data_8VSO
# 
_entry.id   8VSO 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_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   8VSO         pdb_00008vso 10.2210/pdb8vso/pdb 
WWPDB D_1000276247 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-03-19 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8VSO 
_pdbx_database_status.recvd_initial_deposition_date   2024-01-24 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_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           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              michelle.arkin@ucsf.edu 
_pdbx_contact_author.name_first         Michelle 
_pdbx_contact_author.name_last          Arkin 
_pdbx_contact_author.name_mi            R 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-9366-6770 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Vickery, H.R.'        1 ? 
'Virta, J.M.'          2 ? 
'Pennings, M.'         3 ? 
'Konstantinidou, M.'   4 ? 
'van den Oetelaar, M.' 5 ? 
'Neitz, R.J.'          6 ? 
'Ottmann, C.'          7 ? 
'Brunsveld, L.'        8 ? 
'Arkin, M.R.'          9 ? 
# 
_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                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'Ternary structure of 14-3-3 sigma, BRAF phosphopeptide (pS365) and compound 78 (1124378)' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Vickery, H.R.'        1 ? 
primary 'Virta, J.M.'          2 ? 
primary 'Pennings, M.'         3 ? 
primary 'Konstantinidou, M.'   4 ? 
primary 'van den Oetelaar, M.' 5 ? 
primary 'Neitz, R.J.'          6 ? 
primary 'Ottmann, C.'          7 ? 
primary 'Brunsveld, L.'        8 ? 
primary 'Arkin, M.R.'          9 ? 
# 
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 '14-3-3 protein sigma'                                                                   26542.914 1   ?        
? 'residues 1-231'                       ?                              
2 polymer     syn 'Serine/threonine-protein kinase B-raf phosphopeptide'                                   1012.935  1   2.7.11.1 
? 'residues 361-369 (Uniprot numbering)' 'containing phosphoserine 365' 
3 non-polymer syn 'CHLORIDE ION'                                                                           35.453    1   ?        
? ?                                      ?                              
4 non-polymer syn 'MAGNESIUM ION'                                                                          24.305    2   ?        
? ?                                      ?                              
5 non-polymer syn '1-[8-(4-bromophenyl)sulfonyl-5-oxa-2,8-diazaspiro[3.5]nonan-2-yl]-2-chloranyl-ethanone' 423.710   1   ?        
? ?                                      ?                              
6 water       nat water                                                                                    18.015    217 ?        
? ?                                      ?                              
# 
loop_
_entity_name_com.entity_id 
_entity_name_com.name 
1 'Epithelial cell marker protein 1,Stratifin'                              
2 'Proto-oncogene B-Raf,p94,v-Raf murine sarcoma viral oncogene homolog B1' 
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)' no no  
;GAMGSMERASLIQKAKLAEQAERYEDMAAFMKGAVEKGEELSCEERNLLSVAYKNVVGGQRAAWRVLSSIEQKSNEEGSE
EKGPEVREYREKVETELQGVCDTVLGLLDSHLIKEAGDAESRVFYLKMKGDYYRYLAEVATGDDKKRIIDSARSAYQEAM
DISKKEMPPTNPIRLGLALNFSVFHYEIANSPEEAISLAKTTFDEAMADLHTLSEDSYKDSTLIMQLLRDNLTLWT
;
;GAMGSMERASLIQKAKLAEQAERYEDMAAFMKGAVEKGEELSCEERNLLSVAYKNVVGGQRAAWRVLSSIEQKSNEEGSE
EKGPEVREYREKVETELQGVCDTVLGLLDSHLIKEAGDAESRVFYLKMKGDYYRYLAEVATGDDKKRIIDSARSAYQEAM
DISKKEMPPTNPIRLGLALNFSVFHYEIANSPEEAISLAKTTFDEAMADLHTLSEDSYKDSTLIMQLLRDNLTLWT
;
B ? 
2 'polypeptide(L)' no yes 'DRSS(SEP)APNV' DRSSSAPNV P ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3 'CHLORIDE ION'                                                                           CL  
4 'MAGNESIUM ION'                                                                          MG  
5 '1-[8-(4-bromophenyl)sulfonyl-5-oxa-2,8-diazaspiro[3.5]nonan-2-yl]-2-chloranyl-ethanone' WQN 
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   ALA n 
1 3   MET n 
1 4   GLY n 
1 5   SER n 
1 6   MET n 
1 7   GLU n 
1 8   ARG n 
1 9   ALA n 
1 10  SER n 
1 11  LEU n 
1 12  ILE n 
1 13  GLN n 
1 14  LYS n 
1 15  ALA n 
1 16  LYS n 
1 17  LEU n 
1 18  ALA n 
1 19  GLU n 
1 20  GLN n 
1 21  ALA n 
1 22  GLU n 
1 23  ARG n 
1 24  TYR n 
1 25  GLU n 
1 26  ASP n 
1 27  MET n 
1 28  ALA n 
1 29  ALA n 
1 30  PHE n 
1 31  MET n 
1 32  LYS n 
1 33  GLY n 
1 34  ALA n 
1 35  VAL n 
1 36  GLU n 
1 37  LYS n 
1 38  GLY n 
1 39  GLU n 
1 40  GLU n 
1 41  LEU n 
1 42  SER n 
1 43  CYS n 
1 44  GLU n 
1 45  GLU n 
1 46  ARG n 
1 47  ASN n 
1 48  LEU n 
1 49  LEU n 
1 50  SER n 
1 51  VAL n 
1 52  ALA n 
1 53  TYR n 
1 54  LYS n 
1 55  ASN n 
1 56  VAL n 
1 57  VAL n 
1 58  GLY n 
1 59  GLY n 
1 60  GLN n 
1 61  ARG n 
1 62  ALA n 
1 63  ALA n 
1 64  TRP n 
1 65  ARG n 
1 66  VAL n 
1 67  LEU n 
1 68  SER n 
1 69  SER n 
1 70  ILE n 
1 71  GLU n 
1 72  GLN n 
1 73  LYS n 
1 74  SER n 
1 75  ASN n 
1 76  GLU n 
1 77  GLU n 
1 78  GLY n 
1 79  SER n 
1 80  GLU n 
1 81  GLU n 
1 82  LYS n 
1 83  GLY n 
1 84  PRO n 
1 85  GLU n 
1 86  VAL n 
1 87  ARG n 
1 88  GLU n 
1 89  TYR n 
1 90  ARG n 
1 91  GLU n 
1 92  LYS n 
1 93  VAL n 
1 94  GLU n 
1 95  THR n 
1 96  GLU n 
1 97  LEU n 
1 98  GLN n 
1 99  GLY n 
1 100 VAL n 
1 101 CYS n 
1 102 ASP n 
1 103 THR n 
1 104 VAL n 
1 105 LEU n 
1 106 GLY n 
1 107 LEU n 
1 108 LEU n 
1 109 ASP n 
1 110 SER n 
1 111 HIS n 
1 112 LEU n 
1 113 ILE n 
1 114 LYS n 
1 115 GLU n 
1 116 ALA n 
1 117 GLY n 
1 118 ASP n 
1 119 ALA n 
1 120 GLU n 
1 121 SER n 
1 122 ARG n 
1 123 VAL n 
1 124 PHE n 
1 125 TYR n 
1 126 LEU n 
1 127 LYS n 
1 128 MET n 
1 129 LYS n 
1 130 GLY n 
1 131 ASP n 
1 132 TYR n 
1 133 TYR n 
1 134 ARG n 
1 135 TYR n 
1 136 LEU n 
1 137 ALA n 
1 138 GLU n 
1 139 VAL n 
1 140 ALA n 
1 141 THR n 
1 142 GLY n 
1 143 ASP n 
1 144 ASP n 
1 145 LYS n 
1 146 LYS n 
1 147 ARG n 
1 148 ILE n 
1 149 ILE n 
1 150 ASP n 
1 151 SER n 
1 152 ALA n 
1 153 ARG n 
1 154 SER n 
1 155 ALA n 
1 156 TYR n 
1 157 GLN n 
1 158 GLU n 
1 159 ALA n 
1 160 MET n 
1 161 ASP n 
1 162 ILE n 
1 163 SER n 
1 164 LYS n 
1 165 LYS n 
1 166 GLU n 
1 167 MET n 
1 168 PRO n 
1 169 PRO n 
1 170 THR n 
1 171 ASN n 
1 172 PRO n 
1 173 ILE n 
1 174 ARG n 
1 175 LEU n 
1 176 GLY n 
1 177 LEU n 
1 178 ALA n 
1 179 LEU n 
1 180 ASN n 
1 181 PHE n 
1 182 SER n 
1 183 VAL n 
1 184 PHE n 
1 185 HIS n 
1 186 TYR n 
1 187 GLU n 
1 188 ILE n 
1 189 ALA n 
1 190 ASN n 
1 191 SER n 
1 192 PRO n 
1 193 GLU n 
1 194 GLU n 
1 195 ALA n 
1 196 ILE n 
1 197 SER n 
1 198 LEU n 
1 199 ALA n 
1 200 LYS n 
1 201 THR n 
1 202 THR n 
1 203 PHE n 
1 204 ASP n 
1 205 GLU n 
1 206 ALA n 
1 207 MET n 
1 208 ALA n 
1 209 ASP n 
1 210 LEU n 
1 211 HIS n 
1 212 THR n 
1 213 LEU n 
1 214 SER n 
1 215 GLU n 
1 216 ASP n 
1 217 SER n 
1 218 TYR n 
1 219 LYS n 
1 220 ASP n 
1 221 SER n 
1 222 THR n 
1 223 LEU n 
1 224 ILE n 
1 225 MET n 
1 226 GLN n 
1 227 LEU n 
1 228 LEU n 
1 229 ARG n 
1 230 ASP n 
1 231 ASN n 
1 232 LEU n 
1 233 THR n 
1 234 LEU n 
1 235 TRP n 
1 236 THR n 
2 1   ASP n 
2 2   ARG n 
2 3   SER n 
2 4   SER n 
2 5   SEP n 
2 6   ALA n 
2 7   PRO n 
2 8   ASN n 
2 9   VAL 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                   236 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'SFN, HME1' 
_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                   ? 
# 
_pdbx_entity_src_syn.entity_id              2 
_pdbx_entity_src_syn.pdbx_src_id            1 
_pdbx_entity_src_syn.pdbx_alt_source_flag   sample 
_pdbx_entity_src_syn.pdbx_beg_seq_num       1 
_pdbx_entity_src_syn.pdbx_end_seq_num       9 
_pdbx_entity_src_syn.organism_scientific    'Homo sapiens' 
_pdbx_entity_src_syn.organism_common_name   human 
_pdbx_entity_src_syn.ncbi_taxonomy_id       9606 
_pdbx_entity_src_syn.details                ? 
# 
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 
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 
CL  non-polymer         . 'CHLORIDE ION'                                                                           ?               
'Cl -1'                 35.453  
CYS 'L-peptide linking' y CYSTEINE                                                                                 ?               
'C3 H7 N O2 S'          121.158 
GLN 'L-peptide linking' y GLUTAMINE                                                                                ?               
'C5 H10 N2 O3'          146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                                                                          ?               
'C5 H9 N O4'            147.129 
GLY 'peptide linking'   y GLYCINE                                                                                  ?               
'C2 H5 N O2'            75.067  
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 
SEP 'L-peptide linking' n PHOSPHOSERINE                                                                            PHOSPHONOSERINE 
'C3 H8 N O6 P'          185.072 
SER 'L-peptide linking' y SERINE                                                                                   ?               
'C3 H7 N O3'            105.093 
THR 'L-peptide linking' y THREONINE                                                                                ?               
'C4 H9 N O3'            119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                                                                               ?               
'C11 H12 N2 O2'         204.225 
TYR 'L-peptide linking' y TYROSINE                                                                                 ?               
'C9 H11 N O3'           181.189 
VAL 'L-peptide linking' y VALINE                                                                                   ?               
'C5 H11 N O2'           117.146 
WQN non-polymer         . '1-[8-(4-bromophenyl)sulfonyl-5-oxa-2,8-diazaspiro[3.5]nonan-2-yl]-2-chloranyl-ethanone' ?               
'C14 H16 Br Cl N2 O4 S' 423.710 
# 
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   -4  -4  GLY GLY B . n 
A 1 2   ALA 2   -3  -3  ALA ALA B . n 
A 1 3   MET 3   -2  -2  MET MET B . n 
A 1 4   GLY 4   -1  -1  GLY GLY B . n 
A 1 5   SER 5   0   0   SER SER B . n 
A 1 6   MET 6   1   1   MET MET B . n 
A 1 7   GLU 7   2   2   GLU GLU B . n 
A 1 8   ARG 8   3   3   ARG ARG B . n 
A 1 9   ALA 9   4   4   ALA ALA B . n 
A 1 10  SER 10  5   5   SER SER B . n 
A 1 11  LEU 11  6   6   LEU LEU B . n 
A 1 12  ILE 12  7   7   ILE ILE B . n 
A 1 13  GLN 13  8   8   GLN GLN B . n 
A 1 14  LYS 14  9   9   LYS LYS B . n 
A 1 15  ALA 15  10  10  ALA ALA B . n 
A 1 16  LYS 16  11  11  LYS LYS B . n 
A 1 17  LEU 17  12  12  LEU LEU B . n 
A 1 18  ALA 18  13  13  ALA ALA B . n 
A 1 19  GLU 19  14  14  GLU GLU B . n 
A 1 20  GLN 20  15  15  GLN GLN B . n 
A 1 21  ALA 21  16  16  ALA ALA B . n 
A 1 22  GLU 22  17  17  GLU GLU B . n 
A 1 23  ARG 23  18  18  ARG ARG B . n 
A 1 24  TYR 24  19  19  TYR TYR B . n 
A 1 25  GLU 25  20  20  GLU GLU B . n 
A 1 26  ASP 26  21  21  ASP ASP B . n 
A 1 27  MET 27  22  22  MET MET B . n 
A 1 28  ALA 28  23  23  ALA ALA B . n 
A 1 29  ALA 29  24  24  ALA ALA B . n 
A 1 30  PHE 30  25  25  PHE PHE B . n 
A 1 31  MET 31  26  26  MET MET B . n 
A 1 32  LYS 32  27  27  LYS LYS B . n 
A 1 33  GLY 33  28  28  GLY GLY B . n 
A 1 34  ALA 34  29  29  ALA ALA B . n 
A 1 35  VAL 35  30  30  VAL VAL B . n 
A 1 36  GLU 36  31  31  GLU GLU B . n 
A 1 37  LYS 37  32  32  LYS LYS B . n 
A 1 38  GLY 38  33  33  GLY GLY B . n 
A 1 39  GLU 39  34  34  GLU GLU B . n 
A 1 40  GLU 40  35  35  GLU GLU B . n 
A 1 41  LEU 41  36  36  LEU LEU B . n 
A 1 42  SER 42  37  37  SER SER B . n 
A 1 43  CYS 43  38  38  CYS CSO B . n 
A 1 44  GLU 44  39  39  GLU GLU B . n 
A 1 45  GLU 45  40  40  GLU GLU B . n 
A 1 46  ARG 46  41  41  ARG ARG B . n 
A 1 47  ASN 47  42  42  ASN ASN B . n 
A 1 48  LEU 48  43  43  LEU LEU B . n 
A 1 49  LEU 49  44  44  LEU LEU B . n 
A 1 50  SER 50  45  45  SER SER B . n 
A 1 51  VAL 51  46  46  VAL VAL B . n 
A 1 52  ALA 52  47  47  ALA ALA B . n 
A 1 53  TYR 53  48  48  TYR TYR B . n 
A 1 54  LYS 54  49  49  LYS LYS B . n 
A 1 55  ASN 55  50  50  ASN ASN B . n 
A 1 56  VAL 56  51  51  VAL VAL B . n 
A 1 57  VAL 57  52  52  VAL VAL B . n 
A 1 58  GLY 58  53  53  GLY GLY B . n 
A 1 59  GLY 59  54  54  GLY GLY B . n 
A 1 60  GLN 60  55  55  GLN GLN B . n 
A 1 61  ARG 61  56  56  ARG ARG B . n 
A 1 62  ALA 62  57  57  ALA ALA B . n 
A 1 63  ALA 63  58  58  ALA ALA B . n 
A 1 64  TRP 64  59  59  TRP TRP B . n 
A 1 65  ARG 65  60  60  ARG ARG B . n 
A 1 66  VAL 66  61  61  VAL VAL B . n 
A 1 67  LEU 67  62  62  LEU LEU B . n 
A 1 68  SER 68  63  63  SER SER B . n 
A 1 69  SER 69  64  64  SER SER B . n 
A 1 70  ILE 70  65  65  ILE ILE B . n 
A 1 71  GLU 71  66  66  GLU GLU B . n 
A 1 72  GLN 72  67  67  GLN GLN B . n 
A 1 73  LYS 73  68  68  LYS LYS B . n 
A 1 74  SER 74  69  69  SER SER B . n 
A 1 75  ASN 75  70  70  ASN ASN B . n 
A 1 76  GLU 76  71  71  GLU GLU B . n 
A 1 77  GLU 77  72  ?   ?   ?   B . n 
A 1 78  GLY 78  73  ?   ?   ?   B . n 
A 1 79  SER 79  74  74  SER SER B . n 
A 1 80  GLU 80  75  75  GLU GLU B . n 
A 1 81  GLU 81  76  76  GLU GLU B . n 
A 1 82  LYS 82  77  77  LYS LYS B . n 
A 1 83  GLY 83  78  78  GLY GLY B . n 
A 1 84  PRO 84  79  79  PRO PRO B . n 
A 1 85  GLU 85  80  80  GLU GLU B . n 
A 1 86  VAL 86  81  81  VAL VAL B . n 
A 1 87  ARG 87  82  82  ARG ARG B . n 
A 1 88  GLU 88  83  83  GLU GLU B . n 
A 1 89  TYR 89  84  84  TYR TYR B . n 
A 1 90  ARG 90  85  85  ARG ARG B . n 
A 1 91  GLU 91  86  86  GLU GLU B . n 
A 1 92  LYS 92  87  87  LYS LYS B . n 
A 1 93  VAL 93  88  88  VAL VAL B . n 
A 1 94  GLU 94  89  89  GLU GLU B . n 
A 1 95  THR 95  90  90  THR THR B . n 
A 1 96  GLU 96  91  91  GLU GLU B . n 
A 1 97  LEU 97  92  92  LEU LEU B . n 
A 1 98  GLN 98  93  93  GLN GLN B . n 
A 1 99  GLY 99  94  94  GLY GLY B . n 
A 1 100 VAL 100 95  95  VAL VAL B . n 
A 1 101 CYS 101 96  96  CYS CYS B . n 
A 1 102 ASP 102 97  97  ASP ASP B . n 
A 1 103 THR 103 98  98  THR THR B . n 
A 1 104 VAL 104 99  99  VAL VAL B . n 
A 1 105 LEU 105 100 100 LEU LEU B . n 
A 1 106 GLY 106 101 101 GLY GLY B . n 
A 1 107 LEU 107 102 102 LEU LEU B . n 
A 1 108 LEU 108 103 103 LEU LEU B . n 
A 1 109 ASP 109 104 104 ASP ASP B . n 
A 1 110 SER 110 105 105 SER SER B . n 
A 1 111 HIS 111 106 106 HIS HIS B . n 
A 1 112 LEU 112 107 107 LEU LEU B . n 
A 1 113 ILE 113 108 108 ILE ILE B . n 
A 1 114 LYS 114 109 109 LYS LYS B . n 
A 1 115 GLU 115 110 110 GLU GLU B . n 
A 1 116 ALA 116 111 111 ALA ALA B . n 
A 1 117 GLY 117 112 112 GLY GLY B . n 
A 1 118 ASP 118 113 113 ASP ASP B . n 
A 1 119 ALA 119 114 114 ALA ALA B . n 
A 1 120 GLU 120 115 115 GLU GLU B . n 
A 1 121 SER 121 116 116 SER SER B . n 
A 1 122 ARG 122 117 117 ARG ARG B . n 
A 1 123 VAL 123 118 118 VAL VAL B . n 
A 1 124 PHE 124 119 119 PHE PHE B . n 
A 1 125 TYR 125 120 120 TYR TYR B . n 
A 1 126 LEU 126 121 121 LEU LEU B . n 
A 1 127 LYS 127 122 122 LYS LYS B . n 
A 1 128 MET 128 123 123 MET MET B . n 
A 1 129 LYS 129 124 124 LYS LYS B . n 
A 1 130 GLY 130 125 125 GLY GLY B . n 
A 1 131 ASP 131 126 126 ASP ASP B . n 
A 1 132 TYR 132 127 127 TYR TYR B . n 
A 1 133 TYR 133 128 128 TYR TYR B . n 
A 1 134 ARG 134 129 129 ARG ARG B . n 
A 1 135 TYR 135 130 130 TYR TYR B . n 
A 1 136 LEU 136 131 131 LEU LEU B . n 
A 1 137 ALA 137 132 132 ALA ALA B . n 
A 1 138 GLU 138 133 133 GLU GLU B . n 
A 1 139 VAL 139 134 134 VAL VAL B . n 
A 1 140 ALA 140 135 135 ALA ALA B . n 
A 1 141 THR 141 136 136 THR THR B . n 
A 1 142 GLY 142 137 137 GLY GLY B . n 
A 1 143 ASP 143 138 138 ASP ASP B . n 
A 1 144 ASP 144 139 139 ASP ASP B . n 
A 1 145 LYS 145 140 140 LYS LYS B . n 
A 1 146 LYS 146 141 141 LYS LYS B . n 
A 1 147 ARG 147 142 142 ARG ARG B . n 
A 1 148 ILE 148 143 143 ILE ILE B . n 
A 1 149 ILE 149 144 144 ILE ILE B . n 
A 1 150 ASP 150 145 145 ASP ASP B . n 
A 1 151 SER 151 146 146 SER SER B . n 
A 1 152 ALA 152 147 147 ALA ALA B . n 
A 1 153 ARG 153 148 148 ARG ARG B . n 
A 1 154 SER 154 149 149 SER SER B . n 
A 1 155 ALA 155 150 150 ALA ALA B . n 
A 1 156 TYR 156 151 151 TYR TYR B . n 
A 1 157 GLN 157 152 152 GLN GLN B . n 
A 1 158 GLU 158 153 153 GLU GLU B . n 
A 1 159 ALA 159 154 154 ALA ALA B . n 
A 1 160 MET 160 155 155 MET MET B . n 
A 1 161 ASP 161 156 156 ASP ASP B . n 
A 1 162 ILE 162 157 157 ILE ILE B . n 
A 1 163 SER 163 158 158 SER SER B . n 
A 1 164 LYS 164 159 159 LYS LYS B . n 
A 1 165 LYS 165 160 160 LYS LYS B . n 
A 1 166 GLU 166 161 161 GLU GLU B . n 
A 1 167 MET 167 162 162 MET MET B . n 
A 1 168 PRO 168 163 163 PRO PRO B . n 
A 1 169 PRO 169 164 164 PRO PRO B . n 
A 1 170 THR 170 165 165 THR THR B . n 
A 1 171 ASN 171 166 166 ASN ASN B . n 
A 1 172 PRO 172 167 167 PRO PRO B . n 
A 1 173 ILE 173 168 168 ILE ILE B . n 
A 1 174 ARG 174 169 169 ARG ARG B . n 
A 1 175 LEU 175 170 170 LEU LEU B . n 
A 1 176 GLY 176 171 171 GLY GLY B . n 
A 1 177 LEU 177 172 172 LEU LEU B . n 
A 1 178 ALA 178 173 173 ALA ALA B . n 
A 1 179 LEU 179 174 174 LEU LEU B . n 
A 1 180 ASN 180 175 175 ASN ASN B . n 
A 1 181 PHE 181 176 176 PHE PHE B . n 
A 1 182 SER 182 177 177 SER SER B . n 
A 1 183 VAL 183 178 178 VAL VAL B . n 
A 1 184 PHE 184 179 179 PHE PHE B . n 
A 1 185 HIS 185 180 180 HIS HIS B . n 
A 1 186 TYR 186 181 181 TYR TYR B . n 
A 1 187 GLU 187 182 182 GLU GLU B . n 
A 1 188 ILE 188 183 183 ILE ILE B . n 
A 1 189 ALA 189 184 184 ALA ALA B . n 
A 1 190 ASN 190 185 185 ASN ASN B . n 
A 1 191 SER 191 186 186 SER SER B . n 
A 1 192 PRO 192 187 187 PRO PRO B . n 
A 1 193 GLU 193 188 188 GLU GLU B . n 
A 1 194 GLU 194 189 189 GLU GLU B . n 
A 1 195 ALA 195 190 190 ALA ALA B . n 
A 1 196 ILE 196 191 191 ILE ILE B . n 
A 1 197 SER 197 192 192 SER SER B . n 
A 1 198 LEU 198 193 193 LEU LEU B . n 
A 1 199 ALA 199 194 194 ALA ALA B . n 
A 1 200 LYS 200 195 195 LYS LYS B . n 
A 1 201 THR 201 196 196 THR THR B . n 
A 1 202 THR 202 197 197 THR THR B . n 
A 1 203 PHE 203 198 198 PHE PHE B . n 
A 1 204 ASP 204 199 199 ASP ASP B . n 
A 1 205 GLU 205 200 200 GLU GLU B . n 
A 1 206 ALA 206 201 201 ALA ALA B . n 
A 1 207 MET 207 202 202 MET MET B . n 
A 1 208 ALA 208 203 203 ALA ALA B . n 
A 1 209 ASP 209 204 204 ASP ASP B . n 
A 1 210 LEU 210 205 205 LEU LEU B . n 
A 1 211 HIS 211 206 206 HIS HIS B . n 
A 1 212 THR 212 207 207 THR THR B . n 
A 1 213 LEU 213 208 208 LEU LEU B . n 
A 1 214 SER 214 209 209 SER SER B . n 
A 1 215 GLU 215 210 210 GLU GLU B . n 
A 1 216 ASP 216 211 211 ASP ASP B . n 
A 1 217 SER 217 212 212 SER SER B . n 
A 1 218 TYR 218 213 213 TYR TYR B . n 
A 1 219 LYS 219 214 214 LYS LYS B . n 
A 1 220 ASP 220 215 215 ASP ASP B . n 
A 1 221 SER 221 216 216 SER SER B . n 
A 1 222 THR 222 217 217 THR THR B . n 
A 1 223 LEU 223 218 218 LEU LEU B . n 
A 1 224 ILE 224 219 219 ILE ILE B . n 
A 1 225 MET 225 220 220 MET MET B . n 
A 1 226 GLN 226 221 221 GLN GLN B . n 
A 1 227 LEU 227 222 222 LEU LEU B . n 
A 1 228 LEU 228 223 223 LEU LEU B . n 
A 1 229 ARG 229 224 224 ARG ARG B . n 
A 1 230 ASP 230 225 225 ASP ASP B . n 
A 1 231 ASN 231 226 226 ASN ASN B . n 
A 1 232 LEU 232 227 227 LEU LEU B . n 
A 1 233 THR 233 228 228 THR THR B . n 
A 1 234 LEU 234 229 229 LEU LEU B . n 
A 1 235 TRP 235 230 230 TRP TRP B . n 
A 1 236 THR 236 231 231 THR THR B . n 
B 2 1   ASP 1   255 255 ASP ASP P . n 
B 2 2   ARG 2   256 256 ARG ARG P . n 
B 2 3   SER 3   257 257 SER SER P . n 
B 2 4   SER 4   258 258 SER SER P . n 
B 2 5   SEP 5   259 259 SEP SEP P . n 
B 2 6   ALA 6   260 260 ALA ALA P . n 
B 2 7   PRO 7   261 261 PRO PRO P . n 
B 2 8   ASN 8   262 262 ASN ASN P . n 
B 2 9   VAL 9   263 263 VAL VAL P . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        WQN 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   WQN 
_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 3 CL  1   301 263 CL  CL  B . 
D 4 MG  1   302 264 MG  MG  B . 
E 4 MG  1   303 266 MG  MG  B . 
F 5 WQN 1   304 267 WQN 378 B . 
G 6 HOH 1   401 91  HOH HOH B . 
G 6 HOH 2   402 14  HOH HOH B . 
G 6 HOH 3   403 136 HOH HOH B . 
G 6 HOH 4   404 206 HOH HOH B . 
G 6 HOH 5   405 120 HOH HOH B . 
G 6 HOH 6   406 131 HOH HOH B . 
G 6 HOH 7   407 200 HOH HOH B . 
G 6 HOH 8   408 135 HOH HOH B . 
G 6 HOH 9   409 116 HOH HOH B . 
G 6 HOH 10  410 72  HOH HOH B . 
G 6 HOH 11  411 138 HOH HOH B . 
G 6 HOH 12  412 40  HOH HOH B . 
G 6 HOH 13  413 165 HOH HOH B . 
G 6 HOH 14  414 153 HOH HOH B . 
G 6 HOH 15  415 125 HOH HOH B . 
G 6 HOH 16  416 50  HOH HOH B . 
G 6 HOH 17  417 146 HOH HOH B . 
G 6 HOH 18  418 95  HOH HOH B . 
G 6 HOH 19  419 174 HOH HOH B . 
G 6 HOH 20  420 164 HOH HOH B . 
G 6 HOH 21  421 54  HOH HOH B . 
G 6 HOH 22  422 108 HOH HOH B . 
G 6 HOH 23  423 5   HOH HOH B . 
G 6 HOH 24  424 8   HOH HOH B . 
G 6 HOH 25  425 9   HOH HOH B . 
G 6 HOH 26  426 162 HOH HOH B . 
G 6 HOH 27  427 3   HOH HOH B . 
G 6 HOH 28  428 74  HOH HOH B . 
G 6 HOH 29  429 199 HOH HOH B . 
G 6 HOH 30  430 172 HOH HOH B . 
G 6 HOH 31  431 147 HOH HOH B . 
G 6 HOH 32  432 123 HOH HOH B . 
G 6 HOH 33  433 170 HOH HOH B . 
G 6 HOH 34  434 25  HOH HOH B . 
G 6 HOH 35  435 212 HOH HOH B . 
G 6 HOH 36  436 121 HOH HOH B . 
G 6 HOH 37  437 190 HOH HOH B . 
G 6 HOH 38  438 26  HOH HOH B . 
G 6 HOH 39  439 16  HOH HOH B . 
G 6 HOH 40  440 18  HOH HOH B . 
G 6 HOH 41  441 186 HOH HOH B . 
G 6 HOH 42  442 52  HOH HOH B . 
G 6 HOH 43  443 55  HOH HOH B . 
G 6 HOH 44  444 4   HOH HOH B . 
G 6 HOH 45  445 85  HOH HOH B . 
G 6 HOH 46  446 20  HOH HOH B . 
G 6 HOH 47  447 127 HOH HOH B . 
G 6 HOH 48  448 23  HOH HOH B . 
G 6 HOH 49  449 82  HOH HOH B . 
G 6 HOH 50  450 169 HOH HOH B . 
G 6 HOH 51  451 46  HOH HOH B . 
G 6 HOH 52  452 180 HOH HOH B . 
G 6 HOH 53  453 93  HOH HOH B . 
G 6 HOH 54  454 27  HOH HOH B . 
G 6 HOH 55  455 154 HOH HOH B . 
G 6 HOH 56  456 49  HOH HOH B . 
G 6 HOH 57  457 19  HOH HOH B . 
G 6 HOH 58  458 196 HOH HOH B . 
G 6 HOH 59  459 42  HOH HOH B . 
G 6 HOH 60  460 76  HOH HOH B . 
G 6 HOH 61  461 31  HOH HOH B . 
G 6 HOH 62  462 29  HOH HOH B . 
G 6 HOH 63  463 44  HOH HOH B . 
G 6 HOH 64  464 158 HOH HOH B . 
G 6 HOH 65  465 75  HOH HOH B . 
G 6 HOH 66  466 161 HOH HOH B . 
G 6 HOH 67  467 48  HOH HOH B . 
G 6 HOH 68  468 77  HOH HOH B . 
G 6 HOH 69  469 227 HOH HOH B . 
G 6 HOH 70  470 104 HOH HOH B . 
G 6 HOH 71  471 210 HOH HOH B . 
G 6 HOH 72  472 34  HOH HOH B . 
G 6 HOH 73  473 12  HOH HOH B . 
G 6 HOH 74  474 96  HOH HOH B . 
G 6 HOH 75  475 53  HOH HOH B . 
G 6 HOH 76  476 194 HOH HOH B . 
G 6 HOH 77  477 137 HOH HOH B . 
G 6 HOH 78  478 60  HOH HOH B . 
G 6 HOH 79  479 13  HOH HOH B . 
G 6 HOH 80  480 61  HOH HOH B . 
G 6 HOH 81  481 130 HOH HOH B . 
G 6 HOH 82  482 43  HOH HOH B . 
G 6 HOH 83  483 33  HOH HOH B . 
G 6 HOH 84  484 177 HOH HOH B . 
G 6 HOH 85  485 220 HOH HOH B . 
G 6 HOH 86  486 100 HOH HOH B . 
G 6 HOH 87  487 21  HOH HOH B . 
G 6 HOH 88  488 24  HOH HOH B . 
G 6 HOH 89  489 15  HOH HOH B . 
G 6 HOH 90  490 11  HOH HOH B . 
G 6 HOH 91  491 69  HOH HOH B . 
G 6 HOH 92  492 38  HOH HOH B . 
G 6 HOH 93  493 110 HOH HOH B . 
G 6 HOH 94  494 155 HOH HOH B . 
G 6 HOH 95  495 37  HOH HOH B . 
G 6 HOH 96  496 203 HOH HOH B . 
G 6 HOH 97  497 70  HOH HOH B . 
G 6 HOH 98  498 7   HOH HOH B . 
G 6 HOH 99  499 63  HOH HOH B . 
G 6 HOH 100 500 35  HOH HOH B . 
G 6 HOH 101 501 105 HOH HOH B . 
G 6 HOH 102 502 64  HOH HOH B . 
G 6 HOH 103 503 107 HOH HOH B . 
G 6 HOH 104 504 143 HOH HOH B . 
G 6 HOH 105 505 103 HOH HOH B . 
G 6 HOH 106 506 41  HOH HOH B . 
G 6 HOH 107 507 28  HOH HOH B . 
G 6 HOH 108 508 166 HOH HOH B . 
G 6 HOH 109 509 98  HOH HOH B . 
G 6 HOH 110 510 132 HOH HOH B . 
G 6 HOH 111 511 184 HOH HOH B . 
G 6 HOH 112 512 22  HOH HOH B . 
G 6 HOH 113 513 59  HOH HOH B . 
G 6 HOH 114 514 139 HOH HOH B . 
G 6 HOH 115 515 157 HOH HOH B . 
G 6 HOH 116 516 10  HOH HOH B . 
G 6 HOH 117 517 102 HOH HOH B . 
G 6 HOH 118 518 6   HOH HOH B . 
G 6 HOH 119 519 57  HOH HOH B . 
G 6 HOH 120 520 187 HOH HOH B . 
G 6 HOH 121 521 89  HOH HOH B . 
G 6 HOH 122 522 66  HOH HOH B . 
G 6 HOH 123 523 45  HOH HOH B . 
G 6 HOH 124 524 80  HOH HOH B . 
G 6 HOH 125 525 36  HOH HOH B . 
G 6 HOH 126 526 231 HOH HOH B . 
G 6 HOH 127 527 145 HOH HOH B . 
G 6 HOH 128 528 83  HOH HOH B . 
G 6 HOH 129 529 65  HOH HOH B . 
G 6 HOH 130 530 113 HOH HOH B . 
G 6 HOH 131 531 47  HOH HOH B . 
G 6 HOH 132 532 88  HOH HOH B . 
G 6 HOH 133 533 112 HOH HOH B . 
G 6 HOH 134 534 78  HOH HOH B . 
G 6 HOH 135 535 114 HOH HOH B . 
G 6 HOH 136 536 73  HOH HOH B . 
G 6 HOH 137 537 62  HOH HOH B . 
G 6 HOH 138 538 134 HOH HOH B . 
G 6 HOH 139 539 151 HOH HOH B . 
G 6 HOH 140 540 84  HOH HOH B . 
G 6 HOH 141 541 150 HOH HOH B . 
G 6 HOH 142 542 30  HOH HOH B . 
G 6 HOH 143 543 51  HOH HOH B . 
G 6 HOH 144 544 221 HOH HOH B . 
G 6 HOH 145 545 159 HOH HOH B . 
G 6 HOH 146 546 39  HOH HOH B . 
G 6 HOH 147 547 217 HOH HOH B . 
G 6 HOH 148 548 17  HOH HOH B . 
G 6 HOH 149 549 176 HOH HOH B . 
G 6 HOH 150 550 99  HOH HOH B . 
G 6 HOH 151 551 101 HOH HOH B . 
G 6 HOH 152 552 192 HOH HOH B . 
G 6 HOH 153 553 67  HOH HOH B . 
G 6 HOH 154 554 1   HOH HOH B . 
G 6 HOH 155 555 171 HOH HOH B . 
G 6 HOH 156 556 133 HOH HOH B . 
G 6 HOH 157 557 228 HOH HOH B . 
G 6 HOH 158 558 189 HOH HOH B . 
G 6 HOH 159 559 71  HOH HOH B . 
G 6 HOH 160 560 214 HOH HOH B . 
G 6 HOH 161 561 156 HOH HOH B . 
G 6 HOH 162 562 173 HOH HOH B . 
G 6 HOH 163 563 87  HOH HOH B . 
G 6 HOH 164 564 94  HOH HOH B . 
G 6 HOH 165 565 232 HOH HOH B . 
G 6 HOH 166 566 181 HOH HOH B . 
G 6 HOH 167 567 219 HOH HOH B . 
G 6 HOH 168 568 128 HOH HOH B . 
G 6 HOH 169 569 140 HOH HOH B . 
G 6 HOH 170 570 226 HOH HOH B . 
G 6 HOH 171 571 118 HOH HOH B . 
G 6 HOH 172 572 90  HOH HOH B . 
G 6 HOH 173 573 81  HOH HOH B . 
G 6 HOH 174 574 149 HOH HOH B . 
G 6 HOH 175 575 197 HOH HOH B . 
G 6 HOH 176 576 141 HOH HOH B . 
G 6 HOH 177 577 235 HOH HOH B . 
G 6 HOH 178 578 178 HOH HOH B . 
G 6 HOH 179 579 223 HOH HOH B . 
G 6 HOH 180 580 168 HOH HOH B . 
G 6 HOH 181 581 198 HOH HOH B . 
G 6 HOH 182 582 79  HOH HOH B . 
G 6 HOH 183 583 163 HOH HOH B . 
G 6 HOH 184 584 216 HOH HOH B . 
G 6 HOH 185 585 225 HOH HOH B . 
G 6 HOH 186 586 56  HOH HOH B . 
G 6 HOH 187 587 204 HOH HOH B . 
G 6 HOH 188 588 129 HOH HOH B . 
G 6 HOH 189 589 167 HOH HOH B . 
G 6 HOH 190 590 236 HOH HOH B . 
G 6 HOH 191 591 124 HOH HOH B . 
G 6 HOH 192 592 115 HOH HOH B . 
G 6 HOH 193 593 144 HOH HOH B . 
G 6 HOH 194 594 218 HOH HOH B . 
G 6 HOH 195 595 32  HOH HOH B . 
G 6 HOH 196 596 229 HOH HOH B . 
G 6 HOH 197 597 213 HOH HOH B . 
G 6 HOH 198 598 230 HOH HOH B . 
G 6 HOH 199 599 160 HOH HOH B . 
G 6 HOH 200 600 97  HOH HOH B . 
G 6 HOH 201 601 117 HOH HOH B . 
G 6 HOH 202 602 224 HOH HOH B . 
G 6 HOH 203 603 106 HOH HOH B . 
G 6 HOH 204 604 233 HOH HOH B . 
G 6 HOH 205 605 182 HOH HOH B . 
G 6 HOH 206 606 58  HOH HOH B . 
G 6 HOH 207 607 86  HOH HOH B . 
H 6 HOH 1   301 175 HOH HOH P . 
H 6 HOH 2   302 119 HOH HOH P . 
H 6 HOH 3   303 92  HOH HOH P . 
H 6 HOH 4   304 152 HOH HOH P . 
H 6 HOH 5   305 111 HOH HOH P . 
H 6 HOH 6   306 2   HOH HOH P . 
H 6 HOH 7   307 142 HOH HOH P . 
H 6 HOH 8   308 122 HOH HOH P . 
H 6 HOH 9   309 109 HOH HOH P . 
H 6 HOH 10  310 126 HOH HOH P . 
# 
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       ? ? ? ? ? ? ? ? ? ? ? PDB-REDO ? ? ? . 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? autoPROC ? ? ? . 2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless  ? ? ? . 3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? MOLREP   ? ? ? . 4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8VSO 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     82.180 
_cell.length_a_esd                 ? 
_cell.length_b                     112.457 
_cell.length_b_esd                 ? 
_cell.length_c                     62.896 
_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                         8VSO 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                20 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'C 2 2 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                   8VSO 
_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             2.65 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          53.53 
_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              ? 
_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    'PEG4000, HEPES, CaCl2, glycerol' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            277.15 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 4M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-07-12 
_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   0.967697 
_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                        'ESRF BEAMLINE MASSIF-3' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.967697 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   MASSIF-3 
_diffrn_source.pdbx_synchrotron_site       ESRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8VSO 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.5 
_reflns.d_resolution_low                               45.65 
_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                                     46960 
_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                           100 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                11.8 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          14.3 
_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                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.999 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_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                        ? 
# 
_reflns_shell.d_res_high                                    1.5 
_reflns_shell.d_res_low                                     1.53 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.8 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             2289 
_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                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.724 
_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               ? 
# 
_refine.aniso_B[1][1]                            0.89 
_refine.aniso_B[1][2]                            0.00 
_refine.aniso_B[1][3]                            -0.00 
_refine.aniso_B[2][2]                            -0.30 
_refine.aniso_B[2][3]                            0.00 
_refine.aniso_B[3][3]                            -0.59 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               20.550 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  '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                                 8VSO 
_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                            1.50 
_refine.ls_d_res_low                             34.42 
_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                     44581 
_refine.ls_number_reflns_R_free                  2357 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.95 
_refine.ls_percent_reflns_R_free                 5.0 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.16884 
_refine.ls_R_factor_R_free                       0.18877 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.16777 
_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                    ? 
_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                          ? 
_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       ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.063 
_refine.pdbx_overall_ESU_R_Free                  0.064 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_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                             1.244 
_refine.overall_SU_ML                            0.045 
_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                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.50 
_refine_hist.d_res_low                        34.42 
_refine_hist.number_atoms_solvent             217 
_refine_hist.number_atoms_total               2155 
_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       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        1907 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         31 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
_struct.entry_id                     8VSO 
_struct.title                        'Ternary structure of 14-3-3 sigma, BRAF phosphopeptide (pS365) and compound 78 (1124378)' 
_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        8VSO 
_struct_keywords.text            'stabilizer, protein-protein interactions, PEPTIDE BINDING PROTEIN' 
_struct_keywords.pdbx_keywords   'PEPTIDE BINDING PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 4 ? 
F N N 5 ? 
G N N 6 ? 
H N N 6 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP 1433S_HUMAN P31947 ? 1 
;MERASLIQKAKLAEQAERYEDMAAFMKGAVEKGEELSCEERNLLSVAYKNVVGGQRAAWRVLSSIEQKSNEEGSEEKGPE
VREYREKVETELQGVCDTVLGLLDSHLIKEAGDAESRVFYLKMKGDYYRYLAEVATGDDKKRIIDSARSAYQEAMDISKK
EMPPTNPIRLGLALNFSVFHYEIANSPEEAISLAKTTFDEAMADLHTLSEDSYKDSTLIMQLLRDNLTLWT
;
1   
2 UNP BRAF_HUMAN  P15056 ? 2 DRSSSAPNV 361 
# 
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 8VSO B 6 ? 236 ? P31947 1   ? 231 ? 1   231 
2 2 8VSO P 1 ? 9   ? P15056 361 ? 369 ? 255 263 
# 
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 8VSO GLY B 1 ? UNP P31947 ? ? 'expression tag' -4 1 
1 8VSO ALA B 2 ? UNP P31947 ? ? 'expression tag' -3 2 
1 8VSO MET B 3 ? UNP P31947 ? ? 'expression tag' -2 3 
1 8VSO GLY B 4 ? UNP P31947 ? ? 'expression tag' -1 4 
1 8VSO SER B 5 ? UNP P31947 ? ? 'expression tag' 0  5 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   tetrameric 
_pdbx_struct_assembly.oligomeric_count     4 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 5340  ? 
1 MORE         -73   ? 
1 'SSA (A^2)'  23390 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1,2 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H 
# 
_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                ? 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'         1_555 x,y,z   1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000  
0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000  0.0000000000 
2 'crystal symmetry operation' 4_555 x,-y,-z 1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 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 GLU A 7   ? ALA A 21  ? GLU B 2   ALA B 16  1 ? 15 
HELX_P HELX_P2  AA2 ARG A 23  ? LYS A 37  ? ARG B 18  LYS B 32  1 ? 15 
HELX_P HELX_P3  AA3 SER A 42  ? ASN A 75  ? SER B 37  ASN B 70  1 ? 34 
HELX_P HELX_P4  AA4 PRO A 84  ? SER A 110 ? PRO B 79  SER B 105 1 ? 27 
HELX_P HELX_P5  AA5 HIS A 111 ? ALA A 116 ? HIS B 106 ALA B 111 1 ? 6  
HELX_P HELX_P6  AA6 ASP A 118 ? ALA A 140 ? ASP B 113 ALA B 135 1 ? 23 
HELX_P HELX_P7  AA7 ASP A 144 ? MET A 167 ? ASP B 139 MET B 162 1 ? 24 
HELX_P HELX_P8  AA8 ASN A 171 ? ILE A 188 ? ASN B 166 ILE B 183 1 ? 18 
HELX_P HELX_P9  AA9 SER A 191 ? ALA A 208 ? SER B 186 ALA B 203 1 ? 18 
HELX_P HELX_P10 AB1 ASP A 209 ? LEU A 213 ? ASP B 204 LEU B 208 5 ? 5  
HELX_P HELX_P11 AB2 SER A 214 ? THR A 236 ? SER B 209 THR B 231 1 ? 23 
# 
_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 
covale1  covale one  ? A CYS 43  SG  ? ? ? 1_555 F WQN . C2 ? ? B CYS 38  B WQN 304 1_555 ? ? ? ? ? ? ? 1.803 ? ? 
covale2  covale both ? B SER 4   C   ? ? ? 1_555 B SEP 5 N  ? ? P SER 258 P SEP 259 1_555 ? ? ? ? ? ? ? 1.336 ? ? 
covale3  covale both ? B SEP 5   C   ? ? ? 1_555 B ALA 6 N  ? ? P SEP 259 P ALA 260 1_555 ? ? ? ? ? ? ? 1.331 ? ? 
metalc1  metalc ?    ? A GLU 40  OE1 ? ? ? 1_555 E MG  . MG ? ? B GLU 35  B MG  303 6_554 ? ? ? ? ? ? ? 2.598 ? ? 
metalc2  metalc ?    ? A GLU 40  OE2 ? ? ? 1_555 E MG  . MG ? ? B GLU 35  B MG  303 6_554 ? ? ? ? ? ? ? 2.392 ? ? 
metalc3  metalc ?    ? A GLU 94  OE2 ? ? ? 1_555 D MG  . MG ? ? B GLU 89  B MG  302 1_555 ? ? ? ? ? ? ? 2.367 ? ? 
metalc4  metalc ?    ? A GLU 115 O   ? ? ? 1_555 E MG  . MG ? ? B GLU 110 B MG  303 6_554 ? ? ? ? ? ? ? 2.260 ? ? 
metalc5  metalc ?    ? A GLU 193 OE2 ? ? ? 1_555 E MG  . MG ? ? B GLU 188 B MG  303 1_555 ? ? ? ? ? ? ? 2.314 ? ? 
metalc6  metalc ?    ? D MG  .   MG  ? ? ? 1_555 G HOH . O  ? ? B MG  302 B HOH 429 1_555 ? ? ? ? ? ? ? 2.018 ? ? 
metalc7  metalc ?    ? D MG  .   MG  ? ? ? 1_555 G HOH . O  ? ? B MG  302 B HOH 565 1_555 ? ? ? ? ? ? ? 2.198 ? ? 
metalc8  metalc ?    ? E MG  .   MG  ? ? ? 1_555 G HOH . O  ? ? B MG  303 B HOH 517 1_555 ? ? ? ? ? ? ? 2.397 ? ? 
metalc9  metalc ?    ? E MG  .   MG  ? ? ? 1_555 G HOH . O  ? ? B MG  303 B HOH 529 6_555 ? ? ? ? ? ? ? 2.362 ? ? 
metalc10 metalc ?    ? E MG  .   MG  ? ? ? 1_555 G HOH . O  ? ? B MG  303 B HOH 557 6_555 ? ? ? ? ? ? ? 2.423 ? ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
covale ? ? 
metalc ? ? 
# 
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  OE1 ? A GLU 40  ? B GLU 35  ? 1_555 MG ? E MG . ? B MG 303 ? 6_554 OE2 ? A GLU 40  ? B GLU 35  ? 1_555 51.8  ? 
2  OE1 ? A GLU 40  ? B GLU 35  ? 1_555 MG ? E MG . ? B MG 303 ? 6_554 O   ? A GLU 115 ? B GLU 110 ? 1_555 87.8  ? 
3  OE2 ? A GLU 40  ? B GLU 35  ? 1_555 MG ? E MG . ? B MG 303 ? 6_554 O   ? A GLU 115 ? B GLU 110 ? 1_555 87.3  ? 
4  OE1 ? A GLU 40  ? B GLU 35  ? 1_555 MG ? E MG . ? B MG 303 ? 6_554 OE2 ? A GLU 193 ? B GLU 188 ? 1_555 87.9  ? 
5  OE2 ? A GLU 40  ? B GLU 35  ? 1_555 MG ? E MG . ? B MG 303 ? 6_554 OE2 ? A GLU 193 ? B GLU 188 ? 1_555 122.0 ? 
6  O   ? A GLU 115 ? B GLU 110 ? 1_555 MG ? E MG . ? B MG 303 ? 6_554 OE2 ? A GLU 193 ? B GLU 188 ? 1_555 46.3  ? 
7  OE1 ? A GLU 40  ? B GLU 35  ? 1_555 MG ? E MG . ? B MG 303 ? 6_554 O   ? G HOH .   ? B HOH 517 ? 1_555 85.1  ? 
8  OE2 ? A GLU 40  ? B GLU 35  ? 1_555 MG ? E MG . ? B MG 303 ? 6_554 O   ? G HOH .   ? B HOH 517 ? 1_555 119.7 ? 
9  O   ? A GLU 115 ? B GLU 110 ? 1_555 MG ? E MG . ? B MG 303 ? 6_554 O   ? G HOH .   ? B HOH 517 ? 1_555 46.1  ? 
10 OE2 ? A GLU 193 ? B GLU 188 ? 1_555 MG ? E MG . ? B MG 303 ? 6_554 O   ? G HOH .   ? B HOH 517 ? 1_555 2.8   ? 
11 OE1 ? A GLU 40  ? B GLU 35  ? 1_555 MG ? E MG . ? B MG 303 ? 6_554 O   ? G HOH .   ? B HOH 529 ? 6_555 85.3  ? 
12 OE2 ? A GLU 40  ? B GLU 35  ? 1_555 MG ? E MG . ? B MG 303 ? 6_554 O   ? G HOH .   ? B HOH 529 ? 6_555 122.3 ? 
13 O   ? A GLU 115 ? B GLU 110 ? 1_555 MG ? E MG . ? B MG 303 ? 6_554 O   ? G HOH .   ? B HOH 529 ? 6_555 50.0  ? 
14 OE2 ? A GLU 193 ? B GLU 188 ? 1_555 MG ? E MG . ? B MG 303 ? 6_554 O   ? G HOH .   ? B HOH 529 ? 6_555 4.6   ? 
15 O   ? G HOH .   ? B HOH 517 ? 1_555 MG ? E MG . ? B MG 303 ? 6_554 O   ? G HOH .   ? B HOH 529 ? 6_555 3.9   ? 
16 OE1 ? A GLU 40  ? B GLU 35  ? 1_555 MG ? E MG . ? B MG 303 ? 6_554 O   ? G HOH .   ? B HOH 557 ? 6_555 83.9  ? 
17 OE2 ? A GLU 40  ? B GLU 35  ? 1_555 MG ? E MG . ? B MG 303 ? 6_554 O   ? G HOH .   ? B HOH 557 ? 6_555 120.8 ? 
18 O   ? A GLU 115 ? B GLU 110 ? 1_555 MG ? E MG . ? B MG 303 ? 6_554 O   ? G HOH .   ? B HOH 557 ? 6_555 49.4  ? 
19 OE2 ? A GLU 193 ? B GLU 188 ? 1_555 MG ? E MG . ? B MG 303 ? 6_554 O   ? G HOH .   ? B HOH 557 ? 6_555 5.1   ? 
20 O   ? G HOH .   ? B HOH 517 ? 1_555 MG ? E MG . ? B MG 303 ? 6_554 O   ? G HOH .   ? B HOH 557 ? 6_555 3.4   ? 
21 O   ? G HOH .   ? B HOH 529 ? 6_555 MG ? E MG . ? B MG 303 ? 6_554 O   ? G HOH .   ? B HOH 557 ? 6_555 1.6   ? 
22 OE2 ? A GLU 94  ? B GLU 89  ? 1_555 MG ? D MG . ? B MG 302 ? 1_555 O   ? G HOH .   ? B HOH 429 ? 1_555 87.9  ? 
23 OE2 ? A GLU 94  ? B GLU 89  ? 1_555 MG ? D MG . ? B MG 302 ? 1_555 O   ? G HOH .   ? B HOH 565 ? 1_555 106.6 ? 
24 O   ? G HOH .   ? B HOH 429 ? 1_555 MG ? D MG . ? B MG 302 ? 1_555 O   ? G HOH .   ? B HOH 565 ? 1_555 74.1  ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 SEP B 5 ? .   . .  . SEP P 259 ? 1_555 .   . .  . .     .  .  SER 1 SEP Phosphorylation 'Named protein modification'     
2 WQN F . ? CYS A 43 ? WQN B 304 ? 1_555 CYS B 38 ? 1_555 C2 SG CYS 1 WQN None            'Covalent chemical modification' 
# 
_struct_mon_prot_cis.pdbx_id                1 
_struct_mon_prot_cis.label_comp_id          SER 
_struct_mon_prot_cis.label_seq_id           110 
_struct_mon_prot_cis.label_asym_id          A 
_struct_mon_prot_cis.label_alt_id           . 
_struct_mon_prot_cis.pdbx_PDB_ins_code      ? 
_struct_mon_prot_cis.auth_comp_id           SER 
_struct_mon_prot_cis.auth_seq_id            105 
_struct_mon_prot_cis.auth_asym_id           B 
_struct_mon_prot_cis.pdbx_label_comp_id_2   HIS 
_struct_mon_prot_cis.pdbx_label_seq_id_2    111 
_struct_mon_prot_cis.pdbx_label_asym_id_2   A 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2    ? 
_struct_mon_prot_cis.pdbx_auth_comp_id_2    HIS 
_struct_mon_prot_cis.pdbx_auth_seq_id_2     106 
_struct_mon_prot_cis.pdbx_auth_asym_id_2    B 
_struct_mon_prot_cis.pdbx_PDB_model_num     1 
_struct_mon_prot_cis.pdbx_omega_angle       12.70 
# 
_pdbx_entry_details.entry_id                   8VSO 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   Y 
# 
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 ARG B 18  ? ? -104.58 75.39 
2 1 HIS B 106 ? ? -148.64 36.73 
3 1 THR B 136 ? ? -146.13 -5.62 
# 
_pdbx_struct_mod_residue.id               1 
_pdbx_struct_mod_residue.label_asym_id    B 
_pdbx_struct_mod_residue.label_comp_id    SEP 
_pdbx_struct_mod_residue.label_seq_id     5 
_pdbx_struct_mod_residue.auth_asym_id     P 
_pdbx_struct_mod_residue.auth_comp_id     SEP 
_pdbx_struct_mod_residue.auth_seq_id      259 
_pdbx_struct_mod_residue.PDB_ins_code     ? 
_pdbx_struct_mod_residue.parent_comp_id   SER 
_pdbx_struct_mod_residue.details          'modified residue' 
# 
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 B GLU 72 ? A GLU 77 
2 1 Y 1 B GLY 73 ? A GLY 78 
# 
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 
ALA N    N  N N 1   
ALA CA   C  N S 2   
ALA C    C  N N 3   
ALA O    O  N N 4   
ALA CB   C  N N 5   
ALA OXT  O  N N 6   
ALA H    H  N N 7   
ALA H2   H  N N 8   
ALA HA   H  N N 9   
ALA HB1  H  N N 10  
ALA HB2  H  N N 11  
ALA HB3  H  N N 12  
ALA HXT  H  N N 13  
ARG N    N  N N 14  
ARG CA   C  N S 15  
ARG C    C  N N 16  
ARG O    O  N N 17  
ARG CB   C  N N 18  
ARG CG   C  N N 19  
ARG CD   C  N N 20  
ARG NE   N  N N 21  
ARG CZ   C  N N 22  
ARG NH1  N  N N 23  
ARG NH2  N  N N 24  
ARG OXT  O  N N 25  
ARG H    H  N N 26  
ARG H2   H  N N 27  
ARG HA   H  N N 28  
ARG HB2  H  N N 29  
ARG HB3  H  N N 30  
ARG HG2  H  N N 31  
ARG HG3  H  N N 32  
ARG HD2  H  N N 33  
ARG HD3  H  N N 34  
ARG HE   H  N N 35  
ARG HH11 H  N N 36  
ARG HH12 H  N N 37  
ARG HH21 H  N N 38  
ARG HH22 H  N N 39  
ARG HXT  H  N N 40  
ASN N    N  N N 41  
ASN CA   C  N S 42  
ASN C    C  N N 43  
ASN O    O  N N 44  
ASN CB   C  N N 45  
ASN CG   C  N N 46  
ASN OD1  O  N N 47  
ASN ND2  N  N N 48  
ASN OXT  O  N N 49  
ASN H    H  N N 50  
ASN H2   H  N N 51  
ASN HA   H  N N 52  
ASN HB2  H  N N 53  
ASN HB3  H  N N 54  
ASN HD21 H  N N 55  
ASN HD22 H  N N 56  
ASN HXT  H  N N 57  
ASP N    N  N N 58  
ASP CA   C  N S 59  
ASP C    C  N N 60  
ASP O    O  N N 61  
ASP CB   C  N N 62  
ASP CG   C  N N 63  
ASP OD1  O  N N 64  
ASP OD2  O  N N 65  
ASP OXT  O  N N 66  
ASP H    H  N N 67  
ASP H2   H  N N 68  
ASP HA   H  N N 69  
ASP HB2  H  N N 70  
ASP HB3  H  N N 71  
ASP HD2  H  N N 72  
ASP HXT  H  N N 73  
CL  CL   CL N N 74  
CYS N    N  N N 75  
CYS CA   C  N R 76  
CYS C    C  N N 77  
CYS O    O  N N 78  
CYS CB   C  N N 79  
CYS SG   S  N N 80  
CYS OXT  O  N N 81  
CYS H    H  N N 82  
CYS H2   H  N N 83  
CYS HA   H  N N 84  
CYS HB2  H  N N 85  
CYS HB3  H  N N 86  
CYS HG   H  N N 87  
CYS HXT  H  N N 88  
GLN N    N  N N 89  
GLN CA   C  N S 90  
GLN C    C  N N 91  
GLN O    O  N N 92  
GLN CB   C  N N 93  
GLN CG   C  N N 94  
GLN CD   C  N N 95  
GLN OE1  O  N N 96  
GLN NE2  N  N N 97  
GLN OXT  O  N N 98  
GLN H    H  N N 99  
GLN H2   H  N N 100 
GLN HA   H  N N 101 
GLN HB2  H  N N 102 
GLN HB3  H  N N 103 
GLN HG2  H  N N 104 
GLN HG3  H  N N 105 
GLN HE21 H  N N 106 
GLN HE22 H  N N 107 
GLN HXT  H  N N 108 
GLU N    N  N N 109 
GLU CA   C  N S 110 
GLU C    C  N N 111 
GLU O    O  N N 112 
GLU CB   C  N N 113 
GLU CG   C  N N 114 
GLU CD   C  N N 115 
GLU OE1  O  N N 116 
GLU OE2  O  N N 117 
GLU OXT  O  N N 118 
GLU H    H  N N 119 
GLU H2   H  N N 120 
GLU HA   H  N N 121 
GLU HB2  H  N N 122 
GLU HB3  H  N N 123 
GLU HG2  H  N N 124 
GLU HG3  H  N N 125 
GLU HE2  H  N N 126 
GLU HXT  H  N N 127 
GLY N    N  N N 128 
GLY CA   C  N N 129 
GLY C    C  N N 130 
GLY O    O  N N 131 
GLY OXT  O  N N 132 
GLY H    H  N N 133 
GLY H2   H  N N 134 
GLY HA2  H  N N 135 
GLY HA3  H  N N 136 
GLY HXT  H  N N 137 
HIS N    N  N N 138 
HIS CA   C  N S 139 
HIS C    C  N N 140 
HIS O    O  N N 141 
HIS CB   C  N N 142 
HIS CG   C  Y N 143 
HIS ND1  N  Y N 144 
HIS CD2  C  Y N 145 
HIS CE1  C  Y N 146 
HIS NE2  N  Y N 147 
HIS OXT  O  N N 148 
HIS H    H  N N 149 
HIS H2   H  N N 150 
HIS HA   H  N N 151 
HIS HB2  H  N N 152 
HIS HB3  H  N N 153 
HIS HD1  H  N N 154 
HIS HD2  H  N N 155 
HIS HE1  H  N N 156 
HIS HE2  H  N N 157 
HIS HXT  H  N N 158 
HOH O    O  N N 159 
HOH H1   H  N N 160 
HOH H2   H  N N 161 
ILE N    N  N N 162 
ILE CA   C  N S 163 
ILE C    C  N N 164 
ILE O    O  N N 165 
ILE CB   C  N S 166 
ILE CG1  C  N N 167 
ILE CG2  C  N N 168 
ILE CD1  C  N N 169 
ILE OXT  O  N N 170 
ILE H    H  N N 171 
ILE H2   H  N N 172 
ILE HA   H  N N 173 
ILE HB   H  N N 174 
ILE HG12 H  N N 175 
ILE HG13 H  N N 176 
ILE HG21 H  N N 177 
ILE HG22 H  N N 178 
ILE HG23 H  N N 179 
ILE HD11 H  N N 180 
ILE HD12 H  N N 181 
ILE HD13 H  N N 182 
ILE HXT  H  N N 183 
LEU N    N  N N 184 
LEU CA   C  N S 185 
LEU C    C  N N 186 
LEU O    O  N N 187 
LEU CB   C  N N 188 
LEU CG   C  N N 189 
LEU CD1  C  N N 190 
LEU CD2  C  N N 191 
LEU OXT  O  N N 192 
LEU H    H  N N 193 
LEU H2   H  N N 194 
LEU HA   H  N N 195 
LEU HB2  H  N N 196 
LEU HB3  H  N N 197 
LEU HG   H  N N 198 
LEU HD11 H  N N 199 
LEU HD12 H  N N 200 
LEU HD13 H  N N 201 
LEU HD21 H  N N 202 
LEU HD22 H  N N 203 
LEU HD23 H  N N 204 
LEU HXT  H  N N 205 
LYS N    N  N N 206 
LYS CA   C  N S 207 
LYS C    C  N N 208 
LYS O    O  N N 209 
LYS CB   C  N N 210 
LYS CG   C  N N 211 
LYS CD   C  N N 212 
LYS CE   C  N N 213 
LYS NZ   N  N N 214 
LYS OXT  O  N N 215 
LYS H    H  N N 216 
LYS H2   H  N N 217 
LYS HA   H  N N 218 
LYS HB2  H  N N 219 
LYS HB3  H  N N 220 
LYS HG2  H  N N 221 
LYS HG3  H  N N 222 
LYS HD2  H  N N 223 
LYS HD3  H  N N 224 
LYS HE2  H  N N 225 
LYS HE3  H  N N 226 
LYS HZ1  H  N N 227 
LYS HZ2  H  N N 228 
LYS HZ3  H  N N 229 
LYS HXT  H  N N 230 
MET N    N  N N 231 
MET CA   C  N S 232 
MET C    C  N N 233 
MET O    O  N N 234 
MET CB   C  N N 235 
MET CG   C  N N 236 
MET SD   S  N N 237 
MET CE   C  N N 238 
MET OXT  O  N N 239 
MET H    H  N N 240 
MET H2   H  N N 241 
MET HA   H  N N 242 
MET HB2  H  N N 243 
MET HB3  H  N N 244 
MET HG2  H  N N 245 
MET HG3  H  N N 246 
MET HE1  H  N N 247 
MET HE2  H  N N 248 
MET HE3  H  N N 249 
MET HXT  H  N N 250 
MG  MG   MG N N 251 
PHE N    N  N N 252 
PHE CA   C  N S 253 
PHE C    C  N N 254 
PHE O    O  N N 255 
PHE CB   C  N N 256 
PHE CG   C  Y N 257 
PHE CD1  C  Y N 258 
PHE CD2  C  Y N 259 
PHE CE1  C  Y N 260 
PHE CE2  C  Y N 261 
PHE CZ   C  Y N 262 
PHE OXT  O  N N 263 
PHE H    H  N N 264 
PHE H2   H  N N 265 
PHE HA   H  N N 266 
PHE HB2  H  N N 267 
PHE HB3  H  N N 268 
PHE HD1  H  N N 269 
PHE HD2  H  N N 270 
PHE HE1  H  N N 271 
PHE HE2  H  N N 272 
PHE HZ   H  N N 273 
PHE HXT  H  N N 274 
PRO N    N  N N 275 
PRO CA   C  N S 276 
PRO C    C  N N 277 
PRO O    O  N N 278 
PRO CB   C  N N 279 
PRO CG   C  N N 280 
PRO CD   C  N N 281 
PRO OXT  O  N N 282 
PRO H    H  N N 283 
PRO HA   H  N N 284 
PRO HB2  H  N N 285 
PRO HB3  H  N N 286 
PRO HG2  H  N N 287 
PRO HG3  H  N N 288 
PRO HD2  H  N N 289 
PRO HD3  H  N N 290 
PRO HXT  H  N N 291 
SEP N    N  N N 292 
SEP CA   C  N S 293 
SEP CB   C  N N 294 
SEP OG   O  N N 295 
SEP C    C  N N 296 
SEP O    O  N N 297 
SEP OXT  O  N N 298 
SEP P    P  N N 299 
SEP O1P  O  N N 300 
SEP O2P  O  N N 301 
SEP O3P  O  N N 302 
SEP H    H  N N 303 
SEP H2   H  N N 304 
SEP HA   H  N N 305 
SEP HB2  H  N N 306 
SEP HB3  H  N N 307 
SEP HXT  H  N N 308 
SEP HOP2 H  N N 309 
SEP HOP3 H  N N 310 
SER N    N  N N 311 
SER CA   C  N S 312 
SER C    C  N N 313 
SER O    O  N N 314 
SER CB   C  N N 315 
SER OG   O  N N 316 
SER OXT  O  N N 317 
SER H    H  N N 318 
SER H2   H  N N 319 
SER HA   H  N N 320 
SER HB2  H  N N 321 
SER HB3  H  N N 322 
SER HG   H  N N 323 
SER HXT  H  N N 324 
THR N    N  N N 325 
THR CA   C  N S 326 
THR C    C  N N 327 
THR O    O  N N 328 
THR CB   C  N R 329 
THR OG1  O  N N 330 
THR CG2  C  N N 331 
THR OXT  O  N N 332 
THR H    H  N N 333 
THR H2   H  N N 334 
THR HA   H  N N 335 
THR HB   H  N N 336 
THR HG1  H  N N 337 
THR HG21 H  N N 338 
THR HG22 H  N N 339 
THR HG23 H  N N 340 
THR HXT  H  N N 341 
TRP N    N  N N 342 
TRP CA   C  N S 343 
TRP C    C  N N 344 
TRP O    O  N N 345 
TRP CB   C  N N 346 
TRP CG   C  Y N 347 
TRP CD1  C  Y N 348 
TRP CD2  C  Y N 349 
TRP NE1  N  Y N 350 
TRP CE2  C  Y N 351 
TRP CE3  C  Y N 352 
TRP CZ2  C  Y N 353 
TRP CZ3  C  Y N 354 
TRP CH2  C  Y N 355 
TRP OXT  O  N N 356 
TRP H    H  N N 357 
TRP H2   H  N N 358 
TRP HA   H  N N 359 
TRP HB2  H  N N 360 
TRP HB3  H  N N 361 
TRP HD1  H  N N 362 
TRP HE1  H  N N 363 
TRP HE3  H  N N 364 
TRP HZ2  H  N N 365 
TRP HZ3  H  N N 366 
TRP HH2  H  N N 367 
TRP HXT  H  N N 368 
TYR N    N  N N 369 
TYR CA   C  N S 370 
TYR C    C  N N 371 
TYR O    O  N N 372 
TYR CB   C  N N 373 
TYR CG   C  Y N 374 
TYR CD1  C  Y N 375 
TYR CD2  C  Y N 376 
TYR CE1  C  Y N 377 
TYR CE2  C  Y N 378 
TYR CZ   C  Y N 379 
TYR OH   O  N N 380 
TYR OXT  O  N N 381 
TYR H    H  N N 382 
TYR H2   H  N N 383 
TYR HA   H  N N 384 
TYR HB2  H  N N 385 
TYR HB3  H  N N 386 
TYR HD1  H  N N 387 
TYR HD2  H  N N 388 
TYR HE1  H  N N 389 
TYR HE2  H  N N 390 
TYR HH   H  N N 391 
TYR HXT  H  N N 392 
VAL N    N  N N 393 
VAL CA   C  N S 394 
VAL C    C  N N 395 
VAL O    O  N N 396 
VAL CB   C  N N 397 
VAL CG1  C  N N 398 
VAL CG2  C  N N 399 
VAL OXT  O  N N 400 
VAL H    H  N N 401 
VAL H2   H  N N 402 
VAL HA   H  N N 403 
VAL HB   H  N N 404 
VAL HG11 H  N N 405 
VAL HG12 H  N N 406 
VAL HG13 H  N N 407 
VAL HG21 H  N N 408 
VAL HG22 H  N N 409 
VAL HG23 H  N N 410 
VAL HXT  H  N N 411 
WQN C1   C  N N 412 
WQN C10  C  Y N 413 
WQN C11  C  Y N 414 
WQN C12  C  Y N 415 
WQN C13  C  N N 416 
WQN C14  C  N N 417 
WQN C2   C  N N 418 
WQN C3   C  N N 419 
WQN C4   C  N N 420 
WQN C5   C  N N 421 
WQN C6   C  N N 422 
WQN C7   C  Y N 423 
WQN C8   C  Y N 424 
WQN C9   C  Y N 425 
WQN N1   N  N N 426 
WQN N2   N  N N 427 
WQN O1   O  N N 428 
WQN O2   O  N N 429 
WQN O3   O  N N 430 
WQN O4   O  N N 431 
WQN S1   S  N N 432 
WQN BR1  BR N N 433 
WQN H1   H  N N 434 
WQN H2   H  N N 435 
WQN H3   H  N N 436 
WQN H4   H  N N 437 
WQN H5   H  N N 438 
WQN H6   H  N N 439 
WQN H7   H  N N 440 
WQN H8   H  N N 441 
WQN H10  H  N N 442 
WQN H11  H  N N 443 
WQN H12  H  N N 444 
WQN H13  H  N N 445 
WQN H14  H  N N 446 
WQN H15  H  N N 447 
WQN H16  H  N N 448 
WQN H17  H  N N 449 
WQN CL1  CL N N 450 
# 
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 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
HIS N   CA   sing N N 129 
HIS N   H    sing N N 130 
HIS N   H2   sing N N 131 
HIS CA  C    sing N N 132 
HIS CA  CB   sing N N 133 
HIS CA  HA   sing N N 134 
HIS C   O    doub N N 135 
HIS C   OXT  sing N N 136 
HIS CB  CG   sing N N 137 
HIS CB  HB2  sing N N 138 
HIS CB  HB3  sing N N 139 
HIS CG  ND1  sing Y N 140 
HIS CG  CD2  doub Y N 141 
HIS ND1 CE1  doub Y N 142 
HIS ND1 HD1  sing N N 143 
HIS CD2 NE2  sing Y N 144 
HIS CD2 HD2  sing N N 145 
HIS CE1 NE2  sing Y N 146 
HIS CE1 HE1  sing N N 147 
HIS NE2 HE2  sing N N 148 
HIS OXT HXT  sing N N 149 
HOH O   H1   sing N N 150 
HOH O   H2   sing N N 151 
ILE N   CA   sing N N 152 
ILE N   H    sing N N 153 
ILE N   H2   sing N N 154 
ILE CA  C    sing N N 155 
ILE CA  CB   sing N N 156 
ILE CA  HA   sing N N 157 
ILE C   O    doub N N 158 
ILE C   OXT  sing N N 159 
ILE CB  CG1  sing N N 160 
ILE CB  CG2  sing N N 161 
ILE CB  HB   sing N N 162 
ILE CG1 CD1  sing N N 163 
ILE CG1 HG12 sing N N 164 
ILE CG1 HG13 sing N N 165 
ILE CG2 HG21 sing N N 166 
ILE CG2 HG22 sing N N 167 
ILE CG2 HG23 sing N N 168 
ILE CD1 HD11 sing N N 169 
ILE CD1 HD12 sing N N 170 
ILE CD1 HD13 sing N N 171 
ILE OXT HXT  sing N N 172 
LEU N   CA   sing N N 173 
LEU N   H    sing N N 174 
LEU N   H2   sing N N 175 
LEU CA  C    sing N N 176 
LEU CA  CB   sing N N 177 
LEU CA  HA   sing N N 178 
LEU C   O    doub N N 179 
LEU C   OXT  sing N N 180 
LEU CB  CG   sing N N 181 
LEU CB  HB2  sing N N 182 
LEU CB  HB3  sing N N 183 
LEU CG  CD1  sing N N 184 
LEU CG  CD2  sing N N 185 
LEU CG  HG   sing N N 186 
LEU CD1 HD11 sing N N 187 
LEU CD1 HD12 sing N N 188 
LEU CD1 HD13 sing N N 189 
LEU CD2 HD21 sing N N 190 
LEU CD2 HD22 sing N N 191 
LEU CD2 HD23 sing N N 192 
LEU OXT HXT  sing N N 193 
LYS N   CA   sing N N 194 
LYS N   H    sing N N 195 
LYS N   H2   sing N N 196 
LYS CA  C    sing N N 197 
LYS CA  CB   sing N N 198 
LYS CA  HA   sing N N 199 
LYS C   O    doub N N 200 
LYS C   OXT  sing N N 201 
LYS CB  CG   sing N N 202 
LYS CB  HB2  sing N N 203 
LYS CB  HB3  sing N N 204 
LYS CG  CD   sing N N 205 
LYS CG  HG2  sing N N 206 
LYS CG  HG3  sing N N 207 
LYS CD  CE   sing N N 208 
LYS CD  HD2  sing N N 209 
LYS CD  HD3  sing N N 210 
LYS CE  NZ   sing N N 211 
LYS CE  HE2  sing N N 212 
LYS CE  HE3  sing N N 213 
LYS NZ  HZ1  sing N N 214 
LYS NZ  HZ2  sing N N 215 
LYS NZ  HZ3  sing N N 216 
LYS OXT HXT  sing N N 217 
MET N   CA   sing N N 218 
MET N   H    sing N N 219 
MET N   H2   sing N N 220 
MET CA  C    sing N N 221 
MET CA  CB   sing N N 222 
MET CA  HA   sing N N 223 
MET C   O    doub N N 224 
MET C   OXT  sing N N 225 
MET CB  CG   sing N N 226 
MET CB  HB2  sing N N 227 
MET CB  HB3  sing N N 228 
MET CG  SD   sing N N 229 
MET CG  HG2  sing N N 230 
MET CG  HG3  sing N N 231 
MET SD  CE   sing N N 232 
MET CE  HE1  sing N N 233 
MET CE  HE2  sing N N 234 
MET CE  HE3  sing N N 235 
MET OXT HXT  sing N N 236 
PHE N   CA   sing N N 237 
PHE N   H    sing N N 238 
PHE N   H2   sing N N 239 
PHE CA  C    sing N N 240 
PHE CA  CB   sing N N 241 
PHE CA  HA   sing N N 242 
PHE C   O    doub N N 243 
PHE C   OXT  sing N N 244 
PHE CB  CG   sing N N 245 
PHE CB  HB2  sing N N 246 
PHE CB  HB3  sing N N 247 
PHE CG  CD1  doub Y N 248 
PHE CG  CD2  sing Y N 249 
PHE CD1 CE1  sing Y N 250 
PHE CD1 HD1  sing N N 251 
PHE CD2 CE2  doub Y N 252 
PHE CD2 HD2  sing N N 253 
PHE CE1 CZ   doub Y N 254 
PHE CE1 HE1  sing N N 255 
PHE CE2 CZ   sing Y N 256 
PHE CE2 HE2  sing N N 257 
PHE CZ  HZ   sing N N 258 
PHE OXT HXT  sing N N 259 
PRO N   CA   sing N N 260 
PRO N   CD   sing N N 261 
PRO N   H    sing N N 262 
PRO CA  C    sing N N 263 
PRO CA  CB   sing N N 264 
PRO CA  HA   sing N N 265 
PRO C   O    doub N N 266 
PRO C   OXT  sing N N 267 
PRO CB  CG   sing N N 268 
PRO CB  HB2  sing N N 269 
PRO CB  HB3  sing N N 270 
PRO CG  CD   sing N N 271 
PRO CG  HG2  sing N N 272 
PRO CG  HG3  sing N N 273 
PRO CD  HD2  sing N N 274 
PRO CD  HD3  sing N N 275 
PRO OXT HXT  sing N N 276 
SEP N   CA   sing N N 277 
SEP N   H    sing N N 278 
SEP N   H2   sing N N 279 
SEP CA  CB   sing N N 280 
SEP CA  C    sing N N 281 
SEP CA  HA   sing N N 282 
SEP CB  OG   sing N N 283 
SEP CB  HB2  sing N N 284 
SEP CB  HB3  sing N N 285 
SEP OG  P    sing N N 286 
SEP C   O    doub N N 287 
SEP C   OXT  sing N N 288 
SEP OXT HXT  sing N N 289 
SEP P   O1P  doub N N 290 
SEP P   O2P  sing N N 291 
SEP P   O3P  sing N N 292 
SEP O2P HOP2 sing N N 293 
SEP O3P HOP3 sing N N 294 
SER N   CA   sing N N 295 
SER N   H    sing N N 296 
SER N   H2   sing N N 297 
SER CA  C    sing N N 298 
SER CA  CB   sing N N 299 
SER CA  HA   sing N N 300 
SER C   O    doub N N 301 
SER C   OXT  sing N N 302 
SER CB  OG   sing N N 303 
SER CB  HB2  sing N N 304 
SER CB  HB3  sing N N 305 
SER OG  HG   sing N N 306 
SER OXT HXT  sing N N 307 
THR N   CA   sing N N 308 
THR N   H    sing N N 309 
THR N   H2   sing N N 310 
THR CA  C    sing N N 311 
THR CA  CB   sing N N 312 
THR CA  HA   sing N N 313 
THR C   O    doub N N 314 
THR C   OXT  sing N N 315 
THR CB  OG1  sing N N 316 
THR CB  CG2  sing N N 317 
THR CB  HB   sing N N 318 
THR OG1 HG1  sing N N 319 
THR CG2 HG21 sing N N 320 
THR CG2 HG22 sing N N 321 
THR CG2 HG23 sing N N 322 
THR OXT HXT  sing N N 323 
TRP N   CA   sing N N 324 
TRP N   H    sing N N 325 
TRP N   H2   sing N N 326 
TRP CA  C    sing N N 327 
TRP CA  CB   sing N N 328 
TRP CA  HA   sing N N 329 
TRP C   O    doub N N 330 
TRP C   OXT  sing N N 331 
TRP CB  CG   sing N N 332 
TRP CB  HB2  sing N N 333 
TRP CB  HB3  sing N N 334 
TRP CG  CD1  doub Y N 335 
TRP CG  CD2  sing Y N 336 
TRP CD1 NE1  sing Y N 337 
TRP CD1 HD1  sing N N 338 
TRP CD2 CE2  doub Y N 339 
TRP CD2 CE3  sing Y N 340 
TRP NE1 CE2  sing Y N 341 
TRP NE1 HE1  sing N N 342 
TRP CE2 CZ2  sing Y N 343 
TRP CE3 CZ3  doub Y N 344 
TRP CE3 HE3  sing N N 345 
TRP CZ2 CH2  doub Y N 346 
TRP CZ2 HZ2  sing N N 347 
TRP CZ3 CH2  sing Y N 348 
TRP CZ3 HZ3  sing N N 349 
TRP CH2 HH2  sing N N 350 
TRP OXT HXT  sing N N 351 
TYR N   CA   sing N N 352 
TYR N   H    sing N N 353 
TYR N   H2   sing N N 354 
TYR CA  C    sing N N 355 
TYR CA  CB   sing N N 356 
TYR CA  HA   sing N N 357 
TYR C   O    doub N N 358 
TYR C   OXT  sing N N 359 
TYR CB  CG   sing N N 360 
TYR CB  HB2  sing N N 361 
TYR CB  HB3  sing N N 362 
TYR CG  CD1  doub Y N 363 
TYR CG  CD2  sing Y N 364 
TYR CD1 CE1  sing Y N 365 
TYR CD1 HD1  sing N N 366 
TYR CD2 CE2  doub Y N 367 
TYR CD2 HD2  sing N N 368 
TYR CE1 CZ   doub Y N 369 
TYR CE1 HE1  sing N N 370 
TYR CE2 CZ   sing Y N 371 
TYR CE2 HE2  sing N N 372 
TYR CZ  OH   sing N N 373 
TYR OH  HH   sing N N 374 
TYR OXT HXT  sing N N 375 
VAL N   CA   sing N N 376 
VAL N   H    sing N N 377 
VAL N   H2   sing N N 378 
VAL CA  C    sing N N 379 
VAL CA  CB   sing N N 380 
VAL CA  HA   sing N N 381 
VAL C   O    doub N N 382 
VAL C   OXT  sing N N 383 
VAL CB  CG1  sing N N 384 
VAL CB  CG2  sing N N 385 
VAL CB  HB   sing N N 386 
VAL CG1 HG11 sing N N 387 
VAL CG1 HG12 sing N N 388 
VAL CG1 HG13 sing N N 389 
VAL CG2 HG21 sing N N 390 
VAL CG2 HG22 sing N N 391 
VAL CG2 HG23 sing N N 392 
VAL OXT HXT  sing N N 393 
WQN C2  C1   sing N N 394 
WQN O1  C1   doub N N 395 
WQN C1  N1   sing N N 396 
WQN N1  C5   sing N N 397 
WQN N1  C3   sing N N 398 
WQN C5  C4   sing N N 399 
WQN C3  C4   sing N N 400 
WQN O3  S1   doub N N 401 
WQN C4  C6   sing N N 402 
WQN C4  O4   sing N N 403 
WQN C6  N2   sing N N 404 
WQN C12 C11  doub Y N 405 
WQN C12 C7   sing Y N 406 
WQN S1  N2   sing N N 407 
WQN S1  C7   sing N N 408 
WQN S1  O2   doub N N 409 
WQN N2  C13  sing N N 410 
WQN C11 C10  sing Y N 411 
WQN O4  C14  sing N N 412 
WQN C7  C8   doub Y N 413 
WQN C14 C13  sing N N 414 
WQN C10 BR1  sing N N 415 
WQN C10 C9   doub Y N 416 
WQN C8  C9   sing Y N 417 
WQN C11 H1   sing N N 418 
WQN C12 H2   sing N N 419 
WQN C13 H3   sing N N 420 
WQN C13 H4   sing N N 421 
WQN C14 H5   sing N N 422 
WQN C14 H6   sing N N 423 
WQN C2  H7   sing N N 424 
WQN C2  H8   sing N N 425 
WQN C3  H10  sing N N 426 
WQN C3  H11  sing N N 427 
WQN C5  H12  sing N N 428 
WQN C5  H13  sing N N 429 
WQN C6  H14  sing N N 430 
WQN C6  H15  sing N N 431 
WQN C8  H16  sing N N 432 
WQN C9  H17  sing N N 433 
WQN C2  CL1  sing N N 434 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           GM147696 
_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      PDB 
_pdbx_initial_refinement_model.accession_code   3IQJ 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    8VSO 
_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]   0.012168 
_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]   0.008892 
_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]   0.015899 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
BR 
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   . GLY A 1 1   ? 44.355 14.122  -4.615  1.00 54.73  ? -4  GLY B N   1 
ATOM   2    C  CA  . GLY A 1 1   ? 44.150 12.760  -4.138  1.00 49.39  ? -4  GLY B CA  1 
ATOM   3    C  C   . GLY A 1 1   ? 43.984 11.776  -5.293  1.00 41.03  ? -4  GLY B C   1 
ATOM   4    O  O   . GLY A 1 1   ? 44.545 11.992  -6.373  1.00 32.72  ? -4  GLY B O   1 
ATOM   5    N  N   . ALA A 1 2   ? 43.188 10.722  -5.050  1.00 39.23  ? -3  ALA B N   1 
ATOM   6    C  CA  . ALA A 1 2   ? 42.944 9.666   -6.022  1.00 37.04  ? -3  ALA B CA  1 
ATOM   7    C  C   . ALA A 1 2   ? 42.246 10.157  -7.292  1.00 29.93  ? -3  ALA B C   1 
ATOM   8    O  O   . ALA A 1 2   ? 42.374 9.542   -8.349  1.00 33.97  ? -3  ALA B O   1 
ATOM   9    C  CB  . ALA A 1 2   ? 42.119 8.552   -5.391  1.00 45.03  ? -3  ALA B CB  1 
ATOM   10   N  N   . MET A 1 3   ? 41.505 11.266  -7.181  1.00 27.02  ? -2  MET B N   1 
ATOM   11   C  CA  . MET A 1 3   ? 40.786 11.833  -8.314  1.00 22.00  ? -2  MET B CA  1 
ATOM   12   C  C   . MET A 1 3   ? 41.550 12.996  -8.928  1.00 19.28  ? -2  MET B C   1 
ATOM   13   O  O   . MET A 1 3   ? 41.000 13.745  -9.738  1.00 19.69  ? -2  MET B O   1 
ATOM   14   C  CB  . MET A 1 3   ? 39.401 12.315  -7.837  1.00 20.87  ? -2  MET B CB  1 
ATOM   15   C  CG  . MET A 1 3   ? 38.594 11.226  -7.278  1.00 23.06  ? -2  MET B CG  1 
ATOM   16   S  SD  . MET A 1 3   ? 38.084 10.044  -8.508  1.00 25.38  ? -2  MET B SD  1 
ATOM   17   C  CE  . MET A 1 3   ? 37.247 8.888   -7.412  1.00 30.30  ? -2  MET B CE  1 
ATOM   18   N  N   . GLY A 1 4   ? 42.826 13.154  -8.538  1.00 18.38  ? -1  GLY B N   1 
ATOM   19   C  CA  . GLY A 1 4   ? 43.624 14.285  -8.957  1.00 17.76  ? -1  GLY B CA  1 
ATOM   20   C  C   . GLY A 1 4   ? 43.831 14.387  -10.464 1.00 18.94  ? -1  GLY B C   1 
ATOM   21   O  O   . GLY A 1 4   ? 44.018 15.490  -10.992 1.00 19.27  ? -1  GLY B O   1 
ATOM   22   N  N   . SER A 1 5   ? 43.783 13.247  -11.158 1.00 16.68  ? 0   SER B N   1 
ATOM   23   C  CA  . SER A 1 5   ? 43.976 13.271  -12.597 1.00 15.17  ? 0   SER B CA  1 
ATOM   24   C  C   . SER A 1 5   ? 42.715 13.459  -13.428 1.00 14.04  ? 0   SER B C   1 
ATOM   25   O  O   . SER A 1 5   ? 42.802 13.602  -14.645 1.00 15.66  ? 0   SER B O   1 
ATOM   26   C  CB  . SER A 1 5   ? 44.697 12.016  -13.078 1.00 18.72  ? 0   SER B CB  1 
ATOM   27   O  OG  . SER A 1 5   ? 43.870 10.878  -12.931 1.00 24.03  ? 0   SER B OG  1 
ATOM   28   N  N   . MET A 1 6   ? 41.535 13.494  -12.796 1.00 13.72  ? 1   MET B N   1 
ATOM   29   C  CA  . MET A 1 6   ? 40.294 13.646  -13.530 1.00 13.97  ? 1   MET B CA  1 
ATOM   30   C  C   . MET A 1 6   ? 39.861 15.103  -13.564 1.00 13.69  ? 1   MET B C   1 
ATOM   31   O  O   . MET A 1 6   ? 39.922 15.787  -12.547 1.00 14.50  ? 1   MET B O   1 
ATOM   32   C  CB  . MET A 1 6   ? 39.159 12.828  -12.913 1.00 16.22  ? 1   MET B CB  1 
ATOM   33   C  CG  . MET A 1 6   ? 38.115 12.489  -13.914 1.00 20.69  ? 1   MET B CG  1 
ATOM   34   S  SD  . MET A 1 6   ? 36.715 11.476  -13.336 1.00 21.93  ? 1   MET B SD  1 
ATOM   35   C  CE  . MET A 1 6   ? 37.596 10.172  -12.501 1.00 20.36  ? 1   MET B CE  1 
ATOM   36   N  N   . GLU A 1 7   ? 39.358 15.529  -14.720 1.00 13.86  ? 2   GLU B N   1 
ATOM   37   C  CA  . GLU A 1 7   ? 38.812 16.878  -14.856 1.00 15.25  ? 2   GLU B CA  1 
ATOM   38   C  C   . GLU A 1 7   ? 37.680 17.127  -13.856 1.00 14.01  ? 2   GLU B C   1 
ATOM   39   O  O   . GLU A 1 7   ? 36.816 16.272  -13.645 1.00 14.46  ? 2   GLU B O   1 
ATOM   40   C  CB  . GLU A 1 7   ? 38.226 17.098  -16.239 1.00 16.29  ? 2   GLU B CB  1 
ATOM   41   C  CG  . GLU A 1 7   ? 39.239 17.125  -17.345 1.00 18.33  ? 2   GLU B CG  1 
ATOM   42   C  CD  . GLU A 1 7   ? 39.826 18.480  -17.550 1.00 22.59  ? 2   GLU B CD  1 
ATOM   43   O  OE1 . GLU A 1 7   ? 39.721 19.317  -16.623 1.00 20.50  ? 2   GLU B OE1 1 
ATOM   44   O  OE2 . GLU A 1 7   ? 40.353 18.724  -18.670 1.00 20.88  ? 2   GLU B OE2 1 
ATOM   45   N  N   . ARG A 1 8   ? 37.616 18.370  -13.358 1.00 15.10  ? 3   ARG B N   1 
ATOM   46   C  CA  . ARG A 1 8   ? 36.516 18.775  -12.493 1.00 13.92  ? 3   ARG B CA  1 
ATOM   47   C  C   . ARG A 1 8   ? 35.155 18.466  -13.109 1.00 14.11  ? 3   ARG B C   1 
ATOM   48   O  O   . ARG A 1 8   ? 34.290 17.885  -12.441 1.00 13.88  ? 3   ARG B O   1 
ATOM   49   C  CB  . ARG A 1 8   ? 36.627 20.279  -12.165 1.00 15.63  ? 3   ARG B CB  1 
ATOM   50   C  CG  . ARG A 1 8   ? 35.671 20.742  -11.095 1.00 15.62  ? 3   ARG B CG  1 
ATOM   51   C  CD  . ARG A 1 8   ? 35.767 22.266  -10.923 1.00 17.32  ? 3   ARG B CD  1 
ATOM   52   N  NE  . ARG A 1 8   ? 34.996 22.726  -9.783  1.00 16.10  ? 3   ARG B NE  1 
ATOM   53   C  CZ  . ARG A 1 8   ? 33.689 22.904  -9.777  1.00 15.40  ? 3   ARG B CZ  1 
ATOM   54   N  NH1 . ARG A 1 8   ? 32.948 22.668  -10.844 1.00 16.15  ? 3   ARG B NH1 1 
ATOM   55   N  NH2 . ARG A 1 8   ? 33.106 23.335  -8.658  1.00 19.13  ? 3   ARG B NH2 1 
ATOM   56   N  N   . ALA A 1 9   ? 34.946 18.834  -14.387 1.00 13.69  ? 4   ALA B N   1 
ATOM   57   C  CA  . ALA A 1 9   ? 33.650 18.614  -15.009 1.00 14.39  ? 4   ALA B CA  1 
ATOM   58   C  C   . ALA A 1 9   ? 33.296 17.126  -15.135 1.00 13.28  ? 4   ALA B C   1 
ATOM   59   O  O   . ALA A 1 9   ? 32.138 16.739  -15.016 1.00 15.38  ? 4   ALA B O   1 
ATOM   60   C  CB  . ALA A 1 9   ? 33.585 19.273  -16.363 1.00 14.30  ? 4   ALA B CB  1 
ATOM   61   N  N   . SER A 1 10  ? 34.307 16.298  -15.351 1.00 13.31  ? 5   SER B N   1 
ATOM   62   C  CA  . SER A 1 10  ? 34.119 14.851  -15.444 1.00 14.40  ? 5   SER B CA  1 
ATOM   63   C  C   . SER A 1 10  ? 33.748 14.250  -14.089 1.00 13.25  ? 5   SER B C   1 
ATOM   64   O  O   . SER A 1 10  ? 32.897 13.366  -14.022 1.00 14.37  ? 5   SER B O   1 
ATOM   65   C  CB  . SER A 1 10  ? 35.393 14.207  -15.972 1.00 14.75  ? 5   SER B CB  1 
ATOM   66   O  OG  . SER A 1 10  ? 35.611 14.641  -17.304 1.00 16.65  ? 5   SER B OG  1 
ATOM   67   N  N   . LEU A 1 11  ? 34.357 14.759  -13.010 1.00 13.70  ? 6   LEU B N   1 
ATOM   68   C  CA  . LEU A 1 11  ? 34.009 14.349  -11.657 1.00 13.84  ? 6   LEU B CA  1 
ATOM   69   C  C   . LEU A 1 11  ? 32.546 14.673  -11.352 1.00 13.95  ? 6   LEU B C   1 
ATOM   70   O  O   . LEU A 1 11  ? 31.833 13.857  -10.783 1.00 14.25  ? 6   LEU B O   1 
ATOM   71   C  CB  . LEU A 1 11  ? 34.948 15.008  -10.656 1.00 14.08  ? 6   LEU B CB  1 
ATOM   72   C  CG  . LEU A 1 11  ? 36.372 14.488  -10.699 1.00 15.50  ? 6   LEU B CG  1 
ATOM   73   C  CD1 . LEU A 1 11  ? 37.291 15.386  -9.991  1.00 16.33  ? 6   LEU B CD1 1 
ATOM   74   C  CD2 . LEU A 1 11  ? 36.439 13.054  -10.065 1.00 16.00  ? 6   LEU B CD2 1 
ATOM   75   N  N   . ILE A 1 12  ? 32.080 15.837  -11.769 1.00 13.64  ? 7   ILE B N   1 
ATOM   76   C  CA  . ILE A 1 12  ? 30.671 16.229  -11.496 1.00 14.05  ? 7   ILE B CA  1 
ATOM   77   C  C   . ILE A 1 12  ? 29.738 15.360  -12.339 1.00 14.19  ? 7   ILE B C   1 
ATOM   78   O  O   . ILE A 1 12  ? 28.735 14.903  -11.824 1.00 14.66  ? 7   ILE B O   1 
ATOM   79   C  CB  . ILE A 1 12  ? 30.481 17.738  -11.742 1.00 15.75  ? 7   ILE B CB  1 
ATOM   80   C  CG1 . ILE A 1 12  ? 31.202 18.551  -10.664 1.00 18.54  ? 7   ILE B CG1 1 
ATOM   81   C  CG2 . ILE A 1 12  ? 29.009 18.096  -11.833 1.00 16.07  ? 7   ILE B CG2 1 
ATOM   82   C  CD1 . ILE A 1 12  ? 31.736 19.858  -11.154 1.00 19.37  ? 7   ILE B CD1 1 
ATOM   83   N  N   . GLN A 1 13  ? 30.085 15.182  -13.611 1.00 14.00  ? 8   GLN B N   1 
ATOM   84   C  CA  . GLN A 1 13  ? 29.293 14.309  -14.458 1.00 14.99  ? 8   GLN B CA  1 
ATOM   85   C  C   . GLN A 1 13  ? 29.178 12.906  -13.853 1.00 14.38  ? 8   GLN B C   1 
ATOM   86   O  O   . GLN A 1 13  ? 28.087 12.321  -13.812 1.00 15.93  ? 8   GLN B O   1 
ATOM   87   C  CB  . GLN A 1 13  ? 29.893 14.268  -15.856 1.00 17.77  ? 8   GLN B CB  1 
ATOM   88   C  CG  . GLN A 1 13  ? 29.088 13.479  -16.849 1.00 24.32  ? 8   GLN B CG  1 
ATOM   89   C  CD  . GLN A 1 13  ? 29.720 13.500  -18.248 1.00 28.45  ? 8   GLN B CD  1 
ATOM   90   O  OE1 . GLN A 1 13  ? 30.741 14.177  -18.487 1.00 29.06  ? 8   GLN B OE1 1 
ATOM   91   N  NE2 . GLN A 1 13  ? 29.114 12.763  -19.196 1.00 28.10  ? 8   GLN B NE2 1 
ATOM   92   N  N   . LYS A 1 14  ? 30.309 12.351  -13.403 1.00 13.62  ? 9   LYS B N   1 
ATOM   93   C  CA  . LYS A 1 14  ? 30.299 11.014  -12.821 1.00 13.21  ? 9   LYS B CA  1 
ATOM   94   C  C   . LYS A 1 14  ? 29.570 10.953  -11.481 1.00 13.22  ? 9   LYS B C   1 
ATOM   95   O  O   . LYS A 1 14  ? 28.936 9.940   -11.193 1.00 14.13  ? 9   LYS B O   1 
ATOM   96   C  CB  . LYS A 1 14  ? 31.714 10.451  -12.719 1.00 14.74  ? 9   LYS B CB  1 
ATOM   97   C  CG  . LYS A 1 14  ? 32.303 10.123  -14.085 1.00 14.87  ? 9   LYS B CG  1 
ATOM   98   C  CD  . LYS A 1 14  ? 33.687 9.554   -14.014 1.00 15.43  ? 9   LYS B CD  1 
ATOM   99   C  CE  . LYS A 1 14  ? 34.300 9.444   -15.413 1.00 15.63  ? 9   LYS B CE  1 
ATOM   100  N  NZ  . LYS A 1 14  ? 35.668 8.904   -15.381 1.00 17.91  ? 9   LYS B NZ  1 
ATOM   101  N  N   . ALA A 1 15  ? 29.622 12.020  -10.674 1.00 12.22  ? 10  ALA B N   1 
ATOM   102  C  CA  . ALA A 1 15  ? 28.810 12.070  -9.463  1.00 12.86  ? 10  ALA B CA  1 
ATOM   103  C  C   . ALA A 1 15  ? 27.327 11.960  -9.805  1.00 12.59  ? 10  ALA B C   1 
ATOM   104  O  O   . ALA A 1 15  ? 26.587 11.293  -9.089  1.00 13.45  ? 10  ALA B O   1 
ATOM   105  C  CB  . ALA A 1 15  ? 29.070 13.378  -8.673  1.00 13.32  ? 10  ALA B CB  1 
ATOM   106  N  N   . LYS A 1 16  ? 26.886 12.641  -10.870 1.00 13.41  ? 11  LYS B N   1 
ATOM   107  C  CA  . LYS A 1 16  ? 25.485 12.555  -11.269 1.00 14.43  ? 11  LYS B CA  1 
ATOM   108  C  C   . LYS A 1 16  ? 25.117 11.136  -11.703 1.00 13.78  ? 11  LYS B C   1 
ATOM   109  O  O   . LYS A 1 16  ? 24.018 10.640  -11.410 1.00 17.09  ? 11  LYS B O   1 
ATOM   110  C  CB  . LYS A 1 16  ? 25.188 13.581  -12.382 1.00 15.16  ? 11  LYS B CB  1 
ATOM   111  C  CG  . LYS A 1 16  ? 25.179 15.029  -11.897 1.00 15.71  ? 11  LYS B CG  1 
ATOM   112  C  CD  . LYS A 1 16  ? 25.141 16.023  -13.056 1.00 17.38  ? 11  LYS B CD  1 
ATOM   113  C  CE  . LYS A 1 16  ? 25.352 17.443  -12.608 1.00 22.90  ? 11  LYS B CE  1 
ATOM   114  N  NZ  . LYS A 1 16  ? 25.322 18.381  -13.765 1.00 26.25  ? 11  LYS B NZ  1 
ATOM   115  N  N   . LEU A 1 17  ? 26.010 10.490  -12.456 1.00 15.18  ? 12  LEU B N   1 
ATOM   116  C  CA  . LEU A 1 17  ? 25.820 9.094   -12.868 1.00 14.14  ? 12  LEU B CA  1 
ATOM   117  C  C   . LEU A 1 17  ? 25.748 8.137   -11.667 1.00 15.28  ? 12  LEU B C   1 
ATOM   118  O  O   . LEU A 1 17  ? 24.880 7.276   -11.591 1.00 16.61  ? 12  LEU B O   1 
ATOM   119  C  CB  . LEU A 1 17  ? 26.955 8.643   -13.812 1.00 13.97  ? 12  LEU B CB  1 
ATOM   120  C  CG  . LEU A 1 17  ? 26.989 9.319   -15.188 1.00 15.49  ? 12  LEU B CG  1 
ATOM   121  C  CD1 . LEU A 1 17  ? 28.241 8.976   -15.895 1.00 16.74  ? 12  LEU B CD1 1 
ATOM   122  C  CD2 . LEU A 1 17  ? 25.779 8.909   -16.014 1.00 18.82  ? 12  LEU B CD2 1 
ATOM   123  N  N   . ALA A 1 18  ? 26.651 8.330   -10.704 1.00 13.74  ? 13  ALA B N   1 
ATOM   124  C  CA  . ALA A 1 18  ? 26.709 7.523   -9.499  1.00 14.30  ? 13  ALA B CA  1 
ATOM   125  C  C   . ALA A 1 18  ? 25.419 7.684   -8.707  1.00 15.10  ? 13  ALA B C   1 
ATOM   126  O  O   . ALA A 1 18  ? 24.892 6.695   -8.187  1.00 16.03  ? 13  ALA B O   1 
ATOM   127  C  CB  . ALA A 1 18  ? 27.906 7.935   -8.659  1.00 15.36  ? 13  ALA B CB  1 
ATOM   128  N  N   . GLU A 1 19  ? 24.877 8.903   -8.652  1.00 15.72  ? 14  GLU B N   1 
ATOM   129  C  CA  . GLU A 1 19  ? 23.590 9.145   -8.019  1.00 15.81  ? 14  GLU B CA  1 
ATOM   130  C  C   . GLU A 1 19  ? 22.469 8.323   -8.675  1.00 17.63  ? 14  GLU B C   1 
ATOM   131  O  O   . GLU A 1 19  ? 21.692 7.653   -7.979  1.00 19.62  ? 14  GLU B O   1 
ATOM   132  C  CB  . GLU A 1 19  ? 23.257 10.638  -8.016  1.00 18.06  ? 14  GLU B CB  1 
ATOM   133  C  CG  . GLU A 1 19  ? 22.023 10.945  -7.194  1.00 20.28  ? 14  GLU B CG  1 
ATOM   134  C  CD  . GLU A 1 19  ? 21.562 12.388  -7.209  1.00 25.17  ? 14  GLU B CD  1 
ATOM   135  O  OE1 . GLU A 1 19  ? 21.904 13.129  -8.161  1.00 26.82  ? 14  GLU B OE1 1 
ATOM   136  O  OE2 . GLU A 1 19  ? 20.830 12.767  -6.266  1.00 32.83  ? 14  GLU B OE2 1 
ATOM   137  N  N   . GLN A 1 20  ? 22.411 8.348   -10.007 1.00 18.56  ? 15  GLN B N   1 
ATOM   138  C  CA  . GLN A 1 20  ? 21.403 7.575   -10.730 1.00 18.12  ? 15  GLN B CA  1 
ATOM   139  C  C   . GLN A 1 20  ? 21.524 6.073   -10.493 1.00 18.98  ? 15  GLN B C   1 
ATOM   140  O  O   . GLN A 1 20  ? 20.524 5.347   -10.450 1.00 22.26  ? 15  GLN B O   1 
ATOM   141  C  CB  . GLN A 1 20  ? 21.493 7.856   -12.220 1.00 19.06  ? 15  GLN B CB  1 
ATOM   142  C  CG  . GLN A 1 20  ? 21.107 9.294   -12.581 1.00 22.11  ? 15  GLN B CG  1 
ATOM   143  C  CD  . GLN A 1 20  ? 21.255 9.536   -14.046 1.00 34.38  ? 15  GLN B CD  1 
ATOM   144  O  OE1 . GLN A 1 20  ? 20.387 9.170   -14.843 1.00 31.84  ? 15  GLN B OE1 1 
ATOM   145  N  NE2 . GLN A 1 20  ? 22.383 10.133  -14.428 1.00 32.40  ? 15  GLN B NE2 1 
ATOM   146  N  N   . ALA A 1 21  ? 22.760 5.607   -10.322 1.00 16.73  ? 16  ALA B N   1 
ATOM   147  C  CA  . ALA A 1 21  ? 23.057 4.199   -10.108 1.00 16.80  ? 16  ALA B CA  1 
ATOM   148  C  C   . ALA A 1 21  ? 23.012 3.806   -8.632  1.00 18.38  ? 16  ALA B C   1 
ATOM   149  O  O   . ALA A 1 21  ? 23.280 2.657   -8.309  1.00 18.58  ? 16  ALA B O   1 
ATOM   150  C  CB  . ALA A 1 21  ? 24.415 3.884   -10.693 1.00 19.46  ? 16  ALA B CB  1 
ATOM   151  N  N   . GLU A 1 22  ? 22.662 4.757   -7.759  1.00 18.77  ? 17  GLU B N   1 
ATOM   152  C  CA  . GLU A 1 22  ? 22.673 4.544   -6.312  1.00 18.30  ? 17  GLU B CA  1 
ATOM   153  C  C   . GLU A 1 22  ? 24.004 4.033   -5.759  1.00 19.92  ? 17  GLU B C   1 
ATOM   154  O  O   . GLU A 1 22  ? 24.060 3.244   -4.814  1.00 20.23  ? 17  GLU B O   1 
ATOM   155  C  CB  . GLU A 1 22  ? 21.464 3.637   -5.917  1.00 20.44  ? 17  GLU B CB  1 
ATOM   156  C  CG  . GLU A 1 22  ? 20.142 4.336   -6.168  1.00 28.45  ? 17  GLU B CG  1 
ATOM   157  C  CD  . GLU A 1 22  ? 18.878 3.523   -5.938  1.00 35.92  ? 17  GLU B CD  1 
ATOM   158  O  OE1 . GLU A 1 22  ? 18.683 3.011   -4.819  1.00 39.74  ? 17  GLU B OE1 1 
ATOM   159  O  OE2 . GLU A 1 22  ? 18.067 3.424   -6.882  1.00 45.91  ? 17  GLU B OE2 1 
ATOM   160  N  N   . ARG A 1 23  ? 25.099 4.563   -6.317  1.00 16.01  ? 18  ARG B N   1 
ATOM   161  C  CA  . ARG A 1 23  ? 26.461 4.250   -5.921  1.00 15.63  ? 18  ARG B CA  1 
ATOM   162  C  C   . ARG A 1 23  ? 27.016 5.420   -5.108  1.00 16.88  ? 18  ARG B C   1 
ATOM   163  O  O   . ARG A 1 23  ? 27.815 6.229   -5.598  1.00 14.87  ? 18  ARG B O   1 
ATOM   164  C  CB  . ARG A 1 23  ? 27.322 3.986   -7.144  1.00 16.98  ? 18  ARG B CB  1 
ATOM   165  C  CG  . ARG A 1 23  ? 26.936 2.716   -7.879  1.00 17.63  ? 18  ARG B CG  1 
ATOM   166  C  CD  . ARG A 1 23  ? 27.645 1.519   -7.315  1.00 18.79  ? 18  ARG B CD  1 
ATOM   167  N  NE  . ARG A 1 23  ? 29.065 1.612   -7.639  1.00 19.05  ? 18  ARG B NE  1 
ATOM   168  C  CZ  . ARG A 1 23  ? 29.932 0.619   -7.525  1.00 23.13  ? 18  ARG B CZ  1 
ATOM   169  N  NH1 . ARG A 1 23  ? 29.538 -0.611  -7.242  1.00 22.65  ? 18  ARG B NH1 1 
ATOM   170  N  NH2 . ARG A 1 23  ? 31.217 0.852   -7.738  1.00 20.80  ? 18  ARG B NH2 1 
ATOM   171  N  N   . TYR A 1 24  ? 26.571 5.528   -3.852  1.00 15.32  ? 19  TYR B N   1 
ATOM   172  C  CA  . TYR A 1 24  ? 26.814 6.754   -3.108  1.00 14.90  ? 19  TYR B CA  1 
ATOM   173  C  C   . TYR A 1 24  ? 28.245 6.896   -2.586  1.00 14.39  ? 19  TYR B C   1 
ATOM   174  O  O   . TYR A 1 24  ? 28.744 8.007   -2.460  1.00 14.13  ? 19  TYR B O   1 
ATOM   175  C  CB  . TYR A 1 24  ? 25.792 6.893   -1.987  1.00 16.62  ? 19  TYR B CB  1 
ATOM   176  C  CG  . TYR A 1 24  ? 24.380 6.996   -2.529  1.00 18.31  ? 19  TYR B CG  1 
ATOM   177  C  CD1 . TYR A 1 24  ? 23.948 8.141   -3.195  1.00 20.89  ? 19  TYR B CD1 1 
ATOM   178  C  CD2 . TYR A 1 24  ? 23.483 5.934   -2.399  1.00 19.88  ? 19  TYR B CD2 1 
ATOM   179  C  CE1 . TYR A 1 24  ? 22.662 8.225   -3.715  1.00 22.09  ? 19  TYR B CE1 1 
ATOM   180  C  CE2 . TYR A 1 24  ? 22.191 6.018   -2.915  1.00 21.61  ? 19  TYR B CE2 1 
ATOM   181  C  CZ  . TYR A 1 24  ? 21.793 7.156   -3.569  1.00 22.44  ? 19  TYR B CZ  1 
ATOM   182  O  OH  . TYR A 1 24  ? 20.518 7.255   -4.053  1.00 28.85  ? 19  TYR B OH  1 
ATOM   183  N  N   . GLU A 1 25  ? 28.934 5.785   -2.317  1.00 15.60  ? 20  GLU B N   1 
ATOM   184  C  CA  . GLU A 1 25  ? 30.344 5.848   -1.983  1.00 14.56  ? 20  GLU B CA  1 
ATOM   185  C  C   . GLU A 1 25  ? 31.126 6.432   -3.161  1.00 15.23  ? 20  GLU B C   1 
ATOM   186  O  O   . GLU A 1 25  ? 31.976 7.298   -2.968  1.00 14.39  ? 20  GLU B O   1 
ATOM   187  C  CB  . GLU A 1 25  ? 30.928 4.473   -1.565  1.00 17.22  ? 20  GLU B CB  1 
ATOM   188  C  CG  . GLU A 1 25  ? 30.346 3.913   -0.296  1.00 27.17  ? 20  GLU B CG  1 
ATOM   189  C  CD  . GLU A 1 25  ? 31.154 2.730   0.227   1.00 36.65  ? 20  GLU B CD  1 
ATOM   190  O  OE1 . GLU A 1 25  ? 32.255 2.465   -0.321  1.00 44.65  ? 20  GLU B OE1 1 
ATOM   191  O  OE2 . GLU A 1 25  ? 30.689 2.079   1.193   1.00 59.48  ? 20  GLU B OE2 1 
ATOM   192  N  N   . ASP A 1 26  ? 30.875 5.937   -4.380  1.00 14.23  ? 21  ASP B N   1 
ATOM   193  C  CA  . ASP A 1 26  ? 31.506 6.512   -5.558  1.00 13.43  ? 21  ASP B CA  1 
ATOM   194  C  C   . ASP A 1 26  ? 31.173 7.996   -5.706  1.00 13.97  ? 21  ASP B C   1 
ATOM   195  O  O   . ASP A 1 26  ? 32.040 8.818   -6.001  1.00 14.05  ? 21  ASP B O   1 
ATOM   196  C  CB  . ASP A 1 26  ? 31.085 5.810   -6.844  1.00 15.29  ? 21  ASP B CB  1 
ATOM   197  C  CG  . ASP A 1 26  ? 31.604 4.400   -7.042  1.00 16.95  ? 21  ASP B CG  1 
ATOM   198  O  OD1 . ASP A 1 26  ? 32.511 3.986   -6.285  1.00 19.06  ? 21  ASP B OD1 1 
ATOM   199  O  OD2 . ASP A 1 26  ? 31.062 3.699   -7.946  1.00 19.94  ? 21  ASP B OD2 1 
ATOM   200  N  N   . MET A 1 27  ? 29.901 8.324   -5.516  1.00 13.00  ? 22  MET B N   1 
ATOM   201  C  CA  . MET A 1 27  ? 29.446 9.697   -5.654  1.00 12.51  ? 22  MET B CA  1 
ATOM   202  C  C   . MET A 1 27  ? 30.218 10.616  -4.706  1.00 13.48  ? 22  MET B C   1 
ATOM   203  O  O   . MET A 1 27  ? 30.634 11.712  -5.100  1.00 12.49  ? 22  MET B O   1 
ATOM   204  C  CB  . MET A 1 27  ? 27.919 9.759   -5.369  1.00 13.10  ? 22  MET B CB  1 
ATOM   205  C  CG  . MET A 1 27  ? 27.311 11.074  -5.705  1.00 13.37  ? 22  MET B CG  1 
ATOM   206  S  SD  . MET A 1 27  ? 25.601 11.131  -5.178  1.00 14.97  ? 22  MET B SD  1 
ATOM   207  C  CE  . MET A 1 27  ? 25.137 12.790  -5.720  1.00 15.42  ? 22  MET B CE  1 
ATOM   208  N  N   . ALA A 1 28  ? 30.406 10.171  -3.457  1.00 12.52  ? 23  ALA B N   1 
ATOM   209  C  CA  . ALA A 1 28  ? 31.115 10.961  -2.469  1.00 13.26  ? 23  ALA B CA  1 
ATOM   210  C  C   . ALA A 1 28  ? 32.578 11.130  -2.865  1.00 13.45  ? 23  ALA B C   1 
ATOM   211  O  O   . ALA A 1 28  ? 33.132 12.226  -2.742  1.00 13.85  ? 23  ALA B O   1 
ATOM   212  C  CB  . ALA A 1 28  ? 30.989 10.310  -1.107  1.00 14.22  ? 23  ALA B CB  1 
ATOM   213  N  N   . ALA A 1 29  ? 33.203 10.058  -3.363  1.00 13.37  ? 24  ALA B N   1 
ATOM   214  C  CA  . ALA A 1 29  ? 34.593 10.167  -3.793  1.00 13.60  ? 24  ALA B CA  1 
ATOM   215  C  C   . ALA A 1 29  ? 34.746 11.146  -4.962  1.00 13.08  ? 24  ALA B C   1 
ATOM   216  O  O   . ALA A 1 29  ? 35.710 11.917  -5.011  1.00 13.60  ? 24  ALA B O   1 
ATOM   217  C  CB  . ALA A 1 29  ? 35.133 8.810   -4.161  1.00 15.00  ? 24  ALA B CB  1 
ATOM   218  N  N   . PHE A 1 30  ? 33.820 11.094  -5.931  1.00 12.24  ? 25  PHE B N   1 
ATOM   219  C  CA  . PHE A 1 30  ? 33.853 12.024  -7.048  1.00 12.87  ? 25  PHE B CA  1 
ATOM   220  C  C   . PHE A 1 30  ? 33.698 13.465  -6.553  1.00 14.25  ? 25  PHE B C   1 
ATOM   221  O  O   . PHE A 1 30  ? 34.413 14.362  -7.010  1.00 13.68  ? 25  PHE B O   1 
ATOM   222  C  CB  . PHE A 1 30  ? 32.779 11.672  -8.074  1.00 13.63  ? 25  PHE B CB  1 
ATOM   223  C  CG  . PHE A 1 30  ? 32.969 10.370  -8.830  1.00 13.03  ? 25  PHE B CG  1 
ATOM   224  C  CD1 . PHE A 1 30  ? 34.198 10.028  -9.369  1.00 16.10  ? 25  PHE B CD1 1 
ATOM   225  C  CD2 . PHE A 1 30  ? 31.901 9.529   -9.070  1.00 13.82  ? 25  PHE B CD2 1 
ATOM   226  C  CE1 . PHE A 1 30  ? 34.368 8.831   -10.079 1.00 15.35  ? 25  PHE B CE1 1 
ATOM   227  C  CE2 . PHE A 1 30  ? 32.066 8.341   -9.809  1.00 14.85  ? 25  PHE B CE2 1 
ATOM   228  C  CZ  . PHE A 1 30  ? 33.307 8.009   -10.312 1.00 17.29  ? 25  PHE B CZ  1 
ATOM   229  N  N   . MET A 1 31  ? 32.744 13.699  -5.635  1.00 12.78  ? 26  MET B N   1 
ATOM   230  C  CA  . MET A 1 31  ? 32.553 15.054  -5.137  1.00 12.28  ? 26  MET B CA  1 
ATOM   231  C  C   . MET A 1 31  ? 33.692 15.562  -4.251  1.00 13.38  ? 26  MET B C   1 
ATOM   232  O  O   . MET A 1 31  ? 34.007 16.752  -4.316  1.00 13.74  ? 26  MET B O   1 
ATOM   233  C  CB  . MET A 1 31  ? 31.217 15.185  -4.428  1.00 13.86  ? 26  MET B CB  1 
ATOM   234  C  CG  . MET A 1 31  ? 30.007 15.111  -5.362  1.00 14.58  ? 26  MET B CG  1 
ATOM   235  S  SD  . MET A 1 31  ? 30.129 16.184  -6.815  1.00 15.36  ? 26  MET B SD  1 
ATOM   236  C  CE  . MET A 1 31  ? 30.290 17.796  -6.043  1.00 15.13  ? 26  MET B CE  1 
ATOM   237  N  N   . LYS A 1 32  ? 34.301 14.684  -3.443  1.00 12.56  ? 27  LYS B N   1 
ATOM   238  C  CA  . LYS A 1 32  ? 35.513 15.046  -2.729  1.00 13.48  ? 27  LYS B CA  1 
ATOM   239  C  C   . LYS A 1 32  ? 36.588 15.471  -3.725  1.00 14.12  ? 27  LYS B C   1 
ATOM   240  O  O   . LYS A 1 32  ? 37.244 16.499  -3.529  1.00 13.81  ? 27  LYS B O   1 
ATOM   241  C  CB  . LYS A 1 32  ? 35.968 13.893  -1.858  1.00 14.94  ? 27  LYS B CB  1 
ATOM   242  C  CG  . LYS A 1 32  ? 37.319 14.109  -1.129  1.00 15.96  ? 27  LYS B CG  1 
ATOM   243  C  CD  . LYS A 1 32  ? 37.619 13.008  -0.142  1.00 19.43  ? 27  LYS B CD  1 
ATOM   244  C  CE  . LYS A 1 32  ? 38.790 13.267  0.770   1.00 24.96  ? 27  LYS B CE  1 
ATOM   245  N  NZ  . LYS A 1 32  ? 40.063 13.170  0.056   1.00 27.25  ? 27  LYS B NZ  1 
ATOM   246  N  N   . GLY A 1 33  ? 36.738 14.704  -4.817  1.00 14.14  ? 28  GLY B N   1 
ATOM   247  C  CA  . GLY A 1 33  ? 37.697 15.075  -5.847  1.00 13.18  ? 28  GLY B CA  1 
ATOM   248  C  C   . GLY A 1 33  ? 37.414 16.458  -6.423  1.00 14.69  ? 28  GLY B C   1 
ATOM   249  O  O   . GLY A 1 33  ? 38.311 17.254  -6.662  1.00 13.56  ? 28  GLY B O   1 
ATOM   250  N  N   . ALA A 1 34  ? 36.136 16.730  -6.703  1.00 11.96  ? 29  ALA B N   1 
ATOM   251  C  CA  . ALA A 1 34  ? 35.741 18.022  -7.238  1.00 12.98  ? 29  ALA B CA  1 
ATOM   252  C  C   . ALA A 1 34  ? 36.054 19.153  -6.262  1.00 13.14  ? 29  ALA B C   1 
ATOM   253  O  O   . ALA A 1 34  ? 36.567 20.203  -6.649  1.00 13.94  ? 29  ALA B O   1 
ATOM   254  C  CB  . ALA A 1 34  ? 34.253 18.031  -7.599  1.00 14.55  ? 29  ALA B CB  1 
ATOM   255  N  N   . VAL A 1 35  ? 35.744 18.966  -4.977  1.00 13.49  ? 30  VAL B N   1 
ATOM   256  C  CA  . VAL A 1 35  ? 36.070 19.993  -3.991  1.00 12.42  ? 30  VAL B CA  1 
ATOM   257  C  C   . VAL A 1 35  ? 37.575 20.252  -3.967  1.00 14.26  ? 30  VAL B C   1 
ATOM   258  O  O   . VAL A 1 35  ? 38.022 21.401  -3.897  1.00 16.10  ? 30  VAL B O   1 
ATOM   259  C  CB  . VAL A 1 35  ? 35.578 19.579  -2.590  1.00 13.18  ? 30  VAL B CB  1 
ATOM   260  C  CG1 . VAL A 1 35  ? 36.137 20.519  -1.495  1.00 14.76  ? 30  VAL B CG1 1 
ATOM   261  C  CG2 . VAL A 1 35  ? 34.049 19.554  -2.539  1.00 14.32  ? 30  VAL B CG2 1 
ATOM   262  N  N   . GLU A 1 36  ? 38.352 19.170  -4.019  1.00 13.37  ? 31  GLU B N   1 
ATOM   263  C  CA  . GLU A 1 36  ? 39.804 19.302  -3.942  1.00 14.63  ? 31  GLU B CA  1 
ATOM   264  C  C   . GLU A 1 36  ? 40.423 20.015  -5.144  1.00 15.16  ? 31  GLU B C   1 
ATOM   265  O  O   . GLU A 1 36  ? 41.597 20.398  -5.082  1.00 15.28  ? 31  GLU B O   1 
ATOM   266  C  CB  . GLU A 1 36  ? 40.443 17.949  -3.695  1.00 16.46  ? 31  GLU B CB  1 
ATOM   267  C  CG  . GLU A 1 36  ? 40.192 17.455  -2.294  1.00 17.69  ? 31  GLU B CG  1 
ATOM   268  C  CD  . GLU A 1 36  ? 40.629 16.036  -2.010  1.00 21.60  ? 31  GLU B CD  1 
ATOM   269  O  OE1 . GLU A 1 36  ? 40.903 15.262  -2.952  1.00 28.80  ? 31  GLU B OE1 1 
ATOM   270  O  OE2 . GLU A 1 36  ? 40.600 15.687  -0.813  1.00 26.78  ? 31  GLU B OE2 1 
ATOM   271  N  N   . LYS A 1 37  ? 39.659 20.262  -6.206  1.00 15.06  ? 32  LYS B N   1 
ATOM   272  C  CA  . LYS A 1 37  ? 40.149 21.115  -7.278  1.00 15.34  ? 32  LYS B CA  1 
ATOM   273  C  C   . LYS A 1 37  ? 40.378 22.558  -6.836  1.00 15.77  ? 32  LYS B C   1 
ATOM   274  O  O   . LYS A 1 37  ? 41.062 23.312  -7.518  1.00 16.53  ? 32  LYS B O   1 
ATOM   275  C  CB  . LYS A 1 37  ? 39.238 21.102  -8.483  1.00 14.78  ? 32  LYS B CB  1 
ATOM   276  C  CG  . LYS A 1 37  ? 39.047 19.717  -9.099  1.00 15.40  ? 32  LYS B CG  1 
ATOM   277  C  CD  . LYS A 1 37  ? 40.308 19.105  -9.642  1.00 14.70  ? 32  LYS B CD  1 
ATOM   278  C  CE  . LYS A 1 37  ? 40.044 17.727  -10.179 1.00 16.06  ? 32  LYS B CE  1 
ATOM   279  N  NZ  . LYS A 1 37  ? 41.328 17.048  -10.535 1.00 19.23  ? 32  LYS B NZ  1 
ATOM   280  N  N   . GLY A 1 38  ? 39.735 22.965  -5.731  1.00 15.19  ? 33  GLY B N   1 
ATOM   281  C  CA  . GLY A 1 38  ? 40.012 24.257  -5.118  1.00 14.76  ? 33  GLY B CA  1 
ATOM   282  C  C   . GLY A 1 38  ? 39.066 25.375  -5.543  1.00 17.14  ? 33  GLY B C   1 
ATOM   283  O  O   . GLY A 1 38  ? 39.127 26.487  -5.003  1.00 19.86  ? 33  GLY B O   1 
ATOM   284  N  N   . GLU A 1 39  ? 38.182 25.114  -6.508  1.00 16.22  ? 34  GLU B N   1 
ATOM   285  C  CA  . GLU A 1 39  ? 37.202 26.094  -6.926  1.00 17.53  ? 34  GLU B CA  1 
ATOM   286  C  C   . GLU A 1 39  ? 35.962 26.007  -6.038  1.00 18.37  ? 34  GLU B C   1 
ATOM   287  O  O   . GLU A 1 39  ? 35.647 24.973  -5.459  1.00 17.51  ? 34  GLU B O   1 
ATOM   288  C  CB  . GLU A 1 39  ? 36.832 25.897  -8.398  1.00 20.10  ? 34  GLU B CB  1 
ATOM   289  C  CG  . GLU A 1 39  ? 38.020 25.952  -9.353  1.00 23.11  ? 34  GLU B CG  1 
ATOM   290  C  CD  . GLU A 1 39  ? 38.518 27.341  -9.721  1.00 35.82  ? 34  GLU B CD  1 
ATOM   291  O  OE1 . GLU A 1 39  ? 37.995 28.347  -9.187  1.00 33.24  ? 34  GLU B OE1 1 
ATOM   292  O  OE2 . GLU A 1 39  ? 39.412 27.421  -10.593 1.00 48.34  ? 34  GLU B OE2 1 
ATOM   293  N  N   . GLU A 1 40  ? 35.265 27.130  -5.900  1.00 17.22  ? 35  GLU B N   1 
ATOM   294  C  CA  . GLU A 1 40  ? 34.005 27.145  -5.178  1.00 17.50  ? 35  GLU B CA  1 
ATOM   295  C  C   . GLU A 1 40  ? 32.971 26.280  -5.905  1.00 17.78  ? 35  GLU B C   1 
ATOM   296  O  O   . GLU A 1 40  ? 33.113 25.940  -7.082  1.00 18.41  ? 35  GLU B O   1 
ATOM   297  C  CB  . GLU A 1 40  ? 33.513 28.599  -4.976  1.00 17.00  ? 35  GLU B CB  1 
ATOM   298  C  CG  . GLU A 1 40  ? 34.492 29.427  -4.137  1.00 18.71  ? 35  GLU B CG  1 
ATOM   299  C  CD  . GLU A 1 40  ? 34.117 30.858  -3.790  1.00 23.52  ? 35  GLU B CD  1 
ATOM   300  O  OE1 . GLU A 1 40  ? 32.915 31.135  -3.623  1.00 26.06  ? 35  GLU B OE1 1 
ATOM   301  O  OE2 . GLU A 1 40  ? 35.031 31.682  -3.607  1.00 23.70  ? 35  GLU B OE2 1 
ATOM   302  N  N   . LEU A 1 41  ? 31.958 25.842  -5.156  1.00 15.94  ? 36  LEU B N   1 
ATOM   303  C  CA  . LEU A 1 41  ? 30.929 24.975  -5.697  1.00 15.21  ? 36  LEU B CA  1 
ATOM   304  C  C   . LEU A 1 41  ? 29.670 25.789  -5.950  1.00 16.05  ? 36  LEU B C   1 
ATOM   305  O  O   . LEU A 1 41  ? 29.281 26.634  -5.133  1.00 16.90  ? 36  LEU B O   1 
ATOM   306  C  CB  . LEU A 1 41  ? 30.524 23.851  -4.734  1.00 16.85  ? 36  LEU B CB  1 
ATOM   307  C  CG  . LEU A 1 41  ? 31.598 22.936  -4.179  1.00 24.40  ? 36  LEU B CG  1 
ATOM   308  C  CD1 . LEU A 1 41  ? 30.985 21.687  -3.544  1.00 20.18  ? 36  LEU B CD1 1 
ATOM   309  C  CD2 . LEU A 1 41  ? 32.587 22.567  -5.159  1.00 22.37  ? 36  LEU B CD2 1 
ATOM   310  N  N   . SER A 1 42  ? 29.016 25.490  -7.054  1.00 14.53  ? 37  SER B N   1 
ATOM   311  C  CA  . SER A 1 42  ? 27.695 26.028  -7.307  1.00 15.48  ? 37  SER B CA  1 
ATOM   312  C  C   . SER A 1 42  ? 26.656 25.456  -6.414  1.00 15.07  ? 37  SER B C   1 
ATOM   313  O  O   . SER A 1 42  ? 26.809 24.432  -5.741  1.00 13.21  ? 37  SER B O   1 
ATOM   314  C  CB  . SER A 1 42  ? 27.318 25.758  -8.749  1.00 15.82  ? 37  SER B CB  1 
ATOM   315  O  OG  . SER A 1 42  ? 27.053 24.369  -8.910  1.00 17.07  ? 37  SER B OG  1 
ATOM   316  N  N   . CYS A 1 43  ? 25.338 25.950  -6.454  1.00 15.36  ? 38  CYS B N   1 
ATOM   317  C  CA  . CYS A 1 43  ? 24.224 25.365  -5.669  1.00 14.87  ? 38  CYS B CA  1 
ATOM   318  C  C   . CYS A 1 43  ? 24.047 23.889  -6.035  1.00 14.87  ? 38  CYS B C   1 
ATOM   319  O  O   . CYS A 1 43  ? 23.895 23.010  -5.125  1.00 14.78  ? 38  CYS B O   1 
ATOM   320  C  CB  . CYS A 1 43  ? 22.954 26.177  -5.904  1.00 17.15  ? 38  CYS B CB  1 
ATOM   321  S  SG  . CYS A 1 43  ? 21.446 25.433  -5.224  1.00 22.05  ? 38  CYS B SG  1 
ATOM   322  N  N   . GLU A 1 44  ? 23.955 23.555  -7.381  1.00 14.67  ? 39  GLU B N   1 
ATOM   323  C  CA  . GLU A 1 44  ? 23.785 22.177  -7.785  1.00 15.21  ? 39  GLU B CA  1 
ATOM   324  C  C   . GLU A 1 44  ? 24.915 21.282  -7.266  1.00 13.98  ? 39  GLU B C   1 
ATOM   325  O  O   . GLU A 1 44  ? 24.661 20.151  -6.862  1.00 13.59  ? 39  GLU B O   1 
ATOM   326  C  CB  . GLU A 1 44  ? 23.687 22.141  -9.302  1.00 17.83  ? 39  GLU B CB  1 
ATOM   327  C  CG  . GLU A 1 44  ? 23.469 20.770  -9.864  1.00 20.92  ? 39  GLU B CG  1 
ATOM   328  C  CD  . GLU A 1 44  ? 23.322 20.752  -11.370 1.00 31.00  ? 39  GLU B CD  1 
ATOM   329  O  OE1 . GLU A 1 44  ? 23.598 21.791  -12.014 1.00 33.84  ? 39  GLU B OE1 1 
ATOM   330  O  OE2 . GLU A 1 44  ? 22.896 19.700  -11.893 1.00 34.78  ? 39  GLU B OE2 1 
ATOM   331  N  N   . GLU A 1 45  ? 26.155 21.777  -7.313  1.00 13.31  ? 40  GLU B N   1 
ATOM   332  C  CA  . GLU A 1 45  ? 27.303 20.980  -6.887  1.00 13.02  ? 40  GLU B CA  1 
ATOM   333  C  C   . GLU A 1 45  ? 27.294 20.761  -5.370  1.00 13.72  ? 40  GLU B C   1 
ATOM   334  O  O   . GLU A 1 45  ? 27.618 19.661  -4.900  1.00 14.23  ? 40  GLU B O   1 
ATOM   335  C  CB  . GLU A 1 45  ? 28.588 21.648  -7.330  1.00 13.83  ? 40  GLU B CB  1 
ATOM   336  C  CG  . GLU A 1 45  ? 28.733 21.688  -8.877  1.00 14.65  ? 40  GLU B CG  1 
ATOM   337  C  CD  . GLU A 1 45  ? 29.764 22.673  -9.422  1.00 15.21  ? 40  GLU B CD  1 
ATOM   338  O  OE1 . GLU A 1 45  ? 30.294 23.475  -8.642  1.00 15.56  ? 40  GLU B OE1 1 
ATOM   339  O  OE2 . GLU A 1 45  ? 30.019 22.668  -10.658 1.00 17.95  ? 40  GLU B OE2 1 
ATOM   340  N  N   . ARG A 1 46  ? 26.901 21.791  -4.605  1.00 13.45  ? 41  ARG B N   1 
ATOM   341  C  CA  . ARG A 1 46  ? 26.713 21.628  -3.166  1.00 13.72  ? 41  ARG B CA  1 
ATOM   342  C  C   . ARG A 1 46  ? 25.650 20.579  -2.884  1.00 13.71  ? 41  ARG B C   1 
ATOM   343  O  O   . ARG A 1 46  ? 25.798 19.771  -1.976  1.00 13.57  ? 41  ARG B O   1 
ATOM   344  C  CB  . ARG A 1 46  ? 26.321 22.953  -2.475  1.00 14.40  ? 41  ARG B CB  1 
ATOM   345  C  CG  . ARG A 1 46  ? 27.394 23.971  -2.501  1.00 15.39  ? 41  ARG B CG  1 
ATOM   346  C  CD  . ARG A 1 46  ? 27.102 25.240  -1.657  1.00 16.60  ? 41  ARG B CD  1 
ATOM   347  N  NE  . ARG A 1 46  ? 25.924 25.967  -2.115  1.00 15.29  ? 41  ARG B NE  1 
ATOM   348  C  CZ  . ARG A 1 46  ? 25.946 27.066  -2.867  1.00 18.40  ? 41  ARG B CZ  1 
ATOM   349  N  NH1 . ARG A 1 46  ? 27.042 27.478  -3.478  1.00 18.92  ? 41  ARG B NH1 1 
ATOM   350  N  NH2 . ARG A 1 46  ? 24.816 27.737  -3.058  1.00 18.92  ? 41  ARG B NH2 1 
ATOM   351  N  N   . ASN A 1 47  ? 24.563 20.571  -3.660  1.00 14.31  ? 42  ASN B N   1 
ATOM   352  C  CA  . ASN A 1 47  ? 23.569 19.518  -3.524  1.00 15.83  ? 42  ASN B CA  1 
ATOM   353  C  C   . ASN A 1 47  ? 24.168 18.129  -3.761  1.00 15.85  ? 42  ASN B C   1 
ATOM   354  O  O   . ASN A 1 47  ? 23.874 17.200  -3.016  1.00 14.82  ? 42  ASN B O   1 
ATOM   355  C  CB  . ASN A 1 47  ? 22.364 19.756  -4.444  1.00 15.90  ? 42  ASN B CB  1 
ATOM   356  C  CG  . ASN A 1 47  ? 21.383 18.610  -4.428  1.00 23.49  ? 42  ASN B CG  1 
ATOM   357  O  OD1 . ASN A 1 47  ? 21.346 17.723  -5.341  1.00 26.16  ? 42  ASN B OD1 1 
ATOM   358  N  ND2 . ASN A 1 47  ? 20.641 18.523  -3.396  1.00 23.93  ? 42  ASN B ND2 1 
ATOM   359  N  N   . LEU A 1 48  ? 25.005 17.966  -4.792  1.00 13.65  ? 43  LEU B N   1 
ATOM   360  C  CA  . LEU A 1 48  ? 25.582 16.658  -5.047  1.00 14.61  ? 43  LEU B CA  1 
ATOM   361  C  C   . LEU A 1 48  ? 26.472 16.221  -3.881  1.00 13.48  ? 43  LEU B C   1 
ATOM   362  O  O   . LEU A 1 48  ? 26.478 15.055  -3.489  1.00 13.96  ? 43  LEU B O   1 
ATOM   363  C  CB  . LEU A 1 48  ? 26.375 16.652  -6.330  1.00 13.67  ? 43  LEU B CB  1 
ATOM   364  C  CG  . LEU A 1 48  ? 25.588 16.865  -7.607  1.00 13.68  ? 43  LEU B CG  1 
ATOM   365  C  CD1 . LEU A 1 48  ? 26.557 17.182  -8.770  1.00 15.68  ? 43  LEU B CD1 1 
ATOM   366  C  CD2 . LEU A 1 48  ? 24.703 15.695  -7.934  1.00 16.06  ? 43  LEU B CD2 1 
ATOM   367  N  N   . LEU A 1 49  ? 27.269 17.147  -3.361  1.00 13.79  ? 44  LEU B N   1 
ATOM   368  C  CA  . LEU A 1 49  ? 28.141 16.862  -2.232  1.00 13.68  ? 44  LEU B CA  1 
ATOM   369  C  C   . LEU A 1 49  ? 27.335 16.403  -1.017  1.00 14.16  ? 44  LEU B C   1 
ATOM   370  O  O   . LEU A 1 49  ? 27.664 15.422  -0.352  1.00 13.01  ? 44  LEU B O   1 
ATOM   371  C  CB  . LEU A 1 49  ? 28.931 18.108  -1.884  1.00 13.94  ? 44  LEU B CB  1 
ATOM   372  C  CG  . LEU A 1 49  ? 29.909 17.989  -0.694  1.00 14.33  ? 44  LEU B CG  1 
ATOM   373  C  CD1 . LEU A 1 49  ? 31.094 17.093  -1.050  1.00 14.27  ? 44  LEU B CD1 1 
ATOM   374  C  CD2 . LEU A 1 49  ? 30.358 19.370  -0.211  1.00 17.46  ? 44  LEU B CD2 1 
ATOM   375  N  N   . SER A 1 50  ? 26.249 17.129  -0.741  1.00 12.52  ? 45  SER B N   1 
ATOM   376  C  CA  . SER A 1 50  ? 25.374 16.845  0.379   1.00 12.90  ? 45  SER B CA  1 
ATOM   377  C  C   . SER A 1 50  ? 24.699 15.479  0.268   1.00 13.29  ? 45  SER B C   1 
ATOM   378  O  O   . SER A 1 50  ? 24.724 14.677  1.200   1.00 14.12  ? 45  SER B O   1 
ATOM   379  C  CB  . SER A 1 50  ? 24.308 17.931  0.471   1.00 15.43  ? 45  SER B CB  1 
ATOM   380  O  OG  . SER A 1 50  ? 23.390 17.684  1.520   1.00 16.65  ? 45  SER B OG  1 
ATOM   381  N  N   . VAL A 1 51  ? 24.135 15.178  -0.910  1.00 13.40  ? 46  VAL B N   1 
ATOM   382  C  CA  . VAL A 1 51  ? 23.428 13.917  -1.116  1.00 13.70  ? 46  VAL B CA  1 
ATOM   383  C  C   . VAL A 1 51  ? 24.385 12.735  -0.971  1.00 14.21  ? 46  VAL B C   1 
ATOM   384  O  O   . VAL A 1 51  ? 24.059 11.734  -0.338  1.00 14.37  ? 46  VAL B O   1 
ATOM   385  C  CB  . VAL A 1 51  ? 22.762 13.905  -2.502  1.00 17.21  ? 46  VAL B CB  1 
ATOM   386  C  CG1 . VAL A 1 51  ? 22.312 12.485  -2.917  1.00 17.86  ? 46  VAL B CG1 1 
ATOM   387  C  CG2 . VAL A 1 51  ? 21.583 14.888  -2.545  1.00 17.55  ? 46  VAL B CG2 1 
ATOM   388  N  N   . ALA A 1 52  ? 25.581 12.871  -1.539  1.00 13.12  ? 47  ALA B N   1 
ATOM   389  C  CA  . ALA A 1 52  ? 26.525 11.768  -1.509  1.00 14.11  ? 47  ALA B CA  1 
ATOM   390  C  C   . ALA A 1 52  ? 26.890 11.414  -0.069  1.00 13.93  ? 47  ALA B C   1 
ATOM   391  O  O   . ALA A 1 52  ? 26.782 10.249  0.339   1.00 13.47  ? 47  ALA B O   1 
ATOM   392  C  CB  . ALA A 1 52  ? 27.737 12.149  -2.308  1.00 13.23  ? 47  ALA B CB  1 
ATOM   393  N  N   . TYR A 1 53  ? 27.359 12.409  0.692   1.00 12.73  ? 48  TYR B N   1 
ATOM   394  C  CA  . TYR A 1 53  ? 27.805 12.117  2.046   1.00 12.32  ? 48  TYR B CA  1 
ATOM   395  C  C   . TYR A 1 53  ? 26.656 11.767  2.991   1.00 13.55  ? 48  TYR B C   1 
ATOM   396  O  O   . TYR A 1 53  ? 26.823 10.910  3.858   1.00 13.44  ? 48  TYR B O   1 
ATOM   397  C  CB  . TYR A 1 53  ? 28.711 13.244  2.562   1.00 13.02  ? 48  TYR B CB  1 
ATOM   398  C  CG  . TYR A 1 53  ? 30.113 13.084  2.045   1.00 12.77  ? 48  TYR B CG  1 
ATOM   399  C  CD1 . TYR A 1 53  ? 30.955 12.113  2.559   1.00 13.77  ? 48  TYR B CD1 1 
ATOM   400  C  CD2 . TYR A 1 53  ? 30.607 13.910  1.051   1.00 14.79  ? 48  TYR B CD2 1 
ATOM   401  C  CE1 . TYR A 1 53  ? 32.246 11.962  2.098   1.00 13.29  ? 48  TYR B CE1 1 
ATOM   402  C  CE2 . TYR A 1 53  ? 31.927 13.802  0.612   1.00 15.63  ? 48  TYR B CE2 1 
ATOM   403  C  CZ  . TYR A 1 53  ? 32.738 12.804  1.112   1.00 14.95  ? 48  TYR B CZ  1 
ATOM   404  O  OH  . TYR A 1 53  ? 34.049 12.648  0.664   1.00 16.75  ? 48  TYR B OH  1 
ATOM   405  N  N   . LYS A 1 54  ? 25.473 12.350  2.768   1.00 13.77  ? 49  LYS B N   1 
ATOM   406  C  CA  . LYS A 1 54  ? 24.329 12.053  3.607   1.00 15.20  ? 49  LYS B CA  1 
ATOM   407  C  C   . LYS A 1 54  ? 23.951 10.585  3.480   1.00 14.84  ? 49  LYS B C   1 
ATOM   408  O  O   . LYS A 1 54  ? 23.628 9.923   4.461   1.00 15.29  ? 49  LYS B O   1 
ATOM   409  C  CB  . LYS A 1 54  ? 23.123 12.906  3.269   1.00 16.21  ? 49  LYS B CB  1 
ATOM   410  C  CG  . LYS A 1 54  ? 21.979 12.723  4.258   1.00 24.25  ? 49  LYS B CG  1 
ATOM   411  C  CD  . LYS A 1 54  ? 22.258 13.460  5.607   1.00 37.71  ? 49  LYS B CD  1 
ATOM   412  C  CE  . LYS A 1 54  ? 21.225 13.218  6.706   1.00 39.14  ? 49  LYS B CE  1 
ATOM   413  N  NZ  . LYS A 1 54  ? 19.865 12.911  6.185   1.00 37.36  ? 49  LYS B NZ  1 
ATOM   414  N  N   . ASN A 1 55  ? 23.978 10.063  2.251   1.00 14.78  ? 50  ASN B N   1 
ATOM   415  C  CA  . ASN A 1 55  ? 23.659 8.670   2.025   1.00 14.24  ? 50  ASN B CA  1 
ATOM   416  C  C   . ASN A 1 55  ? 24.723 7.755   2.619   1.00 15.54  ? 50  ASN B C   1 
ATOM   417  O  O   . ASN A 1 55  ? 24.396 6.738   3.207   1.00 17.29  ? 50  ASN B O   1 
ATOM   418  C  CB  . ASN A 1 55  ? 23.495 8.412   0.528   1.00 16.29  ? 50  ASN B CB  1 
ATOM   419  C  CG  . ASN A 1 55  ? 22.119 8.689   0.054   1.00 23.49  ? 50  ASN B CG  1 
ATOM   420  O  OD1 . ASN A 1 55  ? 21.220 7.877   0.301   1.00 29.94  ? 50  ASN B OD1 1 
ATOM   421  N  ND2 . ASN A 1 55  ? 21.896 9.774   -0.687  1.00 24.08  ? 50  ASN B ND2 1 
ATOM   422  N  N   . VAL A 1 56  ? 26.002 8.090   2.433   1.00 14.06  ? 51  VAL B N   1 
ATOM   423  C  CA  . VAL A 1 56  ? 27.067 7.279   3.014   1.00 12.80  ? 51  VAL B CA  1 
ATOM   424  C  C   . VAL A 1 56  ? 26.950 7.231   4.536   1.00 16.90  ? 51  VAL B C   1 
ATOM   425  O  O   . VAL A 1 56  ? 26.906 6.145   5.122   1.00 16.02  ? 51  VAL B O   1 
ATOM   426  C  CB  . VAL A 1 56  ? 28.462 7.731   2.588   1.00 14.19  ? 51  VAL B CB  1 
ATOM   427  C  CG1 . VAL A 1 56  ? 29.559 6.998   3.356   1.00 15.04  ? 51  VAL B CG1 1 
ATOM   428  C  CG2 . VAL A 1 56  ? 28.645 7.549   1.077   1.00 15.23  ? 51  VAL B CG2 1 
ATOM   429  N  N   . VAL A 1 57  ? 26.910 8.395   5.180   1.00 13.72  ? 52  VAL B N   1 
ATOM   430  C  CA  . VAL A 1 57  ? 26.859 8.434   6.634   1.00 15.01  ? 52  VAL B CA  1 
ATOM   431  C  C   . VAL A 1 57  ? 25.525 7.890   7.127   1.00 15.33  ? 52  VAL B C   1 
ATOM   432  O  O   . VAL A 1 57  ? 25.480 7.289   8.201   1.00 17.16  ? 52  VAL B O   1 
ATOM   433  C  CB  . VAL A 1 57  ? 27.197 9.852   7.193   1.00 14.55  ? 52  VAL B CB  1 
ATOM   434  C  CG1 . VAL A 1 57  ? 25.994 10.796  7.137   1.00 15.03  ? 52  VAL B CG1 1 
ATOM   435  C  CG2 . VAL A 1 57  ? 27.745 9.764   8.603   1.00 16.75  ? 52  VAL B CG2 1 
ATOM   436  N  N   . GLY A 1 58  ? 24.455 8.046   6.342   1.00 15.71  ? 53  GLY B N   1 
ATOM   437  C  CA  . GLY A 1 58  ? 23.153 7.519   6.716   1.00 17.09  ? 53  GLY B CA  1 
ATOM   438  C  C   . GLY A 1 58  ? 23.174 6.002   6.872   1.00 19.31  ? 53  GLY B C   1 
ATOM   439  O  O   . GLY A 1 58  ? 22.646 5.470   7.839   1.00 19.33  ? 53  GLY B O   1 
ATOM   440  N  N   . GLY A 1 59  ? 23.826 5.308   5.941   1.00 18.00  ? 54  GLY B N   1 
ATOM   441  C  CA  . GLY A 1 59  ? 24.008 3.867   6.062   1.00 18.30  ? 54  GLY B CA  1 
ATOM   442  C  C   . GLY A 1 59  ? 24.807 3.471   7.305   1.00 16.99  ? 54  GLY B C   1 
ATOM   443  O  O   . GLY A 1 59  ? 24.463 2.487   7.984   1.00 18.21  ? 54  GLY B O   1 
ATOM   444  N  N   . GLN A 1 60  ? 25.883 4.220   7.577   1.00 16.30  ? 55  GLN B N   1 
ATOM   445  C  CA  . GLN A 1 60  ? 26.729 3.962   8.731   1.00 15.91  ? 55  GLN B CA  1 
ATOM   446  C  C   . GLN A 1 60  ? 25.955 4.166   10.036  1.00 16.33  ? 55  GLN B C   1 
ATOM   447  O  O   . GLN A 1 60  ? 26.130 3.391   10.982  1.00 15.16  ? 55  GLN B O   1 
ATOM   448  C  CB  . GLN A 1 60  ? 27.955 4.843   8.712   1.00 16.47  ? 55  GLN B CB  1 
ATOM   449  C  CG  . GLN A 1 60  ? 28.876 4.550   7.538   1.00 17.42  ? 55  GLN B CG  1 
ATOM   450  C  CD  . GLN A 1 60  ? 29.983 5.524   7.462   1.00 19.01  ? 55  GLN B CD  1 
ATOM   451  O  OE1 . GLN A 1 60  ? 29.797 6.724   7.639   1.00 19.70  ? 55  GLN B OE1 1 
ATOM   452  N  NE2 . GLN A 1 60  ? 31.165 5.070   7.184   1.00 21.86  ? 55  GLN B NE2 1 
ATOM   453  N  N   . ARG A 1 61  ? 25.162 5.250   10.106  1.00 15.19  ? 56  ARG B N   1 
ATOM   454  C  CA  . ARG A 1 61  ? 24.380 5.564   11.298  1.00 15.33  ? 56  ARG B CA  1 
ATOM   455  C  C   . ARG A 1 61  ? 23.348 4.462   11.546  1.00 15.25  ? 56  ARG B C   1 
ATOM   456  O  O   . ARG A 1 61  ? 23.155 4.041   12.677  1.00 15.52  ? 56  ARG B O   1 
ATOM   457  C  CB  . ARG A 1 61  ? 23.703 6.950   11.172  1.00 15.32  ? 56  ARG B CB  1 
ATOM   458  C  CG  . ARG A 1 61  ? 24.658 8.127   11.154  1.00 16.09  ? 56  ARG B CG  1 
ATOM   459  C  CD  . ARG A 1 61  ? 23.983 9.410   10.670  1.00 17.75  ? 56  ARG B CD  1 
ATOM   460  N  NE  . ARG A 1 61  ? 22.955 9.887   11.597  1.00 17.10  ? 56  ARG B NE  1 
ATOM   461  C  CZ  . ARG A 1 61  ? 21.941 10.669  11.242  1.00 18.27  ? 56  ARG B CZ  1 
ATOM   462  N  NH1 . ARG A 1 61  ? 21.663 10.905  9.964   1.00 16.37  ? 56  ARG B NH1 1 
ATOM   463  N  NH2 . ARG A 1 61  ? 21.210 11.250  12.191  1.00 16.37  ? 56  ARG B NH2 1 
ATOM   464  N  N   . ALA A 1 62  ? 22.684 3.998   10.492  1.00 15.99  ? 57  ALA B N   1 
ATOM   465  C  CA  . ALA A 1 62  ? 21.678 2.964   10.639  1.00 16.62  ? 57  ALA B CA  1 
ATOM   466  C  C   . ALA A 1 62  ? 22.329 1.681   11.145  1.00 17.36  ? 57  ALA B C   1 
ATOM   467  O  O   . ALA A 1 62  ? 21.780 1.014   12.035  1.00 18.18  ? 57  ALA B O   1 
ATOM   468  C  CB  . ALA A 1 62  ? 20.947 2.718   9.328   1.00 18.89  ? 57  ALA B CB  1 
ATOM   469  N  N   . ALA A 1 63  ? 23.507 1.344   10.604  1.00 16.06  ? 58  ALA B N   1 
ATOM   470  C  CA  . ALA A 1 63  ? 24.228 0.141   11.023  1.00 18.11  ? 58  ALA B CA  1 
ATOM   471  C  C   . ALA A 1 63  ? 24.680 0.247   12.472  1.00 17.64  ? 58  ALA B C   1 
ATOM   472  O  O   . ALA A 1 63  ? 24.528 -0.682  13.269  1.00 16.68  ? 58  ALA B O   1 
ATOM   473  C  CB  . ALA A 1 63  ? 25.447 -0.106  10.123  1.00 17.17  ? 58  ALA B CB  1 
ATOM   474  N  N   . TRP A 1 64  ? 25.234 1.409   12.824  1.00 16.95  ? 59  TRP B N   1 
ATOM   475  C  CA  . TRP A 1 64  ? 25.683 1.660   14.183  1.00 15.52  ? 59  TRP B CA  1 
ATOM   476  C  C   . TRP A 1 64  ? 24.546 1.518   15.191  1.00 16.56  ? 59  TRP B C   1 
ATOM   477  O  O   . TRP A 1 64  ? 24.746 0.937   16.264  1.00 16.82  ? 59  TRP B O   1 
ATOM   478  C  CB  . TRP A 1 64  ? 26.352 3.056   14.302  1.00 15.36  ? 59  TRP B CB  1 
ATOM   479  C  CG  . TRP A 1 64  ? 26.961 3.325   15.636  1.00 15.27  ? 59  TRP B CG  1 
ATOM   480  C  CD1 . TRP A 1 64  ? 28.260 3.147   15.998  1.00 15.77  ? 59  TRP B CD1 1 
ATOM   481  C  CD2 . TRP A 1 64  ? 26.297 3.866   16.793  1.00 16.09  ? 59  TRP B CD2 1 
ATOM   482  N  NE1 . TRP A 1 64  ? 28.442 3.525   17.304  1.00 16.62  ? 59  TRP B NE1 1 
ATOM   483  C  CE2 . TRP A 1 64  ? 27.254 3.973   17.813  1.00 17.10  ? 59  TRP B CE2 1 
ATOM   484  C  CE3 . TRP A 1 64  ? 25.003 4.271   17.051  1.00 16.78  ? 59  TRP B CE3 1 
ATOM   485  C  CZ2 . TRP A 1 64  ? 26.940 4.441   19.098  1.00 19.27  ? 59  TRP B CZ2 1 
ATOM   486  C  CZ3 . TRP A 1 64  ? 24.691 4.740   18.320  1.00 18.08  ? 59  TRP B CZ3 1 
ATOM   487  C  CH2 . TRP A 1 64  ? 25.664 4.817   19.323  1.00 16.71  ? 59  TRP B CH2 1 
ATOM   488  N  N   . ARG A 1 65  ? 23.353 2.030   14.836  1.00 16.62  ? 60  ARG B N   1 
ATOM   489  C  CA  . ARG A 1 65  ? 22.219 1.915   15.732  1.00 17.39  ? 60  ARG B CA  1 
ATOM   490  C  C   . ARG A 1 65  ? 21.799 0.462   15.961  1.00 19.84  ? 60  ARG B C   1 
ATOM   491  O  O   . ARG A 1 65  ? 21.494 0.090   17.094  1.00 19.04  ? 60  ARG B O   1 
ATOM   492  C  CB  . ARG A 1 65  ? 21.056 2.721   15.221  1.00 18.38  ? 60  ARG B CB  1 
ATOM   493  C  CG  . ARG A 1 65  ? 21.328 4.227   15.256  1.00 20.14  ? 60  ARG B CG  1 
ATOM   494  C  CD  . ARG A 1 65  ? 20.228 4.954   14.505  1.00 26.69  ? 60  ARG B CD  1 
ATOM   495  N  NE  . ARG A 1 65  ? 20.532 6.376   14.442  1.00 32.11  ? 60  ARG B NE  1 
ATOM   496  C  CZ  . ARG A 1 65  ? 19.951 7.230   13.616  1.00 40.95  ? 60  ARG B CZ  1 
ATOM   497  N  NH1 . ARG A 1 65  ? 19.134 6.820   12.659  1.00 41.96  ? 60  ARG B NH1 1 
ATOM   498  N  NH2 . ARG A 1 65  ? 20.184 8.529   13.765  1.00 39.71  ? 60  ARG B NH2 1 
ATOM   499  N  N   . VAL A 1 66  ? 21.803 -0.349  14.895  1.00 16.96  ? 61  VAL B N   1 
ATOM   500  C  CA  . VAL A 1 66  ? 21.481 -1.761  15.011  1.00 17.30  ? 61  VAL B CA  1 
ATOM   501  C  C   . VAL A 1 66  ? 22.458 -2.428  15.975  1.00 19.24  ? 61  VAL B C   1 
ATOM   502  O  O   . VAL A 1 66  ? 22.046 -3.140  16.900  1.00 18.67  ? 61  VAL B O   1 
ATOM   503  C  CB  . VAL A 1 66  ? 21.502 -2.470  13.638  1.00 18.17  ? 61  VAL B CB  1 
ATOM   504  C  CG1 . VAL A 1 66  ? 21.546 -4.007  13.806  1.00 18.42  ? 61  VAL B CG1 1 
ATOM   505  C  CG2 . VAL A 1 66  ? 20.333 -2.041  12.778  1.00 20.98  ? 61  VAL B CG2 1 
ATOM   506  N  N   . LEU A 1 67  ? 23.760 -2.218  15.740  1.00 16.30  ? 62  LEU B N   1 
ATOM   507  C  CA  . LEU A 1 67  ? 24.810 -2.847  16.525  1.00 17.45  ? 62  LEU B CA  1 
ATOM   508  C  C   . LEU A 1 67  ? 24.842 -2.370  17.976  1.00 20.45  ? 62  LEU B C   1 
ATOM   509  O  O   . LEU A 1 67  ? 25.070 -3.181  18.883  1.00 20.80  ? 62  LEU B O   1 
ATOM   510  C  CB  . LEU A 1 67  ? 26.182 -2.672  15.864  1.00 17.44  ? 62  LEU B CB  1 
ATOM   511  C  CG  . LEU A 1 67  ? 26.344 -3.254  14.462  1.00 17.75  ? 62  LEU B CG  1 
ATOM   512  C  CD1 . LEU A 1 67  ? 27.653 -2.822  13.864  1.00 18.60  ? 62  LEU B CD1 1 
ATOM   513  C  CD2 . LEU A 1 67  ? 26.249 -4.763  14.495  1.00 19.32  ? 62  LEU B CD2 1 
ATOM   514  N  N   . SER A 1 68  ? 24.599 -1.072  18.205  1.00 18.61  ? 63  SER B N   1 
ATOM   515  C  CA  . SER A 1 68  ? 24.566 -0.529  19.556  1.00 19.90  ? 63  SER B CA  1 
ATOM   516  C  C   . SER A 1 68  ? 23.427 -1.162  20.344  1.00 21.14  ? 63  SER B C   1 
ATOM   517  O  O   . SER A 1 68  ? 23.587 -1.474  21.528  1.00 22.38  ? 63  SER B O   1 
ATOM   518  C  CB  . SER A 1 68  ? 24.424 1.005   19.502  1.00 22.99  ? 63  SER B CB  1 
ATOM   519  O  OG  . SER A 1 68  ? 24.460 1.529   20.826  1.00 26.42  ? 63  SER B OG  1 
ATOM   520  N  N   . SER A 1 69  ? 22.289 -1.357  19.682  1.00 20.06  ? 64  SER B N   1 
ATOM   521  C  CA  . SER A 1 69  ? 21.128 -1.964  20.315  1.00 24.49  ? 64  SER B CA  1 
ATOM   522  C  C   . SER A 1 69  ? 21.380 -3.416  20.724  1.00 24.75  ? 64  SER B C   1 
ATOM   523  O  O   . SER A 1 69  ? 21.012 -3.829  21.827  1.00 26.03  ? 64  SER B O   1 
ATOM   524  C  CB  . SER A 1 69  ? 19.932 -1.868  19.390  1.00 24.64  ? 64  SER B CB  1 
ATOM   525  O  OG  . SER A 1 69  ? 18.850 -2.617  19.897  1.00 36.66  ? 64  SER B OG  1 
ATOM   526  N  N   . ILE A 1 70  ? 22.062 -4.169  19.857  1.00 21.85  ? 65  ILE B N   1 
ATOM   527  C  CA  . ILE A 1 70  ? 22.439 -5.549  20.161  1.00 23.16  ? 65  ILE B CA  1 
ATOM   528  C  C   . ILE A 1 70  ? 23.419 -5.575  21.326  1.00 25.18  ? 65  ILE B C   1 
ATOM   529  O  O   . ILE A 1 70  ? 23.313 -6.417  22.230  1.00 27.10  ? 65  ILE B O   1 
ATOM   530  C  CB  . ILE A 1 70  ? 23.003 -6.267  18.920  1.00 21.60  ? 65  ILE B CB  1 
ATOM   531  C  CG1 . ILE A 1 70  ? 21.935 -6.395  17.816  1.00 21.40  ? 65  ILE B CG1 1 
ATOM   532  C  CG2 . ILE A 1 70  ? 23.620 -7.654  19.306  1.00 25.17  ? 65  ILE B CG2 1 
ATOM   533  C  CD1 . ILE A 1 70  ? 22.450 -6.757  16.430  1.00 23.21  ? 65  ILE B CD1 1 
ATOM   534  N  N   . GLU A 1 71  ? 24.349 -4.618  21.321  1.00 21.26  ? 66  GLU B N   1 
ATOM   535  C  CA  . GLU A 1 71  ? 25.378 -4.538  22.336  1.00 22.90  ? 66  GLU B CA  1 
ATOM   536  C  C   . GLU A 1 71  ? 24.779 -4.214  23.703  1.00 31.17  ? 66  GLU B C   1 
ATOM   537  O  O   . GLU A 1 71  ? 25.173 -4.811  24.707  1.00 33.07  ? 66  GLU B O   1 
ATOM   538  C  CB  . GLU A 1 71  ? 26.398 -3.503  21.947  1.00 21.92  ? 66  GLU B CB  1 
ATOM   539  C  CG  . GLU A 1 71  ? 27.615 -3.415  22.856  1.00 22.56  ? 66  GLU B CG  1 
ATOM   540  C  CD  . GLU A 1 71  ? 28.556 -2.302  22.486  1.00 25.19  ? 66  GLU B CD  1 
ATOM   541  O  OE1 . GLU A 1 71  ? 28.143 -1.430  21.679  1.00 28.04  ? 66  GLU B OE1 1 
ATOM   542  O  OE2 . GLU A 1 71  ? 29.676 -2.254  23.049  1.00 26.20  ? 66  GLU B OE2 1 
ATOM   543  N  N   . GLN A 1 72  ? 23.804 -3.298  23.725  1.00 27.61  ? 67  GLN B N   1 
ATOM   544  C  CA  . GLN A 1 72  ? 23.177 -2.891  24.974  1.00 35.34  ? 67  GLN B CA  1 
ATOM   545  C  C   . GLN A 1 72  ? 22.391 -4.061  25.558  1.00 38.96  ? 67  GLN B C   1 
ATOM   546  O  O   . GLN A 1 72  ? 22.438 -4.285  26.767  1.00 43.40  ? 67  GLN B O   1 
ATOM   547  C  CB  . GLN A 1 72  ? 22.255 -1.666  24.805  1.00 35.06  ? 67  GLN B CB  1 
ATOM   548  C  CG  . GLN A 1 72  ? 22.968 -0.330  24.457  1.00 46.24  ? 67  GLN B CG  1 
ATOM   549  C  CD  . GLN A 1 72  ? 24.225 -0.046  25.267  1.00 58.11  ? 67  GLN B CD  1 
ATOM   550  O  OE1 . GLN A 1 72  ? 25.330 0.151   24.720  1.00 60.94  ? 67  GLN B OE1 1 
ATOM   551  N  NE2 . GLN A 1 72  ? 24.088 0.002   26.586  1.00 61.81  ? 67  GLN B NE2 1 
ATOM   552  N  N   . LYS A 1 73  ? 21.684 -4.805  24.699  1.00 34.68  ? 68  LYS B N   1 
ATOM   553  C  CA  . LYS A 1 73  ? 20.979 -6.011  25.116  1.00 44.17  ? 68  LYS B CA  1 
ATOM   554  C  C   . LYS A 1 73  ? 21.876 -7.111  25.682  1.00 50.22  ? 68  LYS B C   1 
ATOM   555  O  O   . LYS A 1 73  ? 21.498 -7.782  26.642  1.00 47.72  ? 68  LYS B O   1 
ATOM   556  C  CB  . LYS A 1 73  ? 20.192 -6.584  23.954  1.00 44.50  ? 68  LYS B CB  1 
ATOM   557  C  CG  . LYS A 1 73  ? 18.973 -5.751  23.599  1.00 51.09  ? 68  LYS B CG  1 
ATOM   558  C  CD  . LYS A 1 73  ? 18.377 -6.182  22.266  1.00 56.70  ? 68  LYS B CD  1 
ATOM   559  C  CE  . LYS A 1 73  ? 17.677 -5.060  21.541  1.00 58.41  ? 68  LYS B CE  1 
ATOM   560  N  NZ  . LYS A 1 73  ? 17.867 -5.174  20.061  1.00 68.87  ? 68  LYS B NZ  1 
ATOM   561  N  N   . SER A 1 74  ? 23.059 -7.305  25.087  1.00 44.13  ? 69  SER B N   1 
ATOM   562  C  CA  . SER A 1 74  ? 24.001 -8.295  25.589  1.00 49.50  ? 69  SER B CA  1 
ATOM   563  C  C   . SER A 1 74  ? 24.545 -7.933  26.970  1.00 51.71  ? 69  SER B C   1 
ATOM   564  O  O   . SER A 1 74  ? 24.824 -8.823  27.770  1.00 57.49  ? 69  SER B O   1 
ATOM   565  C  CB  . SER A 1 74  ? 25.164 -8.488  24.620  1.00 47.35  ? 69  SER B CB  1 
ATOM   566  O  OG  . SER A 1 74  ? 26.101 -7.426  24.716  1.00 51.83  ? 69  SER B OG  1 
ATOM   567  N  N   . ASN A 1 75  ? 24.693 -6.627  27.238  1.00 54.58  ? 70  ASN B N   1 
ATOM   568  C  CA  . ASN A 1 75  ? 25.263 -6.131  28.482  1.00 61.46  ? 70  ASN B CA  1 
ATOM   569  C  C   . ASN A 1 75  ? 24.193 -5.873  29.541  1.00 63.19  ? 70  ASN B C   1 
ATOM   570  O  O   . ASN A 1 75  ? 24.037 -4.747  30.010  1.00 79.74  ? 70  ASN B O   1 
ATOM   571  C  CB  . ASN A 1 75  ? 26.062 -4.839  28.229  1.00 60.06  ? 70  ASN B CB  1 
ATOM   572  C  CG  . ASN A 1 75  ? 27.263 -5.028  27.346  1.00 66.78  ? 70  ASN B CG  1 
ATOM   573  O  OD1 . ASN A 1 75  ? 27.624 -6.149  26.970  1.00 76.94  ? 70  ASN B OD1 1 
ATOM   574  N  ND2 . ASN A 1 75  ? 27.914 -3.927  26.991  1.00 60.06  ? 70  ASN B ND2 1 
ATOM   575  N  N   . GLU A 1 76  ? 23.462 -6.931  29.907  1.00 73.91  ? 71  GLU B N   1 
ATOM   576  C  CA  . GLU A 1 76  ? 22.453 -6.868  30.952  1.00 76.23  ? 71  GLU B CA  1 
ATOM   577  C  C   . GLU A 1 76  ? 22.355 -8.200  31.692  1.00 79.15  ? 71  GLU B C   1 
ATOM   578  O  O   . GLU A 1 76  ? 22.885 -9.209  31.232  1.00 72.18  ? 71  GLU B O   1 
ATOM   579  C  CB  . GLU A 1 76  ? 21.097 -6.507  30.354  1.00 67.01  ? 71  GLU B CB  1 
ATOM   580  C  CG  . GLU A 1 76  ? 20.962 -5.039  30.017  1.00 71.63  ? 71  GLU B CG  1 
ATOM   581  C  CD  . GLU A 1 76  ? 19.713 -4.707  29.234  1.00 75.25  ? 71  GLU B CD  1 
ATOM   582  O  OE1 . GLU A 1 76  ? 18.990 -5.653  28.842  1.00 59.03  ? 71  GLU B OE1 1 
ATOM   583  O  OE2 . GLU A 1 76  ? 19.462 -3.501  29.007  1.00 73.18  ? 71  GLU B OE2 1 
ATOM   584  N  N   . SER A 1 79  ? 21.893 -11.521 30.400  1.00 113.06 ? 74  SER B N   1 
ATOM   585  C  CA  . SER A 1 79  ? 22.247 -11.961 29.029  1.00 109.95 ? 74  SER B CA  1 
ATOM   586  C  C   . SER A 1 79  ? 23.430 -12.922 29.075  1.00 103.75 ? 74  SER B C   1 
ATOM   587  O  O   . SER A 1 79  ? 24.334 -12.705 29.892  1.00 105.19 ? 74  SER B O   1 
ATOM   588  C  CB  . SER A 1 79  ? 22.551 -10.792 28.158  1.00 99.22  ? 74  SER B CB  1 
ATOM   589  O  OG  . SER A 1 79  ? 23.392 -11.173 27.080  1.00 82.55  ? 74  SER B OG  1 
ATOM   590  N  N   . GLU A 1 80  ? 23.410 -13.942 28.225  1.00 95.19  ? 75  GLU B N   1 
ATOM   591  C  CA  . GLU A 1 80  ? 24.539 -14.898 28.137  1.00 77.02  ? 75  GLU B CA  1 
ATOM   592  C  C   . GLU A 1 80  ? 25.751 -14.218 27.496  1.00 80.29  ? 75  GLU B C   1 
ATOM   593  O  O   . GLU A 1 80  ? 25.592 -13.618 26.423  1.00 73.96  ? 75  GLU B O   1 
ATOM   594  C  CB  . GLU A 1 80  ? 24.113 -16.138 27.349  1.00 65.30  ? 75  GLU B CB  1 
ATOM   595  C  CG  . GLU A 1 80  ? 25.060 -17.307 27.520  1.00 60.12  ? 75  GLU B CG  1 
ATOM   596  C  CD  . GLU A 1 80  ? 25.193 -17.752 28.962  1.00 56.74  ? 75  GLU B CD  1 
ATOM   597  O  OE1 . GLU A 1 80  ? 24.159 -18.072 29.573  1.00 49.10  ? 75  GLU B OE1 1 
ATOM   598  O  OE2 . GLU A 1 80  ? 26.326 -17.757 29.475  1.00 57.87  ? 75  GLU B OE2 1 
ATOM   599  N  N   . GLU A 1 81  ? 26.904 -14.302 28.149  1.00 78.86  ? 76  GLU B N   1 
ATOM   600  C  CA  . GLU A 1 81  ? 28.147 -13.733 27.647  1.00 76.22  ? 76  GLU B CA  1 
ATOM   601  C  C   . GLU A 1 81  ? 28.428 -14.256 26.240  1.00 76.61  ? 76  GLU B C   1 
ATOM   602  O  O   . GLU A 1 81  ? 28.444 -15.465 26.015  1.00 64.07  ? 76  GLU B O   1 
ATOM   603  C  CB  . GLU A 1 81  ? 29.325 -14.076 28.587  1.00 80.41  ? 76  GLU B CB  1 
ATOM   604  C  CG  . GLU A 1 81  ? 30.698 -13.631 28.093  1.00 77.09  ? 76  GLU B CG  1 
ATOM   605  C  CD  . GLU A 1 81  ? 30.867 -12.133 27.922  1.00 79.07  ? 76  GLU B CD  1 
ATOM   606  O  OE1 . GLU A 1 81  ? 30.658 -11.395 28.911  1.00 82.04  ? 76  GLU B OE1 1 
ATOM   607  O  OE2 . GLU A 1 81  ? 31.219 -11.696 26.804  1.00 70.80  ? 76  GLU B OE2 1 
ATOM   608  N  N   . LYS A 1 82  ? 28.653 -13.331 25.301  1.00 65.12  ? 77  LYS B N   1 
ATOM   609  C  CA  . LYS A 1 82  ? 28.857 -13.677 23.902  1.00 73.82  ? 77  LYS B CA  1 
ATOM   610  C  C   . LYS A 1 82  ? 30.278 -13.371 23.424  1.00 67.64  ? 77  LYS B C   1 
ATOM   611  O  O   . LYS A 1 82  ? 30.618 -13.641 22.272  1.00 66.94  ? 77  LYS B O   1 
ATOM   612  C  CB  . LYS A 1 82  ? 27.811 -12.950 23.028  1.00 75.97  ? 77  LYS B CB  1 
ATOM   613  C  CG  . LYS A 1 82  ? 27.614 -11.468 23.374  1.00 84.39  ? 77  LYS B CG  1 
ATOM   614  C  CD  . LYS A 1 82  ? 26.694 -10.751 22.405  1.00 84.25  ? 77  LYS B CD  1 
ATOM   615  C  CE  . LYS A 1 82  ? 25.257 -11.201 22.543  1.00 86.57  ? 77  LYS B CE  1 
ATOM   616  N  NZ  . LYS A 1 82  ? 24.337 -10.451 21.648  1.00 83.97  ? 77  LYS B NZ  1 
ATOM   617  N  N   . GLY A 1 83  ? 31.111 -12.824 24.321  1.00 47.73  ? 78  GLY B N   1 
ATOM   618  C  CA  . GLY A 1 83  ? 32.476 -12.457 23.978  1.00 35.11  ? 78  GLY B CA  1 
ATOM   619  C  C   . GLY A 1 83  ? 32.566 -11.061 23.367  1.00 27.06  ? 78  GLY B C   1 
ATOM   620  O  O   . GLY A 1 83  ? 31.589 -10.330 23.325  1.00 28.63  ? 78  GLY B O   1 
ATOM   621  N  N   . PRO A 1 84  ? 33.753 -10.676 22.863  1.00 22.56  ? 79  PRO B N   1 
ATOM   622  C  CA  . PRO A 1 84  ? 34.005 -9.298  22.456  1.00 20.76  ? 79  PRO B CA  1 
ATOM   623  C  C   . PRO A 1 84  ? 33.491 -8.872  21.076  1.00 21.42  ? 79  PRO B C   1 
ATOM   624  O  O   . PRO A 1 84  ? 33.670 -7.719  20.697  1.00 19.21  ? 79  PRO B O   1 
ATOM   625  C  CB  . PRO A 1 84  ? 35.539 -9.259  22.489  1.00 22.20  ? 79  PRO B CB  1 
ATOM   626  C  CG  . PRO A 1 84  ? 35.954 -10.653 22.069  1.00 24.58  ? 79  PRO B CG  1 
ATOM   627  C  CD  . PRO A 1 84  ? 34.941 -11.540 22.730  1.00 25.79  ? 79  PRO B CD  1 
ATOM   628  N  N   . GLU A 1 85  ? 32.853 -9.782  20.339  1.00 20.66  ? 80  GLU B N   1 
ATOM   629  C  CA  . GLU A 1 85  ? 32.624 -9.559  18.918  1.00 19.38  ? 80  GLU B CA  1 
ATOM   630  C  C   . GLU A 1 85  ? 31.651 -8.418  18.632  1.00 17.59  ? 80  GLU B C   1 
ATOM   631  O  O   . GLU A 1 85  ? 31.873 -7.666  17.685  1.00 16.92  ? 80  GLU B O   1 
ATOM   632  C  CB  . GLU A 1 85  ? 32.130 -10.862 18.238  1.00 19.38  ? 80  GLU B CB  1 
ATOM   633  C  CG  . GLU A 1 85  ? 33.208 -11.949 18.134  1.00 20.44  ? 80  GLU B CG  1 
ATOM   634  C  CD  . GLU A 1 85  ? 33.372 -12.884 19.327  1.00 24.50  ? 80  GLU B CD  1 
ATOM   635  O  OE1 . GLU A 1 85  ? 32.726 -12.646 20.372  1.00 22.65  ? 80  GLU B OE1 1 
ATOM   636  O  OE2 . GLU A 1 85  ? 34.135 -13.870 19.216  1.00 24.68  ? 80  GLU B OE2 1 
ATOM   637  N  N   . VAL A 1 86  ? 30.557 -8.321  19.397  1.00 18.39  ? 81  VAL B N   1 
ATOM   638  C  CA  . VAL A 1 86  ? 29.548 -7.296  19.149  1.00 20.19  ? 81  VAL B CA  1 
ATOM   639  C  C   . VAL A 1 86  ? 30.171 -5.921  19.364  1.00 20.79  ? 81  VAL B C   1 
ATOM   640  O  O   . VAL A 1 86  ? 30.038 -5.010  18.537  1.00 18.68  ? 81  VAL B O   1 
ATOM   641  C  CB  . VAL A 1 86  ? 28.267 -7.441  19.998  1.00 24.89  ? 81  VAL B CB  1 
ATOM   642  C  CG1 . VAL A 1 86  ? 27.349 -6.258  19.770  1.00 30.26  ? 81  VAL B CG1 1 
ATOM   643  C  CG2 . VAL A 1 86  ? 27.531 -8.732  19.674  1.00 27.25  ? 81  VAL B CG2 1 
ATOM   644  N  N   . ARG A 1 87  ? 30.884 -5.763  20.482  1.00 17.89  ? 82  ARG B N   1 
ATOM   645  C  CA  . ARG A 1 87  ? 31.569 -4.510  20.763  1.00 18.24  ? 82  ARG B CA  1 
ATOM   646  C  C   . ARG A 1 87  ? 32.617 -4.203  19.698  1.00 17.05  ? 82  ARG B C   1 
ATOM   647  O  O   . ARG A 1 87  ? 32.704 -3.072  19.204  1.00 17.82  ? 82  ARG B O   1 
ATOM   648  C  CB  . ARG A 1 87  ? 32.236 -4.537  22.174  1.00 20.26  ? 82  ARG B CB  1 
ATOM   649  C  CG  . ARG A 1 87  ? 33.164 -3.322  22.448  1.00 24.04  ? 82  ARG B CG  1 
ATOM   650  C  CD  . ARG A 1 87  ? 34.012 -3.451  23.725  1.00 28.22  ? 82  ARG B CD  1 
ATOM   651  N  NE  . ARG A 1 87  ? 34.809 -4.675  23.769  1.00 34.96  ? 82  ARG B NE  1 
ATOM   652  C  CZ  . ARG A 1 87  ? 35.928 -4.907  23.084  1.00 38.38  ? 82  ARG B CZ  1 
ATOM   653  N  NH1 . ARG A 1 87  ? 36.442 -4.013  22.258  1.00 39.12  ? 82  ARG B NH1 1 
ATOM   654  N  NH2 . ARG A 1 87  ? 36.560 -6.065  23.256  1.00 39.13  ? 82  ARG B NH2 1 
ATOM   655  N  N   . GLU A 1 88  ? 33.437 -5.201  19.321  1.00 16.29  ? 83  GLU B N   1 
ATOM   656  C  CA  . GLU A 1 88  ? 34.455 -4.992  18.307  1.00 15.61  ? 83  GLU B CA  1 
ATOM   657  C  C   . GLU A 1 88  ? 33.851 -4.485  16.995  1.00 13.99  ? 83  GLU B C   1 
ATOM   658  O  O   . GLU A 1 88  ? 34.393 -3.576  16.384  1.00 16.33  ? 83  GLU B O   1 
ATOM   659  C  CB  . GLU A 1 88  ? 35.241 -6.293  18.014  1.00 17.93  ? 83  GLU B CB  1 
ATOM   660  C  CG  . GLU A 1 88  ? 36.260 -6.674  19.081  1.00 20.31  ? 83  GLU B CG  1 
ATOM   661  C  CD  . GLU A 1 88  ? 36.819 -8.089  18.954  1.00 24.84  ? 83  GLU B CD  1 
ATOM   662  O  OE1 . GLU A 1 88  ? 36.348 -8.866  18.097  1.00 20.91  ? 83  GLU B OE1 1 
ATOM   663  O  OE2 . GLU A 1 88  ? 37.755 -8.413  19.710  1.00 24.08  ? 83  GLU B OE2 1 
ATOM   664  N  N   . TYR A 1 89  ? 32.758 -5.118  16.558  1.00 14.67  ? 84  TYR B N   1 
ATOM   665  C  CA  . TYR A 1 89  ? 32.190 -4.785  15.269  1.00 15.94  ? 84  TYR B CA  1 
ATOM   666  C  C   . TYR A 1 89  ? 31.484 -3.423  15.323  1.00 17.41  ? 84  TYR B C   1 
ATOM   667  O  O   . TYR A 1 89  ? 31.592 -2.624  14.388  1.00 16.93  ? 84  TYR B O   1 
ATOM   668  C  CB  . TYR A 1 89  ? 31.272 -5.911  14.772  1.00 14.96  ? 84  TYR B CB  1 
ATOM   669  C  CG  . TYR A 1 89  ? 30.774 -5.691  13.369  1.00 13.61  ? 84  TYR B CG  1 
ATOM   670  C  CD1 . TYR A 1 89  ? 31.625 -5.279  12.365  1.00 15.63  ? 84  TYR B CD1 1 
ATOM   671  C  CD2 . TYR A 1 89  ? 29.438 -5.843  13.063  1.00 15.36  ? 84  TYR B CD2 1 
ATOM   672  C  CE1 . TYR A 1 89  ? 31.150 -5.016  11.082  1.00 15.99  ? 84  TYR B CE1 1 
ATOM   673  C  CE2 . TYR A 1 89  ? 28.954 -5.592  11.790  1.00 17.30  ? 84  TYR B CE2 1 
ATOM   674  C  CZ  . TYR A 1 89  ? 29.807 -5.156  10.818  1.00 15.74  ? 84  TYR B CZ  1 
ATOM   675  O  OH  . TYR A 1 89  ? 29.335 -4.893  9.581   1.00 17.82  ? 84  TYR B OH  1 
ATOM   676  N  N   . ARG A 1 90  ? 30.786 -3.144  16.427  1.00 15.50  ? 85  ARG B N   1 
ATOM   677  C  CA  . ARG A 1 90  ? 30.262 -1.793  16.629  1.00 16.18  ? 85  ARG B CA  1 
ATOM   678  C  C   . ARG A 1 90  ? 31.357 -0.730  16.583  1.00 18.14  ? 85  ARG B C   1 
ATOM   679  O  O   . ARG A 1 90  ? 31.184 0.337   15.967  1.00 17.01  ? 85  ARG B O   1 
ATOM   680  C  CB  . ARG A 1 90  ? 29.486 -1.733  17.942  1.00 18.03  ? 85  ARG B CB  1 
ATOM   681  C  CG  . ARG A 1 90  ? 28.699 -0.433  18.174  1.00 17.94  ? 85  ARG B CG  1 
ATOM   682  C  CD  . ARG A 1 90  ? 29.498 0.617   18.901  1.00 18.08  ? 85  ARG B CD  1 
ATOM   683  N  NE  . ARG A 1 90  ? 29.900 0.158   20.227  1.00 19.00  ? 85  ARG B NE  1 
ATOM   684  C  CZ  . ARG A 1 90  ? 30.938 0.602   20.919  1.00 21.54  ? 85  ARG B CZ  1 
ATOM   685  N  NH1 . ARG A 1 90  ? 31.725 1.580   20.472  1.00 21.87  ? 85  ARG B NH1 1 
ATOM   686  N  NH2 . ARG A 1 90  ? 31.210 0.032   22.094  1.00 24.35  ? 85  ARG B NH2 1 
ATOM   687  N  N   . GLU A 1 91  ? 32.486 -1.004  17.243  1.00 16.12  ? 86  GLU B N   1 
ATOM   688  C  CA  . GLU A 1 91  ? 33.625 -0.106  17.219  1.00 17.11  ? 86  GLU B CA  1 
ATOM   689  C  C   . GLU A 1 91  ? 34.155 0.095   15.805  1.00 17.61  ? 86  GLU B C   1 
ATOM   690  O  O   . GLU A 1 91  ? 34.552 1.199   15.443  1.00 19.02  ? 86  GLU B O   1 
ATOM   691  C  CB  . GLU A 1 91  ? 34.739 -0.566  18.140  1.00 19.18  ? 86  GLU B CB  1 
ATOM   692  C  CG  . GLU A 1 91  ? 34.434 -0.372  19.616  1.00 23.45  ? 86  GLU B CG  1 
ATOM   693  C  CD  . GLU A 1 91  ? 35.447 -1.000  20.580  1.00 38.52  ? 86  GLU B CD  1 
ATOM   694  O  OE1 . GLU A 1 91  ? 36.329 -1.766  20.121  1.00 39.97  ? 86  GLU B OE1 1 
ATOM   695  O  OE2 . GLU A 1 91  ? 35.370 -0.703  21.798  1.00 40.63  ? 86  GLU B OE2 1 
ATOM   696  N  N   . LYS A 1 92  ? 34.183 -0.970  15.002  1.00 17.10  ? 87  LYS B N   1 
ATOM   697  C  CA  . LYS A 1 92  ? 34.658 -0.880  13.626  1.00 18.16  ? 87  LYS B CA  1 
ATOM   698  C  C   . LYS A 1 92  ? 33.759 0.053   12.817  1.00 16.08  ? 87  LYS B C   1 
ATOM   699  O  O   . LYS A 1 92  ? 34.247 0.941   12.132  1.00 16.91  ? 87  LYS B O   1 
ATOM   700  C  CB  . LYS A 1 92  ? 34.658 -2.273  12.985  1.00 20.29  ? 87  LYS B CB  1 
ATOM   701  C  CG  . LYS A 1 92  ? 35.064 -2.292  11.488  1.00 29.89  ? 87  LYS B CG  1 
ATOM   702  C  CD  . LYS A 1 92  ? 34.746 -3.633  10.818  1.00 32.15  ? 87  LYS B CD  1 
ATOM   703  C  CE  . LYS A 1 92  ? 34.722 -3.564  9.305   1.00 41.09  ? 87  LYS B CE  1 
ATOM   704  N  NZ  . LYS A 1 92  ? 36.021 -3.110  8.764   1.00 48.09  ? 87  LYS B NZ  1 
ATOM   705  N  N   . VAL A 1 93  ? 32.453 -0.184  12.892  1.00 15.23  ? 88  VAL B N   1 
ATOM   706  C  CA  . VAL A 1 93  ? 31.519 0.683   12.184  1.00 16.15  ? 88  VAL B CA  1 
ATOM   707  C  C   . VAL A 1 93  ? 31.603 2.120   12.702  1.00 15.83  ? 88  VAL B C   1 
ATOM   708  O  O   . VAL A 1 93  ? 31.589 3.062   11.908  1.00 15.58  ? 88  VAL B O   1 
ATOM   709  C  CB  . VAL A 1 93  ? 30.126 0.121   12.265  1.00 15.43  ? 88  VAL B CB  1 
ATOM   710  C  CG1 . VAL A 1 93  ? 29.113 1.107   11.702  1.00 17.10  ? 88  VAL B CG1 1 
ATOM   711  C  CG2 . VAL A 1 93  ? 30.052 -1.238  11.577  1.00 16.70  ? 88  VAL B CG2 1 
ATOM   712  N  N   . GLU A 1 94  ? 31.711 2.293   14.026  1.00 14.70  ? 89  GLU B N   1 
ATOM   713  C  CA  . GLU A 1 94  ? 31.857 3.618   14.625  1.00 16.54  ? 89  GLU B CA  1 
ATOM   714  C  C   . GLU A 1 94  ? 33.075 4.381   14.100  1.00 17.67  ? 89  GLU B C   1 
ATOM   715  O  O   . GLU A 1 94  ? 33.020 5.569   13.784  1.00 16.62  ? 89  GLU B O   1 
ATOM   716  C  CB  . GLU A 1 94  ? 31.912 3.440   16.136  1.00 17.51  ? 89  GLU B CB  1 
ATOM   717  C  CG  . GLU A 1 94  ? 31.904 4.722   16.926  1.00 16.87  ? 89  GLU B CG  1 
ATOM   718  C  CD  . GLU A 1 94  ? 31.836 4.441   18.409  1.00 17.59  ? 89  GLU B CD  1 
ATOM   719  O  OE1 . GLU A 1 94  ? 30.829 3.846   18.859  1.00 18.05  ? 89  GLU B OE1 1 
ATOM   720  O  OE2 . GLU A 1 94  ? 32.787 4.837   19.114  1.00 23.56  ? 89  GLU B OE2 1 
ATOM   721  N  N   . THR A 1 95  ? 34.221 3.705   14.021  1.00 16.29  ? 90  THR B N   1 
ATOM   722  C  CA  . THR A 1 95  ? 35.431 4.320   13.526  1.00 16.00  ? 90  THR B CA  1 
ATOM   723  C  C   . THR A 1 95  ? 35.253 4.762   12.069  1.00 16.03  ? 90  THR B C   1 
ATOM   724  O  O   . THR A 1 95  ? 35.747 5.813   11.687  1.00 16.83  ? 90  THR B O   1 
ATOM   725  C  CB  . THR A 1 95  ? 36.609 3.312   13.740  1.00 20.30  ? 90  THR B CB  1 
ATOM   726  O  OG1 . THR A 1 95  ? 36.744 3.072   15.151  1.00 20.80  ? 90  THR B OG1 1 
ATOM   727  C  CG2 . THR A 1 95  ? 37.874 3.803   13.189  1.00 22.73  ? 90  THR B CG2 1 
ATOM   728  N  N   . GLU A 1 96  ? 34.610 3.933   11.236  1.00 16.33  ? 91  GLU B N   1 
ATOM   729  C  CA  A GLU A 1 96  ? 34.422 4.275   9.837   0.50 15.95  ? 91  GLU B CA  1 
ATOM   730  C  CA  B GLU A 1 96  ? 34.393 4.251   9.833   0.50 16.18  ? 91  GLU B CA  1 
ATOM   731  C  C   . GLU A 1 96  ? 33.500 5.489   9.709   1.00 15.32  ? 91  GLU B C   1 
ATOM   732  O  O   . GLU A 1 96  ? 33.763 6.381   8.895   1.00 15.57  ? 91  GLU B O   1 
ATOM   733  C  CB  A GLU A 1 96  ? 33.901 3.087   9.046   0.50 18.40  ? 91  GLU B CB  1 
ATOM   734  C  CB  B GLU A 1 96  ? 33.768 3.050   9.096   0.50 19.31  ? 91  GLU B CB  1 
ATOM   735  C  CG  A GLU A 1 96  ? 34.940 1.993   8.962   0.50 18.72  ? 91  GLU B CG  1 
ATOM   736  C  CG  B GLU A 1 96  ? 33.723 3.201   7.583   0.50 21.27  ? 91  GLU B CG  1 
ATOM   737  C  CD  A GLU A 1 96  ? 34.531 0.783   8.159   0.50 22.16  ? 91  GLU B CD  1 
ATOM   738  C  CD  B GLU A 1 96  ? 32.913 2.141   6.869   0.50 21.48  ? 91  GLU B CD  1 
ATOM   739  O  OE1 A GLU A 1 96  ? 33.426 0.805   7.578   0.50 20.67  ? 91  GLU B OE1 1 
ATOM   740  O  OE1 B GLU A 1 96  ? 33.462 1.022   6.735   0.50 21.83  ? 91  GLU B OE1 1 
ATOM   741  O  OE2 A GLU A 1 96  ? 35.316 -0.194  8.129   0.50 22.39  ? 91  GLU B OE2 1 
ATOM   742  O  OE2 B GLU A 1 96  ? 31.747 2.397   6.462   0.50 18.12  ? 91  GLU B OE2 1 
ATOM   743  N  N   . LEU A 1 97  ? 32.441 5.520   10.521  1.00 14.72  ? 92  LEU B N   1 
ATOM   744  C  CA  A LEU A 1 97  ? 31.523 6.657   10.584  0.50 15.26  ? 92  LEU B CA  1 
ATOM   745  C  CA  B LEU A 1 97  ? 31.529 6.657   10.592  0.50 17.16  ? 92  LEU B CA  1 
ATOM   746  C  C   . LEU A 1 97  ? 32.256 7.938   10.983  1.00 16.61  ? 92  LEU B C   1 
ATOM   747  O  O   . LEU A 1 97  ? 32.082 8.995   10.357  1.00 15.44  ? 92  LEU B O   1 
ATOM   748  C  CB  A LEU A 1 97  ? 30.376 6.285   11.560  0.50 14.14  ? 92  LEU B CB  1 
ATOM   749  C  CB  B LEU A 1 97  ? 30.426 6.334   11.599  0.50 18.35  ? 92  LEU B CB  1 
ATOM   750  C  CG  A LEU A 1 97  ? 29.173 7.234   11.716  0.50 12.81  ? 92  LEU B CG  1 
ATOM   751  C  CG  B LEU A 1 97  ? 29.424 7.436   11.887  0.50 20.27  ? 92  LEU B CG  1 
ATOM   752  C  CD1 A LEU A 1 97  ? 27.972 6.496   12.248  0.50 14.65  ? 92  LEU B CD1 1 
ATOM   753  C  CD1 B LEU A 1 97  ? 28.883 7.992   10.642  0.50 22.55  ? 92  LEU B CD1 1 
ATOM   754  C  CD2 A LEU A 1 97  ? 29.528 8.402   12.628  0.50 12.89  ? 92  LEU B CD2 1 
ATOM   755  C  CD2 B LEU A 1 97  ? 28.327 6.929   12.704  0.50 20.50  ? 92  LEU B CD2 1 
ATOM   756  N  N   . GLN A 1 98  ? 33.079 7.859   12.037  1.00 15.83  ? 93  GLN B N   1 
ATOM   757  C  CA  . GLN A 1 98  ? 33.877 8.993   12.463  1.00 15.83  ? 93  GLN B CA  1 
ATOM   758  C  C   . GLN A 1 98  ? 34.798 9.449   11.346  1.00 16.06  ? 93  GLN B C   1 
ATOM   759  O  O   . GLN A 1 98  ? 35.051 10.639  11.196  1.00 17.69  ? 93  GLN B O   1 
ATOM   760  C  CB  . GLN A 1 98  ? 34.661 8.658   13.744  1.00 16.66  ? 93  GLN B CB  1 
ATOM   761  C  CG  . GLN A 1 98  ? 33.725 8.510   14.920  1.00 16.76  ? 93  GLN B CG  1 
ATOM   762  C  CD  . GLN A 1 98  ? 34.381 7.902   16.128  1.00 20.03  ? 93  GLN B CD  1 
ATOM   763  O  OE1 . GLN A 1 98  ? 35.257 7.017   15.990  1.00 20.29  ? 93  GLN B OE1 1 
ATOM   764  N  NE2 . GLN A 1 98  ? 33.998 8.360   17.328  1.00 19.53  ? 93  GLN B NE2 1 
ATOM   765  N  N   . GLY A 1 99  ? 35.356 8.498   10.593  1.00 16.25  ? 94  GLY B N   1 
ATOM   766  C  CA  . GLY A 1 99  ? 36.230 8.863   9.492   1.00 15.66  ? 94  GLY B CA  1 
ATOM   767  C  C   . GLY A 1 99  ? 35.531 9.639   8.373   1.00 14.39  ? 94  GLY B C   1 
ATOM   768  O  O   . GLY A 1 99  ? 36.109 10.563  7.815   1.00 16.08  ? 94  GLY B O   1 
ATOM   769  N  N   . VAL A 1 100 ? 34.300 9.250   8.039   1.00 14.29  ? 95  VAL B N   1 
ATOM   770  C  CA  . VAL A 1 100 ? 33.497 9.968   7.060   1.00 15.11  ? 95  VAL B CA  1 
ATOM   771  C  C   . VAL A 1 100 ? 33.204 11.380  7.576   1.00 14.68  ? 95  VAL B C   1 
ATOM   772  O  O   . VAL A 1 100 ? 33.381 12.359  6.864   1.00 15.02  ? 95  VAL B O   1 
ATOM   773  C  CB  . VAL A 1 100 ? 32.216 9.208   6.720   1.00 16.14  ? 95  VAL B CB  1 
ATOM   774  C  CG1 . VAL A 1 100 ? 31.241 10.076  5.904   1.00 17.84  ? 95  VAL B CG1 1 
ATOM   775  C  CG2 . VAL A 1 100 ? 32.522 7.923   5.995   1.00 18.02  ? 95  VAL B CG2 1 
ATOM   776  N  N   . CYS A 1 101 ? 32.786 11.499  8.840   1.00 13.37  ? 96  CYS B N   1 
ATOM   777  C  CA  . CYS A 1 101 ? 32.520 12.810  9.415   1.00 13.81  ? 96  CYS B CA  1 
ATOM   778  C  C   . CYS A 1 101 ? 33.774 13.675  9.383   1.00 14.37  ? 96  CYS B C   1 
ATOM   779  O  O   . CYS A 1 101 ? 33.708 14.849  9.015   1.00 15.24  ? 96  CYS B O   1 
ATOM   780  C  CB  . CYS A 1 101 ? 31.979 12.715  10.837  1.00 14.94  ? 96  CYS B CB  1 
ATOM   781  S  SG  . CYS A 1 101 ? 30.363 11.945  10.978  1.00 16.45  ? 96  CYS B SG  1 
ATOM   782  N  N   . ASP A 1 102 ? 34.926 13.125  9.781   1.00 14.20  ? 97  ASP B N   1 
ATOM   783  C  CA  . ASP A 1 102 ? 36.170 13.874  9.715   1.00 15.61  ? 97  ASP B CA  1 
ATOM   784  C  C   . ASP A 1 102 ? 36.553 14.317  8.305   1.00 14.44  ? 97  ASP B C   1 
ATOM   785  O  O   . ASP A 1 102 ? 37.068 15.406  8.129   1.00 16.46  ? 97  ASP B O   1 
ATOM   786  C  CB  . ASP A 1 102 ? 37.293 13.037  10.334  1.00 17.98  ? 97  ASP B CB  1 
ATOM   787  C  CG  . ASP A 1 102 ? 37.224 12.887  11.847  1.00 25.12  ? 97  ASP B CG  1 
ATOM   788  O  OD1 . ASP A 1 102 ? 36.462 13.619  12.476  1.00 27.27  ? 97  ASP B OD1 1 
ATOM   789  O  OD2 . ASP A 1 102 ? 37.956 12.039  12.382  1.00 30.23  ? 97  ASP B OD2 1 
ATOM   790  N  N   . THR A 1 103 ? 36.276 13.466  7.314   1.00 15.42  ? 98  THR B N   1 
ATOM   791  C  CA  . THR A 1 103 ? 36.509 13.830  5.925   1.00 15.16  ? 98  THR B CA  1 
ATOM   792  C  C   . THR A 1 103 ? 35.666 15.037  5.514   1.00 14.41  ? 98  THR B C   1 
ATOM   793  O  O   . THR A 1 103 ? 36.180 16.000  4.943   1.00 15.21  ? 98  THR B O   1 
ATOM   794  C  CB  . THR A 1 103 ? 36.225 12.640  5.007   1.00 18.05  ? 98  THR B CB  1 
ATOM   795  O  OG1 . THR A 1 103 ? 37.152 11.581  5.247   1.00 18.85  ? 98  THR B OG1 1 
ATOM   796  C  CG2 . THR A 1 103 ? 36.281 13.037  3.542   1.00 17.36  ? 98  THR B CG2 1 
ATOM   797  N  N   . VAL A 1 104 ? 34.361 15.002  5.838   1.00 13.66  ? 99  VAL B N   1 
ATOM   798  C  CA  . VAL A 1 104 ? 33.484 16.108  5.481   1.00 13.41  ? 99  VAL B CA  1 
ATOM   799  C  C   . VAL A 1 104 ? 33.939 17.381  6.192   1.00 12.32  ? 99  VAL B C   1 
ATOM   800  O  O   . VAL A 1 104 ? 34.059 18.448  5.595   1.00 12.74  ? 99  VAL B O   1 
ATOM   801  C  CB  . VAL A 1 104 ? 32.015 15.744  5.802   1.00 13.81  ? 99  VAL B CB  1 
ATOM   802  C  CG1 . VAL A 1 104 ? 31.118 16.969  5.683   1.00 15.85  ? 99  VAL B CG1 1 
ATOM   803  C  CG2 . VAL A 1 104 ? 31.499 14.606  4.915   1.00 15.11  ? 99  VAL B CG2 1 
ATOM   804  N  N   . LEU A 1 105 ? 34.212 17.270  7.502   1.00 13.09  ? 100 LEU B N   1 
ATOM   805  C  CA  . LEU A 1 105 ? 34.614 18.433  8.277   1.00 12.60  ? 100 LEU B CA  1 
ATOM   806  C  C   . LEU A 1 105 ? 35.921 19.007  7.742   1.00 14.09  ? 100 LEU B C   1 
ATOM   807  O  O   . LEU A 1 105 ? 36.094 20.236  7.706   1.00 15.56  ? 100 LEU B O   1 
ATOM   808  C  CB  . LEU A 1 105 ? 34.705 18.106  9.763   1.00 13.40  ? 100 LEU B CB  1 
ATOM   809  C  CG  . LEU A 1 105 ? 33.386 17.782  10.373  1.00 13.40  ? 100 LEU B CG  1 
ATOM   810  C  CD1 . LEU A 1 105 ? 33.520 17.141  11.746  1.00 15.85  ? 100 LEU B CD1 1 
ATOM   811  C  CD2 . LEU A 1 105 ? 32.456 19.014  10.467  1.00 14.68  ? 100 LEU B CD2 1 
ATOM   812  N  N   . GLY A 1 106 ? 36.802 18.110  7.258   1.00 14.61  ? 101 GLY B N   1 
ATOM   813  C  CA  . GLY A 1 106 ? 38.059 18.557  6.687   1.00 15.94  ? 101 GLY B CA  1 
ATOM   814  C  C   . GLY A 1 106 ? 37.873 19.335  5.384   1.00 15.41  ? 101 GLY B C   1 
ATOM   815  O  O   . GLY A 1 106 ? 38.568 20.324  5.143   1.00 18.94  ? 101 GLY B O   1 
ATOM   816  N  N   . LEU A 1 107 ? 36.933 18.901  4.535   1.00 13.64  ? 102 LEU B N   1 
ATOM   817  C  CA  . LEU A 1 107 ? 36.637 19.618  3.307   1.00 13.92  ? 102 LEU B CA  1 
ATOM   818  C  C   . LEU A 1 107 ? 36.070 20.999  3.638   1.00 14.71  ? 102 LEU B C   1 
ATOM   819  O  O   . LEU A 1 107 ? 36.357 21.988  2.959   1.00 14.89  ? 102 LEU B O   1 
ATOM   820  C  CB  . LEU A 1 107 ? 35.649 18.839  2.456   1.00 15.51  ? 102 LEU B CB  1 
ATOM   821  C  CG  . LEU A 1 107 ? 36.160 17.510  1.867   1.00 16.97  ? 102 LEU B CG  1 
ATOM   822  C  CD1 . LEU A 1 107 ? 35.015 16.790  1.191   1.00 20.14  ? 102 LEU B CD1 1 
ATOM   823  C  CD2 . LEU A 1 107 ? 37.329 17.737  0.926   1.00 21.45  ? 102 LEU B CD2 1 
ATOM   824  N  N   . LEU A 1 108 ? 35.184 21.055  4.644   1.00 13.71  ? 103 LEU B N   1 
ATOM   825  C  CA  . LEU A 1 108 ? 34.593 22.328  5.021   1.00 14.69  ? 103 LEU B CA  1 
ATOM   826  C  C   . LEU A 1 108 ? 35.666 23.281  5.549   1.00 14.49  ? 103 LEU B C   1 
ATOM   827  O  O   . LEU A 1 108 ? 35.623 24.485  5.283   1.00 15.10  ? 103 LEU B O   1 
ATOM   828  C  CB  . LEU A 1 108 ? 33.461 22.102  6.043   1.00 14.00  ? 103 LEU B CB  1 
ATOM   829  C  CG  . LEU A 1 108 ? 32.265 21.333  5.538   1.00 14.11  ? 103 LEU B CG  1 
ATOM   830  C  CD1 . LEU A 1 108 ? 31.365 20.948  6.668   1.00 15.73  ? 103 LEU B CD1 1 
ATOM   831  C  CD2 . LEU A 1 108 ? 31.429 22.148  4.585   1.00 15.57  ? 103 LEU B CD2 1 
ATOM   832  N  N   . ASP A 1 109 ? 36.618 22.744  6.313   1.00 14.97  ? 104 ASP B N   1 
ATOM   833  C  CA  . ASP A 1 109 ? 37.678 23.553  6.891   1.00 18.15  ? 104 ASP B CA  1 
ATOM   834  C  C   . ASP A 1 109 ? 38.801 23.900  5.916   1.00 17.49  ? 104 ASP B C   1 
ATOM   835  O  O   . ASP A 1 109 ? 39.518 24.888  6.134   1.00 21.56  ? 104 ASP B O   1 
ATOM   836  C  CB  . ASP A 1 109 ? 38.296 22.828  8.096   1.00 19.54  ? 104 ASP B CB  1 
ATOM   837  C  CG  . ASP A 1 109 ? 38.999 23.813  9.005   1.00 28.94  ? 104 ASP B CG  1 
ATOM   838  O  OD1 . ASP A 1 109 ? 38.375 24.873  9.335   1.00 31.32  ? 104 ASP B OD1 1 
ATOM   839  O  OD2 . ASP A 1 109 ? 40.158 23.536  9.395   1.00 31.92  ? 104 ASP B OD2 1 
ATOM   840  N  N   . SER A 1 110 ? 38.947 23.095  4.859   1.00 18.63  ? 105 SER B N   1 
ATOM   841  C  CA  . SER A 1 110 ? 39.995 23.255  3.867   1.00 20.44  ? 105 SER B CA  1 
ATOM   842  C  C   . SER A 1 110 ? 39.461 23.083  2.448   1.00 22.89  ? 105 SER B C   1 
ATOM   843  O  O   . SER A 1 110 ? 39.681 22.031  1.836   1.00 23.29  ? 105 SER B O   1 
ATOM   844  C  CB  . SER A 1 110 ? 41.096 22.215  4.116   1.00 23.26  ? 105 SER B CB  1 
ATOM   845  O  OG  . SER A 1 110 ? 41.557 22.283  5.453   1.00 26.96  ? 105 SER B OG  1 
ATOM   846  N  N   . HIS A 1 111 ? 38.756 24.082  1.896   1.00 20.35  ? 106 HIS B N   1 
ATOM   847  C  CA  . HIS A 1 111 ? 38.653 25.441  2.412   1.00 20.04  ? 106 HIS B CA  1 
ATOM   848  C  C   . HIS A 1 111 ? 37.282 26.008  2.053   1.00 16.81  ? 106 HIS B C   1 
ATOM   849  O  O   . HIS A 1 111 ? 37.129 27.186  1.744   1.00 19.12  ? 106 HIS B O   1 
ATOM   850  C  CB  . HIS A 1 111 ? 39.752 26.318  1.797   1.00 21.33  ? 106 HIS B CB  1 
ATOM   851  C  CG  . HIS A 1 111 ? 41.118 25.856  2.164   1.00 22.54  ? 106 HIS B CG  1 
ATOM   852  N  ND1 . HIS A 1 111 ? 41.698 26.180  3.374   1.00 22.61  ? 106 HIS B ND1 1 
ATOM   853  C  CD2 . HIS A 1 111 ? 42.020 25.099  1.511   1.00 23.98  ? 106 HIS B CD2 1 
ATOM   854  C  CE1 . HIS A 1 111 ? 42.901 25.626  3.445   1.00 24.77  ? 106 HIS B CE1 1 
ATOM   855  N  NE2 . HIS A 1 111 ? 43.110 24.950  2.334   1.00 23.83  ? 106 HIS B NE2 1 
ATOM   856  N  N   . LEU A 1 112 ? 36.253 25.155  2.089   1.00 15.86  ? 107 LEU B N   1 
ATOM   857  C  CA  . LEU A 1 112 ? 34.958 25.582  1.599   1.00 14.35  ? 107 LEU B CA  1 
ATOM   858  C  C   . LEU A 1 112 ? 34.368 26.768  2.379   1.00 13.85  ? 107 LEU B C   1 
ATOM   859  O  O   . LEU A 1 112 ? 33.899 27.723  1.779   1.00 17.24  ? 107 LEU B O   1 
ATOM   860  C  CB  . LEU A 1 112 ? 33.989 24.428  1.602   1.00 14.75  ? 107 LEU B CB  1 
ATOM   861  C  CG  . LEU A 1 112 ? 34.213 23.313  0.576   1.00 15.98  ? 107 LEU B CG  1 
ATOM   862  C  CD1 . LEU A 1 112 ? 33.327 22.152  0.879   1.00 15.19  ? 107 LEU B CD1 1 
ATOM   863  C  CD2 . LEU A 1 112 ? 33.976 23.805  -0.830  1.00 17.08  ? 107 LEU B CD2 1 
ATOM   864  N  N   . ILE A 1 113 ? 34.364 26.701  3.715   1.00 15.14  ? 108 ILE B N   1 
ATOM   865  C  CA  . ILE A 1 113 ? 33.721 27.723  4.522   1.00 16.00  ? 108 ILE B CA  1 
ATOM   866  C  C   . ILE A 1 113 ? 34.422 29.069  4.329   1.00 17.09  ? 108 ILE B C   1 
ATOM   867  O  O   . ILE A 1 113 ? 33.778 30.090  4.123   1.00 16.58  ? 108 ILE B O   1 
ATOM   868  C  CB  . ILE A 1 113 ? 33.635 27.320  5.994   1.00 15.08  ? 108 ILE B CB  1 
ATOM   869  C  CG1 . ILE A 1 113 ? 32.589 26.198  6.169   1.00 16.22  ? 108 ILE B CG1 1 
ATOM   870  C  CG2 . ILE A 1 113 ? 33.279 28.570  6.862   1.00 16.10  ? 108 ILE B CG2 1 
ATOM   871  C  CD1 . ILE A 1 113 ? 32.579 25.553  7.505   1.00 17.82  ? 108 ILE B CD1 1 
ATOM   872  N  N   . LYS A 1 114 ? 35.748 29.079  4.403   1.00 17.27  ? 109 LYS B N   1 
ATOM   873  C  CA  . LYS A 1 114 ? 36.438 30.362  4.366   1.00 17.93  ? 109 LYS B CA  1 
ATOM   874  C  C   . LYS A 1 114 ? 36.277 31.114  3.047   1.00 18.40  ? 109 LYS B C   1 
ATOM   875  O  O   . LYS A 1 114 ? 36.373 32.341  3.043   1.00 21.51  ? 109 LYS B O   1 
ATOM   876  C  CB  . LYS A 1 114 ? 37.924 30.233  4.710   1.00 21.97  ? 109 LYS B CB  1 
ATOM   877  C  CG  . LYS A 1 114 ? 38.741 29.489  3.715   1.00 23.37  ? 109 LYS B CG  1 
ATOM   878  C  CD  . LYS A 1 114 ? 40.260 29.497  4.067   1.00 24.40  ? 109 LYS B CD  1 
ATOM   879  C  CE  . LYS A 1 114 ? 40.583 28.965  5.443   1.00 26.19  ? 109 LYS B CE  1 
ATOM   880  N  NZ  . LYS A 1 114 ? 40.214 27.539  5.578   1.00 28.63  ? 109 LYS B NZ  1 
ATOM   881  N  N   . GLU A 1 115 ? 36.011 30.410  1.938   1.00 16.32  ? 110 GLU B N   1 
ATOM   882  C  CA  . GLU A 1 115 ? 35.800 31.094  0.676   1.00 16.95  ? 110 GLU B CA  1 
ATOM   883  C  C   . GLU A 1 115 ? 34.326 31.408  0.419   1.00 19.09  ? 110 GLU B C   1 
ATOM   884  O  O   . GLU A 1 115 ? 34.035 32.070  -0.577  1.00 20.81  ? 110 GLU B O   1 
ATOM   885  C  CB  . GLU A 1 115 ? 36.366 30.273  -0.480  1.00 19.50  ? 110 GLU B CB  1 
ATOM   886  C  CG  . GLU A 1 115 ? 37.891 30.123  -0.411  1.00 20.53  ? 110 GLU B CG  1 
ATOM   887  C  CD  . GLU A 1 115 ? 38.657 31.427  -0.590  1.00 30.24  ? 110 GLU B CD  1 
ATOM   888  O  OE1 . GLU A 1 115 ? 38.046 32.475  -0.931  1.00 31.47  ? 110 GLU B OE1 1 
ATOM   889  O  OE2 . GLU A 1 115 ? 39.892 31.401  -0.373  1.00 37.68  ? 110 GLU B OE2 1 
ATOM   890  N  N   . ALA A 1 116 ? 33.425 30.930  1.294   1.00 17.30  ? 111 ALA B N   1 
ATOM   891  C  CA  . ALA A 1 116 ? 31.988 31.086  1.094   1.00 19.76  ? 111 ALA B CA  1 
ATOM   892  C  C   . ALA A 1 116 ? 31.528 32.441  1.634   1.00 19.66  ? 111 ALA B C   1 
ATOM   893  O  O   . ALA A 1 116 ? 31.429 32.631  2.847   1.00 22.36  ? 111 ALA B O   1 
ATOM   894  C  CB  . ALA A 1 116 ? 31.237 29.957  1.783   1.00 18.53  ? 111 ALA B CB  1 
ATOM   895  N  N   . GLY A 1 117 ? 31.215 33.363  0.732   1.00 20.72  ? 112 GLY B N   1 
ATOM   896  C  CA  . GLY A 1 117 ? 30.814 34.716  1.100   1.00 20.99  ? 112 GLY B CA  1 
ATOM   897  C  C   . GLY A 1 117 ? 29.342 35.056  0.891   1.00 23.01  ? 112 GLY B C   1 
ATOM   898  O  O   . GLY A 1 117 ? 28.824 35.982  1.517   1.00 27.31  ? 112 GLY B O   1 
ATOM   899  N  N   . ASP A 1 118 ? 28.647 34.292  0.050   1.00 18.89  ? 113 ASP B N   1 
ATOM   900  C  CA  . ASP A 1 118 ? 27.233 34.531  -0.163  1.00 19.23  ? 113 ASP B CA  1 
ATOM   901  C  C   . ASP A 1 118 ? 26.459 33.802  0.923   1.00 20.16  ? 113 ASP B C   1 
ATOM   902  O  O   . ASP A 1 118 ? 26.917 32.790  1.459   1.00 18.31  ? 113 ASP B O   1 
ATOM   903  C  CB  . ASP A 1 118 ? 26.785 34.089  -1.538  1.00 18.60  ? 113 ASP B CB  1 
ATOM   904  C  CG  . ASP A 1 118 ? 27.337 34.956  -2.636  1.00 22.50  ? 113 ASP B CG  1 
ATOM   905  O  OD1 . ASP A 1 118 ? 28.035 35.946  -2.316  1.00 24.99  ? 113 ASP B OD1 1 
ATOM   906  O  OD2 . ASP A 1 118 ? 27.093 34.633  -3.824  1.00 20.91  ? 113 ASP B OD2 1 
ATOM   907  N  N   . ALA A 1 119 ? 25.277 34.318  1.256   1.00 20.40  ? 114 ALA B N   1 
ATOM   908  C  CA  . ALA A 1 119 ? 24.477 33.694  2.288   1.00 23.29  ? 114 ALA B CA  1 
ATOM   909  C  C   . ALA A 1 119 ? 24.137 32.229  2.011   1.00 18.90  ? 114 ALA B C   1 
ATOM   910  O  O   . ALA A 1 119 ? 24.267 31.400  2.913   1.00 19.43  ? 114 ALA B O   1 
ATOM   911  C  CB  . ALA A 1 119 ? 23.209 34.496  2.484   1.00 22.46  ? 114 ALA B CB  1 
ATOM   912  N  N   . GLU A 1 120 ? 23.738 31.885  0.777   1.00 17.64  ? 115 GLU B N   1 
ATOM   913  C  CA  . GLU A 1 120 ? 23.299 30.529  0.486   1.00 20.36  ? 115 GLU B CA  1 
ATOM   914  C  C   . GLU A 1 120 ? 24.450 29.532  0.680   1.00 18.65  ? 115 GLU B C   1 
ATOM   915  O  O   . GLU A 1 120 ? 24.285 28.478  1.306   1.00 19.88  ? 115 GLU B O   1 
ATOM   916  C  CB  . GLU A 1 120 ? 22.698 30.418  -0.942  1.00 26.66  ? 115 GLU B CB  1 
ATOM   917  C  CG  . GLU A 1 120 ? 21.453 29.568  -0.941  1.00 49.40  ? 115 GLU B CG  1 
ATOM   918  C  CD  . GLU A 1 120 ? 20.358 29.855  -1.950  1.00 49.58  ? 115 GLU B CD  1 
ATOM   919  O  OE1 . GLU A 1 120 ? 20.601 29.615  -3.151  1.00 45.97  ? 115 GLU B OE1 1 
ATOM   920  O  OE2 . GLU A 1 120 ? 19.242 30.259  -1.536  1.00 48.36  ? 115 GLU B OE2 1 
ATOM   921  N  N   . SER A 1 121 ? 25.649 29.898  0.215   1.00 15.81  ? 116 SER B N   1 
ATOM   922  C  CA  . SER A 1 121 ? 26.787 29.019  0.386   1.00 14.89  ? 116 SER B CA  1 
ATOM   923  C  C   . SER A 1 121 ? 27.263 28.927  1.831   1.00 15.58  ? 116 SER B C   1 
ATOM   924  O  O   . SER A 1 121 ? 27.486 27.833  2.357   1.00 15.63  ? 116 SER B O   1 
ATOM   925  C  CB  . SER A 1 121 ? 27.950 29.394  -0.509  1.00 17.65  ? 116 SER B CB  1 
ATOM   926  O  OG  . SER A 1 121 ? 28.397 30.719  -0.305  1.00 19.70  ? 116 SER B OG  1 
ATOM   927  N  N   . ARG A 1 122 ? 27.398 30.085  2.490   1.00 14.61  ? 117 ARG B N   1 
ATOM   928  C  CA  . ARG A 1 122 ? 27.935 30.088  3.838   1.00 15.36  ? 117 ARG B CA  1 
ATOM   929  C  C   . ARG A 1 122 ? 27.009 29.379  4.821   1.00 16.26  ? 117 ARG B C   1 
ATOM   930  O  O   . ARG A 1 122 ? 27.448 28.563  5.632   1.00 14.86  ? 117 ARG B O   1 
ATOM   931  C  CB  . ARG A 1 122 ? 28.222 31.476  4.296   1.00 18.28  ? 117 ARG B CB  1 
ATOM   932  C  CG  . ARG A 1 122 ? 28.991 31.474  5.541   1.00 21.70  ? 117 ARG B CG  1 
ATOM   933  C  CD  . ARG A 1 122 ? 29.601 32.839  5.762   1.00 22.62  ? 117 ARG B CD  1 
ATOM   934  N  NE  . ARG A 1 122 ? 30.559 32.785  6.848   1.00 22.61  ? 117 ARG B NE  1 
ATOM   935  C  CZ  . ARG A 1 122 ? 31.794 32.299  6.754   1.00 29.33  ? 117 ARG B CZ  1 
ATOM   936  N  NH1 . ARG A 1 122 ? 32.344 32.006  5.583   1.00 26.42  ? 117 ARG B NH1 1 
ATOM   937  N  NH2 . ARG A 1 122 ? 32.501 32.131  7.867   1.00 28.60  ? 117 ARG B NH2 1 
ATOM   938  N  N   . VAL A 1 123 ? 25.704 29.664  4.730   1.00 13.69  ? 118 VAL B N   1 
ATOM   939  C  CA  . VAL A 1 123 ? 24.742 28.984  5.582   1.00 13.68  ? 118 VAL B CA  1 
ATOM   940  C  C   . VAL A 1 123 ? 24.712 27.484  5.291   1.00 12.59  ? 118 VAL B C   1 
ATOM   941  O  O   . VAL A 1 123 ? 24.677 26.684  6.224   1.00 12.99  ? 118 VAL B O   1 
ATOM   942  C  CB  . VAL A 1 123 ? 23.332 29.609  5.461   1.00 14.74  ? 118 VAL B CB  1 
ATOM   943  C  CG1 . VAL A 1 123 ? 22.313 28.791  6.194   1.00 16.12  ? 118 VAL B CG1 1 
ATOM   944  C  CG2 . VAL A 1 123 ? 23.332 31.049  5.957   1.00 18.08  ? 118 VAL B CG2 1 
ATOM   945  N  N   . PHE A 1 124 ? 24.710 27.094  4.012   1.00 13.51  ? 119 PHE B N   1 
ATOM   946  C  CA  . PHE A 1 124 ? 24.726 25.673  3.686   1.00 12.93  ? 119 PHE B CA  1 
ATOM   947  C  C   . PHE A 1 124 ? 25.929 24.970  4.329   1.00 11.14  ? 119 PHE B C   1 
ATOM   948  O  O   . PHE A 1 124 ? 25.785 23.912  4.944   1.00 12.80  ? 119 PHE B O   1 
ATOM   949  C  CB  . PHE A 1 124 ? 24.737 25.458  2.165   1.00 13.55  ? 119 PHE B CB  1 
ATOM   950  C  CG  . PHE A 1 124 ? 25.033 24.016  1.835   1.00 15.69  ? 119 PHE B CG  1 
ATOM   951  C  CD1 . PHE A 1 124 ? 24.047 23.048  1.939   1.00 17.41  ? 119 PHE B CD1 1 
ATOM   952  C  CD2 . PHE A 1 124 ? 26.327 23.610  1.550   1.00 17.12  ? 119 PHE B CD2 1 
ATOM   953  C  CE1 . PHE A 1 124 ? 24.338 21.711  1.684   1.00 20.45  ? 119 PHE B CE1 1 
ATOM   954  C  CE2 . PHE A 1 124 ? 26.615 22.261  1.282   1.00 17.63  ? 119 PHE B CE2 1 
ATOM   955  C  CZ  . PHE A 1 124 ? 25.614 21.336  1.330   1.00 19.48  ? 119 PHE B CZ  1 
ATOM   956  N  N   . TYR A 1 125 ? 27.121 25.563  4.200   1.00 12.13  ? 120 TYR B N   1 
ATOM   957  C  CA  . TYR A 1 125 ? 28.318 24.910  4.707   1.00 12.02  ? 120 TYR B CA  1 
ATOM   958  C  C   . TYR A 1 125 ? 28.363 24.877  6.225   1.00 12.62  ? 120 TYR B C   1 
ATOM   959  O  O   . TYR A 1 125 ? 28.812 23.888  6.810   1.00 13.18  ? 120 TYR B O   1 
ATOM   960  C  CB  . TYR A 1 125 ? 29.598 25.511  4.177   1.00 12.00  ? 120 TYR B CB  1 
ATOM   961  C  CG  . TYR A 1 125 ? 29.856 25.335  2.690   1.00 12.09  ? 120 TYR B CG  1 
ATOM   962  C  CD1 . TYR A 1 125 ? 29.731 24.093  2.080   1.00 12.88  ? 120 TYR B CD1 1 
ATOM   963  C  CD2 . TYR A 1 125 ? 30.182 26.413  1.896   1.00 12.25  ? 120 TYR B CD2 1 
ATOM   964  C  CE1 . TYR A 1 125 ? 29.942 23.941  0.706   1.00 11.94  ? 120 TYR B CE1 1 
ATOM   965  C  CE2 . TYR A 1 125 ? 30.422 26.267  0.534   1.00 13.24  ? 120 TYR B CE2 1 
ATOM   966  C  CZ  . TYR A 1 125 ? 30.292 25.030  -0.058  1.00 14.20  ? 120 TYR B CZ  1 
ATOM   967  O  OH  . TYR A 1 125 ? 30.516 24.889  -1.421  1.00 16.00  ? 120 TYR B OH  1 
ATOM   968  N  N   . LEU A 1 126 ? 27.916 25.960  6.877   1.00 12.24  ? 121 LEU B N   1 
ATOM   969  C  CA  . LEU A 1 126 ? 27.875 25.943  8.329   1.00 13.71  ? 121 LEU B CA  1 
ATOM   970  C  C   . LEU A 1 126 ? 26.819 24.986  8.884   1.00 13.52  ? 121 LEU B C   1 
ATOM   971  O  O   . LEU A 1 126 ? 27.069 24.322  9.904   1.00 13.78  ? 121 LEU B O   1 
ATOM   972  C  CB  . LEU A 1 126 ? 27.667 27.334  8.916   1.00 14.27  ? 121 LEU B CB  1 
ATOM   973  C  CG  . LEU A 1 126 ? 28.809 28.278  8.717   1.00 15.36  ? 121 LEU B CG  1 
ATOM   974  C  CD1 . LEU A 1 126 ? 28.318 29.717  8.937   1.00 16.25  ? 121 LEU B CD1 1 
ATOM   975  C  CD2 . LEU A 1 126 ? 29.946 27.921  9.624   1.00 16.51  ? 121 LEU B CD2 1 
ATOM   976  N  N   . LYS A 1 127 ? 25.660 24.879  8.213   1.00 12.10  ? 122 LYS B N   1 
ATOM   977  C  CA  . LYS A 1 127 ? 24.705 23.824  8.532   1.00 12.85  ? 122 LYS B CA  1 
ATOM   978  C  C   . LYS A 1 127 ? 25.350 22.441  8.438   1.00 12.14  ? 122 LYS B C   1 
ATOM   979  O  O   . LYS A 1 127 ? 25.155 21.598  9.305   1.00 12.29  ? 122 LYS B O   1 
ATOM   980  C  CB  . LYS A 1 127 ? 23.485 23.911  7.617   1.00 13.21  ? 122 LYS B CB  1 
ATOM   981  C  CG  . LYS A 1 127 ? 22.467 22.770  7.805   1.00 13.56  ? 122 LYS B CG  1 
ATOM   982  C  CD  . LYS A 1 127 ? 21.430 22.800  6.693   1.00 13.69  ? 122 LYS B CD  1 
ATOM   983  C  CE  . LYS A 1 127 ? 20.653 21.523  6.608   1.00 14.20  ? 122 LYS B CE  1 
ATOM   984  N  NZ  . LYS A 1 127 ? 21.591 20.375  6.212   1.00 15.49  ? 122 LYS B NZ  1 
ATOM   985  N  N   . MET A 1 128 ? 26.097 22.211  7.350   1.00 12.44  ? 123 MET B N   1 
ATOM   986  C  CA  . MET A 1 128 ? 26.740 20.917  7.139   1.00 13.21  ? 123 MET B CA  1 
ATOM   987  C  C   . MET A 1 128 ? 27.729 20.633  8.274   1.00 11.81  ? 123 MET B C   1 
ATOM   988  O  O   . MET A 1 128 ? 27.783 19.503  8.766   1.00 11.73  ? 123 MET B O   1 
ATOM   989  C  CB  . MET A 1 128 ? 27.412 20.864  5.781   1.00 14.01  ? 123 MET B CB  1 
ATOM   990  C  CG  . MET A 1 128 ? 27.793 19.498  5.400   1.00 14.54  ? 123 MET B CG  1 
ATOM   991  S  SD  . MET A 1 128 ? 28.392 19.478  3.678   1.00 19.89  ? 123 MET B SD  1 
ATOM   992  C  CE  . MET A 1 128 ? 28.232 17.726  3.302   1.00 19.78  ? 123 MET B CE  1 
ATOM   993  N  N   . LYS A 1 129 ? 28.510 21.661  8.664   1.00 11.02  ? 124 LYS B N   1 
ATOM   994  C  CA  . LYS A 1 129 ? 29.451 21.511  9.761   1.00 11.63  ? 124 LYS B CA  1 
ATOM   995  C  C   . LYS A 1 129 ? 28.700 21.087  11.035  1.00 12.30  ? 124 LYS B C   1 
ATOM   996  O  O   . LYS A 1 129 ? 29.084 20.157  11.743  1.00 13.31  ? 124 LYS B O   1 
ATOM   997  C  CB  . LYS A 1 129 ? 30.246 22.815  9.941   1.00 13.56  ? 124 LYS B CB  1 
ATOM   998  C  CG  . LYS A 1 129 ? 31.275 22.753  11.051  1.00 13.62  ? 124 LYS B CG  1 
ATOM   999  C  CD  . LYS A 1 129 ? 32.102 23.995  11.078  1.00 17.02  ? 124 LYS B CD  1 
ATOM   1000 C  CE  . LYS A 1 129 ? 33.171 23.958  12.132  1.00 22.81  ? 124 LYS B CE  1 
ATOM   1001 N  NZ  . LYS A 1 129 ? 34.144 25.088  11.959  1.00 25.99  ? 124 LYS B NZ  1 
ATOM   1002 N  N   . GLY A 1 130 ? 27.593 21.774  11.352  1.00 11.90  ? 125 GLY B N   1 
ATOM   1003 C  CA  . GLY A 1 130 ? 26.759 21.386  12.486  1.00 12.82  ? 125 GLY B CA  1 
ATOM   1004 C  C   . GLY A 1 130 ? 26.252 19.947  12.414  1.00 12.29  ? 125 GLY B C   1 
ATOM   1005 O  O   . GLY A 1 130 ? 26.277 19.195  13.385  1.00 11.68  ? 125 GLY B O   1 
ATOM   1006 N  N   . ASP A 1 131 ? 25.809 19.548  11.228  1.00 11.86  ? 126 ASP B N   1 
ATOM   1007 C  CA  . ASP A 1 131 ? 25.255 18.226  11.011  1.00 11.73  ? 126 ASP B CA  1 
ATOM   1008 C  C   . ASP A 1 131 ? 26.296 17.137  11.265  1.00 12.01  ? 126 ASP B C   1 
ATOM   1009 O  O   . ASP A 1 131 ? 26.009 16.154  11.941  1.00 12.48  ? 126 ASP B O   1 
ATOM   1010 C  CB  . ASP A 1 131 ? 24.701 18.084  9.608   1.00 12.28  ? 126 ASP B CB  1 
ATOM   1011 C  CG  . ASP A 1 131 ? 23.396 18.834  9.299   1.00 12.26  ? 126 ASP B CG  1 
ATOM   1012 O  OD1 . ASP A 1 131 ? 22.643 19.145  10.279  1.00 13.51  ? 126 ASP B OD1 1 
ATOM   1013 O  OD2 . ASP A 1 131 ? 23.139 19.072  8.099   1.00 13.79  ? 126 ASP B OD2 1 
ATOM   1014 N  N   . TYR A 1 132 ? 27.527 17.344  10.773  1.00 12.76  ? 127 TYR B N   1 
ATOM   1015 C  CA  . TYR A 1 132 ? 28.520 16.282  10.872  1.00 13.28  ? 127 TYR B CA  1 
ATOM   1016 C  C   . TYR A 1 132 ? 29.128 16.238  12.274  1.00 12.70  ? 127 TYR B C   1 
ATOM   1017 O  O   . TYR A 1 132 ? 29.466 15.153  12.756  1.00 13.99  ? 127 TYR B O   1 
ATOM   1018 C  CB  . TYR A 1 132 ? 29.548 16.330  9.692   1.00 13.22  ? 127 TYR B CB  1 
ATOM   1019 C  CG  . TYR A 1 132 ? 28.888 15.723  8.445   1.00 12.96  ? 127 TYR B CG  1 
ATOM   1020 C  CD1 . TYR A 1 132 ? 28.041 16.474  7.646   1.00 13.68  ? 127 TYR B CD1 1 
ATOM   1021 C  CD2 . TYR A 1 132 ? 29.039 14.372  8.133   1.00 13.66  ? 127 TYR B CD2 1 
ATOM   1022 C  CE1 . TYR A 1 132 ? 27.378 15.915  6.564   1.00 13.34  ? 127 TYR B CE1 1 
ATOM   1023 C  CE2 . TYR A 1 132 ? 28.357 13.793  7.064   1.00 13.90  ? 127 TYR B CE2 1 
ATOM   1024 C  CZ  . TYR A 1 132 ? 27.543 14.563  6.267   1.00 13.70  ? 127 TYR B CZ  1 
ATOM   1025 O  OH  . TYR A 1 132 ? 26.850 14.001  5.202   1.00 15.26  ? 127 TYR B OH  1 
ATOM   1026 N  N   . TYR A 1 133 ? 29.204 17.375  12.980  1.00 13.03  ? 128 TYR B N   1 
ATOM   1027 C  CA  . TYR A 1 133 ? 29.487 17.303  14.414  1.00 13.00  ? 128 TYR B CA  1 
ATOM   1028 C  C   . TYR A 1 133 ? 28.355 16.617  15.185  1.00 13.02  ? 128 TYR B C   1 
ATOM   1029 O  O   . TYR A 1 133 ? 28.585 15.891  16.140  1.00 14.21  ? 128 TYR B O   1 
ATOM   1030 C  CB  . TYR A 1 133 ? 29.800 18.707  15.000  1.00 12.07  ? 128 TYR B CB  1 
ATOM   1031 C  CG  . TYR A 1 133 ? 31.242 19.125  14.826  1.00 13.96  ? 128 TYR B CG  1 
ATOM   1032 C  CD1 . TYR A 1 133 ? 32.256 18.468  15.497  1.00 15.09  ? 128 TYR B CD1 1 
ATOM   1033 C  CD2 . TYR A 1 133 ? 31.582 20.199  14.024  1.00 16.02  ? 128 TYR B CD2 1 
ATOM   1034 C  CE1 . TYR A 1 133 ? 33.577 18.841  15.342  1.00 16.45  ? 128 TYR B CE1 1 
ATOM   1035 C  CE2 . TYR A 1 133 ? 32.905 20.589  13.874  1.00 16.81  ? 128 TYR B CE2 1 
ATOM   1036 C  CZ  . TYR A 1 133 ? 33.898 19.887  14.519  1.00 17.20  ? 128 TYR B CZ  1 
ATOM   1037 O  OH  . TYR A 1 133 ? 35.223 20.236  14.414  1.00 21.68  ? 128 TYR B OH  1 
ATOM   1038 N  N   . ARG A 1 134 ? 27.104 16.842  14.767  1.00 12.68  ? 129 ARG B N   1 
ATOM   1039 C  CA  . ARG A 1 134 ? 25.982 16.181  15.405  1.00 12.90  ? 129 ARG B CA  1 
ATOM   1040 C  C   . ARG A 1 134 ? 26.083 14.656  15.248  1.00 12.42  ? 129 ARG B C   1 
ATOM   1041 O  O   . ARG A 1 134 ? 25.845 13.901  16.189  1.00 14.59  ? 129 ARG B O   1 
ATOM   1042 C  CB  . ARG A 1 134 ? 24.654 16.749  14.883  1.00 12.39  ? 129 ARG B CB  1 
ATOM   1043 C  CG  . ARG A 1 134 ? 23.437 15.941  15.311  1.00 13.22  ? 129 ARG B CG  1 
ATOM   1044 C  CD  . ARG A 1 134 ? 22.134 16.703  15.182  1.00 13.42  ? 129 ARG B CD  1 
ATOM   1045 N  NE  . ARG A 1 134 ? 21.840 17.093  13.809  1.00 12.70  ? 129 ARG B NE  1 
ATOM   1046 C  CZ  . ARG A 1 134 ? 21.237 16.339  12.906  1.00 13.66  ? 129 ARG B CZ  1 
ATOM   1047 N  NH1 . ARG A 1 134 ? 20.736 15.148  13.214  1.00 13.37  ? 129 ARG B NH1 1 
ATOM   1048 N  NH2 . ARG A 1 134 ? 21.113 16.794  11.662  1.00 13.29  ? 129 ARG B NH2 1 
ATOM   1049 N  N   . TYR A 1 135 ? 26.448 14.198  14.051  1.00 12.94  ? 130 TYR B N   1 
ATOM   1050 C  CA  . TYR A 1 135 ? 26.629 12.765  13.840  1.00 14.91  ? 130 TYR B CA  1 
ATOM   1051 C  C   . TYR A 1 135 ? 27.773 12.215  14.692  1.00 13.94  ? 130 TYR B C   1 
ATOM   1052 O  O   . TYR A 1 135 ? 27.672 11.099  15.219  1.00 14.45  ? 130 TYR B O   1 
ATOM   1053 C  CB  . TYR A 1 135 ? 26.807 12.437  12.330  1.00 12.83  ? 130 TYR B CB  1 
ATOM   1054 C  CG  . TYR A 1 135 ? 25.736 13.009  11.442  1.00 13.55  ? 130 TYR B CG  1 
ATOM   1055 C  CD1 . TYR A 1 135 ? 24.421 13.129  11.878  1.00 13.59  ? 130 TYR B CD1 1 
ATOM   1056 C  CD2 . TYR A 1 135 ? 26.013 13.378  10.152  1.00 12.91  ? 130 TYR B CD2 1 
ATOM   1057 C  CE1 . TYR A 1 135 ? 23.439 13.692  11.059  1.00 13.97  ? 130 TYR B CE1 1 
ATOM   1058 C  CE2 . TYR A 1 135 ? 25.043 13.920  9.325   1.00 15.64  ? 130 TYR B CE2 1 
ATOM   1059 C  CZ  . TYR A 1 135 ? 23.754 14.077  9.776   1.00 15.73  ? 130 TYR B CZ  1 
ATOM   1060 O  OH  . TYR A 1 135 ? 22.829 14.638  8.912   1.00 16.80  ? 130 TYR B OH  1 
ATOM   1061 N  N   . LEU A 1 136 ? 28.856 12.977  14.834  1.00 12.81  ? 131 LEU B N   1 
ATOM   1062 C  CA  . LEU A 1 136 ? 29.916 12.597  15.773  1.00 14.07  ? 131 LEU B CA  1 
ATOM   1063 C  C   . LEU A 1 136 ? 29.393 12.527  17.207  1.00 15.37  ? 131 LEU B C   1 
ATOM   1064 O  O   . LEU A 1 136 ? 29.760 11.630  17.965  1.00 15.10  ? 131 LEU B O   1 
ATOM   1065 C  CB  . LEU A 1 136 ? 31.108 13.549  15.729  1.00 15.80  ? 131 LEU B CB  1 
ATOM   1066 C  CG  . LEU A 1 136 ? 31.964 13.487  14.452  1.00 14.93  ? 131 LEU B CG  1 
ATOM   1067 C  CD1 . LEU A 1 136 ? 33.054 14.553  14.454  1.00 17.37  ? 131 LEU B CD1 1 
ATOM   1068 C  CD2 . LEU A 1 136 ? 32.550 12.091  14.257  1.00 15.42  ? 131 LEU B CD2 1 
ATOM   1069 N  N   . ALA A 1 137 ? 28.522 13.466  17.580  1.00 14.48  ? 132 ALA B N   1 
ATOM   1070 C  CA  . ALA A 1 137 ? 27.980 13.491  18.934  1.00 15.12  ? 132 ALA B CA  1 
ATOM   1071 C  C   . ALA A 1 137 ? 27.097 12.279  19.229  1.00 16.97  ? 132 ALA B C   1 
ATOM   1072 O  O   . ALA A 1 137 ? 27.027 11.846  20.376  1.00 18.31  ? 132 ALA B O   1 
ATOM   1073 C  CB  . ALA A 1 137 ? 27.194 14.772  19.168  1.00 15.61  ? 132 ALA B CB  1 
ATOM   1074 N  N   . GLU A 1 138 ? 26.387 11.760  18.216  1.00 15.09  ? 133 GLU B N   1 
ATOM   1075 C  CA  . GLU A 1 138 ? 25.512 10.609  18.382  1.00 16.30  ? 133 GLU B CA  1 
ATOM   1076 C  C   . GLU A 1 138 ? 26.254 9.380   18.920  1.00 16.88  ? 133 GLU B C   1 
ATOM   1077 O  O   . GLU A 1 138 ? 25.657 8.543   19.601  1.00 18.74  ? 133 GLU B O   1 
ATOM   1078 C  CB  . GLU A 1 138 ? 24.824 10.276  17.043  1.00 16.48  ? 133 GLU B CB  1 
ATOM   1079 C  CG  . GLU A 1 138 ? 23.745 11.237  16.574  1.00 18.25  ? 133 GLU B CG  1 
ATOM   1080 C  CD  . GLU A 1 138 ? 23.104 10.886  15.235  1.00 20.01  ? 133 GLU B CD  1 
ATOM   1081 O  OE1 . GLU A 1 138 ? 23.666 10.099  14.429  1.00 19.07  ? 133 GLU B OE1 1 
ATOM   1082 O  OE2 . GLU A 1 138 ? 21.975 11.365  15.016  1.00 20.97  ? 133 GLU B OE2 1 
ATOM   1083 N  N   . VAL A 1 139 ? 27.543 9.259   18.590  1.00 16.38  ? 134 VAL B N   1 
ATOM   1084 C  CA  . VAL A 1 139 ? 28.347 8.107   18.985  1.00 17.84  ? 134 VAL B CA  1 
ATOM   1085 C  C   . VAL A 1 139 ? 29.392 8.428   20.049  1.00 19.49  ? 134 VAL B C   1 
ATOM   1086 O  O   . VAL A 1 139 ? 30.117 7.538   20.493  1.00 22.29  ? 134 VAL B O   1 
ATOM   1087 C  CB  . VAL A 1 139 ? 29.022 7.436   17.753  1.00 17.67  ? 134 VAL B CB  1 
ATOM   1088 C  CG1 . VAL A 1 139 ? 27.974 7.068   16.755  1.00 17.27  ? 134 VAL B CG1 1 
ATOM   1089 C  CG2 . VAL A 1 139 ? 30.118 8.291   17.122  1.00 17.69  ? 134 VAL B CG2 1 
ATOM   1090 N  N   . ALA A 1 140 ? 29.461 9.690   20.487  1.00 17.69  ? 135 ALA B N   1 
ATOM   1091 C  CA  . ALA A 1 140 ? 30.495 10.116  21.419  1.00 20.76  ? 135 ALA B CA  1 
ATOM   1092 C  C   . ALA A 1 140 ? 30.099 9.759   22.849  1.00 23.29  ? 135 ALA B C   1 
ATOM   1093 O  O   . ALA A 1 140 ? 28.911 9.775   23.190  1.00 24.60  ? 135 ALA B O   1 
ATOM   1094 C  CB  . ALA A 1 140 ? 30.748 11.616  21.309  1.00 20.38  ? 135 ALA B CB  1 
ATOM   1095 N  N   . THR A 1 141 ? 31.085 9.350   23.643  1.00 28.08  ? 136 THR B N   1 
ATOM   1096 C  CA  . THR A 1 141 ? 30.774 8.872   25.015  1.00 41.79  ? 136 THR B CA  1 
ATOM   1097 C  C   . THR A 1 141 ? 31.896 9.240   25.966  1.00 55.85  ? 136 THR B C   1 
ATOM   1098 O  O   . THR A 1 141 ? 31.723 9.033   27.174  1.00 57.94  ? 136 THR B O   1 
ATOM   1099 C  CB  . THR A 1 141 ? 30.660 7.345   25.092  1.00 43.43  ? 136 THR B CB  1 
ATOM   1100 O  OG1 . THR A 1 141 ? 31.912 6.799   24.676  1.00 43.55  ? 136 THR B OG1 1 
ATOM   1101 C  CG2 . THR A 1 141 ? 29.540 6.774   24.251  1.00 39.07  ? 136 THR B CG2 1 
ATOM   1102 N  N   . GLY A 1 142 ? 32.981 9.794   25.448  1.00 74.50  ? 137 GLY B N   1 
ATOM   1103 C  CA  . GLY A 1 142 ? 34.138 10.044  26.322  1.00 72.71  ? 137 GLY B CA  1 
ATOM   1104 C  C   . GLY A 1 142 ? 34.334 11.497  26.709  1.00 70.80  ? 137 GLY B C   1 
ATOM   1105 O  O   . GLY A 1 142 ? 33.343 12.238  26.794  1.00 79.61  ? 137 GLY B O   1 
ATOM   1106 N  N   . ASP A 1 143 ? 35.587 11.877  26.925  1.00 65.24  ? 138 ASP B N   1 
ATOM   1107 C  CA  . ASP A 1 143 ? 35.880 13.251  27.401  1.00 68.60  ? 138 ASP B CA  1 
ATOM   1108 C  C   . ASP A 1 143 ? 35.695 14.299  26.293  1.00 59.36  ? 138 ASP B C   1 
ATOM   1109 O  O   . ASP A 1 143 ? 35.961 15.468  26.590  1.00 46.07  ? 138 ASP B O   1 
ATOM   1110 C  CB  . ASP A 1 143 ? 37.290 13.314  27.996  1.00 77.23  ? 138 ASP B CB  1 
ATOM   1111 C  CG  . ASP A 1 143 ? 37.358 14.044  29.332  1.00 84.13  ? 138 ASP B CG  1 
ATOM   1112 O  OD1 . ASP A 1 143 ? 36.408 14.799  29.649  1.00 74.84  ? 138 ASP B OD1 1 
ATOM   1113 O  OD2 . ASP A 1 143 ? 38.362 13.855  30.047  1.00 91.31  ? 138 ASP B OD2 1 
ATOM   1114 N  N   . ASP A 1 144 ? 35.304 13.911  25.076  1.00 49.38  ? 139 ASP B N   1 
ATOM   1115 C  CA  . ASP A 1 144 ? 35.129 14.960  24.086  1.00 52.19  ? 139 ASP B CA  1 
ATOM   1116 C  C   . ASP A 1 144 ? 33.678 15.127  23.643  1.00 39.23  ? 139 ASP B C   1 
ATOM   1117 O  O   . ASP A 1 144 ? 33.419 15.945  22.780  1.00 32.65  ? 139 ASP B O   1 
ATOM   1118 C  CB  . ASP A 1 144 ? 36.033 14.717  22.846  1.00 57.56  ? 139 ASP B CB  1 
ATOM   1119 C  CG  . ASP A 1 144 ? 37.463 15.201  23.009  1.00 62.71  ? 139 ASP B CG  1 
ATOM   1120 O  OD1 . ASP A 1 144 ? 37.663 16.424  23.198  1.00 57.15  ? 139 ASP B OD1 1 
ATOM   1121 O  OD2 . ASP A 1 144 ? 38.380 14.362  22.952  1.00 64.73  ? 139 ASP B OD2 1 
ATOM   1122 N  N   . LYS A 1 145 ? 32.748 14.365  24.223  1.00 30.97  ? 140 LYS B N   1 
ATOM   1123 C  CA  . LYS A 1 145 ? 31.336 14.505  23.915  1.00 31.14  ? 140 LYS B CA  1 
ATOM   1124 C  C   . LYS A 1 145 ? 30.866 15.951  24.103  1.00 26.49  ? 140 LYS B C   1 
ATOM   1125 O  O   . LYS A 1 145 ? 30.199 16.507  23.229  1.00 23.53  ? 140 LYS B O   1 
ATOM   1126 C  CB  . LYS A 1 145 ? 30.545 13.544  24.766  1.00 31.97  ? 140 LYS B CB  1 
ATOM   1127 C  CG  . LYS A 1 145 ? 29.056 13.657  24.644  1.00 38.95  ? 140 LYS B CG  1 
ATOM   1128 C  CD  . LYS A 1 145 ? 28.469 13.156  23.365  1.00 46.63  ? 140 LYS B CD  1 
ATOM   1129 C  CE  . LYS A 1 145 ? 26.958 13.061  23.432  1.00 49.98  ? 140 LYS B CE  1 
ATOM   1130 N  NZ  . LYS A 1 145 ? 26.476 12.366  24.658  1.00 52.60  ? 140 LYS B NZ  1 
ATOM   1131 N  N   . LYS A 1 146 ? 31.272 16.593  25.203  1.00 26.11  ? 141 LYS B N   1 
ATOM   1132 C  CA  . LYS A 1 146 ? 30.862 17.971  25.430  1.00 24.12  ? 141 LYS B CA  1 
ATOM   1133 C  C   . LYS A 1 146 ? 31.423 18.926  24.388  1.00 22.31  ? 141 LYS B C   1 
ATOM   1134 O  O   . LYS A 1 146 ? 30.730 19.842  23.953  1.00 20.34  ? 141 LYS B O   1 
ATOM   1135 C  CB  . LYS A 1 146 ? 31.232 18.440  26.853  1.00 27.12  ? 141 LYS B CB  1 
ATOM   1136 C  CG  . LYS A 1 146 ? 30.326 17.835  27.863  1.00 33.29  ? 141 LYS B CG  1 
ATOM   1137 C  CD  . LYS A 1 146 ? 30.716 18.233  29.309  1.00 42.15  ? 141 LYS B CD  1 
ATOM   1138 C  CE  . LYS A 1 146 ? 29.923 17.491  30.356  1.00 50.43  ? 141 LYS B CE  1 
ATOM   1139 N  NZ  . LYS A 1 146 ? 30.121 18.114  31.696  1.00 61.28  ? 141 LYS B NZ  1 
ATOM   1140 N  N   . ARG A 1 147 ? 32.698 18.751  24.016  1.00 22.33  ? 142 ARG B N   1 
ATOM   1141 C  CA  . ARG A 1 147 ? 33.319 19.660  23.075  1.00 22.40  ? 142 ARG B CA  1 
ATOM   1142 C  C   . ARG A 1 147 ? 32.707 19.418  21.693  1.00 16.54  ? 142 ARG B C   1 
ATOM   1143 O  O   . ARG A 1 147 ? 32.495 20.378  20.967  1.00 17.97  ? 142 ARG B O   1 
ATOM   1144 C  CB  . ARG A 1 147 ? 34.882 19.592  23.057  1.00 26.53  ? 142 ARG B CB  1 
ATOM   1145 C  CG  . ARG A 1 147 ? 35.545 20.602  24.069  1.00 31.36  ? 142 ARG B CG  1 
ATOM   1146 C  CD  . ARG A 1 147 ? 37.066 20.550  23.999  1.00 39.20  ? 142 ARG B CD  1 
ATOM   1147 N  NE  . ARG A 1 147 ? 37.616 19.499  24.850  1.00 39.04  ? 142 ARG B NE  1 
ATOM   1148 C  CZ  . ARG A 1 147 ? 37.826 19.634  26.156  1.00 41.11  ? 142 ARG B CZ  1 
ATOM   1149 N  NH1 . ARG A 1 147 ? 37.775 20.821  26.749  1.00 28.59  ? 142 ARG B NH1 1 
ATOM   1150 N  NH2 . ARG A 1 147 ? 38.104 18.556  26.883  1.00 43.13  ? 142 ARG B NH2 1 
ATOM   1151 N  N   . ILE A 1 148 ? 32.375 18.164  21.353  1.00 17.82  ? 143 ILE B N   1 
ATOM   1152 C  CA  . ILE A 1 148 ? 31.736 17.894  20.069  1.00 16.93  ? 143 ILE B CA  1 
ATOM   1153 C  C   . ILE A 1 148 ? 30.365 18.574  19.986  1.00 15.29  ? 143 ILE B C   1 
ATOM   1154 O  O   . ILE A 1 148 ? 30.041 19.209  18.973  1.00 15.54  ? 143 ILE B O   1 
ATOM   1155 C  CB  . ILE A 1 148 ? 31.654 16.388  19.792  1.00 19.29  ? 143 ILE B CB  1 
ATOM   1156 C  CG1 . ILE A 1 148 ? 33.070 15.773  19.625  1.00 24.47  ? 143 ILE B CG1 1 
ATOM   1157 C  CG2 . ILE A 1 148 ? 30.768 16.131  18.595  1.00 19.59  ? 143 ILE B CG2 1 
ATOM   1158 C  CD1 . ILE A 1 148 ? 33.051 14.278  19.667  1.00 27.83  ? 143 ILE B CD1 1 
ATOM   1159 N  N   . ILE A 1 149 ? 29.576 18.457  21.061  1.00 16.12  ? 144 ILE B N   1 
ATOM   1160 C  CA  . ILE A 1 149 ? 28.266 19.088  21.119  1.00 15.89  ? 144 ILE B CA  1 
ATOM   1161 C  C   . ILE A 1 149 ? 28.406 20.597  20.998  1.00 15.87  ? 144 ILE B C   1 
ATOM   1162 O  O   . ILE A 1 149 ? 27.676 21.254  20.251  1.00 16.36  ? 144 ILE B O   1 
ATOM   1163 C  CB  . ILE A 1 149 ? 27.549 18.662  22.394  1.00 16.78  ? 144 ILE B CB  1 
ATOM   1164 C  CG1 . ILE A 1 149 ? 27.138 17.192  22.291  1.00 21.15  ? 144 ILE B CG1 1 
ATOM   1165 C  CG2 . ILE A 1 149 ? 26.370 19.562  22.689  1.00 16.68  ? 144 ILE B CG2 1 
ATOM   1166 C  CD1 . ILE A 1 149 ? 26.495 16.590  23.611  1.00 22.79  ? 144 ILE B CD1 1 
ATOM   1167 N  N   . ASP A 1 150 ? 29.400 21.186  21.667  1.00 14.83  ? 145 ASP B N   1 
ATOM   1168 C  CA  . ASP A 1 150 ? 29.567 22.616  21.541  1.00 16.79  ? 145 ASP B CA  1 
ATOM   1169 C  C   . ASP A 1 150 ? 29.986 23.053  20.134  1.00 16.58  ? 145 ASP B C   1 
ATOM   1170 O  O   . ASP A 1 150 ? 29.601 24.125  19.676  1.00 16.54  ? 145 ASP B O   1 
ATOM   1171 C  CB  . ASP A 1 150 ? 30.524 23.201  22.573  1.00 20.48  ? 145 ASP B CB  1 
ATOM   1172 C  CG  . ASP A 1 150 ? 30.221 24.705  22.822  1.00 29.57  ? 145 ASP B CG  1 
ATOM   1173 O  OD1 . ASP A 1 150 ? 29.014 25.057  23.128  1.00 36.03  ? 145 ASP B OD1 1 
ATOM   1174 O  OD2 . ASP A 1 150 ? 31.138 25.518  22.688  1.00 35.80  ? 145 ASP B OD2 1 
ATOM   1175 N  N   . SER A 1 151 ? 30.819 22.239  19.459  1.00 16.01  ? 146 SER B N   1 
ATOM   1176 C  CA  . SER A 1 151 ? 31.179 22.543  18.086  1.00 14.63  ? 146 SER B CA  1 
ATOM   1177 C  C   . SER A 1 151 ? 29.958 22.517  17.158  1.00 13.54  ? 146 SER B C   1 
ATOM   1178 O  O   . SER A 1 151 ? 29.846 23.373  16.282  1.00 14.68  ? 146 SER B O   1 
ATOM   1179 C  CB  . SER A 1 151 ? 32.220 21.546  17.603  1.00 18.37  ? 146 SER B CB  1 
ATOM   1180 O  OG  . SER A 1 151 ? 33.461 21.790  18.263  1.00 21.35  ? 146 SER B OG  1 
ATOM   1181 N  N   . ALA A 1 152 ? 29.100 21.507  17.328  1.00 14.22  ? 147 ALA B N   1 
ATOM   1182 C  CA  . ALA A 1 152 ? 27.858 21.475  16.552  1.00 14.39  ? 147 ALA B CA  1 
ATOM   1183 C  C   . ALA A 1 152 ? 27.036 22.753  16.794  1.00 14.10  ? 147 ALA B C   1 
ATOM   1184 O  O   . ALA A 1 152 ? 26.567 23.421  15.868  1.00 13.63  ? 147 ALA B O   1 
ATOM   1185 C  CB  . ALA A 1 152 ? 27.055 20.234  16.882  1.00 13.34  ? 147 ALA B CB  1 
ATOM   1186 N  N   . ARG A 1 153 ? 26.806 23.044  18.073  1.00 13.81  ? 148 ARG B N   1 
ATOM   1187 C  CA  A ARG A 1 153 ? 26.011 24.188  18.483  0.50 14.18  ? 148 ARG B CA  1 
ATOM   1188 C  CA  B ARG A 1 153 ? 26.002 24.185  18.473  0.50 13.51  ? 148 ARG B CA  1 
ATOM   1189 C  C   . ARG A 1 153 ? 26.537 25.483  17.873  1.00 13.40  ? 148 ARG B C   1 
ATOM   1190 O  O   . ARG A 1 153 ? 25.792 26.293  17.339  1.00 14.83  ? 148 ARG B O   1 
ATOM   1191 C  CB  A ARG A 1 153 ? 26.036 24.351  20.021  0.50 15.77  ? 148 ARG B CB  1 
ATOM   1192 C  CB  B ARG A 1 153 ? 25.980 24.326  20.015  0.50 14.22  ? 148 ARG B CB  1 
ATOM   1193 C  CG  A ARG A 1 153 ? 25.218 25.550  20.498  0.50 17.92  ? 148 ARG B CG  1 
ATOM   1194 C  CG  B ARG A 1 153 ? 24.983 25.381  20.487  0.50 15.52  ? 148 ARG B CG  1 
ATOM   1195 C  CD  A ARG A 1 153 ? 25.612 26.003  21.881  0.50 19.79  ? 148 ARG B CD  1 
ATOM   1196 C  CD  B ARG A 1 153 ? 25.074 25.648  21.967  0.50 14.66  ? 148 ARG B CD  1 
ATOM   1197 N  NE  A ARG A 1 153 ? 26.996 26.460  21.918  0.50 21.32  ? 148 ARG B NE  1 
ATOM   1198 N  NE  B ARG A 1 153 ? 25.078 24.425  22.743  0.50 17.50  ? 148 ARG B NE  1 
ATOM   1199 C  CZ  A ARG A 1 153 ? 27.477 27.508  21.254  0.50 20.89  ? 148 ARG B CZ  1 
ATOM   1200 C  CZ  B ARG A 1 153 ? 23.995 23.839  23.204  0.50 16.07  ? 148 ARG B CZ  1 
ATOM   1201 N  NH1 A ARG A 1 153 ? 26.684 28.362  20.620  0.50 19.72  ? 148 ARG B NH1 1 
ATOM   1202 N  NH1 B ARG A 1 153 ? 22.798 24.386  23.038  0.50 14.01  ? 148 ARG B NH1 1 
ATOM   1203 N  NH2 A ARG A 1 153 ? 28.793 27.685  21.206  0.50 21.87  ? 148 ARG B NH2 1 
ATOM   1204 N  NH2 B ARG A 1 153 ? 24.116 22.673  23.844  0.50 17.83  ? 148 ARG B NH2 1 
ATOM   1205 N  N   . SER A 1 154 ? 27.851 25.676  17.952  1.00 14.67  ? 149 SER B N   1 
ATOM   1206 C  CA  . SER A 1 154 ? 28.487 26.882  17.458  1.00 15.46  ? 149 SER B CA  1 
ATOM   1207 C  C   . SER A 1 154 ? 28.329 27.065  15.946  1.00 15.44  ? 149 SER B C   1 
ATOM   1208 O  O   . SER A 1 154 ? 28.053 28.166  15.468  1.00 16.36  ? 149 SER B O   1 
ATOM   1209 C  CB  . SER A 1 154 ? 29.957 26.835  17.869  1.00 18.52  ? 149 SER B CB  1 
ATOM   1210 O  OG  . SER A 1 154 ? 30.627 27.997  17.440  1.00 26.72  ? 149 SER B OG  1 
ATOM   1211 N  N   . ALA A 1 155 ? 28.484 25.970  15.195  1.00 13.84  ? 150 ALA B N   1 
ATOM   1212 C  CA  . ALA A 1 155 ? 28.278 26.013  13.754  1.00 13.46  ? 150 ALA B CA  1 
ATOM   1213 C  C   . ALA A 1 155 ? 26.821 26.344  13.407  1.00 12.67  ? 150 ALA B C   1 
ATOM   1214 O  O   . ALA A 1 155 ? 26.570 27.222  12.570  1.00 13.45  ? 150 ALA B O   1 
ATOM   1215 C  CB  . ALA A 1 155 ? 28.737 24.701  13.101  1.00 14.87  ? 150 ALA B CB  1 
ATOM   1216 N  N   . TYR A 1 156 ? 25.877 25.649  14.053  1.00 13.73  ? 151 TYR B N   1 
ATOM   1217 C  CA  . TYR A 1 156 ? 24.459 25.909  13.814  1.00 12.73  ? 151 TYR B CA  1 
ATOM   1218 C  C   . TYR A 1 156 ? 24.092 27.348  14.167  1.00 14.53  ? 151 TYR B C   1 
ATOM   1219 O  O   . TYR A 1 156 ? 23.376 28.007  13.421  1.00 13.06  ? 151 TYR B O   1 
ATOM   1220 C  CB  . TYR A 1 156 ? 23.567 24.973  14.586  1.00 13.36  ? 151 TYR B CB  1 
ATOM   1221 C  CG  . TYR A 1 156 ? 23.472 23.544  14.085  1.00 12.40  ? 151 TYR B CG  1 
ATOM   1222 C  CD1 . TYR A 1 156 ? 23.203 23.268  12.757  1.00 13.05  ? 151 TYR B CD1 1 
ATOM   1223 C  CD2 . TYR A 1 156 ? 23.544 22.476  14.961  1.00 13.50  ? 151 TYR B CD2 1 
ATOM   1224 C  CE1 . TYR A 1 156 ? 23.025 21.967  12.315  1.00 12.77  ? 151 TYR B CE1 1 
ATOM   1225 C  CE2 . TYR A 1 156 ? 23.387 21.166  14.528  1.00 12.34  ? 151 TYR B CE2 1 
ATOM   1226 C  CZ  . TYR A 1 156 ? 23.079 20.910  13.208  1.00 11.95  ? 151 TYR B CZ  1 
ATOM   1227 O  OH  . TYR A 1 156 ? 22.905 19.593  12.780  1.00 13.54  ? 151 TYR B OH  1 
ATOM   1228 N  N   . GLN A 1 157 ? 24.633 27.854  15.278  1.00 13.51  ? 152 GLN B N   1 
ATOM   1229 C  CA  . GLN A 1 157 ? 24.317 29.209  15.720  1.00 14.54  ? 152 GLN B CA  1 
ATOM   1230 C  C   . GLN A 1 157 ? 24.807 30.242  14.714  1.00 14.94  ? 152 GLN B C   1 
ATOM   1231 O  O   . GLN A 1 157 ? 24.097 31.201  14.423  1.00 16.27  ? 152 GLN B O   1 
ATOM   1232 C  CB  . GLN A 1 157 ? 24.900 29.495  17.112  1.00 15.21  ? 152 GLN B CB  1 
ATOM   1233 C  CG  . GLN A 1 157 ? 24.404 30.841  17.685  1.00 20.01  ? 152 GLN B CG  1 
ATOM   1234 C  CD  . GLN A 1 157 ? 22.918 30.814  17.790  1.00 21.08  ? 152 GLN B CD  1 
ATOM   1235 O  OE1 . GLN A 1 157 ? 22.367 29.951  18.526  1.00 23.16  ? 152 GLN B OE1 1 
ATOM   1236 N  NE2 . GLN A 1 157 ? 22.197 31.714  17.081  1.00 24.29  ? 152 GLN B NE2 1 
ATOM   1237 N  N   . GLU A 1 158 ? 26.050 30.082  14.233  1.00 14.12  ? 153 GLU B N   1 
ATOM   1238 C  CA  . GLU A 1 158 ? 26.585 31.019  13.249  1.00 15.52  ? 153 GLU B CA  1 
ATOM   1239 C  C   . GLU A 1 158 ? 25.731 30.996  11.981  1.00 16.76  ? 153 GLU B C   1 
ATOM   1240 O  O   . GLU A 1 158 ? 25.398 32.041  11.419  1.00 16.78  ? 153 GLU B O   1 
ATOM   1241 C  CB  . GLU A 1 158 ? 28.064 30.724  12.921  1.00 19.01  ? 153 GLU B CB  1 
ATOM   1242 C  CG  . GLU A 1 158 ? 28.635 31.721  11.936  1.00 24.83  ? 153 GLU B CG  1 
ATOM   1243 C  CD  . GLU A 1 158 ? 30.111 31.643  11.571  1.00 38.36  ? 153 GLU B CD  1 
ATOM   1244 O  OE1 . GLU A 1 158 ? 30.871 30.871  12.200  1.00 33.66  ? 153 GLU B OE1 1 
ATOM   1245 O  OE2 . GLU A 1 158 ? 30.497 32.364  10.621  1.00 42.34  ? 153 GLU B OE2 1 
ATOM   1246 N  N   . ALA A 1 159 ? 25.369 29.793  11.537  1.00 13.82  ? 154 ALA B N   1 
ATOM   1247 C  CA  . ALA A 1 159 ? 24.498 29.646  10.384  1.00 13.80  ? 154 ALA B CA  1 
ATOM   1248 C  C   . ALA A 1 159 ? 23.151 30.330  10.606  1.00 14.55  ? 154 ALA B C   1 
ATOM   1249 O  O   . ALA A 1 159 ? 22.663 31.001  9.707   1.00 15.00  ? 154 ALA B O   1 
ATOM   1250 C  CB  . ALA A 1 159 ? 24.279 28.170  10.096  1.00 12.83  ? 154 ALA B CB  1 
ATOM   1251 N  N   . MET A 1 160 ? 22.576 30.156  11.799  1.00 15.03  ? 155 MET B N   1 
ATOM   1252 C  CA  . MET A 1 160 ? 21.278 30.741  12.134  1.00 14.60  ? 155 MET B CA  1 
ATOM   1253 C  C   . MET A 1 160 ? 21.386 32.258  12.084  1.00 15.06  ? 155 MET B C   1 
ATOM   1254 O  O   . MET A 1 160 ? 20.514 32.927  11.525  1.00 15.50  ? 155 MET B O   1 
ATOM   1255 C  CB  . MET A 1 160 ? 20.785 30.334  13.518  1.00 15.46  ? 155 MET B CB  1 
ATOM   1256 C  CG  . MET A 1 160 ? 20.351 28.889  13.626  1.00 17.95  ? 155 MET B CG  1 
ATOM   1257 S  SD  . MET A 1 160 ? 18.773 28.490  12.843  1.00 22.00  ? 155 MET B SD  1 
ATOM   1258 C  CE  . MET A 1 160 ? 17.731 29.721  13.544  1.00 25.24  ? 155 MET B CE  1 
ATOM   1259 N  N   . ASP A 1 161 ? 22.458 32.812  12.658  1.00 16.01  ? 156 ASP B N   1 
ATOM   1260 C  CA  . ASP A 1 161 ? 22.595 34.270  12.684  1.00 19.95  ? 156 ASP B CA  1 
ATOM   1261 C  C   . ASP A 1 161 ? 22.640 34.863  11.268  1.00 19.49  ? 156 ASP B C   1 
ATOM   1262 O  O   . ASP A 1 161 ? 21.963 35.849  10.966  1.00 19.75  ? 156 ASP B O   1 
ATOM   1263 C  CB  . ASP A 1 161 ? 23.830 34.667  13.481  1.00 21.37  ? 156 ASP B CB  1 
ATOM   1264 C  CG  . ASP A 1 161 ? 23.778 34.342  14.963  1.00 24.60  ? 156 ASP B CG  1 
ATOM   1265 O  OD1 . ASP A 1 161 ? 22.692 34.088  15.463  1.00 25.81  ? 156 ASP B OD1 1 
ATOM   1266 O  OD2 . ASP A 1 161 ? 24.857 34.328  15.612  1.00 26.90  ? 156 ASP B OD2 1 
ATOM   1267 N  N   . ILE A 1 162 ? 23.397 34.231  10.363  1.00 16.36  ? 157 ILE B N   1 
ATOM   1268 C  CA  . ILE A 1 162 ? 23.449 34.695  8.987   1.00 15.95  ? 157 ILE B CA  1 
ATOM   1269 C  C   . ILE A 1 162 ? 22.100 34.525  8.305   1.00 16.61  ? 157 ILE B C   1 
ATOM   1270 O  O   . ILE A 1 162 ? 21.657 35.429  7.595   1.00 17.54  ? 157 ILE B O   1 
ATOM   1271 C  CB  . ILE A 1 162 ? 24.580 33.975  8.194   1.00 15.80  ? 157 ILE B CB  1 
ATOM   1272 C  CG1 . ILE A 1 162 ? 25.932 34.258  8.815   1.00 18.25  ? 157 ILE B CG1 1 
ATOM   1273 C  CG2 . ILE A 1 162 ? 24.531 34.352  6.733   1.00 17.02  ? 157 ILE B CG2 1 
ATOM   1274 C  CD1 . ILE A 1 162 ? 27.046 33.286  8.394   1.00 19.70  ? 157 ILE B CD1 1 
ATOM   1275 N  N   . SER A 1 163 ? 21.453 33.361  8.487   1.00 15.02  ? 158 SER B N   1 
ATOM   1276 C  CA  . SER A 1 163 ? 20.215 33.079  7.775   1.00 14.71  ? 158 SER B CA  1 
ATOM   1277 C  C   . SER A 1 163 ? 19.113 34.078  8.145   1.00 18.50  ? 158 SER B C   1 
ATOM   1278 O  O   . SER A 1 163 ? 18.324 34.477  7.285   1.00 17.08  ? 158 SER B O   1 
ATOM   1279 C  CB  . SER A 1 163 ? 19.750 31.636  7.994   1.00 16.74  ? 158 SER B CB  1 
ATOM   1280 O  OG  . SER A 1 163 ? 19.211 31.411  9.272   1.00 19.51  ? 158 SER B OG  1 
ATOM   1281 N  N   . LYS A 1 164 ? 19.073 34.488  9.419   1.00 17.22  ? 159 LYS B N   1 
ATOM   1282 C  CA  . LYS A 1 164 ? 18.039 35.407  9.870   1.00 19.14  ? 159 LYS B CA  1 
ATOM   1283 C  C   . LYS A 1 164 ? 18.254 36.807  9.303   1.00 20.25  ? 159 LYS B C   1 
ATOM   1284 O  O   . LYS A 1 164 ? 17.299 37.538  9.072   1.00 24.13  ? 159 LYS B O   1 
ATOM   1285 C  CB  . LYS A 1 164 ? 17.987 35.414  11.401  1.00 23.30  ? 159 LYS B CB  1 
ATOM   1286 C  CG  . LYS A 1 164 ? 17.397 34.118  11.952  1.00 30.52  ? 159 LYS B CG  1 
ATOM   1287 C  CD  . LYS A 1 164 ? 17.239 34.164  13.494  1.00 33.21  ? 159 LYS B CD  1 
ATOM   1288 C  CE  . LYS A 1 164 ? 16.173 33.250  13.969  1.00 45.72  ? 159 LYS B CE  1 
ATOM   1289 N  NZ  . LYS A 1 164 ? 15.736 33.619  15.337  1.00 53.00  ? 159 LYS B NZ  1 
ATOM   1290 N  N   . LYS A 1 165 ? 19.505 37.183  9.057   1.00 18.31  ? 160 LYS B N   1 
ATOM   1291 C  CA  . LYS A 1 165 ? 19.814 38.494  8.520   1.00 20.06  ? 160 LYS B CA  1 
ATOM   1292 C  C   . LYS A 1 165 ? 19.687 38.564  7.003   1.00 22.41  ? 160 LYS B C   1 
ATOM   1293 O  O   . LYS A 1 165 ? 19.331 39.608  6.462   1.00 25.20  ? 160 LYS B O   1 
ATOM   1294 C  CB  . LYS A 1 165 ? 21.230 38.895  8.901   1.00 23.95  ? 160 LYS B CB  1 
ATOM   1295 C  CG  . LYS A 1 165 ? 21.363 39.338  10.326  1.00 34.43  ? 160 LYS B CG  1 
ATOM   1296 C  CD  . LYS A 1 165 ? 22.737 39.868  10.635  1.00 45.63  ? 160 LYS B CD  1 
ATOM   1297 C  CE  . LYS A 1 165 ? 22.861 40.248  12.095  1.00 55.58  ? 160 LYS B CE  1 
ATOM   1298 N  NZ  . LYS A 1 165 ? 24.178 40.873  12.381  1.00 64.85  ? 160 LYS B NZ  1 
ATOM   1299 N  N   . GLU A 1 166 ? 19.985 37.452  6.314   1.00 19.04  ? 161 GLU B N   1 
ATOM   1300 C  CA  . GLU A 1 166 ? 20.220 37.485  4.882   1.00 17.63  ? 161 GLU B CA  1 
ATOM   1301 C  C   . GLU A 1 166 ? 19.224 36.725  4.011   1.00 19.69  ? 161 GLU B C   1 
ATOM   1302 O  O   . GLU A 1 166 ? 19.228 36.886  2.792   1.00 24.04  ? 161 GLU B O   1 
ATOM   1303 C  CB  . GLU A 1 166 ? 21.657 36.963  4.601   1.00 19.47  ? 161 GLU B CB  1 
ATOM   1304 C  CG  . GLU A 1 166 ? 22.748 37.772  5.275   1.00 24.10  ? 161 GLU B CG  1 
ATOM   1305 C  CD  . GLU A 1 166 ? 22.891 39.204  4.789   1.00 36.84  ? 161 GLU B CD  1 
ATOM   1306 O  OE1 . GLU A 1 166 ? 22.307 39.544  3.731   1.00 37.47  ? 161 GLU B OE1 1 
ATOM   1307 O  OE2 . GLU A 1 166 ? 23.565 39.992  5.493   1.00 43.10  ? 161 GLU B OE2 1 
ATOM   1308 N  N   . MET A 1 167 ? 18.396 35.863  4.603   1.00 17.50  ? 162 MET B N   1 
ATOM   1309 C  CA  . MET A 1 167 ? 17.477 35.050  3.829   1.00 18.10  ? 162 MET B CA  1 
ATOM   1310 C  C   . MET A 1 167 ? 16.048 35.231  4.294   1.00 17.46  ? 162 MET B C   1 
ATOM   1311 O  O   . MET A 1 167 ? 15.806 35.458  5.480   1.00 18.13  ? 162 MET B O   1 
ATOM   1312 C  CB  . MET A 1 167 ? 17.817 33.535  3.992   1.00 19.81  ? 162 MET B CB  1 
ATOM   1313 C  CG  . MET A 1 167 ? 19.151 33.178  3.471   1.00 19.71  ? 162 MET B CG  1 
ATOM   1314 S  SD  . MET A 1 167 ? 19.529 31.511  4.087   1.00 24.00  ? 162 MET B SD  1 
ATOM   1315 C  CE  . MET A 1 167 ? 20.415 30.889  2.744   1.00 25.71  ? 162 MET B CE  1 
ATOM   1316 N  N   . PRO A 1 168 ? 15.058 35.048  3.386   1.00 18.80  ? 163 PRO B N   1 
ATOM   1317 C  CA  . PRO A 1 168 ? 13.651 35.067  3.783   1.00 19.77  ? 163 PRO B CA  1 
ATOM   1318 C  C   . PRO A 1 168 ? 13.326 33.849  4.634   1.00 20.34  ? 163 PRO B C   1 
ATOM   1319 O  O   . PRO A 1 168 ? 13.968 32.797  4.511   1.00 18.67  ? 163 PRO B O   1 
ATOM   1320 C  CB  . PRO A 1 168 ? 12.882 35.064  2.455   1.00 22.40  ? 163 PRO B CB  1 
ATOM   1321 C  CG  . PRO A 1 168 ? 13.785 34.477  1.502   1.00 24.88  ? 163 PRO B CG  1 
ATOM   1322 C  CD  . PRO A 1 168 ? 15.213 34.840  1.939   1.00 22.80  ? 163 PRO B CD  1 
ATOM   1323 N  N   . PRO A 1 169 ? 12.303 33.957  5.499   1.00 18.18  ? 164 PRO B N   1 
ATOM   1324 C  CA  . PRO A 1 169 ? 11.940 32.844  6.369   1.00 17.53  ? 164 PRO B CA  1 
ATOM   1325 C  C   . PRO A 1 169 ? 11.473 31.569  5.682   1.00 19.44  ? 164 PRO B C   1 
ATOM   1326 O  O   . PRO A 1 169 ? 11.441 30.517  6.308   1.00 19.10  ? 164 PRO B O   1 
ATOM   1327 C  CB  . PRO A 1 169 ? 10.845 33.426  7.263   1.00 20.46  ? 164 PRO B CB  1 
ATOM   1328 C  CG  . PRO A 1 169 ? 10.560 34.782  6.777   1.00 22.03  ? 164 PRO B CG  1 
ATOM   1329 C  CD  . PRO A 1 169 ? 11.502 35.174  5.732   1.00 18.94  ? 164 PRO B CD  1 
ATOM   1330 N  N   . THR A 1 170 ? 11.167 31.646  4.381   1.00 17.84  ? 165 THR B N   1 
ATOM   1331 C  CA  . THR A 1 170 ? 10.800 30.480  3.604   1.00 15.97  ? 165 THR B CA  1 
ATOM   1332 C  C   . THR A 1 170 ? 11.948 29.854  2.813   1.00 14.09  ? 165 THR B C   1 
ATOM   1333 O  O   . THR A 1 170 ? 11.740 28.873  2.117   1.00 16.56  ? 165 THR B O   1 
ATOM   1334 C  CB  . THR A 1 170 ? 9.674  30.868  2.618   1.00 18.64  ? 165 THR B CB  1 
ATOM   1335 O  OG1 . THR A 1 170 ? 10.104 32.013  1.924   1.00 20.38  ? 165 THR B OG1 1 
ATOM   1336 C  CG2 . THR A 1 170 ? 8.348  31.121  3.325   1.00 22.74  ? 165 THR B CG2 1 
ATOM   1337 N  N   . ASN A 1 171 ? 13.143 30.448  2.880   1.00 15.81  ? 166 ASN B N   1 
ATOM   1338 C  CA  . ASN A 1 171 ? 14.246 29.915  2.098   1.00 15.49  ? 166 ASN B CA  1 
ATOM   1339 C  C   . ASN A 1 171 ? 14.499 28.460  2.509   1.00 14.56  ? 166 ASN B C   1 
ATOM   1340 O  O   . ASN A 1 171 ? 14.604 28.168  3.712   1.00 16.03  ? 166 ASN B O   1 
ATOM   1341 C  CB  . ASN A 1 171 ? 15.447 30.760  2.289   1.00 16.80  ? 166 ASN B CB  1 
ATOM   1342 C  CG  . ASN A 1 171 ? 16.661 30.225  1.604   1.00 22.16  ? 166 ASN B CG  1 
ATOM   1343 O  OD1 . ASN A 1 171 ? 17.292 29.302  2.104   1.00 21.35  ? 166 ASN B OD1 1 
ATOM   1344 N  ND2 . ASN A 1 171 ? 17.045 30.845  0.478   1.00 24.67  ? 166 ASN B ND2 1 
ATOM   1345 N  N   . PRO A 1 172 ? 14.574 27.482  1.567   1.00 16.60  ? 167 PRO B N   1 
ATOM   1346 C  CA  . PRO A 1 172 ? 14.753 26.086  1.952   1.00 15.37  ? 167 PRO B CA  1 
ATOM   1347 C  C   . PRO A 1 172 ? 15.993 25.799  2.792   1.00 13.87  ? 167 PRO B C   1 
ATOM   1348 O  O   . PRO A 1 172 ? 15.928 24.945  3.675   1.00 14.73  ? 167 PRO B O   1 
ATOM   1349 C  CB  . PRO A 1 172 ? 14.765 25.367  0.609   1.00 16.74  ? 167 PRO B CB  1 
ATOM   1350 C  CG  . PRO A 1 172 ? 13.906 26.218  -0.261  1.00 22.39  ? 167 PRO B CG  1 
ATOM   1351 C  CD  . PRO A 1 172 ? 14.294 27.589  0.127   1.00 21.18  ? 167 PRO B CD  1 
ATOM   1352 N  N   . ILE A 1 173 ? 17.101 26.492  2.522   1.00 15.44  ? 168 ILE B N   1 
ATOM   1353 C  CA  . ILE A 1 173 ? 18.307 26.283  3.314   1.00 14.74  ? 168 ILE B CA  1 
ATOM   1354 C  C   . ILE A 1 173 ? 18.071 26.757  4.750   1.00 14.67  ? 168 ILE B C   1 
ATOM   1355 O  O   . ILE A 1 173 ? 18.401 26.063  5.707   1.00 14.04  ? 168 ILE B O   1 
ATOM   1356 C  CB  . ILE A 1 173 ? 19.534 26.922  2.655   1.00 15.53  ? 168 ILE B CB  1 
ATOM   1357 C  CG1 . ILE A 1 173 ? 19.786 26.290  1.296   1.00 20.70  ? 168 ILE B CG1 1 
ATOM   1358 C  CG2 . ILE A 1 173 ? 20.739 26.765  3.559   1.00 15.79  ? 168 ILE B CG2 1 
ATOM   1359 C  CD1 . ILE A 1 173 ? 20.748 26.969  0.521   1.00 23.71  ? 168 ILE B CD1 1 
ATOM   1360 N  N   . ARG A 1 174 ? 17.497 27.950  4.899   1.00 14.21  ? 169 ARG B N   1 
ATOM   1361 C  CA  . ARG A 1 174 ? 17.138 28.473  6.213   1.00 13.43  ? 169 ARG B CA  1 
ATOM   1362 C  C   . ARG A 1 174 ? 16.212 27.521  6.965   1.00 12.11  ? 169 ARG B C   1 
ATOM   1363 O  O   . ARG A 1 174 ? 16.439 27.238  8.153   1.00 13.00  ? 169 ARG B O   1 
ATOM   1364 C  CB  . ARG A 1 174 ? 16.487 29.839  6.118   1.00 13.68  ? 169 ARG B CB  1 
ATOM   1365 C  CG  . ARG A 1 174 ? 16.155 30.459  7.461   1.00 14.56  ? 169 ARG B CG  1 
ATOM   1366 C  CD  . ARG A 1 174 ? 15.687 31.913  7.373   1.00 16.30  ? 169 ARG B CD  1 
ATOM   1367 N  NE  . ARG A 1 174 ? 15.063 32.343  8.613   1.00 16.43  ? 169 ARG B NE  1 
ATOM   1368 C  CZ  . ARG A 1 174 ? 14.617 33.586  8.825   1.00 16.90  ? 169 ARG B CZ  1 
ATOM   1369 N  NH1 . ARG A 1 174 ? 14.736 34.544  7.906   1.00 16.53  ? 169 ARG B NH1 1 
ATOM   1370 N  NH2 . ARG A 1 174 ? 14.000 33.856  9.966   1.00 16.89  ? 169 ARG B NH2 1 
ATOM   1371 N  N   . LEU A 1 175 ? 15.180 27.006  6.282   1.00 12.45  ? 170 LEU B N   1 
ATOM   1372 C  CA  . LEU A 1 175 ? 14.273 26.051  6.887   1.00 12.47  ? 170 LEU B CA  1 
ATOM   1373 C  C   . LEU A 1 175 ? 14.933 24.726  7.270   1.00 13.07  ? 170 LEU B C   1 
ATOM   1374 O  O   . LEU A 1 175 ? 14.718 24.205  8.370   1.00 14.49  ? 170 LEU B O   1 
ATOM   1375 C  CB  . LEU A 1 175 ? 13.118 25.759  5.935   1.00 14.26  ? 170 LEU B CB  1 
ATOM   1376 C  CG  . LEU A 1 175 ? 12.093 26.894  5.766   1.00 15.51  ? 170 LEU B CG  1 
ATOM   1377 C  CD1 . LEU A 1 175 ? 11.049 26.498  4.741   1.00 17.58  ? 170 LEU B CD1 1 
ATOM   1378 C  CD2 . LEU A 1 175 ? 11.419 27.213  7.047   1.00 17.63  ? 170 LEU B CD2 1 
ATOM   1379 N  N   . GLY A 1 176 ? 15.768 24.187  6.378   1.00 14.07  ? 171 GLY B N   1 
ATOM   1380 C  CA  . GLY A 1 176 ? 16.447 22.936  6.690   1.00 14.42  ? 171 GLY B CA  1 
ATOM   1381 C  C   . GLY A 1 176 ? 17.443 23.071  7.837   1.00 12.23  ? 171 GLY B C   1 
ATOM   1382 O  O   . GLY A 1 176 ? 17.564 22.149  8.652   1.00 13.08  ? 171 GLY B O   1 
ATOM   1383 N  N   . LEU A 1 177 ? 18.095 24.232  7.920   1.00 12.55  ? 172 LEU B N   1 
ATOM   1384 C  CA  . LEU A 1 177 ? 18.966 24.522  9.040   1.00 12.41  ? 172 LEU B CA  1 
ATOM   1385 C  C   . LEU A 1 177 ? 18.193 24.535  10.354  1.00 12.61  ? 172 LEU B C   1 
ATOM   1386 O  O   . LEU A 1 177 ? 18.609 23.933  11.338  1.00 12.83  ? 172 LEU B O   1 
ATOM   1387 C  CB  . LEU A 1 177 ? 19.658 25.865  8.813   1.00 12.70  ? 172 LEU B CB  1 
ATOM   1388 C  CG  . LEU A 1 177 ? 20.282 26.544  10.008  1.00 12.96  ? 172 LEU B CG  1 
ATOM   1389 C  CD1 . LEU A 1 177 ? 21.434 25.681  10.583  1.00 14.38  ? 172 LEU B CD1 1 
ATOM   1390 C  CD2 . LEU A 1 177 ? 20.750 27.911  9.683   1.00 14.08  ? 172 LEU B CD2 1 
ATOM   1391 N  N   . ALA A 1 178 ? 17.102 25.314  10.392  1.00 13.51  ? 173 ALA B N   1 
ATOM   1392 C  CA  . ALA A 1 178 ? 16.308 25.400  11.610  1.00 13.60  ? 173 ALA B CA  1 
ATOM   1393 C  C   . ALA A 1 178 ? 15.750 24.039  12.022  1.00 11.89  ? 173 ALA B C   1 
ATOM   1394 O  O   . ALA A 1 178 ? 15.753 23.682  13.196  1.00 13.65  ? 173 ALA B O   1 
ATOM   1395 C  CB  . ALA A 1 178 ? 15.177 26.413  11.428  1.00 14.80  ? 173 ALA B CB  1 
ATOM   1396 N  N   . LEU A 1 179 ? 15.267 23.251  11.059  1.00 11.51  ? 174 LEU B N   1 
ATOM   1397 C  CA  . LEU A 1 179 ? 14.855 21.886  11.334  1.00 13.36  ? 174 LEU B CA  1 
ATOM   1398 C  C   . LEU A 1 179 ? 15.979 21.100  12.009  1.00 12.38  ? 174 LEU B C   1 
ATOM   1399 O  O   . LEU A 1 179 ? 15.752 20.492  13.072  1.00 13.69  ? 174 LEU B O   1 
ATOM   1400 C  CB  . LEU A 1 179 ? 14.398 21.198  10.040  1.00 15.25  ? 174 LEU B CB  1 
ATOM   1401 C  CG  . LEU A 1 179 ? 13.992 19.729  10.147  1.00 14.40  ? 174 LEU B CG  1 
ATOM   1402 C  CD1 . LEU A 1 179 ? 12.818 19.568  10.994  1.00 18.40  ? 174 LEU B CD1 1 
ATOM   1403 C  CD2 . LEU A 1 179 ? 13.739 19.158  8.732   1.00 16.23  ? 174 LEU B CD2 1 
ATOM   1404 N  N   . ASN A 1 180 ? 17.155 21.079  11.386  1.00 11.87  ? 175 ASN B N   1 
ATOM   1405 C  CA  . ASN A 1 180 ? 18.246 20.289  11.958  1.00 12.70  ? 175 ASN B CA  1 
ATOM   1406 C  C   . ASN A 1 180 ? 18.757 20.806  13.302  1.00 12.66  ? 175 ASN B C   1 
ATOM   1407 O  O   . ASN A 1 180 ? 19.092 20.007  14.178  1.00 13.39  ? 175 ASN B O   1 
ATOM   1408 C  CB  . ASN A 1 180 ? 19.365 20.177  10.966  1.00 12.52  ? 175 ASN B CB  1 
ATOM   1409 C  CG  . ASN A 1 180 ? 19.017 19.210  9.863   1.00 13.69  ? 175 ASN B CG  1 
ATOM   1410 O  OD1 . ASN A 1 180 ? 17.898 18.724  9.750   1.00 13.63  ? 175 ASN B OD1 1 
ATOM   1411 N  ND2 . ASN A 1 180 ? 19.978 18.897  8.983   1.00 13.18  ? 175 ASN B ND2 1 
ATOM   1412 N  N   . PHE A 1 181 ? 18.743 22.132  13.496  1.00 11.26  ? 176 PHE B N   1 
ATOM   1413 C  CA  . PHE A 1 181 ? 19.136 22.676  14.784  1.00 11.59  ? 176 PHE B CA  1 
ATOM   1414 C  C   . PHE A 1 181 ? 18.117 22.283  15.847  1.00 11.91  ? 176 PHE B C   1 
ATOM   1415 O  O   . PHE A 1 181 ? 18.492 21.979  16.980  1.00 12.38  ? 176 PHE B O   1 
ATOM   1416 C  CB  . PHE A 1 181 ? 19.364 24.177  14.688  1.00 11.78  ? 176 PHE B CB  1 
ATOM   1417 C  CG  . PHE A 1 181 ? 20.099 24.897  15.798  1.00 13.31  ? 176 PHE B CG  1 
ATOM   1418 C  CD1 . PHE A 1 181 ? 20.889 24.213  16.704  1.00 13.34  ? 176 PHE B CD1 1 
ATOM   1419 C  CD2 . PHE A 1 181 ? 19.993 26.272  15.936  1.00 14.66  ? 176 PHE B CD2 1 
ATOM   1420 C  CE1 . PHE A 1 181 ? 21.619 24.904  17.688  1.00 14.62  ? 176 PHE B CE1 1 
ATOM   1421 C  CE2 . PHE A 1 181 ? 20.708 26.959  16.923  1.00 16.88  ? 176 PHE B CE2 1 
ATOM   1422 C  CZ  . PHE A 1 181 ? 21.531 26.273  17.785  1.00 14.83  ? 176 PHE B CZ  1 
ATOM   1423 N  N   . SER A 1 182 ? 16.825 22.252  15.492  1.00 12.60  ? 177 SER B N   1 
ATOM   1424 C  CA  . SER A 1 182 ? 15.814 21.811  16.448  1.00 12.85  ? 177 SER B CA  1 
ATOM   1425 C  C   . SER A 1 182 ? 16.009 20.347  16.813  1.00 13.47  ? 177 SER B C   1 
ATOM   1426 O  O   . SER A 1 182 ? 15.839 19.994  17.961  1.00 14.40  ? 177 SER B O   1 
ATOM   1427 C  CB  . SER A 1 182 ? 14.383 22.074  15.952  1.00 14.24  ? 177 SER B CB  1 
ATOM   1428 O  OG  . SER A 1 182 ? 14.002 21.229  14.883  1.00 16.25  ? 177 SER B OG  1 
ATOM   1429 N  N   . VAL A 1 183 ? 16.392 19.502  15.845  1.00 11.89  ? 178 VAL B N   1 
ATOM   1430 C  CA  . VAL A 1 183 ? 16.720 18.105  16.124  1.00 13.79  ? 178 VAL B CA  1 
ATOM   1431 C  C   . VAL A 1 183 ? 17.938 17.996  17.039  1.00 12.70  ? 178 VAL B C   1 
ATOM   1432 O  O   . VAL A 1 183 ? 17.922 17.208  17.990  1.00 14.57  ? 178 VAL B O   1 
ATOM   1433 C  CB  . VAL A 1 183 ? 16.924 17.292  14.812  1.00 13.85  ? 178 VAL B CB  1 
ATOM   1434 C  CG1 . VAL A 1 183 ? 17.513 15.927  15.125  1.00 14.87  ? 178 VAL B CG1 1 
ATOM   1435 C  CG2 . VAL A 1 183 ? 15.596 17.172  14.066  1.00 15.14  ? 178 VAL B CG2 1 
ATOM   1436 N  N   . PHE A 1 184 ? 18.957 18.819  16.789  1.00 12.75  ? 179 PHE B N   1 
ATOM   1437 C  CA  . PHE A 1 184 ? 20.102 18.913  17.684  1.00 12.78  ? 179 PHE B CA  1 
ATOM   1438 C  C   . PHE A 1 184 ? 19.647 19.181  19.121  1.00 13.63  ? 179 PHE B C   1 
ATOM   1439 O  O   . PHE A 1 184 ? 20.047 18.484  20.055  1.00 14.06  ? 179 PHE B O   1 
ATOM   1440 C  CB  . PHE A 1 184 ? 21.048 19.981  17.201  1.00 12.02  ? 179 PHE B CB  1 
ATOM   1441 C  CG  . PHE A 1 184 ? 22.108 20.357  18.205  1.00 13.31  ? 179 PHE B CG  1 
ATOM   1442 C  CD1 . PHE A 1 184 ? 23.262 19.594  18.338  1.00 13.53  ? 179 PHE B CD1 1 
ATOM   1443 C  CD2 . PHE A 1 184 ? 21.931 21.439  19.049  1.00 14.91  ? 179 PHE B CD2 1 
ATOM   1444 C  CE1 . PHE A 1 184 ? 24.222 19.931  19.281  1.00 14.37  ? 179 PHE B CE1 1 
ATOM   1445 C  CE2 . PHE A 1 184 ? 22.885 21.765  20.009  1.00 15.46  ? 179 PHE B CE2 1 
ATOM   1446 C  CZ  . PHE A 1 184 ? 24.034 21.001  20.106  1.00 16.03  ? 179 PHE B CZ  1 
ATOM   1447 N  N   . HIS A 1 185 ? 18.766 20.174  19.306  1.00 12.81  ? 180 HIS B N   1 
ATOM   1448 C  CA  . HIS A 1 185 ? 18.338 20.525  20.651  1.00 13.71  ? 180 HIS B CA  1 
ATOM   1449 C  C   . HIS A 1 185 ? 17.632 19.344  21.307  1.00 13.65  ? 180 HIS B C   1 
ATOM   1450 O  O   . HIS A 1 185 ? 17.829 19.077  22.500  1.00 13.66  ? 180 HIS B O   1 
ATOM   1451 C  CB  . HIS A 1 185 ? 17.400 21.751  20.634  1.00 13.52  ? 180 HIS B CB  1 
ATOM   1452 C  CG  . HIS A 1 185 ? 18.069 23.051  20.375  1.00 12.84  ? 180 HIS B CG  1 
ATOM   1453 N  ND1 . HIS A 1 185 ? 19.189 23.505  21.051  1.00 15.43  ? 180 HIS B ND1 1 
ATOM   1454 C  CD2 . HIS A 1 185 ? 17.778 23.994  19.444  1.00 14.33  ? 180 HIS B CD2 1 
ATOM   1455 C  CE1 . HIS A 1 185 ? 19.533 24.689  20.557  1.00 14.93  ? 180 HIS B CE1 1 
ATOM   1456 N  NE2 . HIS A 1 185 ? 18.704 25.009  19.565  1.00 15.73  ? 180 HIS B NE2 1 
ATOM   1457 N  N   . TYR A 1 186 ? 16.749 18.661  20.565  1.00 13.89  ? 181 TYR B N   1 
ATOM   1458 C  CA  . TYR A 1 186 ? 15.928 17.609  21.145  1.00 15.63  ? 181 TYR B CA  1 
ATOM   1459 C  C   . TYR A 1 186 ? 16.715 16.323  21.406  1.00 16.55  ? 181 TYR B C   1 
ATOM   1460 O  O   . TYR A 1 186 ? 16.601 15.723  22.475  1.00 19.50  ? 181 TYR B O   1 
ATOM   1461 C  CB  . TYR A 1 186 ? 14.745 17.314  20.215  1.00 17.38  ? 181 TYR B CB  1 
ATOM   1462 C  CG  . TYR A 1 186 ? 13.691 16.471  20.846  1.00 17.65  ? 181 TYR B CG  1 
ATOM   1463 C  CD1 . TYR A 1 186 ? 13.795 15.092  20.866  1.00 19.11  ? 181 TYR B CD1 1 
ATOM   1464 C  CD2 . TYR A 1 186 ? 12.617 17.054  21.495  1.00 20.04  ? 181 TYR B CD2 1 
ATOM   1465 C  CE1 . TYR A 1 186 ? 12.814 14.309  21.475  1.00 22.11  ? 181 TYR B CE1 1 
ATOM   1466 C  CE2 . TYR A 1 186 ? 11.648 16.286  22.113  1.00 24.43  ? 181 TYR B CE2 1 
ATOM   1467 C  CZ  . TYR A 1 186 ? 11.745 14.918  22.092  1.00 22.51  ? 181 TYR B CZ  1 
ATOM   1468 O  OH  . TYR A 1 186 ? 10.735 14.179  22.705  1.00 28.98  ? 181 TYR B OH  1 
ATOM   1469 N  N   . GLU A 1 187 ? 17.516 15.905  20.431  1.00 16.72  ? 182 GLU B N   1 
ATOM   1470 C  CA  . GLU A 1 187 ? 18.114 14.575  20.460  1.00 17.17  ? 182 GLU B CA  1 
ATOM   1471 C  C   . GLU A 1 187 ? 19.521 14.565  21.053  1.00 19.13  ? 182 GLU B C   1 
ATOM   1472 O  O   . GLU A 1 187 ? 19.976 13.533  21.553  1.00 21.42  ? 182 GLU B O   1 
ATOM   1473 C  CB  . GLU A 1 187 ? 18.164 13.999  19.036  1.00 18.53  ? 182 GLU B CB  1 
ATOM   1474 C  CG  . GLU A 1 187 ? 16.806 13.743  18.394  1.00 20.28  ? 182 GLU B CG  1 
ATOM   1475 C  CD  . GLU A 1 187 ? 15.982 12.564  18.917  1.00 27.94  ? 182 GLU B CD  1 
ATOM   1476 O  OE1 . GLU A 1 187 ? 16.520 11.767  19.725  1.00 29.74  ? 182 GLU B OE1 1 
ATOM   1477 O  OE2 . GLU A 1 187 ? 14.797 12.435  18.523  1.00 24.43  ? 182 GLU B OE2 1 
ATOM   1478 N  N   . ILE A 1 188 ? 20.234 15.678  20.957  1.00 17.00  ? 183 ILE B N   1 
ATOM   1479 C  CA  . ILE A 1 188 ? 21.626 15.748  21.392  1.00 16.36  ? 183 ILE B CA  1 
ATOM   1480 C  C   . ILE A 1 188 ? 21.821 16.558  22.669  1.00 20.04  ? 183 ILE B C   1 
ATOM   1481 O  O   . ILE A 1 188 ? 22.535 16.124  23.581  1.00 19.70  ? 183 ILE B O   1 
ATOM   1482 C  CB  . ILE A 1 188 ? 22.520 16.328  20.266  1.00 17.87  ? 183 ILE B CB  1 
ATOM   1483 C  CG1 . ILE A 1 188 ? 22.299 15.602  18.957  1.00 19.03  ? 183 ILE B CG1 1 
ATOM   1484 C  CG2 . ILE A 1 188 ? 24.002 16.384  20.689  1.00 18.09  ? 183 ILE B CG2 1 
ATOM   1485 C  CD1 . ILE A 1 188 ? 22.657 14.136  18.933  1.00 20.29  ? 183 ILE B CD1 1 
ATOM   1486 N  N   . ALA A 1 189 ? 21.212 17.766  22.722  1.00 15.92  ? 184 ALA B N   1 
ATOM   1487 C  CA  . ALA A 1 189 ? 21.493 18.715  23.782  1.00 16.88  ? 184 ALA B CA  1 
ATOM   1488 C  C   . ALA A 1 189 ? 20.555 18.630  24.982  1.00 16.29  ? 184 ALA B C   1 
ATOM   1489 O  O   . ALA A 1 189 ? 20.659 19.477  25.876  1.00 20.50  ? 184 ALA B O   1 
ATOM   1490 C  CB  . ALA A 1 189 ? 21.471 20.110  23.215  1.00 18.58  ? 184 ALA B CB  1 
ATOM   1491 N  N   . ASN A 1 190 ? 19.653 17.649  24.993  1.00 17.53  ? 185 ASN B N   1 
ATOM   1492 C  CA  . ASN A 1 190 ? 18.727 17.475  26.104  1.00 20.82  ? 185 ASN B CA  1 
ATOM   1493 C  C   . ASN A 1 190 ? 17.958 18.771  26.377  1.00 21.84  ? 185 ASN B C   1 
ATOM   1494 O  O   . ASN A 1 190 ? 17.774 19.176  27.531  1.00 20.20  ? 185 ASN B O   1 
ATOM   1495 C  CB  . ASN A 1 190 ? 19.483 16.999  27.384  1.00 24.45  ? 185 ASN B CB  1 
ATOM   1496 C  CG  . ASN A 1 190 ? 18.534 16.470  28.461  1.00 35.14  ? 185 ASN B CG  1 
ATOM   1497 O  OD1 . ASN A 1 190 ? 17.486 15.880  28.172  1.00 39.32  ? 185 ASN B OD1 1 
ATOM   1498 N  ND2 . ASN A 1 190 ? 18.855 16.714  29.732  1.00 36.53  ? 185 ASN B ND2 1 
ATOM   1499 N  N   . SER A 1 191 ? 17.518 19.433  25.293  1.00 16.94  ? 186 SER B N   1 
ATOM   1500 C  CA  . SER A 1 191 ? 16.839 20.721  25.377  1.00 15.27  ? 186 SER B CA  1 
ATOM   1501 C  C   . SER A 1 191 ? 15.539 20.652  24.595  1.00 16.54  ? 186 SER B C   1 
ATOM   1502 O  O   . SER A 1 191 ? 15.380 21.370  23.607  1.00 15.29  ? 186 SER B O   1 
ATOM   1503 C  CB  . SER A 1 191 ? 17.737 21.853  24.882  1.00 18.42  ? 186 SER B CB  1 
ATOM   1504 O  OG  . SER A 1 191 ? 18.972 21.937  25.591  1.00 19.24  ? 186 SER B OG  1 
ATOM   1505 N  N   . PRO A 1 192 ? 14.569 19.797  24.991  1.00 16.56  ? 187 PRO B N   1 
ATOM   1506 C  CA  . PRO A 1 192 ? 13.347 19.644  24.207  1.00 17.66  ? 187 PRO B CA  1 
ATOM   1507 C  C   . PRO A 1 192 ? 12.545 20.941  24.087  1.00 16.70  ? 187 PRO B C   1 
ATOM   1508 O  O   . PRO A 1 192 ? 11.923 21.178  23.059  1.00 16.57  ? 187 PRO B O   1 
ATOM   1509 C  CB  . PRO A 1 192 ? 12.588 18.528  24.921  1.00 18.55  ? 187 PRO B CB  1 
ATOM   1510 C  CG  . PRO A 1 192 ? 13.189 18.484  26.321  1.00 17.93  ? 187 PRO B CG  1 
ATOM   1511 C  CD  . PRO A 1 192 ? 14.617 18.892  26.161  1.00 19.90  ? 187 PRO B CD  1 
ATOM   1512 N  N   . GLU A 1 193 ? 12.519 21.763  25.131  1.00 16.30  ? 188 GLU B N   1 
ATOM   1513 C  CA  . GLU A 1 193 ? 11.782 23.020  25.060  1.00 16.61  ? 188 GLU B CA  1 
ATOM   1514 C  C   . GLU A 1 193 ? 12.375 23.984  24.036  1.00 16.73  ? 188 GLU B C   1 
ATOM   1515 O  O   . GLU A 1 193 ? 11.640 24.632  23.279  1.00 16.70  ? 188 GLU B O   1 
ATOM   1516 C  CB  . GLU A 1 193 ? 11.715 23.674  26.449  1.00 19.08  ? 188 GLU B CB  1 
ATOM   1517 C  CG  . GLU A 1 193 ? 10.800 22.926  27.363  1.00 18.73  ? 188 GLU B CG  1 
ATOM   1518 C  CD  . GLU A 1 193 ? 10.698 23.392  28.799  1.00 22.18  ? 188 GLU B CD  1 
ATOM   1519 O  OE1 . GLU A 1 193 ? 11.655 24.018  29.313  1.00 22.09  ? 188 GLU B OE1 1 
ATOM   1520 O  OE2 . GLU A 1 193 ? 9.644  23.093  29.419  1.00 24.08  ? 188 GLU B OE2 1 
ATOM   1521 N  N   . GLU A 1 194 ? 13.710 24.058  23.969  1.00 14.33  ? 189 GLU B N   1 
ATOM   1522 C  CA  . GLU A 1 194 ? 14.371 24.855  22.954  1.00 14.26  ? 189 GLU B CA  1 
ATOM   1523 C  C   . GLU A 1 194 ? 14.037 24.329  21.558  1.00 14.00  ? 189 GLU B C   1 
ATOM   1524 O  O   . GLU A 1 194 ? 13.785 25.117  20.630  1.00 14.98  ? 189 GLU B O   1 
ATOM   1525 C  CB  . GLU A 1 194 ? 15.896 24.875  23.172  1.00 15.33  ? 189 GLU B CB  1 
ATOM   1526 C  CG  . GLU A 1 194 ? 16.615 25.884  22.334  1.00 17.01  ? 189 GLU B CG  1 
ATOM   1527 C  CD  . GLU A 1 194 ? 16.418 27.358  22.684  1.00 20.45  ? 189 GLU B CD  1 
ATOM   1528 O  OE1 . GLU A 1 194 ? 15.960 27.632  23.814  1.00 20.90  ? 189 GLU B OE1 1 
ATOM   1529 O  OE2 . GLU A 1 194 ? 16.761 28.222  21.841  1.00 21.12  ? 189 GLU B OE2 1 
ATOM   1530 N  N   . ALA A 1 195 ? 14.022 23.007  21.415  1.00 14.07  ? 190 ALA B N   1 
ATOM   1531 C  CA  . ALA A 1 195 ? 13.652 22.374  20.151  1.00 14.09  ? 190 ALA B CA  1 
ATOM   1532 C  C   . ALA A 1 195 ? 12.251 22.763  19.685  1.00 14.21  ? 190 ALA B C   1 
ATOM   1533 O  O   . ALA A 1 195 ? 12.057 23.148  18.530  1.00 14.76  ? 190 ALA B O   1 
ATOM   1534 C  CB  . ALA A 1 195 ? 13.751 20.871  20.244  1.00 14.35  ? 190 ALA B CB  1 
ATOM   1535 N  N   . ILE A 1 196 ? 11.291 22.629  20.596  1.00 14.81  ? 191 ILE B N   1 
ATOM   1536 C  CA  . ILE A 1 196 ? 9.897  22.943  20.310  1.00 15.80  ? 191 ILE B CA  1 
ATOM   1537 C  C   . ILE A 1 196 ? 9.741  24.430  19.975  1.00 15.52  ? 191 ILE B C   1 
ATOM   1538 O  O   . ILE A 1 196 ? 9.103  24.785  18.989  1.00 16.00  ? 191 ILE B O   1 
ATOM   1539 C  CB  . ILE A 1 196 ? 9.011  22.512  21.505  1.00 16.34  ? 191 ILE B CB  1 
ATOM   1540 C  CG1 . ILE A 1 196 ? 8.946  20.995  21.640  1.00 18.92  ? 191 ILE B CG1 1 
ATOM   1541 C  CG2 . ILE A 1 196 ? 7.607  23.099  21.387  1.00 17.53  ? 191 ILE B CG2 1 
ATOM   1542 C  CD1 . ILE A 1 196 ? 8.465  20.472  22.981  1.00 19.04  ? 191 ILE B CD1 1 
ATOM   1543 N  N   . SER A 1 197 ? 10.364 25.302  20.762  1.00 14.84  ? 192 SER B N   1 
ATOM   1544 C  CA  . SER A 1 197 ? 10.268 26.724  20.515  1.00 14.77  ? 192 SER B CA  1 
ATOM   1545 C  C   . SER A 1 197 ? 10.803 27.095  19.141  1.00 15.94  ? 192 SER B C   1 
ATOM   1546 O  O   . SER A 1 197 ? 10.208 27.875  18.399  1.00 16.21  ? 192 SER B O   1 
ATOM   1547 C  CB  . SER A 1 197 ? 10.990 27.502  21.598  1.00 17.88  ? 192 SER B CB  1 
ATOM   1548 O  OG  . SER A 1 197 ? 10.913 28.910  21.377  1.00 23.22  ? 192 SER B OG  1 
ATOM   1549 N  N   . LEU A 1 198 ? 11.996 26.594  18.814  1.00 15.53  ? 193 LEU B N   1 
ATOM   1550 C  CA  . LEU A 1 198 ? 12.568 26.864  17.509  1.00 15.45  ? 193 LEU B CA  1 
ATOM   1551 C  C   . LEU A 1 198 ? 11.683 26.342  16.382  1.00 15.24  ? 193 LEU B C   1 
ATOM   1552 O  O   . LEU A 1 198 ? 11.490 27.041  15.387  1.00 15.17  ? 193 LEU B O   1 
ATOM   1553 C  CB  . LEU A 1 198 ? 13.979 26.259  17.405  1.00 16.26  ? 193 LEU B CB  1 
ATOM   1554 C  CG  . LEU A 1 198 ? 14.698 26.451  16.094  1.00 15.68  ? 193 LEU B CG  1 
ATOM   1555 C  CD1 . LEU A 1 198 ? 14.809 27.878  15.699  1.00 16.87  ? 193 LEU B CD1 1 
ATOM   1556 C  CD2 . LEU A 1 198 ? 16.154 25.848  16.175  1.00 16.11  ? 193 LEU B CD2 1 
ATOM   1557 N  N   . ALA A 1 199 ? 11.180 25.116  16.499  1.00 14.54  ? 194 ALA B N   1 
ATOM   1558 C  CA  . ALA A 1 199 ? 10.345 24.570  15.439  1.00 15.18  ? 194 ALA B CA  1 
ATOM   1559 C  C   . ALA A 1 199 ? 9.063  25.383  15.237  1.00 15.47  ? 194 ALA B C   1 
ATOM   1560 O  O   . ALA A 1 199 ? 8.682  25.658  14.098  1.00 15.73  ? 194 ALA B O   1 
ATOM   1561 C  CB  . ALA A 1 199 ? 9.980  23.144  15.719  1.00 16.90  ? 194 ALA B CB  1 
ATOM   1562 N  N   . LYS A 1 200 ? 8.445  25.798  16.350  1.00 16.28  ? 195 LYS B N   1 
ATOM   1563 C  CA  . LYS A 1 200 ? 7.209  26.574  16.295  1.00 17.75  ? 195 LYS B CA  1 
ATOM   1564 C  C   . LYS A 1 200 ? 7.433  27.944  15.666  1.00 15.86  ? 195 LYS B C   1 
ATOM   1565 O  O   . LYS A 1 200 ? 6.711  28.329  14.738  1.00 17.43  ? 195 LYS B O   1 
ATOM   1566 C  CB  . LYS A 1 200 ? 6.626  26.779  17.682  1.00 18.60  ? 195 LYS B CB  1 
ATOM   1567 C  CG  . LYS A 1 200 ? 5.894  25.648  18.246  1.00 24.17  ? 195 LYS B CG  1 
ATOM   1568 C  CD  . LYS A 1 200 ? 5.393  25.959  19.661  1.00 32.33  ? 195 LYS B CD  1 
ATOM   1569 C  CE  . LYS A 1 200 ? 4.437  24.911  20.189  1.00 37.49  ? 195 LYS B CE  1 
ATOM   1570 N  NZ  . LYS A 1 200 ? 4.007  25.227  21.564  1.00 46.76  ? 195 LYS B NZ  1 
ATOM   1571 N  N   . THR A 1 201 ? 8.446  28.672  16.139  1.00 15.15  ? 196 THR B N   1 
ATOM   1572 C  CA  . THR A 1 201 ? 8.747  29.989  15.608  1.00 14.52  ? 196 THR B CA  1 
ATOM   1573 C  C   . THR A 1 201 ? 9.120  29.908  14.127  1.00 16.52  ? 196 THR B C   1 
ATOM   1574 O  O   . THR A 1 201 ? 8.709  30.752  13.324  1.00 16.11  ? 196 THR B O   1 
ATOM   1575 C  CB  . THR A 1 201 ? 9.819  30.674  16.419  1.00 18.81  ? 196 THR B CB  1 
ATOM   1576 O  OG1 . THR A 1 201 ? 9.292  30.987  17.733  1.00 22.76  ? 196 THR B OG1 1 
ATOM   1577 C  CG2 . THR A 1 201 ? 10.294 31.939  15.780  1.00 22.61  ? 196 THR B CG2 1 
ATOM   1578 N  N   . THR A 1 202 ? 9.944  28.922  13.759  1.00 15.44  ? 197 THR B N   1 
ATOM   1579 C  CA  . THR A 1 202 ? 10.307 28.753  12.360  1.00 13.71  ? 197 THR B CA  1 
ATOM   1580 C  C   . THR A 1 202 ? 9.091  28.517  11.473  1.00 15.74  ? 197 THR B C   1 
ATOM   1581 O  O   . THR A 1 202 ? 8.977  29.132  10.412  1.00 16.93  ? 197 THR B O   1 
ATOM   1582 C  CB  . THR A 1 202 ? 11.319 27.609  12.210  1.00 15.32  ? 197 THR B CB  1 
ATOM   1583 O  OG1 . THR A 1 202 ? 12.466 27.874  13.042  1.00 14.98  ? 197 THR B OG1 1 
ATOM   1584 C  CG2 . THR A 1 202 ? 11.785 27.421  10.762  1.00 14.00  ? 197 THR B CG2 1 
ATOM   1585 N  N   . PHE A 1 203 ? 8.221  27.608  11.901  1.00 15.30  ? 198 PHE B N   1 
ATOM   1586 C  CA  . PHE A 1 203 ? 7.020  27.261  11.147  1.00 15.48  ? 198 PHE B CA  1 
ATOM   1587 C  C   . PHE A 1 203 ? 6.150  28.507  10.955  1.00 17.96  ? 198 PHE B C   1 
ATOM   1588 O  O   . PHE A 1 203 ? 5.722  28.791  9.834   1.00 15.81  ? 198 PHE B O   1 
ATOM   1589 C  CB  . PHE A 1 203 ? 6.260  26.147  11.856  1.00 16.21  ? 198 PHE B CB  1 
ATOM   1590 C  CG  . PHE A 1 203 ? 5.048  25.671  11.096  1.00 16.89  ? 198 PHE B CG  1 
ATOM   1591 C  CD1 . PHE A 1 203 ? 3.839  26.338  11.205  1.00 18.14  ? 198 PHE B CD1 1 
ATOM   1592 C  CD2 . PHE A 1 203 ? 5.119  24.574  10.267  1.00 17.43  ? 198 PHE B CD2 1 
ATOM   1593 C  CE1 . PHE A 1 203 ? 2.747  25.921  10.469  1.00 20.19  ? 198 PHE B CE1 1 
ATOM   1594 C  CE2 . PHE A 1 203 ? 4.015  24.139  9.568   1.00 21.08  ? 198 PHE B CE2 1 
ATOM   1595 C  CZ  . PHE A 1 203 ? 2.839  24.816  9.662   1.00 21.40  ? 198 PHE B CZ  1 
ATOM   1596 N  N   . ASP A 1 204 ? 5.915  29.237  12.048  1.00 17.62  ? 199 ASP B N   1 
ATOM   1597 C  CA  . ASP A 1 204 ? 5.034  30.399  12.032  1.00 20.88  ? 199 ASP B CA  1 
ATOM   1598 C  C   . ASP A 1 204 ? 5.572  31.527  11.149  1.00 17.24  ? 199 ASP B C   1 
ATOM   1599 O  O   . ASP A 1 204 ? 4.819  32.135  10.388  1.00 18.03  ? 199 ASP B O   1 
ATOM   1600 C  CB  . ASP A 1 204 ? 4.757  30.845  13.488  1.00 20.89  ? 199 ASP B CB  1 
ATOM   1601 C  CG  . ASP A 1 204 ? 3.856  29.856  14.270  1.00 24.70  ? 199 ASP B CG  1 
ATOM   1602 O  OD1 . ASP A 1 204 ? 3.237  28.988  13.646  1.00 32.69  ? 199 ASP B OD1 1 
ATOM   1603 O  OD2 . ASP A 1 204 ? 3.809  29.944  15.506  1.00 34.82  ? 199 ASP B OD2 1 
ATOM   1604 N  N   . GLU A 1 205 ? 6.874  31.787  11.167  1.00 15.65  ? 200 GLU B N   1 
ATOM   1605 C  CA  . GLU A 1 205 ? 7.446  32.854  10.374  1.00 15.93  ? 200 GLU B CA  1 
ATOM   1606 C  C   . GLU A 1 205 ? 7.452  32.464  8.900   1.00 15.96  ? 200 GLU B C   1 
ATOM   1607 O  O   . GLU A 1 205 ? 7.236  33.299  8.028   1.00 17.56  ? 200 GLU B O   1 
ATOM   1608 C  CB  . GLU A 1 205 ? 8.826  33.237  10.872  1.00 21.10  ? 200 GLU B CB  1 
ATOM   1609 C  CG  . GLU A 1 205 ? 8.783  33.962  12.198  1.00 28.70  ? 200 GLU B CG  1 
ATOM   1610 C  CD  . GLU A 1 205 ? 10.061 34.759  12.383  1.00 49.96  ? 200 GLU B CD  1 
ATOM   1611 O  OE1 . GLU A 1 205 ? 11.130 34.128  12.567  1.00 42.06  ? 200 GLU B OE1 1 
ATOM   1612 O  OE2 . GLU A 1 205 ? 10.007 36.008  12.264  1.00 57.14  ? 200 GLU B OE2 1 
ATOM   1613 N  N   . ALA A 1 206 ? 7.637  31.179  8.608   1.00 15.45  ? 201 ALA B N   1 
ATOM   1614 C  CA  . ALA A 1 206 ? 7.539  30.727  7.233   1.00 14.14  ? 201 ALA B CA  1 
ATOM   1615 C  C   . ALA A 1 206 ? 6.103  30.825  6.700   1.00 15.80  ? 201 ALA B C   1 
ATOM   1616 O  O   . ALA A 1 206 ? 5.890  31.303  5.587   1.00 16.39  ? 201 ALA B O   1 
ATOM   1617 C  CB  . ALA A 1 206 ? 8.044  29.298  7.097   1.00 16.49  ? 201 ALA B CB  1 
ATOM   1618 N  N   . MET A 1 207 ? 5.129  30.379  7.497   1.00 16.54  ? 202 MET B N   1 
ATOM   1619 C  CA  . MET A 1 207 ? 3.719  30.460  7.131   1.00 17.08  ? 202 MET B CA  1 
ATOM   1620 C  C   . MET A 1 207 ? 3.357  31.871  6.673   1.00 16.67  ? 202 MET B C   1 
ATOM   1621 O  O   . MET A 1 207 ? 2.704  32.045  5.642   1.00 17.25  ? 202 MET B O   1 
ATOM   1622 C  CB  . MET A 1 207 ? 2.858  30.059  8.346   1.00 19.14  ? 202 MET B CB  1 
ATOM   1623 C  CG  . MET A 1 207 ? 1.391  30.143  8.136   1.00 27.06  ? 202 MET B CG  1 
ATOM   1624 S  SD  . MET A 1 207 ? 0.772  28.983  6.906   1.00 39.48  ? 202 MET B SD  1 
ATOM   1625 C  CE  . MET A 1 207 ? 1.659  27.685  7.287   1.00 19.20  ? 202 MET B CE  1 
ATOM   1626 N  N   . ALA A 1 208 ? 3.808  32.873  7.431   1.00 16.56  ? 203 ALA B N   1 
ATOM   1627 C  CA  . ALA A 1 208 ? 3.482  34.265  7.163   1.00 16.89  ? 203 ALA B CA  1 
ATOM   1628 C  C   . ALA A 1 208 ? 4.146  34.844  5.916   1.00 17.24  ? 203 ALA B C   1 
ATOM   1629 O  O   . ALA A 1 208 ? 3.778  35.927  5.476   1.00 18.63  ? 203 ALA B O   1 
ATOM   1630 C  CB  . ALA A 1 208 ? 3.845  35.107  8.375   1.00 20.19  ? 203 ALA B CB  1 
ATOM   1631 N  N   . ASP A 1 209 ? 5.145  34.137  5.355   1.00 15.74  ? 204 ASP B N   1 
ATOM   1632 C  CA  . ASP A 1 209 ? 5.856  34.597  4.171   1.00 17.19  ? 204 ASP B CA  1 
ATOM   1633 C  C   . ASP A 1 209 ? 5.530  33.799  2.900   1.00 17.17  ? 204 ASP B C   1 
ATOM   1634 O  O   . ASP A 1 209 ? 5.983  34.158  1.813   1.00 19.61  ? 204 ASP B O   1 
ATOM   1635 C  CB  . ASP A 1 209 ? 7.374  34.550  4.472   1.00 21.66  ? 204 ASP B CB  1 
ATOM   1636 C  CG  . ASP A 1 209 ? 8.357  35.155  3.470   1.00 26.45  ? 204 ASP B CG  1 
ATOM   1637 O  OD1 . ASP A 1 209 ? 8.341  36.372  3.302   1.00 29.20  ? 204 ASP B OD1 1 
ATOM   1638 O  OD2 . ASP A 1 209 ? 9.229  34.380  2.908   1.00 31.49  ? 204 ASP B OD2 1 
ATOM   1639 N  N   . LEU A 1 210 ? 4.695  32.765  3.020   1.00 15.79  ? 205 LEU B N   1 
ATOM   1640 C  CA  . LEU A 1 210 ? 4.321  31.941  1.874   1.00 17.95  ? 205 LEU B CA  1 
ATOM   1641 C  C   . LEU A 1 210 ? 3.670  32.749  0.749   1.00 19.78  ? 205 LEU B C   1 
ATOM   1642 O  O   . LEU A 1 210 ? 3.835  32.412  -0.421  1.00 20.02  ? 205 LEU B O   1 
ATOM   1643 C  CB  . LEU A 1 210 ? 3.401  30.824  2.279   1.00 16.73  ? 205 LEU B CB  1 
ATOM   1644 C  CG  . LEU A 1 210 ? 4.034  29.722  3.150   1.00 19.31  ? 205 LEU B CG  1 
ATOM   1645 C  CD1 . LEU A 1 210 ? 3.021  28.766  3.560   1.00 18.00  ? 205 LEU B CD1 1 
ATOM   1646 C  CD2 . LEU A 1 210 ? 5.153  28.967  2.396   1.00 19.61  ? 205 LEU B CD2 1 
ATOM   1647 N  N   . HIS A 1 211 ? 2.976  33.831  1.104   1.00 18.69  ? 206 HIS B N   1 
ATOM   1648 C  CA  . HIS A 1 211 ? 2.218  34.622  0.134   1.00 20.04  ? 206 HIS B CA  1 
ATOM   1649 C  C   . HIS A 1 211 ? 3.112  35.258  -0.930  1.00 23.72  ? 206 HIS B C   1 
ATOM   1650 O  O   . HIS A 1 211 ? 2.606  35.665  -1.979  1.00 24.24  ? 206 HIS B O   1 
ATOM   1651 C  CB  . HIS A 1 211 ? 1.366  35.695  0.834   1.00 19.76  ? 206 HIS B CB  1 
ATOM   1652 C  CG  . HIS A 1 211 ? 2.137  36.866  1.334   1.00 19.96  ? 206 HIS B CG  1 
ATOM   1653 N  ND1 . HIS A 1 211 ? 2.712  36.949  2.590   1.00 22.06  ? 206 HIS B ND1 1 
ATOM   1654 C  CD2 . HIS A 1 211 ? 2.417  38.026  0.727   1.00 20.64  ? 206 HIS B CD2 1 
ATOM   1655 C  CE1 . HIS A 1 211 ? 3.332  38.115  2.705   1.00 21.32  ? 206 HIS B CE1 1 
ATOM   1656 N  NE2 . HIS A 1 211 ? 3.177  38.767  1.583   1.00 26.78  ? 206 HIS B NE2 1 
ATOM   1657 N  N   . THR A 1 212 ? 4.418  35.385  -0.638  1.00 20.27  ? 207 THR B N   1 
ATOM   1658 C  CA  . THR A 1 212 ? 5.369  36.038  -1.527  1.00 21.15  ? 207 THR B CA  1 
ATOM   1659 C  C   . THR A 1 212 ? 5.889  35.123  -2.625  1.00 19.73  ? 207 THR B C   1 
ATOM   1660 O  O   . THR A 1 212 ? 6.583  35.606  -3.514  1.00 22.52  ? 207 THR B O   1 
ATOM   1661 C  CB  . THR A 1 212 ? 6.568  36.590  -0.740  1.00 19.30  ? 207 THR B CB  1 
ATOM   1662 O  OG1 . THR A 1 212 ? 7.299  35.475  -0.196  1.00 19.98  ? 207 THR B OG1 1 
ATOM   1663 C  CG2 . THR A 1 212 ? 6.143  37.537  0.355   1.00 21.43  ? 207 THR B CG2 1 
ATOM   1664 N  N   . LEU A 1 213 ? 5.600  33.825  -2.514  1.00 18.99  ? 208 LEU B N   1 
ATOM   1665 C  CA  . LEU A 1 213 ? 6.264  32.812  -3.305  1.00 21.93  ? 208 LEU B CA  1 
ATOM   1666 C  C   . LEU A 1 213 ? 5.477  32.428  -4.552  1.00 23.58  ? 208 LEU B C   1 
ATOM   1667 O  O   . LEU A 1 213 ? 4.244  32.468  -4.564  1.00 22.82  ? 208 LEU B O   1 
ATOM   1668 C  CB  . LEU A 1 213 ? 6.470  31.563  -2.481  1.00 22.30  ? 208 LEU B CB  1 
ATOM   1669 C  CG  . LEU A 1 213 ? 7.295  31.755  -1.214  1.00 19.44  ? 208 LEU B CG  1 
ATOM   1670 C  CD1 . LEU A 1 213 ? 7.451  30.445  -0.534  1.00 20.16  ? 208 LEU B CD1 1 
ATOM   1671 C  CD2 . LEU A 1 213 ? 8.636  32.391  -1.512  1.00 21.69  ? 208 LEU B CD2 1 
ATOM   1672 N  N   . SER A 1 214 ? 6.224  32.020  -5.581  1.00 21.94  ? 209 SER B N   1 
ATOM   1673 C  CA  . SER A 1 214 ? 5.663  31.301  -6.708  1.00 22.38  ? 209 SER B CA  1 
ATOM   1674 C  C   . SER A 1 214 ? 5.151  29.917  -6.328  1.00 23.79  ? 209 SER B C   1 
ATOM   1675 O  O   . SER A 1 214 ? 5.454  29.398  -5.242  1.00 24.18  ? 209 SER B O   1 
ATOM   1676 C  CB  . SER A 1 214 ? 6.718  31.127  -7.805  1.00 21.87  ? 209 SER B CB  1 
ATOM   1677 O  OG  . SER A 1 214 ? 7.717  30.237  -7.322  1.00 23.85  ? 209 SER B OG  1 
ATOM   1678 N  N   . GLU A 1 215 ? 4.407  29.297  -7.254  1.00 22.76  ? 210 GLU B N   1 
ATOM   1679 C  CA  A GLU A 1 215 ? 3.888  27.955  -7.051  0.50 26.07  ? 210 GLU B CA  1 
ATOM   1680 C  CA  B GLU A 1 215 ? 3.882  27.958  -7.017  0.50 27.82  ? 210 GLU B CA  1 
ATOM   1681 C  C   . GLU A 1 215 ? 5.004  26.961  -6.721  1.00 30.51  ? 210 GLU B C   1 
ATOM   1682 O  O   . GLU A 1 215 ? 4.882  26.143  -5.805  1.00 26.79  ? 210 GLU B O   1 
ATOM   1683 C  CB  A GLU A 1 215 ? 3.137  27.528  -8.316  0.50 30.57  ? 210 GLU B CB  1 
ATOM   1684 C  CB  B GLU A 1 215 ? 3.009  27.475  -8.198  0.50 34.81  ? 210 GLU B CB  1 
ATOM   1685 C  CG  A GLU A 1 215 ? 2.298  26.279  -8.161  0.50 33.07  ? 210 GLU B CG  1 
ATOM   1686 C  CG  B GLU A 1 215 ? 2.839  25.957  -8.336  0.50 41.49  ? 210 GLU B CG  1 
ATOM   1687 C  CD  A GLU A 1 215 ? 1.576  25.905  -9.437  0.50 33.38  ? 210 GLU B CD  1 
ATOM   1688 C  CD  B GLU A 1 215 ? 2.359  25.156  -7.132  0.50 44.96  ? 210 GLU B CD  1 
ATOM   1689 O  OE1 A GLU A 1 215 ? 1.778  26.597  -10.459 0.50 35.39  ? 210 GLU B OE1 1 
ATOM   1690 O  OE1 B GLU A 1 215 ? 2.230  25.718  -6.020  0.50 50.22  ? 210 GLU B OE1 1 
ATOM   1691 O  OE2 A GLU A 1 215 ? 0.816  24.915  -9.417  0.50 37.06  ? 210 GLU B OE2 1 
ATOM   1692 O  OE2 B GLU A 1 215 ? 2.123  23.940  -7.311  0.50 57.44  ? 210 GLU B OE2 1 
ATOM   1693 N  N   . ASP A 1 216 ? 6.109  27.033  -7.477  1.00 26.34  ? 211 ASP B N   1 
ATOM   1694 C  CA  . ASP A 1 216 ? 7.205  26.099  -7.268  1.00 26.03  ? 211 ASP B CA  1 
ATOM   1695 C  C   . ASP A 1 216 ? 7.928  26.307  -5.939  1.00 25.19  ? 211 ASP B C   1 
ATOM   1696 O  O   . ASP A 1 216 ? 8.218  25.329  -5.250  1.00 25.95  ? 211 ASP B O   1 
ATOM   1697 C  CB  . ASP A 1 216 ? 8.208  26.175  -8.414  1.00 30.49  ? 211 ASP B CB  1 
ATOM   1698 C  CG  . ASP A 1 216 ? 7.683  25.601  -9.734  1.00 40.61  ? 211 ASP B CG  1 
ATOM   1699 O  OD1 . ASP A 1 216 ? 6.498  25.163  -9.781  1.00 44.97  ? 211 ASP B OD1 1 
ATOM   1700 O  OD2 . ASP A 1 216 ? 8.439  25.589  -10.703 1.00 44.91  ? 211 ASP B OD2 1 
ATOM   1701 N  N   . SER A 1 217 ? 8.191  27.570  -5.576  1.00 23.75  ? 212 SER B N   1 
ATOM   1702 C  CA  . SER A 1 217 ? 8.850  27.874  -4.314  1.00 21.86  ? 212 SER B CA  1 
ATOM   1703 C  C   . SER A 1 217 ? 7.950  27.514  -3.124  1.00 25.62  ? 212 SER B C   1 
ATOM   1704 O  O   . SER A 1 217 ? 8.404  26.981  -2.105  1.00 19.79  ? 212 SER B O   1 
ATOM   1705 C  CB  . SER A 1 217 ? 9.284  29.328  -4.273  1.00 25.02  ? 212 SER B CB  1 
ATOM   1706 O  OG  . SER A 1 217 ? 10.231 29.639  -5.295  1.00 23.75  ? 212 SER B OG  1 
ATOM   1707 N  N   . TYR A 1 218 ? 6.642  27.722  -3.297  1.00 23.19  ? 213 TYR B N   1 
ATOM   1708 C  CA  . TYR A 1 218 ? 5.674  27.331  -2.286  1.00 21.44  ? 213 TYR B CA  1 
ATOM   1709 C  C   . TYR A 1 218 ? 5.751  25.842  -1.973  1.00 24.97  ? 213 TYR B C   1 
ATOM   1710 O  O   . TYR A 1 218 ? 5.755  25.428  -0.811  1.00 22.52  ? 213 TYR B O   1 
ATOM   1711 C  CB  . TYR A 1 218 ? 4.280  27.685  -2.783  1.00 24.35  ? 213 TYR B CB  1 
ATOM   1712 C  CG  . TYR A 1 218 ? 3.164  27.439  -1.807  1.00 25.43  ? 213 TYR B CG  1 
ATOM   1713 C  CD1 . TYR A 1 218 ? 2.450  26.241  -1.814  1.00 29.69  ? 213 TYR B CD1 1 
ATOM   1714 C  CD2 . TYR A 1 218 ? 2.732  28.450  -0.966  1.00 25.50  ? 213 TYR B CD2 1 
ATOM   1715 C  CE1 . TYR A 1 218 ? 1.368  26.044  -0.937  1.00 29.93  ? 213 TYR B CE1 1 
ATOM   1716 C  CE2 . TYR A 1 218 ? 1.680  28.261  -0.086  1.00 35.86  ? 213 TYR B CE2 1 
ATOM   1717 C  CZ  . TYR A 1 218 ? 1.012  27.058  -0.062  1.00 25.27  ? 213 TYR B CZ  1 
ATOM   1718 O  OH  . TYR A 1 218 ? -0.034 27.008  0.842   1.00 30.20  ? 213 TYR B OH  1 
ATOM   1719 N  N   . LYS A 1 219 ? 5.799  25.022  -3.028  1.00 24.66  ? 214 LYS B N   1 
ATOM   1720 C  CA  . LYS A 1 219 ? 5.903  23.587  -2.835  1.00 27.28  ? 214 LYS B CA  1 
ATOM   1721 C  C   . LYS A 1 219 ? 7.184  23.210  -2.087  1.00 28.66  ? 214 LYS B C   1 
ATOM   1722 O  O   . LYS A 1 219 ? 7.143  22.411  -1.155  1.00 27.65  ? 214 LYS B O   1 
ATOM   1723 C  CB  . LYS A 1 219 ? 5.777  22.863  -4.206  1.00 34.93  ? 214 LYS B CB  1 
ATOM   1724 C  CG  . LYS A 1 219 ? 4.340  22.905  -4.775  1.00 48.15  ? 214 LYS B CG  1 
ATOM   1725 C  CD  . LYS A 1 219 ? 3.313  22.084  -3.935  1.00 59.60  ? 214 LYS B CD  1 
ATOM   1726 C  CE  . LYS A 1 219 ? 1.894  22.611  -4.004  1.00 64.39  ? 214 LYS B CE  1 
ATOM   1727 N  NZ  . LYS A 1 219 ? 1.271  22.357  -5.327  1.00 71.79  ? 214 LYS B NZ  1 
ATOM   1728 N  N   . ASP A 1 220 ? 8.312  23.803  -2.478  1.00 25.00  ? 215 ASP B N   1 
ATOM   1729 C  CA  . ASP A 1 220 ? 9.581  23.581  -1.792  1.00 26.67  ? 215 ASP B CA  1 
ATOM   1730 C  C   . ASP A 1 220 ? 9.558  23.889  -0.289  1.00 26.05  ? 215 ASP B C   1 
ATOM   1731 O  O   . ASP A 1 220 ? 10.050 23.116  0.536   1.00 22.57  ? 215 ASP B O   1 
ATOM   1732 C  CB  . ASP A 1 220 ? 10.659 24.456  -2.417  1.00 28.72  ? 215 ASP B CB  1 
ATOM   1733 C  CG  . ASP A 1 220 ? 11.117 24.074  -3.822  1.00 37.18  ? 215 ASP B CG  1 
ATOM   1734 O  OD1 . ASP A 1 220 ? 10.913 22.918  -4.214  1.00 33.27  ? 215 ASP B OD1 1 
ATOM   1735 O  OD2 . ASP A 1 220 ? 11.657 24.956  -4.525  1.00 44.17  ? 215 ASP B OD2 1 
ATOM   1736 N  N   . SER A 1 221 ? 9.032  25.069  0.062   1.00 22.81  ? 216 SER B N   1 
ATOM   1737 C  CA  . SER A 1 221 ? 9.021  25.530  1.443   1.00 20.53  ? 216 SER B CA  1 
ATOM   1738 C  C   . SER A 1 221 ? 8.061  24.707  2.301   1.00 21.39  ? 216 SER B C   1 
ATOM   1739 O  O   . SER A 1 221 ? 8.403  24.304  3.414   1.00 22.16  ? 216 SER B O   1 
ATOM   1740 C  CB  . SER A 1 221 ? 8.678  27.019  1.495   1.00 20.16  ? 216 SER B CB  1 
ATOM   1741 O  OG  . SER A 1 221 ? 9.698  27.791  0.869   1.00 20.77  ? 216 SER B OG  1 
ATOM   1742 N  N   . THR A 1 222 ? 6.862  24.427  1.766   1.00 21.85  ? 217 THR B N   1 
ATOM   1743 C  CA  . THR A 1 222 ? 5.836  23.746  2.541   1.00 21.47  ? 217 THR B CA  1 
ATOM   1744 C  C   . THR A 1 222 ? 6.257  22.304  2.798   1.00 21.02  ? 217 THR B C   1 
ATOM   1745 O  O   . THR A 1 222 ? 5.940  21.727  3.843   1.00 22.47  ? 217 THR B O   1 
ATOM   1746 C  CB  . THR A 1 222 ? 4.448  23.861  1.901   1.00 23.02  ? 217 THR B CB  1 
ATOM   1747 O  OG1 . THR A 1 222 ? 4.494  23.370  0.564   1.00 25.38  ? 217 THR B OG1 1 
ATOM   1748 C  CG2 . THR A 1 222 ? 3.925  25.273  1.912   1.00 24.69  ? 217 THR B CG2 1 
ATOM   1749 N  N   . LEU A 1 223 ? 7.038  21.723  1.884   1.00 24.61  ? 218 LEU B N   1 
ATOM   1750 C  CA  . LEU A 1 223 ? 7.565  20.389  2.159   1.00 26.26  ? 218 LEU B CA  1 
ATOM   1751 C  C   . LEU A 1 223 ? 8.367  20.345  3.458   1.00 25.84  ? 218 LEU B C   1 
ATOM   1752 O  O   . LEU A 1 223 ? 8.203  19.452  4.291   1.00 25.49  ? 218 LEU B O   1 
ATOM   1753 C  CB  . LEU A 1 223 ? 8.431  19.894  0.983   1.00 29.93  ? 218 LEU B CB  1 
ATOM   1754 C  CG  . LEU A 1 223 ? 8.948  18.448  1.101   1.00 39.18  ? 218 LEU B CG  1 
ATOM   1755 C  CD1 . LEU A 1 223 ? 9.310  17.895  -0.255  1.00 41.84  ? 218 LEU B CD1 1 
ATOM   1756 C  CD2 . LEU A 1 223 ? 10.169 18.338  2.024   1.00 44.40  ? 218 LEU B CD2 1 
ATOM   1757 N  N   . ILE A 1 224 ? 9.257  21.313  3.663   1.00 24.02  ? 219 ILE B N   1 
ATOM   1758 C  CA  . ILE A 1 224 ? 10.080 21.306  4.865   1.00 21.53  ? 219 ILE B CA  1 
ATOM   1759 C  C   . ILE A 1 224 ? 9.281  21.702  6.102   1.00 19.33  ? 219 ILE B C   1 
ATOM   1760 O  O   . ILE A 1 224 ? 9.513  21.234  7.206   1.00 19.63  ? 219 ILE B O   1 
ATOM   1761 C  CB  . ILE A 1 224 ? 11.305 22.236  4.687   1.00 24.70  ? 219 ILE B CB  1 
ATOM   1762 C  CG1 . ILE A 1 224 ? 12.098 21.879  3.407   1.00 31.83  ? 219 ILE B CG1 1 
ATOM   1763 C  CG2 . ILE A 1 224 ? 12.175 22.176  5.918   1.00 26.56  ? 219 ILE B CG2 1 
ATOM   1764 C  CD1 . ILE A 1 224 ? 12.848 23.053  2.749   1.00 32.39  ? 219 ILE B CD1 1 
ATOM   1765 N  N   . MET A 1 225 ? 8.324  22.612  5.910   1.00 20.02  ? 220 MET B N   1 
ATOM   1766 C  CA  . MET A 1 225 ? 7.466  22.998  7.014   1.00 19.60  ? 220 MET B CA  1 
ATOM   1767 C  C   . MET A 1 225 ? 6.717  21.789  7.572   1.00 18.54  ? 220 MET B C   1 
ATOM   1768 O  O   . MET A 1 225 ? 6.474  21.678  8.775   1.00 17.64  ? 220 MET B O   1 
ATOM   1769 C  CB  . MET A 1 225 ? 6.480  24.067  6.522   1.00 18.34  ? 220 MET B CB  1 
ATOM   1770 C  CG  . MET A 1 225 ? 7.129  25.382  6.296   1.00 18.27  ? 220 MET B CG  1 
ATOM   1771 S  SD  . MET A 1 225 ? 6.024  26.589  5.457   1.00 21.94  ? 220 MET B SD  1 
ATOM   1772 C  CE  . MET A 1 225 ? 4.879  26.835  6.701   1.00 22.17  ? 220 MET B CE  1 
ATOM   1773 N  N   . GLN A 1 226 ? 6.323  20.862  6.685   1.00 18.79  ? 221 GLN B N   1 
ATOM   1774 C  CA  . GLN A 1 226 ? 5.648  19.665  7.135   1.00 18.17  ? 221 GLN B CA  1 
ATOM   1775 C  C   . GLN A 1 226 ? 6.520  18.827  8.068   1.00 19.36  ? 221 GLN B C   1 
ATOM   1776 O  O   . GLN A 1 226 ? 6.035  18.267  9.045   1.00 17.98  ? 221 GLN B O   1 
ATOM   1777 C  CB  . GLN A 1 226 ? 5.182  18.802  5.925   1.00 25.83  ? 221 GLN B CB  1 
ATOM   1778 C  CG  . GLN A 1 226 ? 4.353  17.573  6.329   1.00 29.41  ? 221 GLN B CG  1 
ATOM   1779 C  CD  . GLN A 1 226 ? 3.098  17.936  7.102   1.00 36.06  ? 221 GLN B CD  1 
ATOM   1780 O  OE1 . GLN A 1 226 ? 2.307  18.767  6.661   1.00 40.50  ? 221 GLN B OE1 1 
ATOM   1781 N  NE2 . GLN A 1 226 ? 2.893  17.352  8.279   1.00 29.99  ? 221 GLN B NE2 1 
ATOM   1782 N  N   . LEU A 1 227 ? 7.833  18.787  7.801   1.00 18.48  ? 222 LEU B N   1 
ATOM   1783 C  CA  . LEU A 1 227 ? 8.731  18.109  8.722   1.00 19.01  ? 222 LEU B CA  1 
ATOM   1784 C  C   . LEU A 1 227 ? 8.843  18.750  10.107  1.00 17.88  ? 222 LEU B C   1 
ATOM   1785 O  O   . LEU A 1 227 ? 8.939  18.059  11.120  1.00 17.70  ? 222 LEU B O   1 
ATOM   1786 C  CB  . LEU A 1 227 ? 10.132 18.022  8.093   1.00 21.26  ? 222 LEU B CB  1 
ATOM   1787 C  CG  . LEU A 1 227 ? 10.186 17.274  6.787   1.00 27.06  ? 222 LEU B CG  1 
ATOM   1788 C  CD1 . LEU A 1 227 ? 11.588 17.256  6.243   1.00 27.54  ? 222 LEU B CD1 1 
ATOM   1789 C  CD2 . LEU A 1 227 ? 9.679  15.875  6.947   1.00 30.68  ? 222 LEU B CD2 1 
ATOM   1790 N  N   . LEU A 1 228 ? 8.822  20.094  10.157  1.00 17.49  ? 223 LEU B N   1 
ATOM   1791 C  CA  . LEU A 1 228 ? 8.748  20.774  11.430  1.00 16.39  ? 223 LEU B CA  1 
ATOM   1792 C  C   . LEU A 1 228 ? 7.484  20.353  12.174  1.00 17.68  ? 223 LEU B C   1 
ATOM   1793 O  O   . LEU A 1 228 ? 7.522  20.043  13.360  1.00 18.72  ? 223 LEU B O   1 
ATOM   1794 C  CB  . LEU A 1 228 ? 8.779  22.303  11.217  1.00 17.02  ? 223 LEU B CB  1 
ATOM   1795 C  CG  . LEU A 1 228 ? 10.071 22.895  10.675  1.00 17.45  ? 223 LEU B CG  1 
ATOM   1796 C  CD1 . LEU A 1 228 ? 9.835  24.293  10.113  1.00 19.32  ? 223 LEU B CD1 1 
ATOM   1797 C  CD2 . LEU A 1 228 ? 11.149 22.977  11.760  1.00 18.10  ? 223 LEU B CD2 1 
ATOM   1798 N  N   . ARG A 1 229 ? 6.349  20.369  11.463  1.00 18.45  ? 224 ARG B N   1 
ATOM   1799 C  CA  . ARG A 1 229 ? 5.082  19.961  12.053  1.00 19.18  ? 224 ARG B CA  1 
ATOM   1800 C  C   . ARG A 1 229 ? 5.087  18.499  12.518  1.00 18.91  ? 224 ARG B C   1 
ATOM   1801 O  O   . ARG A 1 229 ? 4.631  18.201  13.611  1.00 20.42  ? 224 ARG B O   1 
ATOM   1802 C  CB  . ARG A 1 229 ? 3.952  20.197  11.035  1.00 23.82  ? 224 ARG B CB  1 
ATOM   1803 C  CG  . ARG A 1 229 ? 2.557  19.704  11.456  1.00 34.56  ? 224 ARG B CG  1 
ATOM   1804 C  CD  . ARG A 1 229 ? 2.068  20.350  12.742  1.00 46.50  ? 224 ARG B CD  1 
ATOM   1805 N  NE  . ARG A 1 229 ? 2.046  21.809  12.667  1.00 47.06  ? 224 ARG B NE  1 
ATOM   1806 C  CZ  . ARG A 1 229 ? 2.129  22.624  13.717  1.00 59.45  ? 224 ARG B CZ  1 
ATOM   1807 N  NH1 . ARG A 1 229 ? 2.094  22.164  14.960  1.00 57.59  ? 224 ARG B NH1 1 
ATOM   1808 N  NH2 . ARG A 1 229 ? 2.258  23.933  13.515  1.00 54.42  ? 224 ARG B NH2 1 
ATOM   1809 N  N   . ASP A 1 230 ? 5.662  17.592  11.726  1.00 19.80  ? 225 ASP B N   1 
ATOM   1810 C  CA  . ASP A 1 230 ? 5.751  16.198  12.130  1.00 18.54  ? 225 ASP B CA  1 
ATOM   1811 C  C   . ASP A 1 230 ? 6.554  16.040  13.421  1.00 18.80  ? 225 ASP B C   1 
ATOM   1812 O  O   . ASP A 1 230 ? 6.191  15.267  14.305  1.00 20.54  ? 225 ASP B O   1 
ATOM   1813 C  CB  . ASP A 1 230 ? 6.407  15.353  11.043  1.00 21.76  ? 225 ASP B CB  1 
ATOM   1814 C  CG  . ASP A 1 230 ? 5.719  15.145  9.721   1.00 27.45  ? 225 ASP B CG  1 
ATOM   1815 O  OD1 . ASP A 1 230 ? 4.469  15.349  9.650   1.00 26.93  ? 225 ASP B OD1 1 
ATOM   1816 O  OD2 . ASP A 1 230 ? 6.435  14.782  8.739   1.00 28.83  ? 225 ASP B OD2 1 
ATOM   1817 N  N   . ASN A 1 231 ? 7.671  16.774  13.545  1.00 18.10  ? 226 ASN B N   1 
ATOM   1818 C  CA  . ASN A 1 231 ? 8.435  16.736  14.776  1.00 16.83  ? 226 ASN B CA  1 
ATOM   1819 C  C   . ASN A 1 231 ? 7.638  17.323  15.940  1.00 18.62  ? 226 ASN B C   1 
ATOM   1820 O  O   . ASN A 1 231 ? 7.625  16.770  17.029  1.00 18.87  ? 226 ASN B O   1 
ATOM   1821 C  CB  . ASN A 1 231 ? 9.785  17.456  14.618  1.00 15.64  ? 226 ASN B CB  1 
ATOM   1822 C  CG  . ASN A 1 231 ? 10.803 16.649  13.858  1.00 18.32  ? 226 ASN B CG  1 
ATOM   1823 O  OD1 . ASN A 1 231 ? 10.672 15.401  13.735  1.00 18.36  ? 226 ASN B OD1 1 
ATOM   1824 N  ND2 . ASN A 1 231 ? 11.849 17.329  13.354  1.00 16.78  ? 226 ASN B ND2 1 
ATOM   1825 N  N   . LEU A 1 232 ? 6.994  18.471  15.728  1.00 17.90  ? 227 LEU B N   1 
ATOM   1826 C  CA  . LEU A 1 232 ? 6.217  19.044  16.810  1.00 18.55  ? 227 LEU B CA  1 
ATOM   1827 C  C   . LEU A 1 232 ? 5.136  18.080  17.299  1.00 19.59  ? 227 LEU B C   1 
ATOM   1828 O  O   . LEU A 1 232 ? 4.925  17.994  18.499  1.00 22.93  ? 227 LEU B O   1 
ATOM   1829 C  CB  . LEU A 1 232 ? 5.629  20.365  16.350  1.00 17.66  ? 227 LEU B CB  1 
ATOM   1830 C  CG  . LEU A 1 232 ? 6.587  21.531  16.348  1.00 18.92  ? 227 LEU B CG  1 
ATOM   1831 C  CD1 . LEU A 1 232 ? 5.992  22.676  15.544  1.00 22.09  ? 227 LEU B CD1 1 
ATOM   1832 C  CD2 . LEU A 1 232 ? 6.934  21.911  17.728  1.00 18.16  ? 227 LEU B CD2 1 
ATOM   1833 N  N   . THR A 1 233 ? 4.540  17.312  16.373  1.00 21.60  ? 228 THR B N   1 
ATOM   1834 C  CA  . THR A 1 233 ? 3.547  16.298  16.735  1.00 23.13  ? 228 THR B CA  1 
ATOM   1835 C  C   . THR A 1 233 ? 4.175  15.178  17.578  1.00 28.58  ? 228 THR B C   1 
ATOM   1836 O  O   . THR A 1 233 ? 3.581  14.680  18.541  1.00 28.01  ? 228 THR B O   1 
ATOM   1837 C  CB  . THR A 1 233 ? 2.868  15.757  15.474  1.00 22.66  ? 228 THR B CB  1 
ATOM   1838 O  OG1 . THR A 1 233 ? 2.249  16.831  14.784  1.00 25.25  ? 228 THR B OG1 1 
ATOM   1839 C  CG2 . THR A 1 233 ? 1.835  14.636  15.790  1.00 29.18  ? 228 THR B CG2 1 
ATOM   1840 N  N   . LEU A 1 234 ? 5.408  14.795  17.229  1.00 24.74  ? 229 LEU B N   1 
ATOM   1841 C  CA  . LEU A 1 234 ? 6.126  13.767  17.955  1.00 26.24  ? 229 LEU B CA  1 
ATOM   1842 C  C   . LEU A 1 234 ? 6.491  14.270  19.346  1.00 27.78  ? 229 LEU B C   1 
ATOM   1843 O  O   . LEU A 1 234 ? 6.430  13.510  20.308  1.00 28.34  ? 229 LEU B O   1 
ATOM   1844 C  CB  . LEU A 1 234 ? 7.389  13.368  17.176  1.00 27.16  ? 229 LEU B CB  1 
ATOM   1845 C  CG  . LEU A 1 234 ? 8.294  12.329  17.827  1.00 30.95  ? 229 LEU B CG  1 
ATOM   1846 C  CD1 . LEU A 1 234 ? 7.612  10.963  17.853  1.00 34.26  ? 229 LEU B CD1 1 
ATOM   1847 C  CD2 . LEU A 1 234 ? 9.635  12.256  17.107  1.00 36.10  ? 229 LEU B CD2 1 
ATOM   1848 N  N   . TRP A 1 235 ? 6.865  15.553  19.447  1.00 23.12  ? 230 TRP B N   1 
ATOM   1849 C  CA  . TRP A 1 235 ? 7.459  16.101  20.655  1.00 22.72  ? 230 TRP B CA  1 
ATOM   1850 C  C   . TRP A 1 235 ? 6.455  16.635  21.680  1.00 27.48  ? 230 TRP B C   1 
ATOM   1851 O  O   . TRP A 1 235 ? 6.834  16.910  22.817  1.00 26.78  ? 230 TRP B O   1 
ATOM   1852 C  CB  . TRP A 1 235 ? 8.400  17.249  20.288  1.00 22.55  ? 230 TRP B CB  1 
ATOM   1853 C  CG  . TRP A 1 235 ? 9.590  16.850  19.473  1.00 19.99  ? 230 TRP B CG  1 
ATOM   1854 C  CD1 . TRP A 1 235 ? 10.079 15.599  19.254  1.00 20.93  ? 230 TRP B CD1 1 
ATOM   1855 C  CD2 . TRP A 1 235 ? 10.403 17.746  18.696  1.00 19.01  ? 230 TRP B CD2 1 
ATOM   1856 N  NE1 . TRP A 1 235 ? 11.188 15.663  18.430  1.00 18.65  ? 230 TRP B NE1 1 
ATOM   1857 C  CE2 . TRP A 1 235 ? 11.408 16.979  18.084  1.00 17.77  ? 230 TRP B CE2 1 
ATOM   1858 C  CE3 . TRP A 1 235 ? 10.388 19.129  18.483  1.00 19.24  ? 230 TRP B CE3 1 
ATOM   1859 C  CZ2 . TRP A 1 235 ? 12.405 17.563  17.288  1.00 18.10  ? 230 TRP B CZ2 1 
ATOM   1860 C  CZ3 . TRP A 1 235 ? 11.372 19.694  17.691  1.00 18.01  ? 230 TRP B CZ3 1 
ATOM   1861 C  CH2 . TRP A 1 235 ? 12.367 18.904  17.118  1.00 18.37  ? 230 TRP B CH2 1 
ATOM   1862 N  N   . THR A 1 236 ? 5.205  16.835  21.247  1.00 29.83  ? 231 THR B N   1 
ATOM   1863 C  CA  . THR A 1 236 ? 4.161  17.405  22.086  1.00 34.08  ? 231 THR B CA  1 
ATOM   1864 C  C   . THR A 1 236 ? 2.891  16.535  22.071  1.00 44.37  ? 231 THR B C   1 
ATOM   1865 O  O   . THR A 1 236 ? 1.859  16.961  22.593  1.00 49.33  ? 231 THR B O   1 
ATOM   1866 C  CB  . THR A 1 236 ? 3.825  18.839  21.638  1.00 31.64  ? 231 THR B CB  1 
ATOM   1867 O  OG1 . THR A 1 236 ? 3.158  18.779  20.371  1.00 32.75  ? 231 THR B OG1 1 
ATOM   1868 C  CG2 . THR A 1 236 ? 5.056  19.724  21.548  1.00 32.88  ? 231 THR B CG2 1 
ATOM   1869 O  OXT . THR A 1 236 ? 2.893  15.420  21.548  1.00 43.20  ? 231 THR B OXT 1 
ATOM   1870 N  N   . ASP B 2 1   ? 9.907  6.535   17.968  1.00 77.55  ? 255 ASP P N   1 
ATOM   1871 C  CA  . ASP B 2 1   ? 10.701 6.822   16.772  1.00 76.54  ? 255 ASP P CA  1 
ATOM   1872 C  C   . ASP B 2 1   ? 11.447 8.149   16.898  1.00 63.87  ? 255 ASP P C   1 
ATOM   1873 O  O   . ASP B 2 1   ? 11.071 9.026   17.671  1.00 57.68  ? 255 ASP P O   1 
ATOM   1874 C  CB  . ASP B 2 1   ? 9.829  6.810   15.498  1.00 76.00  ? 255 ASP P CB  1 
ATOM   1875 C  CG  . ASP B 2 1   ? 8.514  7.550   15.620  1.00 74.04  ? 255 ASP P CG  1 
ATOM   1876 O  OD1 . ASP B 2 1   ? 8.203  8.020   16.727  1.00 77.56  ? 255 ASP P OD1 1 
ATOM   1877 O  OD2 . ASP B 2 1   ? 7.790  7.647   14.606  1.00 62.45  ? 255 ASP P OD2 1 
ATOM   1878 N  N   . ARG B 2 2   ? 12.524 8.268   16.123  1.00 47.37  ? 256 ARG P N   1 
ATOM   1879 C  CA  . ARG B 2 2   ? 13.417 9.407   16.205  1.00 43.15  ? 256 ARG P CA  1 
ATOM   1880 C  C   . ARG B 2 2   ? 12.818 10.608  15.479  1.00 33.88  ? 256 ARG P C   1 
ATOM   1881 O  O   . ARG B 2 2   ? 11.958 10.471  14.615  1.00 33.50  ? 256 ARG P O   1 
ATOM   1882 C  CB  . ARG B 2 2   ? 14.787 9.069   15.595  1.00 42.83  ? 256 ARG P CB  1 
ATOM   1883 C  CG  . ARG B 2 2   ? 15.575 8.044   16.384  1.00 54.97  ? 256 ARG P CG  1 
ATOM   1884 C  CD  . ARG B 2 2   ? 16.740 7.504   15.575  1.00 55.36  ? 256 ARG P CD  1 
ATOM   1885 N  NE  . ARG B 2 2   ? 17.410 6.409   16.268  1.00 63.20  ? 256 ARG P NE  1 
ATOM   1886 C  CZ  . ARG B 2 2   ? 18.337 6.557   17.209  1.00 58.78  ? 256 ARG P CZ  1 
ATOM   1887 N  NH1 . ARG B 2 2   ? 18.951 7.716   17.405  1.00 44.94  ? 256 ARG P NH1 1 
ATOM   1888 N  NH2 . ARG B 2 2   ? 18.689 5.503   17.940  1.00 59.34  ? 256 ARG P NH2 1 
ATOM   1889 N  N   . SER B 2 3   ? 13.290 11.791  15.861  1.00 31.35  ? 257 SER P N   1 
ATOM   1890 C  CA  . SER B 2 3   ? 12.970 13.012  15.141  1.00 25.76  ? 257 SER P CA  1 
ATOM   1891 C  C   . SER B 2 3   ? 13.411 12.945  13.681  1.00 25.36  ? 257 SER P C   1 
ATOM   1892 O  O   . SER B 2 3   ? 14.416 12.311  13.358  1.00 28.39  ? 257 SER P O   1 
ATOM   1893 C  CB  . SER B 2 3   ? 13.667 14.164  15.830  1.00 23.71  ? 257 SER P CB  1 
ATOM   1894 O  OG  . SER B 2 3   ? 13.351 14.181  17.208  1.00 24.77  ? 257 SER P OG  1 
ATOM   1895 N  N   . SER B 2 4   ? 12.685 13.653  12.812  1.00 21.36  ? 258 SER P N   1 
ATOM   1896 C  CA  . SER B 2 4   ? 13.023 13.766  11.405  1.00 22.63  ? 258 SER P CA  1 
ATOM   1897 C  C   . SER B 2 4   ? 13.965 14.938  11.169  1.00 19.45  ? 258 SER P C   1 
ATOM   1898 O  O   . SER B 2 4   ? 13.645 16.064  11.511  1.00 18.37  ? 258 SER P O   1 
ATOM   1899 C  CB  . SER B 2 4   ? 11.779 14.022  10.565  1.00 26.47  ? 258 SER P CB  1 
ATOM   1900 O  OG  . SER B 2 4   ? 10.812 13.010  10.745  1.00 30.34  ? 258 SER P OG  1 
HETATM 1901 N  N   . SEP B 2 5   ? 15.129 14.684  10.565  1.00 21.02  ? 259 SEP P N   1 
HETATM 1902 C  CA  . SEP B 2 5   ? 15.985 15.774  10.134  1.00 18.05  ? 259 SEP P CA  1 
HETATM 1903 C  CB  . SEP B 2 5   ? 17.444 15.479  10.462  1.00 16.73  ? 259 SEP P CB  1 
HETATM 1904 O  OG  . SEP B 2 5   ? 17.845 14.312  9.734   1.00 15.40  ? 259 SEP P OG  1 
HETATM 1905 C  C   . SEP B 2 5   ? 15.746 16.029  8.647   1.00 18.22  ? 259 SEP P C   1 
HETATM 1906 O  O   . SEP B 2 5   ? 14.923 15.355  8.017   1.00 19.45  ? 259 SEP P O   1 
HETATM 1907 P  P   . SEP B 2 5   ? 19.312 13.747  10.039  1.00 15.92  ? 259 SEP P P   1 
HETATM 1908 O  O1P . SEP B 2 5   ? 19.426 12.539  9.092   1.00 17.71  ? 259 SEP P O1P 1 
HETATM 1909 O  O2P . SEP B 2 5   ? 20.281 14.863  9.687   1.00 15.98  ? 259 SEP P O2P 1 
HETATM 1910 O  O3P . SEP B 2 5   ? 19.370 13.367  11.488  1.00 15.88  ? 259 SEP P O3P 1 
ATOM   1911 N  N   . ALA B 2 6   ? 16.462 16.993  8.072   1.00 15.17  ? 260 ALA P N   1 
ATOM   1912 C  CA  . ALA B 2 6   ? 16.231 17.395  6.696   1.00 17.65  ? 260 ALA P CA  1 
ATOM   1913 C  C   . ALA B 2 6   ? 16.537 16.207  5.788   1.00 22.34  ? 260 ALA P C   1 
ATOM   1914 O  O   . ALA B 2 6   ? 17.576 15.569  5.916   1.00 21.33  ? 260 ALA P O   1 
ATOM   1915 C  CB  . ALA B 2 6   ? 17.048 18.600  6.332   1.00 18.53  ? 260 ALA P CB  1 
ATOM   1916 N  N   . PRO B 2 7   ? 15.650 15.857  4.837   1.00 21.50  ? 261 PRO P N   1 
ATOM   1917 C  CA  . PRO B 2 7   ? 15.898 14.712  3.957   1.00 24.03  ? 261 PRO P CA  1 
ATOM   1918 C  C   . PRO B 2 7   ? 16.768 15.130  2.778   1.00 21.99  ? 261 PRO P C   1 
ATOM   1919 O  O   . PRO B 2 7   ? 17.019 16.311  2.577   1.00 23.98  ? 261 PRO P O   1 
ATOM   1920 C  CB  . PRO B 2 7   ? 14.478 14.326  3.501   1.00 26.41  ? 261 PRO P CB  1 
ATOM   1921 C  CG  . PRO B 2 7   ? 13.805 15.646  3.338   1.00 26.14  ? 261 PRO P CG  1 
ATOM   1922 C  CD  . PRO B 2 7   ? 14.362 16.518  4.548   1.00 24.28  ? 261 PRO P CD  1 
ATOM   1923 N  N   . ASN B 2 8   ? 17.177 14.152  1.948   1.00 26.16  ? 262 ASN P N   1 
ATOM   1924 C  CA  . ASN B 2 8   ? 17.742 14.486  0.645   1.00 29.05  ? 262 ASN P CA  1 
ATOM   1925 C  C   . ASN B 2 8   ? 16.686 15.138  -0.248  1.00 38.81  ? 262 ASN P C   1 
ATOM   1926 O  O   . ASN B 2 8   ? 15.514 14.770  -0.207  1.00 40.74  ? 262 ASN P O   1 
ATOM   1927 C  CB  . ASN B 2 8   ? 18.332 13.268  -0.048  1.00 31.65  ? 262 ASN P CB  1 
ATOM   1928 C  CG  . ASN B 2 8   ? 19.547 12.707  0.659   1.00 33.14  ? 262 ASN P CG  1 
ATOM   1929 O  OD1 . ASN B 2 8   ? 19.544 11.561  1.120   1.00 43.43  ? 262 ASN P OD1 1 
ATOM   1930 N  ND2 . ASN B 2 8   ? 20.595 13.504  0.796   1.00 24.78  ? 262 ASN P ND2 1 
ATOM   1931 N  N   . VAL B 2 9   ? 17.111 16.135  -1.028  1.00 38.78  ? 263 VAL P N   1 
ATOM   1932 C  CA  . VAL B 2 9   ? 16.238 16.818  -1.970  1.00 52.66  ? 263 VAL P CA  1 
ATOM   1933 C  C   . VAL B 2 9   ? 16.960 16.971  -3.308  1.00 59.49  ? 263 VAL P C   1 
ATOM   1934 O  O   . VAL B 2 9   ? 16.338 17.321  -4.309  1.00 71.23  ? 263 VAL P O   1 
ATOM   1935 C  CB  . VAL B 2 9   ? 15.764 18.185  -1.426  1.00 51.76  ? 263 VAL P CB  1 
ATOM   1936 C  CG1 . VAL B 2 9   ? 14.716 17.998  -0.334  1.00 60.04  ? 263 VAL P CG1 1 
ATOM   1937 C  CG2 . VAL B 2 9   ? 16.934 19.040  -0.935  1.00 47.73  ? 263 VAL P CG2 1 
ATOM   1938 O  OXT . VAL B 2 9   ? 18.166 16.739  -3.383  1.00 53.14  ? 263 VAL P OXT 1 
HETATM 1939 CL CL  . CL  C 3 .   ? 35.370 -6.281  13.654  1.00 23.02  ? 301 CL  B CL  1 
HETATM 1940 MG MG  . MG  D 4 .   ? 35.037 4.272   19.585  1.00 32.32  ? 302 MG  B MG  1 
HETATM 1941 MG MG  . MG  E 4 .   ? 7.373  22.923  29.006  1.00 15.10  ? 303 MG  B MG  1 
HETATM 1942 C  C1  . WQN F 5 .   ? 22.146 25.171  -2.488  1.00 23.76  ? 304 WQN B C1  1 
HETATM 1943 C  C10 . WQN F 5 .   ? 15.921 20.380  2.590   1.00 38.96  ? 304 WQN B C10 1 
HETATM 1944 C  C11 . WQN F 5 .   ? 16.935 19.465  2.755   1.00 31.38  ? 304 WQN B C11 1 
HETATM 1945 C  C12 . WQN F 5 .   ? 18.237 19.905  2.820   1.00 24.83  ? 304 WQN B C12 1 
HETATM 1946 C  C13 . WQN F 5 .   ? 20.801 20.122  0.681   1.00 20.31  ? 304 WQN B C13 1 
HETATM 1947 C  C14 . WQN F 5 .   ? 21.558 20.062  -0.624  1.00 20.07  ? 304 WQN B C14 1 
HETATM 1948 C  C2  . WQN F 5 .   ? 21.287 25.922  -3.496  1.00 22.51  ? 304 WQN B C2  1 
HETATM 1949 C  C3  . WQN F 5 .   ? 22.330 22.993  -1.182  1.00 19.71  ? 304 WQN B C3  1 
HETATM 1950 C  C4  . WQN F 5 .   ? 20.942 22.283  -1.196  1.00 20.10  ? 304 WQN B C4  1 
HETATM 1951 C  C5  . WQN F 5 .   ? 20.470 23.206  -2.366  1.00 20.77  ? 304 WQN B C5  1 
HETATM 1952 C  C6  . WQN F 5 .   ? 20.119 22.396  0.082   1.00 19.73  ? 304 WQN B C6  1 
HETATM 1953 C  C7  . WQN F 5 .   ? 18.520 21.253  2.699   1.00 20.69  ? 304 WQN B C7  1 
HETATM 1954 C  C8  . WQN F 5 .   ? 17.495 22.176  2.530   1.00 25.49  ? 304 WQN B C8  1 
HETATM 1955 C  C9  . WQN F 5 .   ? 16.184 21.734  2.477   1.00 33.84  ? 304 WQN B C9  1 
HETATM 1956 N  N1  . WQN F 5 .   ? 21.713 23.941  -2.109  1.00 21.56  ? 304 WQN B N1  1 
HETATM 1957 N  N2  . WQN F 5 .   ? 20.706 21.524  1.121   1.00 20.08  ? 304 WQN B N2  1 
HETATM 1958 O  O1  . WQN F 5 .   ? 23.178 25.655  -1.989  1.00 21.92  ? 304 WQN B O1  1 
HETATM 1959 O  O2  . WQN F 5 .   ? 20.349 23.151  2.936   1.00 21.31  ? 304 WQN B O2  1 
HETATM 1960 O  O3  . WQN F 5 .   ? 20.964 20.808  3.463   1.00 26.36  ? 304 WQN B O3  1 
HETATM 1961 O  O4  . WQN F 5 .   ? 21.013 20.932  -1.618  1.00 19.15  ? 304 WQN B O4  1 
HETATM 1962 S  S1  . WQN F 5 .   ? 20.215 21.749  2.678   1.00 22.63  ? 304 WQN B S1  1 
HETATM 1963 BR BR1 . WQN F 5 .   ? 14.138 19.723  2.537   1.00 135.99 ? 304 WQN B BR1 1 
HETATM 1964 O  O   . HOH G 6 .   ? 45.602 17.188  -10.563 1.00 22.37  ? 401 HOH B O   1 
HETATM 1965 O  O   . HOH G 6 .   ? 1.810  13.981  19.969  1.00 30.13  ? 402 HOH B O   1 
HETATM 1966 O  O   . HOH G 6 .   ? 5.243  31.208  16.953  1.00 36.59  ? 403 HOH B O   1 
HETATM 1967 O  O   . HOH G 6 .   ? 37.937 -2.880  18.705  1.00 38.46  ? 404 HOH B O   1 
HETATM 1968 O  O   . HOH G 6 .   ? 31.944 -15.023 20.789  1.00 32.24  ? 405 HOH B O   1 
HETATM 1969 O  O   . HOH G 6 .   ? 42.935 10.449  -10.524 1.00 30.05  ? 406 HOH B O   1 
HETATM 1970 O  O   . HOH G 6 .   ? 10.169 37.913  2.888   1.00 40.39  ? 407 HOH B O   1 
HETATM 1971 O  O   . HOH G 6 .   ? 10.804 38.169  13.291  1.00 39.95  ? 408 HOH B O   1 
HETATM 1972 O  O   . HOH G 6 .   ? 27.103 38.117  -1.394  1.00 29.72  ? 409 HOH B O   1 
HETATM 1973 O  O   . HOH G 6 .   ? 22.712 7.411   15.250  1.00 29.89  ? 410 HOH B O   1 
HETATM 1974 O  O   . HOH G 6 .   ? 8.891  15.429  23.937  1.00 34.33  ? 411 HOH B O   1 
HETATM 1975 O  O   . HOH G 6 .   ? 17.386 30.705  21.984  1.00 20.05  ? 412 HOH B O   1 
HETATM 1976 O  O   . HOH G 6 .   ? 40.481 16.778  1.514   1.00 37.86  ? 413 HOH B O   1 
HETATM 1977 O  O   . HOH G 6 .   ? 23.442 12.250  -15.438 1.00 34.82  ? 414 HOH B O   1 
HETATM 1978 O  O   . HOH G 6 .   ? 30.020 -3.764  25.106  1.00 37.89  ? 415 HOH B O   1 
HETATM 1979 O  O   . HOH G 6 .   ? 36.926 -3.076  16.316  1.00 28.02  ? 416 HOH B O   1 
HETATM 1980 O  O   . HOH G 6 .   ? 38.823 20.324  -20.022 1.00 29.62  ? 417 HOH B O   1 
HETATM 1981 O  O   . HOH G 6 .   ? 23.159 0.441   7.045   1.00 36.65  ? 418 HOH B O   1 
HETATM 1982 O  O   . HOH G 6 .   ? 38.579 -6.972  21.726  1.00 34.63  ? 419 HOH B O   1 
HETATM 1983 O  O   . HOH G 6 .   ? 11.684 25.926  -6.961  1.00 42.94  ? 420 HOH B O   1 
HETATM 1984 O  O   . HOH G 6 .   ? 7.427  35.923  8.255   1.00 25.46  ? 421 HOH B O   1 
HETATM 1985 O  O   . HOH G 6 .   ? 22.230 18.469  -7.726  1.00 29.37  ? 422 HOH B O   1 
HETATM 1986 O  O   . HOH G 6 .   ? 25.395 15.661  3.726   1.00 18.87  ? 423 HOH B O   1 
HETATM 1987 O  O   . HOH G 6 .   ? 31.698 27.023  -2.471  1.00 16.87  ? 424 HOH B O   1 
HETATM 1988 O  O   . HOH G 6 .   ? 30.041 4.904   21.168  1.00 20.60  ? 425 HOH B O   1 
HETATM 1989 O  O   . HOH G 6 .   ? 21.669 5.292   0.740   1.00 37.81  ? 426 HOH B O   1 
HETATM 1990 O  O   . HOH G 6 .   ? 42.674 22.464  -3.796  1.00 15.97  ? 427 HOH B O   1 
HETATM 1991 O  O   . HOH G 6 .   ? 11.267 30.915  19.663  1.00 27.00  ? 428 HOH B O   1 
HETATM 1992 O  O   . HOH G 6 .   ? 35.537 5.097   17.813  1.00 33.47  ? 429 HOH B O   1 
HETATM 1993 O  O   . HOH G 6 .   ? 28.663 -6.958  24.142  1.00 42.18  ? 430 HOH B O   1 
HETATM 1994 O  O   . HOH G 6 .   ? 23.047 7.998   19.700  1.00 31.27  ? 431 HOH B O   1 
HETATM 1995 O  O   . HOH G 6 .   ? 17.596 28.159  -1.493  1.00 39.67  ? 432 HOH B O   1 
HETATM 1996 O  O   . HOH G 6 .   ? 41.092 20.145  6.982   1.00 35.84  ? 433 HOH B O   1 
HETATM 1997 O  O   . HOH G 6 .   ? 26.125 9.117   14.057  1.00 14.81  ? 434 HOH B O   1 
HETATM 1998 O  O   . HOH G 6 .   ? 4.906  12.954  13.883  1.00 35.22  ? 435 HOH B O   1 
HETATM 1999 O  O   . HOH G 6 .   ? 41.667 14.768  -5.475  1.00 29.81  ? 436 HOH B O   1 
HETATM 2000 O  O   . HOH G 6 .   ? 23.099 2.219   -2.521  1.00 35.76  ? 437 HOH B O   1 
HETATM 2001 O  O   . HOH G 6 .   ? 36.177 29.430  -7.526  1.00 24.86  ? 438 HOH B O   1 
HETATM 2002 O  O   . HOH G 6 .   ? 25.789 32.500  -4.830  1.00 21.16  ? 439 HOH B O   1 
HETATM 2003 O  O   . HOH G 6 .   ? 42.303 20.397  -17.857 1.00 20.96  ? 440 HOH B O   1 
HETATM 2004 O  O   . HOH G 6 .   ? 26.720 11.798  -18.413 1.00 39.70  ? 441 HOH B O   1 
HETATM 2005 O  O   . HOH G 6 .   ? 34.975 10.116  0.567   1.00 24.15  ? 442 HOH B O   1 
HETATM 2006 O  O   . HOH G 6 .   ? 24.536 18.051  6.024   1.00 27.37  ? 443 HOH B O   1 
HETATM 2007 O  O   . HOH G 6 .   ? 36.171 22.839  -7.092  1.00 15.13  ? 444 HOH B O   1 
HETATM 2008 O  O   . HOH G 6 .   ? 33.131 27.029  -9.555  1.00 27.68  ? 445 HOH B O   1 
HETATM 2009 O  O   . HOH G 6 .   ? 35.726 6.150   7.035   1.00 25.49  ? 446 HOH B O   1 
HETATM 2010 O  O   . HOH G 6 .   ? 34.997 -15.050 21.506  1.00 31.71  ? 447 HOH B O   1 
HETATM 2011 O  O   . HOH G 6 .   ? 13.730 30.281  13.070  1.00 19.76  ? 448 HOH B O   1 
HETATM 2012 O  O   . HOH G 6 .   ? 14.053 31.484  15.399  1.00 31.51  ? 449 HOH B O   1 
HETATM 2013 O  O   . HOH G 6 .   ? 8.649  13.221  8.979   1.00 37.00  ? 450 HOH B O   1 
HETATM 2014 O  O   . HOH G 6 .   ? 27.195 3.621   4.151   1.00 25.68  ? 451 HOH B O   1 
HETATM 2015 O  O   . HOH G 6 .   ? 29.714 29.250  -5.764  1.00 28.46  ? 452 HOH B O   1 
HETATM 2016 O  O   . HOH G 6 .   ? 36.045 21.352  12.064  1.00 26.75  ? 453 HOH B O   1 
HETATM 2017 O  O   . HOH G 6 .   ? 33.550 7.655   -0.767  1.00 22.15  ? 454 HOH B O   1 
HETATM 2018 O  O   . HOH G 6 .   ? 2.611  33.333  11.460  1.00 28.71  ? 455 HOH B O   1 
HETATM 2019 O  O   . HOH G 6 .   ? 24.601 18.679  3.758   1.00 20.03  ? 456 HOH B O   1 
HETATM 2020 O  O   . HOH G 6 .   ? 21.141 16.202  1.056   1.00 23.43  ? 457 HOH B O   1 
HETATM 2021 O  O   . HOH G 6 .   ? 23.253 16.590  26.178  1.00 35.11  ? 458 HOH B O   1 
HETATM 2022 O  O   . HOH G 6 .   ? 19.095 1.431   12.365  1.00 27.95  ? 459 HOH B O   1 
HETATM 2023 O  O   . HOH G 6 .   ? 26.927 1.007   21.974  1.00 31.64  ? 460 HOH B O   1 
HETATM 2024 O  O   . HOH G 6 .   ? 36.923 23.807  -3.184  1.00 20.79  ? 461 HOH B O   1 
HETATM 2025 O  O   . HOH G 6 .   ? 30.059 18.437  -15.572 1.00 22.32  ? 462 HOH B O   1 
HETATM 2026 O  O   . HOH G 6 .   ? 27.391 17.559  -15.366 1.00 23.86  ? 463 HOH B O   1 
HETATM 2027 O  O   . HOH G 6 .   ? 11.899 21.289  -0.340  1.00 35.57  ? 464 HOH B O   1 
HETATM 2028 O  O   . HOH G 6 .   ? 35.689 16.935  -18.813 1.00 23.44  ? 465 HOH B O   1 
HETATM 2029 O  O   . HOH G 6 .   ? 38.483 16.802  10.025  1.00 35.33  ? 466 HOH B O   1 
HETATM 2030 O  O   . HOH G 6 .   ? 21.991 12.418  -10.883 1.00 23.93  ? 467 HOH B O   1 
HETATM 2031 O  O   . HOH G 6 .   ? 18.042 23.524  27.633  1.00 25.54  ? 468 HOH B O   1 
HETATM 2032 O  O   . HOH G 6 .   ? 30.685 36.677  -2.279  1.00 29.45  ? 469 HOH B O   1 
HETATM 2033 O  O   . HOH G 6 .   ? 26.141 24.063  -11.490 1.00 29.39  ? 470 HOH B O   1 
HETATM 2034 O  O   . HOH G 6 .   ? 31.048 20.707  31.792  1.00 28.41  ? 471 HOH B O   1 
HETATM 2035 O  O   . HOH G 6 .   ? 31.986 24.793  15.279  1.00 25.96  ? 472 HOH B O   1 
HETATM 2036 O  O   . HOH G 6 .   ? 40.984 16.706  -7.077  1.00 19.68  ? 473 HOH B O   1 
HETATM 2037 O  O   . HOH G 6 .   ? 11.040 28.927  -1.260  1.00 26.75  ? 474 HOH B O   1 
HETATM 2038 O  O   . HOH G 6 .   ? 23.641 13.599  23.795  1.00 31.98  ? 475 HOH B O   1 
HETATM 2039 O  O   . HOH G 6 .   ? 18.157 41.784  7.702   1.00 47.83  ? 476 HOH B O   1 
HETATM 2040 O  O   . HOH G 6 .   ? 36.735 0.747   10.937  1.00 27.78  ? 477 HOH B O   1 
HETATM 2041 O  O   . HOH G 6 .   ? 20.687 37.295  12.951  1.00 27.28  ? 478 HOH B O   1 
HETATM 2042 O  O   . HOH G 6 .   ? 33.710 27.778  -0.985  1.00 19.38  ? 479 HOH B O   1 
HETATM 2043 O  O   . HOH G 6 .   ? 41.567 23.477  -10.239 1.00 27.42  ? 480 HOH B O   1 
HETATM 2044 O  O   . HOH G 6 .   ? 32.806 7.367   21.152  1.00 34.61  ? 481 HOH B O   1 
HETATM 2045 O  O   . HOH G 6 .   ? 20.212 23.600  23.667  1.00 22.82  ? 482 HOH B O   1 
HETATM 2046 O  O   . HOH G 6 .   ? 23.793 28.748  20.585  1.00 24.30  ? 483 HOH B O   1 
HETATM 2047 O  O   . HOH G 6 .   ? 29.717 -10.530 21.279  1.00 35.13  ? 484 HOH B O   1 
HETATM 2048 O  O   . HOH G 6 .   ? 33.958 4.241   -3.924  1.00 40.33  ? 485 HOH B O   1 
HETATM 2049 O  O   . HOH G 6 .   ? 14.920 15.693  24.692  1.00 30.04  ? 486 HOH B O   1 
HETATM 2050 O  O   . HOH G 6 .   ? 28.612 21.024  25.317  1.00 23.26  ? 487 HOH B O   1 
HETATM 2051 O  O   . HOH G 6 .   ? 12.319 31.917  11.361  1.00 18.90  ? 488 HOH B O   1 
HETATM 2052 O  O   . HOH G 6 .   ? 11.042 30.622  9.267   1.00 19.77  ? 489 HOH B O   1 
HETATM 2053 O  O   . HOH G 6 .   ? 38.097 11.207  -3.737  1.00 21.17  ? 490 HOH B O   1 
HETATM 2054 O  O   . HOH G 6 .   ? 27.207 23.135  24.059  1.00 26.84  ? 491 HOH B O   1 
HETATM 2055 O  O   . HOH G 6 .   ? 38.840 15.788  4.100   1.00 25.10  ? 492 HOH B O   1 
HETATM 2056 O  O   . HOH G 6 .   ? 18.851 15.090  24.016  1.00 25.08  ? 493 HOH B O   1 
HETATM 2057 O  O   . HOH G 6 .   ? 37.978 28.614  -3.591  1.00 36.15  ? 494 HOH B O   1 
HETATM 2058 O  O   . HOH G 6 .   ? 20.461 6.735   9.059   1.00 32.19  ? 495 HOH B O   1 
HETATM 2059 O  O   . HOH G 6 .   ? 18.306 5.687   -12.139 1.00 42.92  ? 496 HOH B O   1 
HETATM 2060 O  O   . HOH G 6 .   ? 28.526 30.553  16.874  1.00 28.60  ? 497 HOH B O   1 
HETATM 2061 O  O   . HOH G 6 .   ? 20.629 13.726  15.734  1.00 16.85  ? 498 HOH B O   1 
HETATM 2062 O  O   . HOH G 6 .   ? 9.117  25.291  24.340  1.00 26.36  ? 499 HOH B O   1 
HETATM 2063 O  O   . HOH G 6 .   ? 30.711 29.588  -2.797  1.00 27.67  ? 500 HOH B O   1 
HETATM 2064 O  O   . HOH G 6 .   ? 20.458 1.910   18.987  1.00 30.91  ? 501 HOH B O   1 
HETATM 2065 O  O   . HOH G 6 .   ? 11.461 20.222  14.144  1.00 21.04  ? 502 HOH B O   1 
HETATM 2066 O  O   . HOH G 6 .   ? 17.490 29.025  10.084  1.00 25.34  ? 503 HOH B O   1 
HETATM 2067 O  O   . HOH G 6 .   ? 22.269 17.358  -10.425 1.00 33.37  ? 504 HOH B O   1 
HETATM 2068 O  O   . HOH G 6 .   ? 38.071 7.316   12.342  1.00 30.63  ? 505 HOH B O   1 
HETATM 2069 O  O   . HOH G 6 .   ? 35.537 24.642  9.502   1.00 25.72  ? 506 HOH B O   1 
HETATM 2070 O  O   . HOH G 6 .   ? 43.770 18.129  -9.531  1.00 24.63  ? 507 HOH B O   1 
HETATM 2071 O  O   . HOH G 6 .   ? 18.916 7.709   -7.315  1.00 48.74  ? 508 HOH B O   1 
HETATM 2072 O  O   . HOH G 6 .   ? 34.029 22.786  21.072  1.00 30.38  ? 509 HOH B O   1 
HETATM 2073 O  O   . HOH G 6 .   ? 15.314 30.548  10.822  1.00 26.71  ? 510 HOH B O   1 
HETATM 2074 O  O   . HOH G 6 .   ? 8.437  22.789  -6.544  1.00 45.55  ? 511 HOH B O   1 
HETATM 2075 O  O   . HOH G 6 .   ? 11.988 31.710  -0.206  1.00 24.30  ? 512 HOH B O   1 
HETATM 2076 O  O   . HOH G 6 .   ? 30.801 -7.618  22.863  1.00 26.44  ? 513 HOH B O   1 
HETATM 2077 O  O   . HOH G 6 .   ? 19.376 -4.167  16.715  1.00 33.31  ? 514 HOH B O   1 
HETATM 2078 O  O   . HOH G 6 .   ? 19.492 10.297  -2.161  1.00 30.09  ? 515 HOH B O   1 
HETATM 2079 O  O   . HOH G 6 .   ? 37.265 26.837  5.438   1.00 19.34  ? 516 HOH B O   1 
HETATM 2080 O  O   . HOH G 6 .   ? 7.994  20.795  29.918  1.00 28.50  ? 517 HOH B O   1 
HETATM 2081 O  O   . HOH G 6 .   ? 32.503 10.776  17.943  1.00 17.26  ? 518 HOH B O   1 
HETATM 2082 O  O   . HOH G 6 .   ? 34.965 22.024  9.659   1.00 22.16  ? 519 HOH B O   1 
HETATM 2083 O  O   . HOH G 6 .   ? 28.018 30.513  19.247  1.00 38.10  ? 520 HOH B O   1 
HETATM 2084 O  O   . HOH G 6 .   ? -0.088 22.532  10.874  1.00 54.51  ? 521 HOH B O   1 
HETATM 2085 O  O   . HOH G 6 .   ? 20.851 17.731  5.343   1.00 23.92  ? 522 HOH B O   1 
HETATM 2086 O  O   . HOH G 6 .   ? 2.099  37.827  6.849   1.00 22.41  ? 523 HOH B O   1 
HETATM 2087 O  O   . HOH G 6 .   ? 26.662 29.682  -5.303  1.00 27.32  ? 524 HOH B O   1 
HETATM 2088 O  O   . HOH G 6 .   ? 33.383 21.734  -13.541 1.00 23.64  ? 525 HOH B O   1 
HETATM 2089 O  O   . HOH G 6 .   ? 24.582 37.003  0.451   1.00 35.17  ? 526 HOH B O   1 
HETATM 2090 O  O   . HOH G 6 .   ? 3.427  30.831  -9.499  1.00 33.68  ? 527 HOH B O   1 
HETATM 2091 O  O   . HOH G 6 .   ? 6.208  28.466  -9.991  1.00 29.41  ? 528 HOH B O   1 
HETATM 2092 O  O   . HOH G 6 .   ? 35.894 34.102  -1.991  1.00 26.08  ? 529 HOH B O   1 
HETATM 2093 O  O   . HOH G 6 .   ? 7.050  30.264  19.427  1.00 35.59  ? 530 HOH B O   1 
HETATM 2094 O  O   . HOH G 6 .   ? 23.936 21.470  4.891   1.00 18.88  ? 531 HOH B O   1 
HETATM 2095 O  O   . HOH G 6 .   ? 19.535 10.677  -4.709  1.00 35.89  ? 532 HOH B O   1 
HETATM 2096 O  O   . HOH G 6 .   ? 34.718 18.087  26.330  1.00 33.10  ? 533 HOH B O   1 
HETATM 2097 O  O   . HOH G 6 .   ? 18.075 27.838  19.262  1.00 23.44  ? 534 HOH B O   1 
HETATM 2098 O  O   . HOH G 6 .   ? 40.839 19.381  2.236   1.00 32.91  ? 535 HOH B O   1 
HETATM 2099 O  O   . HOH G 6 .   ? 22.902 33.806  -1.271  1.00 25.86  ? 536 HOH B O   1 
HETATM 2100 O  O   . HOH G 6 .   ? 22.423 10.561  7.059   1.00 21.99  ? 537 HOH B O   1 
HETATM 2101 O  O   . HOH G 6 .   ? 39.530 21.948  -1.097  1.00 27.09  ? 538 HOH B O   1 
HETATM 2102 O  O   . HOH G 6 .   ? 34.338 11.874  23.190  1.00 34.03  ? 539 HOH B O   1 
HETATM 2103 O  O   . HOH G 6 .   ? 22.015 26.861  21.659  1.00 25.24  ? 540 HOH B O   1 
HETATM 2104 O  O   . HOH G 6 .   ? 26.564 7.699   22.269  1.00 34.72  ? 541 HOH B O   1 
HETATM 2105 O  O   . HOH G 6 .   ? 27.089 -1.395  -5.805  1.00 25.17  ? 542 HOH B O   1 
HETATM 2106 O  O   . HOH G 6 .   ? 26.049 12.875  -15.876 1.00 22.29  ? 543 HOH B O   1 
HETATM 2107 O  O   . HOH G 6 .   ? 22.604 17.849  -14.801 1.00 44.39  ? 544 HOH B O   1 
HETATM 2108 O  O   . HOH G 6 .   ? 12.524 27.555  -3.411  1.00 35.44  ? 545 HOH B O   1 
HETATM 2109 O  O   . HOH G 6 .   ? 9.178  32.428  -5.582  1.00 24.89  ? 546 HOH B O   1 
HETATM 2110 O  O   . HOH G 6 .   ? 14.650 32.185  -0.738  1.00 33.14  ? 547 HOH B O   1 
HETATM 2111 O  O   . HOH G 6 .   ? 36.838 20.566  -15.960 1.00 18.83  ? 548 HOH B O   1 
HETATM 2112 O  O   . HOH G 6 .   ? 37.879 31.168  -4.436  1.00 47.03  ? 549 HOH B O   1 
HETATM 2113 O  O   . HOH G 6 .   ? 35.484 19.597  18.694  1.00 40.35  ? 550 HOH B O   1 
HETATM 2114 O  O   . HOH G 6 .   ? 35.480 31.600  7.577   1.00 32.43  ? 551 HOH B O   1 
HETATM 2115 O  O   . HOH G 6 .   ? 32.694 -16.543 18.770  1.00 40.61  ? 552 HOH B O   1 
HETATM 2116 O  O   . HOH G 6 .   ? 37.958 24.891  -0.958  1.00 29.93  ? 553 HOH B O   1 
HETATM 2117 O  O   . HOH G 6 .   ? 29.357 3.233   -4.489  1.00 17.57  ? 554 HOH B O   1 
HETATM 2118 O  O   . HOH G 6 .   ? 40.479 12.419  -4.480  1.00 36.63  ? 555 HOH B O   1 
HETATM 2119 O  O   . HOH G 6 .   ? 17.785 9.560   12.003  1.00 37.39  ? 556 HOH B O   1 
HETATM 2120 O  O   . HOH G 6 .   ? 33.725 34.355  -4.626  1.00 21.77  ? 557 HOH B O   1 
HETATM 2121 O  O   . HOH G 6 .   ? 18.426 35.085  0.316   1.00 40.81  ? 558 HOH B O   1 
HETATM 2122 O  O   . HOH G 6 .   ? 32.738 15.319  27.719  1.00 38.59  ? 559 HOH B O   1 
HETATM 2123 O  O   . HOH G 6 .   ? 2.404  21.929  7.239   1.00 45.97  ? 560 HOH B O   1 
HETATM 2124 O  O   . HOH G 6 .   ? 18.106 3.898   11.772  1.00 38.09  ? 561 HOH B O   1 
HETATM 2125 O  O   . HOH G 6 .   ? 25.147 0.209   -5.010  1.00 40.54  ? 562 HOH B O   1 
HETATM 2126 O  O   . HOH G 6 .   ? 27.562 2.807   -2.255  1.00 37.15  ? 563 HOH B O   1 
HETATM 2127 O  O   . HOH G 6 .   ? 31.867 26.903  13.505  1.00 35.25  ? 564 HOH B O   1 
HETATM 2128 O  O   . HOH G 6 .   ? 35.553 2.593   18.263  1.00 39.29  ? 565 HOH B O   1 
HETATM 2129 O  O   . HOH G 6 .   ? 29.139 35.811  7.183   1.00 51.02  ? 566 HOH B O   1 
HETATM 2130 O  O   . HOH G 6 .   ? 37.749 -0.218  15.380  1.00 36.66  ? 567 HOH B O   1 
HETATM 2131 O  O   . HOH G 6 .   ? 46.731 14.646  -7.120  1.00 36.02  ? 568 HOH B O   1 
HETATM 2132 O  O   . HOH G 6 .   ? 37.427 27.984  7.890   1.00 42.51  ? 569 HOH B O   1 
HETATM 2133 O  O   . HOH G 6 .   ? 39.567 22.923  -17.273 1.00 41.33  ? 570 HOH B O   1 
HETATM 2134 O  O   . HOH G 6 .   ? 13.119 30.135  18.619  1.00 39.89  ? 571 HOH B O   1 
HETATM 2135 O  O   . HOH G 6 .   ? 33.964 10.551  20.309  1.00 31.31  ? 572 HOH B O   1 
HETATM 2136 O  O   . HOH G 6 .   ? 7.492  26.782  22.571  1.00 30.49  ? 573 HOH B O   1 
HETATM 2137 O  O   . HOH G 6 .   ? 34.530 24.113  15.540  1.00 45.02  ? 574 HOH B O   1 
HETATM 2138 O  O   . HOH G 6 .   ? 36.463 19.551  -18.482 1.00 33.52  ? 575 HOH B O   1 
HETATM 2139 O  O   . HOH G 6 .   ? 21.681 30.023  -6.754  1.00 30.61  ? 576 HOH B O   1 
HETATM 2140 O  O   . HOH G 6 .   ? 0.147  30.977  14.597  1.00 44.70  ? 577 HOH B O   1 
HETATM 2141 O  O   . HOH G 6 .   ? 18.080 0.403   14.823  1.00 38.85  ? 578 HOH B O   1 
HETATM 2142 O  O   . HOH G 6 .   ? 25.245 6.603   14.716  1.00 19.36  ? 579 HOH B O   1 
HETATM 2143 O  O   . HOH G 6 .   ? 21.934 10.526  20.065  1.00 46.23  ? 580 HOH B O   1 
HETATM 2144 O  O   . HOH G 6 .   ? 20.949 25.466  -8.990  1.00 37.00  ? 581 HOH B O   1 
HETATM 2145 O  O   . HOH G 6 .   ? 36.153 26.839  -2.047  1.00 27.16  ? 582 HOH B O   1 
HETATM 2146 O  O   . HOH G 6 .   ? 37.672 -4.790  14.567  1.00 35.21  ? 583 HOH B O   1 
HETATM 2147 O  O   . HOH G 6 .   ? 7.262  11.568  13.259  1.00 43.27  ? 584 HOH B O   1 
HETATM 2148 O  O   . HOH G 6 .   ? 35.026 22.743  -15.336 1.00 27.00  ? 585 HOH B O   1 
HETATM 2149 O  O   . HOH G 6 .   ? 18.142 12.446  15.716  1.00 26.48  ? 586 HOH B O   1 
HETATM 2150 O  O   . HOH G 6 .   ? 14.046 22.669  -1.655  1.00 39.57  ? 587 HOH B O   1 
HETATM 2151 O  O   . HOH G 6 .   ? 34.598 9.164   3.153   1.00 31.07  ? 588 HOH B O   1 
HETATM 2152 O  O   . HOH G 6 .   ? 34.759 12.390  17.248  1.00 33.91  ? 589 HOH B O   1 
HETATM 2153 O  O   . HOH G 6 .   ? 20.099 21.851  -6.233  1.00 47.46  ? 590 HOH B O   1 
HETATM 2154 O  O   . HOH G 6 .   ? 26.079 15.524  -16.680 1.00 30.79  ? 591 HOH B O   1 
HETATM 2155 O  O   . HOH G 6 .   ? 29.433 21.861  30.000  1.00 26.14  ? 592 HOH B O   1 
HETATM 2156 O  O   . HOH G 6 .   ? 32.844 5.005   3.242   1.00 42.20  ? 593 HOH B O   1 
HETATM 2157 O  O   . HOH G 6 .   ? 27.555 16.311  27.105  1.00 45.92  ? 594 HOH B O   1 
HETATM 2158 O  O   . HOH G 6 .   ? 30.788 20.970  -14.473 1.00 20.71  ? 595 HOH B O   1 
HETATM 2159 O  O   . HOH G 6 .   ? 9.141  19.596  26.617  1.00 33.71  ? 596 HOH B O   1 
HETATM 2160 O  O   . HOH G 6 .   ? 12.705 24.132  -8.592  1.00 47.97  ? 597 HOH B O   1 
HETATM 2161 O  O   . HOH G 6 .   ? 17.769 25.647  -2.084  1.00 32.43  ? 598 HOH B O   1 
HETATM 2162 O  O   . HOH G 6 .   ? 28.529 3.467   22.644  1.00 34.47  ? 599 HOH B O   1 
HETATM 2163 O  O   . HOH G 6 .   ? 27.149 20.292  29.410  1.00 30.80  ? 600 HOH B O   1 
HETATM 2164 O  O   . HOH G 6 .   ? 11.132 33.736  -4.049  1.00 28.29  ? 601 HOH B O   1 
HETATM 2165 O  O   . HOH G 6 .   ? 42.709 22.424  -19.664 1.00 21.66  ? 602 HOH B O   1 
HETATM 2166 O  O   . HOH G 6 .   ? 17.925 29.760  17.164  1.00 38.47  ? 603 HOH B O   1 
HETATM 2167 O  O   . HOH G 6 .   ? 16.923 23.146  -1.379  1.00 38.95  ? 604 HOH B O   1 
HETATM 2168 O  O   . HOH G 6 .   ? 26.317 5.370   23.216  1.00 39.38  ? 605 HOH B O   1 
HETATM 2169 O  O   . HOH G 6 .   ? 26.878 18.950  26.839  1.00 26.37  ? 606 HOH B O   1 
HETATM 2170 O  O   . HOH G 6 .   ? 32.825 7.659   1.947   1.00 34.02  ? 607 HOH B O   1 
HETATM 2171 O  O   . HOH H 6 .   ? 17.914 10.478  9.325   1.00 34.81  ? 301 HOH P O   1 
HETATM 2172 O  O   . HOH H 6 .   ? 13.990 13.130  7.131   1.00 38.35  ? 302 HOH P O   1 
HETATM 2173 O  O   . HOH H 6 .   ? 17.353 12.162  12.750  1.00 28.47  ? 303 HOH P O   1 
HETATM 2174 O  O   . HOH H 6 .   ? 9.026  13.473  12.703  1.00 29.34  ? 304 HOH P O   1 
HETATM 2175 O  O   . HOH H 6 .   ? 19.630 17.127  -1.028  1.00 33.41  ? 305 HOH P O   1 
HETATM 2176 O  O   . HOH H 6 .   ? 19.685 16.349  7.480   1.00 16.36  ? 306 HOH P O   1 
HETATM 2177 O  O   . HOH H 6 .   ? 19.647 16.967  3.193   1.00 25.80  ? 307 HOH P O   1 
HETATM 2178 O  O   . HOH H 6 .   ? 16.901 12.995  6.901   1.00 42.91  ? 308 HOH P O   1 
HETATM 2179 O  O   . HOH H 6 .   ? 15.429 11.829  9.697   1.00 30.35  ? 309 HOH P O   1 
HETATM 2180 O  O   . HOH H 6 .   ? 21.921 7.236   17.617  1.00 38.96  ? 310 HOH P O   1 
# 
