 129 ? 0.4184 0.4544 0.2763 0.0002  0.0195  0.0105  126 ASP   A OD2   
1005 N  N     . THR   A 130 ? 0.2997 0.3505 0.2480 -0.0028 0.0020  0.0182  127 THR   A N     
1006 C  CA    . THR   A 130 ? 0.2824 0.3344 0.2464 -0.0003 -0.0093 0.0155  127 THR   A CA    
1007 C  C     . THR   A 130 ? 0.2869 0.3380 0.2465 0.0026  -0.0165 0.0074  127 THR   A C     
1008 O  O     . THR   A 130 ? 0.2709 0.3283 0.2480 0.0032  -0.0195 0.0023  127 THR   A O     
1009 C  CB    . THR   A 130 ? 0.2901 0.3338 0.2496 0.0003  -0.0178 0.0224  127 THR   A CB    
1010 O  OG1   . THR   A 130 ? 0.2861 0.3283 0.2497 -0.0034 -0.0113 0.0293  127 THR   A OG1   
1011 C  CG2   . THR   A 130 ? 0.2743 0.3222 0.2507 0.0038  -0.0289 0.0194  127 THR   A CG2   
1012 N  N     . LYS   A 131 ? 0.3108 0.3536 0.2462 0.0035  -0.0193 0.0065  128 LYS   A N     
1013 C  CA    . LYS   A 131 ? 0.3186 0.3594 0.2480 0.0053  -0.0272 -0.0020 128 LYS   A CA    
1014 C  C     . LYS   A 131 ? 0.3085 0.3536 0.2482 0.0054  -0.0209 -0.0102 128 LYS   A C     
1015 O  O     . LYS   A 131 ? 0.3003 0.3461 0.2485 0.0052  -0.0280 -0.0165 128 LYS   A O     
1016 C  CB    . LYS   A 131 ? 0.3510 0.3818 0.2493 0.0063  -0.0290 -0.0024 128 LYS   A CB    
1017 C  CG    . LYS   A 131 ? 0.3634 0.3913 0.2554 0.0075  -0.0408 -0.0107 128 LYS   A CG    
1018 C  CD    . LYS   A 131 ? 0.3977 0.4161 0.2587 0.0087  -0.0428 -0.0138 128 LYS   A CD    
1019 C  CE    . LYS   A 131 ? 0.4059 0.4222 0.2647 0.0086  -0.0487 -0.0256 128 LYS   A CE    
1020 N  NZ    . LYS   A 131 ? 0.3944 0.4166 0.2727 0.0070  -0.0617 -0.0283 128 LYS   A NZ    
1021 N  N     . GLN   A 132 ? 0.3078 0.3556 0.2460 0.0057  -0.0079 -0.0097 129 GLN   A N     
1022 C  CA    . GLN   A 132 ? 0.3036 0.3541 0.2495 0.0076  -0.0015 -0.0170 129 GLN   A CA    
1023 C  C     . GLN   A 132 ? 0.2738 0.3311 0.2472 0.0067  -0.0037 -0.0175 129 GLN   A C     
1024 O  O     . GLN   A 132 ? 0.2698 0.3246 0.2494 0.0072  -0.0067 -0.0242 129 GLN   A O     
1025 C  CB    . GLN   A 132 ? 0.3116 0.3675 0.2532 0.0090  0.0129  -0.0155 129 GLN   A CB    
1026 C  CG    . GLN   A 132 ? 0.3175 0.3740 0.2616 0.0136  0.0193  -0.0240 129 GLN   A CG    
1027 C  CD    . GLN   A 132 ? 0.3231 0.3894 0.2666 0.0162  0.0336  -0.0231 129 GLN   A CD    
1028 O  OE1   . GLN   A 132 ? 0.3312 0.4038 0.2701 0.0131  0.0398  -0.0160 129 GLN   A OE1   
1029 N  NE2   . GLN   A 132 ? 0.3265 0.3941 0.2749 0.0218  0.0389  -0.0301 129 GLN   A NE2   
1030 N  N     . ALA   A 133 ? 0.2535 0.3182 0.2417 0.0049  -0.0022 -0.0105 130 ALA   A N     
1031 C  CA    . ALA   A 133 ? 0.2297 0.3015 0.2423 0.0041  -0.0043 -0.0101 130 ALA   A CA    
1032 C  C     . ALA   A 133 ? 0.2271 0.2975 0.2451 0.0029  -0.0165 -0.0128 130 ALA   A C     
1033 O  O     . ALA   A 133 ? 0.2143 0.2875 0.2464 0.0019  -0.0184 -0.0165 130 ALA   A O     
1034 C  CB    . ALA   A 133 ? 0.2175 0.2958 0.2409 0.0025  -0.0009 -0.0027 130 ALA   A CB    
1035 N  N     . GLN   A 134 ? 0.2383 0.3051 0.2451 0.0029  -0.0248 -0.0107 131 GLN   A N     
1036 C  CA    . GLN   A 134 ? 0.2394 0.3085 0.2526 0.0021  -0.0370 -0.0133 131 GLN   A CA    
1037 C  C     . GLN   A 134 ? 0.2493 0.3140 0.2578 0.0002  -0.0405 -0.0219 131 GLN   A C     
1038 O  O     . GLN   A 134 ? 0.2402 0.3099 0.2635 -0.0026 -0.0459 -0.0253 131 GLN   A O     
1039 C  CB    . GLN   A 134 ? 0.2565 0.3218 0.2557 0.0040  -0.0457 -0.0094 131 GLN   A CB    
1040 C  CG    . GLN   A 134 ? 0.2566 0.3284 0.2649 0.0041  -0.0589 -0.0119 131 GLN   A CG    
1041 C  CD    . GLN   A 134 ? 0.2363 0.3198 0.2701 0.0043  -0.0595 -0.0098 131 GLN   A CD    
1042 O  OE1   . GLN   A 134 ? 0.2266 0.3180 0.2773 0.0013  -0.0594 -0.0140 131 GLN   A OE1   
1043 N  NE2   . GLN   A 134 ? 0.2332 0.3164 0.2688 0.0075  -0.0590 -0.0033 131 GLN   A NE2   
1044 N  N     . ASP   A 135 ? 0.2689 0.3240 0.2562 0.0015  -0.0371 -0.0255 132 ASP   A N     
1045 C  CA    . ASP   A 135 ? 0.2843 0.3314 0.2631 0.0001  -0.0401 -0.0346 132 ASP   A CA    
1046 C  C     . ASP   A 135 ? 0.2706 0.3182 0.2662 -0.0013 -0.0351 -0.0379 132 ASP   A C     
1047 O  O     . ASP   A 135 ? 0.2746 0.3191 0.2754 -0.0052 -0.0415 -0.0434 132 ASP   A O     
1048 C  CB    . ASP   A 135 ? 0.3098 0.3464 0.2616 0.0031  -0.0352 -0.0379 132 ASP   A CB    
1049 C  CG    . ASP   A 135 ? 0.3329 0.3656 0.2631 0.0038  -0.0426 -0.0362 132 ASP   A CG    
1050 O  OD1   . ASP   A 135 ? 0.3306 0.3681 0.2669 0.0024  -0.0535 -0.0335 132 ASP   A OD1   
1051 O  OD2   . ASP   A 135 ? 0.3548 0.3801 0.2614 0.0062  -0.0375 -0.0375 132 ASP   A OD2   
1052 N  N     . LEU   A 136 ? 0.2580 0.3091 0.2615 0.0015  -0.0242 -0.0343 133 LEU   A N     
1053 C  CA    . LEU   A 136 ? 0.2479 0.2988 0.2659 0.0014  -0.0196 -0.0363 133 LEU   A CA    
1054 C  C     . LEU   A 136 ? 0.2326 0.2908 0.2711 -0.0035 -0.0262 -0.0347 133 LEU   A C     
1055 O  O     . LEU   A 136 ? 0.2339 0.2870 0.2778 -0.0070 -0.0290 -0.0389 133 LEU   A O     
1056 C  CB    . LEU   A 136 ? 0.2363 0.2939 0.2613 0.0054  -0.0082 -0.0318 133 LEU   A CB    
1057 C  CG    . LEU   A 136 ? 0.2294 0.2849 0.2651 0.0075  -0.0030 -0.0340 133 LEU   A CG    
1058 C  CD1   . LEU   A 136 ? 0.2526 0.2947 0.2721 0.0117  0.0000  -0.0418 133 LEU   A CD1   
1059 C  CD2   . LEU   A 136 ? 0.2114 0.2786 0.2602 0.0102  0.0054  -0.0282 133 LEU   A CD2   
1060 N  N     . ALA   A 137 ? 0.2193 0.2889 0.2687 -0.0039 -0.0280 -0.0284 134 ALA   A N     
1061 C  CA    . ALA   A 137 ? 0.2075 0.2872 0.2764 -0.0076 -0.0336 -0.0267 134 ALA   A CA    
1062 C  C     . ALA   A 137 ? 0.2212 0.2995 0.2894 -0.0127 -0.0439 -0.0322 134 ALA   A C     
1063 O  O     . ALA   A 137 ? 0.2126 0.2947 0.2948 -0.0177 -0.0460 -0.0337 134 ALA   A O     
1064 C  CB    . ALA   A 137 ? 0.1967 0.2862 0.2720 -0.0056 -0.0354 -0.0205 134 ALA   A CB    
1065 N  N     . ARG   A 138 ? 0.2446 0.3179 0.2961 -0.0121 -0.0503 -0.0350 135 ARG   A N     
1066 C  CA    . ARG   A 138 ? 0.2652 0.3378 0.3143 -0.0173 -0.0611 -0.0409 135 ARG   A CA    
1067 C  C     . ARG   A 138 ? 0.2709 0.3317 0.3184 -0.0221 -0.0596 -0.0474 135 ARG   A C     
1068 O  O     . ARG   A 138 ? 0.2688 0.3335 0.3281 -0.0294 -0.0655 -0.0501 135 ARG   A O     
1069 C  CB    . ARG   A 138 ? 0.2974 0.3640 0.3243 -0.0149 -0.0677 -0.0432 135 ARG   A CB    
1070 C  CG    . ARG   A 138 ? 0.3061 0.3835 0.3351 -0.0120 -0.0752 -0.0382 135 ARG   A CG    
1071 C  CD    . ARG   A 138 ? 0.3424 0.4135 0.3490 -0.0108 -0.0844 -0.0413 135 ARG   A CD    
1072 N  NE    . ARG   A 138 ? 0.3603 0.4312 0.3562 -0.0047 -0.0846 -0.0342 135 ARG   A NE    
1073 C  CZ    . ARG   A 138 ? 0.3646 0.4455 0.3690 -0.0017 -0.0924 -0.0296 135 ARG   A CZ    
1074 N  NH1   . ARG   A 138 ? 0.3666 0.4617 0.3898 -0.0043 -0.1016 -0.0325 135 ARG   A NH1   
1075 N  NH2   . ARG   A 138 ? 0.3729 0.4494 0.3661 0.0039  -0.0913 -0.0223 135 ARG   A NH2   
1076 N  N     . SER   A 139 ? 0.2782 0.3249 0.3111 -0.0181 -0.0517 -0.0498 136 SER   A N     
1077 C  CA    . SER   A 139 ? 0.2892 0.3199 0.3166 -0.0205 -0.0499 -0.0564 136 SER   A CA    
1078 C  C     . SER   A 139 ? 0.2713 0.3051 0.3190 -0.0245 -0.0467 -0.0534 136 SER   A C     
1079 O  O     . SER   A 139 ? 0.2817 0.3057 0.3308 -0.0311 -0.0503 -0.0578 136 SER   A O     
1080 C  CB    . SER   A 139 ? 0.3028 0.3204 0.3119 -0.0129 -0.0411 -0.0592 136 SER   A CB    
1081 O  OG    . SER   A 139 ? 0.2860 0.3100 0.3046 -0.0073 -0.0305 -0.0532 136 SER   A OG    
1082 N  N     . TYR   A 140 ? 0.2424 0.2888 0.3045 -0.0212 -0.0405 -0.0460 137 TYR   A N     
1083 C  CA    . TYR   A 140 ? 0.2268 0.2780 0.3073 -0.0245 -0.0374 -0.0422 137 TYR   A CA    
1084 C  C     . TYR   A 140 ? 0.2154 0.2818 0.3131 -0.0322 -0.0445 -0.0405 137 TYR   A C     
1085 O  O     . TYR   A 140 ? 0.2102 0.2800 0.3216 -0.0371 -0.0428 -0.0381 137 TYR   A O     
1086 C  CB    . TYR   A 140 ? 0.2069 0.2668 0.2956 -0.0180 -0.0285 -0.0355 137 TYR   A CB    
1087 C  CG    . TYR   A 140 ? 0.2134 0.2645 0.2910 -0.0102 -0.0200 -0.0362 137 TYR   A CG    
1088 C  CD1   . TYR   A 140 ? 0.2341 0.2676 0.2968 -0.0080 -0.0188 -0.0425 137 TYR   A CD1   
1089 C  CD2   . TYR   A 140 ? 0.1975 0.2588 0.2802 -0.0048 -0.0132 -0.0308 137 TYR   A CD2   
1090 C  CE1   . TYR   A 140 ? 0.2396 0.2684 0.2936 0.0004  -0.0106 -0.0435 137 TYR   A CE1   
1091 C  CE2   . TYR   A 140 ? 0.2031 0.2607 0.2782 0.0021  -0.0052 -0.0314 137 TYR   A CE2   
1092 C  CZ    . TYR   A 140 ? 0.2236 0.2661 0.2848 0.0053  -0.0037 -0.0377 137 TYR   A CZ    
1093 O  OH    . TYR   A 140 ? 0.2291 0.2706 0.2844 0.0133  0.0046  -0.0387 137 TYR   A OH    
1094 N  N     . GLY   A 141 ? 0.2119 0.2887 0.3092 -0.0327 -0.0520 -0.0410 138 GLY   A N     
1095 C  CA    . GLY   A 141 ? 0.2001 0.2948 0.3149 -0.0384 -0.0589 -0.0399 138 GLY   A CA    
1096 C  C     . GLY   A 141 ? 0.1751 0.2862 0.3067 -0.0347 -0.0543 -0.0331 138 GLY   A C     
1097 O  O     . GLY   A 141 ? 0.1667 0.2926 0.3160 -0.0395 -0.0562 -0.0318 138 GLY   A O     
1098 N  N     . ILE   A 142 ? 0.1639 0.2730 0.2896 -0.0266 -0.0484 -0.0293 139 ILE   A N     
1099 C  CA    . ILE   A 142 ? 0.1423 0.2641 0.2817 -0.0228 -0.0440 -0.0234 139 ILE   A CA    
1100 C  C     . ILE   A 142 ? 0.1377 0.2632 0.2715 -0.0161 -0.0461 -0.0206 139 ILE   A C     
1101 O  O     . ILE   A 142 ? 0.1503 0.2665 0.2677 -0.0137 -0.0478 -0.0217 139 ILE   A O     
1102 C  CB    . ILE   A 142 ? 0.1362 0.2515 0.2760 -0.0206 -0.0339 -0.0207 139 ILE   A CB    
1103 C  CG1   . ILE   A 142 ? 0.1449 0.2490 0.2684 -0.0149 -0.0294 -0.0206 139 ILE   A CG1   
1104 C  CG2   . ILE   A 142 ? 0.1428 0.2504 0.2852 -0.0263 -0.0320 -0.0226 139 ILE   A CG2   
1105 C  CD1   . ILE   A 142 ? 0.1398 0.2397 0.2642 -0.0117 -0.0200 -0.0184 139 ILE   A CD1   
1106 N  N     . PRO   A 143 ? 0.1210 0.2581 0.2669 -0.0129 -0.0451 -0.0166 140 PRO   A N     
1107 C  CA    . PRO   A 143 ? 0.1226 0.2595 0.2625 -0.0067 -0.0468 -0.0134 140 PRO   A CA    
1108 C  C     . PRO   A 143 ? 0.1245 0.2499 0.2524 -0.0040 -0.0387 -0.0104 140 PRO   A C     
1109 O  O     . PRO   A 143 ? 0.1186 0.2417 0.2490 -0.0053 -0.0317 -0.0103 140 PRO   A O     
1110 C  CB    . PRO   A 143 ? 0.1081 0.2592 0.2650 -0.0040 -0.0473 -0.0110 140 PRO   A CB    
1111 C  CG    . PRO   A 143 ? 0.1001 0.2620 0.2725 -0.0097 -0.0464 -0.0132 140 PRO   A CG    
1112 C  CD    . PRO   A 143 ? 0.1071 0.2568 0.2714 -0.0150 -0.0427 -0.0153 140 PRO   A CD    
1113 N  N     . PHE   A 144 ? 0.1345 0.2540 0.2498 -0.0004 -0.0406 -0.0078 141 PHE   A N     
1114 C  CA    . PHE   A 144 ? 0.1393 0.2499 0.2426 0.0013  -0.0336 -0.0042 141 PHE   A CA    
1115 C  C     . PHE   A 144 ? 0.1390 0.2498 0.2432 0.0047  -0.0354 0.0007  141 PHE   A C     
1116 O  O     . PHE   A 144 ? 0.1450 0.2550 0.2450 0.0075  -0.0435 0.0015  141 PHE   A O     
1117 C  CB    . PHE   A 144 ? 0.1588 0.2587 0.2412 0.0012  -0.0343 -0.0056 141 PHE   A CB    
1118 C  CG    . PHE   A 144 ? 0.1664 0.2592 0.2360 0.0023  -0.0273 -0.0012 141 PHE   A CG    
1119 C  CD1   . PHE   A 144 ? 0.1552 0.2511 0.2322 0.0016  -0.0180 0.0006  141 PHE   A CD1   
1120 C  CD2   . PHE   A 144 ? 0.1849 0.2691 0.2352 0.0034  -0.0300 0.0013  141 PHE   A CD2   
1121 C  CE1   . PHE   A 144 ? 0.1633 0.2555 0.2305 0.0011  -0.0113 0.0047  141 PHE   A CE1   
1122 C  CE2   . PHE   A 144 ? 0.1932 0.2717 0.2319 0.0027  -0.0227 0.0060  141 PHE   A CE2   
1123 C  CZ    . PHE   A 144 ? 0.1819 0.2653 0.2300 0.0011  -0.0132 0.0075  141 PHE   A CZ    
1124 N  N     . ILE   A 145 ? 0.1321 0.2434 0.2415 0.0046  -0.0285 0.0037  142 ILE   A N     
1125 C  CA    . ILE   A 145 ? 0.1365 0.2447 0.2455 0.0071  -0.0297 0.0080  142 ILE   A CA    
1126 C  C     . ILE   A 145 ? 0.1417 0.2424 0.2412 0.0045  -0.0219 0.0118  142 ILE   A C     
1127 O  O     . ILE   A 145 ? 0.1331 0.2383 0.2376 0.0021  -0.0148 0.0106  142 ILE   A O     
1128 C  CB    . ILE   A 145 ? 0.1229 0.2408 0.2500 0.0086  -0.0296 0.0073  142 ILE   A CB    
1129 C  CG1   . ILE   A 145 ? 0.1194 0.2497 0.2602 0.0092  -0.0343 0.0032  142 ILE   A CG1   
1130 C  CG2   . ILE   A 145 ? 0.1285 0.2406 0.2537 0.0120  -0.0321 0.0105  142 ILE   A CG2   
1131 C  CD1   . ILE   A 145 ? 0.1299 0.2625 0.2699 0.0135  -0.0440 0.0025  142 ILE   A CD1   
1132 N  N     . GLU   A 146 ? 0.1573 0.2473 0.2438 0.0050  -0.0238 0.0163  143 GLU   A N     
1133 C  CA    . GLU   A 146 ? 0.1654 0.2491 0.2438 0.0009  -0.0164 0.0208  143 GLU   A CA    
1134 C  C     . GLU   A 146 ? 0.1587 0.2414 0.2466 0.0010  -0.0168 0.0228  143 GLU   A C     
1135 O  O     . GLU   A 146 ? 0.1632 0.2400 0.2500 0.0051  -0.0240 0.0236  143 GLU   A O     
1136 C  CB    . GLU   A 146 ? 0.1911 0.2620 0.2472 -0.0002 -0.0172 0.0250  143 GLU   A CB    
1137 C  CG    . GLU   A 146 ? 0.2003 0.2728 0.2461 -0.0015 -0.0130 0.0227  143 GLU   A CG    
1138 C  CD    . GLU   A 146 ? 0.2264 0.2880 0.2486 -0.0037 -0.0106 0.0272  143 GLU   A CD    
1139 O  OE1   . GLU   A 146 ? 0.2408 0.2928 0.2543 -0.0059 -0.0107 0.0334  143 GLU   A OE1   
1140 O  OE2   . GLU   A 146 ? 0.2371 0.2992 0.2491 -0.0034 -0.0087 0.0244  143 GLU   A OE2   
1141 N  N     . THR   A 147 ? 0.1486 0.2369 0.2447 -0.0031 -0.0095 0.0230  144 THR   A N     
1142 C  CA    . THR   A 147 ? 0.1416 0.2290 0.2465 -0.0035 -0.0100 0.0237  144 THR   A CA    
1143 C  C     . THR   A 147 ? 0.1470 0.2304 0.2478 -0.0106 -0.0036 0.0275  144 THR   A C     
1144 O  O     . THR   A 147 ? 0.1483 0.2337 0.2427 -0.0147 0.0023  0.0292  144 THR   A O     
1145 C  CB    . THR   A 147 ? 0.1230 0.2250 0.2460 -0.0024 -0.0078 0.0193  144 THR   A CB    
1146 O  OG1   . THR   A 147 ? 0.1160 0.2263 0.2417 -0.0059 -0.0003 0.0188  144 THR   A OG1   
1147 C  CG2   . THR   A 147 ? 0.1143 0.2240 0.2458 0.0026  -0.0126 0.0154  144 THR   A CG2   
1148 N  N     . SER   A 148 ? 0.1497 0.2267 0.2533 -0.0116 -0.0057 0.0284  145 SER   A N     
1149 C  CA    . SER   A 148 ? 0.1547 0.2290 0.2575 -0.0198 -0.0006 0.0312  145 SER   A CA    
1150 C  C     . SER   A 148 ? 0.1444 0.2239 0.2607 -0.0194 -0.0018 0.0276  145 SER   A C     
1151 O  O     . SER   A 148 ? 0.1497 0.2186 0.2641 -0.0161 -0.0073 0.0269  145 SER   A O     
1152 C  CB    . SER   A 148 ? 0.1787 0.2331 0.2647 -0.0242 -0.0022 0.0371  145 SER   A CB    
1153 O  OG    . SER   A 148 ? 0.1856 0.2374 0.2730 -0.0332 0.0018  0.0391  145 SER   A OG    
1154 N  N     . ALA   A 149 ? 0.1288 0.2246 0.2574 -0.0218 0.0034  0.0252  146 ALA   A N     
1155 C  CA    . ALA   A 149 ? 0.1226 0.2239 0.2622 -0.0225 0.0026  0.0220  146 ALA   A CA    
1156 C  C     . ALA   A 149 ? 0.1429 0.2301 0.2759 -0.0293 0.0014  0.0242  146 ALA   A C     
1157 O  O     . ALA   A 149 ? 0.1428 0.2265 0.2798 -0.0283 -0.0021 0.0211  146 ALA   A O     
1158 C  CB    . ALA   A 149 ? 0.1060 0.2268 0.2578 -0.0243 0.0082  0.0201  146 ALA   A CB    
1159 N  N     . LYS   A 150 ? 0.1640 0.2432 0.2865 -0.0368 0.0046  0.0294  147 LYS   A N     
1160 C  CA    . LYS   A 150 ? 0.1892 0.2532 0.3042 -0.0457 0.0039  0.0324  147 LYS   A CA    
1161 C  C     . LYS   A 150 ? 0.2107 0.2495 0.3135 -0.0410 -0.0040 0.0332  147 LYS   A C     
1162 O  O     . LYS   A 150 ? 0.2181 0.2459 0.3205 -0.0432 -0.0074 0.0313  147 LYS   A O     
1163 C  CB    . LYS   A 150 ? 0.2056 0.2684 0.3118 -0.0558 0.0103  0.0385  147 LYS   A CB    
1164 C  CG    . LYS   A 150 ? 0.2277 0.2768 0.3278 -0.0680 0.0106  0.0420  147 LYS   A CG    
1165 C  CD    . LYS   A 150 ? 0.2443 0.2959 0.3371 -0.0790 0.0183  0.0483  147 LYS   A CD    
1166 C  CE    . LYS   A 150 ? 0.2726 0.3042 0.3552 -0.0919 0.0176  0.0531  147 LYS   A CE    
1167 N  NZ    . LYS   A 150 ? 0.2800 0.3253 0.3640 -0.1055 0.0271  0.0577  147 LYS   A NZ    
1168 N  N     . THR   A 151 ? 0.2220 0.2519 0.3148 -0.0340 -0.0074 0.0355  148 THR   A N     
1169 C  CA    . THR   A 151 ? 0.2466 0.2523 0.3270 -0.0283 -0.0154 0.0367  148 THR   A CA    
1170 C  C     . THR   A 151 ? 0.2370 0.2489 0.3260 -0.0150 -0.0214 0.0309  148 THR   A C     
1171 O  O     . THR   A 151 ? 0.2551 0.2505 0.3355 -0.0082 -0.0281 0.0314  148 THR   A O     
1172 C  CB    . THR   A 151 ? 0.2708 0.2603 0.3322 -0.0291 -0.0167 0.0439  148 THR   A CB    
1173 O  OG1   . THR   A 151 ? 0.2608 0.2658 0.3254 -0.0235 -0.0156 0.0428  148 THR   A OG1   
1174 C  CG2   . THR   A 151 ? 0.2847 0.2701 0.3369 -0.0428 -0.0095 0.0503  148 THR   A CG2   
1175 N  N     . ARG   A 152 ? 0.2171 0.2524 0.3214 -0.0118 -0.0185 0.0264  149 ARG   A N     
1176 C  CA    . ARG   A 152 ? 0.2060 0.2527 0.3212 -0.0012 -0.0224 0.0208  149 ARG   A CA    
1177 C  C     . ARG   A 152 ? 0.2068 0.2544 0.3177 0.0057  -0.0264 0.0221  149 ARG   A C     
1178 O  O     . ARG   A 152 ? 0.1962 0.2562 0.3172 0.0128  -0.0289 0.0179  149 ARG   A O     
1179 C  CB    . ARG   A 152 ? 0.2187 0.2578 0.3364 0.0039  -0.0266 0.0164  149 ARG   A CB    
1180 C  CG    . ARG   A 152 ? 0.2167 0.2668 0.3443 0.0152  -0.0303 0.0109  149 ARG   A CG    
1181 C  CD    . ARG   A 152 ? 0.2312 0.2731 0.3594 0.0194  -0.0331 0.0061  149 ARG   A CD    
1182 N  NE    . ARG   A 152 ? 0.2223 0.2828 0.3633 0.0280  -0.0335 0.0007  149 ARG   A NE    
1183 C  CZ    . ARG   A 152 ? 0.2072 0.2867 0.3599 0.0262  -0.0288 -0.0025 149 ARG   A CZ    
1184 N  NH1   . ARG   A 152 ? 0.2003 0.2833 0.3545 0.0170  -0.0241 -0.0015 149 ARG   A NH1   
1185 N  NH2   . ARG   A 152 ? 0.2000 0.2956 0.3631 0.0335  -0.0289 -0.0067 149 ARG   A NH2   
1186 N  N     . GLN   A 153 ? 0.2152 0.2532 0.3124 0.0023  -0.0262 0.0275  150 GLN   A N     
1187 C  CA    . GLN   A 153 ? 0.2209 0.2589 0.3120 0.0085  -0.0311 0.0285  150 GLN   A CA    
1188 C  C     . GLN   A 153 ? 0.1887 0.2488 0.2939 0.0108  -0.0295 0.0239  150 GLN   A C     
1189 O  O     . GLN   A 153 ? 0.1731 0.2431 0.2826 0.0050  -0.0227 0.0235  150 GLN   A O     
1190 C  CB    . GLN   A 153 ? 0.2439 0.2726 0.3182 0.0032  -0.0291 0.0345  150 GLN   A CB    
1191 C  CG    . GLN   A 153 ? 0.2810 0.2855 0.3372 -0.0011 -0.0301 0.0410  150 GLN   A CG    
1192 C  CD    . GLN   A 153 ? 0.3122 0.2975 0.3564 0.0076  -0.0401 0.0433  150 GLN   A CD    
1193 O  OE1   . GLN   A 153 ? 0.3333 0.3171 0.3688 0.0128  -0.0450 0.0450  150 GLN   A OE1   
1194 N  NE2   . GLN   A 153 ? 0.3292 0.2991 0.3717 0.0094  -0.0433 0.0432  150 GLN   A NE2   
1195 N  N     . ARG   A 154 ? 0.1769 0.2441 0.2894 0.0191  -0.0356 0.0204  151 ARG   A N     
1196 C  CA    . ARG   A 154 ? 0.1558 0.2423 0.2805 0.0205  -0.0353 0.0164  151 ARG   A CA    
1197 C  C     . ARG   A 154 ? 0.1337 0.2351 0.2730 0.0169  -0.0285 0.0132  151 ARG   A C     
1198 O  O     . ARG   A 154 ? 0.1216 0.2354 0.2686 0.0161  -0.0272 0.0109  151 ARG   A O     
1199 C  CB    . ARG   A 154 ? 0.1648 0.2492 0.2787 0.0182  -0.0360 0.0185  151 ARG   A CB    
1200 C  CG    . ARG   A 154 ? 0.1899 0.2600 0.2890 0.0232  -0.0442 0.0218  151 ARG   A CG    
1201 C  CD    . ARG   A 154 ? 0.2085 0.2716 0.2915 0.0228  -0.0476 0.0246  151 ARG   A CD    
1202 N  NE    . ARG   A 154 ? 0.6949 0.7431 0.7659 0.0296  -0.0563 0.0280  151 ARG   A NE    
1203 C  CZ    . ARG   A 154 ? 0.7192 0.7494 0.7684 0.0291  -0.0590 0.0340  151 ARG   A CZ    
1204 N  NH1   . ARG   A 154 ? 0.7256 0.7520 0.7618 0.0220  -0.0534 0.0369  151 ARG   A NH1   
1205 N  NH2   . ARG   A 154 ? 0.7390 0.7552 0.7787 0.0368  -0.0679 0.0370  151 ARG   A NH2   
1206 N  N     . VAL   A 155 ? 0.1274 0.2266 0.2701 0.0153  -0.0255 0.0127  152 VAL   A N     
1207 C  CA    . VAL   A 155 ? 0.1078 0.2211 0.2628 0.0123  -0.0197 0.0102  152 VAL   A CA    
1208 C  C     . VAL   A 155 ? 0.0976 0.2254 0.2656 0.0174  -0.0215 0.0060  152 VAL   A C     
1209 O  O     . VAL   A 155 ? 0.0836 0.2233 0.2590 0.0155  -0.0189 0.0049  152 VAL   A O     
1210 C  CB    . VAL   A 155 ? 0.1069 0.2159 0.2620 0.0086  -0.0165 0.0104  152 VAL   A CB    
1211 C  CG1   . VAL   A 155 ? 0.0889 0.2132 0.2563 0.0073  -0.0120 0.0076  152 VAL   A CG1   
1212 C  CG2   . VAL   A 155 ? 0.1163 0.2159 0.2613 0.0013  -0.0130 0.0147  152 VAL   A CG2   
1213 N  N     . GLU   A 156 ? 0.1026 0.2290 0.2729 0.0239  -0.0259 0.0038  153 GLU   A N     
1214 C  CA    . GLU   A 156 ? 0.0949 0.2374 0.2778 0.0292  -0.0275 -0.0001 153 GLU   A CA    
1215 C  C     . GLU   A 156 ? 0.0889 0.2405 0.2752 0.0287  -0.0300 0.0000  153 GLU   A C     
1216 O  O     . GLU   A 156 ? 0.0745 0.2413 0.2717 0.0268  -0.0277 -0.0019 153 GLU   A O     
1217 C  CB    . GLU   A 156 ? 0.1097 0.2480 0.2923 0.0382  -0.0329 -0.0026 153 GLU   A CB    
1218 C  CG    . GLU   A 156 ? 0.1152 0.2533 0.3006 0.0405  -0.0304 -0.0059 153 GLU   A CG    
1219 C  CD    . GLU   A 156 ? 0.1268 0.2657 0.3149 0.0516  -0.0352 -0.0102 153 GLU   A CD    
1220 O  OE1   . GLU   A 156 ? 0.1374 0.2790 0.3269 0.0580  -0.0409 -0.0103 153 GLU   A OE1   
1221 O  OE2   . GLU   A 156 ? 0.1359 0.2731 0.3246 0.0546  -0.0337 -0.0138 153 GLU   A OE2   
1222 N  N     . ASP   A 157 ? 0.0998 0.2410 0.2759 0.0302  -0.0353 0.0021  154 ASP   A N     
1223 C  CA    . ASP   A 157 ? 0.1009 0.2486 0.2777 0.0297  -0.0392 0.0018  154 ASP   A CA    
1224 C  C     . ASP   A 157 ? 0.0827 0.2370 0.2630 0.0220  -0.0336 0.0015  154 ASP   A C     
1225 O  O     . ASP   A 157 ? 0.0716 0.2385 0.2610 0.0204  -0.0347 -0.0007 154 ASP   A O     
1226 C  CB    . ASP   A 157 ? 0.1247 0.2574 0.2855 0.0312  -0.0449 0.0050  154 ASP   A CB    
1227 C  CG    . ASP   A 157 ? 0.1456 0.2724 0.3025 0.0405  -0.0534 0.0052  154 ASP   A CG    
1228 O  OD1   . ASP   A 157 ? 0.1475 0.2838 0.3159 0.0474  -0.0554 0.0019  154 ASP   A OD1   
1229 O  OD2   . ASP   A 157 ? 0.1684 0.2815 0.3101 0.0419  -0.0584 0.0086  154 ASP   A OD2   
1230 N  N     . ALA   A 158 ? 0.0741 0.2198 0.2472 0.0171  -0.0277 0.0039  155 ALA   A N     
1231 C  CA    . ALA   A 158 ? 0.0648 0.2142 0.2396 0.0116  -0.0227 0.0035  155 ALA   A CA    
1232 C  C     . ALA   A 158 ? 0.0512 0.2140 0.2398 0.0104  -0.0196 0.0016  155 ALA   A C     
1233 O  O     . ALA   A 158 ? 0.0484 0.2169 0.2414 0.0073  -0.0193 0.0003  155 ALA   A O     
1234 C  CB    . ALA   A 158 ? 0.0658 0.2069 0.2326 0.0082  -0.0168 0.0060  155 ALA   A CB    
1235 N  N     . PHE   A 159 ? 0.0454 0.2121 0.2397 0.0123  -0.0171 0.0014  156 PHE   A N     
1236 C  CA    . PHE   A 159 ? 0.0352 0.2144 0.2405 0.0112  -0.0137 0.0001  156 PHE   A CA    
1237 C  C     . PHE   A 159 ? 0.0339 0.2259 0.2489 0.0126  -0.0172 -0.0022 156 PHE   A C     
1238 O  O     . PHE   A 159 ? 0.0293 0.2300 0.2511 0.0084  -0.0151 -0.0024 156 PHE   A O     
1239 C  CB    . PHE   A 159 ? 0.0313 0.2121 0.2389 0.0132  -0.0108 -0.0002 156 PHE   A CB    
1240 C  CG    . PHE   A 159 ? 0.0301 0.2042 0.2323 0.0101  -0.0065 0.0019  156 PHE   A CG    
1241 C  CD1   . PHE   A 159 ? 0.0237 0.2027 0.2291 0.0073  -0.0021 0.0029  156 PHE   A CD1   
1242 C  CD2   . PHE   A 159 ? 0.0369 0.2003 0.2310 0.0098  -0.0072 0.0031  156 PHE   A CD2   
1243 C  CE1   . PHE   A 159 ? 0.0228 0.1985 0.2248 0.0056  0.0012  0.0045  156 PHE   A CE1   
1244 C  CE2   . PHE   A 159 ? 0.0357 0.1966 0.2271 0.0064  -0.0031 0.0047  156 PHE   A CE2   
1245 C  CZ    . PHE   A 159 ? 0.0279 0.1963 0.2241 0.0049  0.0008  0.0051  156 PHE   A CZ    
1246 N  N     . TYR   A 160 ? 0.0425 0.2357 0.2581 0.0184  -0.0227 -0.0037 157 TYR   A N     
1247 C  CA    . TYR   A 160 ? 0.0409 0.2505 0.2682 0.0211  -0.0261 -0.0064 157 TYR   A CA    
1248 C  C     . TYR   A 160 ? 0.0422 0.2561 0.2714 0.0162  -0.0297 -0.0068 157 TYR   A C     
1249 O  O     . TYR   A 160 ? 0.0360 0.2658 0.2771 0.0129  -0.0294 -0.0084 157 TYR   A O     
1250 C  CB    . TYR   A 160 ? 0.0525 0.2607 0.2789 0.0305  -0.0319 -0.0081 157 TYR   A CB    
1251 C  CG    . TYR   A 160 ? 0.0556 0.2634 0.2833 0.0360  -0.0292 -0.0097 157 TYR   A CG    
1252 C  CD1   . TYR   A 160 ? 0.0495 0.2554 0.2761 0.0321  -0.0224 -0.0090 157 TYR   A CD1   
1253 C  CD2   . TYR   A 160 ? 0.0668 0.2753 0.2958 0.0460  -0.0340 -0.0124 157 TYR   A CD2   
1254 C  CE1   . TYR   A 160 ? 0.0529 0.2576 0.2791 0.0368  -0.0206 -0.0112 157 TYR   A CE1   
1255 C  CE2   . TYR   A 160 ? 0.0713 0.2766 0.2993 0.0514  -0.0318 -0.0148 157 TYR   A CE2   
1256 C  CZ    . TYR   A 160 ? 0.0646 0.2681 0.2910 0.0462  -0.0251 -0.0144 157 TYR   A CZ    
1257 O  OH    . TYR   A 160 ? 0.0735 0.2739 0.2980 0.0509  -0.0232 -0.0175 157 TYR   A OH    
1258 N  N     . THR   A 161 ? 0.0488 0.2486 0.2657 0.0148  -0.0326 -0.0054 158 THR   A N     
1259 C  CA    . THR   A 161 ? 0.0540 0.2538 0.2689 0.0095  -0.0359 -0.0064 158 THR   A CA    
1260 C  C     . THR   A 161 ? 0.0482 0.2510 0.2679 0.0016  -0.0303 -0.0063 158 THR   A C     
1261 O  O     . THR   A 161 ? 0.0487 0.2599 0.2752 -0.0036 -0.0326 -0.0081 158 THR   A O     
1262 C  CB    . THR   A 161 ? 0.0649 0.2473 0.2627 0.0096  -0.0384 -0.0049 158 THR   A CB    
1263 O  OG1   . THR   A 161 ? 0.0744 0.2535 0.2673 0.0168  -0.0445 -0.0043 158 THR   A OG1   
1264 C  CG2   . THR   A 161 ? 0.0725 0.2532 0.2660 0.0043  -0.0419 -0.0069 158 THR   A CG2   
1265 N  N     . LEU   A 162 ? 0.0453 0.2404 0.2610 0.0005  -0.0235 -0.0041 159 LEU   A N     
1266 C  CA    . LEU   A 162 ? 0.0437 0.2378 0.2613 -0.0057 -0.0185 -0.0033 159 LEU   A CA    
1267 C  C     . LEU   A 162 ? 0.0379 0.2486 0.2695 -0.0086 -0.0169 -0.0036 159 LEU   A C     
1268 O  O     . LEU   A 162 ? 0.0382 0.2518 0.2737 -0.0156 -0.0169 -0.0039 159 LEU   A O     
1269 C  CB    . LEU   A 162 ? 0.0413 0.2263 0.2527 -0.0045 -0.0123 -0.0008 159 LEU   A CB    
1270 C  CG    . LEU   A 162 ? 0.0414 0.2226 0.2526 -0.0089 -0.0075 0.0007  159 LEU   A CG    
1271 C  CD1   . LEU   A 162 ? 0.0515 0.2217 0.2553 -0.0128 -0.0091 -0.0007 159 LEU   A CD1   
1272 C  CD2   . LEU   A 162 ? 0.0383 0.2148 0.2455 -0.0058 -0.0025 0.0029  159 LEU   A CD2   
1273 N  N     . VAL   A 163 ? 0.0338 0.2546 0.2718 -0.0033 -0.0159 -0.0039 160 VAL   A N     
1274 C  CA    . VAL   A 163 ? 0.0316 0.2714 0.2832 -0.0054 -0.0136 -0.0045 160 VAL   A CA    
1275 C  C     . VAL   A 163 ? 0.0336 0.2860 0.2943 -0.0091 -0.0190 -0.0070 160 VAL   A C     
1276 O  O     . VAL   A 163 ? 0.0343 0.2954 0.3024 -0.0166 -0.0167 -0.0064 160 VAL   A O     
1277 C  CB    . VAL   A 163 ? 0.0272 0.2768 0.2839 0.0023  -0.0120 -0.0058 160 VAL   A CB    
1278 C  CG1   . VAL   A 163 ? 0.0241 0.2964 0.2952 0.0006  -0.0095 -0.0071 160 VAL   A CG1   
1279 C  CG2   . VAL   A 163 ? 0.0257 0.2652 0.2746 0.0042  -0.0070 -0.0039 160 VAL   A CG2   
1280 N  N     . ARG   A 164 ? 0.0392 0.2897 0.2973 -0.0046 -0.0263 -0.0091 161 ARG   A N     
1281 C  CA    . ARG   A 164 ? 0.0444 0.3085 0.3114 -0.0077 -0.0331 -0.0119 161 ARG   A CA    
1282 C  C     . ARG   A 164 ? 0.0509 0.3078 0.3147 -0.0188 -0.0335 -0.0118 161 ARG   A C     
1283 O  O     . ARG   A 164 ? 0.0486 0.3206 0.3242 -0.0262 -0.0350 -0.0132 161 ARG   A O     
1284 C  CB    . ARG   A 164 ? 0.0524 0.3134 0.3142 0.0005  -0.0417 -0.0136 161 ARG   A CB    
1285 C  CG    . ARG   A 164 ? 0.0510 0.3198 0.3177 0.0116  -0.0422 -0.0144 161 ARG   A CG    
1286 C  CD    . ARG   A 164 ? 0.0629 0.3259 0.3228 0.0209  -0.0510 -0.0152 161 ARG   A CD    
1287 N  NE    . ARG   A 164 ? 0.0645 0.3310 0.3275 0.0317  -0.0509 -0.0161 161 ARG   A NE    
1288 C  CZ    . ARG   A 164 ? 0.0718 0.3198 0.3218 0.0389  -0.0524 -0.0145 161 ARG   A CZ    
1289 N  NH1   . ARG   A 164 ? 0.0806 0.3077 0.3140 0.0361  -0.0538 -0.0115 161 ARG   A NH1   
1290 N  NH2   . ARG   A 164 ? 0.0722 0.3221 0.3249 0.0484  -0.0522 -0.0160 161 ARG   A NH2   
1291 N  N     . GLU   A 165 ? 0.0526 0.2874 0.3011 -0.0199 -0.0317 -0.0103 162 GLU   A N     
1292 C  CA    . GLU   A 165 ? 0.0641 0.2869 0.3062 -0.0289 -0.0317 -0.0107 162 GLU   A CA    
1293 C  C     . GLU   A 165 ? 0.0643 0.2922 0.3144 -0.0371 -0.0255 -0.0085 162 GLU   A C     
1294 O  O     . GLU   A 165 ? 0.0774 0.3068 0.3310 -0.0466 -0.0276 -0.0097 162 GLU   A O     
1295 C  CB    . GLU   A 165 ? 0.0685 0.2682 0.2930 -0.0259 -0.0295 -0.0097 162 GLU   A CB    
1296 C  CG    . GLU   A 165 ? 0.0757 0.2680 0.2894 -0.0212 -0.0357 -0.0117 162 GLU   A CG    
1297 C  CD    . GLU   A 165 ? 0.0886 0.2819 0.3005 -0.0260 -0.0440 -0.0157 162 GLU   A CD    
1298 O  OE1   . GLU   A 165 ? 0.0979 0.2803 0.3034 -0.0326 -0.0440 -0.0176 162 GLU   A OE1   
1299 O  OE2   . GLU   A 165 ? 0.0890 0.2936 0.3055 -0.0226 -0.0508 -0.0171 162 GLU   A OE2   
1300 N  N     . ILE   A 166 ? 0.0606 0.2910 0.3127 -0.0338 -0.0187 -0.0053 163 ILE   A N     
1301 C  CA    . ILE   A 166 ? 0.0679 0.3025 0.3253 -0.0409 -0.0123 -0.0021 163 ILE   A CA    
1302 C  C     . ILE   A 166 ? 0.0733 0.3328 0.3477 -0.0468 -0.0135 -0.0034 163 ILE   A C     
1303 O  O     . ILE   A 166 ? 0.0826 0.3436 0.3608 -0.0574 -0.0126 -0.0024 163 ILE   A O     
1304 C  CB    . ILE   A 166 ? 0.0605 0.2944 0.3154 -0.0349 -0.0056 0.0012  163 ILE   A CB    
1305 C  CG1   . ILE   A 166 ? 0.0638 0.2775 0.3047 -0.0292 -0.0044 0.0024  163 ILE   A CG1   
1306 C  CG2   . ILE   A 166 ? 0.0644 0.3026 0.3229 -0.0419 0.0006  0.0052  163 ILE   A CG2   
1307 C  CD1   . ILE   A 166 ? 0.0568 0.2715 0.2960 -0.0237 0.0009  0.0050  163 ILE   A CD1   
1308 N  N     . ARG   A 167 ? 0.0750 0.3528 0.3590 -0.0396 -0.0160 -0.0059 164 ARG   A N     
1309 C  CA    . ARG   A 167 ? 0.0855 0.3918 0.3882 -0.0440 -0.0166 -0.0077 164 ARG   A CA    
1310 C  C     . ARG   A 167 ? 0.1083 0.4186 0.4163 -0.0543 -0.0231 -0.0102 164 ARG   A C     
1311 O  O     . ARG   A 167 ? 0.1189 0.4441 0.4384 -0.0650 -0.0208 -0.0094 164 ARG   A O     
1312 C  CB    . ARG   A 167 ? 0.0799 0.4013 0.3899 -0.0323 -0.0217 -0.0115 164 ARG   A CB    
1313 C  CG    . ARG   A 167 ? 0.0718 0.4037 0.3859 -0.0232 -0.0159 -0.0112 164 ARG   A CG    
1314 C  CD    . ARG   A 167 ? 0.0718 0.4199 0.3951 -0.0128 -0.0224 -0.0155 164 ARG   A CD    
1315 N  NE    . ARG   A 167 ? 0.0659 0.4153 0.3876 -0.0022 -0.0182 -0.0160 164 ARG   A NE    
1316 C  CZ    . ARG   A 167 ? 0.0667 0.4149 0.3867 0.0103  -0.0229 -0.0188 164 ARG   A CZ    
1317 N  NH1   . ARG   A 167 ? 0.0707 0.4156 0.3892 0.0140  -0.0322 -0.0204 164 ARG   A NH1   
1318 N  NH2   . ARG   A 167 ? 0.0660 0.4127 0.3830 0.0189  -0.0187 -0.0196 164 ARG   A NH2   
1319 N  N     . GLN   A 168 ? 0.1246 0.4222 0.4236 -0.0514 -0.0310 -0.0130 165 GLN   A N     
1320 C  CA    . GLN   A 168 ? 0.1470 0.4461 0.4480 -0.0599 -0.0393 -0.0165 165 GLN   A CA    
1321 C  C     . GLN   A 168 ? 0.1640 0.4453 0.4577 -0.0735 -0.0369 -0.0151 165 GLN   A C     
1322 O  O     . GLN   A 168 ? 0.1697 0.4580 0.4701 -0.0845 -0.0420 -0.0178 165 GLN   A O     
1323 C  CB    . GLN   A 168 ? 0.1557 0.4451 0.4462 -0.0512 -0.0480 -0.0196 165 GLN   A CB    
1324 C  CG    . GLN   A 168 ? 0.1513 0.4565 0.4487 -0.0380 -0.0512 -0.0207 165 GLN   A CG    
1325 C  CD    . GLN   A 168 ? 0.1652 0.4569 0.4487 -0.0301 -0.0596 -0.0224 165 GLN   A CD    
1326 O  OE1   . GLN   A 168 ? 0.1943 0.4761 0.4692 -0.0355 -0.0655 -0.0246 165 GLN   A OE1   
1327 N  NE2   . GLN   A 168 ? 0.1631 0.4529 0.4426 -0.0175 -0.0601 -0.0213 165 GLN   A NE2   
1328 N  N     . TYR   A 169 ? 0.1703 0.4279 0.4495 -0.0720 -0.0306 -0.0115 166 TYR   A N     
1329 C  CA    . TYR   A 169 ? 0.1938 0.4315 0.4647 -0.0834 -0.0281 -0.0097 166 TYR   A CA    
1330 C  C     . TYR   A 169 ? 0.1989 0.4551 0.4852 -0.0961 -0.0243 -0.0072 166 TYR   A C     
1331 O  O     . TYR   A 169 ? 0.2147 0.4671 0.5024 -0.1092 -0.0268 -0.0081 166 TYR   A O     
1332 C  CB    . TYR   A 169 ? 0.2005 0.4167 0.4572 -0.0767 -0.0211 -0.0055 166 TYR   A CB    
1333 C  CG    . TYR   A 169 ? 0.2227 0.4192 0.4712 -0.0856 -0.0170 -0.0021 166 TYR   A CG    
1334 C  CD1   . TYR   A 169 ? 0.2277 0.4310 0.4821 -0.0912 -0.0102 0.0034  166 TYR   A CD1   
1335 C  CD2   . TYR   A 169 ? 0.2478 0.4170 0.4806 -0.0871 -0.0197 -0.0041 166 TYR   A CD2   
1336 C  CE1   . TYR   A 169 ? 0.2544 0.4372 0.4996 -0.0993 -0.0068 0.0075  166 TYR   A CE1   
1337 C  CE2   . TYR   A 169 ? 0.2690 0.4168 0.4928 -0.0940 -0.0164 -0.0009 166 TYR   A CE2   
1338 C  CZ    . TYR   A 169 ? 0.2741 0.4282 0.5041 -0.1005 -0.0102 0.0053  166 TYR   A CZ    
1339 O  OH    . TYR   A 169 ? 0.3015 0.4333 0.5217 -0.1079 -0.0072 0.0096  166 TYR   A OH    
1340 N  N     . ARG   A 170 ? 0.1932 0.4691 0.4898 -0.0916 -0.0181 -0.0043 167 ARG   A N     
1341 C  CA    . ARG   A 170 ? 0.1922 0.4894 0.5034 -0.1018 -0.0120 -0.0010 167 ARG   A CA    
1342 C  C     . ARG   A 170 ? 0.1934 0.5240 0.5260 -0.1069 -0.0168 -0.0053 167 ARG   A C     
1343 O  O     . ARG   A 170 ? 0.2081 0.5492 0.5501 -0.1214 -0.0154 -0.0041 167 ARG   A O     
1344 C  CB    . ARG   A 170 ? 0.1751 0.4803 0.4868 -0.0927 -0.0035 0.0028  167 ARG   A CB    
1345 C  CG    . ARG   A 170 ? 0.1745 0.4520 0.4675 -0.0844 -0.0006 0.0058  167 ARG   A CG    
1346 C  CD    . ARG   A 170 ? 0.1575 0.4461 0.4521 -0.0737 0.0053  0.0075  167 ARG   A CD    
1347 N  NE    . ARG   A 170 ? 0.1585 0.4253 0.4383 -0.0726 0.0104  0.0125  167 ARG   A NE    
1348 C  CZ    . ARG   A 170 ? 0.1548 0.4212 0.4295 -0.0638 0.0150  0.0146  167 ARG   A CZ    
1349 N  NH1   . ARG   A 170 ? 0.1608 0.4073 0.4223 -0.0637 0.0183  0.0193  167 ARG   A NH1   
1350 N  NH2   . ARG   A 170 ? 0.1366 0.4219 0.4191 -0.0554 0.0160  0.0119  167 ARG   A NH2   
1351 N  N     . LEU   A 171 ? 0.1885 0.5341 0.5276 -0.0951 -0.0228 -0.0099 168 LEU   A N     
1352 C  CA    . LEU   A 171 ? 0.1863 0.5665 0.5469 -0.0964 -0.0283 -0.0143 168 LEU   A CA    
1353 C  C     . LEU   A 171 ? 0.1980 0.5735 0.5566 -0.0990 -0.0407 -0.0197 168 LEU   A C     
1354 O  O     . LEU   A 171 ? 0.1935 0.5570 0.5413 -0.0870 -0.0468 -0.0220 168 LEU   A O     
1355 C  CB    . LEU   A 171 ? 0.1786 0.5780 0.5469 -0.0795 -0.0268 -0.0157 168 LEU   A CB    
1356 C  CG    . LEU   A 171 ? 0.1731 0.5905 0.5502 -0.0786 -0.0155 -0.0125 168 LEU   A CG    
1357 C  CD1   . LEU   A 171 ? 0.1809 0.5738 0.5425 -0.0840 -0.0066 -0.0063 168 LEU   A CD1   
1358 C  CD2   . LEU   A 171 ? 0.1581 0.5900 0.5400 -0.0606 -0.0147 -0.0151 168 LEU   A CD2   
1359 N  N     . MET   B 4   ? 0.5264 0.4498 0.3406 -0.0404 -0.0159 -0.0153 1   MET   B N     
1360 C  CA    . MET   B 4   ? 0.5218 0.4413 0.3353 -0.0355 -0.0138 -0.0133 1   MET   B CA    
1361 C  C     . MET   B 4   ? 0.5124 0.4202 0.3315 -0.0295 -0.0127 -0.0083 1   MET   B C     
1362 O  O     . MET   B 4   ? 0.5100 0.4084 0.3318 -0.0294 -0.0122 -0.0106 1   MET   B O     
1363 C  CB    . MET   B 4   ? 0.5278 0.4409 0.3377 -0.0363 -0.0114 -0.0229 1   MET   B CB    
1364 C  CG    . MET   B 4   ? 0.5259 0.4387 0.3342 -0.0323 -0.0095 -0.0209 1   MET   B CG    
1365 S  SD    . MET   B 4   ? 0.5348 0.4424 0.3397 -0.0332 -0.0066 -0.0327 1   MET   B SD    
1366 C  CE    . MET   B 4   ? 0.5427 0.4674 0.3420 -0.0409 -0.0080 -0.0398 1   MET   B CE    
1367 N  N     . THR   B 5   ? 0.5075 0.4165 0.3283 -0.0252 -0.0122 -0.0023 2   THR   B N     
1368 C  CA    . THR   B 5   ? 0.4998 0.3993 0.3259 -0.0196 -0.0109 0.0017  2   THR   B CA    
1369 C  C     . THR   B 5   ? 0.4960 0.3828 0.3208 -0.0175 -0.0082 -0.0036 2   THR   B C     
1370 O  O     . THR   B 5   ? 0.5032 0.3900 0.3245 -0.0173 -0.0069 -0.0062 2   THR   B O     
1371 C  CB    . THR   B 5   ? 0.4977 0.4019 0.3273 -0.0161 -0.0114 0.0095  2   THR   B CB    
1372 O  OG1   . THR   B 5   ? 0.5031 0.4210 0.3344 -0.0180 -0.0141 0.0155  2   THR   B OG1   
1373 C  CG2   . THR   B 5   ? 0.4910 0.3874 0.3275 -0.0109 -0.0103 0.0126  2   THR   B CG2   
1374 N  N     . GLU   B 6   ? 0.4879 0.3658 0.3161 -0.0159 -0.0073 -0.0044 3   GLU   B N     
1375 C  CA    . GLU   B 6   ? 0.4802 0.3467 0.3085 -0.0137 -0.0050 -0.0080 3   GLU   B CA    
1376 C  C     . GLU   B 6   ? 0.4632 0.3256 0.2953 -0.0090 -0.0038 -0.0040 3   GLU   B C     
1377 O  O     . GLU   B 6   ? 0.4614 0.3277 0.2973 -0.0074 -0.0046 0.0003  3   GLU   B O     
1378 C  CB    . GLU   B 6   ? 0.4870 0.3474 0.3169 -0.0162 -0.0052 -0.0115 3   GLU   B CB    
1379 C  CG    . GLU   B 6   ? 0.5000 0.3635 0.3272 -0.0213 -0.0064 -0.0167 3   GLU   B CG    
1380 C  CD    . GLU   B 6   ? 0.5082 0.3676 0.3388 -0.0245 -0.0076 -0.0177 3   GLU   B CD    
1381 O  OE1   . GLU   B 6   ? 0.5110 0.3675 0.3454 -0.0226 -0.0075 -0.0134 3   GLU   B OE1   
1382 O  OE2   . GLU   B 6   ? 0.5192 0.3788 0.3490 -0.0291 -0.0085 -0.0230 3   GLU   B OE2   
1383 N  N     . TYR   B 7   ? 0.4539 0.3091 0.2855 -0.0068 -0.0018 -0.0061 4   TYR   B N     
1384 C  CA    . TYR   B 7   ? 0.4421 0.2936 0.2768 -0.0029 -0.0004 -0.0036 4   TYR   B CA    
1385 C  C     . TYR   B 7   ? 0.4393 0.2830 0.2748 -0.0024 0.0009  -0.0061 4   TYR   B C     
1386 O  O     . TYR   B 7   ? 0.4438 0.2833 0.2773 -0.0027 0.0019  -0.0096 4   TYR   B O     
1387 C  CB    . TYR   B 7   ? 0.4370 0.2900 0.2708 -0.0008 0.0003  -0.0019 4   TYR   B CB    
1388 C  CG    . TYR   B 7   ? 0.4358 0.2969 0.2711 -0.0010 -0.0014 0.0028  4   TYR   B CG    
1389 C  CD1   . TYR   B 7   ? 0.4402 0.3090 0.2717 -0.0040 -0.0027 0.0030  4   TYR   B CD1   
1390 C  CD2   . TYR   B 7   ? 0.4319 0.2939 0.2732 0.0017  -0.0017 0.0071  4   TYR   B CD2   
1391 C  CE1   . TYR   B 7   ? 0.4413 0.3189 0.2750 -0.0044 -0.0047 0.0088  4   TYR   B CE1   
1392 C  CE2   . TYR   B 7   ? 0.4329 0.3020 0.2777 0.0019  -0.0035 0.0125  4   TYR   B CE2   
1393 C  CZ    . TYR   B 7   ? 0.4376 0.3148 0.2784 -0.0012 -0.0052 0.0142  4   TYR   B CZ    
1394 O  OH    . TYR   B 7   ? 0.4405 0.3262 0.2854 -0.0013 -0.0073 0.0209  4   TYR   B OH    
1395 N  N     . LYS   B 8   ? 0.4378 0.2809 0.2767 -0.0017 0.0010  -0.0042 5   LYS   B N     
1396 C  CA    . LYS   B 8   ? 0.4346 0.2726 0.2753 -0.0016 0.0019  -0.0047 5   LYS   B CA    
1397 C  C     . LYS   B 8   ? 0.4274 0.2642 0.2690 0.0017  0.0036  -0.0038 5   LYS   B C     
1398 O  O     . LYS   B 8   ? 0.4209 0.2615 0.2646 0.0031  0.0039  -0.0022 5   LYS   B O     
1399 C  CB    . LYS   B 8   ? 0.4376 0.2785 0.2813 -0.0035 0.0009  -0.0025 5   LYS   B CB    
1400 C  CG    . LYS   B 8   ? 0.4456 0.2877 0.2890 -0.0075 -0.0010 -0.0032 5   LYS   B CG    
1401 C  CD    . LYS   B 8   ? 0.4517 0.2934 0.2986 -0.0102 -0.0019 -0.0011 5   LYS   B CD    
1402 C  CE    . LYS   B 8   ? 0.4600 0.3022 0.3073 -0.0147 -0.0039 -0.0021 5   LYS   B CE    
1403 N  NZ    . LYS   B 8   ? 0.4618 0.3125 0.3077 -0.0154 -0.0050 -0.0014 5   LYS   B NZ    
1404 N  N     . LEU   B 9   ? 0.4269 0.2589 0.2674 0.0028  0.0048  -0.0054 6   LEU   B N     
1405 C  CA    . LEU   B 9   ? 0.4221 0.2536 0.2630 0.0055  0.0064  -0.0047 6   LEU   B CA    
1406 C  C     . LEU   B 9   ? 0.4211 0.2499 0.2642 0.0058  0.0071  -0.0039 6   LEU   B C     
1407 O  O     . LEU   B 9   ? 0.4269 0.2515 0.2710 0.0047  0.0067  -0.0045 6   LEU   B O     
1408 C  CB    . LEU   B 9   ? 0.4224 0.2527 0.2603 0.0065  0.0072  -0.0064 6   LEU   B CB    
1409 C  CG    . LEU   B 9   ? 0.4221 0.2567 0.2580 0.0056  0.0062  -0.0060 6   LEU   B CG    
1410 C  CD1   . LEU   B 9   ? 0.4235 0.2590 0.2565 0.0063  0.0071  -0.0070 6   LEU   B CD1   
1411 C  CD2   . LEU   B 9   ? 0.4184 0.2566 0.2573 0.0065  0.0055  -0.0029 6   LEU   B CD2   
1412 N  N     . VAL   B 10  ? 0.4174 0.2491 0.2619 0.0070  0.0079  -0.0024 7   VAL   B N     
1413 C  CA    . VAL   B 10  ? 0.4163 0.2482 0.2631 0.0071  0.0084  -0.0004 7   VAL   B CA    
1414 C  C     . VAL   B 10  ? 0.4122 0.2446 0.2584 0.0093  0.0100  -0.0008 7   VAL   B C     
1415 O  O     . VAL   B 10  ? 0.4097 0.2449 0.2555 0.0100  0.0106  -0.0018 7   VAL   B O     
1416 C  CB    . VAL   B 10  ? 0.4133 0.2520 0.2625 0.0055  0.0078  0.0021  7   VAL   B CB    
1417 C  CG1   . VAL   B 10  ? 0.4145 0.2552 0.2663 0.0049  0.0079  0.0056  7   VAL   B CG1   
1418 C  CG2   . VAL   B 10  ? 0.4161 0.2556 0.2659 0.0031  0.0063  0.0027  7   VAL   B CG2   
1419 N  N     . VAL   B 11  ? 0.4139 0.2435 0.2613 0.0102  0.0105  0.0000  8   VAL   B N     
1420 C  CA    . VAL   B 11  ? 0.4136 0.2446 0.2610 0.0119  0.0118  0.0001  8   VAL   B CA    
1421 C  C     . VAL   B 11  ? 0.4122 0.2486 0.2625 0.0112  0.0117  0.0037  8   VAL   B C     
1422 O  O     . VAL   B 11  ? 0.4129 0.2482 0.2665 0.0107  0.0109  0.0068  8   VAL   B O     
1423 C  CB    . VAL   B 11  ? 0.4174 0.2435 0.2646 0.0137  0.0126  -0.0014 8   VAL   B CB    
1424 C  CG1   . VAL   B 11  ? 0.4171 0.2459 0.2637 0.0153  0.0140  -0.0014 8   VAL   B CG1   
1425 C  CG2   . VAL   B 11  ? 0.4217 0.2446 0.2661 0.0135  0.0125  -0.0049 8   VAL   B CG2   
1426 N  N     . VAL   B 12  ? 0.4069 0.2496 0.2567 0.0110  0.0125  0.0032  9   VAL   B N     
1427 C  CA    . VAL   B 12  ? 0.4048 0.2561 0.2566 0.0097  0.0124  0.0062  9   VAL   B CA    
1428 C  C     . VAL   B 12  ? 0.4018 0.2565 0.2532 0.0105  0.0137  0.0053  9   VAL   B C     
1429 O  O     . VAL   B 12  ? 0.4020 0.2528 0.2517 0.0117  0.0145  0.0023  9   VAL   B O     
1430 C  CB    . VAL   B 12  ? 0.4020 0.2610 0.2540 0.0075  0.0122  0.0053  9   VAL   B CB    
1431 C  CG1   . VAL   B 12  ? 0.4046 0.2609 0.2571 0.0064  0.0108  0.0066  9   VAL   B CG1   
1432 C  CG2   . VAL   B 12  ? 0.3998 0.2604 0.2509 0.0080  0.0133  0.0002  9   VAL   B CG2   
1433 N  N     . GLY   B 13  ? 0.3993 0.2625 0.2525 0.0093  0.0136  0.0085  10  GLY   B N     
1434 C  CA    . GLY   B 13  ? 0.3979 0.2657 0.2511 0.0096  0.0145  0.0084  10  GLY   B CA    
1435 C  C     . GLY   B 13  ? 0.3986 0.2727 0.2551 0.0092  0.0138  0.0146  10  GLY   B C     
1436 O  O     . GLY   B 13  ? 0.4010 0.2725 0.2605 0.0094  0.0126  0.0191  10  GLY   B O     
1437 N  N     . ALA   B 14  ? 0.3970 0.2791 0.2536 0.0086  0.0144  0.0152  11  ALA   B N     
1438 C  CA    . ALA   B 14  ? 0.3962 0.2870 0.2564 0.0081  0.0136  0.0218  11  ALA   B CA    
1439 C  C     . ALA   B 14  ? 0.3973 0.2794 0.2617 0.0116  0.0133  0.0257  11  ALA   B C     
1440 O  O     . ALA   B 14  ? 0.3965 0.2684 0.2597 0.0142  0.0142  0.0219  11  ALA   B O     
1441 C  CB    . ALA   B 14  ? 0.3945 0.2959 0.2535 0.0065  0.0145  0.0203  11  ALA   B CB    
1442 N  N     . GLY   B 15  ? 0.3987 0.2862 0.2688 0.0116  0.0119  0.0335  12  GLY   B N     
1443 C  CA    . GLY   B 15  ? 0.4029 0.2829 0.2794 0.0153  0.0117  0.0370  12  GLY   B CA    
1444 C  C     . GLY   B 15  ? 0.4013 0.2801 0.2768 0.0180  0.0134  0.0338  12  GLY   B C     
1445 O  O     . GLY   B 15  ? 0.3975 0.2861 0.2706 0.0165  0.0139  0.0338  12  GLY   B O     
1446 N  N     . GLY   B 16  ? 0.4057 0.2731 0.2827 0.0216  0.0144  0.0305  13  GLY   B N     
1447 C  CA    . GLY   B 16  ? 0.4058 0.2728 0.2832 0.0245  0.0160  0.0282  13  GLY   B CA    
1448 C  C     . GLY   B 16  ? 0.4027 0.2677 0.2723 0.0238  0.0176  0.0211  13  GLY   B C     
1449 O  O     . GLY   B 16  ? 0.4057 0.2720 0.2750 0.0255  0.0190  0.0194  13  GLY   B O     
1450 N  N     . VAL   B 17  ? 0.4019 0.2641 0.2662 0.0213  0.0174  0.0175  14  VAL   B N     
1451 C  CA    . VAL   B 17  ? 0.4005 0.2612 0.2590 0.0203  0.0185  0.0122  14  VAL   B CA    
1452 C  C     . VAL   B 17  ? 0.4051 0.2573 0.2620 0.0225  0.0194  0.0083  14  VAL   B C     
1453 O  O     . VAL   B 17  ? 0.4069 0.2593 0.2604 0.0222  0.0203  0.0055  14  VAL   B O     
1454 C  CB    . VAL   B 17  ? 0.3960 0.2581 0.2510 0.0171  0.0179  0.0099  14  VAL   B CB    
1455 C  CG1   . VAL   B 17  ? 0.3935 0.2666 0.2493 0.0144  0.0174  0.0120  14  VAL   B CG1   
1456 C  CG2   . VAL   B 17  ? 0.3969 0.2527 0.2514 0.0169  0.0169  0.0091  14  VAL   B CG2   
1457 N  N     . GLY   B 18  ? 0.4099 0.2557 0.2696 0.0242  0.0190  0.0080  15  GLY   B N     
1458 C  CA    . GLY   B 18  ? 0.4142 0.2538 0.2727 0.0260  0.0200  0.0034  15  GLY   B CA    
1459 C  C     . GLY   B 18  ? 0.4160 0.2495 0.2721 0.0245  0.0190  0.0008  15  GLY   B C     
1460 O  O     . GLY   B 18  ? 0.4216 0.2525 0.2746 0.0247  0.0197  -0.0035 15  GLY   B O     
1461 N  N     . LYS   B 19  ? 0.4136 0.2463 0.2711 0.0228  0.0175  0.0035  16  LYS   B N     
1462 C  CA    . LYS   B 19  ? 0.4164 0.2445 0.2719 0.0211  0.0164  0.0015  16  LYS   B CA    
1463 C  C     . LYS   B 19  ? 0.4233 0.2449 0.2811 0.0226  0.0168  -0.0023 16  LYS   B C     
1464 O  O     . LYS   B 19  ? 0.4254 0.2450 0.2792 0.0218  0.0170  -0.0066 16  LYS   B O     
1465 C  CB    . LYS   B 19  ? 0.4165 0.2463 0.2743 0.0190  0.0148  0.0056  16  LYS   B CB    
1466 C  CG    . LYS   B 19  ? 0.4110 0.2490 0.2669 0.0172  0.0146  0.0077  16  LYS   B CG    
1467 C  CD    . LYS   B 19  ? 0.4111 0.2537 0.2692 0.0147  0.0131  0.0117  16  LYS   B CD    
1468 C  CE    . LYS   B 19  ? 0.4136 0.2585 0.2781 0.0150  0.0122  0.0179  16  LYS   B CE    
1469 N  NZ    . LYS   B 19  ? 0.4125 0.2647 0.2785 0.0158  0.0128  0.0207  16  LYS   B NZ    
1470 N  N     . SER   B 20  ? 0.4279 0.2468 0.2928 0.0246  0.0168  -0.0006 17  SER   B N     
1471 C  CA    . SER   B 20  ? 0.4352 0.2472 0.3049 0.0263  0.0173  -0.0049 17  SER   B CA    
1472 C  C     . SER   B 20  ? 0.4386 0.2521 0.3049 0.0280  0.0195  -0.0116 17  SER   B C     
1473 O  O     . SER   B 20  ? 0.4456 0.2564 0.3098 0.0273  0.0199  -0.0176 17  SER   B O     
1474 C  CB    . SER   B 20  ? 0.4365 0.2457 0.3169 0.0287  0.0169  -0.0010 17  SER   B CB    
1475 O  OG    . SER   B 20  ? 0.4367 0.2440 0.3213 0.0263  0.0145  0.0048  17  SER   B OG    
1476 N  N     . ALA   B 21  ? 0.4370 0.2561 0.3027 0.0299  0.0209  -0.0103 18  ALA   B N     
1477 C  CA    . ALA   B 21  ? 0.4392 0.2622 0.3023 0.0316  0.0231  -0.0155 18  ALA   B CA    
1478 C  C     . ALA   B 21  ? 0.4411 0.2668 0.2954 0.0287  0.0231  -0.0185 18  ALA   B C     
1479 O  O     . ALA   B 21  ? 0.4441 0.2725 0.2962 0.0290  0.0246  -0.0241 18  ALA   B O     
1480 C  CB    . ALA   B 21  ? 0.4344 0.2639 0.2982 0.0333  0.0242  -0.0122 18  ALA   B CB    
1481 N  N     . LEU   B 22  ? 0.4395 0.2656 0.2896 0.0258  0.0214  -0.0147 19  LEU   B N     
1482 C  CA    . LEU   B 22  ? 0.4417 0.2707 0.2851 0.0232  0.0209  -0.0157 19  LEU   B CA    
1483 C  C     . LEU   B 22  ? 0.4481 0.2738 0.2903 0.0216  0.0200  -0.0194 19  LEU   B C     
1484 O  O     . LEU   B 22  ? 0.4499 0.2794 0.2879 0.0203  0.0204  -0.0227 19  LEU   B O     
1485 C  CB    . LEU   B 22  ? 0.4364 0.2666 0.2781 0.0214  0.0196  -0.0108 19  LEU   B CB    
1486 C  CG    . LEU   B 22  ? 0.4344 0.2695 0.2757 0.0216  0.0203  -0.0081 19  LEU   B CG    
1487 C  CD1   . LEU   B 22  ? 0.4315 0.2670 0.2731 0.0199  0.0191  -0.0050 19  LEU   B CD1   
1488 C  CD2   . LEU   B 22  ? 0.4352 0.2751 0.2727 0.0207  0.0210  -0.0090 19  LEU   B CD2   
1489 N  N     . THR   B 23  ? 0.4525 0.2724 0.2986 0.0212  0.0188  -0.0185 20  THR   B N     
1490 C  CA    . THR   B 23  ? 0.4601 0.2764 0.3061 0.0193  0.0178  -0.0221 20  THR   B CA    
1491 C  C     . THR   B 23  ? 0.4674 0.2829 0.3153 0.0205  0.0194  -0.0295 20  THR   B C     
1492 O  O     . THR   B 23  ? 0.4738 0.2920 0.3181 0.0185  0.0195  -0.0344 20  THR   B O     
1493 C  CB    . THR   B 23  ? 0.4606 0.2712 0.3116 0.0185  0.0161  -0.0188 20  THR   B CB    
1494 O  OG1   . THR   B 23  ? 0.4590 0.2725 0.3085 0.0176  0.0151  -0.0129 20  THR   B OG1   
1495 C  CG2   . THR   B 23  ? 0.4669 0.2745 0.3174 0.0156  0.0147  -0.0219 20  THR   B CG2   
1496 N  N     . ILE   B 24  ? 0.4707 0.2840 0.3249 0.0239  0.0209  -0.0304 21  ILE   B N     
1497 C  CA    . ILE   B 24  ? 0.4801 0.2925 0.3382 0.0257  0.0228  -0.0386 21  ILE   B CA    
1498 C  C     . ILE   B 24  ? 0.4823 0.3046 0.3336 0.0254  0.0247  -0.0432 21  ILE   B C     
1499 O  O     . ILE   B 24  ? 0.4962 0.3209 0.3468 0.0246  0.0259  -0.0513 21  ILE   B O     
1500 C  CB    . ILE   B 24  ? 0.4806 0.2884 0.3489 0.0300  0.0238  -0.0377 21  ILE   B CB    
1501 C  CG1   . ILE   B 24  ? 0.4808 0.2795 0.3571 0.0295  0.0216  -0.0335 21  ILE   B CG1   
1502 C  CG2   . ILE   B 24  ? 0.4886 0.2976 0.3614 0.0328  0.0265  -0.0470 21  ILE   B CG2   
1503 C  CD1   . ILE   B 24  ? 0.4819 0.2775 0.3688 0.0332  0.0217  -0.0286 21  ILE   B CD1   
1504 N  N     . GLN   B 25  ? 0.4767 0.3055 0.3236 0.0256  0.0251  -0.0381 22  GLN   B N     
1505 C  CA    . GLN   B 25  ? 0.4760 0.3154 0.3166 0.0245  0.0265  -0.0407 22  GLN   B CA    
1506 C  C     . GLN   B 25  ? 0.4761 0.3193 0.3104 0.0204  0.0251  -0.0425 22  GLN   B C     
1507 O  O     . GLN   B 25  ? 0.4821 0.3327 0.3136 0.0192  0.0264  -0.0492 22  GLN   B O     
1508 C  CB    . GLN   B 25  ? 0.4691 0.3142 0.3066 0.0245  0.0265  -0.0339 22  GLN   B CB    
1509 C  CG    . GLN   B 25  ? 0.4698 0.3198 0.3103 0.0276  0.0289  -0.0351 22  GLN   B CG    
1510 C  CD    . GLN   B 25  ? 0.4730 0.3337 0.3108 0.0275  0.0312  -0.0416 22  GLN   B CD    
1511 O  OE1   . GLN   B 25  ? 0.4746 0.3391 0.3089 0.0253  0.0314  -0.0470 22  GLN   B OE1   
1512 N  NE2   . GLN   B 25  ? 0.4736 0.3407 0.3131 0.0298  0.0332  -0.0413 22  GLN   B NE2   
1513 N  N     . LEU   B 26  ? 0.4718 0.3115 0.3042 0.0183  0.0227  -0.0367 23  LEU   B N     
1514 C  CA    . LEU   B 26  ? 0.4713 0.3154 0.2984 0.0145  0.0210  -0.0366 23  LEU   B CA    
1515 C  C     . LEU   B 26  ? 0.4845 0.3281 0.3121 0.0130  0.0213  -0.0450 23  LEU   B C     
1516 O  O     . LEU   B 26  ? 0.4890 0.3418 0.3117 0.0102  0.0213  -0.0484 23  LEU   B O     
1517 C  CB    . LEU   B 26  ? 0.4648 0.3037 0.2923 0.0134  0.0186  -0.0301 23  LEU   B CB    
1518 C  CG    . LEU   B 26  ? 0.4651 0.3091 0.2883 0.0099  0.0166  -0.0286 23  LEU   B CG    
1519 C  CD1   . LEU   B 26  ? 0.4643 0.3175 0.2838 0.0088  0.0164  -0.0238 23  LEU   B CD1   
1520 C  CD2   . LEU   B 26  ? 0.4611 0.2991 0.2863 0.0091  0.0145  -0.0246 23  LEU   B CD2   
1521 N  N     . ILE   B 27  ? 0.4930 0.3265 0.3273 0.0146  0.0214  -0.0480 24  ILE   B N     
1522 C  CA    . ILE   B 27  ? 0.5043 0.3347 0.3408 0.0127  0.0211  -0.0557 24  ILE   B CA    
1523 C  C     . ILE   B 27  ? 0.5170 0.3511 0.3560 0.0142  0.0240  -0.0661 24  ILE   B C     
1524 O  O     . ILE   B 27  ? 0.5249 0.3664 0.3602 0.0113  0.0246  -0.0736 24  ILE   B O     
1525 C  CB    . ILE   B 27  ? 0.5037 0.3215 0.3477 0.0131  0.0196  -0.0535 24  ILE   B CB    
1526 C  CG1   . ILE   B 27  ? 0.4965 0.3131 0.3378 0.0114  0.0170  -0.0444 24  ILE   B CG1   
1527 C  CG2   . ILE   B 27  ? 0.5137 0.3272 0.3617 0.0109  0.0194  -0.0620 24  ILE   B CG2   
1528 C  CD1   . ILE   B 27  ? 0.4958 0.3172 0.3316 0.0071  0.0152  -0.0447 24  ILE   B CD1   
1529 N  N     . GLN   B 28  ? 0.5230 0.3531 0.3685 0.0187  0.0259  -0.0667 25  GLN   B N     
1530 C  CA    . GLN   B 28  ? 0.5353 0.3668 0.3863 0.0212  0.0289  -0.0773 25  GLN   B CA    
1531 C  C     . GLN   B 28  ? 0.5349 0.3794 0.3817 0.0228  0.0315  -0.0789 25  GLN   B C     
1532 O  O     . GLN   B 28  ? 0.5407 0.3892 0.3916 0.0251  0.0344  -0.0882 25  GLN   B O     
1533 C  CB    . GLN   B 28  ? 0.5363 0.3554 0.3998 0.0257  0.0294  -0.0769 25  GLN   B CB    
1534 C  CG    . GLN   B 28  ? 0.5390 0.3456 0.4087 0.0241  0.0267  -0.0745 25  GLN   B CG    
1535 C  CD    . GLN   B 28  ? 0.5456 0.3412 0.4294 0.0284  0.0272  -0.0747 25  GLN   B CD    
1536 O  OE1   . GLN   B 28  ? 0.5489 0.3464 0.4378 0.0329  0.0295  -0.0760 25  GLN   B OE1   
1537 N  NE2   . GLN   B 28  ? 0.5466 0.3313 0.4378 0.0269  0.0250  -0.0728 25  GLN   B NE2   
1538 N  N     . ASN   B 29  ? 0.5297 0.3805 0.3694 0.0217  0.0306  -0.0698 26  ASN   B N     
1539 C  CA    . ASN   B 29  ? 0.5285 0.3929 0.3635 0.0221  0.0326  -0.0698 26  ASN   B CA    
1540 C  C     . ASN   B 29  ? 0.5273 0.3910 0.3698 0.0273  0.0354  -0.0726 26  ASN   B C     
1541 O  O     . ASN   B 29  ? 0.5334 0.4081 0.3753 0.0283  0.0382  -0.0792 26  ASN   B O     
1542 C  CB    . ASN   B 29  ? 0.5381 0.4166 0.3667 0.0184  0.0336  -0.0775 26  ASN   B CB    
1543 C  CG    . ASN   B 29  ? 0.5417 0.4366 0.3645 0.0174  0.0350  -0.0750 26  ASN   B CG    
1544 O  OD1   . ASN   B 29  ? 0.5468 0.4425 0.3671 0.0172  0.0337  -0.0647 26  ASN   B OD1   
1545 N  ND2   . ASN   B 29  ? 0.5549 0.4634 0.3760 0.0167  0.0378  -0.0846 26  ASN   B ND2   
1546 N  N     . HIS   B 30  ? 0.5211 0.3733 0.3708 0.0306  0.0346  -0.0673 27  HIS   B N     
1547 C  CA    . HIS   B 30  ? 0.5158 0.3689 0.3725 0.0356  0.0368  -0.0670 27  HIS   B CA    
1548 C  C     . HIS   B 30  ? 0.5074 0.3522 0.3678 0.0372  0.0348  -0.0565 27  HIS   B C     
1549 O  O     . HIS   B 30  ? 0.5105 0.3476 0.3702 0.0351  0.0322  -0.0514 27  HIS   B O     
1550 C  CB    . HIS   B 30  ? 0.5249 0.3735 0.3924 0.0396  0.0391  -0.0773 27  HIS   B CB    
1551 C  CG    . HIS   B 30  ? 0.5255 0.3586 0.4021 0.0405  0.0372  -0.0764 27  HIS   B CG    
1552 N  ND1   . HIS   B 30  ? 0.5292 0.3538 0.4182 0.0453  0.0373  -0.0736 27  HIS   B ND1   
1553 C  CD2   . HIS   B 30  ? 0.5292 0.3546 0.4048 0.0370  0.0349  -0.0773 27  HIS   B CD2   
1554 C  CE1   . HIS   B 30  ? 0.5327 0.3449 0.4281 0.0445  0.0351  -0.0724 27  HIS   B CE1   
1555 N  NE2   . HIS   B 30  ? 0.5321 0.3445 0.4193 0.0394  0.0337  -0.0749 27  HIS   B NE2   
1556 N  N     . PHE   B 31  ? 0.5051 0.3532 0.3701 0.0408  0.0363  -0.0539 28  PHE   B N     
1557 C  CA    . PHE   B 31  ? 0.4988 0.3433 0.3663 0.0418  0.0347  -0.0440 28  PHE   B CA    
1558 C  C     . PHE   B 31  ? 0.5090 0.3452 0.3892 0.0461  0.0347  -0.0433 28  PHE   B C     
1559 O  O     . PHE   B 31  ? 0.5182 0.3564 0.4064 0.0504  0.0370  -0.0483 28  PHE   B O     
1560 C  CB    . PHE   B 31  ? 0.4902 0.3453 0.3543 0.0421  0.0358  -0.0401 28  PHE   B CB    
1561 C  CG    . PHE   B 31  ? 0.4812 0.3346 0.3482 0.0428  0.0344  -0.0310 28  PHE   B CG    
1562 C  CD1   . PHE   B 31  ? 0.4765 0.3245 0.3405 0.0398  0.0316  -0.0248 28  PHE   B CD1   
1563 C  CD2   . PHE   B 31  ? 0.4786 0.3371 0.3514 0.0463  0.0358  -0.0290 28  PHE   B CD2   
1564 C  CE1   . PHE   B 31  ? 0.4702 0.3188 0.3365 0.0399  0.0304  -0.0174 28  PHE   B CE1   
1565 C  CE2   . PHE   B 31  ? 0.4737 0.3326 0.3489 0.0463  0.0343  -0.0207 28  PHE   B CE2   
1566 C  CZ    . PHE   B 31  ? 0.4668 0.3211 0.3382 0.0429  0.0317  -0.0152 28  PHE   B CZ    
1567 N  N     . VAL   B 32  ? 0.5145 0.3429 0.3977 0.0452  0.0320  -0.0361 29  VAL   B N     
1568 C  CA    . VAL   B 32  ? 0.5239 0.3452 0.4201 0.0488  0.0313  -0.0327 29  VAL   B CA    
1569 C  C     . VAL   B 32  ? 0.5281 0.3552 0.4265 0.0504  0.0308  -0.0237 29  VAL   B C     
1570 O  O     . VAL   B 32  ? 0.5274 0.3564 0.4196 0.0471  0.0289  -0.0168 29  VAL   B O     
1571 C  CB    . VAL   B 32  ? 0.5241 0.3352 0.4232 0.0464  0.0285  -0.0298 29  VAL   B CB    
1572 C  CG1   . VAL   B 32  ? 0.5319 0.3375 0.4308 0.0449  0.0289  -0.0392 29  VAL   B CG1   
1573 C  CG2   . VAL   B 32  ? 0.5204 0.3336 0.4101 0.0419  0.0262  -0.0227 29  VAL   B CG2   
1574 N  N     . ASP   B 33  ? 0.5373 0.3675 0.4447 0.0552  0.0327  -0.0247 30  ASP   B N     
1575 C  CA    . ASP   B 33  ? 0.5357 0.3736 0.4475 0.0577  0.0329  -0.0175 30  ASP   B CA    
1576 C  C     . ASP   B 33  ? 0.5336 0.3682 0.4526 0.0576  0.0300  -0.0071 30  ASP   B C     
1577 O  O     . ASP   B 33  ? 0.5298 0.3720 0.4502 0.0581  0.0294  0.0001  30  ASP   B O     
1578 C  CB    . ASP   B 33  ? 0.5476 0.3881 0.4703 0.0638  0.0357  -0.0225 30  ASP   B CB    
1579 C  CG    . ASP   B 33  ? 0.5489 0.4018 0.4709 0.0654  0.0370  -0.0187 30  ASP   B CG    
1580 O  OD1   . ASP   B 33  ? 0.5477 0.4070 0.4584 0.0612  0.0363  -0.0152 30  ASP   B OD1   
1581 O  OD2   . ASP   B 33  ? 0.5584 0.4142 0.4917 0.0708  0.0387  -0.0198 30  ASP   B OD2   
1582 N  N     . GLU   B 34  ? 0.5339 0.3584 0.4584 0.0570  0.0283  -0.0067 31  GLU   B N     
1583 C  CA    . GLU   B 34  ? 0.5279 0.3499 0.4599 0.0562  0.0252  0.0037  31  GLU   B CA    
1584 C  C     . GLU   B 34  ? 0.5278 0.3385 0.4612 0.0539  0.0237  0.0011  31  GLU   B C     
1585 O  O     . GLU   B 34  ? 0.5412 0.3449 0.4801 0.0562  0.0252  -0.0072 31  GLU   B O     
1586 C  CB    . GLU   B 34  ? 0.5340 0.3551 0.4830 0.0620  0.0255  0.0071  31  GLU   B CB    
1587 C  CG    . GLU   B 34  ? 0.9242 0.7449 0.8837 0.0618  0.0223  0.0197  31  GLU   B CG    
1588 C  CD    . GLU   B 34  ? 0.9310 0.7512 0.9088 0.0681  0.0227  0.0232  31  GLU   B CD    
1589 O  OE1   . GLU   B 34  ? 0.9348 0.7547 0.9167 0.0728  0.0258  0.0145  31  GLU   B OE1   
1590 O  OE2   . GLU   B 34  ? 0.9324 0.7542 0.9208 0.0684  0.0199  0.0349  31  GLU   B OE2   
1591 N  N     . TYR   B 35  ? 0.5143 0.3244 0.4452 0.0498  0.0209  0.0083  32  TYR   B N     
1592 C  CA    . TYR   B 35  ? 0.5102 0.3107 0.4421 0.0469  0.0193  0.0065  32  TYR   B CA    
1593 C  C     . TYR   B 35  ? 0.5080 0.3103 0.4435 0.0439  0.0160  0.0183  32  TYR   B C     
1594 O  O     . TYR   B 35  ? 0.5015 0.3141 0.4308 0.0422  0.0154  0.0243  32  TYR   B O     
1595 C  CB    . TYR   B 35  ? 0.5036 0.3049 0.4205 0.0431  0.0200  -0.0004 32  TYR   B CB    
1596 C  CG    . TYR   B 35  ? 0.5057 0.2981 0.4229 0.0404  0.0189  -0.0046 32  TYR   B CG    
1597 C  CD1   . TYR   B 35  ? 0.5148 0.3000 0.4365 0.0421  0.0204  -0.0145 32  TYR   B CD1   
1598 C  CD2   . TYR   B 35  ? 0.4994 0.2914 0.4130 0.0360  0.0163  0.0009  32  TYR   B CD2   
1599 C  CE1   . TYR   B 35  ? 0.5166 0.2941 0.4389 0.0390  0.0192  -0.0186 32  TYR   B CE1   
1600 C  CE2   . TYR   B 35  ? 0.5068 0.2913 0.4213 0.0332  0.0151  -0.0024 32  TYR   B CE2   
1601 C  CZ    . TYR   B 35  ? 0.5143 0.2913 0.4330 0.0345  0.0165  -0.0121 32  TYR   B CZ    
1602 O  OH    . TYR   B 35  ? 0.5193 0.2897 0.4387 0.0311  0.0151  -0.0153 32  TYR   B OH    
1603 N  N     . ASP   B 36  ? 0.5116 0.3052 0.4569 0.0430  0.0139  0.0210  33  ASP   B N     
1604 C  CA    . ASP   B 36  ? 0.5073 0.3034 0.4576 0.0398  0.0106  0.0331  33  ASP   B CA    
1605 C  C     . ASP   B 36  ? 0.4995 0.3043 0.4354 0.0345  0.0097  0.0351  33  ASP   B C     
1606 O  O     . ASP   B 36  ? 0.5008 0.3015 0.4287 0.0317  0.0099  0.0289  33  ASP   B O     
1607 C  CB    . ASP   B 36  ? 0.5172 0.3014 0.4792 0.0388  0.0086  0.0340  33  ASP   B CB    
1608 C  CG    . ASP   B 36  ? 0.5184 0.3065 0.4882 0.0356  0.0049  0.0482  33  ASP   B CG    
1609 O  OD1   . ASP   B 36  ? 0.5107 0.3115 0.4720 0.0324  0.0040  0.0549  33  ASP   B OD1   
1610 O  OD2   . ASP   B 36  ? 0.5318 0.3109 0.5168 0.0361  0.0030  0.0523  33  ASP   B OD2   
1611 N  N     . PRO   B 37  ? 0.4908 0.3083 0.4238 0.0330  0.0088  0.0435  34  PRO   B N     
1612 C  CA    . PRO   B 37  ? 0.4804 0.3071 0.4008 0.0283  0.0084  0.0441  34  PRO   B CA    
1613 C  C     . PRO   B 37  ? 0.4809 0.3086 0.4008 0.0235  0.0060  0.0487  34  PRO   B C     
1614 O  O     . PRO   B 37  ? 0.4758 0.3102 0.3853 0.0200  0.0061  0.0470  34  PRO   B O     
1615 C  CB    . PRO   B 37  ? 0.4750 0.3162 0.3948 0.0280  0.0081  0.0513  34  PRO   B CB    
1616 C  CG    . PRO   B 37  ? 0.4806 0.3204 0.4122 0.0329  0.0084  0.0548  34  PRO   B CG    
1617 C  CD    . PRO   B 37  ? 0.4892 0.3141 0.4316 0.0356  0.0081  0.0523  34  PRO   B CD    
1618 N  N     . THR   B 38  ? 0.4854 0.3066 0.4169 0.0231  0.0038  0.0543  35  THR   B N     
1619 C  CA    . THR   B 38  ? 0.4829 0.3063 0.4149 0.0180  0.0013  0.0601  35  THR   B CA    
1620 C  C     . THR   B 38  ? 0.4855 0.2965 0.4162 0.0167  0.0013  0.0524  35  THR   B C     
1621 O  O     . THR   B 38  ? 0.4859 0.2986 0.4157 0.0123  -0.0006 0.0559  35  THR   B O     
1622 C  CB    . THR   B 38  ? 0.4894 0.3162 0.4357 0.0171  -0.0017 0.0736  35  THR   B CB    
1623 O  OG1   . THR   B 38  ? 0.4991 0.3119 0.4591 0.0212  -0.0019 0.0728  35  THR   B OG1   
1624 C  CG2   . THR   B 38  ? 0.4834 0.3262 0.4299 0.0171  -0.0022 0.0822  35  THR   B CG2   
1625 N  N     . ILE   B 39  ? 0.4873 0.2873 0.4176 0.0202  0.0034  0.0421  36  ILE   B N     
1626 C  CA    . ILE   B 39  ? 0.4912 0.2810 0.4199 0.0184  0.0034  0.0342  36  ILE   B CA    
1627 C  C     . ILE   B 39  ? 0.4823 0.2776 0.3959 0.0158  0.0043  0.0287  36  ILE   B C     
1628 O  O     . ILE   B 39  ? 0.4805 0.2794 0.3854 0.0177  0.0065  0.0232  36  ILE   B O     
1629 C  CB    . ILE   B 39  ? 0.4975 0.2758 0.4311 0.0224  0.0054  0.0242  36  ILE   B CB    
1630 C  CG1   . ILE   B 39  ? 0.5070 0.2781 0.4583 0.0255  0.0044  0.0288  36  ILE   B CG1   
1631 C  CG2   . ILE   B 39  ? 0.5012 0.2722 0.4307 0.0196  0.0054  0.0152  36  ILE   B CG2   
1632 C  CD1   . ILE   B 39  ? 0.5145 0.2764 0.4717 0.0302  0.0070  0.0180  36  ILE   B CD1   
1633 N  N     . GLU   B 40  ? 0.4822 0.2779 0.3943 0.0113  0.0025  0.0305  37  GLU   B N     
1634 C  CA    . GLU   B 40  ? 0.4790 0.2788 0.3795 0.0088  0.0030  0.0257  37  GLU   B CA    
1635 C  C     . GLU   B 40  ? 0.4861 0.2761 0.3874 0.0072  0.0026  0.0188  37  GLU   B C     
1636 O  O     . GLU   B 40  ? 0.4956 0.2806 0.4049 0.0046  0.0005  0.0221  37  GLU   B O     
1637 C  CB    . GLU   B 40  ? 0.4728 0.2834 0.3715 0.0048  0.0012  0.0336  37  GLU   B CB    
1638 C  CG    . GLU   B 40  ? 0.4694 0.2850 0.3582 0.0023  0.0016  0.0294  37  GLU   B CG    
1639 C  CD    . GLU   B 40  ? 0.4630 0.2925 0.3495 -0.0006 0.0008  0.0357  37  GLU   B CD    
1640 O  OE1   . GLU   B 40  ? 0.4676 0.3004 0.3563 -0.0045 -0.0011 0.0398  37  GLU   B OE1   
1641 O  OE2   . GLU   B 40  ? 0.4542 0.2920 0.3373 0.0008  0.0020  0.0363  37  GLU   B OE2   
1642 N  N     . ASP   B 41  ? 0.4844 0.2727 0.3778 0.0085  0.0045  0.0096  38  ASP   B N     
1643 C  CA    . ASP   B 41  ? 0.4890 0.2698 0.3827 0.0072  0.0045  0.0016  38  ASP   B CA    
1644 C  C     . ASP   B 41  ? 0.4818 0.2675 0.3636 0.0065  0.0057  -0.0047 38  ASP   B C     
1645 O  O     . ASP   B 41  ? 0.4750 0.2671 0.3502 0.0084  0.0070  -0.0042 38  ASP   B O     
1646 C  CB    . ASP   B 41  ? 0.4995 0.2718 0.4010 0.0106  0.0059  -0.0041 38  ASP   B CB    
1647 C  CG    . ASP   B 41  ? 0.5144 0.2765 0.4250 0.0086  0.0048  -0.0083 38  ASP   B CG    
1648 O  OD1   . ASP   B 41  ? 0.5155 0.2773 0.4235 0.0040  0.0031  -0.0092 38  ASP   B OD1   
1649 O  OD2   . ASP   B 41  ? 0.5229 0.2774 0.4440 0.0116  0.0055  -0.0110 38  ASP   B OD2   
1650 N  N     . SER   B 42  ? 0.4835 0.2664 0.3635 0.0037  0.0050  -0.0102 39  SER   B N     
1651 C  CA    . SER   B 42  ? 0.4797 0.2680 0.3497 0.0024  0.0056  -0.0150 39  SER   B CA    
1652 C  C     . SER   B 42  ? 0.4844 0.2705 0.3529 0.0033  0.0072  -0.0247 39  SER   B C     
1653 O  O     . SER   B 42  ? 0.4936 0.2724 0.3693 0.0036  0.0075  -0.0293 39  SER   B O     
1654 C  CB    . SER   B 42  ? 0.4799 0.2708 0.3482 -0.0020 0.0034  -0.0133 39  SER   B CB    
1655 O  OG    . SER   B 42  ? 0.4895 0.2734 0.3638 -0.0050 0.0022  -0.0167 39  SER   B OG    
1656 N  N     . TYR   B 43  ? 0.4771 0.2702 0.3367 0.0035  0.0081  -0.0274 40  TYR   B N     
1657 C  CA    . TYR   B 43  ? 0.4798 0.2754 0.3355 0.0035  0.0097  -0.0360 40  TYR   B CA    
1658 C  C     . TYR   B 43  ? 0.4751 0.2787 0.3227 0.0002  0.0086  -0.0367 40  TYR   B C     
1659 O  O     . TYR   B 43  ? 0.4627 0.2707 0.3069 0.0003  0.0078  -0.0306 40  TYR   B O     
1660 C  CB    . TYR   B 43  ? 0.4786 0.2772 0.3322 0.0075  0.0120  -0.0364 40  TYR   B CB    
1661 C  CG    . TYR   B 43  ? 0.4837 0.2762 0.3457 0.0111  0.0131  -0.0357 40  TYR   B CG    
1662 C  CD1   . TYR   B 43  ? 0.4816 0.2731 0.3467 0.0128  0.0125  -0.0274 40  TYR   B CD1   
1663 C  CD2   . TYR   B 43  ? 0.4955 0.2843 0.3627 0.0130  0.0148  -0.0434 40  TYR   B CD2   
1664 C  CE1   . TYR   B 43  ? 0.4872 0.2746 0.3604 0.0161  0.0133  -0.0255 40  TYR   B CE1   
1665 C  CE2   . TYR   B 43  ? 0.5012 0.2848 0.3774 0.0169  0.0159  -0.0422 40  TYR   B CE2   
1666 C  CZ    . TYR   B 43  ? 0.4970 0.2799 0.3763 0.0184  0.0149  -0.0326 40  TYR   B CZ    
1667 O  OH    . TYR   B 43  ? 0.5032 0.2825 0.3919 0.0222  0.0156  -0.0301 40  TYR   B OH    
1668 N  N     . ARG   B 44  ? 0.4835 0.2894 0.3290 -0.0026 0.0086  -0.0442 41  ARG   B N     
1669 C  CA    . ARG   B 44  ? 0.4834 0.2986 0.3220 -0.0062 0.0072  -0.0443 41  ARG   B CA    
1670 C  C     . ARG   B 44  ? 0.4881 0.3120 0.3210 -0.0065 0.0088  -0.0506 41  ARG   B C     
1671 O  O     . ARG   B 44  ? 0.4964 0.3182 0.3319 -0.0065 0.0102  -0.0586 41  ARG   B O     
1672 C  CB    . ARG   B 44  ? 0.4890 0.3019 0.3301 -0.0108 0.0051  -0.0466 41  ARG   B CB    
1673 C  CG    . ARG   B 44  ? 0.4863 0.2977 0.3294 -0.0120 0.0030  -0.0384 41  ARG   B CG    
1674 C  CD    . ARG   B 44  ? 0.4949 0.3039 0.3415 -0.0169 0.0008  -0.0399 41  ARG   B CD    
1675 N  NE    . ARG   B 44  ? 0.5075 0.3059 0.3623 -0.0172 0.0012  -0.0446 41  ARG   B NE    
1676 C  CZ    . ARG   B 44  ? 0.5097 0.2998 0.3716 -0.0144 0.0015  -0.0404 41  ARG   B CZ    
1677 N  NH1   . ARG   B 44  ? 0.5194 0.2998 0.3904 -0.0145 0.0018  -0.0448 41  ARG   B NH1   
1678 N  NH2   . ARG   B 44  ? 0.5055 0.2979 0.3664 -0.0118 0.0015  -0.0318 41  ARG   B NH2   
1679 N  N     . LYS   B 45  ? 0.4866 0.3208 0.3130 -0.0069 0.0084  -0.0465 42  LYS   B N     
1680 C  CA    . LYS   B 45  ? 0.4908 0.3357 0.3117 -0.0075 0.0098  -0.0507 42  LYS   B CA    
1681 C  C     . LYS   B 45  ? 0.4883 0.3453 0.3034 -0.0102 0.0079  -0.0454 42  LYS   B C     
1682 O  O     . LYS   B 45  ? 0.4831 0.3399 0.2985 -0.0083 0.0070  -0.0369 42  LYS   B O     
1683 C  CB    . LYS   B 45  ? 0.4867 0.3318 0.3074 -0.0033 0.0118  -0.0478 42  LYS   B CB    
1684 C  CG    . LYS   B 45  ? 0.4907 0.3479 0.3064 -0.0039 0.0134  -0.0516 42  LYS   B CG    
1685 C  CD    . LYS   B 45  ? 0.4857 0.3435 0.3016 -0.0002 0.0152  -0.0481 42  LYS   B CD    
1686 C  CE    . LYS   B 45  ? 0.4909 0.3611 0.3027 -0.0009 0.0172  -0.0529 42  LYS   B CE    
1687 N  NZ    . LYS   B 45  ? 0.4861 0.3595 0.2971 0.0016  0.0181  -0.0467 42  LYS   B NZ    
1688 N  N     . GLN   B 46  ? 0.4911 0.3589 0.3021 -0.0144 0.0074  -0.0507 43  GLN   B N     
1689 C  CA    . GLN   B 46  ? 0.4894 0.3714 0.2953 -0.0176 0.0055  -0.0459 43  GLN   B CA    
1690 C  C     . GLN   B 46  ? 0.4851 0.3771 0.2874 -0.0164 0.0065  -0.0421 43  GLN   B C     
1691 O  O     . GLN   B 46  ? 0.4893 0.3854 0.2898 -0.0161 0.0088  -0.0487 43  GLN   B O     
1692 C  CB    . GLN   B 46  ? 0.5011 0.3915 0.3043 -0.0231 0.0047  -0.0541 43  GLN   B CB    
1693 C  CG    . GLN   B 46  ? 0.5032 0.4105 0.3013 -0.0274 0.0023  -0.0493 43  GLN   B CG    
1694 C  CD    . GLN   B 46  ? 0.5151 0.4300 0.3109 -0.0332 0.0016  -0.0586 43  GLN   B CD    
1695 O  OE1   . GLN   B 46  ? 0.5168 0.4232 0.3160 -0.0349 0.0005  -0.0616 43  GLN   B OE1   
1696 N  NE2   . GLN   B 46  ? 0.5213 0.4531 0.3114 -0.0368 0.0022  -0.0633 43  GLN   B NE2   
1697 N  N     . VAL   B 47  ? 0.4749 0.3707 0.2773 -0.0155 0.0048  -0.0315 44  VAL   B N     
1698 C  CA    . VAL   B 47  ? 0.4711 0.3759 0.2716 -0.0147 0.0051  -0.0255 44  VAL   B CA    
1699 C  C     . VAL   B 47  ? 0.4635 0.3789 0.2640 -0.0169 0.0021  -0.0156 44  VAL   B C     
1700 O  O     . VAL   B 47  ? 0.4653 0.3780 0.2682 -0.0174 0.0000  -0.0127 44  VAL   B O     
1701 C  CB    . VAL   B 47  ? 0.4672 0.3610 0.2717 -0.0098 0.0065  -0.0216 44  VAL   B CB    
1702 C  CG1   . VAL   B 47  ? 0.4706 0.3566 0.2758 -0.0074 0.0095  -0.0299 44  VAL   B CG1   
1703 C  CG2   . VAL   B 47  ? 0.4602 0.3432 0.2698 -0.0075 0.0051  -0.0158 44  VAL   B CG2   
1704 N  N     . VAL   B 48  ? 0.4602 0.3882 0.2586 -0.0182 0.0017  -0.0100 45  VAL   B N     
1705 C  CA    . VAL   B 48  ? 0.4563 0.3953 0.2564 -0.0200 -0.0015 0.0013  45  VAL   B CA    
1706 C  C     . VAL   B 48  ? 0.4495 0.3819 0.2554 -0.0163 -0.0017 0.0104  45  VAL   B C     
1707 O  O     . VAL   B 48  ? 0.4462 0.3793 0.2512 -0.0154 0.0000  0.0104  45  VAL   B O     
1708 C  CB    . VAL   B 48  ? 0.4610 0.4219 0.2553 -0.0253 -0.0023 0.0022  45  VAL   B CB    
1709 C  CG1   . VAL   B 48  ? 0.4605 0.4335 0.2581 -0.0271 -0.0060 0.0158  45  VAL   B CG1   
1710 C  CG2   . VAL   B 48  ? 0.4661 0.4339 0.2551 -0.0294 -0.0020 -0.0085 45  VAL   B CG2   
1711 N  N     . ILE   B 49  ? 0.4448 0.3708 0.2574 -0.0142 -0.0037 0.0173  46  ILE   B N     
1712 C  CA    . ILE   B 49  ? 0.4373 0.3560 0.2574 -0.0108 -0.0041 0.0252  46  ILE   B CA    
1713 C  C     . ILE   B 49  ? 0.4366 0.3626 0.2631 -0.0115 -0.0075 0.0360  46  ILE   B C     
1714 O  O     . ILE   B 49  ? 0.4368 0.3612 0.2662 -0.0110 -0.0089 0.0364  46  ILE   B O     
1715 C  CB    . ILE   B 49  ? 0.4328 0.3342 0.2567 -0.0066 -0.0025 0.0208  46  ILE   B CB    
1716 C  CG1   . ILE   B 49  ? 0.4319 0.3262 0.2509 -0.0057 0.0005  0.0113  46  ILE   B CG1   
1717 C  CG2   . ILE   B 49  ? 0.4302 0.3249 0.2624 -0.0035 -0.0029 0.0275  46  ILE   B CG2   
1718 C  CD1   . ILE   B 49  ? 0.4280 0.3082 0.2501 -0.0026 0.0017  0.0072  46  ILE   B CD1   
1719 N  N     . ASP   B 50  ? 0.4365 0.3713 0.2661 -0.0127 -0.0090 0.0453  47  ASP   B N     
1720 C  CA    . ASP   B 50  ? 0.4349 0.3768 0.2730 -0.0130 -0.0125 0.0575  47  ASP   B CA    
1721 C  C     . ASP   B 50  ? 0.4355 0.3918 0.2703 -0.0167 -0.0148 0.0590  47  ASP   B C     
1722 O  O     . ASP   B 50  ? 0.4341 0.3914 0.2762 -0.0156 -0.0173 0.0652  47  ASP   B O     
1723 C  CB    . ASP   B 50  ? 0.4321 0.3593 0.2813 -0.0081 -0.0128 0.0598  47  ASP   B CB    
1724 C  CG    . ASP   B 50  ? 0.4294 0.3433 0.2828 -0.0049 -0.0108 0.0582  47  ASP   B CG    
1725 O  OD1   . ASP   B 50  ? 0.4328 0.3507 0.2873 -0.0062 -0.0110 0.0635  47  ASP   B OD1   
1726 O  OD2   . ASP   B 50  ? 0.4270 0.3278 0.2826 -0.0015 -0.0090 0.0517  47  ASP   B OD2   
1727 N  N     . GLY   B 51  ? 0.4385 0.4065 0.2629 -0.0210 -0.0140 0.0531  48  GLY   B N     
1728 C  CA    . GLY   B 51  ? 0.4422 0.4265 0.2625 -0.0256 -0.0162 0.0537  48  GLY   B CA    
1729 C  C     . GLY   B 51  ? 0.4410 0.4174 0.2585 -0.0253 -0.0154 0.0438  48  GLY   B C     
1730 O  O     . GLY   B 51  ? 0.4445 0.4334 0.2576 -0.0295 -0.0169 0.0420  48  GLY   B O     
1731 N  N     . GLU   B 52  ? 0.4385 0.3955 0.2585 -0.0208 -0.0133 0.0378  49  GLU   B N     
1732 C  CA    . GLU   B 52  ? 0.4398 0.3881 0.2588 -0.0204 -0.0127 0.0299  49  GLU   B CA    
1733 C  C     . GLU   B 52  ? 0.4416 0.3840 0.2530 -0.0216 -0.0097 0.0170  49  GLU   B C     
1734 O  O     . GLU   B 52  ? 0.4422 0.3748 0.2534 -0.0187 -0.0072 0.0138  49  GLU   B O     
1735 C  CB    . GLU   B 52  ? 0.4359 0.3675 0.2628 -0.0149 -0.0119 0.0310  49  GLU   B CB    
1736 C  CG    . GLU   B 52  ? 0.4364 0.3612 0.2632 -0.0148 -0.0117 0.0249  49  GLU   B CG    
1737 C  CD    . GLU   B 52  ? 0.4326 0.3464 0.2676 -0.0102 -0.0115 0.0269  49  GLU   B CD    
1738 O  OE1   . GLU   B 52  ? 0.4335 0.3380 0.2721 -0.0066 -0.0099 0.0275  49  GLU   B OE1   
1739 O  OE2   . GLU   B 52  ? 0.4374 0.3530 0.2751 -0.0105 -0.0128 0.0275  49  GLU   B OE2   
1740 N  N     . THR   B 53  ? 0.4458 0.3939 0.2522 -0.0256 -0.0100 0.0099  50  THR   B N     
1741 C  CA    . THR   B 53  ? 0.4498 0.3894 0.2519 -0.0261 -0.0072 -0.0027 50  THR   B CA    
1742 C  C     . THR   B 53  ? 0.4494 0.3716 0.2564 -0.0226 -0.0066 -0.0043 50  THR   B C     
1743 O  O     . THR   B 53  ? 0.4528 0.3759 0.2626 -0.0234 -0.0086 -0.0013 50  THR   B O     
1744 C  CB    . THR   B 53  ? 0.4539 0.4057 0.2497 -0.0321 -0.0075 -0.0109 50  THR   B CB    
1745 O  OG1   . THR   B 53  ? 0.4562 0.4261 0.2472 -0.0353 -0.0077 -0.0091 50  THR   B OG1   
1746 C  CG2   . THR   B 53  ? 0.4559 0.3966 0.2501 -0.0322 -0.0048 -0.0240 50  THR   B CG2   
1747 N  N     . CYS   B 54  ? 0.4527 0.3616 0.2610 -0.0190 -0.0041 -0.0078 51  CYS   B N     
1748 C  CA    . CYS   B 54  ? 0.4515 0.3456 0.2647 -0.0155 -0.0035 -0.0081 51  CYS   B CA    
1749 C  C     . CYS   B 54  ? 0.4535 0.3382 0.2656 -0.0161 -0.0016 -0.0177 51  CYS   B C     
1750 O  O     . CYS   B 54  ? 0.4558 0.3420 0.2648 -0.0169 0.0001  -0.0237 51  CYS   B O     
1751 C  CB    . CYS   B 54  ? 0.4482 0.3349 0.2649 -0.0109 -0.0021 -0.0038 51  CYS   B CB    
1752 S  SG    . CYS   B 54  ? 0.4600 0.3541 0.2808 -0.0093 -0.0038 0.0073  51  CYS   B SG    
1753 N  N     . LEU   B 55  ? 0.4507 0.3271 0.2661 -0.0159 -0.0020 -0.0187 52  LEU   B N     
1754 C  CA    . LEU   B 55  ? 0.4515 0.3175 0.2681 -0.0160 -0.0005 -0.0259 52  LEU   B CA    
1755 C  C     . LEU   B 55  ? 0.4416 0.2974 0.2624 -0.0114 0.0007  -0.0223 52  LEU   B C     
1756 O  O     . LEU   B 55  ? 0.4341 0.2886 0.2578 -0.0105 -0.0003 -0.0175 52  LEU   B O     
1757 C  CB    . LEU   B 55  ? 0.4578 0.3228 0.2760 -0.0198 -0.0022 -0.0285 52  LEU   B CB    
1758 C  CG    . LEU   B 55  ? 0.4636 0.3162 0.2860 -0.0199 -0.0013 -0.0336 52  LEU   B CG    
1759 C  CD1   . LEU   B 55  ? 0.4692 0.3185 0.2909 -0.0192 0.0009  -0.0416 52  LEU   B CD1   
1760 C  CD2   . LEU   B 55  ? 0.4695 0.3221 0.2936 -0.0247 -0.0033 -0.0358 52  LEU   B CD2   
1761 N  N     . LEU   B 56  ? 0.4396 0.2903 0.2606 -0.0087 0.0029  -0.0246 53  LEU   B N     
1762 C  CA    . LEU   B 56  ? 0.4346 0.2773 0.2594 -0.0050 0.0038  -0.0209 53  LEU   B CA    
1763 C  C     . LEU   B 56  ? 0.4373 0.2709 0.2661 -0.0052 0.0041  -0.0240 53  LEU   B C     
1764 O  O     . LEU   B 56  ? 0.4428 0.2740 0.2717 -0.0061 0.0049  -0.0300 53  LEU   B O     
1765 C  CB    . LEU   B 56  ? 0.4319 0.2747 0.2555 -0.0021 0.0058  -0.0209 53  LEU   B CB    
1766 C  CG    . LEU   B 56  ? 0.4306 0.2831 0.2508 -0.0025 0.0054  -0.0177 53  LEU   B CG    
1767 C  CD1   . LEU   B 56  ? 0.4292 0.2814 0.2489 0.0000  0.0073  -0.0174 53  LEU   B CD1   
1768 C  CD2   . LEU   B 56  ? 0.4245 0.2799 0.2470 -0.0022 0.0036  -0.0107 53  LEU   B CD2   
1769 N  N     . ASP   B 57  ? 0.4330 0.2629 0.2655 -0.0045 0.0035  -0.0198 54  ASP   B N     
1770 C  CA    . ASP   B 57  ? 0.4370 0.2591 0.2745 -0.0050 0.0033  -0.0201 54  ASP   B CA    
1771 C  C     . ASP   B 57  ? 0.4323 0.2519 0.2722 -0.0015 0.0045  -0.0160 54  ASP   B C     
1772 O  O     . ASP   B 57  ? 0.4258 0.2483 0.2665 -0.0012 0.0040  -0.0116 54  ASP   B O     
1773 C  CB    . ASP   B 57  ? 0.4406 0.2641 0.2799 -0.0086 0.0012  -0.0184 54  ASP   B CB    
1774 C  CG    . ASP   B 57  ? 0.4470 0.2632 0.2922 -0.0101 0.0005  -0.0180 54  ASP   B CG    
1775 O  OD1   . ASP   B 57  ? 0.4502 0.2602 0.2988 -0.0082 0.0017  -0.0190 54  ASP   B OD1   
1776 O  OD2   . ASP   B 57  ? 0.4509 0.2687 0.2980 -0.0132 -0.0012 -0.0161 54  ASP   B OD2   
1777 N  N     . ILE   B 58  ? 0.4329 0.2484 0.2740 0.0009  0.0062  -0.0179 55  ILE   B N     
1778 C  CA    . ILE   B 58  ? 0.4293 0.2443 0.2719 0.0040  0.0074  -0.0143 55  ILE   B CA    
1779 C  C     . ILE   B 58  ? 0.4332 0.2433 0.2820 0.0044  0.0072  -0.0117 55  ILE   B C     
1780 O  O     . ILE   B 58  ? 0.4386 0.2429 0.2912 0.0047  0.0075  -0.0146 55  ILE   B O     
1781 C  CB    . ILE   B 58  ? 0.4301 0.2459 0.2703 0.0065  0.0093  -0.0170 55  ILE   B CB    
1782 C  CG1   . ILE   B 58  ? 0.4295 0.2516 0.2643 0.0057  0.0092  -0.0185 55  ILE   B CG1   
1783 C  CG2   . ILE   B 58  ? 0.4257 0.2421 0.2672 0.0092  0.0104  -0.0135 55  ILE   B CG2   
1784 C  CD1   . ILE   B 58  ? 0.4299 0.2540 0.2625 0.0074  0.0110  -0.0210 55  ILE   B CD1   
1785 N  N     . LEU   B 59  ? 0.4273 0.2404 0.2775 0.0044  0.0067  -0.0065 56  LEU   B N     
1786 C  CA    . LEU   B 59  ? 0.4318 0.2431 0.2879 0.0045  0.0063  -0.0022 56  LEU   B CA    
1787 C  C     . LEU   B 59  ? 0.4289 0.2422 0.2853 0.0075  0.0078  -0.0003 56  LEU   B C     
1788 O  O     . LEU   B 59  ? 0.4269 0.2462 0.2803 0.0080  0.0084  0.0010  56  LEU   B O     
1789 C  CB    . LEU   B 59  ? 0.4292 0.2456 0.2868 0.0017  0.0047  0.0026  56  LEU   B CB    
1790 C  CG    . LEU   B 59  ? 0.4308 0.2482 0.2946 0.0009  0.0039  0.0088  56  LEU   B CG    
1791 C  CD1   . LEU   B 59  ? 0.4373 0.2456 0.3081 0.0003  0.0030  0.0090  56  LEU   B CD1   
1792 C  CD2   . LEU   B 59  ? 0.4294 0.2549 0.2937 -0.0023 0.0026  0.0134  56  LEU   B CD2   
1793 N  N     . ASP   B 60  ? 0.4350 0.2435 0.2962 0.0093  0.0084  -0.0005 57  ASP   B N     
1794 C  CA    . ASP   B 60  ? 0.4352 0.2457 0.2982 0.0121  0.0096  0.0018  57  ASP   B CA    
1795 C  C     . ASP   B 60  ? 0.4365 0.2503 0.3052 0.0111  0.0083  0.0093  57  ASP   B C     
1796 O  O     . ASP   B 60  ? 0.4417 0.2508 0.3177 0.0105  0.0071  0.0121  57  ASP   B O     
1797 C  CB    . ASP   B 60  ? 0.4418 0.2466 0.3080 0.0149  0.0109  -0.0022 57  ASP   B CB    
1798 C  CG    . ASP   B 60  ? 0.4414 0.2484 0.3110 0.0180  0.0121  0.0007  57  ASP   B CG    
1799 O  OD1   . ASP   B 60  ? 0.4366 0.2504 0.3026 0.0181  0.0125  0.0034  57  ASP   B OD1   
1800 O  OD2   . ASP   B 60  ? 0.4482 0.2502 0.3248 0.0202  0.0125  -0.0002 57  ASP   B OD2   
1801 N  N     . THR   B 61  ? 0.4338 0.2564 0.2999 0.0106  0.0085  0.0125  58  THR   B N     
1802 C  CA    . THR   B 61  ? 0.4344 0.2641 0.3044 0.0085  0.0072  0.0197  58  THR   B CA    
1803 C  C     . THR   B 61  ? 0.4410 0.2733 0.3161 0.0104  0.0074  0.0244  58  THR   B C     
1804 O  O     . THR   B 61  ? 0.4421 0.2743 0.3151 0.0131  0.0091  0.0216  58  THR   B O     
1805 C  CB    . THR   B 61  ? 0.4259 0.2661 0.2911 0.0064  0.0073  0.0199  58  THR   B CB    
1806 O  OG1   . THR   B 61  ? 0.4177 0.2622 0.2792 0.0081  0.0090  0.0172  58  THR   B OG1   
1807 C  CG2   . THR   B 61  ? 0.4249 0.2635 0.2864 0.0050  0.0070  0.0159  58  THR   B CG2   
1808 N  N     . ALA   B 62  ? 0.4510 0.2870 0.3329 0.0087  0.0056  0.0323  59  ALA   B N     
1809 C  CA    . ALA   B 62  ? 0.4576 0.2975 0.3463 0.0102  0.0052  0.0389  59  ALA   B CA    
1810 C  C     . ALA   B 62  ? 0.4646 0.3171 0.3564 0.0064  0.0032  0.0484  59  ALA   B C     
1811 O  O     . ALA   B 62  ? 0.4674 0.3328 0.3551 0.0051  0.0038  0.0496  59  ALA   B O     
1812 C  CB    . ALA   B 62  ? 0.4668 0.2948 0.3647 0.0128  0.0047  0.0395  59  ALA   B CB    
1813 N  N     . TYR   B 67  ? 0.4422 0.4291 0.3292 -0.0270 -0.0037 0.0886  64  TYR   B N     
1814 C  CA    . TYR   B 67  ? 0.4399 0.4266 0.3242 -0.0290 -0.0034 0.0844  64  TYR   B CA    
1815 C  C     . TYR   B 67  ? 0.4419 0.4092 0.3323 -0.0281 -0.0055 0.0887  64  TYR   B C     
1816 O  O     . TYR   B 67  ? 0.4483 0.4133 0.3474 -0.0293 -0.0083 0.1001  64  TYR   B O     
1817 C  CB    . TYR   B 67  ? 0.4410 0.4539 0.3252 -0.0355 -0.0044 0.0910  64  TYR   B CB    
1818 C  CG    . TYR   B 67  ? 0.4431 0.4557 0.3268 -0.0378 -0.0047 0.0893  64  TYR   B CG    
1819 C  CD1   . TYR   B 67  ? 0.4392 0.4514 0.3163 -0.0362 -0.0019 0.0764  64  TYR   B CD1   
1820 C  CD2   . TYR   B 67  ? 0.4485 0.4570 0.3392 -0.0407 -0.0079 0.1002  64  TYR   B CD2   
1821 C  CE1   . TYR   B 67  ? 0.4400 0.4515 0.3169 -0.0378 -0.0022 0.0748  64  TYR   B CE1   
1822 C  CE2   . TYR   B 67  ? 0.4485 0.4565 0.3387 -0.0429 -0.0082 0.0985  64  TYR   B CE2   
1823 C  CZ    . TYR   B 67  ? 0.4430 0.4527 0.3260 -0.0413 -0.0053 0.0858  64  TYR   B CZ    
1824 O  OH    . TYR   B 67  ? 0.4381 0.4480 0.3209 -0.0433 -0.0056 0.0841  64  TYR   B OH    
1825 N  N     . SER   B 68  ? 0.4367 0.3905 0.3232 -0.0260 -0.0042 0.0792  65  SER   B N     
1826 C  CA    . SER   B 68  ? 0.4354 0.3743 0.3267 -0.0265 -0.0061 0.0818  65  SER   B CA    
1827 C  C     . SER   B 68  ? 0.4267 0.3689 0.3126 -0.0280 -0.0051 0.0748  65  SER   B C     
1828 O  O     . SER   B 68  ? 0.4199 0.3623 0.2993 -0.0254 -0.0025 0.0648  65  SER   B O     
1829 C  CB    . SER   B 68  ? 0.4397 0.3556 0.3332 -0.0216 -0.0058 0.0776  65  SER   B CB    
1830 O  OG    . SER   B 68  ? 0.4490 0.3511 0.3470 -0.0224 -0.0074 0.0784  65  SER   B OG    
1831 N  N     . ALA   B 69  ? 0.4250 0.3701 0.3147 -0.0322 -0.0072 0.0807  66  ALA   B N     
1832 C  CA    . ALA   B 69  ? 0.4197 0.3662 0.3052 -0.0332 -0.0063 0.0741  66  ALA   B CA    
1833 C  C     . ALA   B 69  ? 0.4172 0.3418 0.3004 -0.0288 -0.0054 0.0650  66  ALA   B C     
1834 O  O     . ALA   B 69  ? 0.4119 0.3366 0.2909 -0.0281 -0.0043 0.0578  66  ALA   B O     
1835 C  CB    . ALA   B 69  ? 0.4234 0.3770 0.3143 -0.0390 -0.0091 0.0833  66  ALA   B CB    
1836 N  N     . MET   B 70  ? 0.4187 0.3264 0.3055 -0.0262 -0.0062 0.0658  67  MET   B N     
1837 C  CA    . MET   B 70  ? 0.4207 0.3099 0.3054 -0.0226 -0.0054 0.0574  67  MET   B CA    
1838 C  C     . MET   B 70  ? 0.4185 0.3070 0.2956 -0.0181 -0.0024 0.0477  67  MET   B C     
1839 O  O     . MET   B 70  ? 0.4161 0.2942 0.2901 -0.0158 -0.0016 0.0406  67  MET   B O     
1840 C  CB    . MET   B 70  ? 0.4242 0.2971 0.3157 -0.0209 -0.0066 0.0599  67  MET   B CB    
1841 C  CG    . MET   B 70  ? 0.4300 0.3005 0.3312 -0.0252 -0.0098 0.0694  67  MET   B CG    
1842 S  SD    . MET   B 70  ? 0.4316 0.3020 0.3323 -0.0299 -0.0113 0.0680  67  MET   B SD    
1843 C  CE    . MET   B 70  ? 0.4335 0.2848 0.3301 -0.0261 -0.0099 0.0555  67  MET   B CE    
1844 N  N     . ARG   B 71  ? 0.4195 0.3201 0.2943 -0.0175 -0.0009 0.0477  68  ARG   B N     
1845 C  CA    . ARG   B 71  ? 0.4231 0.3229 0.2922 -0.0137 0.0017  0.0389  68  ARG   B CA    
1846 C  C     . ARG   B 71  ? 0.4188 0.3242 0.2843 -0.0139 0.0029  0.0325  68  ARG   B C     
1847 O  O     . ARG   B 71  ? 0.4159 0.3120 0.2787 -0.0109 0.0039  0.0257  68  ARG   B O     
1848 C  CB    . ARG   B 71  ? 0.4280 0.3390 0.2964 -0.0135 0.0028  0.0402  68  ARG   B CB    
1849 C  CG    . ARG   B 71  ? 0.4389 0.3426 0.3113 -0.0120 0.0019  0.0456  68  ARG   B CG    
1850 C  CD    . ARG   B 71  ? 0.4443 0.3524 0.3143 -0.0099 0.0036  0.0430  68  ARG   B CD    
1851 N  NE    . ARG   B 71  ? 0.4539 0.3596 0.3294 -0.0092 0.0023  0.0506  68  ARG   B NE    
1852 C  CZ    . ARG   B 71  ? 0.4635 0.3836 0.3423 -0.0117 0.0012  0.0588  68  ARG   B CZ    
1853 N  NH1   . ARG   B 71  ? 0.4633 0.4026 0.3390 -0.0153 0.0017  0.0591  68  ARG   B NH1   
1854 N  NH2   . ARG   B 71  ? 0.4743 0.3905 0.3600 -0.0107 -0.0003 0.0667  68  ARG   B NH2   
1855 N  N     . ASP   B 72  ? 0.4156 0.3372 0.2818 -0.0174 0.0026  0.0350  69  ASP   B N     
1856 C  CA    . ASP   B 72  ? 0.4152 0.3433 0.2796 -0.0173 0.0037  0.0292  69  ASP   B CA    
1857 C  C     . ASP   B 72  ? 0.4123 0.3277 0.2770 -0.0169 0.0024  0.0282  69  ASP   B C     
1858 O  O     . ASP   B 72  ? 0.4091 0.3230 0.2722 -0.0148 0.0035  0.0221  69  ASP   B O     
1859 C  CB    . ASP   B 72  ? 0.4187 0.3680 0.2844 -0.0216 0.0036  0.0326  69  ASP   B CB    
1860 C  CG    . ASP   B 72  ? 0.4210 0.3866 0.2851 -0.0216 0.0060  0.0281  69  ASP   B CG    
1861 O  OD1   . ASP   B 72  ? 0.4252 0.3855 0.2877 -0.0188 0.0072  0.0244  69  ASP   B OD1   
1862 O  OD2   . ASP   B 72  ? 0.4280 0.4127 0.2926 -0.0246 0.0066  0.0280  69  ASP   B OD2   
1863 N  N     . GLN   B 73  ? 0.4122 0.3187 0.2798 -0.0190 0.0001  0.0342  70  GLN   B N     
1864 C  CA    . GLN   B 73  ? 0.4141 0.3098 0.2821 -0.0195 -0.0012 0.0329  70  GLN   B CA    
1865 C  C     . GLN   B 73  ? 0.4114 0.2938 0.2759 -0.0151 0.0000  0.0258  70  GLN   B C     
1866 O  O     . GLN   B 73  ? 0.4102 0.2910 0.2729 -0.0144 0.0001  0.0216  70  GLN   B O     
1867 C  CB    . GLN   B 73  ? 0.4205 0.3086 0.2937 -0.0228 -0.0038 0.0398  70  GLN   B CB    
1868 C  CG    . GLN   B 73  ? 0.4246 0.3016 0.2982 -0.0239 -0.0052 0.0371  70  GLN   B CG    
1869 C  CD    . GLN   B 73  ? 0.4229 0.3096 0.2948 -0.0261 -0.0054 0.0357  70  GLN   B CD    
1870 O  OE1   . GLN   B 73  ? 0.4258 0.3244 0.3004 -0.0301 -0.0065 0.0412  70  GLN   B OE1   
1871 N  NE2   . GLN   B 73  ? 0.4221 0.3054 0.2902 -0.0234 -0.0044 0.0290  70  GLN   B NE2   
1872 N  N     . TYR   B 74  ? 0.4117 0.2863 0.2758 -0.0124 0.0008  0.0249  71  TYR   B N     
1873 C  CA    . TYR   B 74  ? 0.4122 0.2757 0.2731 -0.0088 0.0018  0.0189  71  TYR   B CA    
1874 C  C     . TYR   B 74  ? 0.4085 0.2772 0.2664 -0.0061 0.0037  0.0137  71  TYR   B C     
1875 O  O     . TYR   B 74  ? 0.4054 0.2680 0.2610 -0.0039 0.0041  0.0096  71  TYR   B O     
1876 C  CB    . TYR   B 74  ? 0.4156 0.2691 0.2775 -0.0068 0.0020  0.0193  71  TYR   B CB    
1877 C  CG    . TYR   B 74  ? 0.4144 0.2719 0.2769 -0.0053 0.0031  0.0214  71  TYR   B CG    
1878 C  CD1   . TYR   B 74  ? 0.4089 0.2717 0.2681 -0.0031 0.0050  0.0177  71  TYR   B CD1   
1879 C  CD2   . TYR   B 74  ? 0.4194 0.2741 0.2867 -0.0058 0.0022  0.0269  71  TYR   B CD2   
1880 C  CE1   . TYR   B 74  ? 0.4102 0.2771 0.2700 -0.0021 0.0059  0.0194  71  TYR   B CE1   
1881 C  CE2   . TYR   B 74  ? 0.4184 0.2775 0.2867 -0.0044 0.0030  0.0295  71  TYR   B CE2   
1882 C  CZ    . TYR   B 74  ? 0.4139 0.2796 0.2779 -0.0028 0.0048  0.0255  71  TYR   B CZ    
1883 O  OH    . TYR   B 74  ? 0.4148 0.2859 0.2797 -0.0020 0.0055  0.0279  71  TYR   B OH    
1884 N  N     . MET   B 75  ? 0.4048 0.2857 0.2633 -0.0066 0.0047  0.0141  72  MET   B N     
1885 C  CA    . MET   B 75  ? 0.4005 0.2868 0.2583 -0.0041 0.0065  0.0084  72  MET   B CA    
1886 C  C     . MET   B 75  ? 0.4010 0.2914 0.2599 -0.0046 0.0061  0.0068  72  MET   B C     
1887 O  O     . MET   B 75  ? 0.4003 0.2895 0.2598 -0.0018 0.0070  0.0025  72  MET   B O     
1888 C  CB    . MET   B 75  ? 0.3983 0.2973 0.2569 -0.0048 0.0080  0.0078  72  MET   B CB    
1889 C  CG    . MET   B 75  ? 0.3982 0.2934 0.2557 -0.0034 0.0088  0.0078  72  MET   B CG    
1890 S  SD    . MET   B 75  ? 0.3987 0.3092 0.2565 -0.0045 0.0105  0.0060  72  MET   B SD    
1891 C  CE    . MET   B 75  ? 0.3985 0.3018 0.2555 -0.0037 0.0101  0.0100  72  MET   B CE    
1892 N  N     . ARG   B 76  ? 0.4021 0.2980 0.2623 -0.0081 0.0046  0.0108  73  ARG   B N     
1893 C  CA    . ARG   B 76  ? 0.4026 0.3029 0.2640 -0.0087 0.0040  0.0097  73  ARG   B CA    
1894 C  C     . ARG   B 76  ? 0.4066 0.2941 0.2663 -0.0076 0.0028  0.0088  73  ARG   B C     
1895 O  O     . ARG   B 76  ? 0.4067 0.2943 0.2669 -0.0056 0.0030  0.0060  73  ARG   B O     
1896 C  CB    . ARG   B 76  ? 0.4033 0.3133 0.2665 -0.0134 0.0026  0.0149  73  ARG   B CB    
1897 C  CG    . ARG   B 76  ? 0.4017 0.3286 0.2664 -0.0148 0.0039  0.0153  73  ARG   B CG    
1898 C  CD    . ARG   B 76  ? 0.4040 0.3437 0.2708 -0.0195 0.0026  0.0203  73  ARG   B CD    
1899 N  NE    . ARG   B 76  ? 0.4098 0.3431 0.2776 -0.0235 0.0000  0.0279  73  ARG   B NE    
1900 C  CZ    . ARG   B 76  ? 0.4103 0.3487 0.2795 -0.0264 -0.0007 0.0342  73  ARG   B CZ    
1901 N  NH1   . ARG   B 76  ? 0.4084 0.3608 0.2771 -0.0263 0.0010  0.0336  73  ARG   B NH1   
1902 N  NH2   . ARG   B 76  ? 0.4166 0.3471 0.2887 -0.0296 -0.0033 0.0412  73  ARG   B NH2   
1903 N  N     . THR   B 77  ? 0.4122 0.2898 0.2706 -0.0090 0.0017  0.0110  74  THR   B N     
1904 C  CA    . THR   B 77  ? 0.4159 0.2830 0.2724 -0.0091 0.0005  0.0096  74  THR   B CA    
1905 C  C     . THR   B 77  ? 0.4141 0.2751 0.2681 -0.0052 0.0017  0.0058  74  THR   B C     
1906 O  O     . THR   B 77  ? 0.4179 0.2777 0.2708 -0.0049 0.0010  0.0043  74  THR   B O     
1907 C  CB    . THR   B 77  ? 0.4210 0.2812 0.2789 -0.0122 -0.0010 0.0127  74  THR   B CB    
1908 O  OG1   . THR   B 77  ? 0.4219 0.2895 0.2827 -0.0163 -0.0025 0.0168  74  THR   B OG1   
1909 C  CG2   . THR   B 77  ? 0.4258 0.2761 0.2821 -0.0128 -0.0020 0.0096  74  THR   B CG2   
1910 N  N     . GLY   B 78  ? 0.4131 0.2723 0.2666 -0.0028 0.0032  0.0049  75  GLY   B N     
1911 C  CA    . GLY   B 78  ? 0.4134 0.2672 0.2650 0.0004  0.0043  0.0022  75  GLY   B CA    
1912 C  C     . GLY   B 78  ? 0.4132 0.2705 0.2660 0.0024  0.0045  0.0004  75  GLY   B C     
1913 O  O     . GLY   B 78  ? 0.4091 0.2737 0.2651 0.0031  0.0052  -0.0003 75  GLY   B O     
1914 N  N     . GLU   B 79  ? 0.4177 0.2708 0.2688 0.0032  0.0039  -0.0001 76  GLU   B N     
1915 C  CA    . GLU   B 79  ? 0.4186 0.2747 0.2725 0.0053  0.0038  -0.0003 76  GLU   B CA    
1916 C  C     . GLU   B 79  ? 0.4183 0.2717 0.2736 0.0082  0.0052  -0.0014 76  GLU   B C     
1917 O  O     . GLU   B 79  ? 0.4148 0.2710 0.2751 0.0102  0.0055  -0.0019 76  GLU   B O     
1918 C  CB    . GLU   B 79  ? 0.4242 0.2800 0.2761 0.0040  0.0020  0.0010  76  GLU   B CB    
1919 C  CG    . GLU   B 79  ? 0.4317 0.2926 0.2844 0.0014  0.0006  0.0019  76  GLU   B CG    
1920 C  CD    . GLU   B 79  ? 0.4408 0.3016 0.2901 -0.0015 -0.0012 0.0023  76  GLU   B CD    
1921 O  OE1   . GLU   B 79  ? 0.4425 0.3021 0.2896 -0.0011 -0.0016 0.0023  76  GLU   B OE1   
1922 O  OE2   . GLU   B 79  ? 0.4543 0.3174 0.3036 -0.0046 -0.0023 0.0025  76  GLU   B OE2   
1923 N  N     . GLY   B 80  ? 0.4184 0.2665 0.2703 0.0082  0.0059  -0.0017 77  GLY   B N     
1924 C  CA    . GLY   B 80  ? 0.4167 0.2620 0.2694 0.0102  0.0071  -0.0024 77  GLY   B CA    
1925 C  C     . GLY   B 80  ? 0.4157 0.2586 0.2659 0.0099  0.0083  -0.0032 77  GLY   B C     
1926 O  O     . GLY   B 80  ? 0.4187 0.2593 0.2661 0.0086  0.0079  -0.0027 77  GLY   B O     
1927 N  N     . PHE   B 81  ? 0.4121 0.2556 0.2642 0.0111  0.0096  -0.0044 78  PHE   B N     
1928 C  CA    . PHE   B 81  ? 0.4118 0.2552 0.2624 0.0108  0.0107  -0.0047 78  PHE   B CA    
1929 C  C     . PHE   B 81  ? 0.4120 0.2524 0.2620 0.0120  0.0116  -0.0050 78  PHE   B C     
1930 O  O     . PHE   B 81  ? 0.4162 0.2569 0.2691 0.0128  0.0119  -0.0061 78  PHE   B O     
1931 C  CB    . PHE   B 81  ? 0.4087 0.2594 0.2621 0.0102  0.0114  -0.0060 78  PHE   B CB    
1932 C  CG    . PHE   B 81  ? 0.4060 0.2613 0.2598 0.0085  0.0105  -0.0049 78  PHE   B CG    
1933 C  CD1   . PHE   B 81  ? 0.4085 0.2670 0.2649 0.0087  0.0100  -0.0059 78  PHE   B CD1   
1934 C  CD2   . PHE   B 81  ? 0.4066 0.2635 0.2590 0.0066  0.0100  -0.0021 78  PHE   B CD2   
1935 C  CE1   . PHE   B 81  ? 0.4083 0.2723 0.2652 0.0068  0.0092  -0.0045 78  PHE   B CE1   
1936 C  CE2   . PHE   B 81  ? 0.4077 0.2691 0.2610 0.0045  0.0090  -0.0001 78  PHE   B CE2   
1937 C  CZ    . PHE   B 81  ? 0.4069 0.2724 0.2619 0.0044  0.0086  -0.0016 78  PHE   B CZ    
1938 N  N     . LEU   B 82  ? 0.4163 0.2539 0.2633 0.0120  0.0119  -0.0041 79  LEU   B N     
1939 C  CA    . LEU   B 82  ? 0.4154 0.2518 0.2617 0.0129  0.0129  -0.0042 79  LEU   B CA    
1940 C  C     . LEU   B 82  ? 0.4159 0.2563 0.2634 0.0126  0.0138  -0.0043 79  LEU   B C     
1941 O  O     . LEU   B 82  ? 0.4139 0.2549 0.2609 0.0123  0.0137  -0.0027 79  LEU   B O     
1942 C  CB    . LEU   B 82  ? 0.4212 0.2542 0.2644 0.0134  0.0131  -0.0037 79  LEU   B CB    
1943 C  CG    . LEU   B 82  ? 0.4253 0.2569 0.2662 0.0133  0.0127  -0.0038 79  LEU   B CG    
1944 C  CD1   . LEU   B 82  ? 0.4285 0.2588 0.2670 0.0140  0.0135  -0.0049 79  LEU   B CD1   
1945 C  CD2   . LEU   B 82  ? 0.4260 0.2590 0.2684 0.0134  0.0126  -0.0026 79  LEU   B CD2   
1946 N  N     . CYS   B 83  ? 0.4141 0.2576 0.2640 0.0124  0.0146  -0.0061 80  CYS   B N     
1947 C  CA    . CYS   B 83  ? 0.4148 0.2644 0.2657 0.0115  0.0155  -0.0068 80  CYS   B CA    
1948 C  C     . CYS   B 83  ? 0.4100 0.2584 0.2598 0.0119  0.0162  -0.0059 80  CYS   B C     
1949 O  O     . CYS   B 83  ? 0.4111 0.2584 0.2625 0.0118  0.0166  -0.0075 80  CYS   B O     
1950 C  CB    . CYS   B 83  ? 0.4179 0.2728 0.2723 0.0105  0.0160  -0.0107 80  CYS   B CB    
1951 S  SG    . CYS   B 83  ? 0.4333 0.2917 0.2891 0.0101  0.0154  -0.0115 80  CYS   B SG    
1952 N  N     . VAL   B 84  ? 0.4054 0.2544 0.2538 0.0124  0.0162  -0.0033 81  VAL   B N     
1953 C  CA    . VAL   B 84  ? 0.4034 0.2520 0.2511 0.0134  0.0170  -0.0021 81  VAL   B CA    
1954 C  C     . VAL   B 84  ? 0.3988 0.2550 0.2478 0.0123  0.0175  -0.0013 81  VAL   B C     
1955 O  O     . VAL   B 84  ? 0.4003 0.2618 0.2503 0.0115  0.0171  0.0006  81  VAL   B O     
1956 C  CB    . VAL   B 84  ? 0.4051 0.2494 0.2520 0.0152  0.0169  -0.0003 81  VAL   B CB    
1957 C  CG1   . VAL   B 84  ? 0.4086 0.2532 0.2552 0.0166  0.0179  0.0003  81  VAL   B CG1   
1958 C  CG2   . VAL   B 84  ? 0.4093 0.2478 0.2544 0.0155  0.0163  -0.0016 81  VAL   B CG2   
1959 N  N     . PHE   B 85  ? 0.3971 0.2547 0.2463 0.0120  0.0183  -0.0022 82  PHE   B N     
1960 C  CA    . PHE   B 85  ? 0.3948 0.2605 0.2451 0.0108  0.0187  -0.0012 82  PHE   B CA    
1961 C  C     . PHE   B 85  ? 0.3955 0.2597 0.2453 0.0123  0.0194  0.0005  82  PHE   B C     
1962 O  O     . PHE   B 85  ? 0.3981 0.2563 0.2466 0.0136  0.0196  0.0000  82  PHE   B O     
1963 C  CB    . PHE   B 85  ? 0.3937 0.2649 0.2454 0.0080  0.0191  -0.0052 82  PHE   B CB    
1964 C  CG    . PHE   B 85  ? 0.3919 0.2585 0.2449 0.0074  0.0194  -0.0077 82  PHE   B CG    
1965 C  CD1   . PHE   B 85  ? 0.3908 0.2598 0.2441 0.0066  0.0199  -0.0068 82  PHE   B CD1   
1966 C  CD2   . PHE   B 85  ? 0.3923 0.2524 0.2470 0.0077  0.0191  -0.0099 82  PHE   B CD2   
1967 C  CE1   . PHE   B 85  ? 0.3922 0.2570 0.2474 0.0056  0.0200  -0.0080 82  PHE   B CE1   
1968 C  CE2   . PHE   B 85  ? 0.3933 0.2492 0.2506 0.0070  0.0190  -0.0107 82  PHE   B CE2   
1969 C  CZ    . PHE   B 85  ? 0.3936 0.2517 0.2511 0.0057  0.0194  -0.0096 82  PHE   B CZ    
1970 N  N     . ALA   B 86  ? 0.3947 0.2657 0.2456 0.0123  0.0198  0.0028  83  ALA   B N     
1971 C  CA    . ALA   B 86  ? 0.3962 0.2677 0.2472 0.0137  0.0206  0.0041  83  ALA   B CA    
1972 C  C     . ALA   B 86  ? 0.3955 0.2721 0.2469 0.0107  0.0210  0.0025  83  ALA   B C     
1973 O  O     . ALA   B 86  ? 0.3977 0.2812 0.2501 0.0081  0.0207  0.0014  83  ALA   B O     
1974 C  CB    . ALA   B 86  ? 0.3960 0.2719 0.2496 0.0159  0.0207  0.0082  83  ALA   B CB    
1975 N  N     . ILE   B 87  ? 0.3969 0.2712 0.2477 0.0107  0.0215  0.0023  84  ILE   B N     
1976 C  CA    . ILE   B 87  ? 0.3986 0.2764 0.2509 0.0074  0.0216  0.0009  84  ILE   B CA    
1977 C  C     . ILE   B 87  ? 0.3987 0.2868 0.2521 0.0062  0.0220  0.0025  84  ILE   B C     
1978 O  O     . ILE   B 87  ? 0.4001 0.2926 0.2550 0.0027  0.0219  0.0006  84  ILE   B O     
1979 C  CB    . ILE   B 87  ? 0.4000 0.2739 0.2520 0.0070  0.0218  0.0017  84  ILE   B CB    
1980 C  CG1   . ILE   B 87  ? 0.4010 0.2773 0.2513 0.0098  0.0228  0.0044  84  ILE   B CG1   
1981 C  CG2   . ILE   B 87  ? 0.4013 0.2669 0.2533 0.0071  0.0211  0.0007  84  ILE   B CG2   
1982 C  CD1   . ILE   B 87  ? 0.4032 0.2839 0.2542 0.0078  0.0232  0.0061  84  ILE   B CD1   
1983 N  N     . ASN   B 88  ? 0.3990 0.2911 0.2526 0.0091  0.0223  0.0060  85  ASN   B N     
1984 C  CA    . ASN   B 88  ? 0.3977 0.3010 0.2533 0.0084  0.0224  0.0087  85  ASN   B CA    
1985 C  C     . ASN   B 88  ? 0.3973 0.3076 0.2539 0.0074  0.0215  0.0102  85  ASN   B C     
1986 O  O     . ASN   B 88  ? 0.3993 0.3197 0.2581 0.0074  0.0212  0.0141  85  ASN   B O     
1987 C  CB    . ASN   B 88  ? 0.3958 0.3006 0.2530 0.0125  0.0233  0.0123  85  ASN   B CB    
1988 C  CG    . ASN   B 88  ? 0.3948 0.2948 0.2536 0.0166  0.0231  0.0143  85  ASN   B CG    
1989 O  OD1   . ASN   B 88  ? 0.3909 0.2834 0.2481 0.0166  0.0225  0.0124  85  ASN   B OD1   
1990 N  ND2   . ASN   B 88  ? 0.3939 0.2982 0.2569 0.0200  0.0235  0.0180  85  ASN   B ND2   
1991 N  N     . ASN   B 89  ? 0.3989 0.3052 0.2543 0.0064  0.0210  0.0076  86  ASN   B N     
1992 C  CA    . ASN   B 89  ? 0.3999 0.3149 0.2560 0.0046  0.0201  0.0090  86  ASN   B CA    
1993 C  C     . ASN   B 89  ? 0.3998 0.3159 0.2547 0.0010  0.0200  0.0029  86  ASN   B C     
1994 O  O     . ASN   B 89  ? 0.3972 0.3049 0.2513 0.0020  0.0200  0.0005  86  ASN   B O     
1995 C  CB    . ASN   B 89  ? 0.4031 0.3158 0.2608 0.0078  0.0193  0.0141  86  ASN   B CB    
1996 C  CG    . ASN   B 89  ? 0.4031 0.3283 0.2619 0.0051  0.0182  0.0171  86  ASN   B CG    
1997 O  OD1   . ASN   B 89  ? 0.4035 0.3295 0.2609 0.0032  0.0178  0.0147  86  ASN   B OD1   
1998 N  ND2   . ASN   B 89  ? 0.4060 0.3430 0.2675 0.0046  0.0176  0.0225  86  ASN   B ND2   
1999 N  N     . THR   B 90  ? 0.4003 0.3278 0.2556 -0.0032 0.0201  0.0001  87  THR   B N     
2000 C  CA    . THR   B 90  ? 0.4016 0.3321 0.2571 -0.0069 0.0205  -0.0074 87  THR   B CA    
2001 C  C     . THR   B 90  ? 0.3995 0.3346 0.2543 -0.0070 0.0200  -0.0072 87  THR   B C     
2002 O  O     . THR   B 90  ? 0.4019 0.3327 0.2570 -0.0075 0.0205  -0.0127 87  THR   B O     
2003 C  CB    . THR   B 90  ? 0.4033 0.3446 0.2599 -0.0116 0.0208  -0.0118 87  THR   B CB    
2004 O  OG1   . THR   B 90  ? 0.4060 0.3377 0.2638 -0.0110 0.0212  -0.0125 87  THR   B OG1   
2005 C  CG2   . THR   B 90  ? 0.4047 0.3502 0.2627 -0.0154 0.0215  -0.0210 87  THR   B CG2   
2006 N  N     . LYS   B 91  ? 0.3998 0.3438 0.2544 -0.0066 0.0191  -0.0003 88  LYS   B N     
2007 C  CA    . LYS   B 91  ? 0.3983 0.3487 0.2524 -0.0076 0.0185  0.0009  88  LYS   B CA    
2008 C  C     . LYS   B 91  ? 0.3956 0.3310 0.2494 -0.0042 0.0184  0.0007  88  LYS   B C     
2009 O  O     . LYS   B 91  ? 0.3944 0.3315 0.2479 -0.0054 0.0186  -0.0028 88  LYS   B O     
2010 C  CB    . LYS   B 91  ? 0.4016 0.3644 0.2570 -0.0080 0.0171  0.0104  88  LYS   B CB    
2011 C  CG    . LYS   B 91  ? 0.4047 0.3756 0.2604 -0.0094 0.0161  0.0139  88  LYS   B CG    
2012 C  CD    . LYS   B 91  ? 0.4086 0.3929 0.2624 -0.0142 0.0169  0.0064  88  LYS   B CD    
2013 C  CE    . LYS   B 91  ? 0.4107 0.4092 0.2645 -0.0167 0.0158  0.0114  88  LYS   B CE    
2014 N  NZ    . LYS   B 91  ? 0.4121 0.3984 0.2667 -0.0139 0.0152  0.0141  88  LYS   B NZ    
2015 N  N     . SER   B 92  ? 0.3916 0.3136 0.2456 -0.0003 0.0183  0.0037  89  SER   B N     
2016 C  CA    . SER   B 92  ? 0.3904 0.2996 0.2440 0.0024  0.0181  0.0033  89  SER   B CA    
2017 C  C     . SER   B 92  ? 0.3918 0.2954 0.2449 0.0016  0.0189  -0.0043 89  SER   B C     
2018 O  O     . SER   B 92  ? 0.3904 0.2900 0.2434 0.0021  0.0187  -0.0058 89  SER   B O     
2019 C  CB    . SER   B 92  ? 0.3891 0.2871 0.2430 0.0064  0.0181  0.0069  89  SER   B CB    
2020 O  OG    . SER   B 92  ? 0.3898 0.2827 0.2430 0.0070  0.0190  0.0040  89  SER   B OG    
2021 N  N     . PHE   B 93  ? 0.3956 0.2995 0.2495 0.0001  0.0197  -0.0088 90  PHE   B N     
2022 C  CA    . PHE   B 93  ? 0.4024 0.3003 0.2583 -0.0006 0.0203  -0.0156 90  PHE   B CA    
2023 C  C     . PHE   B 93  ? 0.4078 0.3156 0.2652 -0.0033 0.0209  -0.0214 90  PHE   B C     
2024 O  O     . PHE   B 93  ? 0.4118 0.3154 0.2710 -0.0025 0.0211  -0.0252 90  PHE   B O     
2025 C  CB    . PHE   B 93  ? 0.4028 0.2981 0.2606 -0.0019 0.0208  -0.0181 90  PHE   B CB    
2026 C  CG    . PHE   B 93  ? 0.4065 0.2952 0.2688 -0.0027 0.0212  -0.0245 90  PHE   B CG    
2027 C  CD1   . PHE   B 93  ? 0.4074 0.2844 0.2710 -0.0001 0.0207  -0.0235 90  PHE   B CD1   
2028 C  CD2   . PHE   B 93  ? 0.4082 0.3029 0.2744 -0.0062 0.0219  -0.0315 90  PHE   B CD2   
2029 C  CE1   . PHE   B 93  ? 0.4104 0.2814 0.2800 -0.0005 0.0208  -0.0283 90  PHE   B CE1   
2030 C  CE2   . PHE   B 93  ? 0.4117 0.2993 0.2843 -0.0066 0.0222  -0.0376 90  PHE   B CE2   
2031 C  CZ    . PHE   B 93  ? 0.4138 0.2893 0.2885 -0.0035 0.0216  -0.0354 90  PHE   B CZ    
2032 N  N     . GLU   B 94  ? 0.4163 0.3389 0.2731 -0.0065 0.0211  -0.0218 91  GLU   B N     
2033 C  CA    . GLU   B 94  ? 0.4229 0.3586 0.2806 -0.0098 0.0218  -0.0281 91  GLU   B CA    
2034 C  C     . GLU   B 94  ? 0.4207 0.3593 0.2772 -0.0089 0.0213  -0.0255 91  GLU   B C     
2035 O  O     . GLU   B 94  ? 0.4250 0.3707 0.2831 -0.0105 0.0222  -0.0319 91  GLU   B O     
2036 C  CB    . GLU   B 94  ? 0.4294 0.3827 0.2862 -0.0140 0.0219  -0.0283 91  GLU   B CB    
2037 C  CG    . GLU   B 94  ? 0.4380 0.3898 0.2971 -0.0161 0.0227  -0.0342 91  GLU   B CG    
2038 C  CD    . GLU   B 94  ? 0.4495 0.4195 0.3076 -0.0209 0.0227  -0.0352 91  GLU   B CD    
2039 O  OE1   . GLU   B 94  ? 0.4527 0.4341 0.3080 -0.0214 0.0217  -0.0271 91  GLU   B OE1   
2040 O  OE2   . GLU   B 94  ? 0.4619 0.4350 0.3227 -0.0243 0.0237  -0.0437 91  GLU   B OE2   
2041 N  N     . ASP   B 95  ? 0.4183 0.3505 0.2730 -0.0063 0.0201  -0.0169 92  ASP   B N     
2042 C  CA    . ASP   B 95  ? 0.4146 0.3486 0.2685 -0.0057 0.0192  -0.0127 92  ASP   B CA    
2043 C  C     . ASP   B 95  ? 0.4142 0.3363 0.2691 -0.0032 0.0194  -0.0160 92  ASP   B C     
2044 O  O     . ASP   B 95  ? 0.4152 0.3409 0.2699 -0.0036 0.0189  -0.0146 92  ASP   B O     
2045 C  CB    . ASP   B 95  ? 0.4170 0.3448 0.2702 -0.0034 0.0177  -0.0030 92  ASP   B CB    
2046 C  CG    . ASP   B 95  ? 0.4198 0.3619 0.2734 -0.0056 0.0166  0.0043  92  ASP   B CG    
2047 O  OD1   . ASP   B 95  ? 0.4208 0.3789 0.2740 -0.0093 0.0170  0.0019  92  ASP   B OD1   
2048 O  OD2   . ASP   B 95  ? 0.4250 0.3623 0.2801 -0.0037 0.0153  0.0121  92  ASP   B OD2   
2049 N  N     . ILE   B 96  ? 0.4122 0.3214 0.2684 -0.0011 0.0198  -0.0192 93  ILE   B N     
2050 C  CA    . ILE   B 96  ? 0.4107 0.3080 0.2682 0.0016  0.0196  -0.0204 93  ILE   B CA    
2051 C  C     . ILE   B 96  ? 0.4119 0.3159 0.2720 0.0007  0.0203  -0.0260 93  ILE   B C     
2052 O  O     . ILE   B 96  ? 0.4096 0.3116 0.2695 0.0017  0.0196  -0.0241 93  ILE   B O     
2053 C  CB    . ILE   B 96  ? 0.4100 0.2958 0.2696 0.0031  0.0198  -0.0227 93  ILE   B CB    
2054 C  CG1   . ILE   B 96  ? 0.4101 0.2895 0.2667 0.0044  0.0192  -0.0169 93  ILE   B CG1   
2055 C  CG2   . ILE   B 96  ? 0.4096 0.2865 0.2722 0.0052  0.0196  -0.0246 93  ILE   B CG2   
2056 C  CD1   . ILE   B 96  ? 0.4102 0.2824 0.2643 0.0068  0.0183  -0.0117 93  ILE   B CD1   
2057 N  N     . HIS   B 97  ? 0.4164 0.3291 0.2795 -0.0014 0.0217  -0.0336 94  HIS   B N     
2058 C  CA    . HIS   B 97  ? 0.4212 0.3408 0.2881 -0.0018 0.0228  -0.0407 94  HIS   B CA    
2059 C  C     . HIS   B 97  ? 0.4181 0.3492 0.2820 -0.0032 0.0223  -0.0369 94  HIS   B C     
2060 O  O     . HIS   B 97  ? 0.4168 0.3494 0.2831 -0.0023 0.0227  -0.0396 94  HIS   B O     
2061 C  CB    . HIS   B 97  ? 0.4262 0.3553 0.2972 -0.0043 0.0246  -0.0508 94  HIS   B CB    
2062 C  CG    . HIS   B 97  ? 0.4306 0.3790 0.2982 -0.0086 0.0252  -0.0514 94  HIS   B CG    
2063 N  ND1   . HIS   B 97  ? 0.4322 0.3847 0.2962 -0.0106 0.0245  -0.0469 94  HIS   B ND1   
2064 C  CD2   . HIS   B 97  ? 0.4323 0.3990 0.2997 -0.0114 0.0262  -0.0557 94  HIS   B CD2   
2065 C  CE1   . HIS   B 97  ? 0.4329 0.4054 0.2948 -0.0147 0.0249  -0.0478 94  HIS   B CE1   
2066 N  NE2   . HIS   B 97  ? 0.4355 0.4175 0.2991 -0.0154 0.0260  -0.0533 94  HIS   B NE2   
2067 N  N     . HIS   B 98  ? 0.4190 0.3588 0.2788 -0.0054 0.0214  -0.0300 95  HIS   B N     
2068 C  CA    . HIS   B 98  ? 0.4205 0.3710 0.2783 -0.0073 0.0204  -0.0242 95  HIS   B CA    
2069 C  C     . HIS   B 98  ? 0.4203 0.3578 0.2778 -0.0046 0.0190  -0.0191 95  HIS   B C     
2070 O  O     . HIS   B 98  ? 0.4204 0.3639 0.2787 -0.0053 0.0189  -0.0191 95  HIS   B O     
2071 C  CB    . HIS   B 98  ? 0.4221 0.3823 0.2773 -0.0099 0.0192  -0.0158 95  HIS   B CB    
2072 C  CG    . HIS   B 98  ? 0.4252 0.4014 0.2800 -0.0133 0.0202  -0.0195 95  HIS   B CG    
2073 N  ND1   . HIS   B 98  ? 0.4293 0.4241 0.2846 -0.0168 0.0217  -0.0267 95  HIS   B ND1   
2074 C  CD2   . HIS   B 98  ? 0.4287 0.4068 0.2825 -0.0142 0.0199  -0.0170 95  HIS   B CD2   
2075 C  CE1   . HIS   B 98  ? 0.4313 0.4389 0.2858 -0.0200 0.0222  -0.0289 95  HIS   B CE1   
2076 N  NE2   . HIS   B 98  ? 0.4318 0.4291 0.2853 -0.0185 0.0210  -0.0226 95  HIS   B NE2   
2077 N  N     . TYR   B 99  ? 0.4235 0.3450 0.2801 -0.0019 0.0181  -0.0153 96  TYR   B N     
2078 C  CA    . TYR   B 99  ? 0.4251 0.3341 0.2814 0.0004  0.0169  -0.0117 96  TYR   B CA    
2079 C  C     . TYR   B 99  ? 0.4275 0.3335 0.2866 0.0020  0.0176  -0.0176 96  TYR   B C     
2080 O  O     . TYR   B 99  ? 0.4296 0.3361 0.2889 0.0019  0.0168  -0.0158 96  TYR   B O     
2081 C  CB    . TYR   B 99  ? 0.4286 0.3232 0.2833 0.0028  0.0162  -0.0084 96  TYR   B CB    
2082 C  CG    . TYR   B 99  ? 0.4299 0.3263 0.2835 0.0021  0.0153  -0.0017 96  TYR   B CG    
2083 C  CD1   . TYR   B 99  ? 0.4337 0.3314 0.2877 0.0012  0.0138  0.0047  96  TYR   B CD1   
2084 C  CD2   . TYR   B 99  ? 0.4322 0.3294 0.2854 0.0024  0.0158  -0.0013 96  TYR   B CD2   
2085 C  CE1   . TYR   B 99  ? 0.4352 0.3344 0.2904 0.0008  0.0128  0.0115  96  TYR   B CE1   
2086 C  CE2   . TYR   B 99  ? 0.4356 0.3352 0.2892 0.0022  0.0149  0.0053  96  TYR   B CE2   
2087 C  CZ    . TYR   B 99  ? 0.4358 0.3360 0.2909 0.0016  0.0134  0.0118  96  TYR   B CZ    
2088 O  OH    . TYR   B 99  ? 0.4414 0.3438 0.2990 0.0017  0.0124  0.0189  96  TYR   B OH    
2089 N  N     . ARG   B 100 ? 0.4282 0.3312 0.2904 0.0032  0.0188  -0.0243 97  ARG   B N     
2090 C  CA    . ARG   B 100 ? 0.4342 0.3340 0.3012 0.0052  0.0194  -0.0294 97  ARG   B CA    
2091 C  C     . ARG   B 100 ? 0.4298 0.3441 0.2991 0.0037  0.0204  -0.0336 97  ARG   B C     
2092 O  O     . ARG   B 100 ? 0.4290 0.3429 0.3009 0.0051  0.0202  -0.0343 97  ARG   B O     
2093 C  CB    . ARG   B 100 ? 0.4418 0.3352 0.3139 0.0067  0.0204  -0.0352 97  ARG   B CB    
2094 C  CG    . ARG   B 100 ? 0.4490 0.3376 0.3281 0.0094  0.0206  -0.0389 97  ARG   B CG    
2095 C  CD    . ARG   B 100 ? 0.4611 0.3444 0.3481 0.0106  0.0215  -0.0450 97  ARG   B CD    
2096 N  NE    . ARG   B 100 ? 0.4688 0.3493 0.3645 0.0135  0.0216  -0.0482 97  ARG   B NE    
2097 C  CZ    . ARG   B 100 ? 0.4735 0.3450 0.3706 0.0159  0.0199  -0.0426 97  ARG   B CZ    
2098 N  NH1   . ARG   B 100 ? 0.4748 0.3390 0.3654 0.0156  0.0183  -0.0349 97  ARG   B NH1   
2099 N  NH2   . ARG   B 100 ? 0.4805 0.3517 0.3862 0.0185  0.0200  -0.0450 97  ARG   B NH2   
2100 N  N     . GLU   B 101 ? 0.4316 0.3605 0.3000 0.0007  0.0215  -0.0364 98  GLU   B N     
2101 C  CA    . GLU   B 101 ? 0.4371 0.3833 0.3071 -0.0014 0.0227  -0.0405 98  GLU   B CA    
2102 C  C     . GLU   B 101 ? 0.4294 0.3797 0.2963 -0.0026 0.0211  -0.0326 98  GLU   B C     
2103 O  O     . GLU   B 101 ? 0.4293 0.3856 0.2988 -0.0023 0.0216  -0.0350 98  GLU   B O     
2104 C  CB    . GLU   B 101 ? 0.4453 0.4083 0.3141 -0.0051 0.0241  -0.0448 98  GLU   B CB    
2105 C  CG    . GLU   B 101 ? 0.4553 0.4174 0.3296 -0.0042 0.0263  -0.0561 98  GLU   B CG    
2106 C  CD    . GLU   B 101 ? 0.4663 0.4273 0.3483 -0.0014 0.0278  -0.0644 98  GLU   B CD    
2107 O  OE1   . GLU   B 101 ? 0.4758 0.4525 0.3589 -0.0028 0.0290  -0.0682 98  GLU   B OE1   
2108 O  OE2   . GLU   B 101 ? 0.4792 0.4245 0.3667 0.0021  0.0276  -0.0666 98  GLU   B OE2   
2109 N  N     . GLN   B 102 ? 0.4271 0.3738 0.2896 -0.0040 0.0192  -0.0234 99  GLN   B N     
2110 C  CA    . GLN   B 102 ? 0.4250 0.3741 0.2858 -0.0057 0.0173  -0.0152 99  GLN   B CA    
2111 C  C     . GLN   B 102 ? 0.4204 0.3577 0.2826 -0.0031 0.0166  -0.0151 99  GLN   B C     
2112 O  O     . GLN   B 102 ? 0.4237 0.3683 0.2870 -0.0044 0.0161  -0.0138 99  GLN   B O     
2113 C  CB    . GLN   B 102 ? 0.4302 0.3738 0.2882 -0.0068 0.0154  -0.0059 99  GLN   B CB    
2114 C  CG    . GLN   B 102 ? 0.4326 0.3916 0.2896 -0.0102 0.0155  -0.0032 99  GLN   B CG    
2115 C  CD    . GLN   B 102 ? 0.4383 0.3918 0.2947 -0.0105 0.0136  0.0064  99  GLN   B CD    
2116 O  OE1   . GLN   B 102 ? 0.4430 0.3796 0.2993 -0.0076 0.0129  0.0082  99  GLN   B OE1   
2117 N  NE2   . GLN   B 102 ? 0.4392 0.4085 0.2959 -0.0143 0.0128  0.0126  99  GLN   B NE2   
2118 N  N     . ILE   B 103 ? 0.4136 0.3347 0.2761 0.0002  0.0163  -0.0163 100 ILE   B N     
2119 C  CA    . ILE   B 103 ? 0.4078 0.3187 0.2714 0.0023  0.0152  -0.0153 100 ILE   B CA    
2120 C  C     . ILE   B 103 ? 0.4066 0.3238 0.2753 0.0038  0.0165  -0.0216 100 ILE   B C     
2121 O  O     . ILE   B 103 ? 0.4008 0.3204 0.2706 0.0036  0.0157  -0.0199 100 ILE   B O     
2122 C  CB    . ILE   B 103 ? 0.4069 0.3017 0.2694 0.0050  0.0147  -0.0145 100 ILE   B CB    
2123 C  CG1   . ILE   B 103 ? 0.4061 0.2954 0.2646 0.0040  0.0137  -0.0091 100 ILE   B CG1   
2124 C  CG2   . ILE   B 103 ? 0.4075 0.2948 0.2710 0.0065  0.0134  -0.0132 100 ILE   B CG2   
2125 C  CD1   . ILE   B 103 ? 0.4075 0.2851 0.2648 0.0063  0.0138  -0.0095 100 ILE   B CD1   
2126 N  N     . LYS   B 104 ? 0.4084 0.3281 0.2812 0.0053  0.0185  -0.0290 101 LYS   B N     
2127 C  CA    . LYS   B 104 ? 0.4139 0.3405 0.2937 0.0071  0.0201  -0.0364 101 LYS   B CA    
2128 C  C     . LYS   B 104 ? 0.4136 0.3575 0.2929 0.0044  0.0206  -0.0365 101 LYS   B C     
2129 O  O     . LYS   B 104 ? 0.4130 0.3609 0.2965 0.0058  0.0208  -0.0382 101 LYS   B O     
2130 C  CB    . LYS   B 104 ? 0.4188 0.3472 0.3037 0.0082  0.0223  -0.0454 101 LYS   B CB    
2131 C  CG    . LYS   B 104 ? 0.4254 0.3383 0.3156 0.0117  0.0220  -0.0470 101 LYS   B CG    
2132 C  CD    . LYS   B 104 ? 0.4303 0.3440 0.3274 0.0123  0.0241  -0.0562 101 LYS   B CD    
2133 C  CE    . LYS   B 104 ? 0.4346 0.3662 0.3338 0.0102  0.0266  -0.0652 101 LYS   B CE    
2134 N  NZ    . LYS   B 104 ? 0.4411 0.3731 0.3488 0.0109  0.0288  -0.0761 101 LYS   B NZ    
2135 N  N     . ARG   B 105 ? 0.4136 0.3691 0.2884 0.0005  0.0206  -0.0340 102 ARG   B N     
2136 C  CA    . ARG   B 105 ? 0.4149 0.3894 0.2892 -0.0029 0.0210  -0.0329 102 ARG   B CA    
2137 C  C     . ARG   B 105 ? 0.4074 0.3782 0.2803 -0.0037 0.0187  -0.0251 102 ARG   B C     
2138 O  O     . ARG   B 105 ? 0.4072 0.3869 0.2833 -0.0036 0.0192  -0.0271 102 ARG   B O     
2139 C  CB    . ARG   B 105 ? 0.4218 0.4100 0.2917 -0.0075 0.0209  -0.0295 102 ARG   B CB    
2140 C  CG    . ARG   B 105 ? 0.4280 0.4382 0.2975 -0.0118 0.0211  -0.0272 102 ARG   B CG    
2141 C  CD    . ARG   B 105 ? 0.4364 0.4668 0.3034 -0.0163 0.0219  -0.0270 102 ARG   B CD    
2142 N  NE    . ARG   B 105 ? 0.4435 0.4779 0.3069 -0.0205 0.0191  -0.0140 102 ARG   B NE    
2143 C  CZ    . ARG   B 105 ? 0.4494 0.5048 0.3109 -0.0256 0.0189  -0.0096 102 ARG   B CZ    
2144 N  NH1   . ARG   B 105 ? 0.4498 0.5071 0.3102 -0.0291 0.0160  0.0036  102 ARG   B NH1   
2145 N  NH2   . ARG   B 105 ? 0.4535 0.5287 0.3152 -0.0275 0.0215  -0.0185 102 ARG   B NH2   
2146 N  N     . VAL   B 106 ? 0.4024 0.3603 0.2712 -0.0044 0.0163  -0.0168 103 VAL   B N     
2147 C  CA    . VAL   B 106 ? 0.3997 0.3527 0.2674 -0.0058 0.0139  -0.0097 103 VAL   B CA    
2148 C  C     . VAL   B 106 ? 0.3977 0.3444 0.2689 -0.0024 0.0139  -0.0131 103 VAL   B C     
2149 O  O     . VAL   B 106 ? 0.3962 0.3499 0.2689 -0.0038 0.0132  -0.0114 103 VAL   B O     
2150 C  CB    . VAL   B 106 ? 0.4005 0.3393 0.2645 -0.0066 0.0118  -0.0024 103 VAL   B CB    
2151 C  CG1   . VAL   B 106 ? 0.4017 0.3325 0.2653 -0.0077 0.0094  0.0029  103 VAL   B CG1   
2152 C  CG2   . VAL   B 106 ? 0.4002 0.3472 0.2625 -0.0100 0.0113  0.0029  103 VAL   B CG2   
2153 N  N     . LYS   B 107 ? 0.3984 0.3334 0.2715 0.0016  0.0146  -0.0174 104 LYS   B N     
2154 C  CA    . LYS   B 107 ? 0.4014 0.3304 0.2788 0.0049  0.0142  -0.0193 104 LYS   B CA    
2155 C  C     . LYS   B 107 ? 0.4070 0.3489 0.2916 0.0067  0.0163  -0.0262 104 LYS   B C     
2156 O  O     . LYS   B 107 ? 0.4074 0.3500 0.2964 0.0086  0.0158  -0.0263 104 LYS   B O     
2157 C  CB    . LYS   B 107 ? 0.4009 0.3150 0.2791 0.0082  0.0141  -0.0205 104 LYS   B CB    
2158 C  CG    . LYS   B 107 ? 0.3995 0.3012 0.2715 0.0071  0.0123  -0.0147 104 LYS   B CG    
2159 C  CD    . LYS   B 107 ? 0.4010 0.2992 0.2705 0.0056  0.0101  -0.0096 104 LYS   B CD    
2160 C  CE    . LYS   B 107 ? 0.4018 0.2875 0.2665 0.0052  0.0087  -0.0061 104 LYS   B CE    
2161 N  NZ    . LYS   B 107 ? 0.4048 0.2884 0.2668 0.0024  0.0066  -0.0019 104 LYS   B NZ    
2162 N  N     . ASP   B 108 ? 0.4130 0.3659 0.2992 0.0062  0.0187  -0.0324 105 ASP   B N     
2163 C  CA    . ASP   B 108 ? 0.4175 0.3830 0.3115 0.0082  0.0213  -0.0413 105 ASP   B CA    
2164 C  C     . ASP   B 108 ? 0.4216 0.3756 0.3241 0.0136  0.0216  -0.0453 105 ASP   B C     
2165 O  O     . ASP   B 108 ? 0.4211 0.3809 0.3314 0.0163  0.0224  -0.0491 105 ASP   B O     
2166 C  CB    . ASP   B 108 ? 0.4204 0.4014 0.3155 0.0063  0.0213  -0.0399 105 ASP   B CB    
2167 C  CG    . ASP   B 108 ? 0.4246 0.4214 0.3283 0.0085  0.0244  -0.0501 105 ASP   B CG    
2168 O  OD1   . ASP   B 108 ? 0.4262 0.4268 0.3332 0.0096  0.0268  -0.0588 105 ASP   B OD1   
2169 O  OD2   . ASP   B 108 ? 0.4278 0.4332 0.3354 0.0092  0.0243  -0.0498 105 ASP   B OD2   
2170 N  N     . SER   B 109 ? 0.4276 0.3660 0.3291 0.0150  0.0208  -0.0439 106 SER   B N     
2171 C  CA    . SER   B 109 ? 0.4335 0.3598 0.3430 0.0196  0.0204  -0.0451 106 SER   B CA    
2172 C  C     . SER   B 109 ? 0.4351 0.3505 0.3447 0.0201  0.0207  -0.0469 106 SER   B C     
2173 O  O     . SER   B 109 ? 0.4346 0.3478 0.3357 0.0172  0.0203  -0.0439 106 SER   B O     
2174 C  CB    . SER   B 109 ? 0.4363 0.3541 0.3433 0.0200  0.0175  -0.0364 106 SER   B CB    
2175 O  OG    . SER   B 109 ? 0.4420 0.3497 0.3568 0.0239  0.0166  -0.0357 106 SER   B OG    
2176 N  N     . GLU   B 110 ? 0.4408 0.3495 0.3610 0.0238  0.0213  -0.0511 107 GLU   B N     
2177 C  CA    . GLU   B 110 ? 0.4444 0.3411 0.3658 0.0243  0.0211  -0.0512 107 GLU   B CA    
2178 C  C     . GLU   B 110 ? 0.4409 0.3248 0.3597 0.0251  0.0182  -0.0416 107 GLU   B C     
2179 O  O     . GLU   B 110 ? 0.4421 0.3169 0.3592 0.0246  0.0176  -0.0394 107 GLU   B O     
2180 C  CB    . GLU   B 110 ? 0.4569 0.3516 0.3921 0.0273  0.0229  -0.0600 107 GLU   B CB    
2181 C  CG    . GLU   B 110 ? 0.4634 0.3636 0.3980 0.0250  0.0253  -0.0688 107 GLU   B CG    
2182 C  CD    . GLU   B 110 ? 0.4694 0.3879 0.4004 0.0226  0.0275  -0.0749 107 GLU   B CD    
2183 O  OE1   . GLU   B 110 ? 0.4802 0.4070 0.4155 0.0244  0.0280  -0.0766 107 GLU   B OE1   
2184 O  OE2   . GLU   B 110 ? 0.4768 0.4028 0.4009 0.0189  0.0285  -0.0776 107 GLU   B OE2   
2185 N  N     . ASP   B 111 ? 0.4379 0.3226 0.3563 0.0259  0.0165  -0.0361 108 ASP   B N     
2186 C  CA    . ASP   B 111 ? 0.4343 0.3098 0.3501 0.0262  0.0137  -0.0273 108 ASP   B CA    
2187 C  C     . ASP   B 111 ? 0.4300 0.3035 0.3322 0.0225  0.0126  -0.0223 108 ASP   B C     
2188 O  O     . ASP   B 111 ? 0.4324 0.3082 0.3298 0.0211  0.0112  -0.0180 108 ASP   B O     
2189 C  CB    . ASP   B 111 ? 0.4364 0.3151 0.3577 0.0282  0.0122  -0.0237 108 ASP   B CB    
2190 C  CG    . ASP   B 111 ? 0.4426 0.3206 0.3797 0.0327  0.0126  -0.0265 108 ASP   B CG    
2191 O  OD1   . ASP   B 111 ? 0.4489 0.3222 0.3929 0.0340  0.0140  -0.0315 108 ASP   B OD1   
2192 O  OD2   . ASP   B 111 ? 0.4426 0.3247 0.3859 0.0348  0.0115  -0.0237 108 ASP   B OD2   
2193 N  N     . VAL   B 112 ? 0.4244 0.2938 0.3215 0.0209  0.0133  -0.0231 109 VAL   B N     
2194 C  CA    . VAL   B 112 ? 0.4190 0.2862 0.3053 0.0181  0.0125  -0.0189 109 VAL   B CA    
2195 C  C     . VAL   B 112 ? 0.4188 0.2765 0.3026 0.0183  0.0113  -0.0146 109 VAL   B C     
2196 O  O     . VAL   B 112 ? 0.4209 0.2749 0.3068 0.0187  0.0122  -0.0164 109 VAL   B O     
2197 C  CB    . VAL   B 112 ? 0.4166 0.2887 0.2987 0.0160  0.0141  -0.0222 109 VAL   B CB    
2198 C  CG1   . VAL   B 112 ? 0.4155 0.2855 0.2885 0.0134  0.0131  -0.0173 109 VAL   B CG1   
2199 C  CG2   . VAL   B 112 ? 0.4148 0.2991 0.3002 0.0155  0.0156  -0.0270 109 VAL   B CG2   
2200 N  N     . PRO   B 113 ? 0.4167 0.2716 0.2960 0.0175  0.0094  -0.0093 110 PRO   B N     
2201 C  CA    . PRO   B 113 ? 0.4190 0.2676 0.2948 0.0171  0.0085  -0.0056 110 PRO   B CA    
2202 C  C     . PRO   B 113 ? 0.4176 0.2640 0.2874 0.0157  0.0097  -0.0070 110 PRO   B C     
2203 O  O     . PRO   B 113 ? 0.4141 0.2623 0.2786 0.0142  0.0100  -0.0073 110 PRO   B O     
2204 C  CB    . PRO   B 113 ? 0.4180 0.2674 0.2892 0.0158  0.0066  -0.0015 110 PRO   B CB    
2205 C  CG    . PRO   B 113 ? 0.4186 0.2739 0.2945 0.0164  0.0061  -0.0021 110 PRO   B CG    
2206 C  CD    . PRO   B 113 ? 0.4174 0.2764 0.2950 0.0166  0.0081  -0.0071 110 PRO   B CD    
2207 N  N     . MET   B 114 ? 0.4207 0.2636 0.2926 0.0163  0.0103  -0.0073 111 MET   B N     
2208 C  CA    . MET   B 114 ? 0.4204 0.2625 0.2880 0.0153  0.0116  -0.0089 111 MET   B CA    
2209 C  C     . MET   B 114 ? 0.4181 0.2558 0.2866 0.0154  0.0116  -0.0071 111 MET   B C     
2210 O  O     . MET   B 114 ? 0.4192 0.2550 0.2944 0.0164  0.0110  -0.0061 111 MET   B O     
2211 C  CB    . MET   B 114 ? 0.4281 0.2753 0.2995 0.0152  0.0132  -0.0140 111 MET   B CB    
2212 C  CG    . MET   B 114 ? 0.4322 0.2818 0.2994 0.0138  0.0143  -0.0153 111 MET   B CG    
2213 S  SD    . MET   B 114 ? 0.4421 0.3023 0.3124 0.0127  0.0160  -0.0214 111 MET   B SD    
2214 C  CE    . MET   B 114 ? 0.4408 0.3067 0.3096 0.0122  0.0153  -0.0198 111 MET   B CE    
2215 N  N     . VAL   B 115 ? 0.4112 0.2479 0.2739 0.0145  0.0121  -0.0061 112 VAL   B N     
2216 C  CA    . VAL   B 115 ? 0.4089 0.2432 0.2714 0.0142  0.0123  -0.0044 112 VAL   B CA    
2217 C  C     . VAL   B 115 ? 0.4042 0.2402 0.2639 0.0135  0.0138  -0.0066 112 VAL   B C     
2218 O  O     . VAL   B 115 ? 0.4042 0.2420 0.2596 0.0133  0.0141  -0.0067 112 VAL   B O     
2219 C  CB    . VAL   B 115 ? 0.4099 0.2434 0.2675 0.0138  0.0114  -0.0004 112 VAL   B CB    
2220 C  CG1   . VAL   B 115 ? 0.4109 0.2439 0.2681 0.0132  0.0117  0.0016  112 VAL   B CG1   
2221 C  CG2   . VAL   B 115 ? 0.4117 0.2457 0.2715 0.0140  0.0096  0.0025  112 VAL   B CG2   
2222 N  N     . LEU   B 116 ? 0.4025 0.2384 0.2659 0.0129  0.0144  -0.0080 113 LEU   B N     
2223 C  CA    . LEU   B 116 ? 0.3998 0.2386 0.2610 0.0119  0.0156  -0.0094 113 LEU   B CA    
2224 C  C     . LEU   B 116 ? 0.3981 0.2357 0.2554 0.0119  0.0157  -0.0059 113 LEU   B C     
2225 O  O     . LEU   B 116 ? 0.4016 0.2369 0.2607 0.0116  0.0150  -0.0034 113 LEU   B O     
2226 C  CB    . LEU   B 116 ? 0.4019 0.2417 0.2694 0.0108  0.0163  -0.0132 113 LEU   B CB    
2227 C  CG    . LEU   B 116 ? 0.4007 0.2459 0.2665 0.0092  0.0175  -0.0153 113 LEU   B CG    
2228 C  CD1   . LEU   B 116 ? 0.3984 0.2503 0.2606 0.0089  0.0180  -0.0166 113 LEU   B CD1   
2229 C  CD2   . LEU   B 116 ? 0.4037 0.2497 0.2763 0.0075  0.0180  -0.0200 113 LEU   B CD2   
2230 N  N     . VAL   B 117 ? 0.3956 0.2356 0.2484 0.0121  0.0164  -0.0055 114 VAL   B N     
2231 C  CA    . VAL   B 117 ? 0.3981 0.2380 0.2474 0.0126  0.0168  -0.0031 114 VAL   B CA    
2232 C  C     . VAL   B 117 ? 0.3976 0.2417 0.2467 0.0122  0.0178  -0.0034 114 VAL   B C     
2233 O  O     . VAL   B 117 ? 0.3985 0.2457 0.2473 0.0124  0.0181  -0.0039 114 VAL   B O     
2234 C  CB    . VAL   B 117 ? 0.3985 0.2369 0.2440 0.0139  0.0165  -0.0024 114 VAL   B CB    
2235 C  CG1   . VAL   B 117 ? 0.4009 0.2405 0.2437 0.0148  0.0174  -0.0016 114 VAL   B CG1   
2236 C  CG2   . VAL   B 117 ? 0.4008 0.2367 0.2460 0.0138  0.0153  -0.0018 114 VAL   B CG2   
2237 N  N     . GLY   B 118 ? 0.3986 0.2438 0.2485 0.0114  0.0182  -0.0023 115 GLY   B N     
2238 C  CA    . GLY   B 118 ? 0.3982 0.2483 0.2478 0.0110  0.0191  -0.0018 115 GLY   B CA    
2239 C  C     . GLY   B 118 ? 0.4002 0.2513 0.2467 0.0128  0.0199  0.0001  115 GLY   B C     
2240 O  O     . GLY   B 118 ? 0.4031 0.2546 0.2487 0.0124  0.0200  0.0015  115 GLY   B O     
2241 N  N     . ASN   B 119 ? 0.3991 0.2509 0.2447 0.0147  0.0202  0.0001  116 ASN   B N     
2242 C  CA    . ASN   B 119 ? 0.4019 0.2542 0.2462 0.0171  0.0212  0.0005  116 ASN   B CA    
2243 C  C     . ASN   B 119 ? 0.4012 0.2597 0.2469 0.0176  0.0223  0.0019  116 ASN   B C     
2244 O  O     . ASN   B 119 ? 0.4016 0.2638 0.2488 0.0158  0.0220  0.0025  116 ASN   B O     
2245 C  CB    . ASN   B 119 ? 0.4034 0.2517 0.2478 0.0191  0.0209  -0.0003 116 ASN   B CB    
2246 C  CG    . ASN   B 119 ? 0.4078 0.2552 0.2519 0.0215  0.0219  -0.0018 116 ASN   B CG    
2247 O  OD1   . ASN   B 119 ? 0.4063 0.2549 0.2479 0.0213  0.0225  -0.0032 116 ASN   B OD1   
2248 N  ND2   . ASN   B 119 ? 0.4076 0.2549 0.2553 0.0238  0.0224  -0.0013 116 ASN   B ND2   
2249 N  N     . LYS   B 120 ? 0.4044 0.2650 0.2498 0.0198  0.0235  0.0017  117 LYS   B N     
2250 C  CA    . LYS   B 120 ? 0.4057 0.2731 0.2529 0.0210  0.0248  0.0029  117 LYS   B CA    
2251 C  C     . LYS   B 120 ? 0.4063 0.2780 0.2521 0.0181  0.0249  0.0040  117 LYS   B C     
2252 O  O     . LYS   B 120 ? 0.4058 0.2833 0.2533 0.0173  0.0253  0.0055  117 LYS   B O     
2253 C  CB    . LYS   B 120 ? 0.4035 0.2744 0.2545 0.0221  0.0247  0.0050  117 LYS   B CB    
2254 C  CG    . LYS   B 120 ? 0.4046 0.2711 0.2578 0.0237  0.0238  0.0056  117 LYS   B CG    
2255 C  CD    . LYS   B 120 ? 0.4052 0.2763 0.2639 0.0260  0.0239  0.0090  117 LYS   B CD    
2256 C  CE    . LYS   B 120 ? 0.4080 0.2742 0.2699 0.0271  0.0227  0.0106  117 LYS   B CE    
2257 N  NZ    . LYS   B 120 ? 0.4084 0.2805 0.2761 0.0280  0.0219  0.0161  117 LYS   B NZ    
2258 N  N     . SER   B 121 ? 0.4104 0.2796 0.2539 0.0163  0.0244  0.0038  118 SER   B N     
2259 C  CA    . SER   B 121 ? 0.4117 0.2849 0.2554 0.0132  0.0241  0.0062  118 SER   B CA    
2260 C  C     . SER   B 121 ? 0.4136 0.2956 0.2572 0.0138  0.0257  0.0072  118 SER   B C     
2261 O  O     . SER   B 121 ? 0.4151 0.3017 0.2598 0.0109  0.0256  0.0098  118 SER   B O     
2262 C  CB    . SER   B 121 ? 0.4137 0.2839 0.2562 0.0113  0.0230  0.0074  118 SER   B CB    
2263 O  OG    . SER   B 121 ? 0.4151 0.2883 0.2543 0.0127  0.0238  0.0066  118 SER   B OG    
2264 N  N     . ASP   B 122 ? 0.4131 0.2975 0.2563 0.0175  0.0273  0.0050  119 ASP   B N     
2265 C  CA    . ASP   B 122 ? 0.4141 0.3078 0.2578 0.0190  0.0292  0.0050  119 ASP   B CA    
2266 C  C     . ASP   B 122 ? 0.4122 0.3108 0.2595 0.0197  0.0297  0.0067  119 ASP   B C     
2267 O  O     . ASP   B 122 ? 0.4134 0.3209 0.2620 0.0206  0.0312  0.0073  119 ASP   B O     
2268 C  CB    . ASP   B 122 ? 0.4157 0.3099 0.2593 0.0232  0.0310  0.0006  119 ASP   B CB    
2269 C  CG    . ASP   B 122 ? 0.4166 0.3042 0.2639 0.0267  0.0309  -0.0010 119 ASP   B CG    
2270 O  OD1   . ASP   B 122 ? 0.4163 0.2956 0.2626 0.0261  0.0294  -0.0016 119 ASP   B OD1   
2271 O  OD2   . ASP   B 122 ? 0.4175 0.3088 0.2694 0.0299  0.0320  -0.0008 119 ASP   B OD2   
2272 N  N     . LEU   B 123 ? 0.4114 0.3060 0.2606 0.0192  0.0285  0.0075  120 LEU   B N     
2273 C  CA    . LEU   B 123 ? 0.4104 0.3118 0.2629 0.0194  0.0287  0.0097  120 LEU   B CA    
2274 C  C     . LEU   B 123 ? 0.4070 0.3128 0.2592 0.0144  0.0279  0.0116  120 LEU   B C     
2275 O  O     . LEU   B 123 ? 0.4073 0.3078 0.2587 0.0109  0.0265  0.0111  120 LEU   B O     
2276 C  CB    . LEU   B 123 ? 0.4119 0.3100 0.2666 0.0204  0.0276  0.0102  120 LEU   B CB    
2277 C  CG    . LEU   B 123 ? 0.4145 0.3087 0.2719 0.0253  0.0281  0.0094  120 LEU   B CG    
2278 C  CD1   . LEU   B 123 ? 0.4133 0.3056 0.2729 0.0250  0.0266  0.0115  120 LEU   B CD1   
2279 C  CD2   . LEU   B 123 ? 0.4165 0.3176 0.2785 0.0293  0.0299  0.0101  120 LEU   B CD2   
2280 N  N     . PRO   B 124 ? 0.4033 0.3192 0.2573 0.0138  0.0288  0.0136  121 PRO   B N     
2281 C  CA    . PRO   B 124 ? 0.4043 0.3246 0.2589 0.0085  0.0280  0.0154  121 PRO   B CA    
2282 C  C     . PRO   B 124 ? 0.4032 0.3252 0.2597 0.0052  0.0267  0.0152  121 PRO   B C     
2283 O  O     . PRO   B 124 ? 0.4054 0.3285 0.2629 0.0002  0.0258  0.0153  121 PRO   B O     
2284 C  CB    . PRO   B 124 ? 0.4040 0.3357 0.2597 0.0094  0.0296  0.0174  121 PRO   B CB    
2285 C  CG    . PRO   B 124 ? 0.4038 0.3384 0.2620 0.0152  0.0308  0.0169  121 PRO   B CG    
2286 C  CD    . PRO   B 124 ? 0.4046 0.3281 0.2612 0.0182  0.0306  0.0141  121 PRO   B CD    
2287 N  N     . SER   B 125 ? 0.3997 0.3231 0.2574 0.0076  0.0266  0.0151  122 SER   B N     
2288 C  CA    . SER   B 125 ? 0.4005 0.3289 0.2595 0.0041  0.0255  0.0148  122 SER   B CA    
2289 C  C     . SER   B 125 ? 0.4003 0.3205 0.2582 0.0027  0.0244  0.0115  122 SER   B C     
2290 O  O     . SER   B 125 ? 0.3983 0.3196 0.2564 0.0042  0.0240  0.0118  122 SER   B O     
2291 C  CB    . SER   B 125 ? 0.3986 0.3369 0.2603 0.0066  0.0256  0.0180  122 SER   B CB    
2292 O  OG    . SER   B 125 ? 0.4000 0.3481 0.2636 0.0068  0.0266  0.0206  122 SER   B OG    
2293 N  N     . ARG   B 126 ? 0.4034 0.3162 0.2608 -0.0003 0.0239  0.0090  123 ARG   B N     
2294 C  CA    . ARG   B 126 ? 0.4058 0.3106 0.2629 -0.0011 0.0230  0.0054  123 ARG   B CA    
2295 C  C     . ARG   B 126 ? 0.4040 0.3150 0.2629 -0.0051 0.0225  0.0021  123 ARG   B C     
2296 O  O     . ARG   B 126 ? 0.4050 0.3238 0.2656 -0.0088 0.0224  0.0017  123 ARG   B O     
2297 C  CB    . ARG   B 126 ? 0.4108 0.3058 0.2685 -0.0021 0.0226  0.0044  123 ARG   B CB    
2298 C  CG    . ARG   B 126 ? 0.4166 0.3106 0.2783 -0.0072 0.0219  0.0030  123 ARG   B CG    
2299 C  CD    . ARG   B 126 ? 0.4215 0.3066 0.2844 -0.0071 0.0212  0.0048  123 ARG   B CD    
2300 N  NE    . ARG   B 126 ? 0.4223 0.2993 0.2850 -0.0052 0.0207  0.0023  123 ARG   B NE    
2301 C  CZ    . ARG   B 126 ? 0.4224 0.2936 0.2834 -0.0026 0.0204  0.0042  123 ARG   B CZ    
2302 N  NH1   . ARG   B 126 ? 0.4240 0.2892 0.2854 -0.0012 0.0199  0.0016  123 ARG   B NH1   
2303 N  NH2   . ARG   B 126 ? 0.4229 0.2956 0.2817 -0.0018 0.0206  0.0084  123 ARG   B NH2   
2304 N  N     . THR   B 127 ? 0.4026 0.3116 0.2609 -0.0045 0.0221  -0.0004 124 THR   B N     
2305 C  CA    . THR   B 127 ? 0.4011 0.3173 0.2605 -0.0082 0.0218  -0.0047 124 THR   B CA    
2306 C  C     . THR   B 127 ? 0.4072 0.3153 0.2683 -0.0095 0.0216  -0.0105 124 THR   B C     
2307 O  O     . THR   B 127 ? 0.4120 0.3248 0.2755 -0.0133 0.0216  -0.0163 124 THR   B O     
2308 C  CB    . THR   B 127 ? 0.3970 0.3223 0.2549 -0.0067 0.0215  -0.0018 124 THR   B CB    
2309 O  OG1   . THR   B 127 ? 0.3957 0.3134 0.2523 -0.0032 0.0214  -0.0009 124 THR   B OG1   
2310 C  CG2   . THR   B 127 ? 0.3949 0.3281 0.2531 -0.0046 0.0216  0.0045  124 THR   B CG2   
2311 N  N     . VAL   B 128 ? 0.4107 0.3076 0.2710 -0.0062 0.0215  -0.0094 125 VAL   B N     
2312 C  CA    . VAL   B 128 ? 0.4153 0.3039 0.2784 -0.0066 0.0212  -0.0140 125 VAL   B CA    
2313 C  C     . VAL   B 128 ? 0.4236 0.3031 0.2900 -0.0072 0.0208  -0.0130 125 VAL   B C     
2314 O  O     . VAL   B 128 ? 0.4216 0.2959 0.2860 -0.0046 0.0206  -0.0085 125 VAL   B O     
2315 C  CB    . VAL   B 128 ? 0.4135 0.2978 0.2741 -0.0032 0.0210  -0.0133 125 VAL   B CB    
2316 C  CG1   . VAL   B 128 ? 0.4148 0.2932 0.2790 -0.0037 0.0209  -0.0184 125 VAL   B CG1   
2317 C  CG2   . VAL   B 128 ? 0.4114 0.3054 0.2693 -0.0028 0.0211  -0.0119 125 VAL   B CG2   
2318 N  N     . ASP   B 129 ? 0.4369 0.3159 0.3090 -0.0111 0.0206  -0.0172 126 ASP   B N     
2319 C  CA    . ASP   B 129 ? 0.4469 0.3178 0.3245 -0.0127 0.0198  -0.0156 126 ASP   B CA    
2320 C  C     . ASP   B 129 ? 0.4489 0.3096 0.3290 -0.0101 0.0191  -0.0149 126 ASP   B C     
2321 O  O     . ASP   B 129 ? 0.4477 0.3071 0.3295 -0.0092 0.0193  -0.0199 126 ASP   B O     
2322 C  CB    . ASP   B 129 ? 0.4608 0.3320 0.3462 -0.0176 0.0196  -0.0216 126 ASP   B CB    
2323 C  CG    . ASP   B 129 ? 0.4685 0.3518 0.3514 -0.0208 0.0202  -0.0234 126 ASP   B CG    
2324 O  OD1   . ASP   B 129 ? 0.4795 0.3666 0.3606 -0.0218 0.0200  -0.0183 126 ASP   B OD1   
2325 O  OD2   . ASP   B 129 ? 0.4778 0.3682 0.3604 -0.0222 0.0208  -0.0295 126 ASP   B OD2   
2326 N  N     . THR   B 130 ? 0.4532 0.3089 0.3336 -0.0091 0.0182  -0.0086 127 THR   B N     
2327 C  CA    . THR   B 130 ? 0.4555 0.3029 0.3385 -0.0069 0.0173  -0.0065 127 THR   B CA    
2328 C  C     . THR   B 130 ? 0.4578 0.2993 0.3503 -0.0079 0.0168  -0.0122 127 THR   B C     
2329 O  O     . THR   B 130 ? 0.4579 0.2964 0.3508 -0.0054 0.0168  -0.0140 127 THR   B O     
2330 C  CB    . THR   B 130 ? 0.4593 0.3055 0.3415 -0.0070 0.0163  0.0015  127 THR   B CB    
2331 O  OG1   . THR   B 130 ? 0.4597 0.3133 0.3338 -0.0060 0.0174  0.0038  127 THR   B OG1   
2332 C  CG2   . THR   B 130 ? 0.4608 0.3023 0.3425 -0.0042 0.0154  0.0047  127 THR   B CG2   
2333 N  N     . LYS   B 131 ? 0.4621 0.3026 0.3625 -0.0116 0.0166  -0.0155 128 LYS   B N     
2334 C  CA    . LYS   B 131 ? 0.4668 0.3011 0.3782 -0.0123 0.0164  -0.0221 128 LYS   B CA    
2335 C  C     . LYS   B 131 ? 0.4647 0.3034 0.3737 -0.0107 0.0179  -0.0306 128 LYS   B C     
2336 O  O     . LYS   B 131 ? 0.4709 0.3046 0.3865 -0.0089 0.0178  -0.0342 128 LYS   B O     
2337 C  CB    . LYS   B 131 ? 0.4735 0.3054 0.3952 -0.0169 0.0160  -0.0257 128 LYS   B CB    
2338 C  CG    . LYS   B 131 ? 0.4773 0.3040 0.4110 -0.0173 0.0164  -0.0353 128 LYS   B CG    
2339 C  CD    . LYS   B 131 ? 0.9142 0.7362 0.8604 -0.0220 0.0157  -0.0388 128 LYS   B CD    
2340 C  CE    . LYS   B 131 ? 0.9212 0.7356 0.8823 -0.0216 0.0160  -0.0480 128 LYS   B CE    
2341 N  NZ    . LYS   B 131 ? 0.9192 0.7418 0.8769 -0.0208 0.0183  -0.0600 128 LYS   B NZ    
2342 N  N     . GLN   B 132 ? 0.4584 0.3074 0.3592 -0.0116 0.0191  -0.0332 129 GLN   B N     
2343 C  CA    . GLN   B 132 ? 0.4539 0.3096 0.3524 -0.0108 0.0204  -0.0403 129 GLN   B CA    
2344 C  C     . GLN   B 132 ? 0.4443 0.2970 0.3390 -0.0064 0.0202  -0.0370 129 GLN   B C     
2345 O  O     . GLN   B 132 ? 0.4432 0.2973 0.3407 -0.0054 0.0208  -0.0428 129 GLN   B O     
2346 C  CB    . GLN   B 132 ? 0.4560 0.3246 0.3457 -0.0121 0.0213  -0.0404 129 GLN   B CB    
2347 C  CG    . GLN   B 132 ? 0.4641 0.3403 0.3547 -0.0167 0.0216  -0.0429 129 GLN   B CG    
2348 C  CD    . GLN   B 132 ? 0.4670 0.3575 0.3496 -0.0176 0.0222  -0.0421 129 GLN   B CD    
2349 O  OE1   . GLN   B 132 ? 0.4723 0.3711 0.3536 -0.0181 0.0229  -0.0470 129 GLN   B OE1   
2350 N  NE2   . GLN   B 132 ? 0.4655 0.3601 0.3435 -0.0179 0.0218  -0.0355 129 GLN   B NE2   
2351 N  N     . ALA   B 133 ? 0.4346 0.2847 0.3231 -0.0042 0.0194  -0.0286 130 ALA   B N     
2352 C  CA    . ALA   B 133 ? 0.4270 0.2744 0.3112 -0.0006 0.0190  -0.0250 130 ALA   B CA    
2353 C  C     . ALA   B 133 ? 0.4261 0.2648 0.3181 0.0009  0.0180  -0.0246 130 ALA   B C     
2354 O  O     . ALA   B 133 ? 0.4217 0.2599 0.3147 0.0030  0.0180  -0.0267 130 ALA   B O     
2355 C  CB    . ALA   B 133 ? 0.4241 0.2718 0.3007 0.0006  0.0186  -0.0176 130 ALA   B CB    
2356 N  N     . GLN   B 134 ? 0.4286 0.2615 0.3268 -0.0003 0.0169  -0.0212 131 GLN   B N     
2357 C  CA    . GLN   B 134 ? 0.4299 0.2548 0.3377 0.0009  0.0156  -0.0193 131 GLN   B CA    
2358 C  C     . GLN   B 134 ? 0.4329 0.2567 0.3498 0.0015  0.0164  -0.0283 131 GLN   B C     
2359 O  O     . GLN   B 134 ? 0.4365 0.2572 0.3577 0.0043  0.0160  -0.0284 131 GLN   B O     
2360 C  CB    . GLN   B 134 ? 0.4331 0.2531 0.3479 -0.0015 0.0141  -0.0140 131 GLN   B CB    
2361 C  CG    . GLN   B 134 ? 0.4311 0.2530 0.3384 -0.0017 0.0132  -0.0044 131 GLN   B CG    
2362 C  CD    . GLN   B 134 ? 0.4380 0.2564 0.3533 -0.0043 0.0114  0.0022  131 GLN   B CD    
2363 O  OE1   . GLN   B 134 ? 0.4427 0.2579 0.3673 -0.0070 0.0113  -0.0008 131 GLN   B OE1   
2364 N  NE2   . GLN   B 134 ? 0.4376 0.2574 0.3498 -0.0040 0.0101  0.0112  131 GLN   B NE2   
2365 N  N     . ASP   B 135 ? 0.4368 0.2644 0.3566 -0.0012 0.0178  -0.0364 132 ASP   B N     
2366 C  CA    . ASP   B 135 ? 0.4419 0.2701 0.3713 -0.0011 0.0190  -0.0471 132 ASP   B CA    
2367 C  C     . ASP   B 135 ? 0.4362 0.2712 0.3600 0.0014  0.0201  -0.0506 132 ASP   B C     
2368 O  O     . ASP   B 135 ? 0.4355 0.2690 0.3671 0.0035  0.0206  -0.0556 132 ASP   B O     
2369 C  CB    . ASP   B 135 ? 0.4472 0.2806 0.3794 -0.0054 0.0203  -0.0557 132 ASP   B CB    
2370 C  CG    . ASP   B 135 ? 0.4566 0.2823 0.3981 -0.0083 0.0191  -0.0540 132 ASP   B CG    
2371 O  OD1   . ASP   B 135 ? 0.4608 0.2768 0.4090 -0.0069 0.0173  -0.0463 132 ASP   B OD1   
2372 O  OD2   . ASP   B 135 ? 0.4619 0.2926 0.4042 -0.0125 0.0200  -0.0598 132 ASP   B OD2   
2373 N  N     . LEU   B 136 ? 0.4315 0.2743 0.3426 0.0011  0.0205  -0.0475 133 LEU   B N     
2374 C  CA    . LEU   B 136 ? 0.4269 0.2768 0.3324 0.0027  0.0213  -0.0492 133 LEU   B CA    
2375 C  C     . LEU   B 136 ? 0.4263 0.2697 0.3330 0.0064  0.0201  -0.0440 133 LEU   B C     
2376 O  O     . LEU   B 136 ? 0.4260 0.2717 0.3366 0.0081  0.0207  -0.0483 133 LEU   B O     
2377 C  CB    . LEU   B 136 ? 0.4241 0.2822 0.3175 0.0015  0.0214  -0.0451 133 LEU   B CB    
2378 C  CG    . LEU   B 136 ? 0.4216 0.2890 0.3093 0.0021  0.0221  -0.0461 133 LEU   B CG    
2379 C  CD1   . LEU   B 136 ? 0.4248 0.3025 0.3169 0.0003  0.0238  -0.0562 133 LEU   B CD1   
2380 C  CD2   . LEU   B 136 ? 0.4175 0.2910 0.2956 0.0011  0.0218  -0.0402 133 LEU   B CD2   
2381 N  N     . ALA   B 137 ? 0.4266 0.2633 0.3304 0.0073  0.0184  -0.0351 134 ALA   B N     
2382 C  CA    . ALA   B 137 ? 0.4261 0.2582 0.3302 0.0101  0.0170  -0.0294 134 ALA   B CA    
2383 C  C     . ALA   B 137 ? 0.4327 0.2593 0.3505 0.0119  0.0165  -0.0318 134 ALA   B C     
2384 O  O     . ALA   B 137 ? 0.4300 0.2569 0.3503 0.0144  0.0162  -0.0316 134 ALA   B O     
2385 C  CB    . ALA   B 137 ? 0.4254 0.2539 0.3240 0.0100  0.0156  -0.0204 134 ALA   B CB    
2386 N  N     . ARG   B 138 ? 0.4408 0.2627 0.3683 0.0105  0.0165  -0.0343 135 ARG   B N     
2387 C  CA    . ARG   B 138 ? 0.4524 0.2682 0.3956 0.0122  0.0161  -0.0373 135 ARG   B CA    
2388 C  C     . ARG   B 138 ? 0.4500 0.2713 0.3977 0.0138  0.0181  -0.0479 135 ARG   B C     
2389 O  O     . ARG   B 138 ? 0.4528 0.2716 0.4099 0.0169  0.0178  -0.0486 135 ARG   B O     
2390 C  CB    . ARG   B 138 ? 0.4638 0.2737 0.4166 0.0095  0.0158  -0.0388 135 ARG   B CB    
2391 C  CG    . ARG   B 138 ? 0.4780 0.2788 0.4496 0.0112  0.0146  -0.0391 135 ARG   B CG    
2392 C  CD    . ARG   B 138 ? 0.4918 0.2860 0.4736 0.0079  0.0140  -0.0398 135 ARG   B CD    
2393 N  NE    . ARG   B 138 ? 0.4955 0.2899 0.4684 0.0048  0.0126  -0.0301 135 ARG   B NE    
2394 C  CZ    . ARG   B 138 ? 0.5000 0.2984 0.4659 0.0009  0.0135  -0.0326 135 ARG   B CZ    
2395 N  NH1   . ARG   B 138 ? 0.5048 0.3061 0.4739 -0.0012 0.0155  -0.0443 135 ARG   B NH1   
2396 N  NH2   . ARG   B 138 ? 0.4976 0.2982 0.4535 -0.0009 0.0125  -0.0236 135 ARG   B NH2   
2397 N  N     . SER   B 139 ? 0.4493 0.2798 0.3906 0.0115  0.0202  -0.0558 136 SER   B N     
2398 C  CA    . SER   B 139 ? 0.4522 0.2914 0.3970 0.0123  0.0225  -0.0667 136 SER   B CA    
2399 C  C     . SER   B 139 ? 0.4485 0.2928 0.3874 0.0149  0.0223  -0.0634 136 SER   B C     
2400 O  O     . SER   B 139 ? 0.4538 0.3027 0.3993 0.0169  0.0235  -0.0699 136 SER   B O     
2401 C  CB    . SER   B 139 ? 0.4511 0.3016 0.3901 0.0085  0.0245  -0.0748 136 SER   B CB    
2402 O  OG    . SER   B 139 ? 0.4432 0.3005 0.3671 0.0070  0.0241  -0.0683 136 SER   B OG    
2403 N  N     . TYR   B 140 ? 0.4430 0.2864 0.3704 0.0148  0.0207  -0.0536 137 TYR   B N     
2404 C  CA    . TYR   B 140 ? 0.4391 0.2865 0.3609 0.0166  0.0202  -0.0497 137 TYR   B CA    
2405 C  C     . TYR   B 140 ? 0.4380 0.2774 0.3659 0.0197  0.0182  -0.0430 137 TYR   B C     
2406 O  O     . TYR   B 140 ? 0.4393 0.2822 0.3659 0.0214  0.0178  -0.0413 137 TYR   B O     
2407 C  CB    . TYR   B 140 ? 0.4384 0.2889 0.3457 0.0149  0.0196  -0.0433 137 TYR   B CB    
2408 C  CG    . TYR   B 140 ? 0.4389 0.2995 0.3394 0.0119  0.0211  -0.0473 137 TYR   B CG    
2409 C  CD1   . TYR   B 140 ? 0.4411 0.3120 0.3453 0.0108  0.0231  -0.0565 137 TYR   B CD1   
2410 C  CD2   . TYR   B 140 ? 0.4387 0.2999 0.3293 0.0103  0.0205  -0.0415 137 TYR   B CD2   
2411 C  CE1   . TYR   B 140 ? 0.4412 0.3236 0.3389 0.0075  0.0241  -0.0591 137 TYR   B CE1   
2412 C  CE2   . TYR   B 140 ? 0.4391 0.3105 0.3242 0.0076  0.0215  -0.0435 137 TYR   B CE2   
2413 C  CZ    . TYR   B 140 ? 0.4394 0.3220 0.3277 0.0060  0.0232  -0.0518 137 TYR   B CZ    
2414 O  OH    . TYR   B 140 ? 0.4403 0.3350 0.3231 0.0029  0.0239  -0.0527 137 TYR   B OH    
2415 N  N     . GLY   B 141 ? 0.4361 0.2664 0.3706 0.0199  0.0168  -0.0386 138 GLY   B N     
2416 C  CA    . GLY   B 141 ? 0.4361 0.2603 0.3760 0.0221  0.0144  -0.0302 138 GLY   B CA    
2417 C  C     . GLY   B 141 ? 0.4305 0.2557 0.3577 0.0213  0.0128  -0.0212 138 GLY   B C     
2418 O  O     . GLY   B 141 ? 0.4320 0.2578 0.3596 0.0229  0.0113  -0.0160 138 GLY   B O     
2419 N  N     . ILE   B 142 ? 0.4222 0.2484 0.3385 0.0187  0.0132  -0.0197 139 ILE   B N     
2420 C  CA    . ILE   B 142 ? 0.4185 0.2459 0.3234 0.0180  0.0121  -0.0130 139 ILE   B CA    
2421 C  C     . ILE   B 142 ? 0.4160 0.2401 0.3181 0.0162  0.0113  -0.0075 139 ILE   B C     
2422 O  O     . ILE   B 142 ? 0.4158 0.2375 0.3224 0.0150  0.0118  -0.0095 139 ILE   B O     
2423 C  CB    . ILE   B 142 ? 0.4156 0.2489 0.3099 0.0170  0.0134  -0.0161 139 ILE   B CB    
2424 C  CG1   . ILE   B 142 ? 0.4149 0.2501 0.3056 0.0150  0.0149  -0.0196 139 ILE   B CG1   
2425 C  CG2   . ILE   B 142 ? 0.4148 0.2533 0.3120 0.0182  0.0142  -0.0209 139 ILE   B CG2   
2426 C  CD1   . ILE   B 142 ? 0.4115 0.2525 0.2927 0.0139  0.0157  -0.0202 139 ILE   B CD1   
2427 N  N     . PRO   B 143 ? 0.4107 0.2357 0.3055 0.0157  0.0100  -0.0010 140 PRO   B N     
2428 C  CA    . PRO   B 143 ? 0.4096 0.2340 0.3005 0.0139  0.0096  0.0036  140 PRO   B CA    
2429 C  C     . PRO   B 143 ? 0.4041 0.2305 0.2872 0.0127  0.0114  -0.0001 140 PRO   B C     
2430 O  O     . PRO   B 143 ? 0.4016 0.2307 0.2794 0.0131  0.0125  -0.0039 140 PRO   B O     
2431 C  CB    . PRO   B 143 ? 0.4096 0.2369 0.2944 0.0137  0.0081  0.0098  140 PRO   B CB    
2432 C  CG    . PRO   B 143 ? 0.4102 0.2383 0.2983 0.0154  0.0072  0.0096  140 PRO   B CG    
2433 C  CD    . PRO   B 143 ? 0.4087 0.2364 0.2990 0.0166  0.0089  0.0019  140 PRO   B CD    
2434 N  N     . PHE   B 144 ? 0.4037 0.2296 0.2873 0.0110  0.0115  0.0019  141 PHE   B N     
2435 C  CA    . PHE   B 144 ? 0.4008 0.2295 0.2774 0.0098  0.0130  0.0003  141 PHE   B CA    
2436 C  C     . PHE   B 144 ? 0.4044 0.2353 0.2757 0.0090  0.0125  0.0060  141 PHE   B C     
2437 O  O     . PHE   B 144 ? 0.4069 0.2372 0.2827 0.0077  0.0112  0.0111  141 PHE   B O     
2438 C  CB    . PHE   B 144 ? 0.4006 0.2287 0.2828 0.0082  0.0138  -0.0034 141 PHE   B CB    
2439 C  CG    . PHE   B 144 ? 0.3974 0.2295 0.2739 0.0067  0.0149  -0.0035 141 PHE   B CG    
2440 C  CD1   . PHE   B 144 ? 0.3937 0.2300 0.2628 0.0075  0.0160  -0.0055 141 PHE   B CD1   
2441 C  CD2   . PHE   B 144 ? 0.3989 0.2309 0.2786 0.0044  0.0147  -0.0013 141 PHE   B CD2   
2442 C  CE1   . PHE   B 144 ? 0.3923 0.2329 0.2574 0.0066  0.0170  -0.0051 141 PHE   B CE1   
2443 C  CE2   . PHE   B 144 ? 0.3977 0.2345 0.2725 0.0032  0.0157  -0.0013 141 PHE   B CE2   
2444 C  CZ    . PHE   B 144 ? 0.3942 0.2353 0.2619 0.0045  0.0169  -0.0033 141 PHE   B CZ    
2445 N  N     . ILE   B 145 ? 0.4043 0.2384 0.2672 0.0095  0.0136  0.0050  142 ILE   B N     
2446 C  CA    . ILE   B 145 ? 0.4089 0.2468 0.2664 0.0089  0.0138  0.0085  142 ILE   B CA    
2447 C  C     . ILE   B 145 ? 0.4108 0.2516 0.2640 0.0093  0.0155  0.0059  142 ILE   B C     
2448 O  O     . ILE   B 145 ? 0.4098 0.2502 0.2610 0.0106  0.0163  0.0027  142 ILE   B O     
2449 C  CB    . ILE   B 145 ? 0.4092 0.2485 0.2619 0.0098  0.0131  0.0097  142 ILE   B CB    
2450 C  CG1   . ILE   B 145 ? 0.4111 0.2498 0.2685 0.0092  0.0111  0.0138  142 ILE   B CG1   
2451 C  CG2   . ILE   B 145 ? 0.4095 0.2542 0.2560 0.0095  0.0140  0.0106  142 ILE   B CG2   
2452 C  CD1   . ILE   B 145 ? 0.4116 0.2529 0.2647 0.0095  0.0102  0.0146  142 ILE   B CD1   
2453 N  N     . GLU   B 146 ? 0.4186 0.2631 0.2710 0.0081  0.0160  0.0083  143 GLU   B N     
2454 C  CA    . GLU   B 146 ? 0.4217 0.2702 0.2704 0.0089  0.0177  0.0067  143 GLU   B CA    
2455 C  C     . GLU   B 146 ? 0.4257 0.2774 0.2691 0.0103  0.0183  0.0069  143 GLU   B C     
2456 O  O     . GLU   B 146 ? 0.4314 0.2857 0.2736 0.0093  0.0177  0.0096  143 GLU   B O     
2457 C  CB    . GLU   B 146 ? 0.4265 0.2781 0.2781 0.0067  0.0180  0.0083  143 GLU   B CB    
2458 C  CG    . GLU   B 146 ? 0.4295 0.2793 0.2854 0.0056  0.0180  0.0052  143 GLU   B CG    
2459 C  CD    . GLU   B 146 ? 0.4332 0.2872 0.2912 0.0033  0.0186  0.0053  143 GLU   B CD    
2460 O  OE1   . GLU   B 146 ? 0.4380 0.2967 0.2940 0.0029  0.0191  0.0081  143 GLU   B OE1   
2461 O  OE2   . GLU   B 146 ? 0.4377 0.2911 0.2995 0.0017  0.0185  0.0022  143 GLU   B OE2   
2462 N  N     . THR   B 147 ? 0.4272 0.2790 0.2682 0.0126  0.0195  0.0039  144 THR   B N     
2463 C  CA    . THR   B 147 ? 0.4295 0.2836 0.2667 0.0142  0.0204  0.0022  144 THR   B CA    
2464 C  C     . THR   B 147 ? 0.4310 0.2886 0.2682 0.0163  0.0223  0.0006  144 THR   B C     
2465 O  O     . THR   B 147 ? 0.4301 0.2885 0.2697 0.0164  0.0226  0.0014  144 THR   B O     
2466 C  CB    . THR   B 147 ? 0.4281 0.2773 0.2643 0.0154  0.0198  -0.0003 144 THR   B CB    
2467 O  OG1   . THR   B 147 ? 0.4287 0.2744 0.2669 0.0166  0.0199  -0.0014 144 THR   B OG1   
2468 C  CG2   . THR   B 147 ? 0.4295 0.2766 0.2657 0.0138  0.0180  0.0012  144 THR   B CG2   
2469 N  N     . SER   B 148 ? 0.4351 0.2960 0.2702 0.0177  0.0235  -0.0019 145 SER   B N     
2470 C  CA    . SER   B 148 ? 0.4387 0.3026 0.2753 0.0207  0.0255  -0.0043 145 SER   B CA    
2471 C  C     . SER   B 148 ? 0.4448 0.3066 0.2809 0.0227  0.0262  -0.0092 145 SER   B C     
2472 O  O     . SER   B 148 ? 0.4503 0.3158 0.2831 0.0216  0.0265  -0.0113 145 SER   B O     
2473 C  CB    . SER   B 148 ? 0.4411 0.3139 0.2773 0.0203  0.0269  -0.0033 145 SER   B CB    
2474 O  OG    . SER   B 148 ? 0.4433 0.3190 0.2820 0.0238  0.0289  -0.0062 145 SER   B OG    
2475 N  N     . ALA   B 149 ? 0.4469 0.3027 0.2865 0.0250  0.0261  -0.0105 146 ALA   B N     
2476 C  CA    . ALA   B 149 ? 0.4485 0.3008 0.2896 0.0269  0.0268  -0.0156 146 ALA   B CA    
2477 C  C     . ALA   B 149 ? 0.4522 0.3104 0.2954 0.0297  0.0294  -0.0198 146 ALA   B C     
2478 O  O     . ALA   B 149 ? 0.4626 0.3206 0.3065 0.0308  0.0304  -0.0258 146 ALA   B O     
2479 C  CB    . ALA   B 149 ? 0.4468 0.2914 0.2927 0.0283  0.0258  -0.0146 146 ALA   B CB    
2480 N  N     . LYS   B 150 ? 0.4493 0.3137 0.2939 0.0306  0.0304  -0.0171 147 LYS   B N     
2481 C  CA    . LYS   B 150 ? 0.4522 0.3239 0.2994 0.0334  0.0330  -0.0207 147 LYS   B CA    
2482 C  C     . LYS   B 150 ? 0.4573 0.3390 0.2989 0.0314  0.0343  -0.0236 147 LYS   B C     
2483 O  O     . LYS   B 150 ? 0.4619 0.3487 0.3049 0.0334  0.0366  -0.0301 147 LYS   B O     
2484 C  CB    . LYS   B 150 ? 0.4496 0.3258 0.3000 0.0345  0.0334  -0.0159 147 LYS   B CB    
2485 C  CG    . LYS   B 150 ? 0.4508 0.3342 0.3064 0.0385  0.0360  -0.0187 147 LYS   B CG    
2486 C  CD    . LYS   B 150 ? 0.4507 0.3346 0.3124 0.0406  0.0357  -0.0136 147 LYS   B CD    
2487 C  CE    . LYS   B 150 ? 0.4502 0.3454 0.3148 0.0427  0.0378  -0.0134 147 LYS   B CE    
2488 N  NZ    . LYS   B 150 ? 0.4581 0.3561 0.3288 0.0477  0.0406  -0.0201 147 LYS   B NZ    
2489 N  N     . THR   B 151 ? 0.4567 0.3420 0.2930 0.0272  0.0328  -0.0188 148 THR   B N     
2490 C  CA    . THR   B 151 ? 0.4587 0.3557 0.2901 0.0244  0.0336  -0.0192 148 THR   B CA    
2491 C  C     . THR   B 151 ? 0.4638 0.3596 0.2905 0.0213  0.0319  -0.0197 148 THR   B C     
2492 O  O     . THR   B 151 ? 0.4691 0.3757 0.2916 0.0187  0.0323  -0.0201 148 THR   B O     
2493 C  CB    . THR   B 151 ? 0.4544 0.3580 0.2847 0.0215  0.0329  -0.0121 148 THR   B CB    
2494 O  OG1   . THR   B 151 ? 0.4495 0.3459 0.2792 0.0186  0.0301  -0.0064 148 THR   B OG1   
2495 C  CG2   . THR   B 151 ? 0.4516 0.3575 0.2863 0.0240  0.0343  -0.0109 148 THR   B CG2   
2496 N  N     . ARG   B 152 ? 0.4643 0.3487 0.2920 0.0214  0.0300  -0.0193 149 ARG   B N     
2497 C  CA    . ARG   B 152 ? 0.4685 0.3502 0.2928 0.0187  0.0281  -0.0191 149 ARG   B CA    
2498 C  C     . ARG   B 152 ? 0.4625 0.3459 0.2851 0.0152  0.0257  -0.0111 149 ARG   B C     
2499 O  O     . ARG   B 152 ? 0.4694 0.3524 0.2900 0.0130  0.0240  -0.0097 149 ARG   B O     
2500 C  CB    . ARG   B 152 ? 0.4774 0.3650 0.2993 0.0186  0.0294  -0.0268 149 ARG   B CB    
2501 C  CG    . ARG   B 152 ? 0.4832 0.3700 0.3018 0.0157  0.0276  -0.0280 149 ARG   B CG    
2502 C  CD    . ARG   B 152 ? 0.4925 0.3878 0.3090 0.0155  0.0296  -0.0371 149 ARG   B CD    
2503 N  NE    . ARG   B 152 ? 0.4987 0.3845 0.3169 0.0158  0.0288  -0.0419 149 ARG   B NE    
2504 C  CZ    . ARG   B 152 ? 0.5012 0.3861 0.3165 0.0127  0.0264  -0.0396 149 ARG   B CZ    
2505 N  NH1   . ARG   B 152 ? 0.5016 0.3943 0.3128 0.0095  0.0247  -0.0325 149 ARG   B NH1   
2506 N  NH2   . ARG   B 152 ? 0.5050 0.3812 0.3222 0.0127  0.0256  -0.0436 149 ARG   B NH2   
2507 N  N     . GLN   B 153 ? 0.4568 0.3411 0.2814 0.0148  0.0257  -0.0062 150 GLN   B N     
2508 C  CA    . GLN   B 153 ? 0.4481 0.3327 0.2735 0.0116  0.0235  0.0012  150 GLN   B CA    
2509 C  C     . GLN   B 153 ? 0.4415 0.3160 0.2687 0.0112  0.0213  0.0027  150 GLN   B C     
2510 O  O     . GLN   B 153 ? 0.4372 0.3039 0.2669 0.0131  0.0214  0.0012  150 GLN   B O     
2511 C  CB    . GLN   B 153 ? 0.4498 0.3358 0.2781 0.0115  0.0242  0.0041  150 GLN   B CB    
2512 C  CG    . GLN   B 153 ? 0.4523 0.3439 0.2819 0.0077  0.0228  0.0111  150 GLN   B CG    
2513 C  CD    . GLN   B 153 ? 0.4547 0.3600 0.2809 0.0056  0.0235  0.0127  150 GLN   B CD    
2514 O  OE1   . GLN   B 153 ? 0.4588 0.3682 0.2831 0.0032  0.0221  0.0155  150 GLN   B OE1   
2515 N  NE2   . GLN   B 153 ? 0.4571 0.3711 0.2827 0.0061  0.0256  0.0115  150 GLN   B NE2   
2516 N  N     . ARG   B 154 ? 0.4331 0.3096 0.2592 0.0089  0.0195  0.0058  151 ARG   B N     
2517 C  CA    . ARG   B 154 ? 0.4281 0.2974 0.2566 0.0084  0.0172  0.0079  151 ARG   B CA    
2518 C  C     . ARG   B 154 ? 0.4262 0.2886 0.2539 0.0105  0.0174  0.0026  151 ARG   B C     
2519 O  O     . ARG   B 154 ? 0.4241 0.2803 0.2542 0.0106  0.0161  0.0037  151 ARG   B O     
2520 C  CB    . ARG   B 154 ? 0.4243 0.2882 0.2584 0.0079  0.0162  0.0120  151 ARG   B CB    
2521 C  CG    . ARG   B 154 ? 0.4245 0.2943 0.2611 0.0053  0.0156  0.0180  151 ARG   B CG    
2522 C  CD    . ARG   B 154 ? 0.4238 0.2873 0.2677 0.0042  0.0140  0.0218  151 ARG   B CD    
2523 N  NE    . ARG   B 154 ? 0.4282 0.2905 0.2746 0.0035  0.0118  0.0252  151 ARG   B NE    
2524 C  CZ    . ARG   B 154 ? 0.4292 0.2852 0.2830 0.0035  0.0101  0.0276  151 ARG   B CZ    
2525 N  NH1   . ARG   B 154 ? 0.4291 0.2789 0.2886 0.0037  0.0104  0.0260  151 ARG   B NH1   
2526 N  NH2   . ARG   B 154 ? 0.4307 0.2872 0.2867 0.0033  0.0082  0.0310  151 ARG   B NH2   
2527 N  N     . VAL   B 155 ? 0.4267 0.2907 0.2515 0.0117  0.0190  -0.0029 152 VAL   B N     
2528 C  CA    . VAL   B 155 ? 0.4271 0.2837 0.2524 0.0132  0.0189  -0.0072 152 VAL   B CA    
2529 C  C     . VAL   B 155 ? 0.4304 0.2870 0.2543 0.0113  0.0169  -0.0066 152 VAL   B C     
2530 O  O     . VAL   B 155 ? 0.4268 0.2772 0.2528 0.0116  0.0158  -0.0059 152 VAL   B O     
2531 C  CB    . VAL   B 155 ? 0.4282 0.2848 0.2533 0.0154  0.0209  -0.0135 152 VAL   B CB    
2532 C  CG1   . VAL   B 155 ? 0.4299 0.2789 0.2566 0.0161  0.0203  -0.0168 152 VAL   B CG1   
2533 C  CG2   . VAL   B 155 ? 0.4262 0.2821 0.2542 0.0178  0.0225  -0.0131 152 VAL   B CG2   
2534 N  N     . GLU   B 156 ? 0.4377 0.3029 0.2580 0.0092  0.0167  -0.0071 153 GLU   B N     
2535 C  CA    . GLU   B 156 ? 0.4427 0.3104 0.2615 0.0069  0.0146  -0.0057 153 GLU   B CA    
2536 C  C     . GLU   B 156 ? 0.4410 0.3062 0.2637 0.0064  0.0125  0.0016  153 GLU   B C     
2537 O  O     . GLU   B 156 ? 0.4405 0.3018 0.2652 0.0064  0.0110  0.0026  153 GLU   B O     
2538 C  CB    . GLU   B 156 ? 0.4519 0.3325 0.2660 0.0042  0.0148  -0.0067 153 GLU   B CB    
2539 C  CG    . GLU   B 156 ? 0.4584 0.3410 0.2699 0.0049  0.0172  -0.0159 153 GLU   B CG    
2540 C  CD    . GLU   B 156 ? 0.4703 0.3664 0.2769 0.0016  0.0173  -0.0193 153 GLU   B CD    
2541 O  OE1   . GLU   B 156 ? 0.4734 0.3818 0.2776 -0.0008 0.0167  -0.0142 153 GLU   B OE1   
2542 O  OE2   . GLU   B 156 ? 0.4791 0.3739 0.2845 0.0011  0.0178  -0.0270 153 GLU   B OE2   
2543 N  N     . ASP   B 157 ? 0.4401 0.3076 0.2650 0.0062  0.0126  0.0063  154 ASP   B N     
2544 C  CA    . ASP   B 157 ? 0.4397 0.3044 0.2701 0.0059  0.0109  0.0126  154 ASP   B CA    
2545 C  C     . ASP   B 157 ? 0.4297 0.2843 0.2640 0.0080  0.0107  0.0104  154 ASP   B C     
2546 O  O     . ASP   B 157 ? 0.4269 0.2795 0.2652 0.0080  0.0090  0.0130  154 ASP   B O     
2547 C  CB    . ASP   B 157 ? 0.4465 0.3139 0.2789 0.0053  0.0115  0.0162  154 ASP   B CB    
2548 C  CG    . ASP   B 157 ? 0.4528 0.3216 0.2913 0.0036  0.0092  0.0243  154 ASP   B CG    
2549 O  OD1   . ASP   B 157 ? 0.4564 0.3191 0.3002 0.0045  0.0078  0.0256  154 ASP   B OD1   
2550 O  OD2   . ASP   B 157 ? 0.4594 0.3360 0.2981 0.0013  0.0089  0.0294  154 ASP   B OD2   
2551 N  N     . ALA   B 158 ? 0.4225 0.2722 0.2562 0.0098  0.0124  0.0059  155 ALA   B N     
2552 C  CA    . ALA   B 158 ? 0.4172 0.2601 0.2543 0.0112  0.0124  0.0043  155 ALA   B CA    
2553 C  C     . ALA   B 158 ? 0.4162 0.2577 0.2527 0.0110  0.0113  0.0030  155 ALA   B C     
2554 O  O     . ALA   B 158 ? 0.4152 0.2550 0.2558 0.0112  0.0102  0.0044  155 ALA   B O     
2555 C  CB    . ALA   B 158 ? 0.4152 0.2557 0.2515 0.0126  0.0142  0.0009  155 ALA   B CB    
2556 N  N     . PHE   B 159 ? 0.4182 0.2610 0.2505 0.0106  0.0116  -0.0001 156 PHE   B N     
2557 C  CA    . PHE   B 159 ? 0.4183 0.2602 0.2498 0.0098  0.0104  -0.0017 156 PHE   B CA    
2558 C  C     . PHE   B 159 ? 0.4182 0.2651 0.2505 0.0082  0.0084  0.0022  156 PHE   B C     
2559 O  O     . PHE   B 159 ? 0.4162 0.2619 0.2510 0.0082  0.0072  0.0030  156 PHE   B O     
2560 C  CB    . PHE   B 159 ? 0.4224 0.2646 0.2502 0.0093  0.0113  -0.0066 156 PHE   B CB    
2561 C  CG    . PHE   B 159 ? 0.4235 0.2598 0.2528 0.0111  0.0128  -0.0096 156 PHE   B CG    
2562 C  CD1   . PHE   B 159 ? 0.4239 0.2554 0.2557 0.0112  0.0122  -0.0099 156 PHE   B CD1   
2563 C  CD2   . PHE   B 159 ? 0.4249 0.2618 0.2538 0.0125  0.0146  -0.0115 156 PHE   B CD2   
2564 C  CE1   . PHE   B 159 ? 0.4224 0.2498 0.2568 0.0126  0.0131  -0.0110 156 PHE   B CE1   
2565 C  CE2   . PHE   B 159 ? 0.4254 0.2576 0.2571 0.0144  0.0157  -0.0131 156 PHE   B CE2   
2566 C  CZ    . PHE   B 159 ? 0.4229 0.2503 0.2575 0.0144  0.0148  -0.0125 156 PHE   B CZ    
2567 N  N     . TYR   B 160 ? 0.4216 0.2752 0.2522 0.0068  0.0080  0.0050  157 TYR   B N     
2568 C  CA    . TYR   B 160 ? 0.4233 0.2836 0.2549 0.0050  0.0057  0.0100  157 TYR   B CA    
2569 C  C     . TYR   B 160 ? 0.4169 0.2740 0.2563 0.0064  0.0044  0.0149  157 TYR   B C     
2570 O  O     . TYR   B 160 ? 0.4184 0.2776 0.2609 0.0061  0.0026  0.0178  157 TYR   B O     
2571 C  CB    . TYR   B 160 ? 0.4317 0.3020 0.2600 0.0028  0.0055  0.0128  157 TYR   B CB    
2572 C  CG    . TYR   B 160 ? 0.4429 0.3193 0.2641 0.0010  0.0066  0.0069  157 TYR   B CG    
2573 C  CD1   . TYR   B 160 ? 0.4472 0.3172 0.2663 0.0021  0.0083  -0.0009 157 TYR   B CD1   
2574 C  CD2   . TYR   B 160 ? 0.4512 0.3406 0.2687 -0.0020 0.0060  0.0091  157 TYR   B CD2   
2575 C  CE1   . TYR   B 160 ? 0.4557 0.3307 0.2700 0.0006  0.0095  -0.0075 157 TYR   B CE1   
2576 C  CE2   . TYR   B 160 ? 0.4594 0.3558 0.2708 -0.0039 0.0073  0.0022  157 TYR   B CE2   
2577 C  CZ    . TYR   B 160 ? 0.4602 0.3487 0.2704 -0.0023 0.0092  -0.0068 157 TYR   B CZ    
2578 O  OH    . TYR   B 160 ? 0.4714 0.3666 0.2772 -0.0041 0.0106  -0.0146 157 TYR   B OH    
2579 N  N     . THR   B 161 ? 0.4107 0.2629 0.2538 0.0079  0.0055  0.0154  158 THR   B N     
2580 C  CA    . THR   B 161 ? 0.4074 0.2554 0.2593 0.0095  0.0048  0.0179  158 THR   B CA    
2581 C  C     . THR   B 161 ? 0.4030 0.2473 0.2570 0.0109  0.0049  0.0143  158 THR   B C     
2582 O  O     . THR   B 161 ? 0.4027 0.2470 0.2637 0.0119  0.0037  0.0165  158 THR   B O     
2583 C  CB    . THR   B 161 ? 0.4056 0.2493 0.2603 0.0102  0.0062  0.0172  158 THR   B CB    
2584 O  OG1   . THR   B 161 ? 0.4080 0.2566 0.2613 0.0084  0.0058  0.0215  158 THR   B OG1   
2585 C  CG2   . THR   B 161 ? 0.4043 0.2435 0.2689 0.0116  0.0058  0.0178  158 THR   B CG2   
2586 N  N     . LEU   B 162 ? 0.4010 0.2432 0.2502 0.0110  0.0062  0.0092  159 LEU   B N     
2587 C  CA    . LEU   B 162 ? 0.3995 0.2399 0.2503 0.0118  0.0063  0.0063  159 LEU   B CA    
2588 C  C     . LEU   B 162 ? 0.4033 0.2476 0.2538 0.0108  0.0045  0.0080  159 LEU   B C     
2589 O  O     . LEU   B 162 ? 0.4020 0.2471 0.2574 0.0117  0.0039  0.0083  159 LEU   B O     
2590 C  CB    . LEU   B 162 ? 0.3986 0.2363 0.2448 0.0117  0.0078  0.0022  159 LEU   B CB    
2591 C  CG    . LEU   B 162 ? 0.3968 0.2343 0.2444 0.0117  0.0080  0.0000  159 LEU   B CG    
2592 C  CD1   . LEU   B 162 ? 0.3946 0.2330 0.2484 0.0131  0.0084  -0.0007 159 LEU   B CD1   
2593 C  CD2   . LEU   B 162 ? 0.3976 0.2328 0.2420 0.0115  0.0091  -0.0022 159 LEU   B CD2   
2594 N  N     . VAL   B 163 ? 0.4083 0.2564 0.2536 0.0088  0.0037  0.0089  160 VAL   B N     
2595 C  CA    . VAL   B 163 ? 0.4136 0.2674 0.2583 0.0072  0.0018  0.0109  160 VAL   B CA    
2596 C  C     . VAL   B 163 ? 0.4145 0.2716 0.2669 0.0083  0.0001  0.0169  160 VAL   B C     
2597 O  O     . VAL   B 163 ? 0.4135 0.2731 0.2699 0.0087  -0.0012 0.0181  160 VAL   B O     
2598 C  CB    . VAL   B 163 ? 0.4183 0.2775 0.2560 0.0043  0.0014  0.0100  160 VAL   B CB    
2599 C  CG1   . VAL   B 163 ? 0.4208 0.2885 0.2582 0.0020  -0.0010 0.0131  160 VAL   B CG1   
2600 C  CG2   . VAL   B 163 ? 0.4194 0.2744 0.2520 0.0036  0.0029  0.0034  160 VAL   B CG2   
2601 N  N     . ARG   B 164 ? 0.4192 0.2764 0.2749 0.0088  -0.0001 0.0209  161 ARG   B N     
2602 C  CA    . ARG   B 164 ? 0.4228 0.2822 0.2880 0.0100  -0.0019 0.0275  161 ARG   B CA    
2603 C  C     . ARG   B 164 ? 0.4202 0.2743 0.2941 0.0131  -0.0013 0.0250  161 ARG   B C     
2604 O  O     . ARG   B 164 ? 0.4194 0.2762 0.3010 0.0144  -0.0028 0.0283  161 ARG   B O     
2605 C  CB    . ARG   B 164 ? 0.4283 0.2878 0.2964 0.0096  -0.0022 0.0324  161 ARG   B CB    
2606 C  CG    . ARG   B 164 ? 0.4359 0.3052 0.2981 0.0063  -0.0036 0.0373  161 ARG   B CG    
2607 C  CD    . ARG   B 164 ? 0.4423 0.3126 0.3031 0.0051  -0.0029 0.0397  161 ARG   B CD    
2608 N  NE    . ARG   B 164 ? 0.4492 0.3321 0.3061 0.0016  -0.0045 0.0459  161 ARG   B NE    
2609 C  CZ    . ARG   B 164 ? 0.4515 0.3393 0.3076 -0.0003 -0.0045 0.0502  161 ARG   B CZ    
2610 N  NH1   . ARG   B 164 ? 0.4518 0.3321 0.3096 0.0010  -0.0027 0.0481  161 ARG   B NH1   
2611 N  NH2   . ARG   B 164 ? 0.4561 0.3578 0.3096 -0.0037 -0.0063 0.0568  161 ARG   B NH2   
2612 N  N     . GLU   B 165 ? 0.4205 0.2686 0.2932 0.0141  0.0010  0.0191  162 GLU   B N     
2613 C  CA    . GLU   B 165 ? 0.4207 0.2659 0.3008 0.0166  0.0021  0.0152  162 GLU   B CA    
2614 C  C     . GLU   B 165 ? 0.4200 0.2691 0.2999 0.0168  0.0016  0.0136  162 GLU   B C     
2615 O  O     . GLU   B 165 ? 0.4174 0.2679 0.3060 0.0190  0.0015  0.0131  162 GLU   B O     
2616 C  CB    . GLU   B 165 ? 0.4201 0.2610 0.2973 0.0167  0.0045  0.0094  162 GLU   B CB    
2617 C  CG    . GLU   B 165 ? 0.4238 0.2609 0.3036 0.0167  0.0050  0.0104  162 GLU   B CG    
2618 C  CD    . GLU   B 165 ? 0.4267 0.2613 0.3192 0.0185  0.0046  0.0116  162 GLU   B CD    
2619 O  OE1   . GLU   B 165 ? 0.4253 0.2587 0.3236 0.0201  0.0059  0.0061  162 GLU   B OE1   
2620 O  OE2   . GLU   B 165 ? 0.4309 0.2653 0.3281 0.0182  0.0029  0.0181  162 GLU   B OE2   
2621 N  N     . ILE   B 166 ? 0.4219 0.2731 0.2926 0.0144  0.0014  0.0124  163 ILE   B N     
2622 C  CA    . ILE   B 166 ? 0.4228 0.2780 0.2929 0.0138  0.0009  0.0110  163 ILE   B CA    
2623 C  C     . ILE   B 166 ? 0.4256 0.2868 0.3010 0.0141  -0.0014 0.0163  163 ILE   B C     
2624 O  O     . ILE   B 166 ? 0.4260 0.2906 0.3082 0.0158  -0.0018 0.0164  163 ILE   B O     
2625 C  CB    . ILE   B 166 ? 0.4214 0.2765 0.2820 0.0108  0.0010  0.0087  163 ILE   B CB    
2626 C  CG1   . ILE   B 166 ? 0.4207 0.2706 0.2777 0.0108  0.0031  0.0047  163 ILE   B CG1   
2627 C  CG2   . ILE   B 166 ? 0.4223 0.2820 0.2830 0.0095  0.0001  0.0082  163 ILE   B CG2   
2628 C  CD1   . ILE   B 166 ? 0.4217 0.2697 0.2713 0.0084  0.0031  0.0029  163 ILE   B CD1   
2629 N  N     . ARG   B 167 ? 0.4326 0.2964 0.3051 0.0124  -0.0030 0.0210  164 ARG   B N     
2630 C  CA    . ARG   B 167 ? 0.4387 0.3100 0.3153 0.0120  -0.0056 0.0274  164 ARG   B CA    
2631 C  C     . ARG   B 167 ? 0.4423 0.3131 0.3326 0.0158  -0.0062 0.0308  164 ARG   B C     
2632 O  O     . ARG   B 167 ? 0.4475 0.3241 0.3438 0.0168  -0.0077 0.0340  164 ARG   B O     
2633 C  CB    . ARG   B 167 ? 0.4416 0.3170 0.3127 0.0092  -0.0068 0.0319  164 ARG   B CB    
2634 C  CG    . ARG   B 167 ? 0.4471 0.3334 0.3208 0.0076  -0.0099 0.0393  164 ARG   B CG    
2635 C  CD    . ARG   B 167 ? 0.4513 0.3435 0.3216 0.0051  -0.0110 0.0447  164 ARG   B CD    
2636 N  NE    . ARG   B 167 ? 0.4521 0.3460 0.3099 0.0016  -0.0099 0.0391  164 ARG   B NE    
2637 C  CZ    . ARG   B 167 ? 0.4558 0.3511 0.3083 -0.0001 -0.0090 0.0390  164 ARG   B CZ    
2638 N  NH1   . ARG   B 167 ? 0.4551 0.3484 0.3132 0.0014  -0.0091 0.0442  164 ARG   B NH1   
2639 N  NH2   . ARG   B 167 ? 0.4591 0.3580 0.3015 -0.0032 -0.0081 0.0333  164 ARG   B NH2   
2640 N  N     . GLN   B 168 ? 0.4470 0.3109 0.3430 0.0181  -0.0048 0.0297  165 GLN   B N     
2641 C  CA    . GLN   B 168 ? 0.4532 0.3152 0.3643 0.0219  -0.0052 0.0321  165 GLN   B CA    
2642 C  C     . GLN   B 168 ? 0.4489 0.3110 0.3656 0.0246  -0.0036 0.0254  165 GLN   B C     
2643 O  O     . GLN   B 168 ? 0.4519 0.3171 0.3802 0.0275  -0.0045 0.0275  165 GLN   B O     
2644 C  CB    . GLN   B 168 ? 0.4602 0.3149 0.3761 0.0226  -0.0045 0.0325  165 GLN   B CB    
2645 C  CG    . GLN   B 168 ? 0.4696 0.3272 0.3838 0.0202  -0.0067 0.0413  165 GLN   B CG    
2646 C  CD    . GLN   B 168 ? 0.4760 0.3271 0.3919 0.0198  -0.0057 0.0414  165 GLN   B CD    
2647 O  OE1   . GLN   B 168 ? 0.4815 0.3338 0.3874 0.0169  -0.0054 0.0422  165 GLN   B OE1   
2648 N  NE2   . GLN   B 168 ? 0.4825 0.3271 0.4116 0.0225  -0.0053 0.0402  165 GLN   B NE2   
2649 N  N     . TYR   B 169 ? 0.4436 0.3036 0.3525 0.0236  -0.0012 0.0179  166 TYR   B N     
2650 C  CA    . TYR   B 169 ? 0.4411 0.3040 0.3538 0.0253  0.0005  0.0117  166 TYR   B CA    
2651 C  C     . TYR   B 169 ? 0.4401 0.3112 0.3521 0.0247  -0.0010 0.0141  166 TYR   B C     
2652 O  O     . TYR   B 169 ? 0.4408 0.3165 0.3599 0.0269  -0.0002 0.0111  166 TYR   B O     
2653 C  CB    . TYR   B 169 ? 0.4391 0.3000 0.3430 0.0236  0.0029  0.0050  166 TYR   B CB    
2654 C  CG    . TYR   B 169 ? 0.4416 0.2977 0.3504 0.0251  0.0051  -0.0002 166 TYR   B CG    
2655 C  CD1   . TYR   B 169 ? 0.4450 0.3031 0.3651 0.0282  0.0065  -0.0053 166 TYR   B CD1   
2656 C  CD2   . TYR   B 169 ? 0.4409 0.2916 0.3437 0.0235  0.0058  -0.0006 166 TYR   B CD2   
2657 C  CE1   . TYR   B 169 ? 0.4462 0.3007 0.3714 0.0291  0.0085  -0.0111 166 TYR   B CE1   
2658 C  CE2   . TYR   B 169 ? 0.4427 0.2900 0.3500 0.0244  0.0076  -0.0055 166 TYR   B CE2   
2659 C  CZ    . TYR   B 169 ? 0.4465 0.2956 0.3649 0.0270  0.0089  -0.0110 166 TYR   B CZ    
2660 O  OH    . TYR   B 169 ? 0.4497 0.2962 0.3732 0.0274  0.0108  -0.0170 166 TYR   B OH    
2661 N  N     . ARG   B 170 ? 0.4421 0.3162 0.3461 0.0215  -0.0031 0.0190  167 ARG   B N     
2662 C  CA    . ARG   B 170 ? 0.4425 0.3253 0.3461 0.0203  -0.0049 0.0216  167 ARG   B CA    
2663 C  C     . ARG   B 170 ? 0.4477 0.3357 0.3649 0.0237  -0.0066 0.0269  167 ARG   B C     
2664 O  O     . ARG   B 170 ? 0.4495 0.3452 0.3703 0.0243  -0.0072 0.0274  167 ARG   B O     
2665 C  CB    . ARG   B 170 ? 0.4430 0.3284 0.3354 0.0156  -0.0067 0.0246  167 ARG   B CB    
2666 C  CG    . ARG   B 170 ? 0.4442 0.3263 0.3252 0.0122  -0.0054 0.0192  167 ARG   B CG    
2667 C  CD    . ARG   B 170 ? 0.4467 0.3309 0.3180 0.0077  -0.0069 0.0205  167 ARG   B CD    
2668 N  NE    . ARG   B 170 ? 0.4479 0.3285 0.3114 0.0048  -0.0058 0.0154  167 ARG   B NE    
2669 C  CZ    . ARG   B 170 ? 0.4525 0.3299 0.3078 0.0018  -0.0057 0.0132  167 ARG   B CZ    
2670 N  NH1   . ARG   B 170 ? 0.4566 0.3358 0.3090 0.0009  -0.0065 0.0153  167 ARG   B NH1   
2671 N  NH2   . ARG   B 170 ? 0.4549 0.3280 0.3059 -0.0002 -0.0048 0.0090  167 ARG   B NH2   
2672 N  N     . LEU   B 171 ? 0.4563 0.3407 0.3819 0.0260  -0.0074 0.0316  168 LEU   B N     
2673 C  CA    . LEU   B 171 ? 0.4630 0.3518 0.4039 0.0296  -0.0095 0.0382  168 LEU   B CA    
2674 C  C     . LEU   B 171 ? 0.4688 0.3539 0.4243 0.0349  -0.0073 0.0327  168 LEU   B C     
2675 O  O     . LEU   B 171 ? 0.4762 0.3641 0.4470 0.0388  -0.0085 0.0366  168 LEU   B O     
2676 C  CB    . LEU   B 171 ? 0.4675 0.3550 0.4122 0.0291  -0.0119 0.0474  168 LEU   B CB    
2677 C  CG    . LEU   B 171 ? 0.4672 0.3604 0.3988 0.0238  -0.0139 0.0528  168 LEU   B CG    
2678 C  CD1   . LEU   B 171 ? 0.4732 0.3676 0.4112 0.0235  -0.0164 0.0629  168 LEU   B CD1   
2679 C  CD2   . LEU   B 171 ? 0.4662 0.3709 0.3937 0.0215  -0.0158 0.0552  168 LEU   B CD2   
2680 N  N     . LYS   B 172 ? 0.4707 0.3502 0.4221 0.0349  -0.0042 0.0235  169 LYS   B N     
2681 C  CA    . LYS   B 172 ? 0.4764 0.3533 0.4400 0.0391  -0.0016 0.0161  169 LYS   B CA    
2682 C  C     . LYS   B 172 ? 0.4791 0.3639 0.4396 0.0391  0.0004  0.0087  169 LYS   B C     
2683 O  O     . LYS   B 172 ? 0.4835 0.3712 0.4298 0.0351  0.0007  0.0075  169 LYS   B O     
2684 C  CB    . LYS   B 172 ? 0.4753 0.3427 0.4365 0.0384  0.0003  0.0110  169 LYS   B CB    
2685 C  CG    . LYS   B 172 ? 0.4791 0.3437 0.4532 0.0422  0.0030  0.0021  169 LYS   B CG    
2686 C  CD    . LYS   B 172 ? 0.4802 0.3387 0.4482 0.0402  0.0054  -0.0049 169 LYS   B CD    
2687 C  CE    . LYS   B 172 ? 0.4810 0.3408 0.4585 0.0428  0.0086  -0.0164 169 LYS   B CE    
2688 N  NZ    . LYS   B 172 ? 0.4813 0.3524 0.4543 0.0426  0.0103  -0.0219 169 LYS   B NZ    
2689 O  OXT   . LYS   B 172 ? 0.4854 0.3743 0.4583 0.0431  0.0019  0.0041  169 LYS   B OXT   
2690 P  PB    . GDP   C .   ? 0.0365 0.2610 0.2462 -0.0070 0.0346  0.0121  201 GDP   A PB    
2691 O  O1B   . GDP   C .   ? 0.0282 0.2507 0.2413 -0.0068 0.0295  0.0116  201 GDP   A O1B   
2692 O  O2B   . GDP   C .   ? 0.0398 0.2525 0.2397 -0.0034 0.0357  0.0117  201 GDP   A O2B   
2693 O  O3B   . GDP   C .   ? 0.0331 0.2758 0.2517 -0.0032 0.0389  0.0113  201 GDP   A O3B   
2694 O  O3A   . GDP   C .   ? 0.0440 0.2637 0.2483 -0.0165 0.0357  0.0141  201 GDP   A O3A   
2695 P  PA    . GDP   C .   ? 0.0487 0.2691 0.2562 -0.0250 0.0332  0.0149  201 GDP   A PA    
2696 O  O1A   . GDP   C .   ? 0.0469 0.2512 0.2487 -0.0253 0.0271  0.0145  201 GDP   A O1A   
2697 O  O2A   . GDP   C .   ? 0.0403 0.2790 0.2605 -0.0256 0.0331  0.0136  201 GDP   A O2A   
2698 O  "O5'" . GDP   C .   ? 0.0612 0.2765 0.2606 -0.0329 0.0372  0.0179  201 GDP   A "O5'" 
2699 C  "C5'" . GDP   C .   ? 0.0653 0.2956 0.2679 -0.0357 0.0445  0.0190  201 GDP   A "C5'" 
2700 C  "C4'" . GDP   C .   ? 0.0796 0.3057 0.2758 -0.0474 0.0476  0.0227  201 GDP   A "C4'" 
2701 O  "O4'" . GDP   C .   ? 0.0908 0.2951 0.2704 -0.0482 0.0462  0.0253  201 GDP   A "O4'" 
2702 C  "C3'" . GDP   C .   ? 0.0822 0.3067 0.2835 -0.0562 0.0432  0.0230  201 GDP   A "C3'" 
2703 O  "O3'" . GDP   C .   ? 0.0929 0.3248 0.2957 -0.0684 0.0479  0.0259  201 GDP   A "O3'" 
2704 C  "C2'" . GDP   C .   ? 0.0895 0.2867 0.2767 -0.0565 0.0373  0.0243  201 GDP   A "C2'" 
2705 O  "O2'" . GDP   C .   ? 0.1032 0.2896 0.2871 -0.0664 0.0343  0.0259  201 GDP   A "O2'" 
2706 C  "C1'" . GDP   C .   ? 0.0984 0.2867 0.2724 -0.0550 0.0412  0.0273  201 GDP   A "C1'" 
2707 N  N9    . GDP   C .   ? 0.1014 0.2679 0.2630 -0.0489 0.0353  0.0275  201 GDP   A N9    
2708 C  C8    . GDP   C .   ? 0.0895 0.2543 0.2545 -0.0401 0.0307  0.0242  201 GDP   A C8    
2709 N  N7    . GDP   C .   ? 0.0961 0.2434 0.2500 -0.0366 0.0260  0.0250  201 GDP   A N7    
2710 C  C5    . GDP   C .   ? 0.1138 0.2496 0.2553 -0.0430 0.0274  0.0294  201 GDP   A C5    
2711 C  C6    . GDP   C .   ? 0.1317 0.2465 0.2558 -0.0431 0.0239  0.0331  201 GDP   A C6    
2712 O  O6    . GDP   C .   ? 0.1295 0.2350 0.2495 -0.0358 0.0178  0.0317  201 GDP   A O6    
2713 N  N1    . GDP   C .   ? 0.1509 0.2577 0.2638 -0.0515 0.0273  0.0384  201 GDP   A N1    
2714 C  C2    . GDP   C .   ? 0.1525 0.2720 0.2713 -0.0605 0.0343  0.0399  201 GDP   A C2    
2715 N  N2    . GDP   C .   ? 0.1724 0.2847 0.2798 -0.0700 0.0385  0.0457  201 GDP   A N2    
2716 N  N3    . GDP   C .   ? 0.1355 0.2763 0.2713 -0.0602 0.0374  0.0362  201 GDP   A N3    
2717 C  C4    . GDP   C .   ? 0.1167 0.2656 0.2636 -0.0518 0.0341  0.0312  201 GDP   A C4    
2718 MG MG    . MG    D .   ? 0.0186 0.2569 0.2441 -0.0014 0.0259  0.0106  202 MG    A MG    
2719 O  OBB   . A1ILA E .   ? 0.0731 0.2604 0.2921 -0.0043 0.0348  -0.0074 203 A1ILA A OBB   
2720 C  CAS   . A1ILA E .   ? 0.0746 0.2607 0.2925 -0.0044 0.0340  -0.0070 203 A1ILA A CAS   
2721 C  CAT   . A1ILA E .   ? 0.0770 0.2612 0.2923 -0.0048 0.0327  -0.0068 203 A1ILA A CAT   
2722 C  CAZ   . A1ILA E .   ? 0.0764 0.2619 0.2923 -0.0057 0.0313  -0.0068 203 A1ILA A CAZ   
2723 C  CAU   . A1ILA E .   ? 0.0804 0.2614 0.2921 -0.0046 0.0329  -0.0065 203 A1ILA A CAU   
2724 O  OBA   . A1ILA E .   ? 0.0811 0.2615 0.2921 -0.0040 0.0343  -0.0064 203 A1ILA A OBA   
2725 C  CAV   . A1ILA E .   ? 0.0833 0.2620 0.2919 -0.0051 0.0316  -0.0062 203 A1ILA A CAV   
2726 C  CAW   . A1ILA E .   ? 0.0828 0.2628 0.2919 -0.0062 0.0301  -0.0063 203 A1ILA A CAW   
2727 C  CAX   . A1ILA E .   ? 0.0793 0.2629 0.2922 -0.0065 0.0300  -0.0065 203 A1ILA A CAX   
2728 S  SAI   . A1ILA E .   ? 0.0787 0.2653 0.2924 -0.0083 0.0281  -0.0066 203 A1ILA A SAI   
2729 O  OAH   . A1ILA E .   ? 0.0770 0.2647 0.2920 -0.0090 0.0284  -0.0070 203 A1ILA A OAH   
2730 O  OAY   . A1ILA E .   ? 0.0828 0.2666 0.2922 -0.0095 0.0270  -0.0062 203 A1ILA A OAY   
2731 N  NAJ   . A1ILA E .   ? 0.0761 0.2667 0.2935 -0.0075 0.0277  -0.0065 203 A1ILA A NAJ   
2732 C  CAK   . A1ILA E .   ? 0.0776 0.2686 0.2942 -0.0070 0.0268  -0.0061 203 A1ILA A CAK   
2733 S  SBK   . A1ILA E .   ? 0.0818 0.2703 0.2942 -0.0080 0.0255  -0.0057 203 A1ILA A SBK   
2734 C  CAF   . A1ILA E .   ? 0.0813 0.2725 0.2954 -0.0061 0.0248  -0.0055 203 A1ILA A CAF   
2735 C  CAE   . A1ILA E .   ? 0.0838 0.2748 0.2960 -0.0057 0.0236  -0.0052 203 A1ILA A CAE   
2736 CL CLBI  . A1ILA E .   ? 0.0876 0.2756 0.2955 -0.0076 0.0228  -0.0048 203 A1ILA A CLBI  
2737 C  CAD   . A1ILA E .   ? 0.0840 0.2768 0.2971 -0.0036 0.0230  -0.0051 203 A1ILA A CAD   
2738 C  CAC   . A1ILA E .   ? 0.0818 0.2761 0.2975 -0.0021 0.0237  -0.0054 203 A1ILA A CAC   
2739 C  CAB   . A1ILA E .   ? 0.0790 0.2735 0.2968 -0.0030 0.0249  -0.0057 203 A1ILA A CAB   
2740 O  OAA   . A1ILA E .   ? 0.0771 0.2728 0.2972 -0.0017 0.0255  -0.0060 203 A1ILA A OAA   
2741 C  CAG   . A1ILA E .   ? 0.0786 0.2718 0.2958 -0.0048 0.0255  -0.0058 203 A1ILA A CAG   
2742 N  NAL   . A1ILA E .   ? 0.0763 0.2696 0.2951 -0.0056 0.0266  -0.0061 203 A1ILA A NAL   
2743 C  CAM   . A1ILA E .   ? 0.0733 0.2683 0.2953 -0.0047 0.0276  -0.0064 203 A1ILA A CAM   
2744 C  CAN   . A1ILA E .   ? 0.0743 0.2657 0.2953 -0.0036 0.0290  -0.0063 203 A1ILA A CAN   
2745 C  CAO   . A1ILA E .   ? 0.0746 0.2633 0.2943 -0.0043 0.0305  -0.0064 203 A1ILA A CAO   
2746 C  CAP   . A1ILA E .   ? 0.0757 0.2621 0.2945 -0.0038 0.0318  -0.0063 203 A1ILA A CAP   
2747 C  CAQ   . A1ILA E .   ? 0.0770 0.2613 0.2938 -0.0041 0.0332  -0.0063 203 A1ILA A CAQ   
2748 N  NAR   . A1ILA E .   ? 0.0745 0.2607 0.2933 -0.0043 0.0342  -0.0067 203 A1ILA A NAR   
2749 C  CBC   . A1ILA E .   ? 0.0728 0.2605 0.2935 -0.0044 0.0356  -0.0069 203 A1ILA A CBC   
2750 C  CBD   . A1ILA E .   ? 0.0727 0.2603 0.2944 -0.0044 0.0352  -0.0068 203 A1ILA A CBD   
2751 C  CBE   . A1ILA E .   ? 0.0716 0.2603 0.2946 -0.0050 0.0367  -0.0069 203 A1ILA A CBE   
2752 C  CBF   . A1ILA E .   ? 0.0736 0.2615 0.2944 -0.0058 0.0381  -0.0068 203 A1ILA A CBF   
2753 N  NBJ   . A1ILA E .   ? 0.0776 0.2619 0.2949 -0.0062 0.0381  -0.0063 203 A1ILA A NBJ   
2754 C  CBG   . A1ILA E .   ? 0.0732 0.2621 0.2936 -0.0052 0.0385  -0.0070 203 A1ILA A CBG   
2755 C  CBH   . A1ILA E .   ? 0.0747 0.2614 0.2933 -0.0046 0.0370  -0.0068 203 A1ILA A CBH   
2756 C  C1    . EDO   F .   ? 0.1291 0.4328 0.3289 0.0833  -0.0077 -0.0138 204 EDO   A C1    
2757 O  O1    . EDO   F .   ? 0.1325 0.4171 0.3271 0.0814  -0.0064 -0.0131 204 EDO   A O1    
2758 C  C2    . EDO   F .   ? 0.1280 0.4391 0.3294 0.0807  -0.0091 -0.0135 204 EDO   A C2    
2759 O  O2    . EDO   F .   ? 0.1200 0.4366 0.3281 0.0719  -0.0079 -0.0128 204 EDO   A O2    
2760 P  PB    . GDP   G .   ? 0.4397 0.2779 0.3154 0.0253  0.0155  0.0176  201 GDP   B PB    
2761 O  O1B   . GDP   G .   ? 0.4434 0.2725 0.3201 0.0251  0.0150  0.0145  201 GDP   B O1B   
2762 O  O2B   . GDP   G .   ? 0.4349 0.2778 0.3027 0.0223  0.0156  0.0156  201 GDP   B O2B   
2763 O  O3B   . GDP   G .   ? 0.4431 0.2875 0.3258 0.0257  0.0144  0.0253  201 GDP   B O3B   
2764 O  O3A   . GDP   G .   ? 0.4386 0.2764 0.3139 0.0284  0.0175  0.0138  201 GDP   B O3A   
2765 P  PA    . GDP   G .   ? 0.4460 0.2770 0.3264 0.0322  0.0188  0.0097  201 GDP   B PA    
2766 O  O1A   . GDP   G .   ? 0.4417 0.2685 0.3159 0.0315  0.0198  0.0027  201 GDP   B O1A   
2767 O  O2A   . GDP   G .   ? 0.4532 0.2795 0.3439 0.0336  0.0175  0.0138  201 GDP   B O2A   
2768 O  "O5'" . GDP   G .   ? 0.4373 0.2752 0.3179 0.0343  0.0204  0.0101  201 GDP   B "O5'" 
2769 C  "C5'" . GDP   G .   ? 0.4329 0.2788 0.3173 0.0348  0.0200  0.0164  201 GDP   B "C5'" 
2770 C  "C4'" . GDP   G .   ? 0.4311 0.2818 0.3181 0.0380  0.0219  0.0155  201 GDP   B "C4'" 
2771 O  "O4'" . GDP   G .   ? 0.4265 0.2820 0.3055 0.0365  0.0232  0.0120  201 GDP   B "O4'" 
2772 C  "C3'" . GDP   G .   ? 0.4370 0.2814 0.3299 0.0423  0.0235  0.0103  201 GDP   B "C3'" 
2773 O  "O3'" . GDP   G .   ? 0.4360 0.2860 0.3366 0.0461  0.0244  0.0132  201 GDP   B "O3'" 
2774 C  "C2'" . GDP   G .   ? 0.4351 0.2796 0.3195 0.0416  0.0254  0.0028  201 GDP   B "C2'" 
2775 O  "O2'" . GDP   G .   ? 0.4413 0.2866 0.3296 0.0455  0.0278  -0.0024 201 GDP   B "O2'" 
2776 C  "C1'" . GDP   G .   ? 0.4281 0.2815 0.3065 0.0390  0.0253  0.0060  201 GDP   B "C1'" 
2777 N  N9    . GDP   G .   ? 0.4225 0.2757 0.2916 0.0361  0.0258  0.0016  201 GDP   B N9    
2778 C  C8    . GDP   G .   ? 0.4217 0.2694 0.2867 0.0338  0.0248  -0.0003 201 GDP   B C8    
2779 N  N7    . GDP   G .   ? 0.4186 0.2678 0.2767 0.0316  0.0252  -0.0028 201 GDP   B N7    
2780 C  C5    . GDP   G .   ? 0.4173 0.2730 0.2747 0.0320  0.0265  -0.0026 201 GDP   B C5    
2781 C  C6    . GDP   G .   ? 0.4182 0.2791 0.2703 0.0299  0.0272  -0.0034 201 GDP   B C6    
2782 O  O6    . GDP   G .   ? 0.4199 0.2788 0.2673 0.0273  0.0265  -0.0045 201 GDP   B O6    
2783 N  N1    . GDP   G .   ? 0.4174 0.2855 0.2710 0.0307  0.0284  -0.0021 201 GDP   B N1    
2784 C  C2    . GDP   G .   ? 0.4170 0.2881 0.2767 0.0338  0.0290  -0.0004 201 GDP   B C2    
2785 N  N2    . GDP   G .   ? 0.4161 0.2957 0.2772 0.0345  0.0303  0.0009  201 GDP   B N2    
2786 N  N3    . GDP   G .   ? 0.4177 0.2842 0.2829 0.0360  0.0283  0.0010  201 GDP   B N3    
2787 C  C4    . GDP   G .   ? 0.4187 0.2775 0.2831 0.0351  0.0270  0.0001  201 GDP   B C4    
2788 MG MG    . MG    H .   ? 0.4556 0.2747 0.3417 0.0244  0.0127  0.0170  202 MG    B MG    
2789 O  OBB   . A1ILA I .   ? 0.4531 0.3544 0.3501 -0.0360 0.0335  0.0174  203 A1ILA B OBB   
2790 C  CAS   . A1ILA I .   ? 0.4437 0.3529 0.3500 -0.0325 0.0329  0.0169  203 A1ILA B CAS   
2791 C  CAT   . A1ILA I .   ? 0.4357 0.3525 0.3465 -0.0316 0.0347  0.0165  203 A1ILA B CAT   
2792 C  CAZ   . A1ILA I .   ? 0.4337 0.3597 0.3480 -0.0344 0.0385  0.0162  203 A1ILA B CAZ   
2793 C  CAU   . A1ILA I .   ? 0.4348 0.3504 0.3464 -0.0279 0.0328  0.0164  203 A1ILA B CAU   
2794 O  OBA   . A1ILA I .   ? 0.4375 0.3453 0.3460 -0.0252 0.0291  0.0166  203 A1ILA B OBA   
2795 C  CAV   . A1ILA I .   ? 0.4314 0.3538 0.3468 -0.0269 0.0346  0.0160  203 A1ILA B CAV   
2796 C  CAW   . A1ILA I .   ? 0.4279 0.3591 0.3465 -0.0291 0.0384  0.0157  203 A1ILA B CAW   
2797 C  CAX   . A1ILA I .   ? 0.4290 0.3624 0.3473 -0.0330 0.0403  0.0158  203 A1ILA B CAX   
2798 S  SAI   . A1ILA I .   ? 0.4289 0.3739 0.3514 -0.0356 0.0446  0.0154  203 A1ILA B SAI   
2799 O  OAH   . A1ILA I .   ? 0.4369 0.3802 0.3522 -0.0413 0.0473  0.0159  203 A1ILA B OAH   
2800 O  OAY   . A1ILA I .   ? 0.4275 0.3788 0.3526 -0.0331 0.0462  0.0149  203 A1ILA B OAY   
2801 N  NAJ   . A1ILA I .   ? 0.4157 0.3674 0.3473 -0.0346 0.0441  0.0149  203 A1ILA B NAJ   
2802 C  CAK   . A1ILA I .   ? 0.4039 0.3614 0.3434 -0.0306 0.0432  0.0143  203 A1ILA B CAK   
2803 S  SBK   . A1ILA I .   ? 0.4002 0.3615 0.3426 -0.0265 0.0432  0.0138  203 A1ILA B SBK   
2804 C  CAF   . A1ILA I .   ? 0.3871 0.3544 0.3393 -0.0236 0.0416  0.0132  203 A1ILA B CAF   
2805 C  CAE   . A1ILA I .   ? 0.3797 0.3510 0.3371 -0.0200 0.0409  0.0126  203 A1ILA B CAE   
2806 CL CLBI  . A1ILA I .   ? 0.3809 0.3516 0.3349 -0.0176 0.0415  0.0124  203 A1ILA B CLBI  
2807 C  CAD   . A1ILA I .   ? 0.3713 0.3469 0.3360 -0.0184 0.0396  0.0122  203 A1ILA B CAD   
2808 C  CAC   . A1ILA I .   ? 0.3705 0.3463 0.3374 -0.0201 0.0390  0.0124  203 A1ILA B CAC   
2809 C  CAB   . A1ILA I .   ? 0.3781 0.3490 0.3390 -0.0236 0.0398  0.0130  203 A1ILA B CAB   
2810 O  OAA   . A1ILA I .   ? 0.3758 0.3459 0.3380 -0.0253 0.0392  0.0131  203 A1ILA B OAA   
2811 C  CAG   . A1ILA I .   ? 0.3863 0.3527 0.3397 -0.0255 0.0410  0.0134  203 A1ILA B CAG   
2812 N  NAL   . A1ILA I .   ? 0.3954 0.3563 0.3415 -0.0294 0.0419  0.0140  203 A1ILA B NAL   
2813 C  CAM   . A1ILA I .   ? 0.3972 0.3543 0.3413 -0.0323 0.0414  0.0144  203 A1ILA B CAM   
2814 C  CAN   . A1ILA I .   ? 0.3975 0.3468 0.3408 -0.0293 0.0373  0.0146  203 A1ILA B CAN   
2815 C  CAO   . A1ILA I .   ? 0.4111 0.3480 0.3439 -0.0306 0.0356  0.0153  203 A1ILA B CAO   
2816 C  CAP   . A1ILA I .   ? 0.4147 0.3463 0.3453 -0.0269 0.0328  0.0154  203 A1ILA B CAP   
2817 C  CAQ   . A1ILA I .   ? 0.4254 0.3449 0.3477 -0.0260 0.0296  0.0159  203 A1ILA B CAQ   
2818 N  NAR   . A1ILA I .   ? 0.4390 0.3496 0.3506 -0.0299 0.0306  0.0166  203 A1ILA B NAR   
2819 C  CBC   . A1ILA I .   ? 0.4492 0.3508 0.3544 -0.0307 0.0288  0.0169  203 A1ILA B CBC   
2820 C  CBD   . A1ILA I .   ? 0.4419 0.3485 0.3540 -0.0298 0.0283  0.0166  203 A1ILA B CBD   
2821 C  CBE   . A1ILA I .   ? 0.4522 0.3479 0.3565 -0.0294 0.0258  0.0169  203 A1ILA B CBE   
2822 C  CBF   . A1ILA I .   ? 0.4584 0.3463 0.3583 -0.0249 0.0220  0.0170  203 A1ILA B CBF   
2823 N  NBJ   . A1ILA I .   ? 0.4495 0.3448 0.3588 -0.0200 0.0198  0.0164  203 A1ILA B NBJ   
2824 C  CBG   . A1ILA I .   ? 0.4660 0.3476 0.3578 -0.0266 0.0227  0.0175  203 A1ILA B CBG   
2825 C  CBH   . A1ILA I .   ? 0.4594 0.3508 0.3580 -0.0272 0.0251  0.0172  203 A1ILA B CBH   
2826 C  C1    . EDO   J .   ? 0.3546 0.3847 0.3935 0.0029  0.0248  0.0044  204 EDO   B C1    
2827 O  O1    . EDO   J .   ? 0.3584 0.3899 0.3967 0.0039  0.0273  0.0044  204 EDO   B O1    
2828 C  C2    . EDO   J .   ? 0.3574 0.3873 0.3947 0.0048  0.0256  0.0037  204 EDO   B C2    
2829 O  O2    . EDO   J .   ? 0.3569 0.3932 0.3985 0.0065  0.0286  0.0031  204 EDO   B O2    
2830 O  O     . HOH   K .   ? 0.1617 0.2763 0.2983 -0.0171 0.0392  0.0017  301 HOH   A O     
2831 O  O     . HOH   K .   ? 0.1180 0.2691 0.2977 -0.0130 0.0394  -0.0022 302 HOH   A O     
2832 O  O     . HOH   K .   ? 0.1743 0.4287 0.3570 0.0848  -0.0047 -0.0128 303 HOH   A O     
2833 O  O     . HOH   K .   ? 0.1528 0.3504 0.3599 -0.0205 0.0198  -0.0057 304 HOH   A O     
2834 O  O     . HOH   K .   ? 0.2259 0.3727 0.3917 -0.0022 0.0382  -0.0027 305 HOH   A O     
2835 O  O     . HOH   K .   ? 0.2525 0.3687 0.3754 -0.0065 0.0058  0.0032  306 HOH   A O     
2836 O  O     . HOH   K .   ? 0.2532 0.4087 0.4172 0.0407  0.0099  -0.0057 307 HOH   A O     
2837 O  O     . HOH   K .   ? 0.0984 0.2626 0.2971 -0.0050 0.0345  -0.0040 308 HOH   A O     
2838 O  O     . HOH   K .   ? 0.1254 0.3125 0.3027 -0.0047 0.0059  -0.0011 309 HOH   A O     
2839 O  O     . HOH   K .   ? 0.1087 0.2648 0.2920 -0.0040 0.0302  -0.0036 310 HOH   A O     
2840 O  O     . HOH   K .   ? 0.2447 0.5065 0.4246 0.0867  -0.0081 -0.0125 311 HOH   A O     
2841 O  O     . HOH   K .   ? 0.0892 0.2655 0.3002 0.0049  0.0288  -0.0060 312 HOH   A O     
2842 O  O     . HOH   K .   ? 0.1074 0.2648 0.2962 -0.0064 0.0356  -0.0030 313 HOH   A O     
2843 O  O     . HOH   K .   ? 0.1102 0.2692 0.2959 -0.0098 0.0395  -0.0028 314 HOH   A O     
2844 O  O     . HOH   K .   ? 0.1569 0.2643 0.3033 -0.0012 0.0283  -0.0011 315 HOH   A O     
2845 O  O     . HOH   K .   ? 0.0966 0.2703 0.3064 -0.0075 0.0373  -0.0054 316 HOH   A O     
2846 O  O     . HOH   K .   ? 0.2437 0.3162 0.3409 0.0066  0.0140  0.0046  317 HOH   A O     
2847 O  O     . HOH   K .   ? 0.1987 0.3303 0.3359 0.0191  0.0041  0.0008  318 HOH   A O     
2848 O  O     . HOH   K .   ? 0.1835 0.3498 0.3732 0.0261  0.0195  -0.0067 319 HOH   A O     
2849 O  O     . HOH   K .   ? 0.1326 0.2679 0.2942 -0.0041 0.0320  -0.0007 320 HOH   A O     
2850 O  O     . HOH   K .   ? 0.2026 0.3933 0.3710 0.0324  -0.0007 -0.0033 321 HOH   A O     
2851 O  O     . HOH   K .   ? 0.3610 0.4223 0.4611 -0.0198 0.0314  0.0013  322 HOH   A O     
2852 O  O     . HOH   K .   ? 0.2518 0.4227 0.4114 -0.0184 0.0038  0.0004  323 HOH   A O     
2853 O  O     . HOH   K .   ? 0.0881 0.2747 0.3035 -0.0086 0.0412  -0.0063 324 HOH   A O     
2854 O  O     . HOH   K .   ? 0.1637 0.4524 0.3914 0.0269  0.0043  -0.0091 325 HOH   A O     
2855 O  O     . HOH   K .   ? 0.2179 0.3748 0.3682 0.0052  0.0018  0.0010  326 HOH   A O     
2856 O  O     . HOH   K .   ? 0.2125 0.4075 0.4206 -0.0167 0.0477  -0.0057 327 HOH   A O     
2857 O  O     . HOH   K .   ? 0.0863 0.3006 0.2980 -0.0179 0.0159  -0.0050 328 HOH   A O     
2858 O  O     . HOH   K .   ? 0.2783 0.4616 0.4447 0.0573  0.0028  -0.0077 329 HOH   A O     
2859 O  O     . HOH   K .   ? 0.1306 0.2901 0.3162 -0.0066 0.0383  -0.0031 330 HOH   A O     
2860 O  O     . HOH   K .   ? 0.1853 0.3491 0.3309 -0.0075 -0.0024 0.0018  331 HOH   A O     
2861 O  O     . HOH   K .   ? 0.2658 0.3483 0.3769 0.0186  0.0134  0.0012  332 HOH   A O     
2862 O  O     . HOH   K .   ? 0.1249 0.3757 0.3459 -0.0047 0.0095  -0.0057 333 HOH   A O     
2863 O  O     . HOH   K .   ? 0.1933 0.2950 0.3151 -0.0029 0.0165  0.0029  334 HOH   A O     
2864 O  O     . HOH   K .   ? 0.2925 0.4025 0.4226 -0.0016 0.0287  -0.0001 335 HOH   A O     
2865 O  O     . HOH   K .   ? 0.1244 0.2770 0.2971 -0.0164 0.0430  -0.0016 336 HOH   A O     
2866 O  O     . HOH   K .   ? 0.2233 0.3140 0.3328 0.0402  0.0059  -0.0017 337 HOH   A O     
2867 O  O     . HOH   K .   ? 0.2460 0.3570 0.3762 -0.0295 0.0424  0.0019  338 HOH   A O     
2868 O  O     . HOH   K .   ? 0.1055 0.2669 0.2966 -0.0099 0.0388  -0.0033 339 HOH   A O     
2869 O  O     . HOH   K .   ? 0.1016 0.3811 0.3221 0.0025  0.0025  -0.0061 340 HOH   A O     
2870 O  O     . HOH   K .   ? 0.2765 0.4977 0.5024 0.0003  0.0191  -0.0065 341 HOH   A O     
2871 O  O     . HOH   K .   ? 0.1412 0.3231 0.3349 0.0344  0.0161  -0.0079 342 HOH   A O     
2872 O  O     . HOH   K .   ? 0.1037 0.3339 0.3174 -0.0201 0.0126  -0.0050 343 HOH   A O     
2873 O  O     . HOH   K .   ? 0.1011 0.2824 0.2989 -0.0251 0.0471  -0.0043 344 HOH   A O     
2874 O  O     . HOH   K .   ? 0.1756 0.2928 0.3159 -0.0035 0.0256  0.0004  345 HOH   A O     
2875 O  O     . HOH   K .   ? 0.2508 0.3949 0.4172 -0.0220 0.0429  -0.0011 346 HOH   A O     
2876 O  O     . HOH   K .   ? 0.1797 0.2894 0.3101 0.0352  0.0097  -0.0026 347 HOH   A O     
2877 O  O     . HOH   K .   ? 0.1829 0.4845 0.4109 0.0414  0.0029  -0.0110 348 HOH   A O     
2878 O  O     . HOH   K .   ? 0.2766 0.3768 0.4139 0.0260  0.0190  -0.0048 349 HOH   A O     
2879 O  O     . HOH   K .   ? 0.3289 0.4369 0.4776 0.0185  0.0228  -0.0052 350 HOH   A O     
2880 O  O     . HOH   K .   ? 0.3785 0.4813 0.4991 0.0453  0.0071  -0.0037 351 HOH   A O     
2881 O  O     . HOH   K .   ? 0.2118 0.2648 0.3077 0.0021  0.0233  -0.0001 352 HOH   A O     
2882 O  O     . HOH   K .   ? 0.1338 0.3007 0.3247 0.0017  0.0353  -0.0081 353 HOH   A O     
2883 O  O     . HOH   K .   ? 0.0876 0.2713 0.2995 -0.0065 0.0402  -0.0061 354 HOH   A O     
2884 O  O     . HOH   K .   ? 0.2917 0.4975 0.5194 0.0000  0.0252  -0.0069 355 HOH   A O     
2885 O  O     . HOH   K .   ? 0.1998 0.4110 0.3690 0.0620  -0.0039 -0.0078 356 HOH   A O     
2886 O  O     . HOH   K .   ? 0.1516 0.2693 0.3027 -0.0238 0.0384  -0.0011 357 HOH   A O     
2887 O  O     . HOH   K .   ? 0.3408 0.4571 0.4729 0.0020  0.0339  -0.0015 358 HOH   A O     
2888 O  O     . HOH   K .   ? 0.1667 0.4319 0.3984 -0.0019 0.0112  -0.0071 359 HOH   A O     
2889 O  O     . HOH   K .   ? 0.2161 0.3179 0.3381 -0.0249 0.0405  0.0027  360 HOH   A O     
2890 O  O     . HOH   K .   ? 0.1095 0.2651 0.2931 -0.0037 0.0322  -0.0031 361 HOH   A O     
2891 O  O     . HOH   K .   ? 0.1095 0.2941 0.2940 -0.0304 0.0142  -0.0039 362 HOH   A O     
2892 O  O     . HOH   K .   ? 0.1763 0.2988 0.3111 0.0393  0.0065  -0.0028 363 HOH   A O     
2893 O  O     . HOH   K .   ? 0.1915 0.3571 0.3770 -0.0091 0.0424  -0.0034 364 HOH   A O     
2894 O  O     . HOH   K .   ? 0.1701 0.3067 0.3211 -0.0254 0.0170  -0.0043 365 HOH   A O     
2895 O  O     . HOH   K .   ? 0.1576 0.3083 0.3062 0.0145  0.0028  0.0004  366 HOH   A O     
2896 O  O     . HOH   K .   ? 0.1505 0.3361 0.3218 0.0570  0.0049  -0.0083 367 HOH   A O     
2897 O  O     . HOH   K .   ? 0.1811 0.3372 0.3531 -0.0042 0.0416  -0.0031 368 HOH   A O     
2898 O  O     . HOH   K .   ? 0.2778 0.4113 0.4278 -0.0210 0.0435  0.0005  369 HOH   A O     
2899 O  O     . HOH   K .   ? 0.1878 0.2891 0.3140 -0.0229 0.0387  0.0022  370 HOH   A O     
2900 O  O     . HOH   K .   ? 0.2579 0.3124 0.3531 0.0121  0.0193  -0.0003 371 HOH   A O     
2901 O  O     . HOH   K .   ? 0.3183 0.4419 0.4553 -0.0206 0.0436  0.0016  372 HOH   A O     
2902 O  O     . HOH   K .   ? 0.1396 0.3452 0.3622 -0.0075 0.0233  -0.0063 373 HOH   A O     
2903 O  O     . HOH   K .   ? 0.2768 0.4630 0.4478 -0.0130 0.0037  -0.0004 374 HOH   A O     
2904 O  O     . HOH   K .   ? 0.2609 0.5344 0.4343 0.1034  -0.0117 -0.0145 375 HOH   A O     
2905 O  O     . HOH   K .   ? 0.2665 0.3750 0.3970 -0.0036 0.0241  0.0012  376 HOH   A O     
2906 O  O     . HOH   L .   ? 0.4553 0.3599 0.3374 -0.0218 0.0390  0.0164  301 HOH   B O     
2907 O  O     . HOH   L .   ? 0.3490 0.3881 0.3716 -0.0143 -0.0190 0.0104  302 HOH   B O     
2908 O  O     . HOH   L .   ? 0.4138 0.3425 0.3580 -0.0008 0.0055  0.0145  303 HOH   B O     
2909 O  O     . HOH   L .   ? 0.4110 0.4606 0.4208 0.0003  -0.0342 0.0110  304 HOH   B O     
2910 O  O     . HOH   L .   ? 0.6434 0.5012 0.4891 0.0204  0.0147  0.0076  305 HOH   B O     
2911 O  O     . HOH   L .   ? 0.5312 0.4527 0.4363 -0.0396 -0.0276 0.0142  306 HOH   B O     
2912 O  O     . HOH   L .   ? 0.3322 0.3343 0.3304 -0.0157 -0.0125 0.0110  307 HOH   B O     
2913 O  O     . HOH   L .   ? 0.3320 0.4191 0.3943 0.0067  0.0495  0.0013  308 HOH   B O     
2914 O  O     . HOH   L .   ? 0.4759 0.4120 0.3635 -0.0337 0.0535  0.0157  309 HOH   B O     
2915 O  O     . HOH   L .   ? 0.4906 0.4167 0.4346 -0.0035 0.0098  0.0145  310 HOH   B O     
2916 O  O     . HOH   L .   ? 0.3776 0.4295 0.3568 -0.0150 -0.0516 0.0133  311 HOH   B O     
2917 O  O     . HOH   L .   ? 0.5064 0.4195 0.4230 -0.0077 0.0201  0.0151  312 HOH   B O     
2918 O  O     . HOH   L .   ? 0.4180 0.4158 0.4332 -0.0103 0.0246  0.0104  313 HOH   B O     
2919 O  O     . HOH   L .   ? 0.3390 0.3407 0.3395 0.0285  -0.0181 0.0095  314 HOH   B O     
2920 O  O     . HOH   L .   ? 0.4467 0.3570 0.3703 0.0002  0.0008  0.0156  315 HOH   B O     
2921 O  O     . HOH   L .   ? 0.5287 0.4372 0.4125 -0.0097 0.0382  0.0146  316 HOH   B O     
2922 O  O     . HOH   L .   ? 0.4025 0.3416 0.3239 0.0159  0.0314  0.0075  317 HOH   B O     
2923 O  O     . HOH   L .   ? 0.3591 0.3685 0.3195 -0.0395 -0.0414 0.0144  318 HOH   B O     
2924 O  O     . HOH   L .   ? 0.3643 0.3259 0.3167 0.0008  -0.0248 0.0143  319 HOH   B O     
2925 O  O     . HOH   L .   ? 0.3685 0.3692 0.2989 0.0087  0.0600  0.0067  320 HOH   B O     
2926 O  O     . HOH   L .   ? 0.4952 0.4003 0.3650 -0.0278 0.0456  0.0168  321 HOH   B O     
2927 O  O     . HOH   L .   ? 0.4722 0.4103 0.4149 0.0192  -0.0190 0.0137  322 HOH   B O     
2928 O  O     . HOH   L .   ? 0.4489 0.3520 0.3585 -0.0116 0.0193  0.0162  323 HOH   B O     
2929 O  O     . HOH   L .   ? 0.3976 0.3232 0.3381 0.0071  -0.0044 0.0144  324 HOH   B O     
2930 O  O     . HOH   L .   ? 0.4635 0.4002 0.3814 -0.0131 -0.0333 0.0162  325 HOH   B O     
2931 O  O     . HOH   L .   ? 0.3963 0.3345 0.3395 -0.0035 0.0061  0.0086  326 HOH   B O     
2932 O  O     . HOH   L .   ? 0.2858 0.3064 0.3184 -0.0043 0.0044  0.0089  327 HOH   B O     
2933 O  O     . HOH   L .   ? 0.3861 0.3038 0.3185 0.0036  -0.0019 0.0150  328 HOH   B O     
2934 O  O     . HOH   L .   ? 0.3853 0.3721 0.3774 0.0041  0.0200  0.0061  329 HOH   B O     
2935 O  O     . HOH   L .   ? 0.4958 0.4013 0.4121 -0.0036 0.0074  0.0157  330 HOH   B O     
2936 O  O     . HOH   L .   ? 0.4587 0.3761 0.3930 0.0026  0.0013  0.0149  331 HOH   B O     
2937 O  O     . HOH   L .   ? 0.3682 0.2876 0.2955 -0.0033 -0.0004 0.0145  332 HOH   B O     
2938 O  O     . HOH   L .   ? 0.3667 0.3247 0.3306 -0.0106 0.0012  0.0091  333 HOH   B O     
2939 O  O     . HOH   L .   ? 0.3932 0.3186 0.3264 0.0119  -0.0148 0.0147  334 HOH   B O     
2940 O  O     . HOH   L .   ? 0.3235 0.3483 0.3608 -0.0129 0.0317  0.0088  335 HOH   B O     
2941 O  O     . HOH   L .   ? 0.4731 0.4152 0.4114 -0.0191 -0.0161 0.0134  336 HOH   B O     
2942 O  O     . HOH   L .   ? 0.4842 0.3631 0.3544 0.0195  0.0144  0.0059  337 HOH   B O     
2943 O  O     . HOH   L .   ? 0.4988 0.4079 0.3955 -0.0240 -0.0276 0.0160  338 HOH   B O     
2944 O  O     . HOH   L .   ? 0.3169 0.3654 0.3711 0.0038  0.0313  0.0036  339 HOH   B O     
2945 O  O     . HOH   L .   ? 0.2696 0.3533 0.3279 -0.0002 0.0506  0.0028  340 HOH   B O     
2946 O  O     . HOH   L .   ? 0.3868 0.3039 0.3128 -0.0050 0.0129  0.0149  341 HOH   B O     
2947 O  O     . HOH   L .   ? 0.4275 0.4789 0.4296 0.0216  0.0536  0.0012  342 HOH   B O     
2948 O  O     . HOH   L .   ? 0.4335 0.3215 0.3245 -0.0040 0.0006  0.0140  343 HOH   B O     
2949 O  O     . HOH   L .   ? 0.4163 0.4208 0.4409 -0.0052 0.0198  0.0098  344 HOH   B O     
2950 O  O     . HOH   L .   ? 0.2712 0.2877 0.2993 -0.0062 0.0058  0.0085  345 HOH   B O     
2951 O  O     . HOH   L .   ? 0.3527 0.3586 0.3239 -0.0295 -0.0340 0.0135  346 HOH   B O     
2952 O  O     . HOH   L .   ? 0.5172 0.5338 0.5061 -0.0272 0.0507  0.0106  347 HOH   B O     
2953 O  O     . HOH   L .   ? 0.3818 0.3540 0.3696 -0.0145 0.0249  0.0121  348 HOH   B O     
2954 O  O     . HOH   L .   ? 0.5599 0.5262 0.4362 0.0352  0.0614  0.0040  349 HOH   B O     
2955 O  O     . HOH   L .   ? 0.4719 0.4244 0.4424 -0.0127 0.0208  0.0130  350 HOH   B O     
2956 O  O     . HOH   L .   ? 0.4459 0.4295 0.4259 0.0331  -0.0226 0.0102  351 HOH   B O     
2957 O  O     . HOH   L .   ? 0.5400 0.4890 0.4192 0.0340  0.0535  0.0047  352 HOH   B O     
2958 O  O     . HOH   L .   ? 0.4377 0.4182 0.4372 -0.0109 0.0225  0.0113  353 HOH   B O     
2959 O  O     . HOH   L .   ? 0.4501 0.4096 0.4164 -0.0039 0.0080  0.0081  354 HOH   B O     
# 
