data_8WUR
# 
_entry.id   8WUR 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.398 
_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   8WUR         pdb_00008wur 10.2210/pdb8wur/pdb 
WWPDB D_1300042016 ?            ?                   
# 
_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       2024-11-13 
# 
_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             ? 
# 
_database_PDB_caveat.id     1 
_database_PDB_caveat.text   'FNO A 301 HAS WRONG CHIRALITY AT ATOM C06' 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8WUR 
_pdbx_database_status.recvd_initial_deposition_date   2023-10-21 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBJ 
_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              rmsl_2040@163.com 
_pdbx_contact_author.name_first         Jian 
_pdbx_contact_author.name_last          Li 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-9511-4219 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Zhao, Z.Y.' 1 ? 
'Li, W.W.'   2 ? 
'Zhang, J.'  3 ? 
'Li, J.'     4 ? 
# 
_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                   CH 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Viruses 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           1999-4915 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            16 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     
'Structural Basis for the Inhibition of SARS-CoV-2 M pro D48N Mutant by Shikonin and PF-07321332.' 
_citation.year                      2023 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.3390/v16010065 
_citation.pdbx_database_id_PubMed   38257765 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Zhao, Z.' 1 ?                   
primary 'Zhu, Q.'  2 ?                   
primary 'Zhou, X.' 3 0009-0007-8138-1923 
primary 'Li, W.'   4 ?                   
primary 'Yin, X.'  5 ?                   
primary 'Li, J.'   6 ?                   
# 
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 '3C-like proteinase nsp5'                                                         32786.477 2  3.4.22.69 D48N ? 
? 
2 non-polymer syn '2-[(1R)-4-methyl-1-oxidanyl-pent-3-enyl]-5,8-bis(oxidanyl)naphthalene-1,4-dione' 288.295   1  ?         ?    ? 
? 
3 water       nat water                                                                             18.015    90 ?         ?    ? 
? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        '3CL-PRO,3CLp,Main protease,Mpro,Non-structural protein 5,nsp5,SARS coronavirus main proteinase' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;FRKMAFPSGKVEGCMVQVTCGTTTLNGLWLDDVVYCPRHVICTSENMLNPNYEDLLIRKSNHNFLVQAGNVQLRVIGHSM
QNCVLKLKVDTANPKTPKYKFVRIQPGQTFSVLACYNGSPSGVYQCAMRPNFTIKGSFLAGSCGSVGFNIDYDCVSFCYM
HHMELPTGVHAGTDLEGNFYGPFVDRQTAQAAGTDTTITVNVLAWLYAAVINGDRWFLNRFTTTLNDFNLVAMKYNYEPL
TQDHVDILGPLSAQTGIAVLDMCASLKELLQNGMNGRTILGSALLEDEFTPFDVVR
;
_entity_poly.pdbx_seq_one_letter_code_can   
;FRKMAFPSGKVEGCMVQVTCGTTTLNGLWLDDVVYCPRHVICTSENMLNPNYEDLLIRKSNHNFLVQAGNVQLRVIGHSM
QNCVLKLKVDTANPKTPKYKFVRIQPGQTFSVLACYNGSPSGVYQCAMRPNFTIKGSFLAGSCGSVGFNIDYDCVSFCYM
HHMELPTGVHAGTDLEGNFYGPFVDRQTAQAAGTDTTITVNVLAWLYAAVINGDRWFLNRFTTTLNDFNLVAMKYNYEPL
TQDHVDILGPLSAQTGIAVLDMCASLKELLQNGMNGRTILGSALLEDEFTPFDVVR
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 '2-[(1R)-4-methyl-1-oxidanyl-pent-3-enyl]-5,8-bis(oxidanyl)naphthalene-1,4-dione' FNO 
3 water                                                                             HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   PHE n 
1 2   ARG n 
1 3   LYS n 
1 4   MET n 
1 5   ALA n 
1 6   PHE n 
1 7   PRO n 
1 8   SER n 
1 9   GLY n 
1 10  LYS n 
1 11  VAL n 
1 12  GLU n 
1 13  GLY n 
1 14  CYS n 
1 15  MET n 
1 16  VAL n 
1 17  GLN n 
1 18  VAL n 
1 19  THR n 
1 20  CYS n 
1 21  GLY n 
1 22  THR n 
1 23  THR n 
1 24  THR n 
1 25  LEU n 
1 26  ASN n 
1 27  GLY n 
1 28  LEU n 
1 29  TRP n 
1 30  LEU n 
1 31  ASP n 
1 32  ASP n 
1 33  VAL n 
1 34  VAL n 
1 35  TYR n 
1 36  CYS n 
1 37  PRO n 
1 38  ARG n 
1 39  HIS n 
1 40  VAL n 
1 41  ILE n 
1 42  CYS n 
1 43  THR n 
1 44  SER n 
1 45  GLU n 
1 46  ASN n 
1 47  MET n 
1 48  LEU n 
1 49  ASN n 
1 50  PRO n 
1 51  ASN n 
1 52  TYR n 
1 53  GLU n 
1 54  ASP n 
1 55  LEU n 
1 56  LEU n 
1 57  ILE n 
1 58  ARG n 
1 59  LYS n 
1 60  SER n 
1 61  ASN n 
1 62  HIS n 
1 63  ASN n 
1 64  PHE n 
1 65  LEU n 
1 66  VAL n 
1 67  GLN n 
1 68  ALA n 
1 69  GLY n 
1 70  ASN n 
1 71  VAL n 
1 72  GLN n 
1 73  LEU n 
1 74  ARG n 
1 75  VAL n 
1 76  ILE n 
1 77  GLY n 
1 78  HIS n 
1 79  SER n 
1 80  MET n 
1 81  GLN n 
1 82  ASN n 
1 83  CYS n 
1 84  VAL n 
1 85  LEU n 
1 86  LYS n 
1 87  LEU n 
1 88  LYS n 
1 89  VAL n 
1 90  ASP n 
1 91  THR n 
1 92  ALA n 
1 93  ASN n 
1 94  PRO n 
1 95  LYS n 
1 96  THR n 
1 97  PRO n 
1 98  LYS n 
1 99  TYR n 
1 100 LYS n 
1 101 PHE n 
1 102 VAL n 
1 103 ARG n 
1 104 ILE n 
1 105 GLN n 
1 106 PRO n 
1 107 GLY n 
1 108 GLN n 
1 109 THR n 
1 110 PHE n 
1 111 SER n 
1 112 VAL n 
1 113 LEU n 
1 114 ALA n 
1 115 CYS n 
1 116 TYR n 
1 117 ASN n 
1 118 GLY n 
1 119 SER n 
1 120 PRO n 
1 121 SER n 
1 122 GLY n 
1 123 VAL n 
1 124 TYR n 
1 125 GLN n 
1 126 CYS n 
1 127 ALA n 
1 128 MET n 
1 129 ARG n 
1 130 PRO n 
1 131 ASN n 
1 132 PHE n 
1 133 THR n 
1 134 ILE n 
1 135 LYS n 
1 136 GLY n 
1 137 SER n 
1 138 PHE n 
1 139 LEU n 
1 140 ALA n 
1 141 GLY n 
1 142 SER n 
1 143 CYS n 
1 144 GLY n 
1 145 SER n 
1 146 VAL n 
1 147 GLY n 
1 148 PHE n 
1 149 ASN n 
1 150 ILE n 
1 151 ASP n 
1 152 TYR n 
1 153 ASP n 
1 154 CYS n 
1 155 VAL n 
1 156 SER n 
1 157 PHE n 
1 158 CYS n 
1 159 TYR n 
1 160 MET n 
1 161 HIS n 
1 162 HIS n 
1 163 MET n 
1 164 GLU n 
1 165 LEU n 
1 166 PRO n 
1 167 THR n 
1 168 GLY n 
1 169 VAL n 
1 170 HIS n 
1 171 ALA n 
1 172 GLY n 
1 173 THR n 
1 174 ASP n 
1 175 LEU n 
1 176 GLU n 
1 177 GLY n 
1 178 ASN n 
1 179 PHE n 
1 180 TYR n 
1 181 GLY n 
1 182 PRO n 
1 183 PHE n 
1 184 VAL n 
1 185 ASP n 
1 186 ARG n 
1 187 GLN n 
1 188 THR n 
1 189 ALA n 
1 190 GLN n 
1 191 ALA n 
1 192 ALA n 
1 193 GLY n 
1 194 THR n 
1 195 ASP n 
1 196 THR n 
1 197 THR n 
1 198 ILE n 
1 199 THR n 
1 200 VAL n 
1 201 ASN n 
1 202 VAL n 
1 203 LEU n 
1 204 ALA n 
1 205 TRP n 
1 206 LEU n 
1 207 TYR n 
1 208 ALA n 
1 209 ALA n 
1 210 VAL n 
1 211 ILE n 
1 212 ASN n 
1 213 GLY n 
1 214 ASP n 
1 215 ARG n 
1 216 TRP n 
1 217 PHE n 
1 218 LEU n 
1 219 ASN n 
1 220 ARG n 
1 221 PHE n 
1 222 THR n 
1 223 THR n 
1 224 THR n 
1 225 LEU n 
1 226 ASN n 
1 227 ASP n 
1 228 PHE n 
1 229 ASN n 
1 230 LEU n 
1 231 VAL n 
1 232 ALA n 
1 233 MET n 
1 234 LYS n 
1 235 TYR n 
1 236 ASN n 
1 237 TYR n 
1 238 GLU n 
1 239 PRO n 
1 240 LEU n 
1 241 THR n 
1 242 GLN n 
1 243 ASP n 
1 244 HIS n 
1 245 VAL n 
1 246 ASP n 
1 247 ILE n 
1 248 LEU n 
1 249 GLY n 
1 250 PRO n 
1 251 LEU n 
1 252 SER n 
1 253 ALA n 
1 254 GLN n 
1 255 THR n 
1 256 GLY n 
1 257 ILE n 
1 258 ALA n 
1 259 VAL n 
1 260 LEU n 
1 261 ASP n 
1 262 MET n 
1 263 CYS n 
1 264 ALA n 
1 265 SER n 
1 266 LEU n 
1 267 LYS n 
1 268 GLU n 
1 269 LEU n 
1 270 LEU n 
1 271 GLN n 
1 272 ASN n 
1 273 GLY n 
1 274 MET n 
1 275 ASN n 
1 276 GLY n 
1 277 ARG n 
1 278 THR n 
1 279 ILE n 
1 280 LEU n 
1 281 GLY n 
1 282 SER n 
1 283 ALA n 
1 284 LEU n 
1 285 LEU n 
1 286 GLU n 
1 287 ASP n 
1 288 GLU n 
1 289 PHE n 
1 290 THR n 
1 291 PRO n 
1 292 PHE n 
1 293 ASP n 
1 294 VAL n 
1 295 VAL n 
1 296 ARG 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                   296 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 ? 
_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      'Severe acute respiratory syndrome coronavirus 2' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     2697049 
_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 BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                                                                           ?        'C3 H7 N O2' 
89.093  
ARG 'L-peptide linking' y ARGININE                                                                          ?        
'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE                                                                        ?        'C4 H8 N2 O3' 
132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                                                                   ?        'C4 H7 N O4' 
133.103 
CYS 'L-peptide linking' y CYSTEINE                                                                          ?        
'C3 H7 N O2 S'   121.158 
FNO non-polymer         . '2-[(1R)-4-methyl-1-oxidanyl-pent-3-enyl]-5,8-bis(oxidanyl)naphthalene-1,4-dione' shikonin 'C16 H16 O5' 
288.295 
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 
PHE 'L-peptide linking' y PHENYLALANINE                                                                     ?        'C9 H11 N O2' 
165.189 
PRO 'L-peptide linking' y PROLINE                                                                           ?        'C5 H9 N O2' 
115.130 
SER 'L-peptide linking' y SERINE                                                                            ?        'C3 H7 N O3' 
105.093 
THR 'L-peptide linking' y THREONINE                                                                         ?        'C4 H9 N O3' 
119.119 
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 
# 
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   PHE 1   3   ?   ?   ?   A . n 
A 1 2   ARG 2   4   4   ARG ARG A . n 
A 1 3   LYS 3   5   5   LYS LYS A . n 
A 1 4   MET 4   6   6   MET MET A . n 
A 1 5   ALA 5   7   7   ALA ALA A . n 
A 1 6   PHE 6   8   8   PHE PHE A . n 
A 1 7   PRO 7   9   9   PRO PRO A . n 
A 1 8   SER 8   10  10  SER SER A . n 
A 1 9   GLY 9   11  11  GLY GLY A . n 
A 1 10  LYS 10  12  12  LYS LYS A . n 
A 1 11  VAL 11  13  13  VAL VAL A . n 
A 1 12  GLU 12  14  14  GLU GLU A . n 
A 1 13  GLY 13  15  15  GLY GLY A . n 
A 1 14  CYS 14  16  16  CYS CYS A . n 
A 1 15  MET 15  17  17  MET MET A . n 
A 1 16  VAL 16  18  18  VAL VAL A . n 
A 1 17  GLN 17  19  19  GLN GLN A . n 
A 1 18  VAL 18  20  20  VAL VAL A . n 
A 1 19  THR 19  21  21  THR THR A . n 
A 1 20  CYS 20  22  22  CYS CYS A . n 
A 1 21  GLY 21  23  23  GLY GLY A . n 
A 1 22  THR 22  24  24  THR THR A . n 
A 1 23  THR 23  25  25  THR THR A . n 
A 1 24  THR 24  26  26  THR THR A . n 
A 1 25  LEU 25  27  27  LEU LEU A . n 
A 1 26  ASN 26  28  28  ASN ASN A . n 
A 1 27  GLY 27  29  29  GLY GLY A . n 
A 1 28  LEU 28  30  30  LEU LEU A . n 
A 1 29  TRP 29  31  31  TRP TRP A . n 
A 1 30  LEU 30  32  32  LEU LEU A . n 
A 1 31  ASP 31  33  33  ASP ASP A . n 
A 1 32  ASP 32  34  34  ASP ASP A . n 
A 1 33  VAL 33  35  35  VAL VAL A . n 
A 1 34  VAL 34  36  36  VAL VAL A . n 
A 1 35  TYR 35  37  37  TYR TYR A . n 
A 1 36  CYS 36  38  38  CYS CYS A . n 
A 1 37  PRO 37  39  39  PRO PRO A . n 
A 1 38  ARG 38  40  40  ARG ARG A . n 
A 1 39  HIS 39  41  41  HIS HIS A . n 
A 1 40  VAL 40  42  42  VAL VAL A . n 
A 1 41  ILE 41  43  43  ILE ILE A . n 
A 1 42  CYS 42  44  44  CYS CYS A . n 
A 1 43  THR 43  45  45  THR THR A . n 
A 1 44  SER 44  46  46  SER SER A . n 
A 1 45  GLU 45  47  47  GLU GLU A . n 
A 1 46  ASN 46  48  48  ASN ASN A . n 
A 1 47  MET 47  49  49  MET MET A . n 
A 1 48  LEU 48  50  50  LEU LEU A . n 
A 1 49  ASN 49  51  51  ASN ASN A . n 
A 1 50  PRO 50  52  52  PRO PRO A . n 
A 1 51  ASN 51  53  53  ASN ASN A . n 
A 1 52  TYR 52  54  54  TYR TYR A . n 
A 1 53  GLU 53  55  55  GLU GLU A . n 
A 1 54  ASP 54  56  56  ASP ASP A . n 
A 1 55  LEU 55  57  57  LEU LEU A . n 
A 1 56  LEU 56  58  58  LEU LEU A . n 
A 1 57  ILE 57  59  59  ILE ILE A . n 
A 1 58  ARG 58  60  60  ARG ARG A . n 
A 1 59  LYS 59  61  61  LYS LYS A . n 
A 1 60  SER 60  62  62  SER SER A . n 
A 1 61  ASN 61  63  63  ASN ASN A . n 
A 1 62  HIS 62  64  64  HIS HIS A . n 
A 1 63  ASN 63  65  65  ASN ASN A . n 
A 1 64  PHE 64  66  66  PHE PHE A . n 
A 1 65  LEU 65  67  67  LEU LEU A . n 
A 1 66  VAL 66  68  68  VAL VAL A . n 
A 1 67  GLN 67  69  69  GLN GLN A . n 
A 1 68  ALA 68  70  70  ALA ALA A . n 
A 1 69  GLY 69  71  71  GLY GLY A . n 
A 1 70  ASN 70  72  72  ASN ASN A . n 
A 1 71  VAL 71  73  73  VAL VAL A . n 
A 1 72  GLN 72  74  74  GLN GLN A . n 
A 1 73  LEU 73  75  75  LEU LEU A . n 
A 1 74  ARG 74  76  76  ARG ARG A . n 
A 1 75  VAL 75  77  77  VAL VAL A . n 
A 1 76  ILE 76  78  78  ILE ILE A . n 
A 1 77  GLY 77  79  79  GLY GLY A . n 
A 1 78  HIS 78  80  80  HIS HIS A . n 
A 1 79  SER 79  81  81  SER SER A . n 
A 1 80  MET 80  82  82  MET MET A . n 
A 1 81  GLN 81  83  83  GLN GLN A . n 
A 1 82  ASN 82  84  84  ASN ASN A . n 
A 1 83  CYS 83  85  85  CYS CYS A . n 
A 1 84  VAL 84  86  86  VAL VAL A . n 
A 1 85  LEU 85  87  87  LEU LEU A . n 
A 1 86  LYS 86  88  88  LYS LYS A . n 
A 1 87  LEU 87  89  89  LEU LEU A . n 
A 1 88  LYS 88  90  90  LYS LYS A . n 
A 1 89  VAL 89  91  91  VAL VAL A . n 
A 1 90  ASP 90  92  92  ASP ASP A . n 
A 1 91  THR 91  93  93  THR THR A . n 
A 1 92  ALA 92  94  94  ALA ALA A . n 
A 1 93  ASN 93  95  95  ASN ASN A . n 
A 1 94  PRO 94  96  96  PRO PRO A . n 
A 1 95  LYS 95  97  97  LYS LYS A . n 
A 1 96  THR 96  98  98  THR THR A . n 
A 1 97  PRO 97  99  99  PRO PRO A . n 
A 1 98  LYS 98  100 100 LYS LYS A . n 
A 1 99  TYR 99  101 101 TYR TYR A . n 
A 1 100 LYS 100 102 102 LYS LYS A . n 
A 1 101 PHE 101 103 103 PHE PHE A . n 
A 1 102 VAL 102 104 104 VAL VAL A . n 
A 1 103 ARG 103 105 105 ARG ARG A . n 
A 1 104 ILE 104 106 106 ILE ILE A . n 
A 1 105 GLN 105 107 107 GLN GLN A . n 
A 1 106 PRO 106 108 108 PRO PRO A . n 
A 1 107 GLY 107 109 109 GLY GLY A . n 
A 1 108 GLN 108 110 110 GLN GLN A . n 
A 1 109 THR 109 111 111 THR THR A . n 
A 1 110 PHE 110 112 112 PHE PHE A . n 
A 1 111 SER 111 113 113 SER SER A . n 
A 1 112 VAL 112 114 114 VAL VAL A . n 
A 1 113 LEU 113 115 115 LEU LEU A . n 
A 1 114 ALA 114 116 116 ALA ALA A . n 
A 1 115 CYS 115 117 117 CYS CYS A . n 
A 1 116 TYR 116 118 118 TYR TYR A . n 
A 1 117 ASN 117 119 119 ASN ASN A . n 
A 1 118 GLY 118 120 120 GLY GLY A . n 
A 1 119 SER 119 121 121 SER SER A . n 
A 1 120 PRO 120 122 122 PRO PRO A . n 
A 1 121 SER 121 123 123 SER SER A . n 
A 1 122 GLY 122 124 124 GLY GLY A . n 
A 1 123 VAL 123 125 125 VAL VAL A . n 
A 1 124 TYR 124 126 126 TYR TYR A . n 
A 1 125 GLN 125 127 127 GLN GLN A . n 
A 1 126 CYS 126 128 128 CYS CYS A . n 
A 1 127 ALA 127 129 129 ALA ALA A . n 
A 1 128 MET 128 130 130 MET MET A . n 
A 1 129 ARG 129 131 131 ARG ARG A . n 
A 1 130 PRO 130 132 132 PRO PRO A . n 
A 1 131 ASN 131 133 133 ASN ASN A . n 
A 1 132 PHE 132 134 134 PHE PHE A . n 
A 1 133 THR 133 135 135 THR THR A . n 
A 1 134 ILE 134 136 136 ILE ILE A . n 
A 1 135 LYS 135 137 137 LYS LYS A . n 
A 1 136 GLY 136 138 138 GLY GLY A . n 
A 1 137 SER 137 139 139 SER SER A . n 
A 1 138 PHE 138 140 140 PHE PHE A . n 
A 1 139 LEU 139 141 141 LEU LEU A . n 
A 1 140 ALA 140 142 142 ALA ALA A . n 
A 1 141 GLY 141 143 143 GLY GLY A . n 
A 1 142 SER 142 144 144 SER SER A . n 
A 1 143 CYS 143 145 145 CYS CYS A . n 
A 1 144 GLY 144 146 146 GLY GLY A . n 
A 1 145 SER 145 147 147 SER SER A . n 
A 1 146 VAL 146 148 148 VAL VAL A . n 
A 1 147 GLY 147 149 149 GLY GLY A . n 
A 1 148 PHE 148 150 150 PHE PHE A . n 
A 1 149 ASN 149 151 151 ASN ASN A . n 
A 1 150 ILE 150 152 152 ILE ILE A . n 
A 1 151 ASP 151 153 153 ASP ASP A . n 
A 1 152 TYR 152 154 154 TYR TYR A . n 
A 1 153 ASP 153 155 155 ASP ASP A . n 
A 1 154 CYS 154 156 156 CYS CYS A . n 
A 1 155 VAL 155 157 157 VAL VAL A . n 
A 1 156 SER 156 158 158 SER SER A . n 
A 1 157 PHE 157 159 159 PHE PHE A . n 
A 1 158 CYS 158 160 160 CYS CYS A . n 
A 1 159 TYR 159 161 161 TYR TYR A . n 
A 1 160 MET 160 162 162 MET MET A . n 
A 1 161 HIS 161 163 163 HIS HIS A . n 
A 1 162 HIS 162 164 164 HIS HIS A . n 
A 1 163 MET 163 165 165 MET MET A . n 
A 1 164 GLU 164 166 166 GLU GLU A . n 
A 1 165 LEU 165 167 167 LEU LEU A . n 
A 1 166 PRO 166 168 168 PRO PRO A . n 
A 1 167 THR 167 169 169 THR THR A . n 
A 1 168 GLY 168 170 170 GLY GLY A . n 
A 1 169 VAL 169 171 171 VAL VAL A . n 
A 1 170 HIS 170 172 172 HIS HIS A . n 
A 1 171 ALA 171 173 173 ALA ALA A . n 
A 1 172 GLY 172 174 174 GLY GLY A . n 
A 1 173 THR 173 175 175 THR THR A . n 
A 1 174 ASP 174 176 176 ASP ASP A . n 
A 1 175 LEU 175 177 177 LEU LEU A . n 
A 1 176 GLU 176 178 178 GLU GLU A . n 
A 1 177 GLY 177 179 179 GLY GLY A . n 
A 1 178 ASN 178 180 180 ASN ASN A . n 
A 1 179 PHE 179 181 181 PHE PHE A . n 
A 1 180 TYR 180 182 182 TYR TYR A . n 
A 1 181 GLY 181 183 183 GLY GLY A . n 
A 1 182 PRO 182 184 184 PRO PRO A . n 
A 1 183 PHE 183 185 185 PHE PHE A . n 
A 1 184 VAL 184 186 186 VAL VAL A . n 
A 1 185 ASP 185 187 187 ASP ASP A . n 
A 1 186 ARG 186 188 188 ARG ARG A . n 
A 1 187 GLN 187 189 189 GLN GLN A . n 
A 1 188 THR 188 190 190 THR THR A . n 
A 1 189 ALA 189 191 191 ALA ALA A . n 
A 1 190 GLN 190 192 192 GLN GLN A . n 
A 1 191 ALA 191 193 193 ALA ALA A . n 
A 1 192 ALA 192 194 194 ALA ALA A . n 
A 1 193 GLY 193 195 195 GLY GLY A . n 
A 1 194 THR 194 196 196 THR THR A . n 
A 1 195 ASP 195 197 197 ASP ASP A . n 
A 1 196 THR 196 198 198 THR THR A . n 
A 1 197 THR 197 199 199 THR THR A . n 
A 1 198 ILE 198 200 200 ILE ILE A . n 
A 1 199 THR 199 201 201 THR THR A . n 
A 1 200 VAL 200 202 202 VAL VAL A . n 
A 1 201 ASN 201 203 203 ASN ASN A . n 
A 1 202 VAL 202 204 204 VAL VAL A . n 
A 1 203 LEU 203 205 205 LEU LEU A . n 
A 1 204 ALA 204 206 206 ALA ALA A . n 
A 1 205 TRP 205 207 207 TRP TRP A . n 
A 1 206 LEU 206 208 208 LEU LEU A . n 
A 1 207 TYR 207 209 209 TYR TYR A . n 
A 1 208 ALA 208 210 210 ALA ALA A . n 
A 1 209 ALA 209 211 211 ALA ALA A . n 
A 1 210 VAL 210 212 212 VAL VAL A . n 
A 1 211 ILE 211 213 213 ILE ILE A . n 
A 1 212 ASN 212 214 214 ASN ASN A . n 
A 1 213 GLY 213 215 215 GLY GLY A . n 
A 1 214 ASP 214 216 216 ASP ASP A . n 
A 1 215 ARG 215 217 217 ARG ARG A . n 
A 1 216 TRP 216 218 218 TRP TRP A . n 
A 1 217 PHE 217 219 219 PHE PHE A . n 
A 1 218 LEU 218 220 220 LEU LEU A . n 
A 1 219 ASN 219 221 221 ASN ASN A . n 
A 1 220 ARG 220 222 222 ARG ARG A . n 
A 1 221 PHE 221 223 223 PHE PHE A . n 
A 1 222 THR 222 224 224 THR THR A . n 
A 1 223 THR 223 225 225 THR THR A . n 
A 1 224 THR 224 226 226 THR THR A . n 
A 1 225 LEU 225 227 227 LEU LEU A . n 
A 1 226 ASN 226 228 228 ASN ASN A . n 
A 1 227 ASP 227 229 229 ASP ASP A . n 
A 1 228 PHE 228 230 230 PHE PHE A . n 
A 1 229 ASN 229 231 231 ASN ASN A . n 
A 1 230 LEU 230 232 232 LEU LEU A . n 
A 1 231 VAL 231 233 233 VAL VAL A . n 
A 1 232 ALA 232 234 234 ALA ALA A . n 
A 1 233 MET 233 235 235 MET MET A . n 
A 1 234 LYS 234 236 236 LYS LYS A . n 
A 1 235 TYR 235 237 237 TYR TYR A . n 
A 1 236 ASN 236 238 238 ASN ASN A . n 
A 1 237 TYR 237 239 239 TYR TYR A . n 
A 1 238 GLU 238 240 240 GLU GLU A . n 
A 1 239 PRO 239 241 241 PRO PRO A . n 
A 1 240 LEU 240 242 242 LEU LEU A . n 
A 1 241 THR 241 243 243 THR THR A . n 
A 1 242 GLN 242 244 244 GLN GLN A . n 
A 1 243 ASP 243 245 245 ASP ASP A . n 
A 1 244 HIS 244 246 246 HIS HIS A . n 
A 1 245 VAL 245 247 247 VAL VAL A . n 
A 1 246 ASP 246 248 248 ASP ASP A . n 
A 1 247 ILE 247 249 249 ILE ILE A . n 
A 1 248 LEU 248 250 250 LEU LEU A . n 
A 1 249 GLY 249 251 251 GLY GLY A . n 
A 1 250 PRO 250 252 252 PRO PRO A . n 
A 1 251 LEU 251 253 253 LEU LEU A . n 
A 1 252 SER 252 254 254 SER SER A . n 
A 1 253 ALA 253 255 255 ALA ALA A . n 
A 1 254 GLN 254 256 256 GLN GLN A . n 
A 1 255 THR 255 257 257 THR THR A . n 
A 1 256 GLY 256 258 258 GLY GLY A . n 
A 1 257 ILE 257 259 259 ILE ILE A . n 
A 1 258 ALA 258 260 260 ALA ALA A . n 
A 1 259 VAL 259 261 261 VAL VAL A . n 
A 1 260 LEU 260 262 262 LEU LEU A . n 
A 1 261 ASP 261 263 263 ASP ASP A . n 
A 1 262 MET 262 264 264 MET MET A . n 
A 1 263 CYS 263 265 265 CYS CYS A . n 
A 1 264 ALA 264 266 266 ALA ALA A . n 
A 1 265 SER 265 267 267 SER SER A . n 
A 1 266 LEU 266 268 268 LEU LEU A . n 
A 1 267 LYS 267 269 269 LYS LYS A . n 
A 1 268 GLU 268 270 270 GLU GLU A . n 
A 1 269 LEU 269 271 271 LEU LEU A . n 
A 1 270 LEU 270 272 272 LEU LEU A . n 
A 1 271 GLN 271 273 273 GLN GLN A . n 
A 1 272 ASN 272 274 274 ASN ASN A . n 
A 1 273 GLY 273 275 275 GLY GLY A . n 
A 1 274 MET 274 276 276 MET MET A . n 
A 1 275 ASN 275 277 277 ASN ASN A . n 
A 1 276 GLY 276 278 278 GLY GLY A . n 
A 1 277 ARG 277 279 279 ARG ARG A . n 
A 1 278 THR 278 280 280 THR THR A . n 
A 1 279 ILE 279 281 281 ILE ILE A . n 
A 1 280 LEU 280 282 282 LEU LEU A . n 
A 1 281 GLY 281 283 283 GLY GLY A . n 
A 1 282 SER 282 284 284 SER SER A . n 
A 1 283 ALA 283 285 285 ALA ALA A . n 
A 1 284 LEU 284 286 286 LEU LEU A . n 
A 1 285 LEU 285 287 287 LEU LEU A . n 
A 1 286 GLU 286 288 288 GLU GLU A . n 
A 1 287 ASP 287 289 289 ASP ASP A . n 
A 1 288 GLU 288 290 290 GLU GLU A . n 
A 1 289 PHE 289 291 291 PHE PHE A . n 
A 1 290 THR 290 292 292 THR THR A . n 
A 1 291 PRO 291 293 293 PRO PRO A . n 
A 1 292 PHE 292 294 294 PHE PHE A . n 
A 1 293 ASP 293 295 295 ASP ASP A . n 
A 1 294 VAL 294 296 296 VAL VAL A . n 
A 1 295 VAL 295 297 297 VAL VAL A . n 
A 1 296 ARG 296 298 298 ARG ARG A . n 
B 1 1   PHE 1   3   3   PHE PHE B . n 
B 1 2   ARG 2   4   4   ARG ARG B . n 
B 1 3   LYS 3   5   5   LYS LYS B . n 
B 1 4   MET 4   6   6   MET MET B . n 
B 1 5   ALA 5   7   7   ALA ALA B . n 
B 1 6   PHE 6   8   8   PHE PHE B . n 
B 1 7   PRO 7   9   9   PRO PRO B . n 
B 1 8   SER 8   10  10  SER SER B . n 
B 1 9   GLY 9   11  11  GLY GLY B . n 
B 1 10  LYS 10  12  12  LYS LYS B . n 
B 1 11  VAL 11  13  13  VAL VAL B . n 
B 1 12  GLU 12  14  14  GLU GLU B . n 
B 1 13  GLY 13  15  15  GLY GLY B . n 
B 1 14  CYS 14  16  16  CYS CYS B . n 
B 1 15  MET 15  17  17  MET MET B . n 
B 1 16  VAL 16  18  18  VAL VAL B . n 
B 1 17  GLN 17  19  19  GLN GLN B . n 
B 1 18  VAL 18  20  20  VAL VAL B . n 
B 1 19  THR 19  21  21  THR THR B . n 
B 1 20  CYS 20  22  22  CYS CYS B . n 
B 1 21  GLY 21  23  23  GLY GLY B . n 
B 1 22  THR 22  24  24  THR THR B . n 
B 1 23  THR 23  25  25  THR THR B . n 
B 1 24  THR 24  26  26  THR THR B . n 
B 1 25  LEU 25  27  27  LEU LEU B . n 
B 1 26  ASN 26  28  28  ASN ASN B . n 
B 1 27  GLY 27  29  29  GLY GLY B . n 
B 1 28  LEU 28  30  30  LEU LEU B . n 
B 1 29  TRP 29  31  31  TRP TRP B . n 
B 1 30  LEU 30  32  32  LEU LEU B . n 
B 1 31  ASP 31  33  33  ASP ASP B . n 
B 1 32  ASP 32  34  34  ASP ASP B . n 
B 1 33  VAL 33  35  35  VAL VAL B . n 
B 1 34  VAL 34  36  36  VAL VAL B . n 
B 1 35  TYR 35  37  37  TYR TYR B . n 
B 1 36  CYS 36  38  38  CYS CYS B . n 
B 1 37  PRO 37  39  39  PRO PRO B . n 
B 1 38  ARG 38  40  40  ARG ARG B . n 
B 1 39  HIS 39  41  41  HIS HIS B . n 
B 1 40  VAL 40  42  42  VAL VAL B . n 
B 1 41  ILE 41  43  43  ILE ILE B . n 
B 1 42  CYS 42  44  44  CYS CYS B . n 
B 1 43  THR 43  45  45  THR THR B . n 
B 1 44  SER 44  46  ?   ?   ?   B . n 
B 1 45  GLU 45  47  ?   ?   ?   B . n 
B 1 46  ASN 46  48  ?   ?   ?   B . n 
B 1 47  MET 47  49  ?   ?   ?   B . n 
B 1 48  LEU 48  50  ?   ?   ?   B . n 
B 1 49  ASN 49  51  51  ASN ASN B . n 
B 1 50  PRO 50  52  52  PRO PRO B . n 
B 1 51  ASN 51  53  53  ASN ASN B . n 
B 1 52  TYR 52  54  54  TYR TYR B . n 
B 1 53  GLU 53  55  55  GLU GLU B . n 
B 1 54  ASP 54  56  56  ASP ASP B . n 
B 1 55  LEU 55  57  57  LEU LEU B . n 
B 1 56  LEU 56  58  58  LEU LEU B . n 
B 1 57  ILE 57  59  59  ILE ILE B . n 
B 1 58  ARG 58  60  60  ARG ARG B . n 
B 1 59  LYS 59  61  61  LYS LYS B . n 
B 1 60  SER 60  62  62  SER SER B . n 
B 1 61  ASN 61  63  63  ASN ASN B . n 
B 1 62  HIS 62  64  64  HIS HIS B . n 
B 1 63  ASN 63  65  65  ASN ASN B . n 
B 1 64  PHE 64  66  66  PHE PHE B . n 
B 1 65  LEU 65  67  67  LEU LEU B . n 
B 1 66  VAL 66  68  68  VAL VAL B . n 
B 1 67  GLN 67  69  69  GLN GLN B . n 
B 1 68  ALA 68  70  70  ALA ALA B . n 
B 1 69  GLY 69  71  71  GLY GLY B . n 
B 1 70  ASN 70  72  72  ASN ASN B . n 
B 1 71  VAL 71  73  73  VAL VAL B . n 
B 1 72  GLN 72  74  74  GLN GLN B . n 
B 1 73  LEU 73  75  75  LEU LEU B . n 
B 1 74  ARG 74  76  76  ARG ARG B . n 
B 1 75  VAL 75  77  77  VAL VAL B . n 
B 1 76  ILE 76  78  78  ILE ILE B . n 
B 1 77  GLY 77  79  79  GLY GLY B . n 
B 1 78  HIS 78  80  80  HIS HIS B . n 
B 1 79  SER 79  81  81  SER SER B . n 
B 1 80  MET 80  82  82  MET MET B . n 
B 1 81  GLN 81  83  83  GLN GLN B . n 
B 1 82  ASN 82  84  84  ASN ASN B . n 
B 1 83  CYS 83  85  85  CYS CYS B . n 
B 1 84  VAL 84  86  86  VAL VAL B . n 
B 1 85  LEU 85  87  87  LEU LEU B . n 
B 1 86  LYS 86  88  88  LYS LYS B . n 
B 1 87  LEU 87  89  89  LEU LEU B . n 
B 1 88  LYS 88  90  90  LYS LYS B . n 
B 1 89  VAL 89  91  91  VAL VAL B . n 
B 1 90  ASP 90  92  92  ASP ASP B . n 
B 1 91  THR 91  93  93  THR THR B . n 
B 1 92  ALA 92  94  94  ALA ALA B . n 
B 1 93  ASN 93  95  95  ASN ASN B . n 
B 1 94  PRO 94  96  96  PRO PRO B . n 
B 1 95  LYS 95  97  97  LYS LYS B . n 
B 1 96  THR 96  98  98  THR THR B . n 
B 1 97  PRO 97  99  99  PRO PRO B . n 
B 1 98  LYS 98  100 100 LYS LYS B . n 
B 1 99  TYR 99  101 101 TYR TYR B . n 
B 1 100 LYS 100 102 102 LYS LYS B . n 
B 1 101 PHE 101 103 103 PHE PHE B . n 
B 1 102 VAL 102 104 104 VAL VAL B . n 
B 1 103 ARG 103 105 105 ARG ARG B . n 
B 1 104 ILE 104 106 106 ILE ILE B . n 
B 1 105 GLN 105 107 107 GLN GLN B . n 
B 1 106 PRO 106 108 108 PRO PRO B . n 
B 1 107 GLY 107 109 109 GLY GLY B . n 
B 1 108 GLN 108 110 110 GLN GLN B . n 
B 1 109 THR 109 111 111 THR THR B . n 
B 1 110 PHE 110 112 112 PHE PHE B . n 
B 1 111 SER 111 113 113 SER SER B . n 
B 1 112 VAL 112 114 114 VAL VAL B . n 
B 1 113 LEU 113 115 115 LEU LEU B . n 
B 1 114 ALA 114 116 116 ALA ALA B . n 
B 1 115 CYS 115 117 117 CYS CYS B . n 
B 1 116 TYR 116 118 118 TYR TYR B . n 
B 1 117 ASN 117 119 119 ASN ASN B . n 
B 1 118 GLY 118 120 120 GLY GLY B . n 
B 1 119 SER 119 121 121 SER SER B . n 
B 1 120 PRO 120 122 122 PRO PRO B . n 
B 1 121 SER 121 123 123 SER SER B . n 
B 1 122 GLY 122 124 124 GLY GLY B . n 
B 1 123 VAL 123 125 125 VAL VAL B . n 
B 1 124 TYR 124 126 126 TYR TYR B . n 
B 1 125 GLN 125 127 127 GLN GLN B . n 
B 1 126 CYS 126 128 128 CYS CYS B . n 
B 1 127 ALA 127 129 129 ALA ALA B . n 
B 1 128 MET 128 130 130 MET MET B . n 
B 1 129 ARG 129 131 131 ARG ARG B . n 
B 1 130 PRO 130 132 132 PRO PRO B . n 
B 1 131 ASN 131 133 133 ASN ASN B . n 
B 1 132 PHE 132 134 134 PHE PHE B . n 
B 1 133 THR 133 135 135 THR THR B . n 
B 1 134 ILE 134 136 136 ILE ILE B . n 
B 1 135 LYS 135 137 137 LYS LYS B . n 
B 1 136 GLY 136 138 138 GLY GLY B . n 
B 1 137 SER 137 139 139 SER SER B . n 
B 1 138 PHE 138 140 140 PHE PHE B . n 
B 1 139 LEU 139 141 141 LEU LEU B . n 
B 1 140 ALA 140 142 142 ALA ALA B . n 
B 1 141 GLY 141 143 143 GLY GLY B . n 
B 1 142 SER 142 144 144 SER SER B . n 
B 1 143 CYS 143 145 145 CYS CYS B . n 
B 1 144 GLY 144 146 146 GLY GLY B . n 
B 1 145 SER 145 147 147 SER SER B . n 
B 1 146 VAL 146 148 148 VAL VAL B . n 
B 1 147 GLY 147 149 149 GLY GLY B . n 
B 1 148 PHE 148 150 150 PHE PHE B . n 
B 1 149 ASN 149 151 151 ASN ASN B . n 
B 1 150 ILE 150 152 152 ILE ILE B . n 
B 1 151 ASP 151 153 153 ASP ASP B . n 
B 1 152 TYR 152 154 154 TYR TYR B . n 
B 1 153 ASP 153 155 155 ASP ASP B . n 
B 1 154 CYS 154 156 156 CYS CYS B . n 
B 1 155 VAL 155 157 157 VAL VAL B . n 
B 1 156 SER 156 158 158 SER SER B . n 
B 1 157 PHE 157 159 159 PHE PHE B . n 
B 1 158 CYS 158 160 160 CYS CYS B . n 
B 1 159 TYR 159 161 161 TYR TYR B . n 
B 1 160 MET 160 162 162 MET MET B . n 
B 1 161 HIS 161 163 163 HIS HIS B . n 
B 1 162 HIS 162 164 164 HIS HIS B . n 
B 1 163 MET 163 165 165 MET MET B . n 
B 1 164 GLU 164 166 166 GLU GLU B . n 
B 1 165 LEU 165 167 167 LEU LEU B . n 
B 1 166 PRO 166 168 168 PRO PRO B . n 
B 1 167 THR 167 169 169 THR THR B . n 
B 1 168 GLY 168 170 170 GLY GLY B . n 
B 1 169 VAL 169 171 171 VAL VAL B . n 
B 1 170 HIS 170 172 172 HIS HIS B . n 
B 1 171 ALA 171 173 173 ALA ALA B . n 
B 1 172 GLY 172 174 174 GLY GLY B . n 
B 1 173 THR 173 175 175 THR THR B . n 
B 1 174 ASP 174 176 176 ASP ASP B . n 
B 1 175 LEU 175 177 177 LEU LEU B . n 
B 1 176 GLU 176 178 178 GLU GLU B . n 
B 1 177 GLY 177 179 179 GLY GLY B . n 
B 1 178 ASN 178 180 180 ASN ASN B . n 
B 1 179 PHE 179 181 181 PHE PHE B . n 
B 1 180 TYR 180 182 182 TYR TYR B . n 
B 1 181 GLY 181 183 183 GLY GLY B . n 
B 1 182 PRO 182 184 184 PRO PRO B . n 
B 1 183 PHE 183 185 185 PHE PHE B . n 
B 1 184 VAL 184 186 186 VAL VAL B . n 
B 1 185 ASP 185 187 187 ASP ASP B . n 
B 1 186 ARG 186 188 188 ARG ARG B . n 
B 1 187 GLN 187 189 189 GLN GLN B . n 
B 1 188 THR 188 190 190 THR THR B . n 
B 1 189 ALA 189 191 191 ALA ALA B . n 
B 1 190 GLN 190 192 192 GLN GLN B . n 
B 1 191 ALA 191 193 193 ALA ALA B . n 
B 1 192 ALA 192 194 194 ALA ALA B . n 
B 1 193 GLY 193 195 195 GLY GLY B . n 
B 1 194 THR 194 196 196 THR THR B . n 
B 1 195 ASP 195 197 197 ASP ASP B . n 
B 1 196 THR 196 198 198 THR THR B . n 
B 1 197 THR 197 199 199 THR THR B . n 
B 1 198 ILE 198 200 200 ILE ILE B . n 
B 1 199 THR 199 201 201 THR THR B . n 
B 1 200 VAL 200 202 202 VAL VAL B . n 
B 1 201 ASN 201 203 203 ASN ASN B . n 
B 1 202 VAL 202 204 204 VAL VAL B . n 
B 1 203 LEU 203 205 205 LEU LEU B . n 
B 1 204 ALA 204 206 206 ALA ALA B . n 
B 1 205 TRP 205 207 207 TRP TRP B . n 
B 1 206 LEU 206 208 208 LEU LEU B . n 
B 1 207 TYR 207 209 209 TYR TYR B . n 
B 1 208 ALA 208 210 210 ALA ALA B . n 
B 1 209 ALA 209 211 211 ALA ALA B . n 
B 1 210 VAL 210 212 212 VAL VAL B . n 
B 1 211 ILE 211 213 213 ILE ILE B . n 
B 1 212 ASN 212 214 214 ASN ASN B . n 
B 1 213 GLY 213 215 215 GLY GLY B . n 
B 1 214 ASP 214 216 216 ASP ASP B . n 
B 1 215 ARG 215 217 217 ARG ARG B . n 
B 1 216 TRP 216 218 218 TRP TRP B . n 
B 1 217 PHE 217 219 219 PHE PHE B . n 
B 1 218 LEU 218 220 220 LEU LEU B . n 
B 1 219 ASN 219 221 221 ASN ASN B . n 
B 1 220 ARG 220 222 222 ARG ARG B . n 
B 1 221 PHE 221 223 223 PHE PHE B . n 
B 1 222 THR 222 224 224 THR THR B . n 
B 1 223 THR 223 225 225 THR THR B . n 
B 1 224 THR 224 226 226 THR THR B . n 
B 1 225 LEU 225 227 227 LEU LEU B . n 
B 1 226 ASN 226 228 228 ASN ASN B . n 
B 1 227 ASP 227 229 229 ASP ASP B . n 
B 1 228 PHE 228 230 230 PHE PHE B . n 
B 1 229 ASN 229 231 231 ASN ASN B . n 
B 1 230 LEU 230 232 232 LEU LEU B . n 
B 1 231 VAL 231 233 233 VAL VAL B . n 
B 1 232 ALA 232 234 234 ALA ALA B . n 
B 1 233 MET 233 235 235 MET MET B . n 
B 1 234 LYS 234 236 236 LYS LYS B . n 
B 1 235 TYR 235 237 237 TYR TYR B . n 
B 1 236 ASN 236 238 238 ASN ASN B . n 
B 1 237 TYR 237 239 239 TYR TYR B . n 
B 1 238 GLU 238 240 240 GLU GLU B . n 
B 1 239 PRO 239 241 241 PRO PRO B . n 
B 1 240 LEU 240 242 242 LEU LEU B . n 
B 1 241 THR 241 243 243 THR THR B . n 
B 1 242 GLN 242 244 244 GLN GLN B . n 
B 1 243 ASP 243 245 245 ASP ASP B . n 
B 1 244 HIS 244 246 246 HIS HIS B . n 
B 1 245 VAL 245 247 247 VAL VAL B . n 
B 1 246 ASP 246 248 248 ASP ASP B . n 
B 1 247 ILE 247 249 249 ILE ILE B . n 
B 1 248 LEU 248 250 250 LEU LEU B . n 
B 1 249 GLY 249 251 251 GLY GLY B . n 
B 1 250 PRO 250 252 252 PRO PRO B . n 
B 1 251 LEU 251 253 253 LEU LEU B . n 
B 1 252 SER 252 254 254 SER SER B . n 
B 1 253 ALA 253 255 255 ALA ALA B . n 
B 1 254 GLN 254 256 256 GLN GLN B . n 
B 1 255 THR 255 257 257 THR THR B . n 
B 1 256 GLY 256 258 258 GLY GLY B . n 
B 1 257 ILE 257 259 259 ILE ILE B . n 
B 1 258 ALA 258 260 260 ALA ALA B . n 
B 1 259 VAL 259 261 261 VAL VAL B . n 
B 1 260 LEU 260 262 262 LEU LEU B . n 
B 1 261 ASP 261 263 263 ASP ASP B . n 
B 1 262 MET 262 264 264 MET MET B . n 
B 1 263 CYS 263 265 265 CYS CYS B . n 
B 1 264 ALA 264 266 266 ALA ALA B . n 
B 1 265 SER 265 267 267 SER SER B . n 
B 1 266 LEU 266 268 268 LEU LEU B . n 
B 1 267 LYS 267 269 269 LYS LYS B . n 
B 1 268 GLU 268 270 270 GLU GLU B . n 
B 1 269 LEU 269 271 271 LEU LEU B . n 
B 1 270 LEU 270 272 272 LEU LEU B . n 
B 1 271 GLN 271 273 273 GLN GLN B . n 
B 1 272 ASN 272 274 274 ASN ASN B . n 
B 1 273 GLY 273 275 275 GLY GLY B . n 
B 1 274 MET 274 276 276 MET MET B . n 
B 1 275 ASN 275 277 277 ASN ASN B . n 
B 1 276 GLY 276 278 278 GLY GLY B . n 
B 1 277 ARG 277 279 279 ARG ARG B . n 
B 1 278 THR 278 280 280 THR THR B . n 
B 1 279 ILE 279 281 281 ILE ILE B . n 
B 1 280 LEU 280 282 282 LEU LEU B . n 
B 1 281 GLY 281 283 283 GLY GLY B . n 
B 1 282 SER 282 284 284 SER SER B . n 
B 1 283 ALA 283 285 285 ALA ALA B . n 
B 1 284 LEU 284 286 286 LEU LEU B . n 
B 1 285 LEU 285 287 287 LEU LEU B . n 
B 1 286 GLU 286 288 288 GLU GLU B . n 
B 1 287 ASP 287 289 289 ASP ASP B . n 
B 1 288 GLU 288 290 290 GLU GLU B . n 
B 1 289 PHE 289 291 291 PHE PHE B . n 
B 1 290 THR 290 292 292 THR THR B . n 
B 1 291 PRO 291 293 293 PRO PRO B . n 
B 1 292 PHE 292 294 294 PHE PHE B . n 
B 1 293 ASP 293 295 295 ASP ASP B . n 
B 1 294 VAL 294 296 296 VAL VAL B . n 
B 1 295 VAL 295 297 297 VAL VAL B . n 
B 1 296 ARG 296 298 298 ARG ARG B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        FNO 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   FNO 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 FNO 1  301 1  FNO LIG A . 
D 3 HOH 1  401 77 HOH HOH A . 
D 3 HOH 2  402 56 HOH HOH A . 
D 3 HOH 3  403 50 HOH HOH A . 
D 3 HOH 4  404 34 HOH HOH A . 
D 3 HOH 5  405 69 HOH HOH A . 
D 3 HOH 6  406 83 HOH HOH A . 
D 3 HOH 7  407 26 HOH HOH A . 
D 3 HOH 8  408 42 HOH HOH A . 
D 3 HOH 9  409 32 HOH HOH A . 
D 3 HOH 10 410 63 HOH HOH A . 
D 3 HOH 11 411 20 HOH HOH A . 
D 3 HOH 12 412 68 HOH HOH A . 
D 3 HOH 13 413 78 HOH HOH A . 
D 3 HOH 14 414 15 HOH HOH A . 
D 3 HOH 15 415 25 HOH HOH A . 
D 3 HOH 16 416 59 HOH HOH A . 
D 3 HOH 17 417 10 HOH HOH A . 
D 3 HOH 18 418 17 HOH HOH A . 
D 3 HOH 19 419 21 HOH HOH A . 
D 3 HOH 20 420 23 HOH HOH A . 
D 3 HOH 21 421 2  HOH HOH A . 
D 3 HOH 22 422 31 HOH HOH A . 
D 3 HOH 23 423 48 HOH HOH A . 
D 3 HOH 24 424 14 HOH HOH A . 
D 3 HOH 25 425 89 HOH HOH A . 
D 3 HOH 26 426 24 HOH HOH A . 
D 3 HOH 27 427 61 HOH HOH A . 
D 3 HOH 28 428 5  HOH HOH A . 
D 3 HOH 29 429 8  HOH HOH A . 
D 3 HOH 30 430 29 HOH HOH A . 
D 3 HOH 31 431 41 HOH HOH A . 
D 3 HOH 32 432 80 HOH HOH A . 
D 3 HOH 33 433 47 HOH HOH A . 
D 3 HOH 34 434 71 HOH HOH A . 
D 3 HOH 35 435 58 HOH HOH A . 
D 3 HOH 36 436 70 HOH HOH A . 
D 3 HOH 37 437 54 HOH HOH A . 
D 3 HOH 38 438 51 HOH HOH A . 
D 3 HOH 39 439 65 HOH HOH A . 
D 3 HOH 40 440 43 HOH HOH A . 
D 3 HOH 41 441 33 HOH HOH A . 
D 3 HOH 42 442 87 HOH HOH A . 
D 3 HOH 43 443 9  HOH HOH A . 
D 3 HOH 44 444 62 HOH HOH A . 
D 3 HOH 45 445 60 HOH HOH A . 
D 3 HOH 46 446 52 HOH HOH A . 
D 3 HOH 47 447 64 HOH HOH A . 
D 3 HOH 48 448 49 HOH HOH A . 
D 3 HOH 49 449 73 HOH HOH A . 
D 3 HOH 50 450 74 HOH HOH A . 
D 3 HOH 51 451 53 HOH HOH A . 
D 3 HOH 52 452 85 HOH HOH A . 
D 3 HOH 53 453 88 HOH HOH A . 
D 3 HOH 54 454 75 HOH HOH A . 
D 3 HOH 55 455 18 HOH HOH A . 
E 3 HOH 1  301 66 HOH HOH B . 
E 3 HOH 2  302 84 HOH HOH B . 
E 3 HOH 3  303 1  HOH HOH B . 
E 3 HOH 4  304 12 HOH HOH B . 
E 3 HOH 5  305 19 HOH HOH B . 
E 3 HOH 6  306 55 HOH HOH B . 
E 3 HOH 7  307 7  HOH HOH B . 
E 3 HOH 8  308 81 HOH HOH B . 
E 3 HOH 9  309 28 HOH HOH B . 
E 3 HOH 10 310 46 HOH HOH B . 
E 3 HOH 11 311 22 HOH HOH B . 
E 3 HOH 12 312 45 HOH HOH B . 
E 3 HOH 13 313 35 HOH HOH B . 
E 3 HOH 14 314 36 HOH HOH B . 
E 3 HOH 15 315 16 HOH HOH B . 
E 3 HOH 16 316 44 HOH HOH B . 
E 3 HOH 17 317 30 HOH HOH B . 
E 3 HOH 18 318 6  HOH HOH B . 
E 3 HOH 19 319 4  HOH HOH B . 
E 3 HOH 20 320 11 HOH HOH B . 
E 3 HOH 21 321 3  HOH HOH B . 
E 3 HOH 22 322 72 HOH HOH B . 
E 3 HOH 23 323 57 HOH HOH B . 
E 3 HOH 24 324 90 HOH HOH B . 
E 3 HOH 25 325 38 HOH HOH B . 
E 3 HOH 26 326 82 HOH HOH B . 
E 3 HOH 27 327 27 HOH HOH B . 
E 3 HOH 28 328 79 HOH HOH B . 
E 3 HOH 29 329 13 HOH HOH B . 
E 3 HOH 30 330 76 HOH HOH B . 
E 3 HOH 31 331 67 HOH HOH B . 
E 3 HOH 32 332 40 HOH HOH B . 
E 3 HOH 33 333 37 HOH HOH B . 
E 3 HOH 34 334 86 HOH HOH B . 
E 3 HOH 35 335 39 HOH HOH B . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1   1 Y 1 A GLU 47  ? CG  ? A GLU 45  CG  
2   1 Y 1 A GLU 47  ? CD  ? A GLU 45  CD  
3   1 Y 1 A GLU 47  ? OE1 ? A GLU 45  OE1 
4   1 Y 1 A GLU 47  ? OE2 ? A GLU 45  OE2 
5   1 Y 1 A MET 49  ? CG  ? A MET 47  CG  
6   1 Y 1 A MET 49  ? SD  ? A MET 47  SD  
7   1 Y 1 A MET 49  ? CE  ? A MET 47  CE  
8   1 Y 1 A ASN 72  ? CG  ? A ASN 70  CG  
9   1 Y 1 A ASN 72  ? OD1 ? A ASN 70  OD1 
10  1 Y 1 A ASN 72  ? ND2 ? A ASN 70  ND2 
11  1 Y 1 A GLN 74  ? CG  ? A GLN 72  CG  
12  1 Y 1 A GLN 74  ? CD  ? A GLN 72  CD  
13  1 Y 1 A GLN 74  ? OE1 ? A GLN 72  OE1 
14  1 Y 1 A GLN 74  ? NE2 ? A GLN 72  NE2 
15  1 Y 1 A LYS 100 ? CG  ? A LYS 98  CG  
16  1 Y 1 A LYS 100 ? CD  ? A LYS 98  CD  
17  1 Y 1 A LYS 100 ? CE  ? A LYS 98  CE  
18  1 Y 1 A LYS 100 ? NZ  ? A LYS 98  NZ  
19  1 Y 1 A TYR 118 ? CG  ? A TYR 116 CG  
20  1 Y 1 A TYR 118 ? CD1 ? A TYR 116 CD1 
21  1 Y 1 A TYR 118 ? CD2 ? A TYR 116 CD2 
22  1 Y 1 A TYR 118 ? CE1 ? A TYR 116 CE1 
23  1 Y 1 A TYR 118 ? CE2 ? A TYR 116 CE2 
24  1 Y 1 A TYR 118 ? CZ  ? A TYR 116 CZ  
25  1 Y 1 A TYR 118 ? OH  ? A TYR 116 OH  
26  1 Y 1 A ASN 119 ? CG  ? A ASN 117 CG  
27  1 Y 1 A ASN 119 ? OD1 ? A ASN 117 OD1 
28  1 Y 1 A ASN 119 ? ND2 ? A ASN 117 ND2 
29  1 Y 1 A TYR 154 ? CG  ? A TYR 152 CG  
30  1 Y 1 A TYR 154 ? CD1 ? A TYR 152 CD1 
31  1 Y 1 A TYR 154 ? CD2 ? A TYR 152 CD2 
32  1 Y 1 A TYR 154 ? CE1 ? A TYR 152 CE1 
33  1 Y 1 A TYR 154 ? CE2 ? A TYR 152 CE2 
34  1 Y 1 A TYR 154 ? CZ  ? A TYR 152 CZ  
35  1 Y 1 A TYR 154 ? OH  ? A TYR 152 OH  
36  1 Y 1 A GLU 166 ? CG  ? A GLU 164 CG  
37  1 Y 1 A GLU 166 ? CD  ? A GLU 164 CD  
38  1 Y 1 A GLU 166 ? OE1 ? A GLU 164 OE1 
39  1 Y 1 A GLU 166 ? OE2 ? A GLU 164 OE2 
40  1 Y 1 A GLN 189 ? CG  ? A GLN 187 CG  
41  1 Y 1 A GLN 189 ? CD  ? A GLN 187 CD  
42  1 Y 1 A GLN 189 ? OE1 ? A GLN 187 OE1 
43  1 Y 1 A GLN 189 ? NE2 ? A GLN 187 NE2 
44  1 Y 1 A ASN 277 ? CG  ? A ASN 275 CG  
45  1 Y 1 A ASN 277 ? OD1 ? A ASN 275 OD1 
46  1 Y 1 A ASN 277 ? ND2 ? A ASN 275 ND2 
47  1 Y 1 A LEU 286 ? CG  ? A LEU 284 CG  
48  1 Y 1 A LEU 286 ? CD1 ? A LEU 284 CD1 
49  1 Y 1 A LEU 286 ? CD2 ? A LEU 284 CD2 
50  1 Y 1 A ARG 298 ? CG  ? A ARG 296 CG  
51  1 Y 1 A ARG 298 ? CD  ? A ARG 296 CD  
52  1 Y 1 A ARG 298 ? NE  ? A ARG 296 NE  
53  1 Y 1 A ARG 298 ? CZ  ? A ARG 296 CZ  
54  1 Y 1 A ARG 298 ? NH1 ? A ARG 296 NH1 
55  1 Y 1 A ARG 298 ? NH2 ? A ARG 296 NH2 
56  1 Y 1 B GLU 55  ? CG  ? B GLU 53  CG  
57  1 Y 1 B GLU 55  ? CD  ? B GLU 53  CD  
58  1 Y 1 B GLU 55  ? OE1 ? B GLU 53  OE1 
59  1 Y 1 B GLU 55  ? OE2 ? B GLU 53  OE2 
60  1 Y 1 B ILE 59  ? CG1 ? B ILE 57  CG1 
61  1 Y 1 B ILE 59  ? CG2 ? B ILE 57  CG2 
62  1 Y 1 B ILE 59  ? CD1 ? B ILE 57  CD1 
63  1 Y 1 B ARG 60  ? CG  ? B ARG 58  CG  
64  1 Y 1 B ARG 60  ? CD  ? B ARG 58  CD  
65  1 Y 1 B ARG 60  ? NE  ? B ARG 58  NE  
66  1 Y 1 B ARG 60  ? CZ  ? B ARG 58  CZ  
67  1 Y 1 B ARG 60  ? NH1 ? B ARG 58  NH1 
68  1 Y 1 B ARG 60  ? NH2 ? B ARG 58  NH2 
69  1 Y 1 B GLN 74  ? CG  ? B GLN 72  CG  
70  1 Y 1 B GLN 74  ? CD  ? B GLN 72  CD  
71  1 Y 1 B GLN 74  ? OE1 ? B GLN 72  OE1 
72  1 Y 1 B GLN 74  ? NE2 ? B GLN 72  NE2 
73  1 Y 1 B ARG 76  ? CG  ? B ARG 74  CG  
74  1 Y 1 B ARG 76  ? CD  ? B ARG 74  CD  
75  1 Y 1 B ARG 76  ? NE  ? B ARG 74  NE  
76  1 Y 1 B ARG 76  ? CZ  ? B ARG 74  CZ  
77  1 Y 1 B ARG 76  ? NH1 ? B ARG 74  NH1 
78  1 Y 1 B ARG 76  ? NH2 ? B ARG 74  NH2 
79  1 Y 1 B VAL 77  ? CG1 ? B VAL 75  CG1 
80  1 Y 1 B VAL 77  ? CG2 ? B VAL 75  CG2 
81  1 Y 1 B LYS 100 ? CG  ? B LYS 98  CG  
82  1 Y 1 B LYS 100 ? CD  ? B LYS 98  CD  
83  1 Y 1 B LYS 100 ? CE  ? B LYS 98  CE  
84  1 Y 1 B LYS 100 ? NZ  ? B LYS 98  NZ  
85  1 Y 1 B TYR 118 ? CG  ? B TYR 116 CG  
86  1 Y 1 B TYR 118 ? CD1 ? B TYR 116 CD1 
87  1 Y 1 B TYR 118 ? CD2 ? B TYR 116 CD2 
88  1 Y 1 B TYR 118 ? CE1 ? B TYR 116 CE1 
89  1 Y 1 B TYR 118 ? CE2 ? B TYR 116 CE2 
90  1 Y 1 B TYR 118 ? CZ  ? B TYR 116 CZ  
91  1 Y 1 B TYR 118 ? OH  ? B TYR 116 OH  
92  1 Y 1 B ASN 119 ? CG  ? B ASN 117 CG  
93  1 Y 1 B ASN 119 ? OD1 ? B ASN 117 OD1 
94  1 Y 1 B ASN 119 ? ND2 ? B ASN 117 ND2 
95  1 Y 1 B LYS 137 ? CG  ? B LYS 135 CG  
96  1 Y 1 B LYS 137 ? CD  ? B LYS 135 CD  
97  1 Y 1 B LYS 137 ? CE  ? B LYS 135 CE  
98  1 Y 1 B LYS 137 ? NZ  ? B LYS 135 NZ  
99  1 Y 1 B TYR 154 ? CG  ? B TYR 152 CG  
100 1 Y 1 B TYR 154 ? CD1 ? B TYR 152 CD1 
101 1 Y 1 B TYR 154 ? CD2 ? B TYR 152 CD2 
102 1 Y 1 B TYR 154 ? CE1 ? B TYR 152 CE1 
103 1 Y 1 B TYR 154 ? CE2 ? B TYR 152 CE2 
104 1 Y 1 B TYR 154 ? CZ  ? B TYR 152 CZ  
105 1 Y 1 B TYR 154 ? OH  ? B TYR 152 OH  
106 1 Y 1 B GLU 166 ? CG  ? B GLU 164 CG  
107 1 Y 1 B GLU 166 ? CD  ? B GLU 164 CD  
108 1 Y 1 B GLU 166 ? OE1 ? B GLU 164 OE1 
109 1 Y 1 B GLU 166 ? OE2 ? B GLU 164 OE2 
110 1 Y 1 B GLN 189 ? CG  ? B GLN 187 CG  
111 1 Y 1 B GLN 189 ? CD  ? B GLN 187 CD  
112 1 Y 1 B GLN 189 ? OE1 ? B GLN 187 OE1 
113 1 Y 1 B GLN 189 ? NE2 ? B GLN 187 NE2 
114 1 Y 1 B LEU 232 ? CG  ? B LEU 230 CG  
115 1 Y 1 B LEU 232 ? CD1 ? B LEU 230 CD1 
116 1 Y 1 B LEU 232 ? CD2 ? B LEU 230 CD2 
117 1 Y 1 B MET 235 ? CG  ? B MET 233 CG  
118 1 Y 1 B MET 235 ? SD  ? B MET 233 SD  
119 1 Y 1 B MET 235 ? CE  ? B MET 233 CE  
120 1 Y 1 B LYS 236 ? CG  ? B LYS 234 CG  
121 1 Y 1 B LYS 236 ? CD  ? B LYS 234 CD  
122 1 Y 1 B LYS 236 ? CE  ? B LYS 234 CE  
123 1 Y 1 B LYS 236 ? NZ  ? B LYS 234 NZ  
124 1 Y 1 B ASP 245 ? CG  ? B ASP 243 CG  
125 1 Y 1 B ASP 245 ? OD1 ? B ASP 243 OD1 
126 1 Y 1 B ASP 245 ? OD2 ? B ASP 243 OD2 
127 1 Y 1 B ARG 279 ? CG  ? B ARG 277 CG  
128 1 Y 1 B ARG 279 ? CD  ? B ARG 277 CD  
129 1 Y 1 B ARG 279 ? NE  ? B ARG 277 NE  
130 1 Y 1 B ARG 279 ? CZ  ? B ARG 277 CZ  
131 1 Y 1 B ARG 279 ? NH1 ? B ARG 277 NH1 
132 1 Y 1 B ARG 279 ? NH2 ? B ARG 277 NH2 
133 1 Y 1 B LEU 286 ? CG  ? B LEU 284 CG  
134 1 Y 1 B LEU 286 ? CD1 ? B LEU 284 CD1 
135 1 Y 1 B LEU 286 ? CD2 ? B LEU 284 CD2 
136 1 Y 1 B ARG 298 ? CG  ? B ARG 296 CG  
137 1 Y 1 B ARG 298 ? CD  ? B ARG 296 CD  
138 1 Y 1 B ARG 298 ? NE  ? B ARG 296 NE  
139 1 Y 1 B ARG 298 ? CZ  ? B ARG 296 CZ  
140 1 Y 1 B ARG 298 ? NH1 ? B ARG 296 NH1 
141 1 Y 1 B ARG 298 ? NH2 ? B ARG 296 NH2 
# 
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       ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? 1.12_2829 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .         2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .         3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? .         4 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8WUR 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     68.052 
_cell.length_a_esd                 ? 
_cell.length_b                     102.944 
_cell.length_b_esd                 ? 
_cell.length_c                     103.687 
_cell.length_c_esd                 ? 
_cell.volume                       726383.954 
_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                         8WUR 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            'P 2ac 2ab' 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   8WUR 
_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             2.78 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          55.79 
_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, HANGING 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    '0.1M HEPES 7.5, 20% PEG 10000' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            298 
# 
_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 EIGER2 X 9M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2022-03-11 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.97918 
_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                        'SSRF BEAMLINE BL02U1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.97918 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL02U1 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate                          35.3492718145 
_reflns.entry_id                                       8WUR 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.08 
_reflns.d_resolution_low                               73.05 
_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                                     44801 
_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                           100.0 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                12.1 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          18.5 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_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                                   ? 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.1 
_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                                    2.08 
_reflns_shell.d_res_low                                     2.19 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             6441 
_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                                  ? 
_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                                  1.066 
_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]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               43.476140195 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_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                                 8WUR 
_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                            2.08 
_refine.ls_d_res_low                             46.30 
_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                     44714 
_refine.ls_number_reflns_R_free                  3813 
_refine.ls_number_reflns_R_work                  81183 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.9482596425 
_refine.ls_percent_reflns_R_free                 4.48609346322 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.211947239149 
_refine.ls_R_factor_R_free                       0.238493206353 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.210659564362 
_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                    'FLAT BULK SOLVENT MODEL' 
_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                          1.34826381753 
_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               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.11 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9 
_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                 26.1593270121 
_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                             ? 
_refine.overall_SU_ML                            0.248148446519 
_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                       2.08 
_refine_hist.d_res_low                        46.30 
_refine_hist.number_atoms_solvent             90 
_refine_hist.number_atoms_total               4510 
_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        4399 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         21 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.0084522111153  ? 4542 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.968682290854   ? 6189 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0538135263819  ? 714  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.00645023936966 ? 800  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 6.15589983494    ? 2649 ? f_dihedral_angle_d ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.08   2.1021 . . 136 3029 99.968414403  . . . . 0.309620062341 . . . . . . . . . . . 0.317748574728 
'X-RAY DIFFRACTION' 2.1021 2.1297 . . 142 3000 100.0         . . . . 0.291151992158 . . . . . . . . . . . 0.320943396761 
'X-RAY DIFFRACTION' 2.1297 2.1589 . . 150 2985 100.0         . . . . 0.26801770586  . . . . . . . . . . . 0.29360228107  
'X-RAY DIFFRACTION' 2.1589 2.1898 . . 147 3023 99.8739760555 . . . . 0.262903635139 . . . . . . . . . . . 0.302879634183 
'X-RAY DIFFRACTION' 2.1898 2.2224 . . 132 2991 99.936        . . . . 0.265414460601 . . . . . . . . . . . 0.306123729237 
'X-RAY DIFFRACTION' 2.2224 2.2572 . . 142 3008 100.0         . . . . 0.263410653662 . . . . . . . . . . . 0.27836745434  
'X-RAY DIFFRACTION' 2.2572 2.2942 . . 146 3007 100.0         . . . . 0.255363006461 . . . . . . . . . . . 0.323938369642 
'X-RAY DIFFRACTION' 2.2942 2.3337 . . 137 3027 99.9684044234 . . . . 0.239007424977 . . . . . . . . . . . 0.239970006974 
'X-RAY DIFFRACTION' 2.3337 2.3762 . . 143 3007 99.9365482234 . . . . 0.24453572661  . . . . . . . . . . . 0.297879434349 
'X-RAY DIFFRACTION' 2.3762 2.4219 . . 125 2990 99.9358357395 . . . . 0.236544419309 . . . . . . . . . . . 0.251816490798 
'X-RAY DIFFRACTION' 2.4219 2.4713 . . 147 3013 100.0         . . . . 0.235146733022 . . . . . . . . . . . 0.273454038404 
'X-RAY DIFFRACTION' 2.4713 2.525  . . 143 3024 100.0         . . . . 0.233573083108 . . . . . . . . . . . 0.259756630776 
'X-RAY DIFFRACTION' 2.525  2.5838 . . 136 2976 99.7755690927 . . . . 0.238938915998 . . . . . . . . . . . 0.271248997297 
'X-RAY DIFFRACTION' 2.5838 2.6484 . . 136 3026 100.0         . . . . 0.229223728835 . . . . . . . . . . . 0.250716348585 
'X-RAY DIFFRACTION' 2.6484 2.72   . . 148 3015 100.0         . . . . 0.228782074311 . . . . . . . . . . . 0.253372690577 
'X-RAY DIFFRACTION' 2.72   2.8    . . 129 3031 99.9367488931 . . . . 0.23744065995  . . . . . . . . . . . 0.280000046551 
'X-RAY DIFFRACTION' 2.8    2.8904 . . 150 2991 100.0         . . . . 0.220242036968 . . . . . . . . . . . 0.283854912994 
'X-RAY DIFFRACTION' 2.8904 2.9936 . . 131 2984 99.9679075738 . . . . 0.223004875989 . . . . . . . . . . . 0.268849652957 
'X-RAY DIFFRACTION' 2.9936 3.1135 . . 144 3045 99.9060150376 . . . . 0.218785215191 . . . . . . . . . . . 0.255344208053 
'X-RAY DIFFRACTION' 3.1135 3.2551 . . 144 2994 100.0         . . . . 0.230688772132 . . . . . . . . . . . 0.267584820175 
'X-RAY DIFFRACTION' 3.2551 3.4267 . . 145 3012 100.0         . . . . 0.220145801865 . . . . . . . . . . . 0.281402923537 
'X-RAY DIFFRACTION' 3.4267 3.6413 . . 141 3007 99.9682438869 . . . . 0.217110789717 . . . . . . . . . . . 0.207931322903 
'X-RAY DIFFRACTION' 3.6413 3.9223 . . 144 2980 100.0         . . . . 0.195882065151 . . . . . . . . . . . 0.23305791221  
'X-RAY DIFFRACTION' 3.9223 4.3168 . . 145 3012 100.0         . . . . 0.169876154943 . . . . . . . . . . . 0.174101925385 
'X-RAY DIFFRACTION' 4.3168 4.9408 . . 145 3012 100.0         . . . . 0.163019231166 . . . . . . . . . . . 0.188184638735 
'X-RAY DIFFRACTION' 4.9408 6.2225 . . 146 3012 99.9683444128 . . . . 0.187926568135 . . . . . . . . . . . 0.249866137197 
'X-RAY DIFFRACTION' 6.2225 46.30  . . 139 2982 99.4582536648 . . . . 0.18066627024  . . . . . . . . . . . 0.17756407098  
# 
_struct.entry_id                     8WUR 
_struct.title                        'Crystal structure of SARS-Cov-2 main protease D48N mutant in complex with shikonin' 
_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        8WUR 
_struct_keywords.text            'SARS-Cov-2, main protease, mutant, shikonin, VIRAL PROTEIN' 
_struct_keywords.pdbx_keywords   'VIRAL 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 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 3 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    R1A_SARS2 
_struct_ref.pdbx_db_accession          P0DTC1 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;FRKMAFPSGKVEGCMVQVTCGTTTLNGLWLDDVVYCPRHVICTSEDMLNPNYEDLLIRKSNHNFLVQAGNVQLRVIGHSM
QNCVLKLKVDTANPKTPKYKFVRIQPGQTFSVLACYNGSPSGVYQCAMRPNFTIKGSFLNGSCGSVGFNIDYDCVSFCYM
HHMELPTGVHAGTDLEGNFYGPFVDRQTAQAAGTDTTITVNVLAWLYAAVINGDRWFLNRFTTTLNDFNLVAMKYNYEPL
TQDHVDILGPLSAQTGIAVLDMCASLKELLQNGMNGRTILGSALLEDEFTPFDVVR
;
_struct_ref.pdbx_align_begin           3266 
# 
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 8WUR A 1 ? 296 ? P0DTC1 3266 ? 3561 ? 3 298 
2 1 8WUR B 1 ? 296 ? P0DTC1 3266 ? 3561 ? 3 298 
# 
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 8WUR ASN A 46  ? UNP P0DTC1 ASP 3311 'engineered mutation' 48  1 
1 8WUR ALA A 140 ? UNP P0DTC1 ASN 3405 conflict              142 2 
2 8WUR ASN B 46  ? UNP P0DTC1 ASP 3311 'engineered mutation' 48  3 
2 8WUR ALA B 140 ? UNP P0DTC1 ASN 3405 conflict              142 4 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
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)' 1670  ? 
1 MORE         -9    ? 
1 'SSA (A^2)'  25100 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 SER A 8   ? GLY A 13  ? SER A 10  GLY A 15  1 ? 6  
HELX_P HELX_P2  AA2 HIS A 39  ? CYS A 42  ? HIS A 41  CYS A 44  5 ? 4  
HELX_P HELX_P3  AA3 THR A 43  ? MET A 47  ? THR A 45  MET A 49  5 ? 5  
HELX_P HELX_P4  AA4 ASN A 51  ? ARG A 58  ? ASN A 53  ARG A 60  1 ? 8  
HELX_P HELX_P5  AA5 SER A 60  ? HIS A 62  ? SER A 62  HIS A 64  5 ? 3  
HELX_P HELX_P6  AA6 ILE A 198 ? ASN A 212 ? ILE A 200 ASN A 214 1 ? 15 
HELX_P HELX_P7  AA7 THR A 224 ? LYS A 234 ? THR A 226 LYS A 236 1 ? 11 
HELX_P HELX_P8  AA8 THR A 241 ? GLY A 256 ? THR A 243 GLY A 258 1 ? 16 
HELX_P HELX_P9  AA9 ALA A 258 ? GLY A 273 ? ALA A 260 GLY A 275 1 ? 16 
HELX_P HELX_P10 AB1 THR A 290 ? ARG A 296 ? THR A 292 ARG A 298 1 ? 7  
HELX_P HELX_P11 AB2 SER B 8   ? GLY B 13  ? SER B 10  GLY B 15  1 ? 6  
HELX_P HELX_P12 AB3 HIS B 39  ? CYS B 42  ? HIS B 41  CYS B 44  5 ? 4  
HELX_P HELX_P13 AB4 ASN B 51  ? ARG B 58  ? ASN B 53  ARG B 60  1 ? 8  
HELX_P HELX_P14 AB5 SER B 60  ? HIS B 62  ? SER B 62  HIS B 64  5 ? 3  
HELX_P HELX_P15 AB6 ILE B 198 ? ASN B 212 ? ILE B 200 ASN B 214 1 ? 15 
HELX_P HELX_P16 AB7 THR B 224 ? TYR B 235 ? THR B 226 TYR B 237 1 ? 12 
HELX_P HELX_P17 AB8 THR B 241 ? LEU B 248 ? THR B 243 LEU B 250 1 ? 8  
HELX_P HELX_P18 AB9 LEU B 248 ? GLY B 256 ? LEU B 250 GLY B 258 1 ? 9  
HELX_P HELX_P19 AC1 ALA B 258 ? GLY B 273 ? ALA B 260 GLY B 275 1 ? 16 
HELX_P HELX_P20 AC2 THR B 290 ? ARG B 296 ? THR B 292 ARG B 298 1 ? 7  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_struct_conn.id                            covale1 
_struct_conn.conn_type_id                  covale 
_struct_conn.pdbx_leaving_atom_flag        none 
_struct_conn.pdbx_PDB_id                   ? 
_struct_conn.ptnr1_label_asym_id           A 
_struct_conn.ptnr1_label_comp_id           CYS 
_struct_conn.ptnr1_label_seq_id            143 
_struct_conn.ptnr1_label_atom_id           SG 
_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                1_555 
_struct_conn.ptnr2_label_asym_id           C 
_struct_conn.ptnr2_label_comp_id           FNO 
_struct_conn.ptnr2_label_seq_id            . 
_struct_conn.ptnr2_label_atom_id           C19 
_struct_conn.pdbx_ptnr2_label_alt_id       ? 
_struct_conn.pdbx_ptnr2_PDB_ins_code       ? 
_struct_conn.ptnr1_auth_asym_id            A 
_struct_conn.ptnr1_auth_comp_id            CYS 
_struct_conn.ptnr1_auth_seq_id             145 
_struct_conn.ptnr2_auth_asym_id            A 
_struct_conn.ptnr2_auth_comp_id            FNO 
_struct_conn.ptnr2_auth_seq_id             301 
_struct_conn.ptnr2_symmetry                1_555 
_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               1.574 
_struct_conn.pdbx_value_order              ? 
_struct_conn.pdbx_role                     ? 
# 
_struct_conn_type.id          covale 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
_pdbx_modification_feature.ordinal                            1 
_pdbx_modification_feature.label_comp_id                      FNO 
_pdbx_modification_feature.label_asym_id                      C 
_pdbx_modification_feature.label_seq_id                       . 
_pdbx_modification_feature.label_alt_id                       ? 
_pdbx_modification_feature.modified_residue_label_comp_id     CYS 
_pdbx_modification_feature.modified_residue_label_asym_id     A 
_pdbx_modification_feature.modified_residue_label_seq_id      143 
_pdbx_modification_feature.modified_residue_label_alt_id      ? 
_pdbx_modification_feature.auth_comp_id                       FNO 
_pdbx_modification_feature.auth_asym_id                       A 
_pdbx_modification_feature.auth_seq_id                        301 
_pdbx_modification_feature.PDB_ins_code                       ? 
_pdbx_modification_feature.symmetry                           1_555 
_pdbx_modification_feature.modified_residue_auth_comp_id      CYS 
_pdbx_modification_feature.modified_residue_auth_asym_id      A 
_pdbx_modification_feature.modified_residue_auth_seq_id       145 
_pdbx_modification_feature.modified_residue_PDB_ins_code      ? 
_pdbx_modification_feature.modified_residue_symmetry          1_555 
_pdbx_modification_feature.comp_id_linking_atom               C19 
_pdbx_modification_feature.modified_residue_id_linking_atom   SG 
_pdbx_modification_feature.modified_residue_id                CYS 
_pdbx_modification_feature.ref_pcm_id                         1 
_pdbx_modification_feature.ref_comp_id                        FNO 
_pdbx_modification_feature.type                               None 
_pdbx_modification_feature.category                           'Covalent chemical modification' 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 7 ? 
AA2 ? 5 ? 
AA3 ? 3 ? 
AA4 ? 7 ? 
AA5 ? 5 ? 
AA6 ? 3 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA1 6 7 ? anti-parallel 
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA3 1 2 ? parallel      
AA3 2 3 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA4 4 5 ? anti-parallel 
AA4 5 6 ? anti-parallel 
AA4 6 7 ? anti-parallel 
AA5 1 2 ? parallel      
AA5 2 3 ? anti-parallel 
AA5 3 4 ? anti-parallel 
AA5 4 5 ? anti-parallel 
AA6 1 2 ? parallel      
AA6 2 3 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 VAL A 71  ? LEU A 73  ? VAL A 73  LEU A 75  
AA1 2 PHE A 64  ? ALA A 68  ? PHE A 66  ALA A 70  
AA1 3 MET A 15  ? CYS A 20  ? MET A 17  CYS A 22  
AA1 4 THR A 23  ? LEU A 30  ? THR A 25  LEU A 32  
AA1 5 VAL A 33  ? PRO A 37  ? VAL A 35  PRO A 39  
AA1 6 VAL A 84  ? VAL A 89  ? VAL A 86  VAL A 91  
AA1 7 VAL A 75  ? GLN A 81  ? VAL A 77  GLN A 83  
AA2 1 TYR A 99  ? PHE A 101 ? TYR A 101 PHE A 103 
AA2 2 CYS A 154 ? GLU A 164 ? CYS A 156 GLU A 166 
AA2 3 VAL A 146 ? ASP A 151 ? VAL A 148 ASP A 153 
AA2 4 THR A 109 ? TYR A 116 ? THR A 111 TYR A 118 
AA2 5 SER A 119 ? ALA A 127 ? SER A 121 ALA A 129 
AA3 1 TYR A 99  ? PHE A 101 ? TYR A 101 PHE A 103 
AA3 2 CYS A 154 ? GLU A 164 ? CYS A 156 GLU A 166 
AA3 3 HIS A 170 ? THR A 173 ? HIS A 172 THR A 175 
AA4 1 VAL B 71  ? LEU B 73  ? VAL B 73  LEU B 75  
AA4 2 PHE B 64  ? ALA B 68  ? PHE B 66  ALA B 70  
AA4 3 MET B 15  ? CYS B 20  ? MET B 17  CYS B 22  
AA4 4 THR B 23  ? LEU B 30  ? THR B 25  LEU B 32  
AA4 5 VAL B 33  ? PRO B 37  ? VAL B 35  PRO B 39  
AA4 6 VAL B 84  ? VAL B 89  ? VAL B 86  VAL B 91  
AA4 7 VAL B 75  ? GLN B 81  ? VAL B 77  GLN B 83  
AA5 1 TYR B 99  ? PHE B 101 ? TYR B 101 PHE B 103 
AA5 2 CYS B 154 ? GLU B 164 ? CYS B 156 GLU B 166 
AA5 3 VAL B 146 ? ASP B 151 ? VAL B 148 ASP B 153 
AA5 4 THR B 109 ? TYR B 116 ? THR B 111 TYR B 118 
AA5 5 SER B 119 ? ALA B 127 ? SER B 121 ALA B 129 
AA6 1 TYR B 99  ? PHE B 101 ? TYR B 101 PHE B 103 
AA6 2 CYS B 154 ? GLU B 164 ? CYS B 156 GLU B 166 
AA6 3 HIS B 170 ? THR B 173 ? HIS B 172 THR B 175 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O LEU A 73  ? O LEU A 75  N VAL A 66  ? N VAL A 68  
AA1 2 3 O LEU A 65  ? O LEU A 67  N THR A 19  ? N THR A 21  
AA1 3 4 N VAL A 18  ? N VAL A 20  O LEU A 25  ? O LEU A 27  
AA1 4 5 N LEU A 28  ? N LEU A 30  O TYR A 35  ? O TYR A 37  
AA1 5 6 N CYS A 36  ? N CYS A 38  O LEU A 85  ? O LEU A 87  
AA1 6 7 O LYS A 88  ? O LYS A 90  N ILE A 76  ? N ILE A 78  
AA2 1 2 N LYS A 100 ? N LYS A 102 O PHE A 157 ? O PHE A 159 
AA2 2 3 O TYR A 159 ? O TYR A 161 N GLY A 147 ? N GLY A 149 
AA2 3 4 O PHE A 148 ? O PHE A 150 N SER A 111 ? N SER A 113 
AA2 4 5 N ALA A 114 ? N ALA A 116 O SER A 121 ? O SER A 123 
AA3 1 2 N LYS A 100 ? N LYS A 102 O PHE A 157 ? O PHE A 159 
AA3 2 3 N MET A 163 ? N MET A 165 O ALA A 171 ? O ALA A 173 
AA4 1 2 O VAL B 71  ? O VAL B 73  N ALA B 68  ? N ALA B 70  
AA4 2 3 O LEU B 65  ? O LEU B 67  N THR B 19  ? N THR B 21  
AA4 3 4 N VAL B 18  ? N VAL B 20  O LEU B 25  ? O LEU B 27  
AA4 4 5 N LEU B 28  ? N LEU B 30  O TYR B 35  ? O TYR B 37  
AA4 5 6 N VAL B 34  ? N VAL B 36  O LEU B 87  ? O LEU B 89  
AA4 6 7 O LYS B 86  ? O LYS B 88  N SER B 79  ? N SER B 81  
AA5 1 2 N LYS B 100 ? N LYS B 102 O PHE B 157 ? O PHE B 159 
AA5 2 3 O SER B 156 ? O SER B 158 N ASN B 149 ? N ASN B 151 
AA5 3 4 O PHE B 148 ? O PHE B 150 N SER B 111 ? N SER B 113 
AA5 4 5 N PHE B 110 ? N PHE B 112 O CYS B 126 ? O CYS B 128 
AA6 1 2 N LYS B 100 ? N LYS B 102 O PHE B 157 ? O PHE B 159 
AA6 2 3 N MET B 163 ? N MET B 165 O ALA B 171 ? O ALA B 173 
# 
_pdbx_entry_details.entry_id                   8WUR 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 OD2 B ASP 216 ? ? O   B ILE 281 ? ? 1.90 
2 1 CE  A MET 165 ? ? O04 A FNO 301 ? ? 2.04 
# 
loop_
_pdbx_validate_rmsd_bond.id 
_pdbx_validate_rmsd_bond.PDB_model_num 
_pdbx_validate_rmsd_bond.auth_atom_id_1 
_pdbx_validate_rmsd_bond.auth_asym_id_1 
_pdbx_validate_rmsd_bond.auth_comp_id_1 
_pdbx_validate_rmsd_bond.auth_seq_id_1 
_pdbx_validate_rmsd_bond.PDB_ins_code_1 
_pdbx_validate_rmsd_bond.label_alt_id_1 
_pdbx_validate_rmsd_bond.auth_atom_id_2 
_pdbx_validate_rmsd_bond.auth_asym_id_2 
_pdbx_validate_rmsd_bond.auth_comp_id_2 
_pdbx_validate_rmsd_bond.auth_seq_id_2 
_pdbx_validate_rmsd_bond.PDB_ins_code_2 
_pdbx_validate_rmsd_bond.label_alt_id_2 
_pdbx_validate_rmsd_bond.bond_value 
_pdbx_validate_rmsd_bond.bond_target_value 
_pdbx_validate_rmsd_bond.bond_deviation 
_pdbx_validate_rmsd_bond.bond_standard_deviation 
_pdbx_validate_rmsd_bond.linker_flag 
1 1 CD  A GLU 14  ? ? OE1 A GLU 14  ? ? 1.178 1.252 -0.074 0.011 N 
2 1 CD  A GLU 14  ? ? OE2 A GLU 14  ? ? 1.182 1.252 -0.070 0.011 N 
3 1 C   A GLY 29  ? ? O   A GLY 29  ? ? 1.134 1.232 -0.098 0.016 N 
4 1 CB  A SER 113 ? ? OG  A SER 113 ? ? 1.340 1.418 -0.078 0.013 N 
5 1 CB  A CYS 128 ? ? SG  A CYS 128 ? ? 1.659 1.812 -0.153 0.016 N 
6 1 CB  A SER 158 ? ? OG  A SER 158 ? ? 1.326 1.418 -0.092 0.013 N 
7 1 CE1 A TYR 239 ? ? CZ  A TYR 239 ? ? 1.301 1.381 -0.080 0.013 N 
8 1 CB  B CYS 128 ? ? SG  B CYS 128 ? ? 1.666 1.812 -0.146 0.016 N 
9 1 CB  B TRP 218 ? ? CG  B TRP 218 ? ? 1.384 1.498 -0.114 0.018 N 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 N  A GLY 215 ? ? CA A GLY 215 ? ? C  A GLY 215 ? ? 128.95 113.10 15.85  2.50 N 
2 1 CA A LEU 282 ? ? CB A LEU 282 ? ? CG A LEU 282 ? ? 95.00  115.30 -20.30 2.30 N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ASP A 33  ? ? 50.64   -127.41 
2 1 ASN A 84  ? ? 55.04   -121.99 
3 1 ILE A 281 ? ? -103.25 -75.51  
4 1 ASP B 33  ? ? 58.15   -129.18 
5 1 HIS B 41  ? ? -66.80  2.85    
6 1 ASN B 84  ? ? 55.70   -125.69 
7 1 ILE B 281 ? ? -98.70  -76.65  
# 
_pdbx_validate_chiral.id              1 
_pdbx_validate_chiral.PDB_model_num   1 
_pdbx_validate_chiral.auth_atom_id    C06 
_pdbx_validate_chiral.label_alt_id    ? 
_pdbx_validate_chiral.auth_asym_id    A 
_pdbx_validate_chiral.auth_comp_id    FNO 
_pdbx_validate_chiral.auth_seq_id     301 
_pdbx_validate_chiral.PDB_ins_code    ? 
_pdbx_validate_chiral.details         'WRONG HAND' 
_pdbx_validate_chiral.omega           . 
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z           
2 x+1/2,-y+1/2,-z 
3 -x,y+1/2,-z+1/2 
4 -x+1/2,-y,z+1/2 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A PHE 3  ? A PHE 1  
2 1 Y 1 B SER 46 ? B SER 44 
3 1 Y 1 B GLU 47 ? B GLU 45 
4 1 Y 1 B ASN 48 ? B ASN 46 
5 1 Y 1 B MET 49 ? B MET 47 
6 1 Y 1 B LEU 50 ? B LEU 48 
# 
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  
CYS N    N N N 74  
CYS CA   C N R 75  
CYS C    C N N 76  
CYS O    O N N 77  
CYS CB   C N N 78  
CYS SG   S N N 79  
CYS OXT  O N N 80  
CYS H    H N N 81  
CYS H2   H N N 82  
CYS HA   H N N 83  
CYS HB2  H N N 84  
CYS HB3  H N N 85  
CYS HG   H N N 86  
CYS HXT  H N N 87  
FNO C10  C N N 88  
FNO C13  C N N 89  
FNO C15  C Y N 90  
FNO C17  C N N 91  
FNO C20  C N N 92  
FNO C21  C N N 93  
FNO C06  C N R 94  
FNO C07  C N N 95  
FNO C08  C N N 96  
FNO C09  C Y N 97  
FNO C11  C Y N 98  
FNO C12  C N N 99  
FNO C14  C N N 100 
FNO C16  C Y N 101 
FNO C18  C Y N 102 
FNO C19  C Y N 103 
FNO O01  O N N 104 
FNO O02  O N N 105 
FNO O03  O N N 106 
FNO O04  O N N 107 
FNO O05  O N N 108 
FNO H1   H N N 109 
FNO H2   H N N 110 
FNO H3   H N N 111 
FNO H4   H N N 112 
FNO H5   H N N 113 
FNO H6   H N N 114 
FNO H7   H N N 115 
FNO H8   H N N 116 
FNO H9   H N N 117 
FNO H10  H N N 118 
FNO H11  H N N 119 
FNO H12  H N N 120 
FNO H13  H N N 121 
FNO H14  H N N 122 
FNO H15  H N N 123 
FNO H16  H N N 124 
GLN N    N N N 125 
GLN CA   C N S 126 
GLN C    C N N 127 
GLN O    O N N 128 
GLN CB   C N N 129 
GLN CG   C N N 130 
GLN CD   C N N 131 
GLN OE1  O N N 132 
GLN NE2  N N N 133 
GLN OXT  O N N 134 
GLN H    H N N 135 
GLN H2   H N N 136 
GLN HA   H N N 137 
GLN HB2  H N N 138 
GLN HB3  H N N 139 
GLN HG2  H N N 140 
GLN HG3  H N N 141 
GLN HE21 H N N 142 
GLN HE22 H N N 143 
GLN HXT  H N N 144 
GLU N    N N N 145 
GLU CA   C N S 146 
GLU C    C N N 147 
GLU O    O N N 148 
GLU CB   C N N 149 
GLU CG   C N N 150 
GLU CD   C N N 151 
GLU OE1  O N N 152 
GLU OE2  O N N 153 
GLU OXT  O N N 154 
GLU H    H N N 155 
GLU H2   H N N 156 
GLU HA   H N N 157 
GLU HB2  H N N 158 
GLU HB3  H N N 159 
GLU HG2  H N N 160 
GLU HG3  H N N 161 
GLU HE2  H N N 162 
GLU HXT  H N N 163 
GLY N    N N N 164 
GLY CA   C N N 165 
GLY C    C N N 166 
GLY O    O N N 167 
GLY OXT  O N N 168 
GLY H    H N N 169 
GLY H2   H N N 170 
GLY HA2  H N N 171 
GLY HA3  H N N 172 
GLY HXT  H N N 173 
HIS N    N N N 174 
HIS CA   C N S 175 
HIS C    C N N 176 
HIS O    O N N 177 
HIS CB   C N N 178 
HIS CG   C Y N 179 
HIS ND1  N Y N 180 
HIS CD2  C Y N 181 
HIS CE1  C Y N 182 
HIS NE2  N Y N 183 
HIS OXT  O N N 184 
HIS H    H N N 185 
HIS H2   H N N 186 
HIS HA   H N N 187 
HIS HB2  H N N 188 
HIS HB3  H N N 189 
HIS HD1  H N N 190 
HIS HD2  H N N 191 
HIS HE1  H N N 192 
HIS HE2  H N N 193 
HIS HXT  H N N 194 
HOH O    O N N 195 
HOH H1   H N N 196 
HOH H2   H N N 197 
ILE N    N N N 198 
ILE CA   C N S 199 
ILE C    C N N 200 
ILE O    O N N 201 
ILE CB   C N S 202 
ILE CG1  C N N 203 
ILE CG2  C N N 204 
ILE CD1  C N N 205 
ILE OXT  O N N 206 
ILE H    H N N 207 
ILE H2   H N N 208 
ILE HA   H N N 209 
ILE HB   H N N 210 
ILE HG12 H N N 211 
ILE HG13 H N N 212 
ILE HG21 H N N 213 
ILE HG22 H N N 214 
ILE HG23 H N N 215 
ILE HD11 H N N 216 
ILE HD12 H N N 217 
ILE HD13 H N N 218 
ILE HXT  H N N 219 
LEU N    N N N 220 
LEU CA   C N S 221 
LEU C    C N N 222 
LEU O    O N N 223 
LEU CB   C N N 224 
LEU CG   C N N 225 
LEU CD1  C N N 226 
LEU CD2  C N N 227 
LEU OXT  O N N 228 
LEU H    H N N 229 
LEU H2   H N N 230 
LEU HA   H N N 231 
LEU HB2  H N N 232 
LEU HB3  H N N 233 
LEU HG   H N N 234 
LEU HD11 H N N 235 
LEU HD12 H N N 236 
LEU HD13 H N N 237 
LEU HD21 H N N 238 
LEU HD22 H N N 239 
LEU HD23 H N N 240 
LEU HXT  H N N 241 
LYS N    N N N 242 
LYS CA   C N S 243 
LYS C    C N N 244 
LYS O    O N N 245 
LYS CB   C N N 246 
LYS CG   C N N 247 
LYS CD   C N N 248 
LYS CE   C N N 249 
LYS NZ   N N N 250 
LYS OXT  O N N 251 
LYS H    H N N 252 
LYS H2   H N N 253 
LYS HA   H N N 254 
LYS HB2  H N N 255 
LYS HB3  H N N 256 
LYS HG2  H N N 257 
LYS HG3  H N N 258 
LYS HD2  H N N 259 
LYS HD3  H N N 260 
LYS HE2  H N N 261 
LYS HE3  H N N 262 
LYS HZ1  H N N 263 
LYS HZ2  H N N 264 
LYS HZ3  H N N 265 
LYS HXT  H N N 266 
MET N    N N N 267 
MET CA   C N S 268 
MET C    C N N 269 
MET O    O N N 270 
MET CB   C N N 271 
MET CG   C N N 272 
MET SD   S N N 273 
MET CE   C N N 274 
MET OXT  O N N 275 
MET H    H N N 276 
MET H2   H N N 277 
MET HA   H N N 278 
MET HB2  H N N 279 
MET HB3  H N N 280 
MET HG2  H N N 281 
MET HG3  H N N 282 
MET HE1  H N N 283 
MET HE2  H N N 284 
MET HE3  H N N 285 
MET HXT  H N N 286 
PHE N    N N N 287 
PHE CA   C N S 288 
PHE C    C N N 289 
PHE O    O N N 290 
PHE CB   C N N 291 
PHE CG   C Y N 292 
PHE CD1  C Y N 293 
PHE CD2  C Y N 294 
PHE CE1  C Y N 295 
PHE CE2  C Y N 296 
PHE CZ   C Y N 297 
PHE OXT  O N N 298 
PHE H    H N N 299 
PHE H2   H N N 300 
PHE HA   H N N 301 
PHE HB2  H N N 302 
PHE HB3  H N N 303 
PHE HD1  H N N 304 
PHE HD2  H N N 305 
PHE HE1  H N N 306 
PHE HE2  H N N 307 
PHE HZ   H N N 308 
PHE HXT  H N N 309 
PRO N    N N N 310 
PRO CA   C N S 311 
PRO C    C N N 312 
PRO O    O N N 313 
PRO CB   C N N 314 
PRO CG   C N N 315 
PRO CD   C N N 316 
PRO OXT  O N N 317 
PRO H    H N N 318 
PRO HA   H N N 319 
PRO HB2  H N N 320 
PRO HB3  H N N 321 
PRO HG2  H N N 322 
PRO HG3  H N N 323 
PRO HD2  H N N 324 
PRO HD3  H N N 325 
PRO HXT  H N N 326 
SER N    N N N 327 
SER CA   C N S 328 
SER C    C N N 329 
SER O    O N N 330 
SER CB   C N N 331 
SER OG   O N N 332 
SER OXT  O N N 333 
SER H    H N N 334 
SER H2   H N N 335 
SER HA   H N N 336 
SER HB2  H N N 337 
SER HB3  H N N 338 
SER HG   H N N 339 
SER HXT  H N N 340 
THR N    N N N 341 
THR CA   C N S 342 
THR C    C N N 343 
THR O    O N N 344 
THR CB   C N R 345 
THR OG1  O N N 346 
THR CG2  C N N 347 
THR OXT  O N N 348 
THR H    H N N 349 
THR H2   H N N 350 
THR HA   H N N 351 
THR HB   H N N 352 
THR HG1  H N N 353 
THR HG21 H N N 354 
THR HG22 H N N 355 
THR HG23 H N N 356 
THR HXT  H N N 357 
TRP N    N N N 358 
TRP CA   C N S 359 
TRP C    C N N 360 
TRP O    O N N 361 
TRP CB   C N N 362 
TRP CG   C Y N 363 
TRP CD1  C Y N 364 
TRP CD2  C Y N 365 
TRP NE1  N Y N 366 
TRP CE2  C Y N 367 
TRP CE3  C Y N 368 
TRP CZ2  C Y N 369 
TRP CZ3  C Y N 370 
TRP CH2  C Y N 371 
TRP OXT  O N N 372 
TRP H    H N N 373 
TRP H2   H N N 374 
TRP HA   H N N 375 
TRP HB2  H N N 376 
TRP HB3  H N N 377 
TRP HD1  H N N 378 
TRP HE1  H N N 379 
TRP HE3  H N N 380 
TRP HZ2  H N N 381 
TRP HZ3  H N N 382 
TRP HH2  H N N 383 
TRP HXT  H N N 384 
TYR N    N N N 385 
TYR CA   C N S 386 
TYR C    C N N 387 
TYR O    O N N 388 
TYR CB   C N N 389 
TYR CG   C Y N 390 
TYR CD1  C Y N 391 
TYR CD2  C Y N 392 
TYR CE1  C Y N 393 
TYR CE2  C Y N 394 
TYR CZ   C Y N 395 
TYR OH   O N N 396 
TYR OXT  O N N 397 
TYR H    H N N 398 
TYR H2   H N N 399 
TYR HA   H N N 400 
TYR HB2  H N N 401 
TYR HB3  H N N 402 
TYR HD1  H N N 403 
TYR HD2  H N N 404 
TYR HE1  H N N 405 
TYR HE2  H N N 406 
TYR HH   H N N 407 
TYR HXT  H N N 408 
VAL N    N N N 409 
VAL CA   C N S 410 
VAL C    C N N 411 
VAL O    O N N 412 
VAL CB   C N N 413 
VAL CG1  C N N 414 
VAL CG2  C N N 415 
VAL OXT  O N N 416 
VAL H    H N N 417 
VAL H2   H N N 418 
VAL HA   H N N 419 
VAL HB   H N N 420 
VAL HG11 H N N 421 
VAL HG12 H N N 422 
VAL HG13 H N N 423 
VAL HG21 H N N 424 
VAL HG22 H N N 425 
VAL HG23 H N N 426 
VAL HXT  H N N 427 
# 
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  
FNO C21 C17  sing N N 83  
FNO C17 C20  sing N N 84  
FNO C17 C14  doub N N 85  
FNO C14 C08  sing N N 86  
FNO C06 O01  sing N N 87  
FNO C06 C08  sing N N 88  
FNO C06 C07  sing N N 89  
FNO C12 C07  doub N N 90  
FNO C12 C13  sing N N 91  
FNO C07 C10  sing N N 92  
FNO O04 C13  doub N N 93  
FNO C13 C11  sing N N 94  
FNO C10 O02  doub N N 95  
FNO C10 C09  sing N N 96  
FNO C11 C09  doub Y N 97  
FNO C11 C16  sing Y N 98  
FNO C09 C15  sing Y N 99  
FNO O05 C16  sing N N 100 
FNO C16 C19  doub Y N 101 
FNO C15 O03  sing N N 102 
FNO C15 C18  doub Y N 103 
FNO C19 C18  sing Y N 104 
FNO C20 H1   sing N N 105 
FNO C20 H2   sing N N 106 
FNO C20 H3   sing N N 107 
FNO C21 H4   sing N N 108 
FNO C21 H5   sing N N 109 
FNO C21 H6   sing N N 110 
FNO C06 H7   sing N N 111 
FNO C08 H8   sing N N 112 
FNO C08 H9   sing N N 113 
FNO C12 H10  sing N N 114 
FNO C14 H11  sing N N 115 
FNO C18 H12  sing N N 116 
FNO C19 H13  sing N N 117 
FNO O01 H14  sing N N 118 
FNO O03 H15  sing N N 119 
FNO O05 H16  sing N N 120 
GLN N   CA   sing N N 121 
GLN N   H    sing N N 122 
GLN N   H2   sing N N 123 
GLN CA  C    sing N N 124 
GLN CA  CB   sing N N 125 
GLN CA  HA   sing N N 126 
GLN C   O    doub N N 127 
GLN C   OXT  sing N N 128 
GLN CB  CG   sing N N 129 
GLN CB  HB2  sing N N 130 
GLN CB  HB3  sing N N 131 
GLN CG  CD   sing N N 132 
GLN CG  HG2  sing N N 133 
GLN CG  HG3  sing N N 134 
GLN CD  OE1  doub N N 135 
GLN CD  NE2  sing N N 136 
GLN NE2 HE21 sing N N 137 
GLN NE2 HE22 sing N N 138 
GLN OXT HXT  sing N N 139 
GLU N   CA   sing N N 140 
GLU N   H    sing N N 141 
GLU N   H2   sing N N 142 
GLU CA  C    sing N N 143 
GLU CA  CB   sing N N 144 
GLU CA  HA   sing N N 145 
GLU C   O    doub N N 146 
GLU C   OXT  sing N N 147 
GLU CB  CG   sing N N 148 
GLU CB  HB2  sing N N 149 
GLU CB  HB3  sing N N 150 
GLU CG  CD   sing N N 151 
GLU CG  HG2  sing N N 152 
GLU CG  HG3  sing N N 153 
GLU CD  OE1  doub N N 154 
GLU CD  OE2  sing N N 155 
GLU OE2 HE2  sing N N 156 
GLU OXT HXT  sing N N 157 
GLY N   CA   sing N N 158 
GLY N   H    sing N N 159 
GLY N   H2   sing N N 160 
GLY CA  C    sing N N 161 
GLY CA  HA2  sing N N 162 
GLY CA  HA3  sing N N 163 
GLY C   O    doub N N 164 
GLY C   OXT  sing N N 165 
GLY OXT HXT  sing N N 166 
HIS N   CA   sing N N 167 
HIS N   H    sing N N 168 
HIS N   H2   sing N N 169 
HIS CA  C    sing N N 170 
HIS CA  CB   sing N N 171 
HIS CA  HA   sing N N 172 
HIS C   O    doub N N 173 
HIS C   OXT  sing N N 174 
HIS CB  CG   sing N N 175 
HIS CB  HB2  sing N N 176 
HIS CB  HB3  sing N N 177 
HIS CG  ND1  sing Y N 178 
HIS CG  CD2  doub Y N 179 
HIS ND1 CE1  doub Y N 180 
HIS ND1 HD1  sing N N 181 
HIS CD2 NE2  sing Y N 182 
HIS CD2 HD2  sing N N 183 
HIS CE1 NE2  sing Y N 184 
HIS CE1 HE1  sing N N 185 
HIS NE2 HE2  sing N N 186 
HIS OXT HXT  sing N N 187 
HOH O   H1   sing N N 188 
HOH O   H2   sing N N 189 
ILE N   CA   sing N N 190 
ILE N   H    sing N N 191 
ILE N   H2   sing N N 192 
ILE CA  C    sing N N 193 
ILE CA  CB   sing N N 194 
ILE CA  HA   sing N N 195 
ILE C   O    doub N N 196 
ILE C   OXT  sing N N 197 
ILE CB  CG1  sing N N 198 
ILE CB  CG2  sing N N 199 
ILE CB  HB   sing N N 200 
ILE CG1 CD1  sing N N 201 
ILE CG1 HG12 sing N N 202 
ILE CG1 HG13 sing N N 203 
ILE CG2 HG21 sing N N 204 
ILE CG2 HG22 sing N N 205 
ILE CG2 HG23 sing N N 206 
ILE CD1 HD11 sing N N 207 
ILE CD1 HD12 sing N N 208 
ILE CD1 HD13 sing N N 209 
ILE OXT HXT  sing N N 210 
LEU N   CA   sing N N 211 
LEU N   H    sing N N 212 
LEU N   H2   sing N N 213 
LEU CA  C    sing N N 214 
LEU CA  CB   sing N N 215 
LEU CA  HA   sing N N 216 
LEU C   O    doub N N 217 
LEU C   OXT  sing N N 218 
LEU CB  CG   sing N N 219 
LEU CB  HB2  sing N N 220 
LEU CB  HB3  sing N N 221 
LEU CG  CD1  sing N N 222 
LEU CG  CD2  sing N N 223 
LEU CG  HG   sing N N 224 
LEU CD1 HD11 sing N N 225 
LEU CD1 HD12 sing N N 226 
LEU CD1 HD13 sing N N 227 
LEU CD2 HD21 sing N N 228 
LEU CD2 HD22 sing N N 229 
LEU CD2 HD23 sing N N 230 
LEU OXT HXT  sing N N 231 
LYS N   CA   sing N N 232 
LYS N   H    sing N N 233 
LYS N   H2   sing N N 234 
LYS CA  C    sing N N 235 
LYS CA  CB   sing N N 236 
LYS CA  HA   sing N N 237 
LYS C   O    doub N N 238 
LYS C   OXT  sing N N 239 
LYS CB  CG   sing N N 240 
LYS CB  HB2  sing N N 241 
LYS CB  HB3  sing N N 242 
LYS CG  CD   sing N N 243 
LYS CG  HG2  sing N N 244 
LYS CG  HG3  sing N N 245 
LYS CD  CE   sing N N 246 
LYS CD  HD2  sing N N 247 
LYS CD  HD3  sing N N 248 
LYS CE  NZ   sing N N 249 
LYS CE  HE2  sing N N 250 
LYS CE  HE3  sing N N 251 
LYS NZ  HZ1  sing N N 252 
LYS NZ  HZ2  sing N N 253 
LYS NZ  HZ3  sing N N 254 
LYS OXT HXT  sing N N 255 
MET N   CA   sing N N 256 
MET N   H    sing N N 257 
MET N   H2   sing N N 258 
MET CA  C    sing N N 259 
MET CA  CB   sing N N 260 
MET CA  HA   sing N N 261 
MET C   O    doub N N 262 
MET C   OXT  sing N N 263 
MET CB  CG   sing N N 264 
MET CB  HB2  sing N N 265 
MET CB  HB3  sing N N 266 
MET CG  SD   sing N N 267 
MET CG  HG2  sing N N 268 
MET CG  HG3  sing N N 269 
MET SD  CE   sing N N 270 
MET CE  HE1  sing N N 271 
MET CE  HE2  sing N N 272 
MET CE  HE3  sing N N 273 
MET OXT HXT  sing N N 274 
PHE N   CA   sing N N 275 
PHE N   H    sing N N 276 
PHE N   H2   sing N N 277 
PHE CA  C    sing N N 278 
PHE CA  CB   sing N N 279 
PHE CA  HA   sing N N 280 
PHE C   O    doub N N 281 
PHE C   OXT  sing N N 282 
PHE CB  CG   sing N N 283 
PHE CB  HB2  sing N N 284 
PHE CB  HB3  sing N N 285 
PHE CG  CD1  doub Y N 286 
PHE CG  CD2  sing Y N 287 
PHE CD1 CE1  sing Y N 288 
PHE CD1 HD1  sing N N 289 
PHE CD2 CE2  doub Y N 290 
PHE CD2 HD2  sing N N 291 
PHE CE1 CZ   doub Y N 292 
PHE CE1 HE1  sing N N 293 
PHE CE2 CZ   sing Y N 294 
PHE CE2 HE2  sing N N 295 
PHE CZ  HZ   sing N N 296 
PHE OXT HXT  sing N N 297 
PRO N   CA   sing N N 298 
PRO N   CD   sing N N 299 
PRO N   H    sing N N 300 
PRO CA  C    sing N N 301 
PRO CA  CB   sing N N 302 
PRO CA  HA   sing N N 303 
PRO C   O    doub N N 304 
PRO C   OXT  sing N N 305 
PRO CB  CG   sing N N 306 
PRO CB  HB2  sing N N 307 
PRO CB  HB3  sing N N 308 
PRO CG  CD   sing N N 309 
PRO CG  HG2  sing N N 310 
PRO CG  HG3  sing N N 311 
PRO CD  HD2  sing N N 312 
PRO CD  HD3  sing N N 313 
PRO OXT HXT  sing N N 314 
SER N   CA   sing N N 315 
SER N   H    sing N N 316 
SER N   H2   sing N N 317 
SER CA  C    sing N N 318 
SER CA  CB   sing N N 319 
SER CA  HA   sing N N 320 
SER C   O    doub N N 321 
SER C   OXT  sing N N 322 
SER CB  OG   sing N N 323 
SER CB  HB2  sing N N 324 
SER CB  HB3  sing N N 325 
SER OG  HG   sing N N 326 
SER OXT HXT  sing N N 327 
THR N   CA   sing N N 328 
THR N   H    sing N N 329 
THR N   H2   sing N N 330 
THR CA  C    sing N N 331 
THR CA  CB   sing N N 332 
THR CA  HA   sing N N 333 
THR C   O    doub N N 334 
THR C   OXT  sing N N 335 
THR CB  OG1  sing N N 336 
THR CB  CG2  sing N N 337 
THR CB  HB   sing N N 338 
THR OG1 HG1  sing N N 339 
THR CG2 HG21 sing N N 340 
THR CG2 HG22 sing N N 341 
THR CG2 HG23 sing N N 342 
THR OXT HXT  sing N N 343 
TRP N   CA   sing N N 344 
TRP N   H    sing N N 345 
TRP N   H2   sing N N 346 
TRP CA  C    sing N N 347 
TRP CA  CB   sing N N 348 
TRP CA  HA   sing N N 349 
TRP C   O    doub N N 350 
TRP C   OXT  sing N N 351 
TRP CB  CG   sing N N 352 
TRP CB  HB2  sing N N 353 
TRP CB  HB3  sing N N 354 
TRP CG  CD1  doub Y N 355 
TRP CG  CD2  sing Y N 356 
TRP CD1 NE1  sing Y N 357 
TRP CD1 HD1  sing N N 358 
TRP CD2 CE2  doub Y N 359 
TRP CD2 CE3  sing Y N 360 
TRP NE1 CE2  sing Y N 361 
TRP NE1 HE1  sing N N 362 
TRP CE2 CZ2  sing Y N 363 
TRP CE3 CZ3  doub Y N 364 
TRP CE3 HE3  sing N N 365 
TRP CZ2 CH2  doub Y N 366 
TRP CZ2 HZ2  sing N N 367 
TRP CZ3 CH2  sing Y N 368 
TRP CZ3 HZ3  sing N N 369 
TRP CH2 HH2  sing N N 370 
TRP OXT HXT  sing N N 371 
TYR N   CA   sing N N 372 
TYR N   H    sing N N 373 
TYR N   H2   sing N N 374 
TYR CA  C    sing N N 375 
TYR CA  CB   sing N N 376 
TYR CA  HA   sing N N 377 
TYR C   O    doub N N 378 
TYR C   OXT  sing N N 379 
TYR CB  CG   sing N N 380 
TYR CB  HB2  sing N N 381 
TYR CB  HB3  sing N N 382 
TYR CG  CD1  doub Y N 383 
TYR CG  CD2  sing Y N 384 
TYR CD1 CE1  sing Y N 385 
TYR CD1 HD1  sing N N 386 
TYR CD2 CE2  doub Y N 387 
TYR CD2 HD2  sing N N 388 
TYR CE1 CZ   doub Y N 389 
TYR CE1 HE1  sing N N 390 
TYR CE2 CZ   sing Y N 391 
TYR CE2 HE2  sing N N 392 
TYR CZ  OH   sing N N 393 
TYR OH  HH   sing N N 394 
TYR OXT HXT  sing N N 395 
VAL N   CA   sing N N 396 
VAL N   H    sing N N 397 
VAL N   H2   sing N N 398 
VAL CA  C    sing N N 399 
VAL CA  CB   sing N N 400 
VAL CA  HA   sing N N 401 
VAL C   O    doub N N 402 
VAL C   OXT  sing N N 403 
VAL CB  CG1  sing N N 404 
VAL CB  CG2  sing N N 405 
VAL CB  HB   sing N N 406 
VAL CG1 HG11 sing N N 407 
VAL CG1 HG12 sing N N 408 
VAL CG1 HG13 sing N N 409 
VAL CG2 HG21 sing N N 410 
VAL CG2 HG22 sing N N 411 
VAL CG2 HG23 sing N N 412 
VAL OXT HXT  sing N N 413 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   7XB3 
_pdbx_initial_refinement_model.details          ? 
# 
_space_group.name_H-M_alt     'P 21 21 21' 
_space_group.name_Hall        'P 2ac 2ab' 
_space_group.IT_number        19 
_space_group.crystal_system   orthorhombic 
_space_group.id               1 
# 
_atom_sites.entry_id                    8WUR 
_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]   0.014695 
_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]   0.009714 
_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]   0.009644 
_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 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C ? ? 3.54356 2.42580 25.62398 1.50364  0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N ? ? 4.01032 2.96436 19.97189 1.75589  0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O ? ? 4.49882 3.47563 15.80542 1.70748  0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S ? ? 9.55732 6.39887 1.23737  29.19336 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
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   . ARG A 1 2   ? 7.82000   5.51000   -16.87000 1.000 58.44000 ? 4   ARG A N   1 
ATOM   2    C CA  . ARG A 1 2   ? 6.54100   4.85700   -16.93700 1.000 60.11000 ? 4   ARG A CA  1 
ATOM   3    C C   . ARG A 1 2   ? 5.53700   5.66500   -17.65300 1.000 53.46000 ? 4   ARG A C   1 
ATOM   4    O O   . ARG A 1 2   ? 5.53800   6.86100   -17.59400 1.000 53.88000 ? 4   ARG A O   1 
ATOM   5    C CB  . ARG A 1 2   ? 5.99800   4.56900   -15.56800 1.000 55.46000 ? 4   ARG A CB  1 
ATOM   6    C CG  . ARG A 1 2   ? 6.56600   3.35700   -14.96600 1.000 56.91000 ? 4   ARG A CG  1 
ATOM   7    C CD  . ARG A 1 2   ? 5.51600   2.49700   -14.35700 1.000 53.74000 ? 4   ARG A CD  1 
ATOM   8    N NE  . ARG A 1 2   ? 6.16900   1.34400   -13.82100 1.000 53.64000 ? 4   ARG A NE  1 
ATOM   9    C CZ  . ARG A 1 2   ? 5.70500   0.13200   -13.90900 1.000 51.63000 ? 4   ARG A CZ  1 
ATOM   10   N NH1 . ARG A 1 2   ? 4.58200   -0.05600  -14.50400 1.000 48.31000 ? 4   ARG A NH1 1 
ATOM   11   N NH2 . ARG A 1 2   ? 6.38700   -0.86700  -13.41700 1.000 46.97000 ? 4   ARG A NH2 1 
ATOM   12   N N   . LYS A 1 3   ? 4.66500   4.98200   -18.34400 1.000 52.98000 ? 5   LYS A N   1 
ATOM   13   C CA  . LYS A 1 3   ? 3.61800   5.63900   -19.04500 1.000 50.75000 ? 5   LYS A CA  1 
ATOM   14   C C   . LYS A 1 3   ? 2.61000   5.88400   -17.94200 1.000 44.88000 ? 5   LYS A C   1 
ATOM   15   O O   . LYS A 1 3   ? 2.34500   4.99900   -17.23100 1.000 50.90000 ? 5   LYS A O   1 
ATOM   16   C CB  . LYS A 1 3   ? 3.12300   4.69900   -20.10800 1.000 53.15000 ? 5   LYS A CB  1 
ATOM   17   C CG  . LYS A 1 3   ? 2.38400   5.37300   -21.22400 1.000 54.73000 ? 5   LYS A CG  1 
ATOM   18   C CD  . LYS A 1 3   ? 1.83300   4.40800   -22.24500 1.000 51.28000 ? 5   LYS A CD  1 
ATOM   19   C CE  . LYS A 1 3   ? 2.90000   3.71600   -23.03100 1.000 51.79000 ? 5   LYS A CE  1 
ATOM   20   N NZ  . LYS A 1 3   ? 2.38400   2.50400   -23.70800 1.000 57.50000 ? 5   LYS A NZ  1 
ATOM   21   N N   . MET A 1 4   ? 2.10400   7.07200   -17.78000 1.000 40.86000 ? 6   MET A N   1 
ATOM   22   C CA  . MET A 1 4   ? 1.18400   7.35700   -16.73000 1.000 37.64000 ? 6   MET A CA  1 
ATOM   23   C C   . MET A 1 4   ? -0.11200  7.90800   -17.25100 1.000 33.65000 ? 6   MET A C   1 
ATOM   24   O O   . MET A 1 4   ? -0.14000  8.53500   -18.22100 1.000 32.15000 ? 6   MET A O   1 
ATOM   25   C CB  . MET A 1 4   ? 1.72300   8.41500   -15.78200 1.000 36.58000 ? 6   MET A CB  1 
ATOM   26   C CG  . MET A 1 4   ? 2.96500   8.08500   -15.01500 1.000 44.22000 ? 6   MET A CG  1 
ATOM   27   S SD  . MET A 1 4   ? 3.23000   9.08400   -13.58600 1.000 52.01000 ? 6   MET A SD  1 
ATOM   28   C CE  . MET A 1 4   ? 3.52900   10.65800  -14.27900 1.000 38.28000 ? 6   MET A CE  1 
ATOM   29   N N   . ALA A 1 5   ? -1.16600  7.66100   -16.53700 1.000 26.04000 ? 7   ALA A N   1 
ATOM   30   C CA  . ALA A 1 5   ? -2.42300  8.16100   -16.83200 1.000 28.61000 ? 7   ALA A CA  1 
ATOM   31   C C   . ALA A 1 5   ? -2.69600  9.33500   -15.92000 1.000 33.63000 ? 7   ALA A C   1 
ATOM   32   O O   . ALA A 1 5   ? -2.07700  9.46600   -14.94000 1.000 30.89000 ? 7   ALA A O   1 
ATOM   33   C CB  . ALA A 1 5   ? -3.42900  7.10400   -16.58700 1.000 29.81000 ? 7   ALA A CB  1 
ATOM   34   N N   . PHE A 1 6   ? -3.63800  10.16200  -16.26600 1.000 26.89000 ? 8   PHE A N   1 
ATOM   35   C CA  . PHE A 1 6   ? -4.04800  11.24000  -15.45000 1.000 29.79000 ? 8   PHE A CA  1 
ATOM   36   C C   . PHE A 1 6   ? -4.82900  10.79800  -14.22200 1.000 28.80000 ? 8   PHE A C   1 
ATOM   37   O O   . PHE A 1 6   ? -5.52700  9.87500   -14.24500 1.000 28.58000 ? 8   PHE A O   1 
ATOM   38   C CB  . PHE A 1 6   ? -4.89900  12.23600  -16.21900 1.000 31.58000 ? 8   PHE A CB  1 
ATOM   39   C CG  . PHE A 1 6   ? -4.17200  12.96500  -17.28200 1.000 34.24000 ? 8   PHE A CG  1 
ATOM   40   C CD1 . PHE A 1 6   ? -3.44100  14.01700  -16.99700 1.000 34.43000 ? 8   PHE A CD1 1 
ATOM   41   C CD2 . PHE A 1 6   ? -4.22600  12.55800  -18.54500 1.000 33.04000 ? 8   PHE A CD2 1 
ATOM   42   C CE1 . PHE A 1 6   ? -2.76600  14.66100  -17.96300 1.000 38.83000 ? 8   PHE A CE1 1 
ATOM   43   C CE2 . PHE A 1 6   ? -3.56000  13.19000  -19.51500 1.000 37.00000 ? 8   PHE A CE2 1 
ATOM   44   C CZ  . PHE A 1 6   ? -2.83500  14.24800  -19.22900 1.000 35.80000 ? 8   PHE A CZ  1 
ATOM   45   N N   . PRO A 1 7   ? -4.66900  11.60800  -13.11900 1.000 27.79000 ? 9   PRO A N   1 
ATOM   46   C CA  . PRO A 1 7   ? -5.48600  11.28100  -11.95000 1.000 28.40000 ? 9   PRO A CA  1 
ATOM   47   C C   . PRO A 1 7   ? -6.94900  11.31400  -12.36800 1.000 31.61000 ? 9   PRO A C   1 
ATOM   48   O O   . PRO A 1 7   ? -7.38500  12.20200  -13.01200 1.000 31.23000 ? 9   PRO A O   1 
ATOM   49   C CB  . PRO A 1 7   ? -5.17700  12.38400  -11.00100 1.000 30.51000 ? 9   PRO A CB  1 
ATOM   50   C CG  . PRO A 1 7   ? -3.83000  12.76800  -11.30400 1.000 30.85000 ? 9   PRO A CG  1 
ATOM   51   C CD  . PRO A 1 7   ? -3.77400  12.77100  -12.74200 1.000 29.20000 ? 9   PRO A CD  1 
ATOM   52   N N   . SER A 1 8   ? -7.69800  10.32700  -11.99000 1.000 28.17000 ? 10  SER A N   1 
ATOM   53   C CA  . SER A 1 8   ? -9.03300  10.12400  -12.53000 1.000 29.36000 ? 10  SER A CA  1 
ATOM   54   C C   . SER A 1 8   ? -10.14300 10.73100  -11.67700 1.000 30.28000 ? 10  SER A C   1 
ATOM   55   O O   . SER A 1 8   ? -11.31000 10.65300  -12.08400 1.000 27.33000 ? 10  SER A O   1 
ATOM   56   C CB  . SER A 1 8   ? -9.30300  8.62600   -12.70300 1.000 30.38000 ? 10  SER A CB  1 
ATOM   57   O OG  . SER A 1 8   ? -9.14100  7.92100   -11.47300 1.000 27.98000 ? 10  SER A OG  1 
ATOM   58   N N   . GLY A 1 9   ? -9.81300  11.36000  -10.54400 1.000 25.01000 ? 11  GLY A N   1 
ATOM   59   C CA  . GLY A 1 9   ? -10.84000 11.78300  -9.59700  1.000 26.43000 ? 11  GLY A CA  1 
ATOM   60   C C   . GLY A 1 9   ? -11.90500 12.67800  -10.21300 1.000 29.07000 ? 11  GLY A C   1 
ATOM   61   O O   . GLY A 1 9   ? -13.10300 12.46000  -10.02100 1.000 28.14000 ? 11  GLY A O   1 
ATOM   62   N N   . LYS A 1 10  ? -11.50400 13.66800  -10.97300 1.000 29.49000 ? 12  LYS A N   1 
ATOM   63   C CA  . LYS A 1 10  ? -12.40400 14.60600  -11.57900 1.000 29.54000 ? 12  LYS A CA  1 
ATOM   64   C C   . LYS A 1 10  ? -13.39400 13.91400  -12.49600 1.000 30.99000 ? 12  LYS A C   1 
ATOM   65   O O   . LYS A 1 10  ? -14.46500 14.30500  -12.56300 1.000 34.31000 ? 12  LYS A O   1 
ATOM   66   C CB  . LYS A 1 10  ? -11.66200 15.68800  -12.28200 1.000 30.63000 ? 12  LYS A CB  1 
ATOM   67   C CG  . LYS A 1 10  ? -10.92500 16.58800  -11.37600 1.000 33.91000 ? 12  LYS A CG  1 
ATOM   68   C CD  . LYS A 1 10  ? -10.16500 17.60800  -12.14000 1.000 39.24000 ? 12  LYS A CD  1 
ATOM   69   C CE  . LYS A 1 10  ? -9.70500  18.70100  -11.24000 1.000 47.22000 ? 12  LYS A CE  1 
ATOM   70   N NZ  . LYS A 1 10  ? -8.47800  18.31200  -10.56800 1.000 53.71000 ? 12  LYS A NZ  1 
ATOM   71   N N   . VAL A 1 11  ? -12.98700 12.90900  -13.22900 1.000 29.23000 ? 13  VAL A N   1 
ATOM   72   C CA  . VAL A 1 11  ? -13.87400 12.11700  -14.03100 1.000 27.58000 ? 13  VAL A CA  1 
ATOM   73   C C   . VAL A 1 11  ? -14.77200 11.14100  -13.28200 1.000 26.20000 ? 13  VAL A C   1 
ATOM   74   O O   . VAL A 1 11  ? -15.84300 10.94500  -13.64600 1.000 26.52000 ? 13  VAL A O   1 
ATOM   75   C CB  . VAL A 1 11  ? -13.20800 11.46200  -15.20300 1.000 27.01000 ? 13  VAL A CB  1 
ATOM   76   C CG1 . VAL A 1 11  ? -14.22500 10.93300  -16.14900 1.000 27.66000 ? 13  VAL A CG1 1 
ATOM   77   C CG2 . VAL A 1 11  ? -12.30800 12.41100  -15.87100 1.000 28.61000 ? 13  VAL A CG2 1 
ATOM   78   N N   . GLU A 1 12  ? -14.28000 10.54900  -12.22200 1.000 27.89000 ? 14  GLU A N   1 
ATOM   79   C CA  . GLU A 1 12  ? -15.01400 9.59600   -11.43900 1.000 28.02000 ? 14  GLU A CA  1 
ATOM   80   C C   . GLU A 1 12  ? -16.28900 10.17400  -10.90400 1.000 28.18000 ? 14  GLU A C   1 
ATOM   81   O O   . GLU A 1 12  ? -17.24600 9.54100   -10.89500 1.000 29.13000 ? 14  GLU A O   1 
ATOM   82   C CB  . GLU A 1 12  ? -14.20700 9.09700   -10.26000 1.000 29.20000 ? 14  GLU A CB  1 
ATOM   83   C CG  . GLU A 1 12  ? -13.06000 8.16700   -10.54200 1.000 29.26000 ? 14  GLU A CG  1 
ATOM   84   C CD  . GLU A 1 12  ? -12.05300 8.04000   -9.41800  1.000 29.10000 ? 14  GLU A CD  1 
ATOM   85   O OE1 . GLU A 1 12  ? -10.91600 8.24400   -9.65100  1.000 28.16000 ? 14  GLU A OE1 1 
ATOM   86   O OE2 . GLU A 1 12  ? -12.42200 7.73900   -8.33600  1.000 31.92000 ? 14  GLU A OE2 1 
ATOM   87   N N   . GLY A 1 13  ? -16.26800 11.40300  -10.47600 1.000 29.22000 ? 15  GLY A N   1 
ATOM   88   C CA  . GLY A 1 13  ? -17.44700 12.06400  -9.94700  1.000 30.44000 ? 15  GLY A CA  1 
ATOM   89   C C   . GLY A 1 13  ? -18.50400 12.41100  -10.98500 1.000 30.91000 ? 15  GLY A C   1 
ATOM   90   O O   . GLY A 1 13  ? -19.55900 12.94100  -10.62000 1.000 31.17000 ? 15  GLY A O   1 
ATOM   91   N N   . CYS A 1 14  ? -18.25800 12.13900  -12.24700 1.000 30.93000 ? 16  CYS A N   1 
ATOM   92   C CA  . CYS A 1 14  ? -19.17500 12.36400  -13.32900 1.000 27.27000 ? 16  CYS A CA  1 
ATOM   93   C C   . CYS A 1 14  ? -19.77600 11.10100  -13.92400 1.000 28.55000 ? 16  CYS A C   1 
ATOM   94   O O   . CYS A 1 14  ? -20.59300 11.18000  -14.73100 1.000 32.01000 ? 16  CYS A O   1 
ATOM   95   C CB  . CYS A 1 14  ? -18.49900 13.14600  -14.41700 1.000 29.59000 ? 16  CYS A CB  1 
ATOM   96   S SG  . CYS A 1 14  ? -17.79600 14.68500  -14.03200 1.000 36.61000 ? 16  CYS A SG  1 
ATOM   97   N N   . MET A 1 15  ? -19.34000 9.94500   -13.52000 1.000 28.99000 ? 17  MET A N   1 
ATOM   98   C CA  . MET A 1 15  ? -19.83200 8.70500   -14.03600 1.000 25.58000 ? 17  MET A CA  1 
ATOM   99   C C   . MET A 1 15  ? -21.15400 8.31500   -13.42300 1.000 34.04000 ? 17  MET A C   1 
ATOM   100  O O   . MET A 1 15  ? -21.29500 8.34900   -12.26200 1.000 27.91000 ? 17  MET A O   1 
ATOM   101  C CB  . MET A 1 15  ? -18.82800 7.62200   -13.82700 1.000 28.47000 ? 17  MET A CB  1 
ATOM   102  C CG  . MET A 1 15  ? -17.53500 7.82500   -14.52900 1.000 32.49000 ? 17  MET A CG  1 
ATOM   103  S SD  . MET A 1 15  ? -17.67400 8.37600   -16.21100 1.000 48.18000 ? 17  MET A SD  1 
ATOM   104  C CE  . MET A 1 15  ? -18.47600 7.04700   -16.97400 1.000 31.52000 ? 17  MET A CE  1 
ATOM   105  N N   . VAL A 1 16  ? -22.08500 7.92000   -14.26300 1.000 29.08000 ? 18  VAL A N   1 
ATOM   106  C CA  . VAL A 1 16  ? -23.40300 7.46200   -13.92400 1.000 31.95000 ? 18  VAL A CA  1 
ATOM   107  C C   . VAL A 1 16  ? -23.77900 6.24400   -14.71500 1.000 32.82000 ? 18  VAL A C   1 
ATOM   108  O O   . VAL A 1 16  ? -23.12900 5.88700   -15.60400 1.000 30.49000 ? 18  VAL A O   1 
ATOM   109  C CB  . VAL A 1 16  ? -24.48900 8.52200   -14.11700 1.000 30.95000 ? 18  VAL A CB  1 
ATOM   110  C CG1 . VAL A 1 16  ? -24.23300 9.70300   -13.27000 1.000 32.27000 ? 18  VAL A CG1 1 
ATOM   111  C CG2 . VAL A 1 16  ? -24.61800 8.94200   -15.53900 1.000 27.44000 ? 18  VAL A CG2 1 
ATOM   112  N N   . GLN A 1 17  ? -24.84900 5.61000   -14.33200 1.000 33.65000 ? 19  GLN A N   1 
ATOM   113  C CA  . GLN A 1 17  ? -25.37800 4.45700   -15.01600 1.000 34.15000 ? 19  GLN A CA  1 
ATOM   114  C C   . GLN A 1 17  ? -26.67200 4.80100   -15.72600 1.000 36.26000 ? 19  GLN A C   1 
ATOM   115  O O   . GLN A 1 17  ? -27.50000 5.41800   -15.18600 1.000 35.64000 ? 19  GLN A O   1 
ATOM   116  C CB  . GLN A 1 17  ? -25.59200 3.35400   -14.05600 1.000 37.28000 ? 19  GLN A CB  1 
ATOM   117  C CG  . GLN A 1 17  ? -26.32500 2.19500   -14.57800 1.000 38.81000 ? 19  GLN A CG  1 
ATOM   118  C CD  . GLN A 1 17  ? -26.47100 1.07600   -13.58600 1.000 45.99000 ? 19  GLN A CD  1 
ATOM   119  O OE1 . GLN A 1 17  ? -26.51500 -0.03800  -13.96600 1.000 50.62000 ? 19  GLN A OE1 1 
ATOM   120  N NE2 . GLN A 1 17  ? -26.54900 1.38100   -12.33700 1.000 43.89000 ? 19  GLN A NE2 1 
ATOM   121  N N   . VAL A 1 18  ? -26.79800 4.42800   -16.97200 1.000 35.34000 ? 20  VAL A N   1 
ATOM   122  C CA  . VAL A 1 18  ? -27.97500 4.69900   -17.75600 1.000 33.10000 ? 20  VAL A CA  1 
ATOM   123  C C   . VAL A 1 18  ? -28.60100 3.41400   -18.21200 1.000 36.73000 ? 20  VAL A C   1 
ATOM   124  O O   . VAL A 1 18  ? -27.95800 2.59200   -18.76500 1.000 34.94000 ? 20  VAL A O   1 
ATOM   125  C CB  . VAL A 1 18  ? -27.71600 5.60400   -18.95300 1.000 32.80000 ? 20  VAL A CB  1 
ATOM   126  C CG1 . VAL A 1 18  ? -28.97100 5.85900   -19.70000 1.000 33.23000 ? 20  VAL A CG1 1 
ATOM   127  C CG2 . VAL A 1 18  ? -27.13000 6.90800   -18.57300 1.000 28.72000 ? 20  VAL A CG2 1 
ATOM   128  N N   . THR A 1 19  ? -29.87700 3.26300   -17.96500 1.000 35.80000 ? 21  THR A N   1 
ATOM   129  C CA  . THR A 1 19  ? -30.59600 2.04700   -18.31800 1.000 36.85000 ? 21  THR A CA  1 
ATOM   130  C C   . THR A 1 19  ? -31.83400 2.43300   -19.11900 1.000 38.40000 ? 21  THR A C   1 
ATOM   131  O O   . THR A 1 19  ? -32.58200 3.33800   -18.73500 1.000 40.71000 ? 21  THR A O   1 
ATOM   132  C CB  . THR A 1 19  ? -31.00500 1.24400   -17.06600 1.000 42.90000 ? 21  THR A CB  1 
ATOM   133  O OG1 . THR A 1 19  ? -29.83500 0.82100   -16.35600 1.000 43.64000 ? 21  THR A OG1 1 
ATOM   134  C CG2 . THR A 1 19  ? -31.86700 0.01500   -17.42800 1.000 38.64000 ? 21  THR A CG2 1 
ATOM   135  N N   . CYS A 1 20  ? -32.05600 1.79000   -20.21900 1.000 37.08000 ? 22  CYS A N   1 
ATOM   136  C CA  . CYS A 1 20  ? -33.23100 1.97900   -21.00100 1.000 40.71000 ? 22  CYS A CA  1 
ATOM   137  C C   . CYS A 1 20  ? -33.64300 0.58300   -21.32100 1.000 42.26000 ? 22  CYS A C   1 
ATOM   138  O O   . CYS A 1 20  ? -32.94000 -0.12700  -21.95300 1.000 39.34000 ? 22  CYS A O   1 
ATOM   139  C CB  . CYS A 1 20  ? -32.99000 2.77600   -22.25300 1.000 37.23000 ? 22  CYS A CB  1 
ATOM   140  S SG  . CYS A 1 20  ? -34.42500 3.16800   -23.21200 1.000 51.08000 ? 22  CYS A SG  1 
ATOM   141  N N   . GLY A 1 21  ? -34.81000 0.20700   -20.86900 1.000 43.35000 ? 23  GLY A N   1 
ATOM   142  C CA  . GLY A 1 21  ? -35.29200 -1.12900  -21.07300 1.000 45.20000 ? 23  GLY A CA  1 
ATOM   143  C C   . GLY A 1 21  ? -34.39500 -2.11900  -20.41600 1.000 43.52000 ? 23  GLY A C   1 
ATOM   144  O O   . GLY A 1 21  ? -34.15900 -2.05100  -19.27600 1.000 41.86000 ? 23  GLY A O   1 
ATOM   145  N N   . THR A 1 22  ? -33.91000 -3.05800  -21.18600 1.000 45.84000 ? 24  THR A N   1 
ATOM   146  C CA  . THR A 1 22  ? -33.01700 -4.06900  -20.70500 1.000 45.10000 ? 24  THR A CA  1 
ATOM   147  C C   . THR A 1 22  ? -31.54900 -3.77900  -20.97200 1.000 44.58000 ? 24  THR A C   1 
ATOM   148  O O   . THR A 1 22  ? -30.72000 -4.57600  -20.70300 1.000 44.56000 ? 24  THR A O   1 
ATOM   149  C CB  . THR A 1 22  ? -33.37200 -5.40700  -21.33500 1.000 46.24000 ? 24  THR A CB  1 
ATOM   150  O OG1 . THR A 1 22  ? -32.51500 -6.39900  -20.84300 1.000 59.10000 ? 24  THR A OG1 1 
ATOM   151  C CG2 . THR A 1 22  ? -33.18500 -5.37300  -22.76900 1.000 55.45000 ? 24  THR A CG2 1 
ATOM   152  N N   . THR A 1 23  ? -31.24600 -2.63500  -21.52400 1.000 43.61000 ? 25  THR A N   1 
ATOM   153  C CA  . THR A 1 23  ? -29.86900 -2.28400  -21.82600 1.000 41.66000 ? 25  THR A CA  1 
ATOM   154  C C   . THR A 1 23  ? -29.27700 -1.28500  -20.86400 1.000 37.87000 ? 25  THR A C   1 
ATOM   155  O O   . THR A 1 23  ? -29.87800 -0.33700  -20.60000 1.000 41.26000 ? 25  THR A O   1 
ATOM   156  C CB  . THR A 1 23  ? -29.76100 -1.71700  -23.21600 1.000 44.03000 ? 25  THR A CB  1 
ATOM   157  O OG1 . THR A 1 23  ? -30.56900 -2.46600  -24.09000 1.000 45.77000 ? 25  THR A OG1 1 
ATOM   158  C CG2 . THR A 1 23  ? -28.37100 -1.79700  -23.66100 1.000 39.04000 ? 25  THR A CG2 1 
ATOM   159  N N   . THR A 1 24  ? -28.10000 -1.52200  -20.34500 1.000 36.97000 ? 26  THR A N   1 
ATOM   160  C CA  . THR A 1 24  ? -27.46900 -0.60800  -19.40000 1.000 41.10000 ? 26  THR A CA  1 
ATOM   161  C C   . THR A 1 24  ? -26.02100 -0.35700  -19.79900 1.000 38.39000 ? 26  THR A C   1 
ATOM   162  O O   . THR A 1 24  ? -25.30000 -1.27700  -20.19100 1.000 41.17000 ? 26  THR A O   1 
ATOM   163  C CB  . THR A 1 24  ? -27.51800 -1.14800  -17.95800 1.000 40.14000 ? 26  THR A CB  1 
ATOM   164  O OG1 . THR A 1 24  ? -28.87900 -1.37800  -17.57900 1.000 49.05000 ? 26  THR A OG1 1 
ATOM   165  C CG2 . THR A 1 24  ? -26.95800 -0.14800  -17.02500 1.000 38.89000 ? 26  THR A CG2 1 
ATOM   166  N N   . LEU A 1 25  ? -25.59700 0.89500   -19.68700 1.000 38.11000 ? 27  LEU A N   1 
ATOM   167  C CA  . LEU A 1 25  ? -24.22700 1.27000   -19.97500 1.000 35.46000 ? 27  LEU A CA  1 
ATOM   168  C C   . LEU A 1 25  ? -23.88800 2.49500   -19.13500 1.000 34.80000 ? 27  LEU A C   1 
ATOM   169  O O   . LEU A 1 25  ? -24.68000 2.92400   -18.28800 1.000 32.69000 ? 27  LEU A O   1 
ATOM   170  C CB  . LEU A 1 25  ? -24.05100 1.47800   -21.48500 1.000 33.47000 ? 27  LEU A CB  1 
ATOM   171  C CG  . LEU A 1 25  ? -25.06500 2.32600   -22.25200 1.000 33.59000 ? 27  LEU A CG  1 
ATOM   172  C CD1 . LEU A 1 25  ? -25.16800 3.73100   -21.68300 1.000 31.49000 ? 27  LEU A CD1 1 
ATOM   173  C CD2 . LEU A 1 25  ? -24.70900 2.34800   -23.75400 1.000 31.37000 ? 27  LEU A CD2 1 
ATOM   174  N N   . ASN A 1 26  ? -22.73700 3.06700   -19.37300 1.000 29.36000 ? 28  ASN A N   1 
ATOM   175  C CA  . ASN A 1 26  ? -22.26100 4.21400   -18.69500 1.000 28.99000 ? 28  ASN A CA  1 
ATOM   176  C C   . ASN A 1 26  ? -22.61000 5.54700   -19.34200 1.000 30.04000 ? 28  ASN A C   1 
ATOM   177  O O   . ASN A 1 26  ? -22.64900 5.66700   -20.52500 1.000 27.39000 ? 28  ASN A O   1 
ATOM   178  C CB  . ASN A 1 26  ? -20.74300 4.15300   -18.56400 1.000 28.41000 ? 28  ASN A CB  1 
ATOM   179  C CG  . ASN A 1 26  ? -20.24800 2.87700   -17.96100 1.000 32.52000 ? 28  ASN A CG  1 
ATOM   180  O OD1 . ASN A 1 26  ? -20.39500 2.64700   -16.83000 1.000 32.78000 ? 28  ASN A OD1 1 
ATOM   181  N ND2 . ASN A 1 26  ? -19.64100 2.07700   -18.74500 1.000 33.23000 ? 28  ASN A ND2 1 
ATOM   182  N N   . GLY A 1 27  ? -22.81400 6.53400   -18.51200 1.000 25.39000 ? 29  GLY A N   1 
ATOM   183  C CA  . GLY A 1 27  ? -23.10500 7.87500   -18.90300 1.000 24.79000 ? 29  GLY A CA  1 
ATOM   184  C C   . GLY A 1 27  ? -22.21100 8.89700   -18.24200 1.000 26.78000 ? 29  GLY A C   1 
ATOM   185  O O   . GLY A 1 27  ? -21.67500 8.62800   -17.28000 1.000 27.92000 ? 29  GLY A O   1 
ATOM   186  N N   . LEU A 1 28  ? -22.06100 10.05600  -18.81700 1.000 26.30000 ? 30  LEU A N   1 
ATOM   187  C CA  . LEU A 1 28  ? -21.28300 11.11100  -18.27800 1.000 28.44000 ? 30  LEU A CA  1 
ATOM   188  C C   . LEU A 1 28  ? -22.18200 12.29000  -17.90000 1.000 30.59000 ? 30  LEU A C   1 
ATOM   189  O O   . LEU A 1 28  ? -22.78600 12.88400  -18.72300 1.000 27.23000 ? 30  LEU A O   1 
ATOM   190  C CB  . LEU A 1 28  ? -20.21700 11.51200  -19.26800 1.000 24.40000 ? 30  LEU A CB  1 
ATOM   191  C CG  . LEU A 1 28  ? -19.24800 12.60500  -18.90000 1.000 26.88000 ? 30  LEU A CG  1 
ATOM   192  C CD1 . LEU A 1 28  ? -18.26200 12.20100  -17.87000 1.000 26.12000 ? 30  LEU A CD1 1 
ATOM   193  C CD2 . LEU A 1 28  ? -18.57000 13.21400  -20.05900 1.000 26.03000 ? 30  LEU A CD2 1 
ATOM   194  N N   . TRP A 1 29  ? -22.19200 12.61800  -16.63500 1.000 29.17000 ? 31  TRP A N   1 
ATOM   195  C CA  . TRP A 1 29  ? -22.99600 13.65800  -16.03900 1.000 30.61000 ? 31  TRP A CA  1 
ATOM   196  C C   . TRP A 1 29  ? -22.23000 14.92400  -15.80700 1.000 32.39000 ? 31  TRP A C   1 
ATOM   197  O O   . TRP A 1 29  ? -21.44900 14.99900  -14.93600 1.000 29.76000 ? 31  TRP A O   1 
ATOM   198  C CB  . TRP A 1 29  ? -23.56900 13.14000  -14.72900 1.000 30.91000 ? 31  TRP A CB  1 
ATOM   199  C CG  . TRP A 1 29  ? -24.50700 14.03300  -13.97800 1.000 36.35000 ? 31  TRP A CG  1 
ATOM   200  C CD1 . TRP A 1 29  ? -25.22400 15.03300  -14.47100 1.000 37.04000 ? 31  TRP A CD1 1 
ATOM   201  C CD2 . TRP A 1 29  ? -24.84700 13.96000  -12.60200 1.000 36.77000 ? 31  TRP A CD2 1 
ATOM   202  N NE1 . TRP A 1 29  ? -25.96600 15.61900  -13.52000 1.000 38.36000 ? 31  TRP A NE1 1 
ATOM   203  C CE2 . TRP A 1 29  ? -25.76000 14.96700  -12.35000 1.000 39.40000 ? 31  TRP A CE2 1 
ATOM   204  C CE3 . TRP A 1 29  ? -24.46300 13.15200  -11.56100 1.000 35.99000 ? 31  TRP A CE3 1 
ATOM   205  C CZ2 . TRP A 1 29  ? -26.28500 15.17300  -11.11700 1.000 39.57000 ? 31  TRP A CZ2 1 
ATOM   206  C CZ3 . TRP A 1 29  ? -24.98200 13.36700  -10.35900 1.000 38.27000 ? 31  TRP A CZ3 1 
ATOM   207  C CH2 . TRP A 1 29  ? -25.87700 14.35800  -10.13800 1.000 37.24000 ? 31  TRP A CH2 1 
ATOM   208  N N   . LEU A 1 30  ? -22.49600 15.91200  -16.62700 1.000 31.25000 ? 32  LEU A N   1 
ATOM   209  C CA  . LEU A 1 30  ? -21.88000 17.21100  -16.58100 1.000 33.26000 ? 32  LEU A CA  1 
ATOM   210  C C   . LEU A 1 30  ? -22.95600 18.26900  -16.51700 1.000 38.74000 ? 32  LEU A C   1 
ATOM   211  O O   . LEU A 1 30  ? -23.82400 18.27800  -17.31400 1.000 35.98000 ? 32  LEU A O   1 
ATOM   212  C CB  . LEU A 1 30  ? -21.02100 17.42200  -17.78900 1.000 32.77000 ? 32  LEU A CB  1 
ATOM   213  C CG  . LEU A 1 30  ? -19.86300 16.49000  -18.04200 1.000 32.81000 ? 32  LEU A CG  1 
ATOM   214  C CD1 . LEU A 1 30  ? -19.17600 16.76000  -19.34900 1.000 31.41000 ? 32  LEU A CD1 1 
ATOM   215  C CD2 . LEU A 1 30  ? -18.91500 16.39300  -16.90300 1.000 27.67000 ? 32  LEU A CD2 1 
ATOM   216  N N   . ASP A 1 31  ? -22.85500 19.16200  -15.53700 1.000 40.38000 ? 33  ASP A N   1 
ATOM   217  C CA  . ASP A 1 31  ? -23.90400 20.17000  -15.29100 1.000 40.14000 ? 33  ASP A CA  1 
ATOM   218  C C   . ASP A 1 31  ? -25.21900 19.39900  -15.22500 1.000 38.22000 ? 33  ASP A C   1 
ATOM   219  O O   . ASP A 1 31  ? -25.29300 18.39700  -14.49800 1.000 37.78000 ? 33  ASP A O   1 
ATOM   220  C CB  . ASP A 1 31  ? -23.84300 21.28200  -16.33700 1.000 42.13000 ? 33  ASP A CB  1 
ATOM   221  C CG  . ASP A 1 31  ? -22.56300 22.10200  -16.26600 1.000 45.73000 ? 33  ASP A CG  1 
ATOM   222  O OD1 . ASP A 1 31  ? -22.11700 22.46000  -15.15100 1.000 46.68000 ? 33  ASP A OD1 1 
ATOM   223  O OD2 . ASP A 1 31  ? -22.00200 22.41100  -17.34300 1.000 52.73000 ? 33  ASP A OD2 1 
ATOM   224  N N   . ASP A 1 32  ? -26.25000 19.77400  -15.99200 1.000 39.14000 ? 34  ASP A N   1 
ATOM   225  C CA  . ASP A 1 32  ? -27.53400 19.07900  -15.95100 1.000 41.22000 ? 34  ASP A CA  1 
ATOM   226  C C   . ASP A 1 32  ? -27.78400 18.18700  -17.17100 1.000 41.31000 ? 34  ASP A C   1 
ATOM   227  O O   . ASP A 1 32  ? -28.94300 17.91300  -17.49300 1.000 40.76000 ? 34  ASP A O   1 
ATOM   228  C CB  . ASP A 1 32  ? -28.69100 20.07600  -15.78500 1.000 46.66000 ? 34  ASP A CB  1 
ATOM   229  C CG  . ASP A 1 32  ? -28.80000 21.07900  -16.93900 1.000 47.93000 ? 34  ASP A CG  1 
ATOM   230  O OD1 . ASP A 1 32  ? -27.83800 21.24500  -17.71300 1.000 48.54000 ? 34  ASP A OD1 1 
ATOM   231  O OD2 . ASP A 1 32  ? -29.85900 21.72300  -17.06700 1.000 53.76000 ? 34  ASP A OD2 1 
ATOM   232  N N   . VAL A 1 33  ? -26.73100 17.70500  -17.84500 1.000 37.41000 ? 35  VAL A N   1 
ATOM   233  C CA  . VAL A 1 33  ? -26.87200 16.80600  -18.99000 1.000 33.52000 ? 35  VAL A CA  1 
ATOM   234  C C   . VAL A 1 33  ? -26.10400 15.51400  -18.73000 1.000 33.79000 ? 35  VAL A C   1 
ATOM   235  O O   . VAL A 1 33  ? -24.95400 15.54800  -18.27100 1.000 32.47000 ? 35  VAL A O   1 
ATOM   236  C CB  . VAL A 1 33  ? -26.37200 17.45500  -20.29800 1.000 35.34000 ? 35  VAL A CB  1 
ATOM   237  C CG1 . VAL A 1 33  ? -26.58500 16.50300  -21.48500 1.000 32.23000 ? 35  VAL A CG1 1 
ATOM   238  C CG2 . VAL A 1 33  ? -27.04800 18.79600  -20.53800 1.000 38.80000 ? 35  VAL A CG2 1 
ATOM   239  N N   . VAL A 1 34  ? -26.72600 14.38200  -19.04100 1.000 29.47000 ? 36  VAL A N   1 
ATOM   240  C CA  . VAL A 1 34  ? -26.05700 13.08300  -19.07300 1.000 29.81000 ? 36  VAL A CA  1 
ATOM   241  C C   . VAL A 1 34  ? -25.84800 12.69200  -20.53600 1.000 34.15000 ? 36  VAL A C   1 
ATOM   242  O O   . VAL A 1 34  ? -26.81200 12.61300  -21.31200 1.000 30.11000 ? 36  VAL A O   1 
ATOM   243  C CB  . VAL A 1 34  ? -26.86000 12.01400  -18.32100 1.000 31.06000 ? 36  VAL A CB  1 
ATOM   244  C CG1 . VAL A 1 34  ? -26.28800 10.64300  -18.56400 1.000 26.83000 ? 36  VAL A CG1 1 
ATOM   245  C CG2 . VAL A 1 34  ? -26.86900 12.31300  -16.81000 1.000 31.60000 ? 36  VAL A CG2 1 
ATOM   246  N N   . TYR A 1 35  ? -24.58900 12.47200  -20.91700 1.000 29.73000 ? 37  TYR A N   1 
ATOM   247  C CA  . TYR A 1 35  ? -24.20300 12.01900  -22.24900 1.000 28.67000 ? 37  TYR A CA  1 
ATOM   248  C C   . TYR A 1 35  ? -23.94900 10.51600  -22.21800 1.000 31.18000 ? 37  TYR A C   1 
ATOM   249  O O   . TYR A 1 35  ? -23.31900 10.01400  -21.28100 1.000 29.95000 ? 37  TYR A O   1 
ATOM   250  C CB  . TYR A 1 35  ? -22.93500 12.73100  -22.73100 1.000 29.46000 ? 37  TYR A CB  1 
ATOM   251  C CG  . TYR A 1 35  ? -23.01800 14.23100  -22.67500 1.000 33.43000 ? 37  TYR A CG  1 
ATOM   252  C CD1 . TYR A 1 35  ? -22.88500 14.90400  -21.46600 1.000 31.29000 ? 37  TYR A CD1 1 
ATOM   253  C CD2 . TYR A 1 35  ? -23.25600 14.98100  -23.83000 1.000 31.92000 ? 37  TYR A CD2 1 
ATOM   254  C CE1 . TYR A 1 35  ? -22.97600 16.27300  -21.40100 1.000 32.21000 ? 37  TYR A CE1 1 
ATOM   255  C CE2 . TYR A 1 35  ? -23.34200 16.36200  -23.77500 1.000 32.66000 ? 37  TYR A CE2 1 
ATOM   256  C CZ  . TYR A 1 35  ? -23.20900 16.99600  -22.55000 1.000 33.31000 ? 37  TYR A CZ  1 
ATOM   257  O OH  . TYR A 1 35  ? -23.28300 18.35600  -22.46000 1.000 32.91000 ? 37  TYR A OH  1 
ATOM   258  N N   . CYS A 1 36  ? -24.40000 9.81300   -23.23900 1.000 27.32000 ? 38  CYS A N   1 
ATOM   259  C CA  . CYS A 1 36  ? -24.17600 8.36300   -23.29700 1.000 29.96000 ? 38  CYS A CA  1 
ATOM   260  C C   . CYS A 1 36  ? -24.37100 7.90800   -24.73300 1.000 30.70000 ? 38  CYS A C   1 
ATOM   261  O O   . CYS A 1 36  ? -24.89800 8.66200   -25.56800 1.000 28.00000 ? 38  CYS A O   1 
ATOM   262  C CB  . CYS A 1 36  ? -25.12000 7.62300   -22.33700 1.000 30.27000 ? 38  CYS A CB  1 
ATOM   263  S SG  . CYS A 1 36  ? -26.83500 7.48300   -22.89300 1.000 31.44000 ? 38  CYS A SG  1 
ATOM   264  N N   . PRO A 1 37  ? -23.93300 6.68600   -25.07600 1.000 27.57000 ? 39  PRO A N   1 
ATOM   265  C CA  . PRO A 1 37  ? -24.10000 6.21200   -26.46100 1.000 32.11000 ? 39  PRO A CA  1 
ATOM   266  C C   . PRO A 1 37  ? -25.57000 5.96000   -26.76400 1.000 32.58000 ? 39  PRO A C   1 
ATOM   267  O O   . PRO A 1 37  ? -26.29200 5.38600   -25.94800 1.000 28.14000 ? 39  PRO A O   1 
ATOM   268  C CB  . PRO A 1 37  ? -23.29400 4.90700   -26.51100 1.000 28.06000 ? 39  PRO A CB  1 
ATOM   269  C CG  . PRO A 1 37  ? -22.33600 4.96500   -25.30500 1.000 30.11000 ? 39  PRO A CG  1 
ATOM   270  C CD  . PRO A 1 37  ? -23.12800 5.74400   -24.26200 1.000 30.74000 ? 39  PRO A CD  1 
ATOM   271  N N   . ARG A 1 38  ? -25.99700 6.33500   -27.93500 1.000 27.85000 ? 40  ARG A N   1 
ATOM   272  C CA  . ARG A 1 38  ? -27.37000 6.16000   -28.38000 1.000 32.20000 ? 40  ARG A CA  1 
ATOM   273  C C   . ARG A 1 38  ? -27.81400 4.72800   -28.47900 1.000 33.63000 ? 40  ARG A C   1 
ATOM   274  O O   . ARG A 1 38  ? -28.95100 4.46200   -28.46200 1.000 31.49000 ? 40  ARG A O   1 
ATOM   275  C CB  . ARG A 1 38  ? -27.69200 6.91700   -29.64600 1.000 30.25000 ? 40  ARG A CB  1 
ATOM   276  C CG  . ARG A 1 38  ? -27.05800 6.41400   -30.88700 1.000 28.89000 ? 40  ARG A CG  1 
ATOM   277  C CD  . ARG A 1 38  ? -27.40100 7.26000   -32.08600 1.000 29.88000 ? 40  ARG A CD  1 
ATOM   278  N NE  . ARG A 1 38  ? -26.86800 6.70500   -33.28300 1.000 32.69000 ? 40  ARG A NE  1 
ATOM   279  C CZ  . ARG A 1 38  ? -27.07000 7.16200   -34.49600 1.000 35.79000 ? 40  ARG A CZ  1 
ATOM   280  N NH1 . ARG A 1 38  ? -27.84000 8.18600   -34.70000 1.000 32.62000 ? 40  ARG A NH1 1 
ATOM   281  N NH2 . ARG A 1 38  ? -26.50900 6.56300   -35.50000 1.000 30.84000 ? 40  ARG A NH2 1 
ATOM   282  N N   . HIS A 1 39  ? -26.86700 3.83200   -28.52800 1.000 30.00000 ? 41  HIS A N   1 
ATOM   283  C CA  . HIS A 1 39  ? -27.08200 2.41900   -28.59100 1.000 36.76000 ? 41  HIS A CA  1 
ATOM   284  C C   . HIS A 1 39  ? -27.88000 1.97600   -27.37100 1.000 34.34000 ? 41  HIS A C   1 
ATOM   285  O O   . HIS A 1 39  ? -28.42600 0.95200   -27.37100 1.000 33.91000 ? 41  HIS A O   1 
ATOM   286  C CB  . HIS A 1 39  ? -25.71500 1.69700   -28.65500 1.000 44.05000 ? 41  HIS A CB  1 
ATOM   287  C CG  . HIS A 1 39  ? -25.73700 0.29200   -28.15600 1.000 50.62000 ? 41  HIS A CG  1 
ATOM   288  N ND1 . HIS A 1 39  ? -25.49200 -0.03100  -26.85600 1.000 50.47000 ? 41  HIS A ND1 1 
ATOM   289  C CD2 . HIS A 1 39  ? -26.00900 -0.87500  -28.77600 1.000 52.91000 ? 41  HIS A CD2 1 
ATOM   290  C CE1 . HIS A 1 39  ? -25.63800 -1.33000  -26.68100 1.000 52.10000 ? 41  HIS A CE1 1 
ATOM   291  N NE2 . HIS A 1 39  ? -25.92800 -1.87100  -27.83800 1.000 58.22000 ? 41  HIS A NE2 1 
ATOM   292  N N   . VAL A 1 40  ? -27.89900 2.75900   -26.32500 1.000 31.26000 ? 42  VAL A N   1 
ATOM   293  C CA  . VAL A 1 40  ? -28.64400 2.34000   -25.13900 1.000 33.05000 ? 42  VAL A CA  1 
ATOM   294  C C   . VAL A 1 40  ? -30.11100 2.07200   -25.45600 1.000 33.75000 ? 42  VAL A C   1 
ATOM   295  O O   . VAL A 1 40  ? -30.75600 1.29800   -24.74100 1.000 36.89000 ? 42  VAL A O   1 
ATOM   296  C CB  . VAL A 1 40  ? -28.51300 3.38500   -24.00300 1.000 34.00000 ? 42  VAL A CB  1 
ATOM   297  C CG1 . VAL A 1 40  ? -29.35100 4.61800   -24.28700 1.000 33.07000 ? 42  VAL A CG1 1 
ATOM   298  C CG2 . VAL A 1 40  ? -28.89800 2.77900   -22.66000 1.000 34.09000 ? 42  VAL A CG2 1 
ATOM   299  N N   . ILE A 1 41  ? -30.64400 2.68300   -26.49200 1.000 33.14000 ? 43  ILE A N   1 
ATOM   300  C CA  . ILE A 1 41  ? -32.03700 2.51600   -26.86800 1.000 35.76000 ? 43  ILE A CA  1 
ATOM   301  C C   . ILE A 1 41  ? -32.31400 1.35700   -27.78800 1.000 38.75000 ? 43  ILE A C   1 
ATOM   302  O O   . ILE A 1 41  ? -33.37500 1.23400   -28.23600 1.000 40.33000 ? 43  ILE A O   1 
ATOM   303  C CB  . ILE A 1 41  ? -32.69500 3.78300   -27.44800 1.000 33.25000 ? 43  ILE A CB  1 
ATOM   304  C CG1 . ILE A 1 41  ? -32.24100 4.08000   -28.87000 1.000 32.30000 ? 43  ILE A CG1 1 
ATOM   305  C CG2 . ILE A 1 41  ? -32.52700 4.96100   -26.56300 1.000 30.59000 ? 43  ILE A CG2 1 
ATOM   306  C CD1 . ILE A 1 41  ? -32.80900 5.31800   -29.42300 1.000 32.92000 ? 43  ILE A CD1 1 
ATOM   307  N N   . CYS A 1 42  ? -31.32500 0.54000   -28.07100 1.000 38.97000 ? 44  CYS A N   1 
ATOM   308  C CA  . CYS A 1 42  ? -31.45400 -0.58400  -28.94700 1.000 42.99000 ? 44  CYS A CA  1 
ATOM   309  C C   . CYS A 1 42  ? -31.68100 -1.87200  -28.24100 1.000 48.95000 ? 44  CYS A C   1 
ATOM   310  O O   . CYS A 1 42  ? -31.17300 -2.09200  -27.21600 1.000 52.03000 ? 44  CYS A O   1 
ATOM   311  C CB  . CYS A 1 42  ? -30.20900 -0.74600  -29.79000 1.000 45.23000 ? 44  CYS A CB  1 
ATOM   312  S SG  . CYS A 1 42  ? -29.96300 0.45900   -31.04700 1.000 42.34000 ? 44  CYS A SG  1 
ATOM   313  N N   . THR A 1 43  ? -32.46200 -2.73800  -28.83100 1.000 53.70000 ? 45  THR A N   1 
ATOM   314  C CA  . THR A 1 43  ? -32.72600 -4.03800  -28.27300 1.000 54.96000 ? 45  THR A CA  1 
ATOM   315  C C   . THR A 1 43  ? -31.95100 -5.02100  -29.04300 1.000 62.56000 ? 45  THR A C   1 
ATOM   316  O O   . THR A 1 43  ? -31.26200 -4.65200  -29.92900 1.000 62.42000 ? 45  THR A O   1 
ATOM   317  C CB  . THR A 1 43  ? -34.19600 -4.40400  -28.17300 1.000 57.22000 ? 45  THR A CB  1 
ATOM   318  O OG1 . THR A 1 43  ? -34.62400 -5.09400  -29.33100 1.000 65.50000 ? 45  THR A OG1 1 
ATOM   319  C CG2 . THR A 1 43  ? -35.01800 -3.20000  -28.02600 1.000 55.99000 ? 45  THR A CG2 1 
ATOM   320  N N   . SER A 1 44  ? -32.06000 -6.28400  -28.71000 1.000 62.70000 ? 46  SER A N   1 
ATOM   321  C CA  . SER A 1 44  ? -31.27200 -7.28200  -29.37400 1.000 63.55000 ? 46  SER A CA  1 
ATOM   322  C C   . SER A 1 44  ? -31.48000 -7.28900  -30.86700 1.000 67.32000 ? 46  SER A C   1 
ATOM   323  O O   . SER A 1 44  ? -30.56000 -7.36500  -31.61600 1.000 74.54000 ? 46  SER A O   1 
ATOM   324  C CB  . SER A 1 44  ? -31.72700 -8.62200  -28.84200 1.000 66.70000 ? 46  SER A CB  1 
ATOM   325  O OG  . SER A 1 44  ? -33.10700 -8.55300  -28.57500 1.000 65.45000 ? 46  SER A OG  1 
ATOM   326  N N   . GLU A 1 45  ? -32.72900 -7.15900  -31.25400 1.000 66.58000 ? 47  GLU A N   1 
ATOM   327  C CA  . GLU A 1 45  ? -33.19100 -7.20700  -32.60200 1.000 59.23000 ? 47  GLU A CA  1 
ATOM   328  C C   . GLU A 1 45  ? -32.94300 -5.98500  -33.42100 1.000 57.25000 ? 47  GLU A C   1 
ATOM   329  O O   . GLU A 1 45  ? -33.33100 -5.96300  -34.52700 1.000 59.91000 ? 47  GLU A O   1 
ATOM   330  C CB  . GLU A 1 45  ? -34.67400 -7.52200  -32.58500 1.000 60.98000 ? 47  GLU A CB  1 
ATOM   331  N N   . ASN A 1 46  ? -32.36700 -4.95000  -32.86500 1.000 56.66000 ? 48  ASN A N   1 
ATOM   332  C CA  . ASN A 1 46  ? -32.13000 -3.74200  -33.58200 1.000 52.83000 ? 48  ASN A CA  1 
ATOM   333  C C   . ASN A 1 46  ? -30.73300 -3.45300  -33.92600 1.000 50.35000 ? 48  ASN A C   1 
ATOM   334  O O   . ASN A 1 46  ? -30.47200 -2.53500  -34.62400 1.000 47.22000 ? 48  ASN A O   1 
ATOM   335  C CB  . ASN A 1 46  ? -32.50400 -2.58900  -32.72300 1.000 30.00000 ? 48  ASN A CB  1 
ATOM   336  C CG  . ASN A 1 46  ? -33.91600 -2.58300  -32.33100 1.000 30.00000 ? 48  ASN A CG  1 
ATOM   337  O OD1 . ASN A 1 46  ? -34.79100 -2.74500  -33.12800 1.000 30.00000 ? 48  ASN A OD1 1 
ATOM   338  N ND2 . ASN A 1 46  ? -34.14100 -2.31800  -31.08900 1.000 30.00000 ? 48  ASN A ND2 1 
ATOM   339  N N   . MET A 1 47  ? -29.83500 -4.23500  -33.42300 1.000 50.18000 ? 49  MET A N   1 
ATOM   340  C CA  . MET A 1 47  ? -28.44400 -4.01700  -33.62900 1.000 49.49000 ? 49  MET A CA  1 
ATOM   341  C C   . MET A 1 47  ? -27.96400 -4.05000  -35.05700 1.000 43.32000 ? 49  MET A C   1 
ATOM   342  O O   . MET A 1 47  ? -27.13700 -3.27500  -35.40900 1.000 44.85000 ? 49  MET A O   1 
ATOM   343  C CB  . MET A 1 47  ? -27.67700 -5.02000  -32.79600 1.000 56.80000 ? 49  MET A CB  1 
ATOM   344  N N   . LEU A 1 48  ? -28.48300 -4.94500  -35.86900 1.000 42.98000 ? 50  LEU A N   1 
ATOM   345  C CA  . LEU A 1 48  ? -28.09000 -5.02300  -37.25700 1.000 41.44000 ? 50  LEU A CA  1 
ATOM   346  C C   . LEU A 1 48  ? -28.45700 -3.82400  -38.13100 1.000 40.93000 ? 50  LEU A C   1 
ATOM   347  O O   . LEU A 1 48  ? -27.66500 -3.36600  -38.86800 1.000 39.46000 ? 50  LEU A O   1 
ATOM   348  C CB  . LEU A 1 48  ? -28.63800 -6.24900  -37.86300 1.000 41.28000 ? 50  LEU A CB  1 
ATOM   349  C CG  . LEU A 1 48  ? -28.21500 -7.53300  -37.24900 1.000 47.55000 ? 50  LEU A CG  1 
ATOM   350  C CD1 . LEU A 1 48  ? -29.08900 -8.66800  -37.71400 1.000 46.22000 ? 50  LEU A CD1 1 
ATOM   351  C CD2 . LEU A 1 48  ? -26.76800 -7.82300  -37.51900 1.000 44.62000 ? 50  LEU A CD2 1 
ATOM   352  N N   . ASN A 1 49  ? -29.66200 -3.32700  -38.00700 1.000 37.73000 ? 51  ASN A N   1 
ATOM   353  C CA  . ASN A 1 49  ? -30.10800 -2.21600  -38.75700 1.000 35.38000 ? 51  ASN A CA  1 
ATOM   354  C C   . ASN A 1 49  ? -30.97300 -1.30200  -37.94500 1.000 36.00000 ? 51  ASN A C   1 
ATOM   355  O O   . ASN A 1 49  ? -32.11300 -1.18900  -38.17900 1.000 41.20000 ? 51  ASN A O   1 
ATOM   356  C CB  . ASN A 1 49  ? -30.82900 -2.68700  -39.99200 1.000 34.96000 ? 51  ASN A CB  1 
ATOM   357  C CG  . ASN A 1 49  ? -29.95000 -3.43200  -40.93400 1.000 35.71000 ? 51  ASN A CG  1 
ATOM   358  O OD1 . ASN A 1 49  ? -29.20600 -2.86700  -41.61200 1.000 31.48000 ? 51  ASN A OD1 1 
ATOM   359  N ND2 . ASN A 1 49  ? -30.07500 -4.68400  -40.96100 1.000 33.95000 ? 51  ASN A ND2 1 
ATOM   360  N N   . PRO A 1 50  ? -30.32900 -0.63300  -36.93100 1.000 39.18000 ? 52  PRO A N   1 
ATOM   361  C CA  . PRO A 1 50  ? -31.16600 0.25800   -36.14400 1.000 38.17000 ? 52  PRO A CA  1 
ATOM   362  C C   . PRO A 1 50  ? -31.54200 1.55300   -36.82200 1.000 36.24000 ? 52  PRO A C   1 
ATOM   363  O O   . PRO A 1 50  ? -30.81500 2.09900   -37.55400 1.000 30.36000 ? 52  PRO A O   1 
ATOM   364  C CB  . PRO A 1 50  ? -30.35600 0.49700   -34.89600 1.000 37.63000 ? 52  PRO A CB  1 
ATOM   365  C CG  . PRO A 1 50  ? -29.00200 0.52000   -35.35300 1.000 40.60000 ? 52  PRO A CG  1 
ATOM   366  C CD  . PRO A 1 50  ? -28.92300 -0.56500  -36.34500 1.000 38.29000 ? 52  PRO A CD  1 
ATOM   367  N N   . ASN A 1 51  ? -32.73300 1.99500   -36.52200 1.000 34.02000 ? 53  ASN A N   1 
ATOM   368  C CA  . ASN A 1 51  ? -33.25400 3.22900   -36.99900 1.000 33.46000 ? 53  ASN A CA  1 
ATOM   369  C C   . ASN A 1 51  ? -33.40200 4.00800   -35.73900 1.000 35.12000 ? 53  ASN A C   1 
ATOM   370  O O   . ASN A 1 51  ? -34.33900 3.90300   -35.04100 1.000 32.09000 ? 53  ASN A O   1 
ATOM   371  C CB  . ASN A 1 51  ? -34.56400 2.99600   -37.66700 1.000 37.52000 ? 53  ASN A CB  1 
ATOM   372  C CG  . ASN A 1 51  ? -35.03600 4.15500   -38.42600 1.000 38.48000 ? 53  ASN A CG  1 
ATOM   373  O OD1 . ASN A 1 51  ? -34.86000 5.26100   -38.06600 1.000 37.13000 ? 53  ASN A OD1 1 
ATOM   374  N ND2 . ASN A 1 51  ? -35.63100 3.87600   -39.51300 1.000 46.14000 ? 53  ASN A ND2 1 
ATOM   375  N N   . TYR A 1 52  ? -32.42000 4.83000   -35.49800 1.000 35.92000 ? 54  TYR A N   1 
ATOM   376  C CA  . TYR A 1 52  ? -32.33600 5.53400   -34.22500 1.000 35.95000 ? 54  TYR A CA  1 
ATOM   377  C C   . TYR A 1 52  ? -33.41300 6.60900   -34.09900 1.000 32.73000 ? 54  TYR A C   1 
ATOM   378  O O   . TYR A 1 52  ? -33.96200 6.80000   -33.01200 1.000 33.51000 ? 54  TYR A O   1 
ATOM   379  C CB  . TYR A 1 52  ? -30.93700 6.13000   -34.04100 1.000 33.53000 ? 54  TYR A CB  1 
ATOM   380  C CG  . TYR A 1 52  ? -29.90500 5.08200   -33.71100 1.000 29.92000 ? 54  TYR A CG  1 
ATOM   381  C CD1 . TYR A 1 52  ? -29.85800 4.49800   -32.45000 1.000 34.87000 ? 54  TYR A CD1 1 
ATOM   382  C CD2 . TYR A 1 52  ? -29.02000 4.63400   -34.67300 1.000 32.29000 ? 54  TYR A CD2 1 
ATOM   383  C CE1 . TYR A 1 52  ? -28.92300 3.52000   -32.14100 1.000 37.78000 ? 54  TYR A CE1 1 
ATOM   384  C CE2 . TYR A 1 52  ? -28.05800 3.66000   -34.37400 1.000 35.79000 ? 54  TYR A CE2 1 
ATOM   385  C CZ  . TYR A 1 52  ? -28.01600 3.10400   -33.11000 1.000 36.08000 ? 54  TYR A CZ  1 
ATOM   386  O OH  . TYR A 1 52  ? -27.08200 2.13100   -32.80700 1.000 32.13000 ? 54  TYR A OH  1 
ATOM   387  N N   . GLU A 1 53  ? -33.69800 7.33800   -35.18300 1.000 35.04000 ? 55  GLU A N   1 
ATOM   388  C CA  . GLU A 1 53  ? -34.77300 8.33500   -35.15600 1.000 36.98000 ? 55  GLU A CA  1 
ATOM   389  C C   . GLU A 1 53  ? -36.10800 7.69200   -34.77800 1.000 34.68000 ? 55  GLU A C   1 
ATOM   390  O O   . GLU A 1 53  ? -36.87100 8.24000   -33.97100 1.000 33.06000 ? 55  GLU A O   1 
ATOM   391  C CB  . GLU A 1 53  ? -34.87200 9.03000   -36.52400 1.000 43.30000 ? 55  GLU A CB  1 
ATOM   392  C CG  . GLU A 1 53  ? -35.66000 10.35400  -36.54700 1.000 53.29000 ? 55  GLU A CG  1 
ATOM   393  C CD  . GLU A 1 53  ? -36.43600 10.61300  -37.85300 1.000 58.75000 ? 55  GLU A CD  1 
ATOM   394  O OE1 . GLU A 1 53  ? -37.24500 11.57400  -37.87700 1.000 59.64000 ? 55  GLU A OE1 1 
ATOM   395  O OE2 . GLU A 1 53  ? -36.25300 9.86700   -38.84900 1.000 61.21000 ? 55  GLU A OE2 1 
ATOM   396  N N   . ASP A 1 54  ? -36.38900 6.51800   -35.33600 1.000 34.67000 ? 56  ASP A N   1 
ATOM   397  C CA  . ASP A 1 54  ? -37.63500 5.81800   -35.04700 1.000 38.52000 ? 56  ASP A CA  1 
ATOM   398  C C   . ASP A 1 54  ? -37.65200 5.29000   -33.62000 1.000 38.82000 ? 56  ASP A C   1 
ATOM   399  O O   . ASP A 1 54  ? -38.70000 5.30300   -32.95800 1.000 34.70000 ? 56  ASP A O   1 
ATOM   400  C CB  . ASP A 1 54  ? -37.82300 4.67100   -36.04100 1.000 39.16000 ? 56  ASP A CB  1 
ATOM   401  C CG  . ASP A 1 54  ? -39.14300 3.92000   -35.84200 1.000 42.51000 ? 56  ASP A CG  1 
ATOM   402  O OD1 . ASP A 1 54  ? -40.20700 4.50000   -36.12800 1.000 39.12000 ? 56  ASP A OD1 1 
ATOM   403  O OD2 . ASP A 1 54  ? -39.11200 2.74000   -35.43600 1.000 42.57000 ? 56  ASP A OD2 1 
ATOM   404  N N   . LEU A 1 55  ? -36.50700 4.81300   -33.12600 1.000 32.72000 ? 57  LEU A N   1 
ATOM   405  C CA  . LEU A 1 55  ? -36.49100 4.25400   -31.78300 1.000 34.16000 ? 57  LEU A CA  1 
ATOM   406  C C   . LEU A 1 55  ? -36.58100 5.35400   -30.74200 1.000 33.94000 ? 57  LEU A C   1 
ATOM   407  O O   . LEU A 1 55  ? -37.18200 5.15500   -29.68300 1.000 36.08000 ? 57  LEU A O   1 
ATOM   408  C CB  . LEU A 1 55  ? -35.23500 3.40300   -31.57800 1.000 35.57000 ? 57  LEU A CB  1 
ATOM   409  C CG  . LEU A 1 55  ? -35.12500 2.11400   -32.40400 1.000 38.06000 ? 57  LEU A CG  1 
ATOM   410  C CD1 . LEU A 1 55  ? -33.65200 1.68700   -32.55000 1.000 43.09000 ? 57  LEU A CD1 1 
ATOM   411  C CD2 . LEU A 1 55  ? -35.99300 0.97300   -31.84400 1.000 37.53000 ? 57  LEU A CD2 1 
ATOM   412  N N   . LEU A 1 56  ? -36.03500 6.53300   -31.04100 1.000 34.68000 ? 58  LEU A N   1 
ATOM   413  C CA  . LEU A 1 56  ? -36.03000 7.59700   -30.04400 1.000 37.43000 ? 58  LEU A CA  1 
ATOM   414  C C   . LEU A 1 56  ? -37.36400 8.33900   -29.98600 1.000 37.05000 ? 58  LEU A C   1 
ATOM   415  O O   . LEU A 1 56  ? -37.74500 8.83900   -28.92100 1.000 37.16000 ? 58  LEU A O   1 
ATOM   416  C CB  . LEU A 1 56  ? -34.89900 8.58100   -30.32300 1.000 33.97000 ? 58  LEU A CB  1 
ATOM   417  C CG  . LEU A 1 56  ? -34.72500 9.61100   -29.21100 1.000 37.16000 ? 58  LEU A CG  1 
ATOM   418  C CD1 . LEU A 1 56  ? -34.40200 8.91300   -27.90100 1.000 39.46000 ? 58  LEU A CD1 1 
ATOM   419  C CD2 . LEU A 1 56  ? -33.66400 10.65000  -29.55600 1.000 38.26000 ? 58  LEU A CD2 1 
ATOM   420  N N   . ILE A 1 57  ? -38.08500 8.42100   -31.10300 1.000 35.98000 ? 59  ILE A N   1 
ATOM   421  C CA  . ILE A 1 57  ? -39.36800 9.11500   -31.07300 1.000 36.56000 ? 59  ILE A CA  1 
ATOM   422  C C   . ILE A 1 57  ? -40.33700 8.39600   -30.14100 1.000 35.64000 ? 59  ILE A C   1 
ATOM   423  O O   . ILE A 1 57  ? -41.16000 9.04000   -29.48200 1.000 38.07000 ? 59  ILE A O   1 
ATOM   424  C CB  . ILE A 1 57  ? -39.92400 9.27900   -32.50500 1.000 36.63000 ? 59  ILE A CB  1 
ATOM   425  C CG1 . ILE A 1 57  ? -41.04100 10.32000  -32.53300 1.000 41.39000 ? 59  ILE A CG1 1 
ATOM   426  C CG2 . ILE A 1 57  ? -40.37300 7.94900   -33.09700 1.000 36.48000 ? 59  ILE A CG2 1 
ATOM   427  C CD1 . ILE A 1 57  ? -40.56400 11.70300  -32.92800 1.000 47.64000 ? 59  ILE A CD1 1 
ATOM   428  N N   . ARG A 1 58  ? -40.22000 7.07200   -30.02800 1.000 32.00000 ? 60  ARG A N   1 
ATOM   429  C CA  . ARG A 1 58  ? -41.08300 6.23200   -29.21000 1.000 34.52000 ? 60  ARG A CA  1 
ATOM   430  C C   . ARG A 1 58  ? -40.75500 6.25300   -27.72200 1.000 40.51000 ? 60  ARG A C   1 
ATOM   431  O O   . ARG A 1 58  ? -41.43200 5.55700   -26.95600 1.000 40.28000 ? 60  ARG A O   1 
ATOM   432  C CB  . ARG A 1 58  ? -40.99900 4.79100   -29.70600 1.000 34.58000 ? 60  ARG A CB  1 
ATOM   433  C CG  . ARG A 1 58  ? -41.25300 4.66300   -31.18500 1.000 32.10000 ? 60  ARG A CG  1 
ATOM   434  C CD  . ARG A 1 58  ? -41.21300 3.21600   -31.60400 1.000 31.62000 ? 60  ARG A CD  1 
ATOM   435  N NE  . ARG A 1 58  ? -41.31400 3.08900   -33.05300 1.000 34.30000 ? 60  ARG A NE  1 
ATOM   436  C CZ  . ARG A 1 58  ? -42.45100 2.84500   -33.68700 1.000 39.54000 ? 60  ARG A CZ  1 
ATOM   437  N NH1 . ARG A 1 58  ? -43.55800 2.71400   -32.97400 1.000 33.49000 ? 60  ARG A NH1 1 
ATOM   438  N NH2 . ARG A 1 58  ? -42.48400 2.74800   -35.01800 1.000 35.15000 ? 60  ARG A NH2 1 
ATOM   439  N N   . LYS A 1 59  ? -39.72900 6.98600   -27.29600 1.000 36.88000 ? 61  LYS A N   1 
ATOM   440  C CA  . LYS A 1 59  ? -39.32500 7.04900   -25.90100 1.000 41.17000 ? 61  LYS A CA  1 
ATOM   441  C C   . LYS A 1 59  ? -39.88700 8.30000   -25.24600 1.000 40.37000 ? 61  LYS A C   1 
ATOM   442  O O   . LYS A 1 59  ? -40.02600 9.34700   -25.88500 1.000 40.52000 ? 61  LYS A O   1 
ATOM   443  C CB  . LYS A 1 59  ? -37.78700 7.06700   -25.76200 1.000 40.29000 ? 61  LYS A CB  1 
ATOM   444  C CG  . LYS A 1 59  ? -37.09300 5.89100   -26.39500 1.000 37.68000 ? 61  LYS A CG  1 
ATOM   445  C CD  . LYS A 1 59  ? -37.36700 4.62400   -25.60000 1.000 41.67000 ? 61  LYS A CD  1 
ATOM   446  C CE  . LYS A 1 59  ? -36.61700 3.45500   -26.19600 1.000 46.47000 ? 61  LYS A CE  1 
ATOM   447  N NZ  . LYS A 1 59  ? -37.14500 2.15400   -25.73800 1.000 52.01000 ? 61  LYS A NZ  1 
ATOM   448  N N   . SER A 1 60  ? -40.17000 8.19400   -23.95200 1.000 38.29000 ? 62  SER A N   1 
ATOM   449  C CA  . SER A 1 60  ? -40.43600 9.36900   -23.13700 1.000 43.29000 ? 62  SER A CA  1 
ATOM   450  C C   . SER A 1 60  ? -39.37600 9.48200   -22.05100 1.000 43.17000 ? 62  SER A C   1 
ATOM   451  O O   . SER A 1 60  ? -38.54700 8.58500   -21.85400 1.000 39.81000 ? 62  SER A O   1 
ATOM   452  C CB  . SER A 1 60  ? -41.84400 9.32700   -22.52600 1.000 45.63000 ? 62  SER A CB  1 
ATOM   453  O OG  . SER A 1 60  ? -42.00400 8.19400   -21.70100 1.000 50.98000 ? 62  SER A OG  1 
ATOM   454  N N   . ASN A 1 61  ? -39.41500 10.61700  -21.35400 1.000 45.10000 ? 63  ASN A N   1 
ATOM   455  C CA  . ASN A 1 61  ? -38.40100 10.92400  -20.35500 1.000 48.01000 ? 63  ASN A CA  1 
ATOM   456  C C   . ASN A 1 61  ? -38.28500 9.81400   -19.31700 1.000 44.13000 ? 63  ASN A C   1 
ATOM   457  O O   . ASN A 1 61  ? -37.17300 9.43300   -18.93100 1.000 42.68000 ? 63  ASN A O   1 
ATOM   458  C CB  . ASN A 1 61  ? -38.72000 12.26600  -19.70000 1.000 43.62000 ? 63  ASN A CB  1 
ATOM   459  C CG  . ASN A 1 61  ? -38.36700 13.43200  -20.59500 1.000 45.45000 ? 63  ASN A CG  1 
ATOM   460  O OD1 . ASN A 1 61  ? -37.57000 13.28900  -21.52600 1.000 44.58000 ? 63  ASN A OD1 1 
ATOM   461  N ND2 . ASN A 1 61  ? -38.93000 14.59500  -20.31100 1.000 41.57000 ? 63  ASN A ND2 1 
ATOM   462  N N   . HIS A 1 62  ? -39.40400 9.23500   -18.90800 1.000 42.72000 ? 64  HIS A N   1 
ATOM   463  C CA  . HIS A 1 62  ? -39.35600 8.23900   -17.84600 1.000 43.23000 ? 64  HIS A CA  1 
ATOM   464  C C   . HIS A 1 62  ? -38.93200 6.86300   -18.33500 1.000 41.22000 ? 64  HIS A C   1 
ATOM   465  O O   . HIS A 1 62  ? -38.79200 5.95800   -17.51100 1.000 40.50000 ? 64  HIS A O   1 
ATOM   466  C CB  . HIS A 1 62  ? -40.71300 8.15200   -17.13500 1.000 44.98000 ? 64  HIS A CB  1 
ATOM   467  C CG  . HIS A 1 62  ? -41.82300 7.63500   -17.99900 1.000 49.53000 ? 64  HIS A CG  1 
ATOM   468  N ND1 . HIS A 1 62  ? -42.14900 6.29700   -18.07500 1.000 48.40000 ? 64  HIS A ND1 1 
ATOM   469  C CD2 . HIS A 1 62  ? -42.69500 8.28200   -18.81000 1.000 51.68000 ? 64  HIS A CD2 1 
ATOM   470  C CE1 . HIS A 1 62  ? -43.16600 6.14000   -18.90800 1.000 49.16000 ? 64  HIS A CE1 1 
ATOM   471  N NE2 . HIS A 1 62  ? -43.51700 7.32800   -19.36300 1.000 51.41000 ? 64  HIS A NE2 1 
ATOM   472  N N   . ASN A 1 63  ? -38.71900 6.67100   -19.63800 1.000 40.16000 ? 65  ASN A N   1 
ATOM   473  C CA  . ASN A 1 63  ? -38.11600 5.42200   -20.10100 1.000 40.40000 ? 65  ASN A CA  1 
ATOM   474  C C   . ASN A 1 63  ? -36.62700 5.31800   -19.72300 1.000 38.77000 ? 65  ASN A C   1 
ATOM   475  O O   . ASN A 1 63  ? -36.05900 4.22000   -19.76500 1.000 37.08000 ? 65  ASN A O   1 
ATOM   476  C CB  . ASN A 1 63  ? -38.27800 5.29600   -21.62500 1.000 37.87000 ? 65  ASN A CB  1 
ATOM   477  C CG  . ASN A 1 63  ? -39.72700 5.07500   -22.06500 1.000 42.60000 ? 65  ASN A CG  1 
ATOM   478  O OD1 . ASN A 1 63  ? -40.23300 5.77900   -22.95200 1.000 42.39000 ? 65  ASN A OD1 1 
ATOM   479  N ND2 . ASN A 1 63  ? -40.38500 4.07500   -21.47900 1.000 42.08000 ? 65  ASN A ND2 1 
ATOM   480  N N   . PHE A 1 64  ? -35.98500 6.42500   -19.35100 1.000 38.37000 ? 66  PHE A N   1 
ATOM   481  C CA  . PHE A 1 64  ? -34.53800 6.46400   -19.10200 1.000 40.77000 ? 66  PHE A CA  1 
ATOM   482  C C   . PHE A 1 64  ? -34.23900 6.48100   -17.60100 1.000 40.89000 ? 66  PHE A C   1 
ATOM   483  O O   . PHE A 1 64  ? -34.42200 7.50900   -16.94200 1.000 40.30000 ? 66  PHE A O   1 
ATOM   484  C CB  . PHE A 1 64  ? -33.92100 7.69400   -19.75500 1.000 38.27000 ? 66  PHE A CB  1 
ATOM   485  C CG  . PHE A 1 64  ? -34.05700 7.73100   -21.24400 1.000 37.15000 ? 66  PHE A CG  1 
ATOM   486  C CD1 . PHE A 1 64  ? -33.26300 6.92900   -22.04100 1.000 37.03000 ? 66  PHE A CD1 1 
ATOM   487  C CD2 . PHE A 1 64  ? -34.97400 8.58000   -21.84600 1.000 37.38000 ? 66  PHE A CD2 1 
ATOM   488  C CE1 . PHE A 1 64  ? -33.36800 6.97900   -23.42700 1.000 41.84000 ? 66  PHE A CE1 1 
ATOM   489  C CE2 . PHE A 1 64  ? -35.09700 8.63500   -23.21100 1.000 38.47000 ? 66  PHE A CE2 1 
ATOM   490  C CZ  . PHE A 1 64  ? -34.29800 7.83300   -24.01500 1.000 40.72000 ? 66  PHE A CZ  1 
ATOM   491  N N   . LEU A 1 65  ? -33.71400 5.37600   -17.07700 1.000 39.27000 ? 67  LEU A N   1 
ATOM   492  C CA  . LEU A 1 65  ? -33.31300 5.28900   -15.67200 1.000 40.19000 ? 67  LEU A CA  1 
ATOM   493  C C   . LEU A 1 65  ? -31.83400 5.65900   -15.55300 1.000 41.16000 ? 67  LEU A C   1 
ATOM   494  O O   . LEU A 1 65  ? -30.96300 4.93900   -16.05500 1.000 36.84000 ? 67  LEU A O   1 
ATOM   495  C CB  . LEU A 1 65  ? -33.57900 3.88700   -15.12900 1.000 39.89000 ? 67  LEU A CB  1 
ATOM   496  C CG  . LEU A 1 65  ? -33.04100 3.50100   -13.74600 1.000 48.34000 ? 67  LEU A CG  1 
ATOM   497  C CD1 . LEU A 1 65  ? -33.52600 4.45000   -12.63500 1.000 45.83000 ? 67  LEU A CD1 1 
ATOM   498  C CD2 . LEU A 1 65  ? -33.39200 2.03900   -13.41700 1.000 47.16000 ? 67  LEU A CD2 1 
ATOM   499  N N   . VAL A 1 66  ? -31.55800 6.78500   -14.89700 1.000 37.93000 ? 68  VAL A N   1 
ATOM   500  C CA  . VAL A 1 66  ? -30.21100 7.29700   -14.68900 1.000 36.87000 ? 68  VAL A CA  1 
ATOM   501  C C   . VAL A 1 66  ? -29.92000 7.23900   -13.19500 1.000 42.58000 ? 68  VAL A C   1 
ATOM   502  O O   . VAL A 1 66  ? -30.66800 7.81600   -12.39700 1.000 39.43000 ? 68  VAL A O   1 
ATOM   503  C CB  . VAL A 1 66  ? -30.04900 8.73300   -15.20800 1.000 36.53000 ? 68  VAL A CB  1 
ATOM   504  C CG1 . VAL A 1 66  ? -28.59400 9.19300   -15.01300 1.000 37.26000 ? 68  VAL A CG1 1 
ATOM   505  C CG2 . VAL A 1 66  ? -30.45000 8.83400   -16.67200 1.000 36.07000 ? 68  VAL A CG2 1 
ATOM   506  N N   . GLN A 1 67  ? -28.81300 6.59200   -12.82400 1.000 37.26000 ? 69  GLN A N   1 
ATOM   507  C CA  . GLN A 1 67  ? -28.41000 6.41400   -11.43200 1.000 40.38000 ? 69  GLN A CA  1 
ATOM   508  C C   . GLN A 1 67  ? -26.99300 6.93400   -11.22400 1.000 43.38000 ? 69  GLN A C   1 
ATOM   509  O O   . GLN A 1 67  ? -26.04600 6.46900   -11.87800 1.000 36.18000 ? 69  GLN A O   1 
ATOM   510  C CB  . GLN A 1 67  ? -28.49800 4.94300   -11.02100 1.000 42.75000 ? 69  GLN A CB  1 
ATOM   511  C CG  . GLN A 1 67  ? -29.87900 4.33200   -11.20700 1.000 45.01000 ? 69  GLN A CG  1 
ATOM   512  C CD  . GLN A 1 67  ? -29.94800 2.89300   -10.72900 1.000 58.60000 ? 69  GLN A CD  1 
ATOM   513  O OE1 . GLN A 1 67  ? -29.78800 2.61200   -9.53300  1.000 63.42000 ? 69  GLN A OE1 1 
ATOM   514  N NE2 . GLN A 1 67  ? -30.17000 1.96600   -11.66500 1.000 51.13000 ? 69  GLN A NE2 1 
ATOM   515  N N   . ALA A 1 68  ? -26.85400 7.89100   -10.31100 1.000 43.69000 ? 70  ALA A N   1 
ATOM   516  C CA  . ALA A 1 68  ? -25.56200 8.38400   -9.84100  1.000 42.51000 ? 70  ALA A CA  1 
ATOM   517  C C   . ALA A 1 68  ? -25.34200 7.78400   -8.45200  1.000 49.77000 ? 70  ALA A C   1 
ATOM   518  O O   . ALA A 1 68  ? -25.83400 8.31400   -7.44700  1.000 49.80000 ? 70  ALA A O   1 
ATOM   519  C CB  . ALA A 1 68  ? -25.53600 9.91000   -9.81900  1.000 40.24000 ? 70  ALA A CB  1 
ATOM   520  N N   . GLY A 1 69  ? -24.61900 6.67100   -8.39900  1.000 50.22000 ? 71  GLY A N   1 
ATOM   521  C CA  . GLY A 1 69  ? -24.46300 5.97200   -7.13300  1.000 49.61000 ? 71  GLY A CA  1 
ATOM   522  C C   . GLY A 1 69  ? -25.79500 5.39300   -6.68300  1.000 51.53000 ? 71  GLY A C   1 
ATOM   523  O O   . GLY A 1 69  ? -26.41700 4.57600   -7.37500  1.000 53.03000 ? 71  GLY A O   1 
ATOM   524  N N   . ASN A 1 70  ? -26.25500 5.80800   -5.50200  1.000 53.02000 ? 72  ASN A N   1 
ATOM   525  C CA  . ASN A 1 70  ? -27.51600 5.32600   -4.95200  1.000 55.30000 ? 72  ASN A CA  1 
ATOM   526  C C   . ASN A 1 70  ? -28.69600 6.22200   -5.30000  1.000 54.48000 ? 72  ASN A C   1 
ATOM   527  O O   . ASN A 1 70  ? -29.82500 5.91300   -4.90700  1.000 59.76000 ? 72  ASN A O   1 
ATOM   528  C CB  . ASN A 1 70  ? -27.40600 5.18500   -3.42800  1.000 56.41000 ? 72  ASN A CB  1 
ATOM   529  N N   . VAL A 1 71  ? -28.47100 7.30400   -6.04300  1.000 49.94000 ? 73  VAL A N   1 
ATOM   530  C CA  . VAL A 1 71  ? -29.49200 8.30900   -6.30800  1.000 47.09000 ? 73  VAL A CA  1 
ATOM   531  C C   . VAL A 1 71  ? -30.00600 8.12900   -7.72800  1.000 47.07000 ? 73  VAL A C   1 
ATOM   532  O O   . VAL A 1 71  ? -29.22000 8.09400   -8.68300  1.000 44.05000 ? 73  VAL A O   1 
ATOM   533  C CB  . VAL A 1 71  ? -28.92900 9.72700   -6.10600  1.000 44.65000 ? 73  VAL A CB  1 
ATOM   534  C CG1 . VAL A 1 71  ? -30.01700 10.77000  -6.34300  1.000 44.12000 ? 73  VAL A CG1 1 
ATOM   535  C CG2 . VAL A 1 71  ? -28.33500 9.85900   -4.71500  1.000 51.08000 ? 73  VAL A CG2 1 
ATOM   536  N N   . GLN A 1 72  ? -31.32300 8.02200   -7.87900  1.000 44.81000 ? 74  GLN A N   1 
ATOM   537  C CA  . GLN A 1 72  ? -31.91800 8.08400   -9.20300  1.000 43.98000 ? 74  GLN A CA  1 
ATOM   538  C C   . GLN A 1 72  ? -32.03100 9.54400   -9.61000  1.000 45.32000 ? 74  GLN A C   1 
ATOM   539  O O   . GLN A 1 72  ? -32.55300 10.36800  -8.85100  1.000 46.78000 ? 74  GLN A O   1 
ATOM   540  C CB  . GLN A 1 72  ? -33.28700 7.41100   -9.22600  1.000 39.88000 ? 74  GLN A CB  1 
ATOM   541  N N   . LEU A 1 73  ? -31.58400 9.86300   -10.80900 1.000 41.33000 ? 75  LEU A N   1 
ATOM   542  C CA  . LEU A 1 73  ? -31.68900 11.18500  -11.36100 1.000 40.94000 ? 75  LEU A CA  1 
ATOM   543  C C   . LEU A 1 73  ? -32.93400 11.22500  -12.19500 1.000 44.29000 ? 75  LEU A C   1 
ATOM   544  O O   . LEU A 1 73  ? -33.32800 10.24500  -12.74700 1.000 48.77000 ? 75  LEU A O   1 
ATOM   545  C CB  . LEU A 1 73  ? -30.50500 11.56700  -12.20000 1.000 43.22000 ? 75  LEU A CB  1 
ATOM   546  C CG  . LEU A 1 73  ? -29.15400 11.64500  -11.53500 1.000 43.76000 ? 75  LEU A CG  1 
ATOM   547  C CD1 . LEU A 1 73  ? -28.08800 12.20900  -12.44400 1.000 35.57000 ? 75  LEU A CD1 1 
ATOM   548  C CD2 . LEU A 1 73  ? -29.26000 12.47200  -10.30000 1.000 41.64000 ? 75  LEU A CD2 1 
ATOM   549  N N   . ARG A 1 74  ? -33.55500 12.37100  -12.26700 1.000 42.51000 ? 76  ARG A N   1 
ATOM   550  C CA  . ARG A 1 74  ? -34.76900 12.50300  -13.00100 1.000 43.67000 ? 76  ARG A CA  1 
ATOM   551  C C   . ARG A 1 74  ? -34.54500 13.11100  -14.32300 1.000 38.08000 ? 76  ARG A C   1 
ATOM   552  O O   . ARG A 1 74  ? -34.07800 14.17900  -14.38800 1.000 42.40000 ? 76  ARG A O   1 
ATOM   553  C CB  . ARG A 1 74  ? -35.69500 13.40000  -12.22800 1.000 44.29000 ? 76  ARG A CB  1 
ATOM   554  C CG  . ARG A 1 74  ? -37.06400 13.48600  -12.79100 1.000 49.65000 ? 76  ARG A CG  1 
ATOM   555  C CD  . ARG A 1 74  ? -37.86400 14.54500  -12.07100 1.000 54.56000 ? 76  ARG A CD  1 
ATOM   556  N NE  . ARG A 1 74  ? -39.22600 14.53300  -12.48700 1.000 64.06000 ? 76  ARG A NE  1 
ATOM   557  C CZ  . ARG A 1 74  ? -39.95200 13.43000  -12.52500 1.000 69.82000 ? 76  ARG A CZ  1 
ATOM   558  N NH1 . ARG A 1 74  ? -39.41900 12.26900  -12.17400 1.000 66.34000 ? 76  ARG A NH1 1 
ATOM   559  N NH2 . ARG A 1 74  ? -41.21100 13.48300  -12.91200 1.000 70.55000 ? 76  ARG A NH2 1 
ATOM   560  N N   . VAL A 1 75  ? -34.89600 12.41100  -15.37100 1.000 39.13000 ? 77  VAL A N   1 
ATOM   561  C CA  . VAL A 1 75  ? -34.75500 12.93700  -16.70500 1.000 41.45000 ? 77  VAL A CA  1 
ATOM   562  C C   . VAL A 1 75  ? -35.91700 13.82500  -17.06500 1.000 42.40000 ? 77  VAL A C   1 
ATOM   563  O O   . VAL A 1 75  ? -36.99600 13.42900  -16.92800 1.000 40.38000 ? 77  VAL A O   1 
ATOM   564  C CB  . VAL A 1 75  ? -34.63800 11.81600  -17.73100 1.000 42.99000 ? 77  VAL A CB  1 
ATOM   565  C CG1 . VAL A 1 75  ? -34.54300 12.36600  -19.12200 1.000 39.41000 ? 77  VAL A CG1 1 
ATOM   566  C CG2 . VAL A 1 75  ? -33.42400 10.97900  -17.44600 1.000 40.74000 ? 77  VAL A CG2 1 
ATOM   567  N N   . ILE A 1 76  ? -35.64400 15.02600  -17.54000 1.000 43.50000 ? 78  ILE A N   1 
ATOM   568  C CA  . ILE A 1 76  ? -36.67500 15.97000  -17.93400 1.000 42.47000 ? 78  ILE A CA  1 
ATOM   569  C C   . ILE A 1 76  ? -36.57600 16.39000  -19.38800 1.000 47.46000 ? 78  ILE A C   1 
ATOM   570  O O   . ILE A 1 76  ? -37.30200 17.29100  -19.81700 1.000 44.92000 ? 78  ILE A O   1 
ATOM   571  C CB  . ILE A 1 76  ? -36.67700 17.22600  -17.03100 1.000 46.73000 ? 78  ILE A CB  1 
ATOM   572  C CG1 . ILE A 1 76  ? -35.44100 18.07900  -17.30400 1.000 47.38000 ? 78  ILE A CG1 1 
ATOM   573  C CG2 . ILE A 1 76  ? -36.76700 16.83700  -15.55700 1.000 46.72000 ? 78  ILE A CG2 1 
ATOM   574  C CD1 . ILE A 1 76  ? -35.40000 19.35800  -16.49100 1.000 48.41000 ? 78  ILE A CD1 1 
ATOM   575  N N   . GLY A 1 77  ? -35.68800 15.77600  -20.16800 1.000 42.88000 ? 79  GLY A N   1 
ATOM   576  C CA  . GLY A 1 77  ? -35.69500 15.97400  -21.60200 1.000 38.75000 ? 79  GLY A CA  1 
ATOM   577  C C   . GLY A 1 77  ? -34.64500 15.07400  -22.23600 1.000 44.21000 ? 79  GLY A C   1 
ATOM   578  O O   . GLY A 1 77  ? -33.78700 14.53000  -21.54700 1.000 37.63000 ? 79  GLY A O   1 
ATOM   579  N N   . HIS A 1 78  ? -34.75200 14.92800  -23.54800 1.000 43.88000 ? 80  HIS A N   1 
ATOM   580  C CA  . HIS A 1 78  ? -33.76100 14.12600  -24.25500 1.000 40.88000 ? 80  HIS A CA  1 
ATOM   581  C C   . HIS A 1 78  ? -33.70500 14.56000  -25.70200 1.000 44.56000 ? 80  HIS A C   1 
ATOM   582  O O   . HIS A 1 78  ? -34.69900 15.01600  -26.27700 1.000 37.27000 ? 80  HIS A O   1 
ATOM   583  C CB  . HIS A 1 78  ? -34.07500 12.63000  -24.18500 1.000 38.35000 ? 80  HIS A CB  1 
ATOM   584  C CG  . HIS A 1 78  ? -35.43000 12.27900  -24.70600 1.000 45.34000 ? 80  HIS A CG  1 
ATOM   585  N ND1 . HIS A 1 78  ? -36.58400 12.52600  -23.99600 1.000 49.06000 ? 80  HIS A ND1 1 
ATOM   586  C CD2 . HIS A 1 78  ? -35.82100 11.71700  -25.87600 1.000 45.71000 ? 80  HIS A CD2 1 
ATOM   587  C CE1 . HIS A 1 78  ? -37.63000 12.11800  -24.69700 1.000 48.33000 ? 80  HIS A CE1 1 
ATOM   588  N NE2 . HIS A 1 78  ? -37.19400 11.62100  -25.84100 1.000 47.86000 ? 80  HIS A NE2 1 
ATOM   589  N N   . SER A 1 79  ? -32.52900 14.39000  -26.28500 1.000 35.92000 ? 81  SER A N   1 
ATOM   590  C CA  . SER A 1 79  ? -32.32400 14.59800  -27.70600 1.000 35.99000 ? 81  SER A CA  1 
ATOM   591  C C   . SER A 1 79  ? -31.08700 13.80800  -28.09900 1.000 39.46000 ? 81  SER A C   1 
ATOM   592  O O   . SER A 1 79  ? -30.34900 13.29800  -27.25000 1.000 35.31000 ? 81  SER A O   1 
ATOM   593  C CB  . SER A 1 79  ? -32.16100 16.08000  -28.03800 1.000 38.30000 ? 81  SER A CB  1 
ATOM   594  O OG  . SER A 1 79  ? -30.98400 16.58300  -27.44300 1.000 40.56000 ? 81  SER A OG  1 
ATOM   595  N N   . MET A 1 80  ? -30.87400 13.71600  -29.39800 1.000 35.90000 ? 82  MET A N   1 
ATOM   596  C CA  . MET A 1 80  ? -29.78300 12.95400  -29.97300 1.000 33.98000 ? 82  MET A CA  1 
ATOM   597  C C   . MET A 1 80  ? -28.92300 13.89500  -30.80700 1.000 36.12000 ? 82  MET A C   1 
ATOM   598  O O   . MET A 1 80  ? -29.44300 14.72800  -31.55200 1.000 34.44000 ? 82  MET A O   1 
ATOM   599  C CB  . MET A 1 80  ? -30.36600 11.80100  -30.78700 1.000 36.91000 ? 82  MET A CB  1 
ATOM   600  C CG  . MET A 1 80  ? -29.40700 11.01600  -31.61700 1.000 37.20000 ? 82  MET A CG  1 
ATOM   601  S SD  . MET A 1 80  ? -30.22500 9.51800   -32.24000 1.000 36.62000 ? 82  MET A SD  1 
ATOM   602  C CE  . MET A 1 80  ? -31.32100 10.21600  -33.48800 1.000 37.75000 ? 82  MET A CE  1 
ATOM   603  N N   . GLN A 1 81  ? -27.60400 13.81500  -30.62200 1.000 34.37000 ? 83  GLN A N   1 
ATOM   604  C CA  . GLN A 1 81  ? -26.63900 14.58100  -31.41000 1.000 34.25000 ? 83  GLN A CA  1 
ATOM   605  C C   . GLN A 1 81  ? -25.65800 13.56900  -31.99300 1.000 34.76000 ? 83  GLN A C   1 
ATOM   606  O O   . GLN A 1 81  ? -24.83000 13.01400  -31.26600 1.000 30.61000 ? 83  GLN A O   1 
ATOM   607  C CB  . GLN A 1 81  ? -25.92100 15.63600  -30.57200 1.000 35.75000 ? 83  GLN A CB  1 
ATOM   608  C CG  . GLN A 1 81  ? -24.78800 16.34500  -31.32100 1.000 35.93000 ? 83  GLN A CG  1 
ATOM   609  C CD  . GLN A 1 81  ? -24.07600 17.40000  -30.48400 1.000 36.11000 ? 83  GLN A CD  1 
ATOM   610  O OE1 . GLN A 1 81  ? -24.19100 17.42900  -29.26000 1.000 36.05000 ? 83  GLN A OE1 1 
ATOM   611  N NE2 . GLN A 1 81  ? -23.37000 18.30100  -31.15100 1.000 39.88000 ? 83  GLN A NE2 1 
ATOM   612  N N   . ASN A 1 82  ? -25.78100 13.29700  -33.29100 1.000 32.38000 ? 84  ASN A N   1 
ATOM   613  C CA  . ASN A 1 82  ? -24.99700 12.26300  -33.96600 1.000 32.95000 ? 84  ASN A CA  1 
ATOM   614  C C   . ASN A 1 82  ? -25.22100 10.96700  -33.20600 1.000 34.88000 ? 84  ASN A C   1 
ATOM   615  O O   . ASN A 1 82  ? -26.39100 10.56800  -33.06800 1.000 32.42000 ? 84  ASN A O   1 
ATOM   616  C CB  . ASN A 1 82  ? -23.54700 12.74700  -34.09800 1.000 29.85000 ? 84  ASN A CB  1 
ATOM   617  C CG  . ASN A 1 82  ? -23.45100 14.03700  -34.87700 1.000 33.91000 ? 84  ASN A CG  1 
ATOM   618  O OD1 . ASN A 1 82  ? -23.85700 14.09000  -36.03800 1.000 39.96000 ? 84  ASN A OD1 1 
ATOM   619  N ND2 . ASN A 1 82  ? -22.95900 15.09500  -34.24100 1.000 31.33000 ? 84  ASN A ND2 1 
ATOM   620  N N   . CYS A 1 83  ? -24.18600 10.29500  -32.67700 1.000 28.74000 ? 85  CYS A N   1 
ATOM   621  C CA  . CYS A 1 83  ? -24.35500 8.99800   -32.03500 1.000 28.23000 ? 85  CYS A CA  1 
ATOM   622  C C   . CYS A 1 83  ? -24.37600 9.06300   -30.50600 1.000 30.60000 ? 85  CYS A C   1 
ATOM   623  O O   . CYS A 1 83  ? -24.25000 8.02000   -29.85400 1.000 27.69000 ? 85  CYS A O   1 
ATOM   624  C CB  . CYS A 1 83  ? -23.25500 8.03500   -32.48400 1.000 31.54000 ? 85  CYS A CB  1 
ATOM   625  S SG  . CYS A 1 83  ? -23.14900 7.81100   -34.30500 1.000 47.75000 ? 85  CYS A SG  1 
ATOM   626  N N   . VAL A 1 84  ? -24.49400 10.24800  -29.91200 1.000 28.47000 ? 86  VAL A N   1 
ATOM   627  C CA  . VAL A 1 84  ? -24.60500 10.35700  -28.45700 1.000 31.38000 ? 86  VAL A CA  1 
ATOM   628  C C   . VAL A 1 84  ? -26.02000 10.79800  -28.12200 1.000 32.20000 ? 86  VAL A C   1 
ATOM   629  O O   . VAL A 1 84  ? -26.59700 11.64700  -28.80400 1.000 32.59000 ? 86  VAL A O   1 
ATOM   630  C CB  . VAL A 1 84  ? -23.57400 11.31000  -27.81700 1.000 32.93000 ? 86  VAL A CB  1 
ATOM   631  C CG1 . VAL A 1 84  ? -22.14400 10.71000  -27.89300 1.000 30.97000 ? 86  VAL A CG1 1 
ATOM   632  C CG2 . VAL A 1 84  ? -23.64000 12.69800  -28.44500 1.000 32.65000 ? 86  VAL A CG2 1 
ATOM   633  N N   . LEU A 1 85  ? -26.58700 10.17300  -27.10000 1.000 32.69000 ? 87  LEU A N   1 
ATOM   634  C CA  . LEU A 1 85  ? -27.81600 10.63900  -26.48700 1.000 33.86000 ? 87  LEU A CA  1 
ATOM   635  C C   . LEU A 1 85  ? -27.48100 11.66300  -25.40900 1.000 38.43000 ? 87  LEU A C   1 
ATOM   636  O O   . LEU A 1 85  ? -26.45200 11.55400  -24.72000 1.000 29.25000 ? 87  LEU A O   1 
ATOM   637  C CB  . LEU A 1 85  ? -28.56400 9.44400   -25.90800 1.000 34.66000 ? 87  LEU A CB  1 
ATOM   638  C CG  . LEU A 1 85  ? -29.92000 9.54400   -25.21900 1.000 38.43000 ? 87  LEU A CG  1 
ATOM   639  C CD1 . LEU A 1 85  ? -30.97900 10.13600  -26.14700 1.000 40.74000 ? 87  LEU A CD1 1 
ATOM   640  C CD2 . LEU A 1 85  ? -30.30200 8.13700   -24.81100 1.000 40.19000 ? 87  LEU A CD2 1 
ATOM   641  N N   . LYS A 1 86  ? -28.31800 12.69500  -25.30500 1.000 32.24000 ? 88  LYS A N   1 
ATOM   642  C CA  . LYS A 1 86  ? -28.13100 13.76400  -24.32700 1.000 33.54000 ? 88  LYS A CA  1 
ATOM   643  C C   . LYS A 1 86  ? -29.39600 13.83600  -23.49000 1.000 37.29000 ? 88  LYS A C   1 
ATOM   644  O O   . LYS A 1 86  ? -30.47100 14.17000  -24.00900 1.000 35.55000 ? 88  LYS A O   1 
ATOM   645  C CB  . LYS A 1 86  ? -27.85300 15.10100  -25.00000 1.000 34.58000 ? 88  LYS A CB  1 
ATOM   646  C CG  . LYS A 1 86  ? -26.41400 15.32400  -25.33900 1.000 37.13000 ? 88  LYS A CG  1 
ATOM   647  C CD  . LYS A 1 86  ? -26.31600 16.06100  -26.61800 1.000 39.74000 ? 88  LYS A CD  1 
ATOM   648  C CE  . LYS A 1 86  ? -26.27600 17.53700  -26.39200 1.000 38.86000 ? 88  LYS A CE  1 
ATOM   649  N NZ  . LYS A 1 86  ? -26.59900 18.21600  -27.67500 1.000 33.37000 ? 88  LYS A NZ  1 
ATOM   650  N N   . LEU A 1 87  ? -29.26700 13.52200  -22.20700 1.000 32.79000 ? 89  LEU A N   1 
ATOM   651  C CA  . LEU A 1 87  ? -30.38600 13.41000  -21.28000 1.000 37.06000 ? 89  LEU A CA  1 
ATOM   652  C C   . LEU A 1 87  ? -30.34700 14.59400  -20.32600 1.000 38.91000 ? 89  LEU A C   1 
ATOM   653  O O   . LEU A 1 87  ? -29.42500 14.71100  -19.51200 1.000 36.73000 ? 89  LEU A O   1 
ATOM   654  C CB  . LEU A 1 87  ? -30.31600 12.09000  -20.51800 1.000 33.27000 ? 89  LEU A CB  1 
ATOM   655  C CG  . LEU A 1 87  ? -30.37900 10.83500  -21.38300 1.000 31.72000 ? 89  LEU A CG  1 
ATOM   656  C CD1 . LEU A 1 87  ? -30.36600 9.62000   -20.50000 1.000 30.44000 ? 89  LEU A CD1 1 
ATOM   657  C CD2 . LEU A 1 87  ? -31.63400 10.84700  -22.22300 1.000 37.35000 ? 89  LEU A CD2 1 
ATOM   658  N N   . LYS A 1 88  ? -31.33600 15.47800  -20.42400 1.000 42.27000 ? 90  LYS A N   1 
ATOM   659  C CA  . LYS A 1 88  ? -31.43200 16.57000  -19.46700 1.000 44.68000 ? 90  LYS A CA  1 
ATOM   660  C C   . LYS A 1 88  ? -31.99000 16.03800  -18.14900 1.000 41.30000 ? 90  LYS A C   1 
ATOM   661  O O   . LYS A 1 88  ? -32.99400 15.32300  -18.14300 1.000 42.42000 ? 90  LYS A O   1 
ATOM   662  C CB  . LYS A 1 88  ? -32.30600 17.69500  -20.01100 1.000 45.01000 ? 90  LYS A CB  1 
ATOM   663  C CG  . LYS A 1 88  ? -32.05100 19.01600  -19.30600 1.000 51.30000 ? 90  LYS A CG  1 
ATOM   664  C CD  . LYS A 1 88  ? -32.72300 20.17100  -20.02800 1.000 54.93000 ? 90  LYS A CD  1 
ATOM   665  C CE  . LYS A 1 88  ? -32.63300 21.44800  -19.20800 1.000 57.50000 ? 90  LYS A CE  1 
ATOM   666  N NZ  . LYS A 1 88  ? -33.33300 22.57900  -19.87300 1.000 60.68000 ? 90  LYS A NZ  1 
ATOM   667  N N   . VAL A 1 89  ? -31.32600 16.35400  -17.03500 1.000 41.09000 ? 91  VAL A N   1 
ATOM   668  C CA  . VAL A 1 89  ? -31.78500 15.88700  -15.73100 1.000 42.73000 ? 91  VAL A CA  1 
ATOM   669  C C   . VAL A 1 89  ? -32.14900 17.07300  -14.84100 1.000 46.26000 ? 91  VAL A C   1 
ATOM   670  O O   . VAL A 1 89  ? -31.80600 18.22700  -15.11800 1.000 43.89000 ? 91  VAL A O   1 
ATOM   671  C CB  . VAL A 1 89  ? -30.76200 14.97700  -15.01300 1.000 40.74000 ? 91  VAL A CB  1 
ATOM   672  C CG1 . VAL A 1 89  ? -30.84100 13.55000  -15.55100 1.000 41.90000 ? 91  VAL A CG1 1 
ATOM   673  C CG2 . VAL A 1 89  ? -29.36700 15.55400  -15.11000 1.000 40.34000 ? 91  VAL A CG2 1 
ATOM   674  N N   . ASP A 1 90  ? -32.84400 16.73200  -13.73600 1.000 46.76000 ? 92  ASP A N   1 
ATOM   675  C CA  . ASP A 1 90  ? -33.25300 17.66000  -12.67600 1.000 50.27000 ? 92  ASP A CA  1 
ATOM   676  C C   . ASP A 1 90  ? -32.11800 18.50600  -12.13000 1.000 51.45000 ? 92  ASP A C   1 
ATOM   677  O O   . ASP A 1 90  ? -32.32300 19.65700  -11.72600 1.000 52.15000 ? 92  ASP A O   1 
ATOM   678  C CB  . ASP A 1 90  ? -33.80700 16.86500  -11.49400 1.000 49.41000 ? 92  ASP A CB  1 
ATOM   679  C CG  . ASP A 1 90  ? -35.28400 16.87900  -11.44100 1.000 54.78000 ? 92  ASP A CG  1 
ATOM   680  O OD1 . ASP A 1 90  ? -35.87600 17.43800  -12.38900 1.000 60.67000 ? 92  ASP A OD1 1 
ATOM   681  O OD2 . ASP A 1 90  ? -35.84700 16.35400  -10.45200 1.000 57.27000 ? 92  ASP A OD2 1 
ATOM   682  N N   . THR A 1 91  ? -30.94100 17.91800  -12.01200 1.000 46.70000 ? 93  THR A N   1 
ATOM   683  C CA  . THR A 1 91  ? -29.94100 18.35800  -11.05200 1.000 44.01000 ? 93  THR A CA  1 
ATOM   684  C C   . THR A 1 91  ? -28.62600 18.52500  -11.78300 1.000 43.52000 ? 93  THR A C   1 
ATOM   685  O O   . THR A 1 91  ? -28.18900 17.60400  -12.47600 1.000 43.43000 ? 93  THR A O   1 
ATOM   686  C CB  . THR A 1 91  ? -29.80300 17.33000  -9.93000  1.000 46.51000 ? 93  THR A CB  1 
ATOM   687  O OG1 . THR A 1 91  ? -31.08600 17.11500  -9.33200  1.000 46.10000 ? 93  THR A OG1 1 
ATOM   688  C CG2 . THR A 1 91  ? -28.78200 17.78400  -8.86800  1.000 46.95000 ? 93  THR A CG2 1 
ATOM   689  N N   . ALA A 1 92  ? -28.03700 19.70700  -11.67100 1.000 38.63000 ? 94  ALA A N   1 
ATOM   690  C CA  . ALA A 1 92  ? -26.68200 19.90100  -12.15200 1.000 42.84000 ? 94  ALA A CA  1 
ATOM   691  C C   . ALA A 1 92  ? -25.72900 19.09600  -11.27600 1.000 43.53000 ? 94  ALA A C   1 
ATOM   692  O O   . ALA A 1 92  ? -25.87800 19.06100  -10.04900 1.000 41.17000 ? 94  ALA A O   1 
ATOM   693  C CB  . ALA A 1 92  ? -26.32500 21.38400  -12.13400 1.000 43.45000 ? 94  ALA A CB  1 
ATOM   694  N N   . ASN A 1 93  ? -24.77100 18.41200  -11.90400 1.000 39.24000 ? 95  ASN A N   1 
ATOM   695  C CA  . ASN A 1 93  ? -23.84200 17.59600  -11.12100 1.000 36.42000 ? 95  ASN A CA  1 
ATOM   696  C C   . ASN A 1 93  ? -23.04200 18.51200  -10.19500 1.000 37.09000 ? 95  ASN A C   1 
ATOM   697  O O   . ASN A 1 93  ? -22.26800 19.34400  -10.68800 1.000 39.96000 ? 95  ASN A O   1 
ATOM   698  C CB  . ASN A 1 93  ? -22.89400 16.78900  -12.03100 1.000 37.14000 ? 95  ASN A CB  1 
ATOM   699  C CG  . ASN A 1 93  ? -21.98400 15.82500  -11.23600 1.000 36.66000 ? 95  ASN A CG  1 
ATOM   700  O OD1 . ASN A 1 93  ? -22.06000 15.74000  -10.00500 1.000 38.09000 ? 95  ASN A OD1 1 
ATOM   701  N ND2 . ASN A 1 93  ? -21.13700 15.10500  -11.93800 1.000 31.03000 ? 95  ASN A ND2 1 
ATOM   702  N N   . PRO A 1 94  ? -23.19700 18.39900  -8.87500  1.000 36.40000 ? 96  PRO A N   1 
ATOM   703  C CA  . PRO A 1 94  ? -22.37200 19.22900  -7.98400  1.000 38.08000 ? 96  PRO A CA  1 
ATOM   704  C C   . PRO A 1 94  ? -20.87300 19.02000  -8.18200  1.000 41.08000 ? 96  PRO A C   1 
ATOM   705  O O   . PRO A 1 94  ? -20.09200 19.94500  -7.92300  1.000 40.38000 ? 96  PRO A O   1 
ATOM   706  C CB  . PRO A 1 94  ? -22.82800 18.78800  -6.58500  1.000 42.42000 ? 96  PRO A CB  1 
ATOM   707  C CG  . PRO A 1 94  ? -23.36300 17.41700  -6.78100  1.000 37.92000 ? 96  PRO A CG  1 
ATOM   708  C CD  . PRO A 1 94  ? -23.97900 17.40000  -8.13100  1.000 37.56000 ? 96  PRO A CD  1 
ATOM   709  N N   . LYS A 1 95  ? -20.44900 17.85600  -8.67200  1.000 38.77000 ? 97  LYS A N   1 
ATOM   710  C CA  . LYS A 1 95  ? -19.03800 17.53600  -8.85000  1.000 37.46000 ? 97  LYS A CA  1 
ATOM   711  C C   . LYS A 1 95  ? -18.53500 17.82900  -10.26100 1.000 40.84000 ? 97  LYS A C   1 
ATOM   712  O O   . LYS A 1 95  ? -17.44400 17.38100  -10.61900 1.000 38.31000 ? 97  LYS A O   1 
ATOM   713  C CB  . LYS A 1 95  ? -18.78300 16.06300  -8.51900  1.000 37.74000 ? 97  LYS A CB  1 
ATOM   714  C CG  . LYS A 1 95  ? -19.20400 15.63200  -7.11000  1.000 43.30000 ? 97  LYS A CG  1 
ATOM   715  C CD  . LYS A 1 95  ? -18.77600 14.19300  -6.84700  1.000 43.40000 ? 97  LYS A CD  1 
ATOM   716  C CE  . LYS A 1 95  ? -19.12400 13.73800  -5.44400  1.000 48.96000 ? 97  LYS A CE  1 
ATOM   717  N NZ  . LYS A 1 95  ? -18.79700 12.29100  -5.29100  1.000 50.32000 ? 97  LYS A NZ  1 
ATOM   718  N N   . THR A 1 96  ? -19.30000 18.55400  -11.06400 1.000 37.97000 ? 98  THR A N   1 
ATOM   719  C CA  . THR A 1 96  ? -18.87700 18.88100  -12.41200 1.000 36.69000 ? 98  THR A CA  1 
ATOM   720  C C   . THR A 1 96  ? -17.56300 19.63600  -12.36700 1.000 38.39000 ? 98  THR A C   1 
ATOM   721  O O   . THR A 1 96  ? -17.47900 20.67600  -11.70100 1.000 39.90000 ? 98  THR A O   1 
ATOM   722  C CB  . THR A 1 96  ? -19.93600 19.72500  -13.12500 1.000 36.89000 ? 98  THR A CB  1 
ATOM   723  O OG1 . THR A 1 96  ? -21.18500 19.03000  -13.12200 1.000 36.59000 ? 98  THR A OG1 1 
ATOM   724  C CG2 . THR A 1 96  ? -19.53000 20.00300  -14.56100 1.000 36.90000 ? 98  THR A CG2 1 
ATOM   725  N N   . PRO A 1 97  ? -16.51400 19.17300  -13.03600 1.000 35.94000 ? 99  PRO A N   1 
ATOM   726  C CA  . PRO A 1 97  ? -15.26800 19.92000  -13.06500 1.000 36.42000 ? 99  PRO A CA  1 
ATOM   727  C C   . PRO A 1 97  ? -15.32500 20.97800  -14.15600 1.000 37.88000 ? 99  PRO A C   1 
ATOM   728  O O   . PRO A 1 97  ? -16.24200 21.00500  -14.97600 1.000 39.83000 ? 99  PRO A O   1 
ATOM   729  C CB  . PRO A 1 97  ? -14.23200 18.84400  -13.40100 1.000 36.63000 ? 99  PRO A CB  1 
ATOM   730  C CG  . PRO A 1 97  ? -14.97900 17.94100  -14.33400 1.000 33.94000 ? 99  PRO A CG  1 
ATOM   731  C CD  . PRO A 1 97  ? -16.40400 17.89800  -13.77000 1.000 35.22000 ? 99  PRO A CD  1 
ATOM   732  N N   . LYS A 1 98  ? -14.32000 21.85200  -14.15300 1.000 36.47000 ? 100 LYS A N   1 
ATOM   733  C CA  . LYS A 1 98  ? -14.02800 22.64200  -15.33500 1.000 41.40000 ? 100 LYS A CA  1 
ATOM   734  C C   . LYS A 1 98  ? -13.72200 21.69700  -16.49400 1.000 41.46000 ? 100 LYS A C   1 
ATOM   735  O O   . LYS A 1 98  ? -12.89500 20.78800  -16.36200 1.000 38.73000 ? 100 LYS A O   1 
ATOM   736  C CB  . LYS A 1 98  ? -12.84800 23.57500  -15.06900 1.000 35.81000 ? 100 LYS A CB  1 
ATOM   737  N N   . TYR A 1 99  ? -14.40900 21.88600  -17.62000 1.000 36.89000 ? 101 TYR A N   1 
ATOM   738  C CA  . TYR A 1 99  ? -14.28900 20.92100  -18.70300 1.000 37.06000 ? 101 TYR A CA  1 
ATOM   739  C C   . TYR A 1 99  ? -14.55100 21.58100  -20.04800 1.000 38.65000 ? 101 TYR A C   1 
ATOM   740  O O   . TYR A 1 99  ? -15.16800 22.64400  -20.13200 1.000 39.43000 ? 101 TYR A O   1 
ATOM   741  C CB  . TYR A 1 99  ? -15.25000 19.74100  -18.50800 1.000 35.58000 ? 101 TYR A CB  1 
ATOM   742  C CG  . TYR A 1 99  ? -16.70100 20.06200  -18.83700 1.000 36.96000 ? 101 TYR A CG  1 
ATOM   743  C CD1 . TYR A 1 99  ? -17.54200 20.59900  -17.87700 1.000 39.53000 ? 101 TYR A CD1 1 
ATOM   744  C CD2 . TYR A 1 99  ? -17.22100 19.83200  -20.10400 1.000 35.24000 ? 101 TYR A CD2 1 
ATOM   745  C CE1 . TYR A 1 99  ? -18.88000 20.89400  -18.16300 1.000 39.69000 ? 101 TYR A CE1 1 
ATOM   746  C CE2 . TYR A 1 99  ? -18.54700 20.13100  -20.40700 1.000 35.29000 ? 101 TYR A CE2 1 
ATOM   747  C CZ  . TYR A 1 99  ? -19.36900 20.66300  -19.43400 1.000 40.52000 ? 101 TYR A CZ  1 
ATOM   748  O OH  . TYR A 1 99  ? -20.68800 20.95700  -19.70700 1.000 46.64000 ? 101 TYR A OH  1 
ATOM   749  N N   . LYS A 1 100 ? -14.17600 20.88400  -21.09300 1.000 37.87000 ? 102 LYS A N   1 
ATOM   750  C CA  . LYS A 1 100 ? -14.42600 21.20500  -22.46800 1.000 37.39000 ? 102 LYS A CA  1 
ATOM   751  C C   . LYS A 1 100 ? -14.43300 19.93700  -23.27700 1.000 37.20000 ? 102 LYS A C   1 
ATOM   752  O O   . LYS A 1 100 ? -13.87300 18.99600  -22.87200 1.000 31.60000 ? 102 LYS A O   1 
ATOM   753  C CB  . LYS A 1 100 ? -13.39900 22.15700  -23.05800 1.000 38.97000 ? 102 LYS A CB  1 
ATOM   754  C CG  . LYS A 1 100 ? -12.01700 21.59400  -23.12900 1.000 44.97000 ? 102 LYS A CG  1 
ATOM   755  C CD  . LYS A 1 100 ? -10.98800 22.41100  -23.86100 1.000 51.58000 ? 102 LYS A CD  1 
ATOM   756  C CE  . LYS A 1 100 ? -10.47800 23.58900  -23.08200 1.000 57.33000 ? 102 LYS A CE  1 
ATOM   757  N NZ  . LYS A 1 100 ? -9.56200  23.24300  -21.98100 1.000 58.42000 ? 102 LYS A NZ  1 
ATOM   758  N N   . PHE A 1 101 ? -15.10700 19.94900  -24.41100 1.000 36.39000 ? 103 PHE A N   1 
ATOM   759  C CA  . PHE A 1 101 ? -15.08000 18.85500  -25.37700 1.000 36.49000 ? 103 PHE A CA  1 
ATOM   760  C C   . PHE A 1 101 ? -14.10000 19.20300  -26.49100 1.000 39.77000 ? 103 PHE A C   1 
ATOM   761  O O   . PHE A 1 101 ? -14.10400 20.33000  -26.99900 1.000 39.72000 ? 103 PHE A O   1 
ATOM   762  C CB  . PHE A 1 101 ? -16.46400 18.59000  -25.97600 1.000 34.41000 ? 103 PHE A CB  1 
ATOM   763  C CG  . PHE A 1 101 ? -17.50600 18.13500  -24.97300 1.000 34.17000 ? 103 PHE A CG  1 
ATOM   764  C CD1 . PHE A 1 101 ? -17.13600 17.65600  -23.72800 1.000 32.87000 ? 103 PHE A CD1 1 
ATOM   765  C CD2 . PHE A 1 101 ? -18.86600 18.17400  -25.29900 1.000 30.42000 ? 103 PHE A CD2 1 
ATOM   766  C CE1 . PHE A 1 101 ? -18.10400 17.22300  -22.80400 1.000 31.38000 ? 103 PHE A CE1 1 
ATOM   767  C CE2 . PHE A 1 101 ? -19.83800 17.75200  -24.38300 1.000 31.57000 ? 103 PHE A CE2 1 
ATOM   768  C CZ  . PHE A 1 101 ? -19.46100 17.26900  -23.13800 1.000 31.96000 ? 103 PHE A CZ  1 
ATOM   769  N N   . VAL A 1 102 ? -13.27600 18.25000  -26.86900 1.000 35.57000 ? 104 VAL A N   1 
ATOM   770  C CA  . VAL A 1 102 ? -12.32800 18.40800  -27.93100 1.000 35.25000 ? 104 VAL A CA  1 
ATOM   771  C C   . VAL A 1 102 ? -12.25400 17.18700  -28.81300 1.000 35.05000 ? 104 VAL A C   1 
ATOM   772  O O   . VAL A 1 102 ? -12.41900 16.13000  -28.35500 1.000 37.78000 ? 104 VAL A O   1 
ATOM   773  C CB  . VAL A 1 102 ? -10.92000 18.69700  -27.42600 1.000 37.91000 ? 104 VAL A CB  1 
ATOM   774  C CG1 . VAL A 1 102 ? -10.86100 19.89400  -26.56300 1.000 38.69000 ? 104 VAL A CG1 1 
ATOM   775  C CG2 . VAL A 1 102 ? -10.37000 17.53800  -26.68800 1.000 39.66000 ? 104 VAL A CG2 1 
ATOM   776  N N   . ARG A 1 103 ? -11.96800 17.35200  -30.07500 1.000 33.30000 ? 105 ARG A N   1 
ATOM   777  C CA  . ARG A 1 103 ? -11.80200 16.23400  -30.96600 1.000 33.48000 ? 105 ARG A CA  1 
ATOM   778  C C   . ARG A 1 103 ? -10.33400 16.08500  -31.20500 1.000 34.14000 ? 105 ARG A C   1 
ATOM   779  O O   . ARG A 1 103 ? -9.67700  17.01600  -31.49700 1.000 34.62000 ? 105 ARG A O   1 
ATOM   780  C CB  . ARG A 1 103 ? -12.56900 16.39200  -32.24900 1.000 33.22000 ? 105 ARG A CB  1 
ATOM   781  C CG  . ARG A 1 103 ? -12.38300 15.25800  -33.17900 1.000 33.61000 ? 105 ARG A CG  1 
ATOM   782  C CD  . ARG A 1 103 ? -13.39400 15.27100  -34.26500 1.000 35.59000 ? 105 ARG A CD  1 
ATOM   783  N NE  . ARG A 1 103 ? -13.23300 14.19500  -35.18400 1.000 31.58000 ? 105 ARG A NE  1 
ATOM   784  C CZ  . ARG A 1 103 ? -13.93400 13.10800  -35.17300 1.000 34.07000 ? 105 ARG A CZ  1 
ATOM   785  N NH1 . ARG A 1 103 ? -14.85000 12.94700  -34.30200 1.000 31.19000 ? 105 ARG A NH1 1 
ATOM   786  N NH2 . ARG A 1 103 ? -13.71000 12.19500  -36.04400 1.000 32.52000 ? 105 ARG A NH2 1 
ATOM   787  N N   . ILE A 1 104 ? -9.83000  14.90100  -31.04200 1.000 32.54000 ? 106 ILE A N   1 
ATOM   788  C CA  . ILE A 1 104 ? -8.43600  14.63000  -31.23600 1.000 36.26000 ? 106 ILE A CA  1 
ATOM   789  C C   . ILE A 1 104 ? -8.09500  13.95900  -32.55800 1.000 37.97000 ? 106 ILE A C   1 
ATOM   790  O O   . ILE A 1 104 ? -8.92800  13.49500  -33.21200 1.000 33.50000 ? 106 ILE A O   1 
ATOM   791  C CB  . ILE A 1 104 ? -7.85900  13.71700  -30.18000 1.000 35.68000 ? 106 ILE A CB  1 
ATOM   792  C CG1 . ILE A 1 104 ? -8.62400  12.43600  -30.12900 1.000 32.12000 ? 106 ILE A CG1 1 
ATOM   793  C CG2 . ILE A 1 104 ? -7.68300  14.41600  -28.87500 1.000 32.49000 ? 106 ILE A CG2 1 
ATOM   794  C CD1 . ILE A 1 104 ? -7.98400  11.44500  -29.24500 1.000 35.75000 ? 106 ILE A CD1 1 
ATOM   795  N N   . GLN A 1 105 ? -6.83300  13.91100  -32.88100 1.000 33.42000 ? 107 GLN A N   1 
ATOM   796  C CA  . GLN A 1 105 ? -6.33300  13.30100  -34.08200 1.000 38.30000 ? 107 GLN A CA  1 
ATOM   797  C C   . GLN A 1 105 ? -5.46800  12.09600  -33.80600 1.000 34.96000 ? 107 GLN A C   1 
ATOM   798  O O   . GLN A 1 105 ? -4.94200  12.00400  -32.76300 1.000 32.12000 ? 107 GLN A O   1 
ATOM   799  C CB  . GLN A 1 105 ? -5.48600  14.31300  -34.76900 1.000 40.22000 ? 107 GLN A CB  1 
ATOM   800  C CG  . GLN A 1 105 ? -6.20600  15.59000  -35.01300 1.000 44.33000 ? 107 GLN A CG  1 
ATOM   801  C CD  . GLN A 1 105 ? -7.08000  15.51000  -36.20500 1.000 48.33000 ? 107 GLN A CD  1 
ATOM   802  O OE1 . GLN A 1 105 ? -8.27100  15.53600  -36.11800 1.000 53.53000 ? 107 GLN A OE1 1 
ATOM   803  N NE2 . GLN A 1 105 ? -6.47200  15.39000  -37.33200 1.000 55.90000 ? 107 GLN A NE2 1 
ATOM   804  N N   . PRO A 1 106 ? -5.34100  11.19000  -34.75900 1.000 34.39000 ? 108 PRO A N   1 
ATOM   805  C CA  . PRO A 1 106 ? -4.45600  10.03200  -34.58200 1.000 32.32000 ? 108 PRO A CA  1 
ATOM   806  C C   . PRO A 1 106 ? -3.05700  10.44200  -34.16000 1.000 33.98000 ? 108 PRO A C   1 
ATOM   807  O O   . PRO A 1 106 ? -2.49400  11.41200  -34.67100 1.000 32.63000 ? 108 PRO A O   1 
ATOM   808  C CB  . PRO A 1 106 ? -4.43700  9.38800   -35.97200 1.000 36.22000 ? 108 PRO A CB  1 
ATOM   809  C CG  . PRO A 1 106 ? -5.68500  9.79600   -36.58900 1.000 35.39000 ? 108 PRO A CG  1 
ATOM   810  C CD  . PRO A 1 106 ? -6.03500  11.15400  -36.05700 1.000 38.71000 ? 108 PRO A CD  1 
ATOM   811  N N   . GLY A 1 107 ? -2.49100  9.67600   -33.22400 1.000 31.13000 ? 109 GLY A N   1 
ATOM   812  C CA  . GLY A 1 107 ? -1.24500  10.01000  -32.57700 1.000 31.80000 ? 109 GLY A CA  1 
ATOM   813  C C   . GLY A 1 107 ? -1.41200  10.69900  -31.23900 1.000 34.17000 ? 109 GLY A C   1 
ATOM   814  O O   . GLY A 1 107 ? -0.48400  10.66900  -30.42000 1.000 33.62000 ? 109 GLY A O   1 
ATOM   815  N N   . GLN A 1 108 ? -2.53500  11.30900  -30.99400 1.000 30.11000 ? 110 GLN A N   1 
ATOM   816  C CA  . GLN A 1 108 ? -2.72200  11.92500  -29.73600 1.000 29.37000 ? 110 GLN A CA  1 
ATOM   817  C C   . GLN A 1 108 ? -3.00000  10.90700  -28.62800 1.000 31.30000 ? 110 GLN A C   1 
ATOM   818  O O   . GLN A 1 108 ? -3.49700  9.87200   -28.86800 1.000 29.18000 ? 110 GLN A O   1 
ATOM   819  C CB  . GLN A 1 108 ? -3.76400  12.98300  -29.82700 1.000 31.48000 ? 110 GLN A CB  1 
ATOM   820  C CG  . GLN A 1 108 ? -4.03000  13.68700  -28.55900 1.000 35.22000 ? 110 GLN A CG  1 
ATOM   821  C CD  . GLN A 1 108 ? -2.87100  14.53700  -28.13700 1.000 44.88000 ? 110 GLN A CD  1 
ATOM   822  O OE1 . GLN A 1 108 ? -2.11500  14.17900  -27.27800 1.000 39.55000 ? 110 GLN A OE1 1 
ATOM   823  N NE2 . GLN A 1 108 ? -2.73800  15.66300  -28.76200 1.000 42.07000 ? 110 GLN A NE2 1 
ATOM   824  N N   . THR A 1 109 ? -2.62000  11.25700  -27.43100 1.000 29.49000 ? 111 THR A N   1 
ATOM   825  C CA  . THR A 1 109 ? -2.76700  10.46300  -26.25000 1.000 28.86000 ? 111 THR A CA  1 
ATOM   826  C C   . THR A 1 109 ? -3.79700  11.01000  -25.28700 1.000 28.46000 ? 111 THR A C   1 
ATOM   827  O O   . THR A 1 109 ? -4.08700  12.14600  -25.27800 1.000 29.29000 ? 111 THR A O   1 
ATOM   828  C CB  . THR A 1 109 ? -1.44900  10.29400  -25.49400 1.000 32.23000 ? 111 THR A CB  1 
ATOM   829  O OG1 . THR A 1 109 ? -0.90800  11.54700  -25.16300 1.000 30.91000 ? 111 THR A OG1 1 
ATOM   830  C CG2 . THR A 1 109 ? -0.50000  9.59100   -26.29600 1.000 33.63000 ? 111 THR A CG2 1 
ATOM   831  N N   . PHE A 1 110 ? -4.33500  10.11900  -24.50600 1.000 25.55000 ? 112 PHE A N   1 
ATOM   832  C CA  . PHE A 1 110 ? -5.33300  10.38600  -23.51600 1.000 28.28000 ? 112 PHE A CA  1 
ATOM   833  C C   . PHE A 1 110 ? -5.50500  9.24700   -22.52800 1.000 29.05000 ? 112 PHE A C   1 
ATOM   834  O O   . PHE A 1 110 ? -5.08900  8.19800   -22.76700 1.000 26.60000 ? 112 PHE A O   1 
ATOM   835  C CB  . PHE A 1 110 ? -6.67800  10.75800  -24.14400 1.000 27.64000 ? 112 PHE A CB  1 
ATOM   836  C CG  . PHE A 1 110 ? -7.26800  9.70700   -25.02500 1.000 26.59000 ? 112 PHE A CG  1 
ATOM   837  C CD1 . PHE A 1 110 ? -6.93500  9.63200   -26.33700 1.000 30.69000 ? 112 PHE A CD1 1 
ATOM   838  C CD2 . PHE A 1 110 ? -8.15700  8.80700   -24.54600 1.000 29.91000 ? 112 PHE A CD2 1 
ATOM   839  C CE1 . PHE A 1 110 ? -7.45900  8.67600   -27.15000 1.000 31.07000 ? 112 PHE A CE1 1 
ATOM   840  C CE2 . PHE A 1 110 ? -8.70200  7.85300   -25.36100 1.000 29.87000 ? 112 PHE A CE2 1 
ATOM   841  C CZ  . PHE A 1 110 ? -8.34800  7.79300   -26.65900 1.000 31.46000 ? 112 PHE A CZ  1 
ATOM   842  N N   . SER A 1 111 ? -6.16500  9.51300   -21.42900 1.000 24.48000 ? 113 SER A N   1 
ATOM   843  C CA  . SER A 1 111 ? -6.44100  8.52100   -20.45200 1.000 27.18000 ? 113 SER A CA  1 
ATOM   844  C C   . SER A 1 111 ? -7.89300  8.06700   -20.53000 1.000 28.11000 ? 113 SER A C   1 
ATOM   845  O O   . SER A 1 111 ? -8.74900  8.81700   -20.80300 1.000 26.48000 ? 113 SER A O   1 
ATOM   846  C CB  . SER A 1 111 ? -6.20200  9.01000   -19.03600 1.000 28.98000 ? 113 SER A CB  1 
ATOM   847  O OG  . SER A 1 111 ? -4.91500  9.26800   -18.76800 1.000 28.40000 ? 113 SER A OG  1 
ATOM   848  N N   . VAL A 1 112 ? -8.12400  6.82200   -20.24400 1.000 27.43000 ? 114 VAL A N   1 
ATOM   849  C CA  . VAL A 1 112 ? -9.43600  6.27300   -20.22800 1.000 28.95000 ? 114 VAL A CA  1 
ATOM   850  C C   . VAL A 1 112 ? -9.80000  5.71600   -18.87400 1.000 29.12000 ? 114 VAL A C   1 
ATOM   851  O O   . VAL A 1 112 ? -9.07100  4.95500   -18.32500 1.000 25.89000 ? 114 VAL A O   1 
ATOM   852  C CB  . VAL A 1 112 ? -9.62000  5.18600   -21.30600 1.000 32.79000 ? 114 VAL A CB  1 
ATOM   853  C CG1 . VAL A 1 112 ? -10.92200 4.46800   -21.17400 1.000 28.63000 ? 114 VAL A CG1 1 
ATOM   854  C CG2 . VAL A 1 112 ? -9.43700  5.71600   -22.69300 1.000 29.16000 ? 114 VAL A CG2 1 
ATOM   855  N N   . LEU A 1 113 ? -10.94900 6.13600   -18.36700 1.000 26.50000 ? 115 LEU A N   1 
ATOM   856  C CA  . LEU A 1 113 ? -11.51600 5.60500   -17.13900 1.000 25.49000 ? 115 LEU A CA  1 
ATOM   857  C C   . LEU A 1 113 ? -12.52500 4.53100   -17.53600 1.000 27.92000 ? 115 LEU A C   1 
ATOM   858  O O   . LEU A 1 113 ? -13.64300 4.83700   -17.96400 1.000 29.71000 ? 115 LEU A O   1 
ATOM   859  C CB  . LEU A 1 113 ? -12.16200 6.71600   -16.31600 1.000 26.64000 ? 115 LEU A CB  1 
ATOM   860  C CG  . LEU A 1 113 ? -12.75300 6.22900   -14.99200 1.000 27.71000 ? 115 LEU A CG  1 
ATOM   861  C CD1 . LEU A 1 113 ? -11.67900 5.67700   -14.04600 1.000 23.80000 ? 115 LEU A CD1 1 
ATOM   862  C CD2 . LEU A 1 113 ? -13.53000 7.32400   -14.29600 1.000 28.31000 ? 115 LEU A CD2 1 
ATOM   863  N N   . ALA A 1 114 ? -12.11800 3.27300   -17.41800 1.000 26.88000 ? 116 ALA A N   1 
ATOM   864  C CA  . ALA A 1 114 ? -12.97900 2.14200   -17.72000 1.000 28.24000 ? 116 ALA A CA  1 
ATOM   865  C C   . ALA A 1 114 ? -13.93100 1.92500   -16.55600 1.000 30.50000 ? 116 ALA A C   1 
ATOM   866  O O   . ALA A 1 114 ? -13.49700 1.84800   -15.40200 1.000 28.43000 ? 116 ALA A O   1 
ATOM   867  C CB  . ALA A 1 114 ? -12.15300 0.88000   -17.95500 1.000 28.96000 ? 116 ALA A CB  1 
ATOM   868  N N   . CYS A 1 115 ? -15.19400 1.85300   -16.87300 1.000 27.97000 ? 117 CYS A N   1 
ATOM   869  C CA  . CYS A 1 115 ? -16.24500 1.67600   -15.92500 1.000 30.81000 ? 117 CYS A CA  1 
ATOM   870  C C   . CYS A 1 115 ? -17.21200 0.59400   -16.26300 1.000 35.37000 ? 117 CYS A C   1 
ATOM   871  O O   . CYS A 1 115 ? -17.37400 0.27900   -17.38000 1.000 36.39000 ? 117 CYS A O   1 
ATOM   872  C CB  . CYS A 1 115 ? -17.07500 2.92200   -15.79800 1.000 30.20000 ? 117 CYS A CB  1 
ATOM   873  S SG  . CYS A 1 115 ? -16.29100 4.44200   -15.44200 1.000 34.95000 ? 117 CYS A SG  1 
ATOM   874  N N   . TYR A 1 116 ? -17.84500 0.02400   -15.25100 1.000 35.01000 ? 118 TYR A N   1 
ATOM   875  C CA  . TYR A 1 116 ? -18.87400 -0.99700  -15.41000 1.000 37.77000 ? 118 TYR A CA  1 
ATOM   876  C C   . TYR A 1 116 ? -20.16700 -0.62700  -14.71100 1.000 34.98000 ? 118 TYR A C   1 
ATOM   877  O O   . TYR A 1 116 ? -20.22000 -0.56000  -13.54900 1.000 37.06000 ? 118 TYR A O   1 
ATOM   878  C CB  . TYR A 1 116 ? -18.41900 -2.34100  -14.90300 1.000 40.54000 ? 118 TYR A CB  1 
ATOM   879  N N   . ASN A 1 117 ? -21.20600 -0.40200  -15.46700 1.000 36.63000 ? 119 ASN A N   1 
ATOM   880  C CA  . ASN A 1 117 ? -22.49000 -0.04100  -14.91900 1.000 39.86000 ? 119 ASN A CA  1 
ATOM   881  C C   . ASN A 1 117 ? -22.46000 1.19200   -14.06600 1.000 41.42000 ? 119 ASN A C   1 
ATOM   882  O O   . ASN A 1 117 ? -23.12100 1.27500   -13.08800 1.000 42.11000 ? 119 ASN A O   1 
ATOM   883  C CB  . ASN A 1 117 ? -23.09700 -1.21000  -14.13000 1.000 40.37000 ? 119 ASN A CB  1 
ATOM   884  N N   . GLY A 1 118 ? -21.67600 2.14600   -14.46400 1.000 36.63000 ? 120 GLY A N   1 
ATOM   885  C CA  . GLY A 1 118 ? -21.55000 3.36700   -13.75600 1.000 34.17000 ? 120 GLY A CA  1 
ATOM   886  C C   . GLY A 1 118 ? -20.48500 3.45500   -12.70600 1.000 37.01000 ? 120 GLY A C   1 
ATOM   887  O O   . GLY A 1 118 ? -20.30700 4.48900   -12.21000 1.000 38.08000 ? 120 GLY A O   1 
ATOM   888  N N   . SER A 1 119 ? -19.78600 2.38800   -12.40800 1.000 36.21000 ? 121 SER A N   1 
ATOM   889  C CA  . SER A 1 119 ? -18.72900 2.45200   -11.45000 1.000 36.71000 ? 121 SER A CA  1 
ATOM   890  C C   . SER A 1 119 ? -17.33400 2.25800   -12.04900 1.000 35.85000 ? 121 SER A C   1 
ATOM   891  O O   . SER A 1 119 ? -17.05800 1.32200   -12.69100 1.000 31.64000 ? 121 SER A O   1 
ATOM   892  C CB  . SER A 1 119 ? -18.98400 1.59600   -10.24400 1.000 38.15000 ? 121 SER A CB  1 
ATOM   893  O OG  . SER A 1 119 ? -19.08800 0.29400   -10.57800 1.000 46.50000 ? 121 SER A OG  1 
ATOM   894  N N   . PRO A 1 120 ? -16.48100 3.30200   -11.74700 1.000 33.13000 ? 122 PRO A N   1 
ATOM   895  C CA  . PRO A 1 120 ? -15.15100 3.18800   -12.31100 1.000 34.73000 ? 122 PRO A CA  1 
ATOM   896  C C   . PRO A 1 120 ? -14.41500 2.00300   -11.78400 1.000 33.14000 ? 122 PRO A C   1 
ATOM   897  O O   . PRO A 1 120 ? -14.47000 1.72500   -10.66200 1.000 33.47000 ? 122 PRO A O   1 
ATOM   898  C CB  . PRO A 1 120 ? -14.44400 4.47000   -11.91800 1.000 33.13000 ? 122 PRO A CB  1 
ATOM   899  C CG  . PRO A 1 120 ? -15.21700 5.11600   -10.91900 1.000 39.10000 ? 122 PRO A CG  1 
ATOM   900  C CD  . PRO A 1 120 ? -16.59400 4.64500   -11.03100 1.000 34.24000 ? 122 PRO A CD  1 
ATOM   901  N N   . SER A 1 121 ? -13.72100 1.33900   -12.65100 1.000 31.82000 ? 123 SER A N   1 
ATOM   902  C CA  . SER A 1 121 ? -13.00600 0.18000   -12.34100 1.000 34.07000 ? 123 SER A CA  1 
ATOM   903  C C   . SER A 1 121 ? -11.49500 0.28000   -12.45500 1.000 34.91000 ? 123 SER A C   1 
ATOM   904  O O   . SER A 1 121 ? -10.80800 -0.28300  -11.69300 1.000 31.45000 ? 123 SER A O   1 
ATOM   905  C CB  . SER A 1 121 ? -13.58200 -0.84100  -13.26300 1.000 36.98000 ? 123 SER A CB  1 
ATOM   906  O OG  . SER A 1 121 ? -12.74300 -1.88000  -13.48600 1.000 46.50000 ? 123 SER A OG  1 
ATOM   907  N N   . GLY A 1 122 ? -11.03100 0.99900   -13.45400 1.000 33.11000 ? 124 GLY A N   1 
ATOM   908  C CA  . GLY A 1 122 ? -9.65200  1.22100   -13.75500 1.000 30.02000 ? 124 GLY A CA  1 
ATOM   909  C C   . GLY A 1 122 ? -9.35800  2.36100   -14.70100 1.000 30.53000 ? 124 GLY A C   1 
ATOM   910  O O   . GLY A 1 122 ? -10.19000 2.77800   -15.41300 1.000 27.57000 ? 124 GLY A O   1 
ATOM   911  N N   . VAL A 1 123 ? -8.13900  2.81300   -14.69400 1.000 27.80000 ? 125 VAL A N   1 
ATOM   912  C CA  . VAL A 1 123 ? -7.66400  3.86000   -15.53400 1.000 27.26000 ? 125 VAL A CA  1 
ATOM   913  C C   . VAL A 1 123 ? -6.39700  3.48400   -16.23900 1.000 31.06000 ? 125 VAL A C   1 
ATOM   914  O O   . VAL A 1 123 ? -5.53400  2.91000   -15.66700 1.000 31.76000 ? 125 VAL A O   1 
ATOM   915  C CB  . VAL A 1 123 ? -7.51500  5.15900   -14.78500 1.000 28.62000 ? 125 VAL A CB  1 
ATOM   916  C CG1 . VAL A 1 123 ? -6.42000  5.12400   -13.79000 1.000 30.69000 ? 125 VAL A CG1 1 
ATOM   917  C CG2 . VAL A 1 123 ? -7.30200  6.30300   -15.71000 1.000 27.18000 ? 125 VAL A CG2 1 
ATOM   918  N N   . TYR A 1 124 ? -6.33400  3.83600   -17.49600 1.000 28.05000 ? 126 TYR A N   1 
ATOM   919  C CA  . TYR A 1 124 ? -5.19900  3.59400   -18.34400 1.000 34.38000 ? 126 TYR A CA  1 
ATOM   920  C C   . TYR A 1 124 ? -4.91100  4.66000   -19.38100 1.000 33.06000 ? 126 TYR A C   1 
ATOM   921  O O   . TYR A 1 124 ? -5.74600  5.37100   -19.71700 1.000 29.34000 ? 126 TYR A O   1 
ATOM   922  C CB  . TYR A 1 124 ? -5.27900  2.27400   -18.97500 1.000 36.14000 ? 126 TYR A CB  1 
ATOM   923  C CG  . TYR A 1 124 ? -6.36900  2.07100   -19.93400 1.000 36.54000 ? 126 TYR A CG  1 
ATOM   924  C CD1 . TYR A 1 124 ? -7.52900  1.50400   -19.55400 1.000 36.80000 ? 126 TYR A CD1 1 
ATOM   925  C CD2 . TYR A 1 124 ? -6.20800  2.39600   -21.24700 1.000 40.14000 ? 126 TYR A CD2 1 
ATOM   926  C CE1 . TYR A 1 124 ? -8.51700  1.28000   -20.45800 1.000 37.99000 ? 126 TYR A CE1 1 
ATOM   927  C CE2 . TYR A 1 124 ? -7.19600  2.17600   -22.14900 1.000 40.63000 ? 126 TYR A CE2 1 
ATOM   928  C CZ  . TYR A 1 124 ? -8.34600  1.62000   -21.73800 1.000 40.03000 ? 126 TYR A CZ  1 
ATOM   929  O OH  . TYR A 1 124 ? -9.30100  1.41400   -22.60900 1.000 48.57000 ? 126 TYR A OH  1 
ATOM   930  N N   . GLN A 1 125 ? -3.69400  4.72900   -19.84600 1.000 28.34000 ? 127 GLN A N   1 
ATOM   931  C CA  . GLN A 1 125 ? -3.24400  5.73100   -20.80100 1.000 29.86000 ? 127 GLN A CA  1 
ATOM   932  C C   . GLN A 1 125 ? -3.17700  5.09500   -22.18400 1.000 32.26000 ? 127 GLN A C   1 
ATOM   933  O O   . GLN A 1 125 ? -2.76600  3.94100   -22.32100 1.000 34.73000 ? 127 GLN A O   1 
ATOM   934  C CB  . GLN A 1 125 ? -1.87100  6.28800   -20.38100 1.000 35.09000 ? 127 GLN A CB  1 
ATOM   935  C CG  . GLN A 1 125 ? -1.25900  7.34900   -21.28500 1.000 31.41000 ? 127 GLN A CG  1 
ATOM   936  C CD  . GLN A 1 125 ? -1.91800  8.72100   -21.15400 1.000 35.86000 ? 127 GLN A CD  1 
ATOM   937  O OE1 . GLN A 1 125 ? -2.93000  8.88900   -20.46000 1.000 33.47000 ? 127 GLN A OE1 1 
ATOM   938  N NE2 . GLN A 1 125 ? -1.34500  9.71200   -21.83400 1.000 37.91000 ? 127 GLN A NE2 1 
ATOM   939  N N   . CYS A 1 126 ? -3.54100  5.88200   -23.20300 1.000 32.87000 ? 128 CYS A N   1 
ATOM   940  C CA  . CYS A 1 126 ? -3.94800  5.46400   -24.53700 1.000 32.29000 ? 128 CYS A CA  1 
ATOM   941  C C   . CYS A 1 126 ? -3.35000  6.37200   -25.57700 1.000 31.42000 ? 128 CYS A C   1 
ATOM   942  O O   . CYS A 1 126 ? -3.06700  7.53100   -25.29800 1.000 33.78000 ? 128 CYS A O   1 
ATOM   943  C CB  . CYS A 1 126 ? -5.47700  5.63600   -24.77000 1.000 37.21000 ? 128 CYS A CB  1 
ATOM   944  S SG  . CYS A 1 126 ? -6.38800  4.26200   -24.58300 1.000 48.68000 ? 128 CYS A SG  1 
ATOM   945  N N   . ALA A 1 127 ? -3.31800  5.87400   -26.82000 1.000 33.15000 ? 129 ALA A N   1 
ATOM   946  C CA  . ALA A 1 127 ? -3.19600  6.70600   -28.00800 1.000 32.79000 ? 129 ALA A CA  1 
ATOM   947  C C   . ALA A 1 127 ? -4.28600  6.32600   -29.00100 1.000 30.65000 ? 129 ALA A C   1 
ATOM   948  O O   . ALA A 1 127 ? -4.63700  5.15300   -29.13900 1.000 33.86000 ? 129 ALA A O   1 
ATOM   949  C CB  . ALA A 1 127 ? -1.82000  6.57500   -28.70000 1.000 31.85000 ? 129 ALA A CB  1 
ATOM   950  N N   . MET A 1 128 ? -4.83600  7.33600   -29.66200 1.000 28.02000 ? 130 MET A N   1 
ATOM   951  C CA  . MET A 1 128 ? -5.62400  7.14100   -30.87100 1.000 31.69000 ? 130 MET A CA  1 
ATOM   952  C C   . MET A 1 128 ? -4.70100  6.63000   -31.97400 1.000 31.15000 ? 130 MET A C   1 
ATOM   953  O O   . MET A 1 128 ? -3.78600  7.34200   -32.40000 1.000 30.84000 ? 130 MET A O   1 
ATOM   954  C CB  . MET A 1 128 ? -6.28100  8.46900   -31.24400 1.000 31.87000 ? 130 MET A CB  1 
ATOM   955  C CG  . MET A 1 128 ? -7.03700  8.52100   -32.55800 1.000 35.57000 ? 130 MET A CG  1 
ATOM   956  S SD  . MET A 1 128 ? -8.57400  7.62500   -32.52900 1.000 39.83000 ? 130 MET A SD  1 
ATOM   957  C CE  . MET A 1 128 ? -9.51700  8.43800   -31.24300 1.000 34.91000 ? 130 MET A CE  1 
ATOM   958  N N   . ARG A 1 129 ? -4.91000  5.38200   -32.39600 1.000 29.79000 ? 131 ARG A N   1 
ATOM   959  C CA  . ARG A 1 129 ? -4.12500  4.76500   -33.45500 1.000 28.49000 ? 131 ARG A CA  1 
ATOM   960  C C   . ARG A 1 129 ? -4.40700  5.42400   -34.80600 1.000 29.84000 ? 131 ARG A C   1 
ATOM   961  O O   . ARG A 1 129 ? -5.46500  6.02900   -35.00600 1.000 30.73000 ? 131 ARG A O   1 
ATOM   962  C CB  . ARG A 1 129 ? -4.42900  3.26900   -33.55300 1.000 27.27000 ? 131 ARG A CB  1 
ATOM   963  C CG  . ARG A 1 129 ? -4.31600  2.48300   -32.26000 1.000 31.45000 ? 131 ARG A CG  1 
ATOM   964  C CD  . ARG A 1 129 ? -2.91800  2.54300   -31.62400 1.000 31.46000 ? 131 ARG A CD  1 
ATOM   965  N NE  . ARG A 1 129 ? -1.84700  2.35300   -32.59800 1.000 28.13000 ? 131 ARG A NE  1 
ATOM   966  C CZ  . ARG A 1 129 ? -0.55900  2.59900   -32.34600 1.000 33.33000 ? 131 ARG A CZ  1 
ATOM   967  N NH1 . ARG A 1 129 ? -0.18800  3.04700   -31.16000 1.000 26.57000 ? 131 ARG A NH1 1 
ATOM   968  N NH2 . ARG A 1 129 ? 0.36300   2.40600   -33.28500 1.000 29.75000 ? 131 ARG A NH2 1 
ATOM   969  N N   . PRO A 1 130 ? -3.46900  5.30700   -35.76200 1.000 30.43000 ? 132 PRO A N   1 
ATOM   970  C CA  . PRO A 1 130 ? -3.68100  5.92700   -37.08500 1.000 30.52000 ? 132 PRO A CA  1 
ATOM   971  C C   . PRO A 1 130 ? -4.85500  5.35800   -37.84800 1.000 29.24000 ? 132 PRO A C   1 
ATOM   972  O O   . PRO A 1 130 ? -5.35300  6.02000   -38.75900 1.000 30.25000 ? 132 PRO A O   1 
ATOM   973  C CB  . PRO A 1 130 ? -2.35900  5.65700   -37.82700 1.000 30.40000 ? 132 PRO A CB  1 
ATOM   974  C CG  . PRO A 1 130 ? -1.33700  5.47200   -36.73000 1.000 29.75000 ? 132 PRO A CG  1 
ATOM   975  C CD  . PRO A 1 130 ? -2.09200  4.78800   -35.60700 1.000 29.80000 ? 132 PRO A CD  1 
ATOM   976  N N   . ASN A 1 131 ? -5.30000  4.14900   -37.52800 1.000 28.04000 ? 133 ASN A N   1 
ATOM   977  C CA  . ASN A 1 131 ? -6.52300  3.60800   -38.09200 1.000 31.51000 ? 133 ASN A CA  1 
ATOM   978  C C   . ASN A 1 131 ? -7.76200  3.97000   -37.25400 1.000 34.24000 ? 133 ASN A C   1 
ATOM   979  O O   . ASN A 1 131 ? -8.80400  3.32900   -37.40600 1.000 31.95000 ? 133 ASN A O   1 
ATOM   980  C CB  . ASN A 1 131 ? -6.39600  2.08800   -38.24700 1.000 31.46000 ? 133 ASN A CB  1 
ATOM   981  C CG  . ASN A 1 131 ? -6.29600  1.36200   -36.91100 1.000 35.71000 ? 133 ASN A CG  1 
ATOM   982  O OD1 . ASN A 1 131 ? -6.26500  1.97600   -35.84500 1.000 34.39000 ? 133 ASN A OD1 1 
ATOM   983  N ND2 . ASN A 1 131 ? -6.24600  0.04000   -36.97000 1.000 38.36000 ? 133 ASN A ND2 1 
ATOM   984  N N   . PHE A 1 132 ? -7.68900  4.99000   -36.41700 1.000 31.70000 ? 134 PHE A N   1 
ATOM   985  C CA  . PHE A 1 132 ? -8.79500  5.46800   -35.60700 1.000 29.72000 ? 134 PHE A CA  1 
ATOM   986  C C   . PHE A 1 132 ? -9.40700  4.50100   -34.60600 1.000 33.64000 ? 134 PHE A C   1 
ATOM   987  O O   . PHE A 1 132 ? -10.53300 4.51100   -34.37500 1.000 36.91000 ? 134 PHE A O   1 
ATOM   988  C CB  . PHE A 1 132 ? -9.87300  6.02100   -36.50800 1.000 30.14000 ? 134 PHE A CB  1 
ATOM   989  C CG  . PHE A 1 132 ? -9.40700  7.06700   -37.41200 1.000 33.58000 ? 134 PHE A CG  1 
ATOM   990  C CD1 . PHE A 1 132 ? -9.32100  8.33000   -37.00100 1.000 34.91000 ? 134 PHE A CD1 1 
ATOM   991  C CD2 . PHE A 1 132 ? -9.02200  6.77400   -38.67300 1.000 36.10000 ? 134 PHE A CD2 1 
ATOM   992  C CE1 . PHE A 1 132 ? -8.87300  9.30500   -37.83000 1.000 36.68000 ? 134 PHE A CE1 1 
ATOM   993  C CE2 . PHE A 1 132 ? -8.58400  7.74400   -39.51800 1.000 35.04000 ? 134 PHE A CE2 1 
ATOM   994  C CZ  . PHE A 1 132 ? -8.52100  9.01300   -39.09600 1.000 36.54000 ? 134 PHE A CZ  1 
ATOM   995  N N   . THR A 1 133 ? -8.61100  3.67400   -34.02400 1.000 33.44000 ? 135 THR A N   1 
ATOM   996  C CA  . THR A 1 133 ? -9.01900  2.72200   -33.05500 1.000 31.99000 ? 135 THR A CA  1 
ATOM   997  C C   . THR A 1 133 ? -8.19300  2.87900   -31.81800 1.000 34.94000 ? 135 THR A C   1 
ATOM   998  O O   . THR A 1 133 ? -7.26500  3.57200   -31.78300 1.000 29.92000 ? 135 THR A O   1 
ATOM   999  C CB  . THR A 1 133 ? -8.91000  1.27700   -33.53700 1.000 33.78000 ? 135 THR A CB  1 
ATOM   1000 O OG1 . THR A 1 133 ? -7.56800  0.89800   -33.69500 1.000 32.66000 ? 135 THR A OG1 1 
ATOM   1001 C CG2 . THR A 1 133 ? -9.63600  1.07400   -34.79300 1.000 32.47000 ? 135 THR A CG2 1 
ATOM   1002 N N   . ILE A 1 134 ? -8.62700  2.22000   -30.79600 1.000 33.30000 ? 136 ILE A N   1 
ATOM   1003 C CA  . ILE A 1 134 ? -7.98400  2.21800   -29.55400 1.000 37.17000 ? 136 ILE A CA  1 
ATOM   1004 C C   . ILE A 1 134 ? -7.70400  0.81600   -29.10000 1.000 39.39000 ? 136 ILE A C   1 
ATOM   1005 O O   . ILE A 1 134 ? -8.53100  0.01000   -29.15700 1.000 40.71000 ? 136 ILE A O   1 
ATOM   1006 C CB  . ILE A 1 134 ? -8.89000  2.87800   -28.55000 1.000 40.76000 ? 136 ILE A CB  1 
ATOM   1007 C CG1 . ILE A 1 134 ? -9.13900  4.29600   -28.95700 1.000 42.03000 ? 136 ILE A CG1 1 
ATOM   1008 C CG2 . ILE A 1 134 ? -8.32100  2.82800   -27.18900 1.000 48.62000 ? 136 ILE A CG2 1 
ATOM   1009 C CD1 . ILE A 1 134 ? -7.97800  5.17300   -28.78100 1.000 37.71000 ? 136 ILE A CD1 1 
ATOM   1010 N N   . LYS A 1 135 ? -6.51100  0.56800   -28.65000 1.000 38.34000 ? 137 LYS A N   1 
ATOM   1011 C CA  . LYS A 1 135 ? -6.16100  -0.71500  -28.11200 1.000 41.84000 ? 137 LYS A CA  1 
ATOM   1012 C C   . LYS A 1 135 ? -6.40100  -0.57900  -26.65700 1.000 43.74000 ? 137 LYS A C   1 
ATOM   1013 O O   . LYS A 1 135 ? -5.54100  -0.29500  -25.92400 1.000 47.22000 ? 137 LYS A O   1 
ATOM   1014 C CB  . LYS A 1 135 ? -4.73200  -1.07700  -28.38200 1.000 30.00000 ? 137 LYS A CB  1 
ATOM   1015 C CG  . LYS A 1 135 ? -4.40400  -1.33000  -29.82900 1.000 30.00000 ? 137 LYS A CG  1 
ATOM   1016 C CD  . LYS A 1 135 ? -2.92500  -1.31700  -30.05200 1.000 30.00000 ? 137 LYS A CD  1 
ATOM   1017 C CE  . LYS A 1 135 ? -2.57700  -1.56200  -31.48500 1.000 30.00000 ? 137 LYS A CE  1 
ATOM   1018 N NZ  . LYS A 1 135 ? -1.09100  -1.74600  -31.63200 1.000 30.00000 ? 137 LYS A NZ  1 
ATOM   1019 N N   . GLY A 1 136 ? -7.63000  -0.77400  -26.27500 1.000 46.15000 ? 138 GLY A N   1 
ATOM   1020 C CA  . GLY A 1 136 ? -8.10500  -0.67700  -24.92200 1.000 48.87000 ? 138 GLY A CA  1 
ATOM   1021 C C   . GLY A 1 136 ? -8.27700  -1.96900  -24.18400 1.000 54.15000 ? 138 GLY A C   1 
ATOM   1022 O O   . GLY A 1 136 ? -8.09200  -2.99300  -24.70100 1.000 58.26000 ? 138 GLY A O   1 
ATOM   1023 N N   . SER A 1 137 ? -8.66900  -1.88600  -22.94800 1.000 53.48000 ? 139 SER A N   1 
ATOM   1024 C CA  . SER A 1 137 ? -8.89200  -3.06200  -22.19600 1.000 57.31000 ? 139 SER A CA  1 
ATOM   1025 C C   . SER A 1 137 ? -10.27700 -2.86200  -21.72600 1.000 64.32000 ? 139 SER A C   1 
ATOM   1026 O O   . SER A 1 137 ? -10.50300 -2.22600  -20.71000 1.000 65.23000 ? 139 SER A O   1 
ATOM   1027 C CB  . SER A 1 137 ? -7.91400  -3.13100  -21.02500 1.000 61.00000 ? 139 SER A CB  1 
ATOM   1028 O OG  . SER A 1 137 ? -7.63000  -4.47100  -20.62100 1.000 67.43000 ? 139 SER A OG  1 
ATOM   1029 N N   . PHE A 1 138 ? -11.21900 -3.40500  -22.45800 1.000 63.08000 ? 140 PHE A N   1 
ATOM   1030 C CA  . PHE A 1 138 ? -12.59800 -3.25100  -22.05800 1.000 64.57000 ? 140 PHE A CA  1 
ATOM   1031 C C   . PHE A 1 138 ? -13.30500 -4.48300  -21.41800 1.000 70.98000 ? 140 PHE A C   1 
ATOM   1032 O O   . PHE A 1 138 ? -13.34600 -5.58900  -21.94800 1.000 75.18000 ? 140 PHE A O   1 
ATOM   1033 C CB  . PHE A 1 138 ? -13.40300 -2.64600  -23.18900 1.000 62.30000 ? 140 PHE A CB  1 
ATOM   1034 C CG  . PHE A 1 138 ? -13.05800 -1.20200  -23.44800 1.000 58.45000 ? 140 PHE A CG  1 
ATOM   1035 C CD1 . PHE A 1 138 ? -12.95500 -0.31300  -22.40800 1.000 56.32000 ? 140 PHE A CD1 1 
ATOM   1036 C CD2 . PHE A 1 138 ? -12.81600 -0.75700  -24.70500 1.000 54.89000 ? 140 PHE A CD2 1 
ATOM   1037 C CE1 . PHE A 1 138 ? -12.66600 0.97300   -22.61400 1.000 51.82000 ? 140 PHE A CE1 1 
ATOM   1038 C CE2 . PHE A 1 138 ? -12.48800 0.55100   -24.92200 1.000 52.29000 ? 140 PHE A CE2 1 
ATOM   1039 C CZ  . PHE A 1 138 ? -12.43900 1.42400   -23.88100 1.000 51.81000 ? 140 PHE A CZ  1 
ATOM   1040 N N   . LEU A 1 139 ? -13.85800 -4.24500  -20.24900 1.000 66.31000 ? 141 LEU A N   1 
ATOM   1041 C CA  . LEU A 1 139 ? -14.58600 -5.22000  -19.52400 1.000 63.96000 ? 141 LEU A CA  1 
ATOM   1042 C C   . LEU A 1 139 ? -15.85800 -5.25400  -20.33500 1.000 65.82000 ? 141 LEU A C   1 
ATOM   1043 O O   . LEU A 1 139 ? -16.02900 -4.45200  -21.21200 1.000 68.09000 ? 141 LEU A O   1 
ATOM   1044 C CB  . LEU A 1 139 ? -14.78800 -4.75700  -18.09800 1.000 64.26000 ? 141 LEU A CB  1 
ATOM   1045 C CG  . LEU A 1 139 ? -15.19000 -3.33600  -17.80000 1.000 55.30000 ? 141 LEU A CG  1 
ATOM   1046 C CD1 . LEU A 1 139 ? -16.68300 -3.33400  -17.63500 1.000 55.20000 ? 141 LEU A CD1 1 
ATOM   1047 C CD2 . LEU A 1 139 ? -14.52900 -2.93800  -16.53000 1.000 48.77000 ? 141 LEU A CD2 1 
ATOM   1048 N N   . ALA A 1 140 ? -16.73700 -6.18400  -20.07700 1.000 68.86000 ? 142 ALA A N   1 
ATOM   1049 C CA  . ALA A 1 140 ? -17.93000 -6.34200  -20.88600 1.000 66.74000 ? 142 ALA A CA  1 
ATOM   1050 C C   . ALA A 1 140 ? -18.89100 -5.17700  -20.97300 1.000 65.91000 ? 142 ALA A C   1 
ATOM   1051 O O   . ALA A 1 140 ? -19.55200 -4.96600  -21.94700 1.000 71.27000 ? 142 ALA A O   1 
ATOM   1052 C CB  . ALA A 1 140 ? -18.66300 -7.61500  -20.51100 1.000 65.71000 ? 142 ALA A CB  1 
ATOM   1053 N N   . GLY A 1 141 ? -19.02800 -4.43400  -19.93400 1.000 65.73000 ? 143 GLY A N   1 
ATOM   1054 C CA  . GLY A 1 141 ? -19.99500 -3.35400  -20.01000 1.000 53.36000 ? 143 GLY A CA  1 
ATOM   1055 C C   . GLY A 1 141 ? -19.37800 -1.97600  -19.91700 1.000 46.56000 ? 143 GLY A C   1 
ATOM   1056 O O   . GLY A 1 141 ? -19.90800 -1.09300  -19.23100 1.000 48.21000 ? 143 GLY A O   1 
ATOM   1057 N N   . SER A 1 142 ? -18.25700 -1.77800  -20.60600 1.000 49.05000 ? 144 SER A N   1 
ATOM   1058 C CA  . SER A 1 142 ? -17.54400 -0.51400  -20.53300 1.000 41.72000 ? 144 SER A CA  1 
ATOM   1059 C C   . SER A 1 142 ? -18.04900 0.51100   -21.53600 1.000 35.10000 ? 144 SER A C   1 
ATOM   1060 O O   . SER A 1 142 ? -17.50200 1.62000   -21.58200 1.000 31.77000 ? 144 SER A O   1 
ATOM   1061 C CB  . SER A 1 142 ? -16.04500 -0.73900  -20.72600 1.000 44.62000 ? 144 SER A CB  1 
ATOM   1062 O OG  . SER A 1 142 ? -15.76700 -1.06100  -22.07000 1.000 49.72000 ? 144 SER A OG  1 
ATOM   1063 N N   . CYS A 1 143 ? -19.06900 0.17000   -22.33900 1.000 37.20000 ? 145 CYS A N   1 
ATOM   1064 C CA  . CYS A 1 143 ? -19.73100 1.13700   -23.21500 1.000 28.29000 ? 145 CYS A CA  1 
ATOM   1065 C C   . CYS A 1 143 ? -20.05100 2.42700   -22.48900 1.000 30.30000 ? 145 CYS A C   1 
ATOM   1066 O O   . CYS A 1 143 ? -20.63100 2.40800   -21.39800 1.000 26.47000 ? 145 CYS A O   1 
ATOM   1067 C CB  . CYS A 1 143 ? -21.04600 0.56000   -23.73500 1.000 41.55000 ? 145 CYS A CB  1 
ATOM   1068 S SG  . CYS A 1 143 ? -21.22900 0.53700   -25.45100 1.000 55.65000 ? 145 CYS A SG  1 
ATOM   1069 N N   . GLY A 1 144 ? -19.73600 3.54900   -23.13000 1.000 26.44000 ? 146 GLY A N   1 
ATOM   1070 C CA  . GLY A 1 144 ? -19.94100 4.84400   -22.51400 1.000 30.32000 ? 146 GLY A CA  1 
ATOM   1071 C C   . GLY A 1 144 ? -18.80300 5.34100   -21.63700 1.000 27.88000 ? 146 GLY A C   1 
ATOM   1072 O O   . GLY A 1 144 ? -18.86100 6.49400   -21.17400 1.000 25.86000 ? 146 GLY A O   1 
ATOM   1073 N N   . SER A 1 145 ? -17.78900 4.51300   -21.37200 1.000 28.00000 ? 147 SER A N   1 
ATOM   1074 C CA  . SER A 1 145 ? -16.56800 5.00000   -20.72300 1.000 28.84000 ? 147 SER A CA  1 
ATOM   1075 C C   . SER A 1 145 ? -15.89700 6.05600   -21.59600 1.000 27.32000 ? 147 SER A C   1 
ATOM   1076 O O   . SER A 1 145 ? -15.93400 5.98500   -22.82000 1.000 28.81000 ? 147 SER A O   1 
ATOM   1077 C CB  . SER A 1 145 ? -15.58700 3.85500   -20.47600 1.000 28.73000 ? 147 SER A CB  1 
ATOM   1078 O OG  . SER A 1 145 ? -16.09000 2.92500   -19.53100 1.000 31.00000 ? 147 SER A OG  1 
ATOM   1079 N N   . VAL A 1 146 ? -15.26000 7.03700   -20.95900 1.000 23.33000 ? 148 VAL A N   1 
ATOM   1080 C CA  . VAL A 1 146 ? -14.76800 8.20200   -21.67600 1.000 25.06000 ? 148 VAL A CA  1 
ATOM   1081 C C   . VAL A 1 146 ? -13.25500 8.33600   -21.51700 1.000 27.63000 ? 148 VAL A C   1 
ATOM   1082 O O   . VAL A 1 146 ? -12.65600 7.90100   -20.52700 1.000 26.01000 ? 148 VAL A O   1 
ATOM   1083 C CB  . VAL A 1 146 ? -15.47300 9.49700   -21.22000 1.000 27.71000 ? 148 VAL A CB  1 
ATOM   1084 C CG1 . VAL A 1 146 ? -16.97700 9.41200   -21.51100 1.000 26.10000 ? 148 VAL A CG1 1 
ATOM   1085 C CG2 . VAL A 1 146 ? -15.21200 9.77300   -19.73700 1.000 28.63000 ? 148 VAL A CG2 1 
ATOM   1086 N N   . GLY A 1 147 ? -12.68200 9.02000   -22.46800 1.000 25.41000 ? 149 GLY A N   1 
ATOM   1087 C CA  . GLY A 1 147 ? -11.30800 9.33400   -22.58800 1.000 25.88000 ? 149 GLY A CA  1 
ATOM   1088 C C   . GLY A 1 147 ? -11.11800 10.81000  -22.40200 1.000 29.19000 ? 149 GLY A C   1 
ATOM   1089 O O   . GLY A 1 147 ? -11.90900 11.56200  -22.81600 1.000 30.71000 ? 149 GLY A O   1 
ATOM   1090 N N   . PHE A 1 148 ? -10.05000 11.18800  -21.76000 1.000 27.49000 ? 150 PHE A N   1 
ATOM   1091 C CA  . PHE A 1 148 ? -9.73600  12.55100  -21.41800 1.000 30.47000 ? 150 PHE A CA  1 
ATOM   1092 C C   . PHE A 1 148 ? -8.28700  12.92100  -21.18700 1.000 29.23000 ? 150 PHE A C   1 
ATOM   1093 O O   . PHE A 1 148 ? -7.46800  12.10400  -21.01000 1.000 27.22000 ? 150 PHE A O   1 
ATOM   1094 C CB  . PHE A 1 148 ? -10.48200 12.90200  -20.12000 1.000 29.49000 ? 150 PHE A CB  1 
ATOM   1095 C CG  . PHE A 1 148 ? -10.13300 12.02400  -18.96900 1.000 27.13000 ? 150 PHE A CG  1 
ATOM   1096 C CD1 . PHE A 1 148 ? -10.67600 10.82200  -18.85000 1.000 27.06000 ? 150 PHE A CD1 1 
ATOM   1097 C CD2 . PHE A 1 148 ? -9.22000  12.41300  -18.05900 1.000 29.49000 ? 150 PHE A CD2 1 
ATOM   1098 C CE1 . PHE A 1 148 ? -10.34500 10.01100  -17.84400 1.000 27.96000 ? 150 PHE A CE1 1 
ATOM   1099 C CE2 . PHE A 1 148 ? -8.87400  11.61900  -17.01800 1.000 30.08000 ? 150 PHE A CE2 1 
ATOM   1100 C CZ  . PHE A 1 148 ? -9.44900  10.40000  -16.91600 1.000 31.18000 ? 150 PHE A CZ  1 
ATOM   1101 N N   . ASN A 1 149 ? -8.03900  14.20400  -21.16300 1.000 28.85000 ? 151 ASN A N   1 
ATOM   1102 C CA  . ASN A 1 149 ? -6.77700  14.78800  -20.79400 1.000 31.63000 ? 151 ASN A CA  1 
ATOM   1103 C C   . ASN A 1 149 ? -7.04400  15.81200  -19.68600 1.000 31.66000 ? 151 ASN A C   1 
ATOM   1104 O O   . ASN A 1 149 ? -8.09800  16.29500  -19.60500 1.000 32.38000 ? 151 ASN A O   1 
ATOM   1105 C CB  . ASN A 1 149 ? -6.06900  15.43200  -21.94600 1.000 30.89000 ? 151 ASN A CB  1 
ATOM   1106 C CG  . ASN A 1 149 ? -5.47100  14.44000  -22.90100 1.000 34.56000 ? 151 ASN A CG  1 
ATOM   1107 O OD1 . ASN A 1 149 ? -4.43600  13.97700  -22.69600 1.000 36.35000 ? 151 ASN A OD1 1 
ATOM   1108 N ND2 . ASN A 1 149 ? -6.12900  14.17000  -23.93100 1.000 33.79000 ? 151 ASN A ND2 1 
ATOM   1109 N N   . ILE A 1 150 ? -6.09300  16.07500  -18.82500 1.000 33.09000 ? 152 ILE A N   1 
ATOM   1110 C CA  . ILE A 1 150 ? -6.26700  17.04700  -17.78300 1.000 34.08000 ? 152 ILE A CA  1 
ATOM   1111 C C   . ILE A 1 150 ? -5.15100  18.05600  -17.77700 1.000 40.68000 ? 152 ILE A C   1 
ATOM   1112 O O   . ILE A 1 150 ? -4.06300  17.70500  -17.62300 1.000 41.38000 ? 152 ILE A O   1 
ATOM   1113 C CB  . ILE A 1 150 ? -6.45600  16.39700  -16.40600 1.000 35.41000 ? 152 ILE A CB  1 
ATOM   1114 C CG1 . ILE A 1 150 ? -7.64000  15.48700  -16.39800 1.000 32.63000 ? 152 ILE A CG1 1 
ATOM   1115 C CG2 . ILE A 1 150 ? -6.71900  17.42100  -15.36900 1.000 36.31000 ? 152 ILE A CG2 1 
ATOM   1116 C CD1 . ILE A 1 150 ? -7.91300  14.85500  -15.07700 1.000 38.33000 ? 152 ILE A CD1 1 
ATOM   1117 N N   . ASP A 1 151 ? -5.45600  19.30900  -18.00200 1.000 43.40000 ? 153 ASP A N   1 
ATOM   1118 C CA  . ASP A 1 151 ? -4.44300  20.32900  -18.01200 1.000 47.03000 ? 153 ASP A CA  1 
ATOM   1119 C C   . ASP A 1 151 ? -4.84500  21.43100  -17.08500 1.000 48.72000 ? 153 ASP A C   1 
ATOM   1120 O O   . ASP A 1 151 ? -5.83500  22.01400  -17.26400 1.000 49.19000 ? 153 ASP A O   1 
ATOM   1121 C CB  . ASP A 1 151 ? -4.23900  20.84300  -19.41700 1.000 49.73000 ? 153 ASP A CB  1 
ATOM   1122 C CG  . ASP A 1 151 ? -3.79300  19.77300  -20.39100 1.000 54.42000 ? 153 ASP A CG  1 
ATOM   1123 O OD1 . ASP A 1 151 ? -2.65500  19.38600  -20.34300 1.000 60.65000 ? 153 ASP A OD1 1 
ATOM   1124 O OD2 . ASP A 1 151 ? -4.56300  19.32500  -21.22400 1.000 53.99000 ? 153 ASP A OD2 1 
ATOM   1125 N N   . TYR A 1 152 ? -4.05800  21.68900  -16.07200 1.000 48.87000 ? 154 TYR A N   1 
ATOM   1126 C CA  . TYR A 1 152 ? -4.36200  22.70400  -15.10900 1.000 48.85000 ? 154 TYR A CA  1 
ATOM   1127 C C   . TYR A 1 152 ? -5.72600  22.58500  -14.47400 1.000 54.51000 ? 154 TYR A C   1 
ATOM   1128 O O   . TYR A 1 152 ? -6.42500  23.55400  -14.32400 1.000 59.74000 ? 154 TYR A O   1 
ATOM   1129 C CB  . TYR A 1 152 ? -4.15900  24.08800  -15.68500 1.000 53.72000 ? 154 TYR A CB  1 
ATOM   1130 N N   . ASP A 1 153 ? -6.11700  21.39600  -14.12400 1.000 50.37000 ? 155 ASP A N   1 
ATOM   1131 C CA  . ASP A 1 153 ? -7.38900  21.18800  -13.48900 1.000 52.98000 ? 155 ASP A CA  1 
ATOM   1132 C C   . ASP A 1 153 ? -8.58800  21.29300  -14.41700 1.000 48.75000 ? 155 ASP A C   1 
ATOM   1133 O O   . ASP A 1 153 ? -9.67400  21.18700  -13.97500 1.000 46.67000 ? 155 ASP A O   1 
ATOM   1134 C CB  . ASP A 1 153 ? -7.57100  22.10800  -12.30500 1.000 53.31000 ? 155 ASP A CB  1 
ATOM   1135 C CG  . ASP A 1 153 ? -6.59700  21.82900  -11.18600 1.000 63.73000 ? 155 ASP A CG  1 
ATOM   1136 O OD1 . ASP A 1 153 ? -6.41500  20.67500  -10.75200 1.000 63.76000 ? 155 ASP A OD1 1 
ATOM   1137 O OD2 . ASP A 1 153 ? -5.98900  22.79600  -10.72300 1.000 68.36000 ? 155 ASP A OD2 1 
ATOM   1138 N N   . CYS A 1 154 ? -8.36600  21.46600  -15.69600 1.000 44.92000 ? 156 CYS A N   1 
ATOM   1139 C CA  . CYS A 1 154 ? -9.44500  21.51300  -16.64000 1.000 44.02000 ? 156 CYS A CA  1 
ATOM   1140 C C   . CYS A 1 154 ? -9.43400  20.20400  -17.41400 1.000 39.21000 ? 156 CYS A C   1 
ATOM   1141 O O   . CYS A 1 154 ? -8.44500  19.81400  -17.87500 1.000 41.12000 ? 156 CYS A O   1 
ATOM   1142 C CB  . CYS A 1 154 ? -9.28200  22.71200  -17.52300 1.000 46.93000 ? 156 CYS A CB  1 
ATOM   1143 S SG  . CYS A 1 154 ? -10.29000 22.75400  -18.97700 1.000 58.27000 ? 156 CYS A SG  1 
ATOM   1144 N N   . VAL A 1 155 ? -10.55000 19.54900  -17.51600 1.000 36.68000 ? 157 VAL A N   1 
ATOM   1145 C CA  . VAL A 1 155 ? -10.64400 18.30200  -18.18300 1.000 34.99000 ? 157 VAL A CA  1 
ATOM   1146 C C   . VAL A 1 155 ? -11.15300 18.40400  -19.59300 1.000 34.65000 ? 157 VAL A C   1 
ATOM   1147 O O   . VAL A 1 155 ? -12.13000 18.97200  -19.81600 1.000 36.54000 ? 157 VAL A O   1 
ATOM   1148 C CB  . VAL A 1 155 ? -11.61400 17.39700  -17.44300 1.000 34.92000 ? 157 VAL A CB  1 
ATOM   1149 C CG1 . VAL A 1 155 ? -11.65200 16.02600  -18.02200 1.000 30.22000 ? 157 VAL A CG1 1 
ATOM   1150 C CG2 . VAL A 1 155 ? -11.36500 17.35300  -15.96500 1.000 32.94000 ? 157 VAL A CG2 1 
ATOM   1151 N N   . SER A 1 156 ? -10.46700 17.81800  -20.52300 1.000 30.75000 ? 158 SER A N   1 
ATOM   1152 C CA  . SER A 1 156 ? -10.89900 17.76700  -21.88500 1.000 35.17000 ? 158 SER A CA  1 
ATOM   1153 C C   . SER A 1 156 ? -11.40800 16.40300  -22.20300 1.000 32.30000 ? 158 SER A C   1 
ATOM   1154 O O   . SER A 1 156 ? -10.67300 15.52400  -22.15900 1.000 31.94000 ? 158 SER A O   1 
ATOM   1155 C CB  . SER A 1 156 ? -9.74600  17.97900  -22.79800 1.000 34.76000 ? 158 SER A CB  1 
ATOM   1156 O OG  . SER A 1 156 ? -9.37100  19.25000  -22.75200 1.000 45.10000 ? 158 SER A OG  1 
ATOM   1157 N N   . PHE A 1 157 ? -12.65400 16.26200  -22.57800 1.000 28.58000 ? 159 PHE A N   1 
ATOM   1158 C CA  . PHE A 1 157 ? -13.20800 15.00200  -22.92400 1.000 28.13000 ? 159 PHE A CA  1 
ATOM   1159 C C   . PHE A 1 157 ? -13.05400 14.81800  -24.42400 1.000 31.21000 ? 159 PHE A C   1 
ATOM   1160 O O   . PHE A 1 157 ? -13.57200 15.54300  -25.18300 1.000 31.11000 ? 159 PHE A O   1 
ATOM   1161 C CB  . PHE A 1 157 ? -14.65600 14.89500  -22.48600 1.000 28.88000 ? 159 PHE A CB  1 
ATOM   1162 C CG  . PHE A 1 157 ? -14.85300 14.86800  -21.01200 1.000 30.44000 ? 159 PHE A CG  1 
ATOM   1163 C CD1 . PHE A 1 157 ? -14.72400 13.72900  -20.31900 1.000 28.15000 ? 159 PHE A CD1 1 
ATOM   1164 C CD2 . PHE A 1 157 ? -15.15300 15.98000  -20.33500 1.000 29.81000 ? 159 PHE A CD2 1 
ATOM   1165 C CE1 . PHE A 1 157 ? -14.90200 13.69500  -18.98700 1.000 27.65000 ? 159 PHE A CE1 1 
ATOM   1166 C CE2 . PHE A 1 157 ? -15.34300 15.94800  -19.00100 1.000 26.49000 ? 159 PHE A CE2 1 
ATOM   1167 C CZ  . PHE A 1 157 ? -15.20300 14.80200  -18.33100 1.000 29.35000 ? 159 PHE A CZ  1 
ATOM   1168 N N   . CYS A 1 158 ? -12.30400 13.82600  -24.80200 1.000 26.24000 ? 160 CYS A N   1 
ATOM   1169 C CA  . CYS A 1 158 ? -12.03700 13.54700  -26.17400 1.000 30.67000 ? 160 CYS A CA  1 
ATOM   1170 C C   . CYS A 1 158 ? -12.55600 12.28300  -26.79800 1.000 29.54000 ? 160 CYS A C   1 
ATOM   1171 O O   . CYS A 1 158 ? -12.50100 12.14700  -27.94200 1.000 29.80000 ? 160 CYS A O   1 
ATOM   1172 C CB  . CYS A 1 158 ? -10.53200 13.59100  -26.38700 1.000 28.97000 ? 160 CYS A CB  1 
ATOM   1173 S SG  . CYS A 1 158 ? -9.60500  12.29300  -25.63600 1.000 34.17000 ? 160 CYS A SG  1 
ATOM   1174 N N   . TYR A 1 159 ? -13.06700 11.38100  -26.01100 1.000 28.30000 ? 161 TYR A N   1 
ATOM   1175 C CA  . TYR A 1 159 ? -13.44800 10.06900  -26.50800 1.000 27.45000 ? 161 TYR A CA  1 
ATOM   1176 C C   . TYR A 1 159 ? -14.56900 9.50500   -25.65700 1.000 26.20000 ? 161 TYR A C   1 
ATOM   1177 O O   . TYR A 1 159 ? -14.55900 9.65500   -24.43200 1.000 23.74000 ? 161 TYR A O   1 
ATOM   1178 C CB  . TYR A 1 159 ? -12.23400 9.12000   -26.47700 1.000 24.01000 ? 161 TYR A CB  1 
ATOM   1179 C CG  . TYR A 1 159 ? -12.52000 7.69900   -26.90000 1.000 25.94000 ? 161 TYR A CG  1 
ATOM   1180 C CD1 . TYR A 1 159 ? -12.58900 7.35700   -28.24600 1.000 26.61000 ? 161 TYR A CD1 1 
ATOM   1181 C CD2 . TYR A 1 159 ? -12.71700 6.69900   -25.96200 1.000 26.87000 ? 161 TYR A CD2 1 
ATOM   1182 C CE1 . TYR A 1 159 ? -12.84000 6.04900   -28.64900 1.000 27.34000 ? 161 TYR A CE1 1 
ATOM   1183 C CE2 . TYR A 1 159 ? -12.97600 5.36700   -26.36000 1.000 24.96000 ? 161 TYR A CE2 1 
ATOM   1184 C CZ  . TYR A 1 159 ? -13.02400 5.05900   -27.70100 1.000 28.36000 ? 161 TYR A CZ  1 
ATOM   1185 O OH  . TYR A 1 159 ? -13.27900 3.76400   -28.11700 1.000 31.83000 ? 161 TYR A OH  1 
ATOM   1186 N N   . MET A 1 160 ? -15.48400 8.80800   -26.27700 1.000 26.32000 ? 162 MET A N   1 
ATOM   1187 C CA  . MET A 1 160 ? -16.48400 8.02700   -25.62000 1.000 25.14000 ? 162 MET A CA  1 
ATOM   1188 C C   . MET A 1 160 ? -16.52500 6.63900   -26.26400 1.000 26.45000 ? 162 MET A C   1 
ATOM   1189 O O   . MET A 1 160 ? -16.65400 6.53700   -27.41900 1.000 25.24000 ? 162 MET A O   1 
ATOM   1190 C CB  . MET A 1 160 ? -17.85500 8.66600   -25.54600 1.000 26.36000 ? 162 MET A CB  1 
ATOM   1191 C CG  . MET A 1 160 ? -18.93200 7.72000   -25.08600 1.000 26.75000 ? 162 MET A CG  1 
ATOM   1192 S SD  . MET A 1 160 ? -20.51900 8.37900   -24.67700 1.000 31.88000 ? 162 MET A SD  1 
ATOM   1193 C CE  . MET A 1 160 ? -20.27600 9.17700   -23.16300 1.000 29.46000 ? 162 MET A CE  1 
ATOM   1194 N N   . HIS A 1 161 ? -16.43300 5.60600   -25.48900 1.000 24.97000 ? 163 HIS A N   1 
ATOM   1195 C CA  . HIS A 1 161 ? -16.44100 4.26600   -26.00100 1.000 29.84000 ? 163 HIS A CA  1 
ATOM   1196 C C   . HIS A 1 161 ? -17.79700 3.74600   -26.47000 1.000 31.88000 ? 163 HIS A C   1 
ATOM   1197 O O   . HIS A 1 161 ? -18.72800 3.83200   -25.78900 1.000 27.94000 ? 163 HIS A O   1 
ATOM   1198 C CB  . HIS A 1 161 ? -15.82700 3.32000   -25.01300 1.000 29.03000 ? 163 HIS A CB  1 
ATOM   1199 C CG  . HIS A 1 161 ? -15.69500 1.93900   -25.51500 1.000 34.78000 ? 163 HIS A CG  1 
ATOM   1200 N ND1 . HIS A 1 161 ? -14.95400 1.62300   -26.61000 1.000 36.61000 ? 163 HIS A ND1 1 
ATOM   1201 C CD2 . HIS A 1 161 ? -16.20900 0.78600   -25.07500 1.000 39.31000 ? 163 HIS A CD2 1 
ATOM   1202 C CE1 . HIS A 1 161 ? -15.01200 0.33900   -26.82000 1.000 36.79000 ? 163 HIS A CE1 1 
ATOM   1203 N NE2 . HIS A 1 161 ? -15.76200 -0.19500  -25.90000 1.000 38.80000 ? 163 HIS A NE2 1 
ATOM   1204 N N   . HIS A 1 162 ? -17.84600 3.20400   -27.66900 1.000 31.44000 ? 164 HIS A N   1 
ATOM   1205 C CA  . HIS A 1 162 ? -19.05200 2.63200   -28.23700 1.000 34.10000 ? 164 HIS A CA  1 
ATOM   1206 C C   . HIS A 1 162 ? -18.96800 1.14600   -28.49500 1.000 41.55000 ? 164 HIS A C   1 
ATOM   1207 O O   . HIS A 1 162 ? -19.82700 0.48100   -28.09900 1.000 43.29000 ? 164 HIS A O   1 
ATOM   1208 C CB  . HIS A 1 162 ? -19.53300 3.31200   -29.49900 1.000 29.74000 ? 164 HIS A CB  1 
ATOM   1209 C CG  . HIS A 1 162 ? -20.25300 4.61000   -29.30900 1.000 31.21000 ? 164 HIS A CG  1 
ATOM   1210 N ND1 . HIS A 1 162 ? -19.65000 5.73900   -28.84100 1.000 28.72000 ? 164 HIS A ND1 1 
ATOM   1211 C CD2 . HIS A 1 162 ? -21.49100 4.98300   -29.66000 1.000 25.10000 ? 164 HIS A CD2 1 
ATOM   1212 C CE1 . HIS A 1 162 ? -20.50800 6.72800   -28.84900 1.000 27.89000 ? 164 HIS A CE1 1 
ATOM   1213 N NE2 . HIS A 1 162 ? -21.63600 6.28500   -29.32500 1.000 23.02000 ? 164 HIS A NE2 1 
ATOM   1214 N N   . MET A 1 163 ? -17.95000 0.64100   -29.16000 1.000 36.49000 ? 165 MET A N   1 
ATOM   1215 C CA  . MET A 1 163 ? -17.86700 -0.77800  -29.45300 1.000 39.68000 ? 165 MET A CA  1 
ATOM   1216 C C   . MET A 1 163 ? -16.54700 -1.39900  -29.69800 1.000 38.71000 ? 165 MET A C   1 
ATOM   1217 O O   . MET A 1 163 ? -15.62300 -0.73500  -29.95400 1.000 38.80000 ? 165 MET A O   1 
ATOM   1218 C CB  . MET A 1 163 ? -18.60300 -1.06200  -30.69900 1.000 44.91000 ? 165 MET A CB  1 
ATOM   1219 C CG  . MET A 1 163 ? -18.19900 -0.11800  -31.75500 1.000 42.07000 ? 165 MET A CG  1 
ATOM   1220 S SD  . MET A 1 163 ? -19.50400 0.29500   -32.81600 1.000 62.34000 ? 165 MET A SD  1 
ATOM   1221 C CE  . MET A 1 163 ? -20.95900 0.08900   -31.80200 1.000 49.46000 ? 165 MET A CE  1 
ATOM   1222 N N   . GLU A 1 164 ? -16.51200 -2.70900  -29.61400 1.000 39.30000 ? 166 GLU A N   1 
ATOM   1223 C CA  . GLU A 1 164 ? -15.31200 -3.49900  -29.85200 1.000 45.35000 ? 166 GLU A CA  1 
ATOM   1224 C C   . GLU A 1 164 ? -15.37700 -4.06500  -31.26500 1.000 47.77000 ? 166 GLU A C   1 
ATOM   1225 O O   . GLU A 1 164 ? -16.41100 -4.59800  -31.67300 1.000 42.20000 ? 166 GLU A O   1 
ATOM   1226 C CB  . GLU A 1 164 ? -15.17500 -4.63300  -28.83200 1.000 46.76000 ? 166 GLU A CB  1 
ATOM   1227 N N   . LEU A 1 165 ? -14.27700 -3.92200  -32.01900 1.000 43.76000 ? 167 LEU A N   1 
ATOM   1228 C CA  . LEU A 1 165 ? -14.20300 -4.44700  -33.37000 1.000 44.95000 ? 167 LEU A CA  1 
ATOM   1229 C C   . LEU A 1 165 ? -13.82000 -5.91700  -33.33800 1.000 48.27000 ? 167 LEU A C   1 
ATOM   1230 O O   . LEU A 1 165 ? -13.35800 -6.42200  -32.30900 1.000 47.95000 ? 167 LEU A O   1 
ATOM   1231 C CB  . LEU A 1 165 ? -13.20100 -3.63800  -34.18600 1.000 44.70000 ? 167 LEU A CB  1 
ATOM   1232 C CG  . LEU A 1 165 ? -13.69400 -2.20400  -34.35700 1.000 43.68000 ? 167 LEU A CG  1 
ATOM   1233 C CD1 . LEU A 1 165 ? -12.66200 -1.34900  -35.07600 1.000 43.32000 ? 167 LEU A CD1 1 
ATOM   1234 C CD2 . LEU A 1 165 ? -15.04500 -2.17500  -35.06500 1.000 43.50000 ? 167 LEU A CD2 1 
ATOM   1235 N N   . PRO A 1 166 ? -14.03000 -6.65100  -34.43600 1.000 53.37000 ? 168 PRO A N   1 
ATOM   1236 C CA  . PRO A 1 166 ? -13.75100 -8.09600  -34.40600 1.000 54.55000 ? 168 PRO A CA  1 
ATOM   1237 C C   . PRO A 1 166 ? -12.30700 -8.43000  -34.08100 1.000 59.81000 ? 168 PRO A C   1 
ATOM   1238 O O   . PRO A 1 166 ? -12.03700 -9.53200  -33.58400 1.000 60.58000 ? 168 PRO A O   1 
ATOM   1239 C CB  . PRO A 1 166 ? -14.13700 -8.56100  -35.81500 1.000 57.65000 ? 168 PRO A CB  1 
ATOM   1240 C CG  . PRO A 1 166 ? -15.16600 -7.55900  -36.27300 1.000 57.18000 ? 168 PRO A CG  1 
ATOM   1241 C CD  . PRO A 1 166 ? -14.73000 -6.25000  -35.67700 1.000 55.30000 ? 168 PRO A CD  1 
ATOM   1242 N N   . THR A 1 167 ? -11.37500 -7.51200  -34.32100 1.000 50.51000 ? 169 THR A N   1 
ATOM   1243 C CA  . THR A 1 167 ? -9.97700  -7.78700  -34.04900 1.000 55.52000 ? 169 THR A CA  1 
ATOM   1244 C C   . THR A 1 167 ? -9.57800  -7.49300  -32.61000 1.000 55.13000 ? 169 THR A C   1 
ATOM   1245 O O   . THR A 1 167 ? -8.39000  -7.58500  -32.28900 1.000 55.97000 ? 169 THR A O   1 
ATOM   1246 C CB  . THR A 1 167 ? -9.10600  -6.98500  -35.01000 1.000 59.65000 ? 169 THR A CB  1 
ATOM   1247 O OG1 . THR A 1 167 ? -7.72900  -7.20000  -34.69100 1.000 61.98000 ? 169 THR A OG1 1 
ATOM   1248 C CG2 . THR A 1 167 ? -9.44900  -5.50200  -34.91900 1.000 55.20000 ? 169 THR A CG2 1 
ATOM   1249 N N   . GLY A 1 168 ? -10.52200 -7.14100  -31.77300 1.000 56.04000 ? 170 GLY A N   1 
ATOM   1250 C CA  . GLY A 1 168 ? -10.27600 -6.82000  -30.38600 1.000 53.99000 ? 170 GLY A CA  1 
ATOM   1251 C C   . GLY A 1 168 ? -10.07900 -5.36600  -30.00300 1.000 50.66000 ? 170 GLY A C   1 
ATOM   1252 O O   . GLY A 1 168 ? -10.08900 -5.04500  -28.87400 1.000 57.73000 ? 170 GLY A O   1 
ATOM   1253 N N   . VAL A 1 169 ? -9.92100  -4.50500  -30.96300 1.000 48.16000 ? 171 VAL A N   1 
ATOM   1254 C CA  . VAL A 1 169 ? -9.75600  -3.11400  -30.72200 1.000 47.63000 ? 171 VAL A CA  1 
ATOM   1255 C C   . VAL A 1 169 ? -11.08400 -2.41500  -30.52600 1.000 45.17000 ? 171 VAL A C   1 
ATOM   1256 O O   . VAL A 1 169 ? -12.09800 -2.99000  -30.67700 1.000 41.49000 ? 171 VAL A O   1 
ATOM   1257 C CB  . VAL A 1 169 ? -8.88500  -2.52000  -31.76900 1.000 41.88000 ? 171 VAL A CB  1 
ATOM   1258 C CG1 . VAL A 1 169 ? -7.57200  -3.24000  -31.74300 1.000 46.62000 ? 171 VAL A CG1 1 
ATOM   1259 C CG2 . VAL A 1 169 ? -9.52900  -2.66800  -33.09900 1.000 41.69000 ? 171 VAL A CG2 1 
ATOM   1260 N N   . HIS A 1 170 ? -11.02300 -1.17000  -30.15300 1.000 40.72000 ? 172 HIS A N   1 
ATOM   1261 C CA  . HIS A 1 170 ? -12.17600 -0.37800  -29.83900 1.000 38.69000 ? 172 HIS A CA  1 
ATOM   1262 C C   . HIS A 1 170 ? -12.39400 0.86000   -30.66800 1.000 36.05000 ? 172 HIS A C   1 
ATOM   1263 O O   . HIS A 1 170 ? -11.49400 1.43700   -31.10100 1.000 33.28000 ? 172 HIS A O   1 
ATOM   1264 C CB  . HIS A 1 170 ? -12.08900 -0.03000  -28.39700 1.000 42.56000 ? 172 HIS A CB  1 
ATOM   1265 C CG  . HIS A 1 170 ? -11.89400 -1.22200  -27.53300 1.000 47.16000 ? 172 HIS A CG  1 
ATOM   1266 N ND1 . HIS A 1 170 ? -10.67300 -1.59900  -27.05700 1.000 51.91000 ? 172 HIS A ND1 1 
ATOM   1267 C CD2 . HIS A 1 170 ? -12.75600 -2.17400  -27.13500 1.000 48.72000 ? 172 HIS A CD2 1 
ATOM   1268 C CE1 . HIS A 1 170 ? -10.79800 -2.69500  -26.35100 1.000 52.95000 ? 172 HIS A CE1 1 
ATOM   1269 N NE2 . HIS A 1 170 ? -12.05300 -3.06700  -26.39200 1.000 54.54000 ? 172 HIS A NE2 1 
ATOM   1270 N N   . ALA A 1 171 ? -13.64500 1.19800   -30.88700 1.000 32.31000 ? 173 ALA A N   1 
ATOM   1271 C CA  . ALA A 1 171 ? -14.08600 2.32400   -31.68000 1.000 29.84000 ? 173 ALA A CA  1 
ATOM   1272 C C   . ALA A 1 171 ? -15.04300 3.20600   -30.91200 1.000 28.66000 ? 173 ALA A C   1 
ATOM   1273 O O   . ALA A 1 171 ? -15.73600 2.71700   -30.09700 1.000 27.99000 ? 173 ALA A O   1 
ATOM   1274 C CB  . ALA A 1 171 ? -14.71600 1.84200   -32.94800 1.000 28.81000 ? 173 ALA A CB  1 
ATOM   1275 N N   . GLY A 1 172 ? -15.05600 4.48900   -31.18100 1.000 24.37000 ? 174 GLY A N   1 
ATOM   1276 C CA  . GLY A 1 172 ? -15.95800 5.37200   -30.46100 1.000 26.43000 ? 174 GLY A CA  1 
ATOM   1277 C C   . GLY A 1 172 ? -15.98400 6.75600   -31.06800 1.000 28.60000 ? 174 GLY A C   1 
ATOM   1278 O O   . GLY A 1 172 ? -15.45900 6.98500   -32.16000 1.000 28.66000 ? 174 GLY A O   1 
ATOM   1279 N N   . THR A 1 173 ? -16.58800 7.68700   -30.33400 1.000 25.79000 ? 175 THR A N   1 
ATOM   1280 C CA  . THR A 1 173 ? -16.89500 9.02000   -30.84100 1.000 25.03000 ? 175 THR A CA  1 
ATOM   1281 C C   . THR A 1 173 ? -16.23800 10.08200  -29.97900 1.000 25.30000 ? 175 THR A C   1 
ATOM   1282 O O   . THR A 1 173 ? -15.72400 9.79700   -28.90000 1.000 26.47000 ? 175 THR A O   1 
ATOM   1283 C CB  . THR A 1 173 ? -18.41300 9.26700   -30.85200 1.000 27.11000 ? 175 THR A CB  1 
ATOM   1284 O OG1 . THR A 1 173 ? -18.85900 9.47500   -29.50100 1.000 27.03000 ? 175 THR A OG1 1 
ATOM   1285 C CG2 . THR A 1 173 ? -19.12200 8.07600   -31.43300 1.000 23.83000 ? 175 THR A CG2 1 
ATOM   1286 N N   . ASP A 1 174 ? -16.27300 11.32300  -30.46100 1.000 27.30000 ? 176 ASP A N   1 
ATOM   1287 C CA  . ASP A 1 174 ? -16.03700 12.44600  -29.56700 1.000 28.19000 ? 176 ASP A CA  1 
ATOM   1288 C C   . ASP A 1 174 ? -17.31400 12.72000  -28.77400 1.000 28.58000 ? 176 ASP A C   1 
ATOM   1289 O O   . ASP A 1 174 ? -18.32200 12.01200  -28.90200 1.000 27.42000 ? 176 ASP A O   1 
ATOM   1290 C CB  . ASP A 1 174 ? -15.53800 13.67000  -30.35000 1.000 29.87000 ? 176 ASP A CB  1 
ATOM   1291 C CG  . ASP A 1 174 ? -16.53300 14.16000  -31.39800 1.000 32.00000 ? 176 ASP A CG  1 
ATOM   1292 O OD1 . ASP A 1 174 ? -17.75200 13.92900  -31.25300 1.000 29.53000 ? 176 ASP A OD1 1 
ATOM   1293 O OD2 . ASP A 1 174 ? -16.08700 14.80600  -32.36600 1.000 32.34000 ? 176 ASP A OD2 1 
ATOM   1294 N N   . LEU A 1 175 ? -17.28500 13.73100  -27.91200 1.000 28.49000 ? 177 LEU A N   1 
ATOM   1295 C CA  . LEU A 1 175 ? -18.45900 13.94900  -27.06600 1.000 29.01000 ? 177 LEU A CA  1 
ATOM   1296 C C   . LEU A 1 175 ? -19.56700 14.68700  -27.80300 1.000 30.40000 ? 177 LEU A C   1 
ATOM   1297 O O   . LEU A 1 175 ? -20.62900 14.93500  -27.22200 1.000 32.50000 ? 177 LEU A O   1 
ATOM   1298 C CB  . LEU A 1 175 ? -18.07000 14.69800  -25.78800 1.000 30.26000 ? 177 LEU A CB  1 
ATOM   1299 C CG  . LEU A 1 175 ? -17.69200 13.80200  -24.60600 1.000 29.47000 ? 177 LEU A CG  1 
ATOM   1300 C CD1 . LEU A 1 175 ? -18.87300 12.91200  -24.27900 1.000 29.44000 ? 177 LEU A CD1 1 
ATOM   1301 C CD2 . LEU A 1 175 ? -16.47800 12.94500  -24.95900 1.000 25.81000 ? 177 LEU A CD2 1 
ATOM   1302 N N   . GLU A 1 176 ? -19.35000 15.04100  -29.06400 1.000 32.63000 ? 178 GLU A N   1 
ATOM   1303 C CA  . GLU A 1 176 ? -20.43400 15.47700  -29.93200 1.000 33.52000 ? 178 GLU A CA  1 
ATOM   1304 C C   . GLU A 1 176 ? -21.01500 14.32900  -30.72900 1.000 31.14000 ? 178 GLU A C   1 
ATOM   1305 O O   . GLU A 1 176 ? -21.77000 14.56700  -31.67300 1.000 35.06000 ? 178 GLU A O   1 
ATOM   1306 C CB  . GLU A 1 176 ? -19.94900 16.57900  -30.87500 1.000 36.62000 ? 178 GLU A CB  1 
ATOM   1307 C CG  . GLU A 1 176 ? -19.80100 17.93300  -30.18900 1.000 42.35000 ? 178 GLU A CG  1 
ATOM   1308 C CD  . GLU A 1 176 ? -19.32200 19.01900  -31.14100 1.000 51.27000 ? 178 GLU A CD  1 
ATOM   1309 O OE1 . GLU A 1 176 ? -18.99500 20.12800  -30.67100 1.000 57.78000 ? 178 GLU A OE1 1 
ATOM   1310 O OE2 . GLU A 1 176 ? -19.27900 18.76400  -32.36300 1.000 53.36000 ? 178 GLU A OE2 1 
ATOM   1311 N N   . GLY A 1 177 ? -20.65900 13.08900  -30.40300 1.000 28.12000 ? 179 GLY A N   1 
ATOM   1312 C CA  . GLY A 1 177 ? -21.29100 11.95700  -31.06000 1.000 29.90000 ? 179 GLY A CA  1 
ATOM   1313 C C   . GLY A 1 177 ? -20.76500 11.57700  -32.43000 1.000 29.29000 ? 179 GLY A C   1 
ATOM   1314 O O   . GLY A 1 177 ? -21.31200 10.65200  -33.03800 1.000 27.93000 ? 179 GLY A O   1 
ATOM   1315 N N   . ASN A 1 178 ? -19.70900 12.23000  -32.92700 1.000 29.31000 ? 180 ASN A N   1 
ATOM   1316 C CA  . ASN A 1 178 ? -19.12700 11.89600  -34.23000 1.000 28.35000 ? 180 ASN A CA  1 
ATOM   1317 C C   . ASN A 1 178 ? -18.03500 10.85100  -34.06400 1.000 27.42000 ? 180 ASN A C   1 
ATOM   1318 O O   . ASN A 1 178 ? -17.06600 11.06700  -33.32400 1.000 27.62000 ? 180 ASN A O   1 
ATOM   1319 C CB  . ASN A 1 178 ? -18.56000 13.14100  -34.90700 1.000 30.31000 ? 180 ASN A CB  1 
ATOM   1320 C CG  . ASN A 1 178 ? -19.65500 14.06200  -35.41000 1.000 31.86000 ? 180 ASN A CG  1 
ATOM   1321 O OD1 . ASN A 1 178 ? -20.59700 13.60700  -36.03700 1.000 36.42000 ? 180 ASN A OD1 1 
ATOM   1322 N ND2 . ASN A 1 178 ? -19.55400 15.34200  -35.09600 1.000 32.21000 ? 180 ASN A ND2 1 
ATOM   1323 N N   . PHE A 1 179 ? -18.17100 9.74300   -34.78500 1.000 28.18000 ? 181 PHE A N   1 
ATOM   1324 C CA  . PHE A 1 179 ? -17.24200 8.63300   -34.65400 1.000 29.53000 ? 181 PHE A CA  1 
ATOM   1325 C C   . PHE A 1 179 ? -15.83900 9.03900   -35.08200 1.000 28.33000 ? 181 PHE A C   1 
ATOM   1326 O O   . PHE A 1 179 ? -15.64700 9.91500   -35.93500 1.000 26.07000 ? 181 PHE A O   1 
ATOM   1327 C CB  . PHE A 1 179 ? -17.71200 7.43800   -35.48600 1.000 27.18000 ? 181 PHE A CB  1 
ATOM   1328 C CG  . PHE A 1 179 ? -18.39300 6.37500   -34.67900 1.000 30.33000 ? 181 PHE A CG  1 
ATOM   1329 C CD1 . PHE A 1 179 ? -17.65000 5.38400   -34.04200 1.000 28.57000 ? 181 PHE A CD1 1 
ATOM   1330 C CD2 . PHE A 1 179 ? -19.78900 6.36900   -34.54700 1.000 30.04000 ? 181 PHE A CD2 1 
ATOM   1331 C CE1 . PHE A 1 179 ? -18.27100 4.39400   -33.29700 1.000 29.13000 ? 181 PHE A CE1 1 
ATOM   1332 C CE2 . PHE A 1 179 ? -20.42000 5.39500   -33.79700 1.000 29.20000 ? 181 PHE A CE2 1 
ATOM   1333 C CZ  . PHE A 1 179 ? -19.66200 4.39100   -33.17400 1.000 30.47000 ? 181 PHE A CZ  1 
ATOM   1334 N N   . TYR A 1 180 ? -14.84500 8.41600   -34.45500 1.000 28.30000 ? 182 TYR A N   1 
ATOM   1335 C CA  . TYR A 1 180 ? -13.48600 8.47200   -34.97100 1.000 31.09000 ? 182 TYR A CA  1 
ATOM   1336 C C   . TYR A 1 180 ? -13.36100 7.36100   -36.00400 1.000 29.07000 ? 182 TYR A C   1 
ATOM   1337 O O   . TYR A 1 180 ? -13.72000 6.21200   -35.72300 1.000 28.26000 ? 182 TYR A O   1 
ATOM   1338 C CB  . TYR A 1 180 ? -12.43800 8.30700   -33.85400 1.000 28.63000 ? 182 TYR A CB  1 
ATOM   1339 C CG  . TYR A 1 180 ? -12.33400 9.49900   -32.90900 1.000 31.15000 ? 182 TYR A CG  1 
ATOM   1340 C CD1 . TYR A 1 180 ? -11.57900 10.61100  -33.25400 1.000 31.39000 ? 182 TYR A CD1 1 
ATOM   1341 C CD2 . TYR A 1 180 ? -12.98700 9.50700   -31.67300 1.000 26.30000 ? 182 TYR A CD2 1 
ATOM   1342 C CE1 . TYR A 1 180 ? -11.46800 11.70400  -32.40600 1.000 32.43000 ? 182 TYR A CE1 1 
ATOM   1343 C CE2 . TYR A 1 180 ? -12.89100 10.60000  -30.81400 1.000 27.35000 ? 182 TYR A CE2 1 
ATOM   1344 C CZ  . TYR A 1 180 ? -12.12700 11.69800  -31.18900 1.000 30.83000 ? 182 TYR A CZ  1 
ATOM   1345 O OH  . TYR A 1 180 ? -11.99900 12.79600  -30.36400 1.000 27.77000 ? 182 TYR A OH  1 
ATOM   1346 N N   . GLY A 1 181 ? -12.87500 7.70300   -37.19600 1.000 30.29000 ? 183 GLY A N   1 
ATOM   1347 C CA  . GLY A 1 181 ? -12.72100 6.72600   -38.25000 1.000 31.72000 ? 183 GLY A CA  1 
ATOM   1348 C C   . GLY A 1 181 ? -14.02500 6.39000   -38.95200 1.000 36.46000 ? 183 GLY A C   1 
ATOM   1349 O O   . GLY A 1 181 ? -15.07600 6.98800   -38.69600 1.000 36.23000 ? 183 GLY A O   1 
ATOM   1350 N N   . PRO A 1 182 ? -13.98500 5.39800   -39.83500 1.000 35.53000 ? 184 PRO A N   1 
ATOM   1351 C CA  . PRO A 1 182 ? -15.15600 5.10900   -40.67300 1.000 36.48000 ? 184 PRO A CA  1 
ATOM   1352 C C   . PRO A 1 182 ? -16.16200 4.16700   -40.02500 1.000 39.33000 ? 184 PRO A C   1 
ATOM   1353 O O   . PRO A 1 182 ? -16.87900 3.44800   -40.72000 1.000 43.88000 ? 184 PRO A O   1 
ATOM   1354 C CB  . PRO A 1 182 ? -14.52700 4.48200   -41.92100 1.000 35.15000 ? 184 PRO A CB  1 
ATOM   1355 C CG  . PRO A 1 182 ? -13.31100 3.76700   -41.38800 1.000 34.60000 ? 184 PRO A CG  1 
ATOM   1356 C CD  . PRO A 1 182 ? -12.81000 4.58900   -40.21000 1.000 35.55000 ? 184 PRO A CD  1 
ATOM   1357 N N   . PHE A 1 183 ? -16.25400 4.16300   -38.70400 1.000 38.27000 ? 185 PHE A N   1 
ATOM   1358 C CA  . PHE A 1 183 ? -17.08800 3.18000   -38.03500 1.000 35.20000 ? 185 PHE A CA  1 
ATOM   1359 C C   . PHE A 1 183 ? -18.49200 3.74400   -37.76200 1.000 35.66000 ? 185 PHE A C   1 
ATOM   1360 O O   . PHE A 1 183 ? -18.72700 4.95500   -37.81300 1.000 34.75000 ? 185 PHE A O   1 
ATOM   1361 C CB  . PHE A 1 183 ? -16.36800 2.70300   -36.77300 1.000 34.15000 ? 185 PHE A CB  1 
ATOM   1362 C CG  . PHE A 1 183 ? -14.92900 2.27500   -37.03700 1.000 36.46000 ? 185 PHE A CG  1 
ATOM   1363 C CD1 . PHE A 1 183 ? -14.65800 1.12900   -37.78500 1.000 37.61000 ? 185 PHE A CD1 1 
ATOM   1364 C CD2 . PHE A 1 183 ? -13.85300 3.03200   -36.57300 1.000 33.26000 ? 185 PHE A CD2 1 
ATOM   1365 C CE1 . PHE A 1 183 ? -13.34500 0.72500   -38.05200 1.000 38.36000 ? 185 PHE A CE1 1 
ATOM   1366 C CE2 . PHE A 1 183 ? -12.53100 2.63700   -36.83300 1.000 32.99000 ? 185 PHE A CE2 1 
ATOM   1367 C CZ  . PHE A 1 183 ? -12.27600 1.47800   -37.57200 1.000 33.54000 ? 185 PHE A CZ  1 
ATOM   1368 N N   . VAL A 1 184 ? -19.44200 2.84000   -37.56600 1.000 32.53000 ? 186 VAL A N   1 
ATOM   1369 C CA  . VAL A 1 184 ? -20.83900 3.19600   -37.31900 1.000 34.95000 ? 186 VAL A CA  1 
ATOM   1370 C C   . VAL A 1 184 ? -21.32800 2.38800   -36.12600 1.000 36.26000 ? 186 VAL A C   1 
ATOM   1371 O O   . VAL A 1 184 ? -20.86400 1.27000   -35.89600 1.000 35.95000 ? 186 VAL A O   1 
ATOM   1372 C CB  . VAL A 1 184 ? -21.73200 2.93300   -38.55900 1.000 37.38000 ? 186 VAL A CB  1 
ATOM   1373 C CG1 . VAL A 1 184 ? -21.43200 3.93300   -39.67700 1.000 40.16000 ? 186 VAL A CG1 1 
ATOM   1374 C CG2 . VAL A 1 184 ? -21.53800 1.50100   -39.05700 1.000 34.71000 ? 186 VAL A CG2 1 
ATOM   1375 N N   . ASP A 1 185 ? -22.31400 2.90200   -35.40600 1.000 35.51000 ? 187 ASP A N   1 
ATOM   1376 C CA  . ASP A 1 185 ? -22.93900 2.21900   -34.28300 1.000 39.42000 ? 187 ASP A CA  1 
ATOM   1377 C C   . ASP A 1 185 ? -24.01800 1.24100   -34.75300 1.000 38.24000 ? 187 ASP A C   1 
ATOM   1378 O O   . ASP A 1 185 ? -25.15000 1.40500   -34.51300 1.000 35.47000 ? 187 ASP A O   1 
ATOM   1379 C CB  . ASP A 1 185 ? -23.47200 3.17000   -33.20400 1.000 35.72000 ? 187 ASP A CB  1 
ATOM   1380 C CG  . ASP A 1 185 ? -24.36600 4.24300   -33.72300 1.000 34.17000 ? 187 ASP A CG  1 
ATOM   1381 O OD1 . ASP A 1 185 ? -24.52300 4.45000   -34.87900 1.000 34.03000 ? 187 ASP A OD1 1 
ATOM   1382 O OD2 . ASP A 1 185 ? -24.89000 4.91700   -32.93300 1.000 31.09000 ? 187 ASP A OD2 1 
ATOM   1383 N N   . ARG A 1 186 ? -23.57000 0.21200   -35.42800 1.000 39.63000 ? 188 ARG A N   1 
ATOM   1384 C CA  . ARG A 1 186 ? -24.35900 -0.80100  -36.00100 1.000 41.01000 ? 188 ARG A CA  1 
ATOM   1385 C C   . ARG A 1 186 ? -23.50400 -2.03000  -36.03300 1.000 44.28000 ? 188 ARG A C   1 
ATOM   1386 O O   . ARG A 1 186 ? -22.36900 -1.94100  -36.23000 1.000 44.91000 ? 188 ARG A O   1 
ATOM   1387 C CB  . ARG A 1 186 ? -24.63800 -0.33600  -37.41900 1.000 42.83000 ? 188 ARG A CB  1 
ATOM   1388 C CG  . ARG A 1 186 ? -25.42600 -1.22000  -38.33100 1.000 42.96000 ? 188 ARG A CG  1 
ATOM   1389 C CD  . ARG A 1 186 ? -25.65900 -0.60700  -39.69200 1.000 36.41000 ? 188 ARG A CD  1 
ATOM   1390 N NE  . ARG A 1 186 ? -26.15000 -1.62600  -40.58300 1.000 42.89000 ? 188 ARG A NE  1 
ATOM   1391 C CZ  . ARG A 1 186 ? -25.95700 -1.70800  -41.87800 1.000 37.43000 ? 188 ARG A CZ  1 
ATOM   1392 N NH1 . ARG A 1 186 ? -25.28900 -0.81900  -42.51800 1.000 36.28000 ? 188 ARG A NH1 1 
ATOM   1393 N NH2 . ARG A 1 186 ? -26.47100 -2.68500  -42.50200 1.000 36.69000 ? 188 ARG A NH2 1 
ATOM   1394 N N   . GLN A 1 187 ? -24.08600 -3.18700  -35.87400 1.000 46.65000 ? 189 GLN A N   1 
ATOM   1395 C CA  . GLN A 1 187 ? -23.36800 -4.42900  -35.91900 1.000 47.29000 ? 189 GLN A CA  1 
ATOM   1396 C C   . GLN A 1 187 ? -23.23200 -4.99300  -37.32000 1.000 48.99000 ? 189 GLN A C   1 
ATOM   1397 O O   . GLN A 1 187 ? -23.91500 -5.84400  -37.68800 1.000 55.59000 ? 189 GLN A O   1 
ATOM   1398 C CB  . GLN A 1 187 ? -24.03500 -5.45200  -35.02400 1.000 50.76000 ? 189 GLN A CB  1 
ATOM   1399 N N   . THR A 1 188 ? -22.32600 -4.46500  -38.08400 1.000 52.35000 ? 190 THR A N   1 
ATOM   1400 C CA  . THR A 1 188 ? -22.06500 -4.86500  -39.42300 1.000 51.03000 ? 190 THR A CA  1 
ATOM   1401 C C   . THR A 1 188 ? -20.72100 -5.45700  -39.39500 1.000 54.27000 ? 190 THR A C   1 
ATOM   1402 O O   . THR A 1 188 ? -20.13400 -5.57600  -38.37300 1.000 54.52000 ? 190 THR A O   1 
ATOM   1403 C CB  . THR A 1 188 ? -21.98100 -3.65500  -40.35600 1.000 48.72000 ? 190 THR A CB  1 
ATOM   1404 O OG1 . THR A 1 188 ? -20.82600 -2.86600  -40.06600 1.000 61.37000 ? 190 THR A OG1 1 
ATOM   1405 C CG2 . THR A 1 188 ? -23.14800 -2.80700  -40.20500 1.000 46.42000 ? 190 THR A CG2 1 
ATOM   1406 N N   . ALA A 1 189 ? -20.23900 -5.80300  -40.55800 1.000 54.93000 ? 191 ALA A N   1 
ATOM   1407 C CA  . ALA A 1 189 ? -18.93600 -6.29800  -40.67300 1.000 55.27000 ? 191 ALA A CA  1 
ATOM   1408 C C   . ALA A 1 189 ? -18.18400 -5.05200  -40.96700 1.000 57.33000 ? 191 ALA A C   1 
ATOM   1409 O O   . ALA A 1 189 ? -18.37900 -4.50000  -41.98100 1.000 65.05000 ? 191 ALA A O   1 
ATOM   1410 C CB  . ALA A 1 189 ? -18.85200 -7.20100  -41.84600 1.000 56.82000 ? 191 ALA A CB  1 
ATOM   1411 N N   . GLN A 1 190 ? -17.35500 -4.59600  -40.07100 1.000 49.46000 ? 192 GLN A N   1 
ATOM   1412 C CA  . GLN A 1 190 ? -16.55900 -3.45000  -40.28600 1.000 49.50000 ? 192 GLN A CA  1 
ATOM   1413 C C   . GLN A 1 190 ? -15.31400 -3.87000  -39.59900 1.000 47.11000 ? 192 GLN A C   1 
ATOM   1414 O O   . GLN A 1 190 ? -15.37900 -4.52800  -38.62300 1.000 48.41000 ? 192 GLN A O   1 
ATOM   1415 C CB  . GLN A 1 190 ? -17.13200 -2.18100  -39.67100 1.000 46.84000 ? 192 GLN A CB  1 
ATOM   1416 C CG  . GLN A 1 190 ? -17.75500 -2.32600  -38.31100 1.000 49.94000 ? 192 GLN A CG  1 
ATOM   1417 C CD  . GLN A 1 190 ? -18.48800 -1.09600  -37.82000 1.000 48.93000 ? 192 GLN A CD  1 
ATOM   1418 O OE1 . GLN A 1 190 ? -18.32400 -0.02800  -38.30200 1.000 45.61000 ? 192 GLN A OE1 1 
ATOM   1419 N NE2 . GLN A 1 190 ? -19.28500 -1.27900  -36.84600 1.000 46.85000 ? 192 GLN A NE2 1 
ATOM   1420 N N   . ALA A 1 191 ? -14.19300 -3.50800  -40.14900 1.000 48.76000 ? 193 ALA A N   1 
ATOM   1421 C CA  . ALA A 1 191 ? -12.94400 -3.84800  -39.55800 1.000 50.64000 ? 193 ALA A CA  1 
ATOM   1422 C C   . ALA A 1 191 ? -12.00300 -2.71800  -39.68700 1.000 44.68000 ? 193 ALA A C   1 
ATOM   1423 O O   . ALA A 1 191 ? -12.06700 -1.92400  -40.57600 1.000 47.00000 ? 193 ALA A O   1 
ATOM   1424 C CB  . ALA A 1 191 ? -12.37800 -5.06500  -40.20200 1.000 50.03000 ? 193 ALA A CB  1 
ATOM   1425 N N   . ALA A 1 192 ? -11.10000 -2.68500  -38.75800 1.000 47.23000 ? 194 ALA A N   1 
ATOM   1426 C CA  . ALA A 1 192 ? -10.09200 -1.70300  -38.73500 1.000 45.65000 ? 194 ALA A CA  1 
ATOM   1427 C C   . ALA A 1 192 ? -9.09300  -1.90300  -39.82700 1.000 47.61000 ? 194 ALA A C   1 
ATOM   1428 O O   . ALA A 1 192 ? -8.78000  -2.99400  -40.17800 1.000 49.25000 ? 194 ALA A O   1 
ATOM   1429 C CB  . ALA A 1 192 ? -9.39800  -1.79500  -37.42500 1.000 47.71000 ? 194 ALA A CB  1 
ATOM   1430 N N   . GLY A 1 193 ? -8.59100  -0.79800  -40.31400 1.000 49.75000 ? 195 GLY A N   1 
ATOM   1431 C CA  . GLY A 1 193 ? -7.55800  -0.71700  -41.31600 1.000 48.91000 ? 195 GLY A CA  1 
ATOM   1432 C C   . GLY A 1 193 ? -6.23800  -1.16600  -40.71800 1.000 47.74000 ? 195 GLY A C   1 
ATOM   1433 O O   . GLY A 1 193 ? -6.13900  -1.34800  -39.54300 1.000 45.45000 ? 195 GLY A O   1 
ATOM   1434 N N   . THR A 1 194 ? -5.23800  -1.39800  -41.54600 1.000 49.11000 ? 196 THR A N   1 
ATOM   1435 C CA  . THR A 1 194 ? -3.96700  -1.84600  -41.05500 1.000 44.97000 ? 196 THR A CA  1 
ATOM   1436 C C   . THR A 1 194 ? -3.44600  -0.77400  -40.14700 1.000 43.49000 ? 196 THR A C   1 
ATOM   1437 O O   . THR A 1 194 ? -3.51400  0.34500   -40.46200 1.000 45.68000 ? 196 THR A O   1 
ATOM   1438 C CB  . THR A 1 194 ? -2.97600  -2.17400  -42.19400 1.000 49.09000 ? 196 THR A CB  1 
ATOM   1439 O OG1 . THR A 1 194 ? -1.63900  -2.03200  -41.71600 1.000 54.58000 ? 196 THR A OG1 1 
ATOM   1440 C CG2 . THR A 1 194 ? -3.17000  -1.24600  -43.35400 1.000 45.57000 ? 196 THR A CG2 1 
ATOM   1441 N N   . ASP A 1 195 ? -2.95600  -1.16600  -38.99700 1.000 41.01000 ? 197 ASP A N   1 
ATOM   1442 C CA  . ASP A 1 195 ? -2.46000  -0.22700  -38.05200 1.000 40.99000 ? 197 ASP A CA  1 
ATOM   1443 C C   . ASP A 1 195 ? -1.00300  0.03200   -38.31500 1.000 44.37000 ? 197 ASP A C   1 
ATOM   1444 O O   . ASP A 1 195 ? -0.29500  -0.84100  -38.66500 1.000 44.69000 ? 197 ASP A O   1 
ATOM   1445 C CB  . ASP A 1 195 ? -2.71800  -0.67300  -36.63500 1.000 41.77000 ? 197 ASP A CB  1 
ATOM   1446 C CG  . ASP A 1 195 ? -2.54600  0.42800   -35.63500 1.000 38.12000 ? 197 ASP A CG  1 
ATOM   1447 O OD1 . ASP A 1 195 ? -2.77200  1.55000   -35.94000 1.000 39.61000 ? 197 ASP A OD1 1 
ATOM   1448 O OD2 . ASP A 1 195 ? -2.14900  0.15300   -34.54400 1.000 40.70000 ? 197 ASP A OD2 1 
ATOM   1449 N N   . THR A 1 196 ? -0.60100  1.25200   -38.15100 1.000 39.73000 ? 198 THR A N   1 
ATOM   1450 C CA  . THR A 1 196 ? 0.72600   1.64700   -38.39300 1.000 37.66000 ? 198 THR A CA  1 
ATOM   1451 C C   . THR A 1 196 ? 1.35500   2.25900   -37.16400 1.000 38.31000 ? 198 THR A C   1 
ATOM   1452 O O   . THR A 1 196 ? 0.69100   2.64700   -36.27900 1.000 32.11000 ? 198 THR A O   1 
ATOM   1453 C CB  . THR A 1 196 ? 0.77200   2.60500   -39.54800 1.000 39.22000 ? 198 THR A CB  1 
ATOM   1454 O OG1 . THR A 1 196 ? -0.24700  3.54400   -39.42700 1.000 38.69000 ? 198 THR A OG1 1 
ATOM   1455 C CG2 . THR A 1 196 ? 0.57500   1.92300   -40.77700 1.000 39.63000 ? 198 THR A CG2 1 
ATOM   1456 N N   . THR A 1 197 ? 2.65400   2.29200   -37.12000 1.000 30.98000 ? 199 THR A N   1 
ATOM   1457 C CA  . THR A 1 197 ? 3.31500   2.88000   -35.97600 1.000 29.20000 ? 199 THR A CA  1 
ATOM   1458 C C   . THR A 1 197 ? 3.31100   4.39700   -36.14000 1.000 30.04000 ? 199 THR A C   1 
ATOM   1459 O O   . THR A 1 197 ? 3.44800   4.91200   -37.25400 1.000 30.72000 ? 199 THR A O   1 
ATOM   1460 C CB  . THR A 1 197 ? 4.73300   2.30600   -35.85300 1.000 35.06000 ? 199 THR A CB  1 
ATOM   1461 O OG1 . THR A 1 197 ? 4.63700   0.87800   -35.72800 1.000 32.54000 ? 199 THR A OG1 1 
ATOM   1462 C CG2 . THR A 1 197 ? 5.47200   2.86700   -34.63200 1.000 29.26000 ? 199 THR A CG2 1 
ATOM   1463 N N   . ILE A 1 198 ? 3.07300   5.10200   -35.03100 1.000 28.65000 ? 200 ILE A N   1 
ATOM   1464 C CA  . ILE A 1 198 ? 3.07700   6.56500   -35.00300 1.000 29.30000 ? 200 ILE A CA  1 
ATOM   1465 C C   . ILE A 1 198 ? 4.51600   7.09300   -34.97000 1.000 30.78000 ? 200 ILE A C   1 
ATOM   1466 O O   . ILE A 1 198 ? 5.11900   7.25700   -33.89900 1.000 29.29000 ? 200 ILE A O   1 
ATOM   1467 C CB  . ILE A 1 198 ? 2.26600   7.08100   -33.80300 1.000 29.05000 ? 200 ILE A CB  1 
ATOM   1468 C CG1 . ILE A 1 198 ? 0.83000   6.51400   -33.85800 1.000 28.87000 ? 200 ILE A CG1 1 
ATOM   1469 C CG2 . ILE A 1 198 ? 2.26300   8.60500   -33.77300 1.000 27.93000 ? 200 ILE A CG2 1 
ATOM   1470 C CD1 . ILE A 1 198 ? 0.19500   6.33900   -32.47100 1.000 28.70000 ? 200 ILE A CD1 1 
ATOM   1471 N N   . THR A 1 199 ? 5.06000   7.36800   -36.15800 1.000 32.03000 ? 201 THR A N   1 
ATOM   1472 C CA  . THR A 1 199 ? 6.48200   7.68000   -36.29400 1.000 28.43000 ? 201 THR A CA  1 
ATOM   1473 C C   . THR A 1 199 ? 6.88400   8.86200   -35.43200 1.000 28.51000 ? 201 THR A C   1 
ATOM   1474 O O   . THR A 1 199 ? 7.89500   8.81400   -34.73000 1.000 27.56000 ? 201 THR A O   1 
ATOM   1475 C CB  . THR A 1 199 ? 6.82800   7.95000   -37.76500 1.000 30.70000 ? 201 THR A CB  1 
ATOM   1476 O OG1 . THR A 1 199 ? 6.32700   6.88000   -38.56700 1.000 32.48000 ? 201 THR A OG1 1 
ATOM   1477 C CG2 . THR A 1 199 ? 8.37400   8.05800   -37.96100 1.000 29.70000 ? 201 THR A CG2 1 
ATOM   1478 N N   . VAL A 1 200 ? 6.09700   9.94400   -35.46500 1.000 26.93000 ? 202 VAL A N   1 
ATOM   1479 C CA  . VAL A 1 200 ? 6.51600   11.13900  -34.74900 1.000 27.79000 ? 202 VAL A CA  1 
ATOM   1480 C C   . VAL A 1 200 ? 6.59900   10.86800  -33.24800 1.000 32.76000 ? 202 VAL A C   1 
ATOM   1481 O O   . VAL A 1 200 ? 7.41700   11.47300  -32.54200 1.000 31.66000 ? 202 VAL A O   1 
ATOM   1482 C CB  . VAL A 1 200 ? 5.58400   12.31800  -35.08600 1.000 33.63000 ? 202 VAL A CB  1 
ATOM   1483 C CG1 . VAL A 1 200 ? 4.18100   12.11300  -34.48100 1.000 31.46000 ? 202 VAL A CG1 1 
ATOM   1484 C CG2 . VAL A 1 200 ? 6.20800   13.61700  -34.60100 1.000 30.85000 ? 202 VAL A CG2 1 
ATOM   1485 N N   . ASN A 1 201 ? 5.81200   9.91200   -32.74700 1.000 31.31000 ? 203 ASN A N   1 
ATOM   1486 C CA  . ASN A 1 201 ? 5.87800   9.59700   -31.32200 1.000 33.89000 ? 203 ASN A CA  1 
ATOM   1487 C C   . ASN A 1 201 ? 7.12700   8.77400   -30.98000 1.000 30.48000 ? 203 ASN A C   1 
ATOM   1488 O O   . ASN A 1 201 ? 7.74200   8.99100   -29.93100 1.000 30.02000 ? 203 ASN A O   1 
ATOM   1489 C CB  . ASN A 1 201 ? 4.61200   8.85700   -30.88700 1.000 31.64000 ? 203 ASN A CB  1 
ATOM   1490 C CG  . ASN A 1 201 ? 3.37700   9.77200   -30.77400 1.000 34.19000 ? 203 ASN A CG  1 
ATOM   1491 O OD1 . ASN A 1 201 ? 3.43800   10.99600  -30.95900 1.000 32.42000 ? 203 ASN A OD1 1 
ATOM   1492 N ND2 . ASN A 1 201 ? 2.25000   9.16100   -30.46900 1.000 28.68000 ? 203 ASN A ND2 1 
ATOM   1493 N N   . VAL A 1 202 ? 7.49800   7.80900   -31.83200 1.000 30.84000 ? 204 VAL A N   1 
ATOM   1494 C CA  . VAL A 1 202 ? 8.75600   7.07500   -31.61800 1.000 32.24000 ? 204 VAL A CA  1 
ATOM   1495 C C   . VAL A 1 202 ? 9.94300   8.03700   -31.60500 1.000 30.12000 ? 204 VAL A C   1 
ATOM   1496 O O   . VAL A 1 202 ? 10.81600  7.95800   -30.73600 1.000 32.11000 ? 204 VAL A O   1 
ATOM   1497 C CB  . VAL A 1 202 ? 8.93800   5.97100   -32.67500 1.000 34.07000 ? 204 VAL A CB  1 
ATOM   1498 C CG1 . VAL A 1 202 ? 10.25900  5.21000   -32.44100 1.000 33.35000 ? 204 VAL A CG1 1 
ATOM   1499 C CG2 . VAL A 1 202 ? 7.76900   5.01100   -32.66700 1.000 27.10000 ? 204 VAL A CG2 1 
ATOM   1500 N N   . LEU A 1 203 ? 9.99000   8.97800   -32.54900 1.000 30.45000 ? 205 LEU A N   1 
ATOM   1501 C CA  . LEU A 1 203 ? 11.11300  9.91500   -32.58500 1.000 29.77000 ? 205 LEU A CA  1 
ATOM   1502 C C   . LEU A 1 203 ? 11.15500  10.79300  -31.33700 1.000 35.94000 ? 205 LEU A C   1 
ATOM   1503 O O   . LEU A 1 203 ? 12.23700  11.06100  -30.79500 1.000 30.44000 ? 205 LEU A O   1 
ATOM   1504 C CB  . LEU A 1 203 ? 11.04100  10.77700  -33.83900 1.000 26.76000 ? 205 LEU A CB  1 
ATOM   1505 C CG  . LEU A 1 203 ? 11.29500  10.04500  -35.15400 1.000 30.75000 ? 205 LEU A CG  1 
ATOM   1506 C CD1 . LEU A 1 203 ? 10.86100  10.90600  -36.28800 1.000 26.50000 ? 205 LEU A CD1 1 
ATOM   1507 C CD2 . LEU A 1 203 ? 12.82100  9.69000   -35.28000 1.000 29.63000 ? 205 LEU A CD2 1 
ATOM   1508 N N   . ALA A 1 204 ? 9.99100   11.27500  -30.87800 1.000 33.67000 ? 206 ALA A N   1 
ATOM   1509 C CA  . ALA A 1 204 ? 9.95100   12.06600  -29.64900 1.000 33.35000 ? 206 ALA A CA  1 
ATOM   1510 C C   . ALA A 1 204 ? 10.52000  11.28000  -28.47700 1.000 33.68000 ? 206 ALA A C   1 
ATOM   1511 O O   . ALA A 1 204 ? 11.25500  11.81900  -27.64400 1.000 35.81000 ? 206 ALA A O   1 
ATOM   1512 C CB  . ALA A 1 204 ? 8.51600   12.49400  -29.34100 1.000 35.17000 ? 206 ALA A CB  1 
ATOM   1513 N N   . TRP A 1 205 ? 10.18400  9.99800   -28.41600 1.000 31.85000 ? 207 TRP A N   1 
ATOM   1514 C CA  . TRP A 1 205 ? 10.63800  9.11500   -27.35500 1.000 34.44000 ? 207 TRP A CA  1 
ATOM   1515 C C   . TRP A 1 205 ? 12.14100  8.85900   -27.45100 1.000 37.14000 ? 207 TRP A C   1 
ATOM   1516 O O   . TRP A 1 205 ? 12.83900  8.82000   -26.42700 1.000 34.65000 ? 207 TRP A O   1 
ATOM   1517 C CB  . TRP A 1 205 ? 9.81300   7.83000   -27.45900 1.000 34.30000 ? 207 TRP A CB  1 
ATOM   1518 C CG  . TRP A 1 205 ? 10.13700  6.70200   -26.55200 1.000 39.67000 ? 207 TRP A CG  1 
ATOM   1519 C CD1 . TRP A 1 205 ? 9.82600   6.58300   -25.22400 1.000 42.56000 ? 207 TRP A CD1 1 
ATOM   1520 C CD2 . TRP A 1 205 ? 10.77600  5.47900   -26.92600 1.000 42.78000 ? 207 TRP A CD2 1 
ATOM   1521 N NE1 . TRP A 1 205 ? 10.26900  5.37000   -24.74300 1.000 41.76000 ? 207 TRP A NE1 1 
ATOM   1522 C CE2 . TRP A 1 205 ? 10.85600  4.67700   -25.76900 1.000 43.18000 ? 207 TRP A CE2 1 
ATOM   1523 C CE3 . TRP A 1 205 ? 11.30400  4.99200   -28.12800 1.000 41.46000 ? 207 TRP A CE3 1 
ATOM   1524 C CZ2 . TRP A 1 205 ? 11.44900  3.41400   -25.78000 1.000 49.51000 ? 207 TRP A CZ2 1 
ATOM   1525 C CZ3 . TRP A 1 205 ? 11.89000  3.73900   -28.13500 1.000 43.41000 ? 207 TRP A CZ3 1 
ATOM   1526 C CH2 . TRP A 1 205 ? 11.95200  2.96100   -26.97000 1.000 46.81000 ? 207 TRP A CH2 1 
ATOM   1527 N N   . LEU A 1 206 ? 12.66900  8.68800   -28.67300 1.000 33.24000 ? 208 LEU A N   1 
ATOM   1528 C CA  . LEU A 1 206 ? 14.11600  8.58700   -28.83000 1.000 32.88000 ? 208 LEU A CA  1 
ATOM   1529 C C   . LEU A 1 206 ? 14.80300  9.83800   -28.29700 1.000 32.42000 ? 208 LEU A C   1 
ATOM   1530 O O   . LEU A 1 206 ? 15.79100  9.75000   -27.56700 1.000 35.79000 ? 208 LEU A O   1 
ATOM   1531 C CB  . LEU A 1 206 ? 14.47900  8.33300   -30.29800 1.000 29.49000 ? 208 LEU A CB  1 
ATOM   1532 C CG  . LEU A 1 206 ? 14.06600  6.93400   -30.78300 1.000 30.44000 ? 208 LEU A CG  1 
ATOM   1533 C CD1 . LEU A 1 206 ? 14.35900  6.71300   -32.26200 1.000 29.79000 ? 208 LEU A CD1 1 
ATOM   1534 C CD2 . LEU A 1 206 ? 14.70300  5.84100   -29.95100 1.000 30.66000 ? 208 LEU A CD2 1 
ATOM   1535 N N   . TYR A 1 207 ? 14.25500  11.01700  -28.61100 1.000 34.95000 ? 209 TYR A N   1 
ATOM   1536 C CA  . TYR A 1 207 ? 14.75900  12.24700  -28.00600 1.000 36.85000 ? 209 TYR A CA  1 
ATOM   1537 C C   . TYR A 1 207 ? 14.67800  12.19200  -26.47900 1.000 42.40000 ? 209 TYR A C   1 
ATOM   1538 O O   . TYR A 1 207 ? 15.57700  12.67900  -25.78400 1.000 44.94000 ? 209 TYR A O   1 
ATOM   1539 C CB  . TYR A 1 207 ? 13.98700  13.45100  -28.54300 1.000 39.34000 ? 209 TYR A CB  1 
ATOM   1540 C CG  . TYR A 1 207 ? 14.49600  13.95500  -29.86800 1.000 40.38000 ? 209 TYR A CG  1 
ATOM   1541 C CD1 . TYR A 1 207 ? 15.75600  14.52100  -29.97900 1.000 39.84000 ? 209 TYR A CD1 1 
ATOM   1542 C CD2 . TYR A 1 207 ? 13.72100  13.85900  -31.00800 1.000 35.27000 ? 209 TYR A CD2 1 
ATOM   1543 C CE1 . TYR A 1 207 ? 16.22500  14.98800  -31.18900 1.000 41.41000 ? 209 TYR A CE1 1 
ATOM   1544 C CE2 . TYR A 1 207 ? 14.17700  14.31800  -32.22000 1.000 39.76000 ? 209 TYR A CE2 1 
ATOM   1545 C CZ  . TYR A 1 207 ? 15.43300  14.88000  -32.30500 1.000 41.71000 ? 209 TYR A CZ  1 
ATOM   1546 O OH  . TYR A 1 207 ? 15.88200  15.34100  -33.51000 1.000 37.71000 ? 209 TYR A OH  1 
ATOM   1547 N N   . ALA A 1 208 ? 13.61400  11.59600  -25.93600 1.000 38.37000 ? 210 ALA A N   1 
ATOM   1548 C CA  . ALA A 1 208 ? 13.53400  11.44400  -24.49000 1.000 43.85000 ? 210 ALA A CA  1 
ATOM   1549 C C   . ALA A 1 208 ? 14.63800  10.52700  -23.97500 1.000 45.65000 ? 210 ALA A C   1 
ATOM   1550 O O   . ALA A 1 208 ? 15.14200  10.73300  -22.86800 1.000 45.80000 ? 210 ALA A O   1 
ATOM   1551 C CB  . ALA A 1 208 ? 12.15200  10.91900  -24.08400 1.000 42.09000 ? 210 ALA A CB  1 
ATOM   1552 N N   . ALA A 1 209 ? 15.03000  9.52500   -24.76300 1.000 41.93000 ? 211 ALA A N   1 
ATOM   1553 C CA  . ALA A 1 209 ? 16.12400  8.65100   -24.35400 1.000 46.40000 ? 211 ALA A CA  1 
ATOM   1554 C C   . ALA A 1 209 ? 17.45000  9.40800   -24.31900 1.000 47.22000 ? 211 ALA A C   1 
ATOM   1555 O O   . ALA A 1 209 ? 18.24000  9.24400   -23.38600 1.000 46.91000 ? 211 ALA A O   1 
ATOM   1556 C CB  . ALA A 1 209 ? 16.20500  7.45100   -25.29100 1.000 44.27000 ? 211 ALA A CB  1 
ATOM   1557 N N   . VAL A 1 210 ? 17.68900  10.26600  -25.30700 1.000 45.05000 ? 212 VAL A N   1 
ATOM   1558 C CA  . VAL A 1 210 ? 18.89200  11.08800  -25.32400 1.000 46.28000 ? 212 VAL A CA  1 
ATOM   1559 C C   . VAL A 1 210 ? 18.91500  12.05000  -24.13500 1.000 51.00000 ? 212 VAL A C   1 
ATOM   1560 O O   . VAL A 1 210 ? 19.94700  12.20300  -23.46900 1.000 49.25000 ? 212 VAL A O   1 
ATOM   1561 C CB  . VAL A 1 210 ? 18.98700  11.82400  -26.67300 1.000 41.79000 ? 212 VAL A CB  1 
ATOM   1562 C CG1 . VAL A 1 210 ? 20.08400  12.88100  -26.64200 1.000 40.87000 ? 212 VAL A CG1 1 
ATOM   1563 C CG2 . VAL A 1 210 ? 19.23000  10.81600  -27.79900 1.000 38.38000 ? 212 VAL A CG2 1 
ATOM   1564 N N   . ILE A 1 211 ? 17.81000  12.67400  -23.81700 1.000 50.64000 ? 213 ILE A N   1 
ATOM   1565 C CA  . ILE A 1 211 ? 17.74800  13.58200  -22.70100 1.000 50.94000 ? 213 ILE A CA  1 
ATOM   1566 C C   . ILE A 1 211 ? 18.05500  12.87200  -21.39400 1.000 53.63000 ? 213 ILE A C   1 
ATOM   1567 O O   . ILE A 1 211 ? 18.60000  13.44900  -20.52400 1.000 57.54000 ? 213 ILE A O   1 
ATOM   1568 C CB  . ILE A 1 211 ? 16.41800  14.30800  -22.68600 1.000 53.85000 ? 213 ILE A CB  1 
ATOM   1569 C CG1 . ILE A 1 211 ? 16.43000  15.37100  -23.75700 1.000 53.26000 ? 213 ILE A CG1 1 
ATOM   1570 C CG2 . ILE A 1 211 ? 16.14400  14.98000  -21.36600 1.000 53.44000 ? 213 ILE A CG2 1 
ATOM   1571 C CD1 . ILE A 1 211 ? 15.06900  15.79700  -24.18500 1.000 56.03000 ? 213 ILE A CD1 1 
ATOM   1572 N N   . ASN A 1 212 ? 17.71100  11.61900  -21.27500 1.000 54.11000 ? 214 ASN A N   1 
ATOM   1573 C CA  . ASN A 1 212 ? 17.97000  10.85700  -20.09000 1.000 54.72000 ? 214 ASN A CA  1 
ATOM   1574 C C   . ASN A 1 212 ? 19.27200  10.09700  -20.19800 1.000 56.07000 ? 214 ASN A C   1 
ATOM   1575 O O   . ASN A 1 212 ? 19.51100  9.11000   -19.52300 1.000 56.26000 ? 214 ASN A O   1 
ATOM   1576 C CB  . ASN A 1 212 ? 16.89500  9.85100   -19.90800 1.000 52.87000 ? 214 ASN A CB  1 
ATOM   1577 C CG  . ASN A 1 212 ? 16.92300  9.22500   -18.54000 1.000 60.57000 ? 214 ASN A CG  1 
ATOM   1578 O OD1 . ASN A 1 212 ? 17.28400  9.86300   -17.57700 1.000 64.26000 ? 214 ASN A OD1 1 
ATOM   1579 N ND2 . ASN A 1 212 ? 16.51500  7.98400   -18.45100 1.000 59.45000 ? 214 ASN A ND2 1 
ATOM   1580 N N   . GLY A 1 213 ? 20.08300  10.51100  -21.12700 1.000 56.11000 ? 215 GLY A N   1 
ATOM   1581 C CA  . GLY A 1 213 ? 21.35400  9.85300   -21.31400 1.000 57.76000 ? 215 GLY A CA  1 
ATOM   1582 C C   . GLY A 1 213 ? 21.67200  8.60100   -22.11000 1.000 55.80000 ? 215 GLY A C   1 
ATOM   1583 O O   . GLY A 1 213 ? 22.81500  8.34000   -22.18600 1.000 55.13000 ? 215 GLY A O   1 
ATOM   1584 N N   . ASP A 1 214 ? 20.75700  7.87600   -22.71500 1.000 47.13000 ? 216 ASP A N   1 
ATOM   1585 C CA  . ASP A 1 214 ? 21.11800  6.75500   -23.55200 1.000 49.12000 ? 216 ASP A CA  1 
ATOM   1586 C C   . ASP A 1 214 ? 21.45600  7.30500   -24.91000 1.000 51.83000 ? 216 ASP A C   1 
ATOM   1587 O O   . ASP A 1 214 ? 20.73400  8.12700   -25.39100 1.000 46.82000 ? 216 ASP A O   1 
ATOM   1588 C CB  . ASP A 1 214 ? 19.94600  5.92100   -23.83800 1.000 53.70000 ? 216 ASP A CB  1 
ATOM   1589 C CG  . ASP A 1 214 ? 19.86800  4.74200   -23.01000 1.000 57.14000 ? 216 ASP A CG  1 
ATOM   1590 O OD1 . ASP A 1 214 ? 20.86200  4.07000   -22.78300 1.000 60.67000 ? 216 ASP A OD1 1 
ATOM   1591 O OD2 . ASP A 1 214 ? 18.76200  4.47300   -22.58400 1.000 64.69000 ? 216 ASP A OD2 1 
ATOM   1592 N N   . ARG A 1 215 ? 22.54400  6.88700   -25.52200 1.000 45.58000 ? 217 ARG A N   1 
ATOM   1593 C CA  . ARG A 1 215 ? 22.89500  7.34400   -26.83900 1.000 40.96000 ? 217 ARG A CA  1 
ATOM   1594 C C   . ARG A 1 215 ? 23.32800  6.22200   -27.70500 1.000 38.03000 ? 217 ARG A C   1 
ATOM   1595 O O   . ARG A 1 215 ? 23.79600  6.39700   -28.73400 1.000 37.37000 ? 217 ARG A O   1 
ATOM   1596 C CB  . ARG A 1 215 ? 23.98200  8.35400   -26.75300 1.000 43.03000 ? 217 ARG A CB  1 
ATOM   1597 C CG  . ARG A 1 215 ? 23.54500  9.61300   -26.12000 1.000 44.60000 ? 217 ARG A CG  1 
ATOM   1598 C CD  . ARG A 1 215 ? 24.59800  10.66100  -26.08200 1.000 42.86000 ? 217 ARG A CD  1 
ATOM   1599 N NE  . ARG A 1 215 ? 25.23200  10.81600  -27.34800 1.000 43.45000 ? 217 ARG A NE  1 
ATOM   1600 C CZ  . ARG A 1 215 ? 25.19000  11.90100  -28.09100 1.000 47.04000 ? 217 ARG A CZ  1 
ATOM   1601 N NH1 . ARG A 1 215 ? 25.82700  11.91400  -29.22400 1.000 39.56000 ? 217 ARG A NH1 1 
ATOM   1602 N NH2 . ARG A 1 215 ? 24.52800  12.95900  -27.71100 1.000 40.19000 ? 217 ARG A NH2 1 
ATOM   1603 N N   . TRP A 1 216 ? 23.17100  5.03800   -27.23500 1.000 39.45000 ? 218 TRP A N   1 
ATOM   1604 C CA  . TRP A 1 216 ? 23.67400  3.87800   -27.90600 1.000 35.92000 ? 218 TRP A CA  1 
ATOM   1605 C C   . TRP A 1 216 ? 23.21000  3.66400   -29.28900 1.000 37.70000 ? 218 TRP A C   1 
ATOM   1606 O O   . TRP A 1 216 ? 23.88000  3.09100   -30.04300 1.000 32.34000 ? 218 TRP A O   1 
ATOM   1607 C CB  . TRP A 1 216 ? 23.48400  2.59200   -27.08800 1.000 38.63000 ? 218 TRP A CB  1 
ATOM   1608 C CG  . TRP A 1 216 ? 22.12000  2.05200   -26.94700 1.000 43.23000 ? 218 TRP A CG  1 
ATOM   1609 C CD1 . TRP A 1 216 ? 21.30200  2.21700   -25.89700 1.000 44.17000 ? 218 TRP A CD1 1 
ATOM   1610 C CD2 . TRP A 1 216 ? 21.41300  1.23900   -27.86300 1.000 41.83000 ? 218 TRP A CD2 1 
ATOM   1611 N NE1 . TRP A 1 216 ? 20.15200  1.59200   -26.09300 1.000 41.31000 ? 218 TRP A NE1 1 
ATOM   1612 C CE2 . TRP A 1 216 ? 20.17400  0.98200   -27.30000 1.000 42.21000 ? 218 TRP A CE2 1 
ATOM   1613 C CE3 . TRP A 1 216 ? 21.69600  0.71800   -29.10500 1.000 39.62000 ? 218 TRP A CE3 1 
ATOM   1614 C CZ2 . TRP A 1 216 ? 19.22700  0.24800   -27.93100 1.000 41.71000 ? 218 TRP A CZ2 1 
ATOM   1615 C CZ3 . TRP A 1 216 ? 20.77000  -0.00800  -29.71600 1.000 42.74000 ? 218 TRP A CZ3 1 
ATOM   1616 C CH2 . TRP A 1 216 ? 19.53800  -0.25000  -29.13300 1.000 43.04000 ? 218 TRP A CH2 1 
ATOM   1617 N N   . PHE A 1 217 ? 22.01700  4.07700   -29.58600 1.000 36.04000 ? 219 PHE A N   1 
ATOM   1618 C CA  . PHE A 1 217 ? 21.40700  3.83000   -30.88600 1.000 31.98000 ? 219 PHE A CA  1 
ATOM   1619 C C   . PHE A 1 217 ? 21.73600  4.90900   -31.90700 1.000 32.17000 ? 219 PHE A C   1 
ATOM   1620 O O   . PHE A 1 217 ? 21.39300  4.75700   -33.08400 1.000 32.64000 ? 219 PHE A O   1 
ATOM   1621 C CB  . PHE A 1 217 ? 19.87000  3.71500   -30.74100 1.000 35.06000 ? 219 PHE A CB  1 
ATOM   1622 C CG  . PHE A 1 217 ? 19.29200  4.75700   -29.85200 1.000 33.07000 ? 219 PHE A CG  1 
ATOM   1623 C CD1 . PHE A 1 217 ? 19.04500  6.02800   -30.33200 1.000 36.13000 ? 219 PHE A CD1 1 
ATOM   1624 C CD2 . PHE A 1 217 ? 19.03000  4.48500   -28.52100 1.000 36.13000 ? 219 PHE A CD2 1 
ATOM   1625 C CE1 . PHE A 1 217 ? 18.54200  7.00800   -29.50300 1.000 36.26000 ? 219 PHE A CE1 1 
ATOM   1626 C CE2 . PHE A 1 217 ? 18.52900  5.46000   -27.69300 1.000 37.51000 ? 219 PHE A CE2 1 
ATOM   1627 C CZ  . PHE A 1 217 ? 18.28600  6.72200   -28.17700 1.000 36.05000 ? 219 PHE A CZ  1 
ATOM   1628 N N   . LEU A 1 218 ? 22.36000  6.00600   -31.49200 1.000 32.22000 ? 220 LEU A N   1 
ATOM   1629 C CA  . LEU A 1 218 ? 22.74600  7.02900   -32.44700 1.000 36.00000 ? 220 LEU A CA  1 
ATOM   1630 C C   . LEU A 1 218 ? 23.75900  6.46200   -33.44400 1.000 36.79000 ? 220 LEU A C   1 
ATOM   1631 O O   . LEU A 1 218 ? 24.41000  5.44800   -33.19600 1.000 33.46000 ? 220 LEU A O   1 
ATOM   1632 C CB  . LEU A 1 218 ? 23.32300  8.24800   -31.72400 1.000 35.70000 ? 220 LEU A CB  1 
ATOM   1633 C CG  . LEU A 1 218 ? 22.33600  8.91500   -30.75500 1.000 37.72000 ? 220 LEU A CG  1 
ATOM   1634 C CD1 . LEU A 1 218 ? 22.97400  10.11200  -30.06900 1.000 38.74000 ? 220 LEU A CD1 1 
ATOM   1635 C CD2 . LEU A 1 218 ? 21.05100  9.33600   -31.46800 1.000 34.50000 ? 220 LEU A CD2 1 
ATOM   1636 N N   . ASN A 1 219 ? 23.83100  7.09000   -34.61700 1.000 38.17000 ? 221 ASN A N   1 
ATOM   1637 C CA  . ASN A 1 219 ? 24.83700  6.75200   -35.61200 1.000 38.37000 ? 221 ASN A CA  1 
ATOM   1638 C C   . ASN A 1 219 ? 25.30900  8.04400   -36.25400 1.000 37.75000 ? 221 ASN A C   1 
ATOM   1639 O O   . ASN A 1 219 ? 24.88900  9.14000   -35.87400 1.000 32.56000 ? 221 ASN A O   1 
ATOM   1640 C CB  . ASN A 1 219 ? 24.32600  5.71700   -36.63100 1.000 36.08000 ? 221 ASN A CB  1 
ATOM   1641 C CG  . ASN A 1 219 ? 23.21900  6.24100   -37.55000 1.000 35.52000 ? 221 ASN A CG  1 
ATOM   1642 O OD1 . ASN A 1 219 ? 22.95300  7.43500   -37.64600 1.000 36.12000 ? 221 ASN A OD1 1 
ATOM   1643 N ND2 . ASN A 1 219 ? 22.59400  5.32100   -38.26400 1.000 33.83000 ? 221 ASN A ND2 1 
ATOM   1644 N N   . ARG A 1 220 ? 26.21300  7.92000   -37.21800 1.000 36.75000 ? 222 ARG A N   1 
ATOM   1645 C CA  . ARG A 1 220 ? 26.81700  9.08700   -37.82600 1.000 36.70000 ? 222 ARG A CA  1 
ATOM   1646 C C   . ARG A 1 220 ? 26.13300  9.47100   -39.12600 1.000 38.50000 ? 222 ARG A C   1 
ATOM   1647 O O   . ARG A 1 220 ? 26.61300  10.36100  -39.82900 1.000 40.83000 ? 222 ARG A O   1 
ATOM   1648 C CB  . ARG A 1 220 ? 28.31400  8.83600   -38.04300 1.000 42.59000 ? 222 ARG A CB  1 
ATOM   1649 C CG  . ARG A 1 220 ? 28.60000  7.86500   -39.16000 1.000 44.65000 ? 222 ARG A CG  1 
ATOM   1650 C CD  . ARG A 1 220 ? 29.94200  7.15000   -38.94700 1.000 50.54000 ? 222 ARG A CD  1 
ATOM   1651 N NE  . ARG A 1 220 ? 30.05300  5.88800   -39.69200 1.000 51.96000 ? 222 ARG A NE  1 
ATOM   1652 C CZ  . ARG A 1 220 ? 29.21200  4.85200   -39.61000 1.000 49.71000 ? 222 ARG A CZ  1 
ATOM   1653 N NH1 . ARG A 1 220 ? 28.13400  4.88300   -38.80800 1.000 55.18000 ? 222 ARG A NH1 1 
ATOM   1654 N NH2 . ARG A 1 220 ? 29.45100  3.76600   -40.34100 1.000 47.28000 ? 222 ARG A NH2 1 
ATOM   1655 N N   . PHE A 1 221 ? 25.00800  8.84200   -39.45400 1.000 35.76000 ? 223 PHE A N   1 
ATOM   1656 C CA  . PHE A 1 221 ? 24.37000  9.12100   -40.72900 1.000 33.78000 ? 223 PHE A CA  1 
ATOM   1657 C C   . PHE A 1 221 ? 23.27700  10.16600  -40.58600 1.000 36.08000 ? 223 PHE A C   1 
ATOM   1658 O O   . PHE A 1 221 ? 22.77400  10.45600  -39.49600 1.000 34.35000 ? 223 PHE A O   1 
ATOM   1659 C CB  . PHE A 1 221 ? 23.78600  7.84800   -41.34000 1.000 34.81000 ? 223 PHE A CB  1 
ATOM   1660 C CG  . PHE A 1 221 ? 24.83000  6.84300   -41.73300 1.000 42.13000 ? 223 PHE A CG  1 
ATOM   1661 C CD1 . PHE A 1 221 ? 25.65500  7.06800   -42.82800 1.000 46.90000 ? 223 PHE A CD1 1 
ATOM   1662 C CD2 . PHE A 1 221 ? 25.01800  5.69400   -40.98600 1.000 40.21000 ? 223 PHE A CD2 1 
ATOM   1663 C CE1 . PHE A 1 221 ? 26.63900  6.15100   -43.17500 1.000 44.02000 ? 223 PHE A CE1 1 
ATOM   1664 C CE2 . PHE A 1 221 ? 25.99200  4.77500   -41.33400 1.000 44.26000 ? 223 PHE A CE2 1 
ATOM   1665 C CZ  . PHE A 1 221 ? 26.79900  5.00300   -42.43000 1.000 40.96000 ? 223 PHE A CZ  1 
ATOM   1666 N N   . THR A 1 222 ? 22.90000  10.72700  -41.72100 1.000 35.15000 ? 224 THR A N   1 
ATOM   1667 C CA  . THR A 1 222 ? 21.66600  11.48500  -41.76100 1.000 33.93000 ? 224 THR A CA  1 
ATOM   1668 C C   . THR A 1 222 ? 20.82300  10.92400  -42.88900 1.000 35.37000 ? 224 THR A C   1 
ATOM   1669 O O   . THR A 1 222 ? 21.16500  9.88300   -43.46600 1.000 33.38000 ? 224 THR A O   1 
ATOM   1670 C CB  . THR A 1 222 ? 21.93500  12.97800  -41.93200 1.000 36.10000 ? 224 THR A CB  1 
ATOM   1671 O OG1 . THR A 1 222 ? 20.70200  13.70200  -41.78200 1.000 40.87000 ? 224 THR A OG1 1 
ATOM   1672 C CG2 . THR A 1 222 ? 22.56800  13.26600  -43.29300 1.000 39.58000 ? 224 THR A CG2 1 
ATOM   1673 N N   . THR A 1 223 ? 19.71600  11.58700  -43.19800 1.000 33.72000 ? 225 THR A N   1 
ATOM   1674 C CA  . THR A 1 223 ? 18.83200  11.08900  -44.23300 1.000 34.11000 ? 225 THR A CA  1 
ATOM   1675 C C   . THR A 1 223 ? 18.05500  12.26700  -44.77500 1.000 33.07000 ? 225 THR A C   1 
ATOM   1676 O O   . THR A 1 223 ? 17.92200  13.29700  -44.11400 1.000 37.17000 ? 225 THR A O   1 
ATOM   1677 C CB  . THR A 1 223 ? 17.89500  10.00000  -43.69400 1.000 34.37000 ? 225 THR A CB  1 
ATOM   1678 O OG1 . THR A 1 223 ? 17.16600  9.39400   -44.77200 1.000 32.81000 ? 225 THR A OG1 1 
ATOM   1679 C CG2 . THR A 1 223 ? 16.90400  10.59900  -42.67700 1.000 32.96000 ? 225 THR A CG2 1 
ATOM   1680 N N   . THR A 1 224 ? 17.58000  12.12500  -46.00800 1.000 34.43000 ? 226 THR A N   1 
ATOM   1681 C CA  . THR A 1 224 ? 16.54500  13.02800  -46.47000 1.000 35.78000 ? 226 THR A CA  1 
ATOM   1682 C C   . THR A 1 224 ? 15.20500  12.56200  -45.92100 1.000 33.64000 ? 226 THR A C   1 
ATOM   1683 O O   . THR A 1 224 ? 15.01900  11.38500  -45.59600 1.000 31.66000 ? 226 THR A O   1 
ATOM   1684 C CB  . THR A 1 224 ? 16.45500  13.08100  -48.00000 1.000 32.97000 ? 226 THR A CB  1 
ATOM   1685 O OG1 . THR A 1 224 ? 16.02500  11.81200  -48.48700 1.000 34.01000 ? 226 THR A OG1 1 
ATOM   1686 C CG2 . THR A 1 224 ? 17.79700  13.44100  -48.63800 1.000 38.38000 ? 226 THR A CG2 1 
ATOM   1687 N N   . LEU A 1 225 ? 14.26200  13.50400  -45.84400 1.000 35.39000 ? 227 LEU A N   1 
ATOM   1688 C CA  . LEU A 1 225 ? 12.90100  13.17700  -45.43200 1.000 33.70000 ? 227 LEU A CA  1 
ATOM   1689 C C   . LEU A 1 225 ? 12.28900  12.13700  -46.36000 1.000 32.34000 ? 227 LEU A C   1 
ATOM   1690 O O   . LEU A 1 225 ? 11.67700  11.16500  -45.90600 1.000 32.58000 ? 227 LEU A O   1 
ATOM   1691 C CB  . LEU A 1 225 ? 12.04200  14.44600  -45.40200 1.000 37.73000 ? 227 LEU A CB  1 
ATOM   1692 C CG  . LEU A 1 225 ? 10.63700  14.32000  -44.79000 1.000 35.13000 ? 227 LEU A CG  1 
ATOM   1693 C CD1 . LEU A 1 225 ? 10.74400  13.81100  -43.38500 1.000 32.98000 ? 227 LEU A CD1 1 
ATOM   1694 C CD2 . LEU A 1 225 ? 9.89000   15.65100  -44.84000 1.000 34.98000 ? 227 LEU A CD2 1 
ATOM   1695 N N   . ASN A 1 226 ? 12.46900  12.30200  -47.67300 1.000 32.99000 ? 228 ASN A N   1 
ATOM   1696 C CA  . ASN A 1 226 ? 11.86600  11.33900  -48.58500 1.000 36.11000 ? 228 ASN A CA  1 
ATOM   1697 C C   . ASN A 1 226 ? 12.47000  9.95600   -48.41900 1.000 34.60000 ? 228 ASN A C   1 
ATOM   1698 O O   . ASN A 1 226 ? 11.74500  8.96200   -48.34000 1.000 32.60000 ? 228 ASN A O   1 
ATOM   1699 C CB  . ASN A 1 226 ? 11.98800  11.77400  -50.04000 1.000 38.81000 ? 228 ASN A CB  1 
ATOM   1700 C CG  . ASN A 1 226 ? 11.08700  10.94100  -50.94000 1.000 43.72000 ? 228 ASN A CG  1 
ATOM   1701 O OD1 . ASN A 1 226 ? 9.90800   10.74100  -50.62700 1.000 49.96000 ? 228 ASN A OD1 1 
ATOM   1702 N ND2 . ASN A 1 226 ? 11.63700  10.41200  -52.01900 1.000 49.63000 ? 228 ASN A ND2 1 
ATOM   1703 N N   . ASP A 1 227 ? 13.81500  9.86900   -48.37500 1.000 33.85000 ? 229 ASP A N   1 
ATOM   1704 C CA  . ASP A 1 227 ? 14.46200  8.58100   -48.12600 1.000 32.28000 ? 229 ASP A CA  1 
ATOM   1705 C C   . ASP A 1 227 ? 14.00100  7.96600   -46.79900 1.000 31.69000 ? 229 ASP A C   1 
ATOM   1706 O O   . ASP A 1 227 ? 13.74200  6.75900   -46.72200 1.000 31.42000 ? 229 ASP A O   1 
ATOM   1707 C CB  . ASP A 1 227 ? 15.98900  8.74200   -48.13700 1.000 30.40000 ? 229 ASP A CB  1 
ATOM   1708 C CG  . ASP A 1 227 ? 16.56600  8.85000   -49.55600 1.000 32.00000 ? 229 ASP A CG  1 
ATOM   1709 O OD1 . ASP A 1 227 ? 15.83200  8.62300   -50.53800 1.000 34.50000 ? 229 ASP A OD1 1 
ATOM   1710 O OD2 . ASP A 1 227 ? 17.77200  9.15900   -49.68500 1.000 38.40000 ? 229 ASP A OD2 1 
ATOM   1711 N N   . PHE A 1 228 ? 13.91200  8.76500   -45.74100 1.000 29.84000 ? 230 PHE A N   1 
ATOM   1712 C CA  . PHE A 1 228 ? 13.39900  8.20800   -44.49000 1.000 32.64000 ? 230 PHE A CA  1 
ATOM   1713 C C   . PHE A 1 228 ? 12.03000  7.56600   -44.69100 1.000 33.65000 ? 230 PHE A C   1 
ATOM   1714 O O   . PHE A 1 228 ? 11.79200  6.42900   -44.26400 1.000 33.72000 ? 230 PHE A O   1 
ATOM   1715 C CB  . PHE A 1 228 ? 13.29700  9.26500   -43.39400 1.000 30.89000 ? 230 PHE A CB  1 
ATOM   1716 C CG  . PHE A 1 228 ? 12.63200  8.73300   -42.15800 1.000 34.78000 ? 230 PHE A CG  1 
ATOM   1717 C CD1 . PHE A 1 228 ? 13.35100  7.95900   -41.25400 1.000 32.35000 ? 230 PHE A CD1 1 
ATOM   1718 C CD2 . PHE A 1 228 ? 11.26500  8.92900   -41.94200 1.000 34.12000 ? 230 PHE A CD2 1 
ATOM   1719 C CE1 . PHE A 1 228 ? 12.72900  7.44100   -40.12700 1.000 34.53000 ? 230 PHE A CE1 1 
ATOM   1720 C CE2 . PHE A 1 228 ? 10.63900  8.41000   -40.82700 1.000 33.05000 ? 230 PHE A CE2 1 
ATOM   1721 C CZ  . PHE A 1 228 ? 11.36200  7.67300   -39.91800 1.000 31.95000 ? 230 PHE A CZ  1 
ATOM   1722 N N   . ASN A 1 229 ? 11.10700  8.29100   -45.34500 1.000 31.27000 ? 231 ASN A N   1 
ATOM   1723 C CA  . ASN A 1 229 ? 9.74500   7.78200   -45.48500 1.000 32.64000 ? 231 ASN A CA  1 
ATOM   1724 C C   . ASN A 1 229 ? 9.69100   6.55600   -46.38100 1.000 35.77000 ? 231 ASN A C   1 
ATOM   1725 O O   . ASN A 1 229 ? 8.86800   5.66600   -46.14800 1.000 33.86000 ? 231 ASN A O   1 
ATOM   1726 C CB  . ASN A 1 229 ? 8.81300   8.86700   -46.03200 1.000 35.98000 ? 231 ASN A CB  1 
ATOM   1727 C CG  . ASN A 1 229 ? 8.50700   9.95700   -45.00000 1.000 35.64000 ? 231 ASN A CG  1 
ATOM   1728 O OD1 . ASN A 1 229 ? 8.43600   9.69300   -43.81100 1.000 34.41000 ? 231 ASN A OD1 1 
ATOM   1729 N ND2 . ASN A 1 229 ? 8.32200   11.18700  -45.46900 1.000 37.97000 ? 231 ASN A ND2 1 
ATOM   1730 N N   . LEU A 1 230 ? 10.54300  6.48500   -47.41100 1.000 30.75000 ? 232 LEU A N   1 
ATOM   1731 C CA  . LEU A 1 230 ? 10.55800  5.28800   -48.24700 1.000 32.41000 ? 232 LEU A CA  1 
ATOM   1732 C C   . LEU A 1 230 ? 10.94100  4.06100   -47.42700 1.000 31.80000 ? 232 LEU A C   1 
ATOM   1733 O O   . LEU A 1 230 ? 10.35000  2.99000   -47.58600 1.000 34.78000 ? 232 LEU A O   1 
ATOM   1734 C CB  . LEU A 1 230 ? 11.51800  5.47800   -49.43000 1.000 30.55000 ? 232 LEU A CB  1 
ATOM   1735 C CG  . LEU A 1 230 ? 10.97900  6.35900   -50.55100 1.000 33.69000 ? 232 LEU A CG  1 
ATOM   1736 C CD1 . LEU A 1 230 ? 12.09800  6.87000   -51.45500 1.000 35.63000 ? 232 LEU A CD1 1 
ATOM   1737 C CD2 . LEU A 1 230 ? 9.90100   5.60000   -51.36300 1.000 34.67000 ? 232 LEU A CD2 1 
ATOM   1738 N N   . VAL A 1 231 ? 11.92500  4.20100   -46.54400 1.000 29.67000 ? 233 VAL A N   1 
ATOM   1739 C CA  . VAL A 1 231 ? 12.32700  3.07900   -45.69900 1.000 32.85000 ? 233 VAL A CA  1 
ATOM   1740 C C   . VAL A 1 231 ? 11.24100  2.77400   -44.67200 1.000 32.11000 ? 233 VAL A C   1 
ATOM   1741 O O   . VAL A 1 231 ? 10.77300  1.63700   -44.55300 1.000 32.09000 ? 233 VAL A O   1 
ATOM   1742 C CB  . VAL A 1 231 ? 13.67300  3.38600   -45.01500 1.000 30.69000 ? 233 VAL A CB  1 
ATOM   1743 C CG1 . VAL A 1 231 ? 14.06200  2.28300   -44.03200 1.000 33.52000 ? 233 VAL A CG1 1 
ATOM   1744 C CG2 . VAL A 1 231 ? 14.78300  3.56800   -46.05500 1.000 34.33000 ? 233 VAL A CG2 1 
ATOM   1745 N N   . ALA A 1 232 ? 10.83600  3.78700   -43.90900 1.000 34.01000 ? 234 ALA A N   1 
ATOM   1746 C CA  . ALA A 1 232 ? 9.95400   3.56000   -42.76500 1.000 36.73000 ? 234 ALA A CA  1 
ATOM   1747 C C   . ALA A 1 232 ? 8.64800   2.89500   -43.18500 1.000 35.53000 ? 234 ALA A C   1 
ATOM   1748 O O   . ALA A 1 232 ? 8.12600   2.02300   -42.48000 1.000 35.15000 ? 234 ALA A O   1 
ATOM   1749 C CB  . ALA A 1 232 ? 9.68400   4.88600   -42.05400 1.000 36.60000 ? 234 ALA A CB  1 
ATOM   1750 N N   . MET A 1 233 ? 8.12100   3.26800   -44.34300 1.000 35.20000 ? 235 MET A N   1 
ATOM   1751 C CA  . MET A 1 233 ? 6.85300   2.70100   -44.77900 1.000 36.76000 ? 235 MET A CA  1 
ATOM   1752 C C   . MET A 1 233 ? 6.95000   1.21500   -45.09100 1.000 37.34000 ? 235 MET A C   1 
ATOM   1753 O O   . MET A 1 233 ? 5.92800   0.52400   -45.06400 1.000 36.58000 ? 235 MET A O   1 
ATOM   1754 C CB  . MET A 1 233 ? 6.34200   3.49600   -45.96600 1.000 38.23000 ? 235 MET A CB  1 
ATOM   1755 C CG  . MET A 1 233 ? 5.95300   4.89400   -45.50100 1.000 46.02000 ? 235 MET A CG  1 
ATOM   1756 S SD  . MET A 1 233 ? 5.19500   5.93000   -46.75200 1.000 55.08000 ? 235 MET A SD  1 
ATOM   1757 C CE  . MET A 1 233 ? 3.95100   4.79900   -47.39200 1.000 58.47000 ? 235 MET A CE  1 
ATOM   1758 N N   . LYS A 1 234 ? 8.14900   0.69200   -45.34300 1.000 33.38000 ? 236 LYS A N   1 
ATOM   1759 C CA  . LYS A 1 234 ? 8.31000   -0.75300  -45.45900 1.000 35.23000 ? 236 LYS A CA  1 
ATOM   1760 C C   . LYS A 1 234 ? 8.20500   -1.47000  -44.11700 1.000 35.33000 ? 236 LYS A C   1 
ATOM   1761 O O   . LYS A 1 234 ? 8.11200   -2.70400  -44.09100 1.000 39.30000 ? 236 LYS A O   1 
ATOM   1762 C CB  . LYS A 1 234 ? 9.65500   -1.06500  -46.12500 1.000 37.21000 ? 236 LYS A CB  1 
ATOM   1763 C CG  . LYS A 1 234 ? 9.70200   -0.61500  -47.58900 1.000 40.12000 ? 236 LYS A CG  1 
ATOM   1764 C CD  . LYS A 1 234 ? 11.12700  -0.70300  -48.15900 1.000 45.09000 ? 236 LYS A CD  1 
ATOM   1765 C CE  . LYS A 1 234 ? 11.29600  0.19200   -49.38400 1.000 43.26000 ? 236 LYS A CE  1 
ATOM   1766 N NZ  . LYS A 1 234 ? 12.75100  0.34300   -49.74500 1.000 43.80000 ? 236 LYS A NZ  1 
ATOM   1767 N N   . TYR A 1 235 ? 8.18700   -0.74300  -43.03800 1.000 33.94000 ? 237 TYR A N   1 
ATOM   1768 C CA  . TYR A 1 235 ? 8.01600   -1.33300  -41.74800 1.000 34.34000 ? 237 TYR A CA  1 
ATOM   1769 C C   . TYR A 1 235 ? 6.64300   -0.96600  -41.16400 1.000 36.09000 ? 237 TYR A C   1 
ATOM   1770 O O   . TYR A 1 235 ? 6.40100   -1.14100  -40.02300 1.000 36.20000 ? 237 TYR A O   1 
ATOM   1771 C CB  . TYR A 1 235 ? 9.10100   -0.90300  -40.81000 1.000 32.84000 ? 237 TYR A CB  1 
ATOM   1772 C CG  . TYR A 1 235 ? 10.49800  -1.26400  -41.16800 1.000 36.35000 ? 237 TYR A CG  1 
ATOM   1773 C CD1 . TYR A 1 235 ? 11.05700  -2.40000  -40.72100 1.000 39.79000 ? 237 TYR A CD1 1 
ATOM   1774 C CD2 . TYR A 1 235 ? 11.27600  -0.42400  -41.89200 1.000 36.50000 ? 237 TYR A CD2 1 
ATOM   1775 C CE1 . TYR A 1 235 ? 12.36700  -2.70500  -41.00100 1.000 42.67000 ? 237 TYR A CE1 1 
ATOM   1776 C CE2 . TYR A 1 235 ? 12.56300  -0.72600  -42.19200 1.000 37.97000 ? 237 TYR A CE2 1 
ATOM   1777 C CZ  . TYR A 1 235 ? 13.10000  -1.87400  -41.73900 1.000 40.89000 ? 237 TYR A CZ  1 
ATOM   1778 O OH  . TYR A 1 235 ? 14.35500  -2.16100  -42.01700 1.000 43.51000 ? 237 TYR A OH  1 
ATOM   1779 N N   . ASN A 1 236 ? 5.76000   -0.46700  -41.98400 1.000 34.40000 ? 238 ASN A N   1 
ATOM   1780 C CA  . ASN A 1 236 ? 4.47100   -0.00400  -41.53700 1.000 38.72000 ? 238 ASN A CA  1 
ATOM   1781 C C   . ASN A 1 236 ? 4.50800   1.15600   -40.55300 1.000 38.63000 ? 238 ASN A C   1 
ATOM   1782 O O   . ASN A 1 236 ? 3.79800   1.18000   -39.63500 1.000 36.83000 ? 238 ASN A O   1 
ATOM   1783 C CB  . ASN A 1 236 ? 3.62000   -1.13400  -41.01300 1.000 38.98000 ? 238 ASN A CB  1 
ATOM   1784 C CG  . ASN A 1 236 ? 3.05800   -1.97900  -42.11200 1.000 46.93000 ? 238 ASN A CG  1 
ATOM   1785 O OD1 . ASN A 1 236 ? 2.82700   -1.51800  -43.18400 1.000 48.40000 ? 238 ASN A OD1 1 
ATOM   1786 N ND2 . ASN A 1 236 ? 2.82800   -3.21000  -41.83300 1.000 52.58000 ? 238 ASN A ND2 1 
ATOM   1787 N N   . TYR A 1 237 ? 5.37600   2.10500   -40.79000 1.000 34.31000 ? 239 TYR A N   1 
ATOM   1788 C CA  . TYR A 1 237 ? 5.47800   3.26100   -39.98400 1.000 30.25000 ? 239 TYR A CA  1 
ATOM   1789 C C   . TYR A 1 237 ? 4.76300   4.34700   -40.73400 1.000 35.74000 ? 239 TYR A C   1 
ATOM   1790 O O   . TYR A 1 237 ? 4.77300   4.36900   -41.90800 1.000 34.55000 ? 239 TYR A O   1 
ATOM   1791 C CB  . TYR A 1 237 ? 6.91500   3.62700   -39.73200 1.000 31.71000 ? 239 TYR A CB  1 
ATOM   1792 C CG  . TYR A 1 237 ? 7.50500   3.10800   -38.47800 1.000 28.88000 ? 239 TYR A CG  1 
ATOM   1793 C CD1 . TYR A 1 237 ? 7.60300   1.79200   -38.24000 1.000 29.81000 ? 239 TYR A CD1 1 
ATOM   1794 C CD2 . TYR A 1 237 ? 7.96900   3.93700   -37.55300 1.000 26.69000 ? 239 TYR A CD2 1 
ATOM   1795 C CE1 . TYR A 1 237 ? 8.14500   1.32100   -37.09900 1.000 27.82000 ? 239 TYR A CE1 1 
ATOM   1796 C CE2 . TYR A 1 237 ? 8.45200   3.48100   -36.41000 1.000 30.68000 ? 239 TYR A CE2 1 
ATOM   1797 C CZ  . TYR A 1 237 ? 8.56100   2.16600   -36.20100 1.000 29.42000 ? 239 TYR A CZ  1 
ATOM   1798 O OH  . TYR A 1 237 ? 9.06400   1.76300   -35.06600 1.000 31.70000 ? 239 TYR A OH  1 
ATOM   1799 N N   . GLU A 1 238 ? 4.10300   5.22100   -40.01100 1.000 35.15000 ? 240 GLU A N   1 
ATOM   1800 C CA  . GLU A 1 238 ? 3.39000   6.34400   -40.60700 1.000 35.06000 ? 240 GLU A CA  1 
ATOM   1801 C C   . GLU A 1 238 ? 4.38200   7.29400   -41.28500 1.000 34.06000 ? 240 GLU A C   1 
ATOM   1802 O O   . GLU A 1 238 ? 5.46400   7.53500   -40.75300 1.000 32.26000 ? 240 GLU A O   1 
ATOM   1803 C CB  . GLU A 1 238 ? 2.61700   7.11600   -39.52800 1.000 34.52000 ? 240 GLU A CB  1 
ATOM   1804 C CG  . GLU A 1 238 ? 1.26300   6.54500   -39.17200 1.000 36.26000 ? 240 GLU A CG  1 
ATOM   1805 C CD  . GLU A 1 238 ? 0.30400   6.62600   -40.34300 1.000 43.70000 ? 240 GLU A CD  1 
ATOM   1806 O OE1 . GLU A 1 238 ? -0.21000  5.56800   -40.77600 1.000 45.13000 ? 240 GLU A OE1 1 
ATOM   1807 O OE2 . GLU A 1 238 ? 0.09400   7.75400   -40.84900 1.000 46.15000 ? 240 GLU A OE2 1 
ATOM   1808 N N   . PRO A 1 239 ? 4.02200   7.86600   -42.43300 1.000 34.69000 ? 241 PRO A N   1 
ATOM   1809 C CA  . PRO A 1 239 ? 4.90200   8.86500   -43.04500 1.000 38.10000 ? 241 PRO A CA  1 
ATOM   1810 C C   . PRO A 1 239 ? 5.13100   10.03900  -42.11000 1.000 37.68000 ? 241 PRO A C   1 
ATOM   1811 O O   . PRO A 1 239 ? 4.25700   10.43400  -41.33500 1.000 37.80000 ? 241 PRO A O   1 
ATOM   1812 C CB  . PRO A 1 239 ? 4.13500   9.28500   -44.31000 1.000 39.85000 ? 241 PRO A CB  1 
ATOM   1813 C CG  . PRO A 1 239 ? 2.76900   8.74500   -44.15500 1.000 39.40000 ? 241 PRO A CG  1 
ATOM   1814 C CD  . PRO A 1 239 ? 2.86700   7.55000   -43.28400 1.000 35.84000 ? 241 PRO A CD  1 
ATOM   1815 N N   . LEU A 1 240 ? 6.33200   10.58900  -42.17400 1.000 33.46000 ? 242 LEU A N   1 
ATOM   1816 C CA  . LEU A 1 240 ? 6.69000   11.75100  -41.38300 1.000 35.63000 ? 242 LEU A CA  1 
ATOM   1817 C C   . LEU A 1 240 ? 6.52600   12.98300  -42.26100 1.000 37.39000 ? 242 LEU A C   1 
ATOM   1818 O O   . LEU A 1 240 ? 7.04900   13.01700  -43.37600 1.000 37.01000 ? 242 LEU A O   1 
ATOM   1819 C CB  . LEU A 1 240 ? 8.12500   11.63300  -40.86000 1.000 36.12000 ? 242 LEU A CB  1 
ATOM   1820 C CG  . LEU A 1 240 ? 8.57400   12.55900  -39.72900 1.000 36.62000 ? 242 LEU A CG  1 
ATOM   1821 C CD1 . LEU A 1 240 ? 8.04100   12.08400  -38.35900 1.000 36.16000 ? 242 LEU A CD1 1 
ATOM   1822 C CD2 . LEU A 1 240 ? 10.10300  12.68000  -39.72700 1.000 34.08000 ? 242 LEU A CD2 1 
ATOM   1823 N N   . THR A 1 241 ? 5.79400   13.97800  -41.76800 1.000 34.79000 ? 243 THR A N   1 
ATOM   1824 C CA  . THR A 1 241 ? 5.53400   15.20400  -42.50400 1.000 36.85000 ? 243 THR A CA  1 
ATOM   1825 C C   . THR A 1 241 ? 6.46000   16.32100  -42.03500 1.000 39.47000 ? 243 THR A C   1 
ATOM   1826 O O   . THR A 1 241 ? 7.16600   16.20800  -41.02800 1.000 40.31000 ? 243 THR A O   1 
ATOM   1827 C CB  . THR A 1 241 ? 4.07600   15.64700  -42.32400 1.000 37.17000 ? 243 THR A CB  1 
ATOM   1828 O OG1 . THR A 1 241 ? 3.91400   16.15700  -40.99500 1.000 40.46000 ? 243 THR A OG1 1 
ATOM   1829 C CG2 . THR A 1 241 ? 3.11800   14.48400  -42.52000 1.000 36.66000 ? 243 THR A CG2 1 
ATOM   1830 N N   . GLN A 1 242 ? 6.43800   17.42700  -42.78500 1.000 42.18000 ? 244 GLN A N   1 
ATOM   1831 C CA  . GLN A 1 242 ? 7.16700   18.62300  -42.37700 1.000 41.43000 ? 244 GLN A CA  1 
ATOM   1832 C C   . GLN A 1 242 ? 6.59200   19.21800  -41.09500 1.000 45.63000 ? 244 GLN A C   1 
ATOM   1833 O O   . GLN A 1 242 ? 7.31400   19.86800  -40.32800 1.000 46.91000 ? 244 GLN A O   1 
ATOM   1834 C CB  . GLN A 1 242 ? 7.13400   19.65500  -43.50300 1.000 46.50000 ? 244 GLN A CB  1 
ATOM   1835 C CG  . GLN A 1 242 ? 7.99900   20.87200  -43.25400 1.000 47.93000 ? 244 GLN A CG  1 
ATOM   1836 C CD  . GLN A 1 242 ? 9.43600   20.48400  -43.02500 1.000 49.92000 ? 244 GLN A CD  1 
ATOM   1837 O OE1 . GLN A 1 242 ? 10.02700  19.76800  -43.83000 1.000 48.08000 ? 244 GLN A OE1 1 
ATOM   1838 N NE2 . GLN A 1 242 ? 10.00200  20.92800  -41.90500 1.000 50.07000 ? 244 GLN A NE2 1 
ATOM   1839 N N   . ASP A 1 243 ? 5.29300   19.02400  -40.85400 1.000 41.21000 ? 245 ASP A N   1 
ATOM   1840 C CA  . ASP A 1 243 ? 4.71200   19.44200  -39.58100 1.000 44.21000 ? 245 ASP A CA  1 
ATOM   1841 C C   . ASP A 1 243 ? 5.30300   18.64600  -38.42600 1.000 41.49000 ? 245 ASP A C   1 
ATOM   1842 O O   . ASP A 1 243 ? 5.57200   19.19800  -37.35100 1.000 42.95000 ? 245 ASP A O   1 
ATOM   1843 C CB  . ASP A 1 243 ? 3.19000   19.26400  -39.61200 1.000 43.49000 ? 245 ASP A CB  1 
ATOM   1844 C CG  . ASP A 1 243 ? 2.46200   20.48600  -40.14200 1.000 50.16000 ? 245 ASP A CG  1 
ATOM   1845 O OD1 . ASP A 1 243 ? 3.07600   21.28900  -40.88100 1.000 52.46000 ? 245 ASP A OD1 1 
ATOM   1846 O OD2 . ASP A 1 243 ? 1.25500   20.62400  -39.84100 1.000 52.72000 ? 245 ASP A OD2 1 
ATOM   1847 N N   . HIS A 1 244 ? 5.46900   17.33500  -38.61600 1.000 38.65000 ? 246 HIS A N   1 
ATOM   1848 C CA  . HIS A 1 244 ? 6.10700   16.51300  -37.59300 1.000 39.37000 ? 246 HIS A CA  1 
ATOM   1849 C C   . HIS A 1 244 ? 7.54300   16.96400  -37.35200 1.000 41.17000 ? 246 HIS A C   1 
ATOM   1850 O O   . HIS A 1 244 ? 7.97900   17.10700  -36.20000 1.000 41.62000 ? 246 HIS A O   1 
ATOM   1851 C CB  . HIS A 1 244 ? 6.07100   15.03800  -38.00200 1.000 36.96000 ? 246 HIS A CB  1 
ATOM   1852 C CG  . HIS A 1 244 ? 4.69100   14.46700  -38.12500 1.000 37.96000 ? 246 HIS A CG  1 
ATOM   1853 N ND1 . HIS A 1 244 ? 4.38400   13.46000  -39.01300 1.000 37.72000 ? 246 HIS A ND1 1 
ATOM   1854 C CD2 . HIS A 1 244 ? 3.53500   14.76000  -37.47400 1.000 36.57000 ? 246 HIS A CD2 1 
ATOM   1855 C CE1 . HIS A 1 244 ? 3.10000   13.15600  -38.90800 1.000 35.01000 ? 246 HIS A CE1 1 
ATOM   1856 N NE2 . HIS A 1 244 ? 2.56300   13.93500  -37.98700 1.000 33.71000 ? 246 HIS A NE2 1 
ATOM   1857 N N   . VAL A 1 245 ? 8.29000   17.20500  -38.42500 1.000 40.45000 ? 247 VAL A N   1 
ATOM   1858 C CA  . VAL A 1 245 ? 9.64200   17.72300  -38.29100 1.000 42.32000 ? 247 VAL A CA  1 
ATOM   1859 C C   . VAL A 1 245 ? 9.63400   19.01400  -37.48300 1.000 45.76000 ? 247 VAL A C   1 
ATOM   1860 O O   . VAL A 1 245 ? 10.39100  19.17000  -36.51500 1.000 42.25000 ? 247 VAL A O   1 
ATOM   1861 C CB  . VAL A 1 245 ? 10.27200  17.92100  -39.68000 1.000 43.36000 ? 247 VAL A CB  1 
ATOM   1862 C CG1 . VAL A 1 245 ? 11.57300  18.71400  -39.57200 1.000 43.10000 ? 247 VAL A CG1 1 
ATOM   1863 C CG2 . VAL A 1 245 ? 10.51800  16.57500  -40.32500 1.000 42.02000 ? 247 VAL A CG2 1 
ATOM   1864 N N   . ASP A 1 246 ? 8.76600   19.96000  -37.86800 1.000 46.10000 ? 248 ASP A N   1 
ATOM   1865 C CA  . ASP A 1 246 ? 8.66700   21.22000  -37.13200 1.000 46.56000 ? 248 ASP A CA  1 
ATOM   1866 C C   . ASP A 1 246 ? 8.35100   20.97700  -35.66400 1.000 45.00000 ? 248 ASP A C   1 
ATOM   1867 O O   . ASP A 1 246 ? 8.86500   21.67300  -34.78200 1.000 45.67000 ? 248 ASP A O   1 
ATOM   1868 C CB  . ASP A 1 246 ? 7.59200   22.11400  -37.74600 1.000 45.29000 ? 248 ASP A CB  1 
ATOM   1869 C CG  . ASP A 1 246 ? 8.00600   22.70700  -39.07700 1.000 46.86000 ? 248 ASP A CG  1 
ATOM   1870 O OD1 . ASP A 1 246 ? 9.16300   22.51500  -39.51900 1.000 52.41000 ? 248 ASP A OD1 1 
ATOM   1871 O OD2 . ASP A 1 246 ? 7.16500   23.39100  -39.68600 1.000 56.42000 ? 248 ASP A OD2 1 
ATOM   1872 N N   . ILE A 1 247 ? 7.51600   19.97800  -35.38600 1.000 42.93000 ? 249 ILE A N   1 
ATOM   1873 C CA  . ILE A 1 247 ? 7.07800   19.74800  -34.01700 1.000 45.58000 ? 249 ILE A CA  1 
ATOM   1874 C C   . ILE A 1 247 ? 8.23000   19.22300  -33.16800 1.000 43.03000 ? 249 ILE A C   1 
ATOM   1875 O O   . ILE A 1 247 ? 8.36000   19.56900  -31.98800 1.000 42.20000 ? 249 ILE A O   1 
ATOM   1876 C CB  . ILE A 1 247 ? 5.86100   18.80200  -34.01700 1.000 43.58000 ? 249 ILE A CB  1 
ATOM   1877 C CG1 . ILE A 1 247 ? 4.59900   19.59400  -34.37100 1.000 47.59000 ? 249 ILE A CG1 1 
ATOM   1878 C CG2 . ILE A 1 247 ? 5.68400   18.15800  -32.68800 1.000 40.02000 ? 249 ILE A CG2 1 
ATOM   1879 C CD1 . ILE A 1 247 ? 3.49300   18.76800  -35.02500 1.000 44.65000 ? 249 ILE A CD1 1 
ATOM   1880 N N   . LEU A 1 248 ? 9.10400   18.47800  -33.76000 1.000 43.53000 ? 250 LEU A N   1 
ATOM   1881 C CA  . LEU A 1 248 ? 10.22800  17.95500  -33.03800 1.000 42.72000 ? 250 LEU A CA  1 
ATOM   1882 C C   . LEU A 1 248 ? 11.38100  18.93400  -32.91600 1.000 43.69000 ? 250 LEU A C   1 
ATOM   1883 O O   . LEU A 1 248 ? 12.32400  18.63600  -32.30400 1.000 44.57000 ? 250 LEU A O   1 
ATOM   1884 C CB  . LEU A 1 248 ? 10.70800  16.70000  -33.69500 1.000 42.19000 ? 250 LEU A CB  1 
ATOM   1885 C CG  . LEU A 1 248 ? 9.77700   15.52400  -33.73900 1.000 41.33000 ? 250 LEU A CG  1 
ATOM   1886 C CD1 . LEU A 1 248 ? 10.12200  14.62400  -34.86400 1.000 35.10000 ? 250 LEU A CD1 1 
ATOM   1887 C CD2 . LEU A 1 248 ? 9.66500   14.79700  -32.45000 1.000 36.71000 ? 250 LEU A CD2 1 
ATOM   1888 N N   . GLY A 1 249 ? 11.25700  20.11600  -33.47400 1.000 44.59000 ? 251 GLY A N   1 
ATOM   1889 C CA  . GLY A 1 249 ? 12.32000  21.08400  -33.44700 1.000 42.71000 ? 251 GLY A CA  1 
ATOM   1890 C C   . GLY A 1 249 ? 12.83000  21.47400  -32.10200 1.000 48.21000 ? 251 GLY A C   1 
ATOM   1891 O O   . GLY A 1 249 ? 13.98900  21.56700  -31.92900 1.000 46.25000 ? 251 GLY A O   1 
ATOM   1892 N N   . PRO A 1 250 ? 11.88000  21.70100  -31.12300 1.000 48.74000 ? 252 PRO A N   1 
ATOM   1893 C CA  . PRO A 1 250 ? 12.39900  22.00300  -29.79800 1.000 45.71000 ? 252 PRO A CA  1 
ATOM   1894 C C   . PRO A 1 250 ? 13.24500  20.95500  -29.15000 1.000 46.83000 ? 252 PRO A C   1 
ATOM   1895 O O   . PRO A 1 250 ? 14.21200  21.26500  -28.55400 1.000 47.54000 ? 252 PRO A O   1 
ATOM   1896 C CB  . PRO A 1 250 ? 11.13900  22.11100  -28.98100 1.000 47.89000 ? 252 PRO A CB  1 
ATOM   1897 C CG  . PRO A 1 250 ? 10.26300  22.85200  -29.84900 1.000 47.04000 ? 252 PRO A CG  1 
ATOM   1898 C CD  . PRO A 1 250 ? 10.39800  22.05400  -31.08400 1.000 48.07000 ? 252 PRO A CD  1 
ATOM   1899 N N   . LEU A 1 251 ? 12.84900  19.72000  -29.25200 1.000 45.88000 ? 253 LEU A N   1 
ATOM   1900 C CA  . LEU A 1 251 ? 13.59100  18.62300  -28.70800 1.000 44.28000 ? 253 LEU A CA  1 
ATOM   1901 C C   . LEU A 1 251 ? 14.93300  18.50400  -29.40600 1.000 46.60000 ? 253 LEU A C   1 
ATOM   1902 O O   . LEU A 1 251 ? 15.89500  18.16800  -28.81100 1.000 46.83000 ? 253 LEU A O   1 
ATOM   1903 C CB  . LEU A 1 251 ? 12.81500  17.35100  -28.86500 1.000 42.56000 ? 253 LEU A CB  1 
ATOM   1904 C CG  . LEU A 1 251 ? 11.62700  17.15000  -27.95300 1.000 49.90000 ? 253 LEU A CG  1 
ATOM   1905 C CD1 . LEU A 1 251 ? 10.77800  15.97800  -28.32100 1.000 41.28000 ? 253 LEU A CD1 1 
ATOM   1906 C CD2 . LEU A 1 251 ? 12.05800  16.99900  -26.52900 1.000 46.09000 ? 253 LEU A CD2 1 
ATOM   1907 N N   . SER A 1 252 ? 14.96200  18.74700  -30.68500 1.000 44.53000 ? 254 SER A N   1 
ATOM   1908 C CA  . SER A 1 252 ? 16.17700  18.69800  -31.43400 1.000 46.94000 ? 254 SER A CA  1 
ATOM   1909 C C   . SER A 1 252 ? 17.08300  19.76500  -30.89600 1.000 49.28000 ? 254 SER A C   1 
ATOM   1910 O O   . SER A 1 252 ? 18.22000  19.55100  -30.71100 1.000 48.26000 ? 254 SER A O   1 
ATOM   1911 C CB  . SER A 1 252 ? 15.90300  18.93600  -32.87800 1.000 43.64000 ? 254 SER A CB  1 
ATOM   1912 O OG  . SER A 1 252 ? 17.05100  19.23700  -33.56500 1.000 49.41000 ? 254 SER A OG  1 
ATOM   1913 N N   . ALA A 1 253 ? 16.53200  20.91600  -30.62600 1.000 50.48000 ? 255 ALA A N   1 
ATOM   1914 C CA  . ALA A 1 253 ? 17.28100  22.01000  -30.09900 1.000 49.49000 ? 255 ALA A CA  1 
ATOM   1915 C C   . ALA A 1 253 ? 17.83500  21.70800  -28.75000 1.000 48.72000 ? 255 ALA A C   1 
ATOM   1916 O O   . ALA A 1 253 ? 18.94100  21.99500  -28.49500 1.000 51.83000 ? 255 ALA A O   1 
ATOM   1917 C CB  . ALA A 1 253 ? 16.41900  23.22100  -30.02400 1.000 48.30000 ? 255 ALA A CB  1 
ATOM   1918 N N   . GLN A 1 254 ? 17.04500  21.12100  -27.89700 1.000 51.08000 ? 256 GLN A N   1 
ATOM   1919 C CA  . GLN A 1 254 ? 17.48200  20.79100  -26.57700 1.000 49.51000 ? 256 GLN A CA  1 
ATOM   1920 C C   . GLN A 1 254 ? 18.54900  19.78200  -26.57500 1.000 51.03000 ? 256 GLN A C   1 
ATOM   1921 O O   . GLN A 1 254 ? 19.42400  19.87400  -25.79900 1.000 55.77000 ? 256 GLN A O   1 
ATOM   1922 C CB  . GLN A 1 254 ? 16.33100  20.34200  -25.72400 1.000 51.64000 ? 256 GLN A CB  1 
ATOM   1923 C CG  . GLN A 1 254 ? 16.67700  19.90800  -24.33100 1.000 54.69000 ? 256 GLN A CG  1 
ATOM   1924 C CD  . GLN A 1 254 ? 15.46700  19.38900  -23.57200 1.000 65.66000 ? 256 GLN A CD  1 
ATOM   1925 O OE1 . GLN A 1 254 ? 14.34600  19.50800  -24.03600 1.000 65.76000 ? 256 GLN A OE1 1 
ATOM   1926 N NE2 . GLN A 1 254 ? 15.68800  18.80900  -22.40600 1.000 60.28000 ? 256 GLN A NE2 1 
ATOM   1927 N N   . THR A 1 255 ? 18.45500  18.78000  -27.42000 1.000 49.91000 ? 257 THR A N   1 
ATOM   1928 C CA  . THR A 1 255 ? 19.45000  17.71000  -27.45200 1.000 51.40000 ? 257 THR A CA  1 
ATOM   1929 C C   . THR A 1 255 ? 20.63900  17.84100  -28.37200 1.000 46.46000 ? 257 THR A C   1 
ATOM   1930 O O   . THR A 1 255 ? 21.54700  17.09800  -28.26100 1.000 50.73000 ? 257 THR A O   1 
ATOM   1931 C CB  . THR A 1 255 ? 18.84400  16.34700  -27.81000 1.000 46.98000 ? 257 THR A CB  1 
ATOM   1932 O OG1 . THR A 1 255 ? 18.41200  16.37800  -29.15300 1.000 44.17000 ? 257 THR A OG1 1 
ATOM   1933 C CG2 . THR A 1 255 ? 17.74500  16.04200  -26.96900 1.000 48.17000 ? 257 THR A CG2 1 
ATOM   1934 N N   . GLY A 1 256 ? 20.60000  18.76200  -29.28400 1.000 47.16000 ? 258 GLY A N   1 
ATOM   1935 C CA  . GLY A 1 256 ? 21.65700  18.93800  -30.22800 1.000 44.40000 ? 258 GLY A CA  1 
ATOM   1936 C C   . GLY A 1 256 ? 21.69300  17.95600  -31.36700 1.000 50.38000 ? 258 GLY A C   1 
ATOM   1937 O O   . GLY A 1 256 ? 22.65000  17.91200  -32.08400 1.000 47.97000 ? 258 GLY A O   1 
ATOM   1938 N N   . ILE A 1 257 ? 20.64300  17.17200  -31.52400 1.000 45.99000 ? 259 ILE A N   1 
ATOM   1939 C CA  . ILE A 1 257 ? 20.55700  16.21100  -32.57100 1.000 43.29000 ? 259 ILE A CA  1 
ATOM   1940 C C   . ILE A 1 257 ? 19.50100  16.62700  -33.55800 1.000 43.51000 ? 259 ILE A C   1 
ATOM   1941 O O   . ILE A 1 257 ? 18.38600  16.76900  -33.21000 1.000 39.94000 ? 259 ILE A O   1 
ATOM   1942 C CB  . ILE A 1 257 ? 20.19000  14.87300  -31.99200 1.000 40.82000 ? 259 ILE A CB  1 
ATOM   1943 C CG1 . ILE A 1 257 ? 21.16900  14.50300  -30.91600 1.000 42.25000 ? 259 ILE A CG1 1 
ATOM   1944 C CG2 . ILE A 1 257 ? 20.18200  13.84900  -33.06300 1.000 39.54000 ? 259 ILE A CG2 1 
ATOM   1945 C CD1 . ILE A 1 257 ? 21.04300  13.10300  -30.44900 1.000 42.84000 ? 259 ILE A CD1 1 
ATOM   1946 N N   . ALA A 1 258 ? 19.89900  16.79900  -34.79600 1.000 42.73000 ? 260 ALA A N   1 
ATOM   1947 C CA  . ALA A 1 258 ? 18.98000  17.22300  -35.84000 1.000 40.05000 ? 260 ALA A CA  1 
ATOM   1948 C C   . ALA A 1 258 ? 17.91000  16.16000  -36.06800 1.000 37.45000 ? 260 ALA A C   1 
ATOM   1949 O O   . ALA A 1 258 ? 18.13600  14.96200  -35.86200 1.000 34.22000 ? 260 ALA A O   1 
ATOM   1950 C CB  . ALA A 1 258 ? 19.74900  17.50800  -37.13400 1.000 40.12000 ? 260 ALA A CB  1 
ATOM   1951 N N   . VAL A 1 259 ? 16.72100  16.61200  -36.48200 1.000 39.83000 ? 261 VAL A N   1 
ATOM   1952 C CA  . VAL A 1 259 ? 15.58700  15.69400  -36.61600 1.000 37.47000 ? 261 VAL A CA  1 
ATOM   1953 C C   . VAL A 1 259 ? 15.91500  14.58300  -37.61000 1.000 36.13000 ? 261 VAL A C   1 
ATOM   1954 O O   . VAL A 1 259 ? 15.74200  13.39200  -37.32000 1.000 34.58000 ? 261 VAL A O   1 
ATOM   1955 C CB  . VAL A 1 259 ? 14.30900  16.46300  -37.01800 1.000 39.39000 ? 261 VAL A CB  1 
ATOM   1956 C CG1 . VAL A 1 259 ? 13.12800  15.50100  -37.20200 1.000 34.59000 ? 261 VAL A CG1 1 
ATOM   1957 C CG2 . VAL A 1 259 ? 13.97500  17.53600  -35.97500 1.000 41.04000 ? 261 VAL A CG2 1 
ATOM   1958 N N   . LEU A 1 260 ? 16.41500  14.94800  -38.79000 1.000 35.97000 ? 262 LEU A N   1 
ATOM   1959 C CA  . LEU A 1 260 ? 16.75900  13.92000  -39.77200 1.000 35.40000 ? 262 LEU A CA  1 
ATOM   1960 C C   . LEU A 1 260 ? 17.93300  13.04700  -39.32100 1.000 35.11000 ? 262 LEU A C   1 
ATOM   1961 O O   . LEU A 1 260 ? 18.08300  11.93000  -39.82500 1.000 36.74000 ? 262 LEU A O   1 
ATOM   1962 C CB  . LEU A 1 260 ? 17.05300  14.56700  -41.13000 1.000 36.30000 ? 262 LEU A CB  1 
ATOM   1963 C CG  . LEU A 1 260 ? 15.84600  15.24600  -41.78500 1.000 33.11000 ? 262 LEU A CG  1 
ATOM   1964 C CD1 . LEU A 1 260 ? 16.22400  15.94800  -43.08800 1.000 38.94000 ? 262 LEU A CD1 1 
ATOM   1965 C CD2 . LEU A 1 260 ? 14.77200  14.22400  -42.04600 1.000 35.02000 ? 262 LEU A CD2 1 
ATOM   1966 N N   . ASP A 1 261 ? 18.74700  13.50800  -38.36700 1.000 35.37000 ? 263 ASP A N   1 
ATOM   1967 C CA  . ASP A 1 261 ? 19.75800  12.62600  -37.78300 1.000 36.35000 ? 263 ASP A CA  1 
ATOM   1968 C C   . ASP A 1 261 ? 19.11300  11.57000  -36.89400 1.000 35.20000 ? 263 ASP A C   1 
ATOM   1969 O O   . ASP A 1 261 ? 19.49100  10.39400  -36.93900 1.000 31.48000 ? 263 ASP A O   1 
ATOM   1970 C CB  . ASP A 1 261 ? 20.78400  13.43200  -36.97800 1.000 36.02000 ? 263 ASP A CB  1 
ATOM   1971 C CG  . ASP A 1 261 ? 21.77300  14.18300  -37.86000 1.000 41.32000 ? 263 ASP A CG  1 
ATOM   1972 O OD1 . ASP A 1 261 ? 21.65200  14.12900  -39.10200 1.000 39.81000 ? 263 ASP A OD1 1 
ATOM   1973 O OD2 . ASP A 1 261 ? 22.68200  14.83700  -37.29800 1.000 48.46000 ? 263 ASP A OD2 1 
ATOM   1974 N N   . MET A 1 262 ? 18.13600  11.97300  -36.07400 1.000 32.19000 ? 264 MET A N   1 
ATOM   1975 C CA  . MET A 1 262 ? 17.38600  10.98500  -35.30000 1.000 32.68000 ? 264 MET A CA  1 
ATOM   1976 C C   . MET A 1 262 ? 16.63300  10.03700  -36.21900 1.000 30.41000 ? 264 MET A C   1 
ATOM   1977 O O   . MET A 1 262 ? 16.50000  8.84000   -35.92300 1.000 29.64000 ? 264 MET A O   1 
ATOM   1978 C CB  . MET A 1 262 ? 16.41900  11.68600  -34.34100 1.000 34.35000 ? 264 MET A CB  1 
ATOM   1979 C CG  . MET A 1 262 ? 15.85800  10.74900  -33.27400 1.000 33.35000 ? 264 MET A CG  1 
ATOM   1980 S SD  . MET A 1 262 ? 17.14600  10.13100  -32.17700 1.000 34.57000 ? 264 MET A SD  1 
ATOM   1981 C CE  . MET A 1 262 ? 17.37100  11.53600  -31.09400 1.000 32.12000 ? 264 MET A CE  1 
ATOM   1982 N N   . CYS A 1 263 ? 16.15000  10.54800  -37.35000 1.000 29.61000 ? 265 CYS A N   1 
ATOM   1983 C CA  . CYS A 1 263 ? 15.50100  9.69700   -38.34400 1.000 28.63000 ? 265 CYS A CA  1 
ATOM   1984 C C   . CYS A 1 263 ? 16.43700  8.59600   -38.84000 1.000 31.56000 ? 265 CYS A C   1 
ATOM   1985 O O   . CYS A 1 263 ? 16.02100  7.43900   -38.99800 1.000 28.37000 ? 265 CYS A O   1 
ATOM   1986 C CB  . CYS A 1 263 ? 15.01300  10.55000  -39.51600 1.000 30.28000 ? 265 CYS A CB  1 
ATOM   1987 S SG  . CYS A 1 263 ? 13.48700  11.49200  -39.13700 1.000 32.20000 ? 265 CYS A SG  1 
ATOM   1988 N N   . ALA A 1 264 ? 17.70600  8.94300   -39.10600 1.000 28.09000 ? 266 ALA A N   1 
ATOM   1989 C CA  . ALA A 1 264 ? 18.68300  7.93800   -39.53600 1.000 29.91000 ? 266 ALA A CA  1 
ATOM   1990 C C   . ALA A 1 264 ? 18.91500  6.89500   -38.45100 1.000 30.62000 ? 266 ALA A C   1 
ATOM   1991 O O   . ALA A 1 264 ? 19.08200  5.70600   -38.74600 1.000 32.09000 ? 266 ALA A O   1 
ATOM   1992 C CB  . ALA A 1 264 ? 20.01800  8.60700   -39.90600 1.000 31.56000 ? 266 ALA A CB  1 
ATOM   1993 N N   . SER A 1 265 ? 18.94800  7.32400   -37.18600 1.000 24.49000 ? 267 SER A N   1 
ATOM   1994 C CA  . SER A 1 265 ? 19.04700  6.36100   -36.09500 1.000 28.54000 ? 267 SER A CA  1 
ATOM   1995 C C   . SER A 1 265 ? 17.86200  5.39200   -36.08600 1.000 31.01000 ? 267 SER A C   1 
ATOM   1996 O O   . SER A 1 265 ? 18.04300  4.17400   -35.94600 1.000 30.29000 ? 267 SER A O   1 
ATOM   1997 C CB  . SER A 1 265 ? 19.16400  7.11100   -34.76300 1.000 33.20000 ? 267 SER A CB  1 
ATOM   1998 O OG  . SER A 1 265 ? 18.82500  6.26100   -33.67100 1.000 39.59000 ? 267 SER A OG  1 
ATOM   1999 N N   . LEU A 1 266 ? 16.62700  5.91100   -36.23600 1.000 30.71000 ? 268 LEU A N   1 
ATOM   2000 C CA  . LEU A 1 266 ? 15.44800  5.03300   -36.28300 1.000 28.03000 ? 268 LEU A CA  1 
ATOM   2001 C C   . LEU A 1 266 ? 15.50400  4.06400   -37.46500 1.000 31.04000 ? 268 LEU A C   1 
ATOM   2002 O O   . LEU A 1 266 ? 15.18400  2.87600   -37.31900 1.000 31.89000 ? 268 LEU A O   1 
ATOM   2003 C CB  . LEU A 1 266 ? 14.15500  5.86000   -36.34900 1.000 28.64000 ? 268 LEU A CB  1 
ATOM   2004 C CG  . LEU A 1 266 ? 12.84100  5.06100   -36.49900 1.000 32.32000 ? 268 LEU A CG  1 
ATOM   2005 C CD1 . LEU A 1 266 ? 12.65700  4.03200   -35.36400 1.000 28.54000 ? 268 LEU A CD1 1 
ATOM   2006 C CD2 . LEU A 1 266 ? 11.64900  6.00700   -36.52700 1.000 32.59000 ? 268 LEU A CD2 1 
ATOM   2007 N N   . LYS A 1 267 ? 15.87500  4.55400   -38.65800 1.000 26.23000 ? 269 LYS A N   1 
ATOM   2008 C CA  . LYS A 1 267 ? 16.06800  3.65800   -39.79800 1.000 28.81000 ? 269 LYS A CA  1 
ATOM   2009 C C   . LYS A 1 267 ? 16.94900  2.47500   -39.42600 1.000 31.30000 ? 269 LYS A C   1 
ATOM   2010 O O   . LYS A 1 267 ? 16.66400  1.33100   -39.79400 1.000 30.81000 ? 269 LYS A O   1 
ATOM   2011 C CB  . LYS A 1 267 ? 16.70500  4.41000   -40.98400 1.000 29.87000 ? 269 LYS A CB  1 
ATOM   2012 C CG  . LYS A 1 267 ? 15.77200  5.36200   -41.70600 1.000 36.68000 ? 269 LYS A CG  1 
ATOM   2013 C CD  . LYS A 1 267 ? 16.53700  6.33100   -42.62100 1.000 38.62000 ? 269 LYS A CD  1 
ATOM   2014 C CE  . LYS A 1 267 ? 17.20000  5.61500   -43.78500 1.000 37.77000 ? 269 LYS A CE  1 
ATOM   2015 N NZ  . LYS A 1 267 ? 17.71900  6.61400   -44.77000 1.000 39.46000 ? 269 LYS A NZ  1 
ATOM   2016 N N   . GLU A 1 268 ? 18.03600  2.73800   -38.69100 1.000 29.14000 ? 270 GLU A N   1 
ATOM   2017 C CA  . GLU A 1 268 ? 18.96300  1.66900   -38.33400 1.000 33.88000 ? 270 GLU A CA  1 
ATOM   2018 C C   . GLU A 1 268 ? 18.39100  0.77500   -37.23700 1.000 32.36000 ? 270 GLU A C   1 
ATOM   2019 O O   . GLU A 1 268 ? 18.55400  -0.45000  -37.28000 1.000 33.27000 ? 270 GLU A O   1 
ATOM   2020 C CB  . GLU A 1 268 ? 20.30400  2.27600   -37.90900 1.000 32.91000 ? 270 GLU A CB  1 
ATOM   2021 C CG  . GLU A 1 268 ? 21.35600  1.27100   -37.50800 1.000 32.65000 ? 270 GLU A CG  1 
ATOM   2022 C CD  . GLU A 1 268 ? 22.71800  1.93200   -37.31100 1.000 38.57000 ? 270 GLU A CD  1 
ATOM   2023 O OE1 . GLU A 1 268 ? 23.38600  2.24800   -38.31900 1.000 34.57000 ? 270 GLU A OE1 1 
ATOM   2024 O OE2 . GLU A 1 268 ? 23.10900  2.15100   -36.15300 1.000 36.15000 ? 270 GLU A OE2 1 
ATOM   2025 N N   . LEU A 1 269 ? 17.71200  1.37200   -36.25300 1.000 33.02000 ? 271 LEU A N   1 
ATOM   2026 C CA  . LEU A 1 269 ? 17.02500  0.57700   -35.23600 1.000 34.51000 ? 271 LEU A CA  1 
ATOM   2027 C C   . LEU A 1 269 ? 16.03300  -0.39200  -35.86900 1.000 34.27000 ? 271 LEU A C   1 
ATOM   2028 O O   . LEU A 1 269 ? 15.92100  -1.54500  -35.43100 1.000 37.37000 ? 271 LEU A O   1 
ATOM   2029 C CB  . LEU A 1 269 ? 16.31900  1.50200   -34.23900 1.000 33.08000 ? 271 LEU A CB  1 
ATOM   2030 C CG  . LEU A 1 269 ? 17.15300  2.11900   -33.11600 1.000 34.21000 ? 271 LEU A CG  1 
ATOM   2031 C CD1 . LEU A 1 269 ? 16.34900  3.18400   -32.37900 1.000 35.80000 ? 271 LEU A CD1 1 
ATOM   2032 C CD2 . LEU A 1 269 ? 17.59600  1.03600   -32.14700 1.000 34.62000 ? 271 LEU A CD2 1 
ATOM   2033 N N   . LEU A 1 270 ? 15.31100  0.04800   -36.90800 1.000 31.34000 ? 272 LEU A N   1 
ATOM   2034 C CA  . LEU A 1 270 ? 14.35600  -0.83200  -37.58100 1.000 33.13000 ? 272 LEU A CA  1 
ATOM   2035 C C   . LEU A 1 270 ? 15.06800  -1.93400  -38.35100 1.000 38.83000 ? 272 LEU A C   1 
ATOM   2036 O O   . LEU A 1 270 ? 14.54600  -3.04800  -38.49600 1.000 37.83000 ? 272 LEU A O   1 
ATOM   2037 C CB  . LEU A 1 270 ? 13.47800  -0.02500  -38.53700 1.000 34.35000 ? 272 LEU A CB  1 
ATOM   2038 C CG  . LEU A 1 270 ? 12.55700  0.98800   -37.86300 1.000 34.14000 ? 272 LEU A CG  1 
ATOM   2039 C CD1 . LEU A 1 270 ? 11.92600  1.89700   -38.88500 1.000 30.66000 ? 272 LEU A CD1 1 
ATOM   2040 C CD2 . LEU A 1 270 ? 11.50700  0.24500   -37.08800 1.000 32.51000 ? 272 LEU A CD2 1 
ATOM   2041 N N   . GLN A 1 271 ? 16.24400  -1.61800  -38.89100 1.000 36.42000 ? 273 GLN A N   1 
ATOM   2042 C CA  . GLN A 1 271 ? 17.01900  -2.59300  -39.65200 1.000 35.42000 ? 273 GLN A CA  1 
ATOM   2043 C C   . GLN A 1 271 ? 17.60700  -3.66700  -38.74800 1.000 36.45000 ? 273 GLN A C   1 
ATOM   2044 O O   . GLN A 1 271 ? 17.67100  -4.83900  -39.13400 1.000 37.10000 ? 273 GLN A O   1 
ATOM   2045 C CB  . GLN A 1 271 ? 18.12400  -1.85300  -40.39900 1.000 34.13000 ? 273 GLN A CB  1 
ATOM   2046 C CG  . GLN A 1 271 ? 19.27300  -2.68100  -40.93400 1.000 36.88000 ? 273 GLN A CG  1 
ATOM   2047 C CD  . GLN A 1 271 ? 20.38800  -1.76900  -41.44500 1.000 34.75000 ? 273 GLN A CD  1 
ATOM   2048 O OE1 . GLN A 1 271 ? 20.26900  -1.18100  -42.52000 1.000 38.90000 ? 273 GLN A OE1 1 
ATOM   2049 N NE2 . GLN A 1 271 ? 21.45700  -1.62900  -40.66600 1.000 34.01000 ? 273 GLN A NE2 1 
ATOM   2050 N N   . ASN A 1 272 ? 18.02700  -3.28800  -37.53300 1.000 35.82000 ? 274 ASN A N   1 
ATOM   2051 C CA  . ASN A 1 272 ? 18.80800  -4.15800  -36.65500 1.000 39.71000 ? 274 ASN A CA  1 
ATOM   2052 C C   . ASN A 1 272 ? 18.02500  -4.74800  -35.48600 1.000 47.35000 ? 274 ASN A C   1 
ATOM   2053 O O   . ASN A 1 272 ? 18.49500  -5.71600  -34.87700 1.000 41.97000 ? 274 ASN A O   1 
ATOM   2054 C CB  . ASN A 1 272 ? 19.99800  -3.39200  -36.06100 1.000 35.20000 ? 274 ASN A CB  1 
ATOM   2055 C CG  . ASN A 1 272 ? 20.99200  -2.96200  -37.11300 1.000 36.29000 ? 274 ASN A CG  1 
ATOM   2056 O OD1 . ASN A 1 272 ? 20.94200  -3.41700  -38.25200 1.000 36.24000 ? 274 ASN A OD1 1 
ATOM   2057 N ND2 . ASN A 1 272 ? 21.89900  -2.08600  -36.73800 1.000 31.22000 ? 274 ASN A ND2 1 
ATOM   2058 N N   . GLY A 1 273 ? 16.86900  -4.19300  -35.13700 1.000 44.98000 ? 275 GLY A N   1 
ATOM   2059 C CA  . GLY A 1 273 ? 16.29300  -4.50500  -33.84600 1.000 47.35000 ? 275 GLY A CA  1 
ATOM   2060 C C   . GLY A 1 273 ? 17.08700  -3.84700  -32.73300 1.000 48.63000 ? 275 GLY A C   1 
ATOM   2061 O O   . GLY A 1 273 ? 17.92000  -2.95500  -32.95200 1.000 49.76000 ? 275 GLY A O   1 
ATOM   2062 N N   . MET A 1 274 ? 16.83700  -4.30500  -31.51500 1.000 52.56000 ? 276 MET A N   1 
ATOM   2063 C CA  . MET A 1 274 ? 17.47400  -3.68400  -30.36500 1.000 52.86000 ? 276 MET A CA  1 
ATOM   2064 C C   . MET A 1 274 ? 18.60400  -4.51500  -29.76400 1.000 61.19000 ? 276 MET A C   1 
ATOM   2065 O O   . MET A 1 274 ? 19.24900  -4.05000  -28.81100 1.000 59.17000 ? 276 MET A O   1 
ATOM   2066 C CB  . MET A 1 274 ? 16.41600  -3.34300  -29.30600 1.000 54.09000 ? 276 MET A CB  1 
ATOM   2067 C CG  . MET A 1 274 ? 15.63300  -2.09000  -29.70000 1.000 50.90000 ? 276 MET A CG  1 
ATOM   2068 S SD  . MET A 1 274 ? 14.33600  -1.47000  -28.59100 1.000 69.58000 ? 276 MET A SD  1 
ATOM   2069 C CE  . MET A 1 274 ? 15.30400  -0.95900  -27.18300 1.000 52.90000 ? 276 MET A CE  1 
ATOM   2070 N N   . ASN A 1 275 ? 18.89900  -5.68800  -30.34400 1.000 61.94000 ? 277 ASN A N   1 
ATOM   2071 C CA  . ASN A 1 275 ? 20.01100  -6.54900  -29.92500 1.000 59.73000 ? 277 ASN A CA  1 
ATOM   2072 C C   . ASN A 1 275 ? 20.04000  -6.71700  -28.40500 1.000 64.20000 ? 277 ASN A C   1 
ATOM   2073 O O   . ASN A 1 275 ? 21.04900  -6.45300  -27.74400 1.000 60.25000 ? 277 ASN A O   1 
ATOM   2074 C CB  . ASN A 1 275 ? 21.34600  -6.00800  -30.44700 1.000 60.26000 ? 277 ASN A CB  1 
ATOM   2075 N N   . GLY A 1 276 ? 18.90100  -7.14700  -27.85100 1.000 61.72000 ? 278 GLY A N   1 
ATOM   2076 C CA  . GLY A 1 276 ? 18.76300  -7.38800  -26.43000 1.000 63.19000 ? 278 GLY A CA  1 
ATOM   2077 C C   . GLY A 1 276 ? 18.83200  -6.16400  -25.54900 1.000 62.32000 ? 278 GLY A C   1 
ATOM   2078 O O   . GLY A 1 276 ? 18.72600  -6.29900  -24.32600 1.000 66.95000 ? 278 GLY A O   1 
ATOM   2079 N N   . ARG A 1 277 ? 18.93500  -4.99800  -26.12500 1.000 60.96000 ? 279 ARG A N   1 
ATOM   2080 C CA  . ARG A 1 277 ? 18.98500  -3.76700  -25.36900 1.000 58.79000 ? 279 ARG A CA  1 
ATOM   2081 C C   . ARG A 1 277 ? 17.66000  -3.10200  -25.10900 1.000 57.39000 ? 279 ARG A C   1 
ATOM   2082 O O   . ARG A 1 277 ? 16.65900  -3.56500  -25.54200 1.000 56.58000 ? 279 ARG A O   1 
ATOM   2083 C CB  . ARG A 1 277 ? 19.97000  -2.81300  -25.99300 1.000 55.64000 ? 279 ARG A CB  1 
ATOM   2084 C CG  . ARG A 1 277 ? 21.37700  -3.31300  -25.85600 1.000 58.20000 ? 279 ARG A CG  1 
ATOM   2085 C CD  . ARG A 1 277 ? 22.38000  -2.38900  -26.45000 1.000 56.10000 ? 279 ARG A CD  1 
ATOM   2086 N NE  . ARG A 1 277 ? 22.52900  -2.70100  -27.84800 1.000 61.44000 ? 279 ARG A NE  1 
ATOM   2087 C CZ  . ARG A 1 277 ? 23.45500  -2.17900  -28.63800 1.000 61.47000 ? 279 ARG A CZ  1 
ATOM   2088 N NH1 . ARG A 1 277 ? 24.34000  -1.30600  -28.16900 1.000 62.04000 ? 279 ARG A NH1 1 
ATOM   2089 N NH2 . ARG A 1 277 ? 23.50100  -2.55300  -29.89000 1.000 64.14000 ? 279 ARG A NH2 1 
ATOM   2090 N N   . THR A 1 278 ? 17.68600  -2.02900  -24.34800 1.000 55.13000 ? 280 THR A N   1 
ATOM   2091 C CA  . THR A 1 278 ? 16.50700  -1.30600  -24.01000 1.000 57.50000 ? 280 THR A CA  1 
ATOM   2092 C C   . THR A 1 278 ? 16.73900  0.14100   -24.16000 1.000 56.55000 ? 280 THR A C   1 
ATOM   2093 O O   . THR A 1 278 ? 17.84000  0.59300   -24.08300 1.000 54.91000 ? 280 THR A O   1 
ATOM   2094 C CB  . THR A 1 278 ? 16.09900  -1.47200  -22.55900 1.000 61.35000 ? 280 THR A CB  1 
ATOM   2095 O OG1 . THR A 1 278 ? 17.09600  -0.92700  -21.70800 1.000 62.79000 ? 280 THR A OG1 1 
ATOM   2096 C CG2 . THR A 1 278 ? 15.82400  -2.89200  -22.23200 1.000 58.01000 ? 280 THR A CG2 1 
ATOM   2097 N N   . ILE A 1 279 ? 15.66700  0.87300   -24.33700 1.000 59.47000 ? 281 ILE A N   1 
ATOM   2098 C CA  . ILE A 1 279 ? 15.82700  2.27900   -24.52000 1.000 59.81000 ? 281 ILE A CA  1 
ATOM   2099 C C   . ILE A 1 279 ? 15.48900  3.10700   -23.29800 1.000 61.17000 ? 281 ILE A C   1 
ATOM   2100 O O   . ILE A 1 279 ? 16.43200  3.54400   -22.66700 1.000 67.21000 ? 281 ILE A O   1 
ATOM   2101 C CB  . ILE A 1 279 ? 15.29100  2.76600   -25.88700 1.000 48.64000 ? 281 ILE A CB  1 
ATOM   2102 C CG1 . ILE A 1 279 ? 16.34200  2.47300   -26.92800 1.000 48.22000 ? 281 ILE A CG1 1 
ATOM   2103 C CG2 . ILE A 1 279 ? 15.03900  4.24500   -25.87400 1.000 47.22000 ? 281 ILE A CG2 1 
ATOM   2104 C CD1 . ILE A 1 279 ? 15.96800  2.75800   -28.34000 1.000 40.56000 ? 281 ILE A CD1 1 
ATOM   2105 N N   . LEU A 1 280 ? 14.23400  3.32000   -22.94000 1.000 56.92000 ? 282 LEU A N   1 
ATOM   2106 C CA  . LEU A 1 280 ? 14.00900  4.11400   -21.74000 1.000 61.73000 ? 282 LEU A CA  1 
ATOM   2107 C C   . LEU A 1 280 ? 13.94400  3.07900   -20.70900 1.000 65.08000 ? 282 LEU A C   1 
ATOM   2108 O O   . LEU A 1 280 ? 14.73000  3.03400   -19.81700 1.000 71.20000 ? 282 LEU A O   1 
ATOM   2109 C CB  . LEU A 1 280 ? 12.82000  4.95100   -21.86300 1.000 54.67000 ? 282 LEU A CB  1 
ATOM   2110 C CG  . LEU A 1 280 ? 13.56800  6.18900   -22.20800 1.000 50.84000 ? 282 LEU A CG  1 
ATOM   2111 C CD1 . LEU A 1 280 ? 12.79400  7.06900   -23.14000 1.000 47.98000 ? 282 LEU A CD1 1 
ATOM   2112 C CD2 . LEU A 1 280 ? 14.02900  6.97700   -21.02100 1.000 50.22000 ? 282 LEU A CD2 1 
ATOM   2113 N N   . GLY A 1 281 ? 13.06300  2.15600   -20.88800 1.000 62.33000 ? 283 GLY A N   1 
ATOM   2114 C CA  . GLY A 1 281 ? 13.03700  0.96700   -20.07300 1.000 65.21000 ? 283 GLY A CA  1 
ATOM   2115 C C   . GLY A 1 281 ? 12.41900  -0.14900  -20.85800 1.000 63.14000 ? 283 GLY A C   1 
ATOM   2116 O O   . GLY A 1 281 ? 12.11300  -1.18500  -20.34200 1.000 65.68000 ? 283 GLY A O   1 
ATOM   2117 N N   . SER A 1 282 ? 12.22200  0.08600   -22.12900 1.000 59.45000 ? 284 SER A N   1 
ATOM   2118 C CA  . SER A 1 282 ? 11.53700  -0.81200  -22.95700 1.000 55.59000 ? 284 SER A CA  1 
ATOM   2119 C C   . SER A 1 282 ? 12.42400  -1.42200  -23.93600 1.000 57.42000 ? 284 SER A C   1 
ATOM   2120 O O   . SER A 1 282 ? 13.45300  -0.88800  -24.28300 1.000 55.33000 ? 284 SER A O   1 
ATOM   2121 C CB  . SER A 1 282 ? 10.44600  -0.03200  -23.66400 1.000 52.48000 ? 284 SER A CB  1 
ATOM   2122 O OG  . SER A 1 282 ? 9.95400   -0.73700  -24.74600 1.000 54.43000 ? 284 SER A OG  1 
ATOM   2123 N N   . ALA A 1 283 ? 11.94700  -2.56300  -24.36200 1.000 55.11000 ? 285 ALA A N   1 
ATOM   2124 C CA  . ALA A 1 283 ? 12.53300  -3.38200  -25.34800 1.000 54.99000 ? 285 ALA A CA  1 
ATOM   2125 C C   . ALA A 1 283 ? 11.80300  -3.27500  -26.65400 1.000 56.61000 ? 285 ALA A C   1 
ATOM   2126 O O   . ALA A 1 283 ? 11.96900  -4.10200  -27.50900 1.000 57.95000 ? 285 ALA A O   1 
ATOM   2127 C CB  . ALA A 1 283 ? 12.48100  -4.77700  -24.87900 1.000 60.15000 ? 285 ALA A CB  1 
ATOM   2128 N N   . LEU A 1 284 ? 10.95200  -2.27600  -26.79000 1.000 57.42000 ? 286 LEU A N   1 
ATOM   2129 C CA  . LEU A 1 284 ? 10.20400  -2.09200  -28.00300 1.000 50.81000 ? 286 LEU A CA  1 
ATOM   2130 C C   . LEU A 1 284 ? 10.21200  -0.66600  -28.33200 1.000 46.42000 ? 286 LEU A C   1 
ATOM   2131 O O   . LEU A 1 284 ? 10.36800  0.13900   -27.49100 1.000 45.37000 ? 286 LEU A O   1 
ATOM   2132 C CB  . LEU A 1 284 ? 8.75900   -2.48800  -27.83000 1.000 58.13000 ? 286 LEU A CB  1 
ATOM   2133 N N   . LEU A 1 285 ? 10.04500  -0.36200  -29.58900 1.000 44.87000 ? 287 LEU A N   1 
ATOM   2134 C CA  . LEU A 1 285 ? 9.95500   1.03000   -30.00800 1.000 41.69000 ? 287 LEU A CA  1 
ATOM   2135 C C   . LEU A 1 285 ? 8.57600   1.54200   -29.60300 1.000 43.88000 ? 287 LEU A C   1 
ATOM   2136 O O   . LEU A 1 285 ? 7.55800   1.10000   -30.13700 1.000 39.90000 ? 287 LEU A O   1 
ATOM   2137 C CB  . LEU A 1 285 ? 10.21000  1.15000   -31.50500 1.000 39.99000 ? 287 LEU A CB  1 
ATOM   2138 C CG  . LEU A 1 285 ? 11.68900  0.84500   -31.82900 1.000 39.42000 ? 287 LEU A CG  1 
ATOM   2139 C CD1 . LEU A 1 285 ? 11.96000  1.08100   -33.28500 1.000 36.32000 ? 287 LEU A CD1 1 
ATOM   2140 C CD2 . LEU A 1 285 ? 12.63400  1.66500   -30.95400 1.000 40.82000 ? 287 LEU A CD2 1 
ATOM   2141 N N   . GLU A 1 286 ? 8.54300   2.46000   -28.64700 1.000 43.07000 ? 288 GLU A N   1 
ATOM   2142 C CA  . GLU A 1 286 ? 7.30500   2.90600   -28.02100 1.000 42.08000 ? 288 GLU A CA  1 
ATOM   2143 C C   . GLU A 1 286 ? 6.70800   4.08700   -28.78400 1.000 37.69000 ? 288 GLU A C   1 
ATOM   2144 O O   . GLU A 1 286 ? 7.39200   5.08900   -29.01500 1.000 35.19000 ? 288 GLU A O   1 
ATOM   2145 C CB  . GLU A 1 286 ? 7.60300   3.28500   -26.57100 1.000 40.64000 ? 288 GLU A CB  1 
ATOM   2146 C CG  . GLU A 1 286 ? 6.54000   4.10000   -25.93300 1.000 45.00000 ? 288 GLU A CG  1 
ATOM   2147 C CD  . GLU A 1 286 ? 5.27700   3.29600   -25.68500 1.000 50.25000 ? 288 GLU A CD  1 
ATOM   2148 O OE1 . GLU A 1 286 ? 5.39200   2.15400   -25.18100 1.000 52.28000 ? 288 GLU A OE1 1 
ATOM   2149 O OE2 . GLU A 1 286 ? 4.18400   3.79000   -26.05000 1.000 45.21000 ? 288 GLU A OE2 1 
ATOM   2150 N N   . ASP A 1 287 ? 5.43200   3.98200   -29.18400 1.000 36.90000 ? 289 ASP A N   1 
ATOM   2151 C CA  . ASP A 1 287 ? 4.84700   5.04000   -30.00400 1.000 34.49000 ? 289 ASP A CA  1 
ATOM   2152 C C   . ASP A 1 287 ? 3.63200   5.72100   -29.36300 1.000 36.68000 ? 289 ASP A C   1 
ATOM   2153 O O   . ASP A 1 287 ? 2.89100   6.42800   -30.04800 1.000 32.41000 ? 289 ASP A O   1 
ATOM   2154 C CB  . ASP A 1 287 ? 4.51500   4.50500   -31.40300 1.000 32.30000 ? 289 ASP A CB  1 
ATOM   2155 C CG  . ASP A 1 287 ? 3.19500   3.72800   -31.46900 1.000 33.74000 ? 289 ASP A CG  1 
ATOM   2156 O OD1 . ASP A 1 287 ? 2.67100   3.31400   -30.42200 1.000 32.02000 ? 289 ASP A OD1 1 
ATOM   2157 O OD2 . ASP A 1 287 ? 2.72200   3.48300   -32.60100 1.000 30.00000 ? 289 ASP A OD2 1 
ATOM   2158 N N   . GLU A 1 288 ? 3.43400   5.58300   -28.05300 1.000 37.38000 ? 290 GLU A N   1 
ATOM   2159 C CA  . GLU A 1 288 ? 2.28600   6.21200   -27.41100 1.000 36.47000 ? 290 GLU A CA  1 
ATOM   2160 C C   . GLU A 1 288 ? 2.71400   7.30600   -26.42500 1.000 38.95000 ? 290 GLU A C   1 
ATOM   2161 O O   . GLU A 1 288 ? 2.04900   7.52500   -25.41700 1.000 37.01000 ? 290 GLU A O   1 
ATOM   2162 C CB  . GLU A 1 288 ? 1.38600   5.15300   -26.75100 1.000 36.26000 ? 290 GLU A CB  1 
ATOM   2163 C CG  . GLU A 1 288 ? 0.94400   4.00700   -27.71500 1.000 36.40000 ? 290 GLU A CG  1 
ATOM   2164 C CD  . GLU A 1 288 ? -0.50900  3.46500   -27.52300 1.000 41.75000 ? 290 GLU A CD  1 
ATOM   2165 O OE1 . GLU A 1 288 ? -1.04700  3.49500   -26.39800 1.000 39.35000 ? 290 GLU A OE1 1 
ATOM   2166 O OE2 . GLU A 1 288 ? -1.11300  2.97000   -28.51700 1.000 38.05000 ? 290 GLU A OE2 1 
ATOM   2167 N N   . PHE A 1 289 ? 3.82200   8.01200   -26.70800 1.000 36.31000 ? 291 PHE A N   1 
ATOM   2168 C CA  . PHE A 1 289 ? 4.18400   9.26000   -26.02700 1.000 37.54000 ? 291 PHE A CA  1 
ATOM   2169 C C   . PHE A 1 289 ? 4.37600   10.35700  -27.05900 1.000 39.07000 ? 291 PHE A C   1 
ATOM   2170 O O   . PHE A 1 289 ? 5.19600   10.21000  -27.97100 1.000 38.37000 ? 291 PHE A O   1 
ATOM   2171 C CB  . PHE A 1 289 ? 5.49600   9.18800   -25.24100 1.000 38.82000 ? 291 PHE A CB  1 
ATOM   2172 C CG  . PHE A 1 289 ? 5.52700   8.19300   -24.14200 1.000 45.53000 ? 291 PHE A CG  1 
ATOM   2173 C CD1 . PHE A 1 289 ? 5.04100   8.51600   -22.88900 1.000 47.50000 ? 291 PHE A CD1 1 
ATOM   2174 C CD2 . PHE A 1 289 ? 6.14000   6.96100   -24.32400 1.000 48.24000 ? 291 PHE A CD2 1 
ATOM   2175 C CE1 . PHE A 1 289 ? 5.10600   7.59300   -21.84600 1.000 52.50000 ? 291 PHE A CE1 1 
ATOM   2176 C CE2 . PHE A 1 289 ? 6.21800   6.03400   -23.28100 1.000 50.10000 ? 291 PHE A CE2 1 
ATOM   2177 C CZ  . PHE A 1 289 ? 5.70200   6.34200   -22.05100 1.000 51.67000 ? 291 PHE A CZ  1 
ATOM   2178 N N   . THR A 1 290 ? 3.71200   11.47400  -26.87000 1.000 38.11000 ? 292 THR A N   1 
ATOM   2179 C CA  . THR A 1 290 ? 3.76900   12.48600  -27.91000 1.000 36.96000 ? 292 THR A CA  1 
ATOM   2180 C C   . THR A 1 290 ? 4.93100   13.45100  -27.68600 1.000 38.21000 ? 292 THR A C   1 
ATOM   2181 O O   . THR A 1 290 ? 5.52600   13.48900  -26.61300 1.000 37.68000 ? 292 THR A O   1 
ATOM   2182 C CB  . THR A 1 290 ? 2.45700   13.25300  -27.94700 1.000 37.41000 ? 292 THR A CB  1 
ATOM   2183 O OG1 . THR A 1 290 ? 2.40100   14.12200  -26.81700 1.000 37.88000 ? 292 THR A OG1 1 
ATOM   2184 C CG2 . THR A 1 290 ? 1.27500   12.27700  -27.89700 1.000 35.36000 ? 292 THR A CG2 1 
ATOM   2185 N N   . PRO A 1 291 ? 5.29200   14.23300  -28.70700 1.000 36.78000 ? 293 PRO A N   1 
ATOM   2186 C CA  . PRO A 1 291 ? 6.23400   15.34400  -28.48300 1.000 36.98000 ? 293 PRO A CA  1 
ATOM   2187 C C   . PRO A 1 291 ? 5.85100   16.24200  -27.31600 1.000 43.19000 ? 293 PRO A C   1 
ATOM   2188 O O   . PRO A 1 291 ? 6.71400   16.60100  -26.49200 1.000 40.99000 ? 293 PRO A O   1 
ATOM   2189 C CB  . PRO A 1 291 ? 6.18300   16.09800  -29.81600 1.000 35.26000 ? 293 PRO A CB  1 
ATOM   2190 C CG  . PRO A 1 291 ? 5.88300   15.02800  -30.82500 1.000 36.95000 ? 293 PRO A CG  1 
ATOM   2191 C CD  . PRO A 1 291 ? 4.99000   14.03300  -30.13600 1.000 35.96000 ? 293 PRO A CD  1 
ATOM   2192 N N   . PHE A 1 292 ? 4.56800   16.61400  -27.23500 1.000 39.75000 ? 294 PHE A N   1 
ATOM   2193 C CA  . PHE A 1 292 ? 4.05200   17.39100  -26.11000 1.000 40.90000 ? 294 PHE A CA  1 
ATOM   2194 C C   . PHE A 1 292 ? 4.26100   16.65900  -24.78700 1.000 43.61000 ? 294 PHE A C   1 
ATOM   2195 O O   . PHE A 1 292 ? 4.67200   17.26800  -23.79500 1.000 46.50000 ? 294 PHE A O   1 
ATOM   2196 C CB  . PHE A 1 292 ? 2.56600   17.69700  -26.35200 1.000 44.42000 ? 294 PHE A CB  1 
ATOM   2197 C CG  . PHE A 1 292 ? 1.95600   18.69900  -25.38300 1.000 49.18000 ? 294 PHE A CG  1 
ATOM   2198 C CD1 . PHE A 1 292 ? 1.56000   18.31200  -24.10800 1.000 46.65000 ? 294 PHE A CD1 1 
ATOM   2199 C CD2 . PHE A 1 292 ? 1.74500   20.01800  -25.76900 1.000 50.51000 ? 294 PHE A CD2 1 
ATOM   2200 C CE1 . PHE A 1 292 ? 0.98700   19.23100  -23.22200 1.000 49.72000 ? 294 PHE A CE1 1 
ATOM   2201 C CE2 . PHE A 1 292 ? 1.17300   20.94000  -24.89400 1.000 51.86000 ? 294 PHE A CE2 1 
ATOM   2202 C CZ  . PHE A 1 292 ? 0.79600   20.54400  -23.61900 1.000 53.01000 ? 294 PHE A CZ  1 
ATOM   2203 N N   . ASP A 1 293 ? 3.99100   15.34500  -24.75500 1.000 42.00000 ? 295 ASP A N   1 
ATOM   2204 C CA  . ASP A 1 293 ? 4.20200   14.56200  -23.53400 1.000 39.49000 ? 295 ASP A CA  1 
ATOM   2205 C C   . ASP A 1 293 ? 5.65400   14.61900  -23.07400 1.000 48.29000 ? 295 ASP A C   1 
ATOM   2206 O O   . ASP A 1 293 ? 5.92300   14.71900  -21.87100 1.000 51.78000 ? 295 ASP A O   1 
ATOM   2207 C CB  . ASP A 1 293 ? 3.80800   13.09300  -23.75100 1.000 35.70000 ? 295 ASP A CB  1 
ATOM   2208 C CG  . ASP A 1 293 ? 2.29000   12.86800  -23.74100 1.000 46.25000 ? 295 ASP A CG  1 
ATOM   2209 O OD1 . ASP A 1 293 ? 1.57100   13.72800  -23.18300 1.000 44.09000 ? 295 ASP A OD1 1 
ATOM   2210 O OD2 . ASP A 1 293 ? 1.82400   11.83000  -24.29600 1.000 39.06000 ? 295 ASP A OD2 1 
ATOM   2211 N N   . VAL A 1 294 ? 6.60300   14.53000  -24.01500 1.000 44.84000 ? 296 VAL A N   1 
ATOM   2212 C CA  . VAL A 1 294 ? 8.00900   14.35000  -23.65300 1.000 47.49000 ? 296 VAL A CA  1 
ATOM   2213 C C   . VAL A 1 294 ? 8.52000   15.56300  -22.88900 1.000 52.71000 ? 296 VAL A C   1 
ATOM   2214 O O   . VAL A 1 294 ? 9.20800   15.43300  -21.86900 1.000 53.24000 ? 296 VAL A O   1 
ATOM   2215 C CB  . VAL A 1 294 ? 8.85300   14.06600  -24.91600 1.000 41.48000 ? 296 VAL A CB  1 
ATOM   2216 C CG1 . VAL A 1 294 ? 10.33100  14.36200  -24.66900 1.000 44.54000 ? 296 VAL A CG1 1 
ATOM   2217 C CG2 . VAL A 1 294 ? 8.66500   12.63100  -25.36100 1.000 36.22000 ? 296 VAL A CG2 1 
ATOM   2218 N N   . VAL A 1 295 ? 8.18400   16.76400  -23.36200 1.000 54.18000 ? 297 VAL A N   1 
ATOM   2219 C CA  . VAL A 1 295 ? 8.57100   17.98100  -22.65300 1.000 56.87000 ? 297 VAL A CA  1 
ATOM   2220 C C   . VAL A 1 295 ? 8.11100   17.93300  -21.19600 1.000 59.97000 ? 297 VAL A C   1 
ATOM   2221 O O   . VAL A 1 295 ? 8.80100   18.41900  -20.29100 1.000 64.91000 ? 297 VAL A O   1 
ATOM   2222 C CB  . VAL A 1 295 ? 8.02100   19.21300  -23.39300 1.000 55.92000 ? 297 VAL A CB  1 
ATOM   2223 C CG1 . VAL A 1 295 ? 8.38200   20.48200  -22.65600 1.000 57.85000 ? 297 VAL A CG1 1 
ATOM   2224 C CG2 . VAL A 1 295 ? 8.55500   19.23300  -24.81800 1.000 48.04000 ? 297 VAL A CG2 1 
ATOM   2225 N N   . ARG A 1 296 ? 6.95500   17.32300  -20.93800 1.000 63.89000 ? 298 ARG A N   1 
ATOM   2226 C CA  . ARG A 1 296 ? 6.49100   17.12400  -19.56100 1.000 57.24000 ? 298 ARG A CA  1 
ATOM   2227 C C   . ARG A 1 296 ? 7.14600   15.90300  -18.91900 1.000 57.07000 ? 298 ARG A C   1 
ATOM   2228 O O   . ARG A 1 296 ? 8.34500   15.91500  -18.61000 1.000 65.27000 ? 298 ARG A O   1 
ATOM   2229 C CB  . ARG A 1 296 ? 4.96900   16.97900  -19.52800 1.000 58.13000 ? 298 ARG A CB  1 
ATOM   2230 N N   . PHE B 1 1   ? -3.81100  -6.44000  -24.25800 1.000 67.42000 ? 3   PHE B N   1 
ATOM   2231 C CA  . PHE B 1 1   ? -4.04100  -6.45200  -22.81300 1.000 69.12000 ? 3   PHE B CA  1 
ATOM   2232 C C   . PHE B 1 1   ? -3.38000  -5.25100  -22.13900 1.000 66.28000 ? 3   PHE B C   1 
ATOM   2233 O O   . PHE B 1 1   ? -2.15800  -5.09100  -22.19900 1.000 70.67000 ? 3   PHE B O   1 
ATOM   2234 C CB  . PHE B 1 1   ? -3.51600  -7.75400  -22.19600 1.000 68.29000 ? 3   PHE B CB  1 
ATOM   2235 C CG  . PHE B 1 1   ? -4.21900  -8.15900  -20.92500 1.000 64.52000 ? 3   PHE B CG  1 
ATOM   2236 C CD1 . PHE B 1 1   ? -5.58400  -8.39300  -20.91100 1.000 69.77000 ? 3   PHE B CD1 1 
ATOM   2237 C CD2 . PHE B 1 1   ? -3.50800  -8.32100  -19.74900 1.000 61.92000 ? 3   PHE B CD2 1 
ATOM   2238 C CE1 . PHE B 1 1   ? -6.22900  -8.77000  -19.74400 1.000 69.53000 ? 3   PHE B CE1 1 
ATOM   2239 C CE2 . PHE B 1 1   ? -4.14600  -8.69700  -18.57700 1.000 63.84000 ? 3   PHE B CE2 1 
ATOM   2240 C CZ  . PHE B 1 1   ? -5.50600  -8.92000  -18.57300 1.000 66.65000 ? 3   PHE B CZ  1 
ATOM   2241 N N   . ARG B 1 2   ? -4.18400  -4.40700  -21.49500 1.000 63.99000 ? 4   ARG B N   1 
ATOM   2242 C CA  . ARG B 1 2   ? -3.67600  -3.22100  -20.81900 1.000 55.59000 ? 4   ARG B CA  1 
ATOM   2243 C C   . ARG B 1 2   ? -3.53800  -3.48300  -19.32900 1.000 52.84000 ? 4   ARG B C   1 
ATOM   2244 O O   . ARG B 1 2   ? -4.44200  -4.04200  -18.70100 1.000 55.64000 ? 4   ARG B O   1 
ATOM   2245 C CB  . ARG B 1 2   ? -4.59300  -2.01900  -21.03600 1.000 55.84000 ? 4   ARG B CB  1 
ATOM   2246 C CG  . ARG B 1 2   ? -4.61300  -1.49800  -22.44100 1.000 50.60000 ? 4   ARG B CG  1 
ATOM   2247 C CD  . ARG B 1 2   ? -3.95800  -0.13100  -22.51900 1.000 49.42000 ? 4   ARG B CD  1 
ATOM   2248 N NE  . ARG B 1 2   ? -3.86200  0.32500   -23.90400 1.000 48.39000 ? 4   ARG B NE  1 
ATOM   2249 C CZ  . ARG B 1 2   ? -2.88500  1.09500   -24.38000 1.000 46.28000 ? 4   ARG B CZ  1 
ATOM   2250 N NH1 . ARG B 1 2   ? -1.91100  1.51500   -23.58300 1.000 47.98000 ? 4   ARG B NH1 1 
ATOM   2251 N NH2 . ARG B 1 2   ? -2.88600  1.46100   -25.65900 1.000 40.86000 ? 4   ARG B NH2 1 
ATOM   2252 N N   . LYS B 1 3   ? -2.50400  -2.98200  -18.75300 1.000 50.34000 ? 5   LYS B N   1 
ATOM   2253 C CA  . LYS B 1 3   ? -2.39900  -3.01100  -17.35400 1.000 48.16000 ? 5   LYS B CA  1 
ATOM   2254 C C   . LYS B 1 3   ? -3.26700  -1.83400  -16.95600 1.000 41.45000 ? 5   LYS B C   1 
ATOM   2255 O O   . LYS B 1 3   ? -3.20700  -0.84500  -17.60300 1.000 42.64000 ? 5   LYS B O   1 
ATOM   2256 C CB  . LYS B 1 3   ? -0.98600  -2.68900  -16.96300 1.000 52.66000 ? 5   LYS B CB  1 
ATOM   2257 C CG  . LYS B 1 3   ? -0.12000  -3.86900  -16.67800 1.000 55.90000 ? 5   LYS B CG  1 
ATOM   2258 C CD  . LYS B 1 3   ? 1.27400   -3.42400  -16.38000 1.000 52.03000 ? 5   LYS B CD  1 
ATOM   2259 C CE  . LYS B 1 3   ? 1.66800   -4.15100  -15.15800 1.000 49.46000 ? 5   LYS B CE  1 
ATOM   2260 N NZ  . LYS B 1 3   ? 0.76600   -3.70300  -14.10200 1.000 53.68000 ? 5   LYS B NZ  1 
ATOM   2261 N N   . MET B 1 4   ? -4.05300  -1.94000  -15.92300 1.000 37.31000 ? 6   MET B N   1 
ATOM   2262 C CA  . MET B 1 4   ? -4.84100  -0.82500  -15.48500 1.000 38.30000 ? 6   MET B CA  1 
ATOM   2263 C C   . MET B 1 4   ? -4.49200  -0.41100  -14.08500 1.000 32.27000 ? 6   MET B C   1 
ATOM   2264 O O   . MET B 1 4   ? -4.16300  -1.21500  -13.32200 1.000 34.57000 ? 6   MET B O   1 
ATOM   2265 C CB  . MET B 1 4   ? -6.33000  -1.06800  -15.61800 1.000 36.67000 ? 6   MET B CB  1 
ATOM   2266 C CG  . MET B 1 4   ? -6.90700  -0.80800  -16.99300 1.000 41.22000 ? 6   MET B CG  1 
ATOM   2267 S SD  . MET B 1 4   ? -8.66200  -0.79800  -17.11900 1.000 40.52000 ? 6   MET B SD  1 
ATOM   2268 C CE  . MET B 1 4   ? -9.04600  -2.20600  -16.19600 1.000 40.37000 ? 6   MET B CE  1 
ATOM   2269 N N   . ALA B 1 5   ? -4.56600  0.85900   -13.78600 1.000 30.68000 ? 7   ALA B N   1 
ATOM   2270 C CA  . ALA B 1 5   ? -4.36800  1.36700   -12.47200 1.000 28.66000 ? 7   ALA B CA  1 
ATOM   2271 C C   . ALA B 1 5   ? -5.72800  1.55400   -11.88400 1.000 31.42000 ? 7   ALA B C   1 
ATOM   2272 O O   . ALA B 1 5   ? -6.65400  1.65500   -12.57800 1.000 30.34000 ? 7   ALA B O   1 
ATOM   2273 C CB  . ALA B 1 5   ? -3.66100  2.67400   -12.50100 1.000 27.74000 ? 7   ALA B CB  1 
ATOM   2274 N N   . PHE B 1 6   ? -5.82100  1.60000   -10.58400 1.000 25.62000 ? 8   PHE B N   1 
ATOM   2275 C CA  . PHE B 1 6   ? -7.04000  1.83900   -9.91600  1.000 26.29000 ? 8   PHE B CA  1 
ATOM   2276 C C   . PHE B 1 6   ? -7.46100  3.29000   -10.05400 1.000 25.68000 ? 8   PHE B C   1 
ATOM   2277 O O   . PHE B 1 6   ? -6.66600  4.09800   -10.11700 1.000 29.03000 ? 8   PHE B O   1 
ATOM   2278 C CB  . PHE B 1 6   ? -6.91400  1.53600   -8.44200  1.000 29.68000 ? 8   PHE B CB  1 
ATOM   2279 C CG  . PHE B 1 6   ? -6.88600  0.10500   -8.10000  1.000 31.38000 ? 8   PHE B CG  1 
ATOM   2280 C CD1 . PHE B 1 6   ? -8.00600  -0.60900  -8.06900  1.000 36.51000 ? 8   PHE B CD1 1 
ATOM   2281 C CD2 . PHE B 1 6   ? -5.73900  -0.50000  -7.78700  1.000 30.77000 ? 8   PHE B CD2 1 
ATOM   2282 C CE1 . PHE B 1 6   ? -7.97700  -1.92200  -7.76600  1.000 41.07000 ? 8   PHE B CE1 1 
ATOM   2283 C CE2 . PHE B 1 6   ? -5.69900  -1.80800  -7.47600  1.000 33.29000 ? 8   PHE B CE2 1 
ATOM   2284 C CZ  . PHE B 1 6   ? -6.81900  -2.52200  -7.45800  1.000 35.08000 ? 8   PHE B CZ  1 
ATOM   2285 N N   . PRO B 1 7   ? -8.71900  3.59600   -10.10100 1.000 28.18000 ? 9   PRO B N   1 
ATOM   2286 C CA  . PRO B 1 7   ? -9.15000  4.99800   -10.05500 1.000 28.32000 ? 9   PRO B CA  1 
ATOM   2287 C C   . PRO B 1 7   ? -8.60000  5.65000   -8.79400  1.000 29.55000 ? 9   PRO B C   1 
ATOM   2288 O O   . PRO B 1 7   ? -8.61800  5.06700   -7.70600  1.000 29.51000 ? 9   PRO B O   1 
ATOM   2289 C CB  . PRO B 1 7   ? -10.68300 4.90000   -10.03200 1.000 30.59000 ? 9   PRO B CB  1 
ATOM   2290 C CG  . PRO B 1 7   ? -11.01300 3.54700   -10.53100 1.000 30.43000 ? 9   PRO B CG  1 
ATOM   2291 C CD  . PRO B 1 7   ? -9.85100  2.66100   -10.14500 1.000 28.16000 ? 9   PRO B CD  1 
ATOM   2292 N N   . SER B 1 8   ? -8.06300  6.84900   -8.94800  1.000 29.85000 ? 10  SER B N   1 
ATOM   2293 C CA  . SER B 1 8   ? -7.23900  7.43500   -7.89600  1.000 29.38000 ? 10  SER B CA  1 
ATOM   2294 C C   . SER B 1 8   ? -7.96300  8.50900   -7.09100  1.000 30.61000 ? 10  SER B C   1 
ATOM   2295 O O   . SER B 1 8   ? -7.36800  9.07400   -6.16500  1.000 31.61000 ? 10  SER B O   1 
ATOM   2296 C CB  . SER B 1 8   ? -5.95600  8.00400   -8.50200  1.000 26.42000 ? 10  SER B CB  1 
ATOM   2297 O OG  . SER B 1 8   ? -6.25300  8.94700   -9.51600  1.000 28.57000 ? 10  SER B OG  1 
ATOM   2298 N N   . GLY B 1 9   ? -9.24500  8.75700   -7.39600  1.000 29.99000 ? 11  GLY B N   1 
ATOM   2299 C CA  . GLY B 1 9   ? -9.98000  9.83900   -6.75100  1.000 30.07000 ? 11  GLY B CA  1 
ATOM   2300 C C   . GLY B 1 9   ? -9.95900  9.81400   -5.23100  1.000 30.21000 ? 11  GLY B C   1 
ATOM   2301 O O   . GLY B 1 9   ? -9.81700  10.85500  -4.59300  1.000 33.00000 ? 11  GLY B O   1 
ATOM   2302 N N   . LYS B 1 10  ? -10.11700 8.63400   -4.62900  1.000 27.52000 ? 12  LYS B N   1 
ATOM   2303 C CA  . LYS B 1 10  ? -10.14800 8.56800   -3.16600  1.000 33.88000 ? 12  LYS B CA  1 
ATOM   2304 C C   . LYS B 1 10  ? -8.81400  8.96600   -2.54000  1.000 32.22000 ? 12  LYS B C   1 
ATOM   2305 O O   . LYS B 1 10  ? -8.78400  9.49400   -1.41800  1.000 33.36000 ? 12  LYS B O   1 
ATOM   2306 C CB  . LYS B 1 10  ? -10.53200 7.16200   -2.70900  1.000 33.88000 ? 12  LYS B CB  1 
ATOM   2307 C CG  . LYS B 1 10  ? -11.96800 6.79200   -2.99300  1.000 36.02000 ? 12  LYS B CG  1 
ATOM   2308 C CD  . LYS B 1 10  ? -12.14500 5.28900   -2.86400  1.000 40.94000 ? 12  LYS B CD  1 
ATOM   2309 C CE  . LYS B 1 10  ? -13.56500 4.92600   -2.46700  1.000 48.92000 ? 12  LYS B CE  1 
ATOM   2310 N NZ  . LYS B 1 10  ? -14.44900 4.80100   -3.65500  1.000 50.60000 ? 12  LYS B NZ  1 
ATOM   2311 N N   . VAL B 1 11  ? -7.70800  8.72200   -3.23200  1.000 29.10000 ? 13  VAL B N   1 
ATOM   2312 C CA  . VAL B 1 11  ? -6.39200  9.08300   -2.71400  1.000 29.87000 ? 13  VAL B CA  1 
ATOM   2313 C C   . VAL B 1 11  ? -6.05500  10.53200  -3.03300  1.000 31.54000 ? 13  VAL B C   1 
ATOM   2314 O O   . VAL B 1 11  ? -5.40200  11.21600  -2.23700  1.000 30.80000 ? 13  VAL B O   1 
ATOM   2315 C CB  . VAL B 1 11  ? -5.32800  8.11800   -3.28600  1.000 29.89000 ? 13  VAL B CB  1 
ATOM   2316 C CG1 . VAL B 1 11  ? -3.91900  8.48100   -2.77400  1.000 27.50000 ? 13  VAL B CG1 1 
ATOM   2317 C CG2 . VAL B 1 11  ? -5.70600  6.66500   -2.97200  1.000 27.63000 ? 13  VAL B CG2 1 
ATOM   2318 N N   . GLU B 1 12  ? -6.51100  11.01200  -4.19300  1.000 32.08000 ? 14  GLU B N   1 
ATOM   2319 C CA  . GLU B 1 12  ? -6.28400  12.40100  -4.57500  1.000 30.97000 ? 14  GLU B CA  1 
ATOM   2320 C C   . GLU B 1 12  ? -6.70500  13.36600  -3.46800  1.000 30.79000 ? 14  GLU B C   1 
ATOM   2321 O O   . GLU B 1 12  ? -5.98600  14.32200  -3.16400  1.000 32.20000 ? 14  GLU B O   1 
ATOM   2322 C CB  . GLU B 1 12  ? -7.02900  12.71100  -5.87600  1.000 30.04000 ? 14  GLU B CB  1 
ATOM   2323 C CG  . GLU B 1 12  ? -6.31800  12.20000  -7.14900  1.000 29.30000 ? 14  GLU B CG  1 
ATOM   2324 C CD  . GLU B 1 12  ? -7.21300  12.28600  -8.39600  1.000 34.60000 ? 14  GLU B CD  1 
ATOM   2325 O OE1 . GLU B 1 12  ? -7.49400  11.22900  -9.02300  1.000 31.38000 ? 14  GLU B OE1 1 
ATOM   2326 O OE2 . GLU B 1 12  ? -7.62600  13.41400  -8.75700  1.000 32.82000 ? 14  GLU B OE2 1 
ATOM   2327 N N   . GLY B 1 13  ? -7.85500  13.12200  -2.84300  1.000 31.96000 ? 15  GLY B N   1 
ATOM   2328 C CA  . GLY B 1 13  ? -8.33500  13.98300  -1.77400  1.000 32.48000 ? 15  GLY B CA  1 
ATOM   2329 C C   . GLY B 1 13  ? -7.55500  13.90800  -0.48000  1.000 35.15000 ? 15  GLY B C   1 
ATOM   2330 O O   . GLY B 1 13  ? -7.91600  14.60300  0.47400   1.000 38.06000 ? 15  GLY B O   1 
ATOM   2331 N N   . CYS B 1 14  ? -6.49700  13.09800  -0.41600  1.000 35.84000 ? 16  CYS B N   1 
ATOM   2332 C CA  . CYS B 1 14  ? -5.66800  12.97800  0.77700   1.000 34.85000 ? 16  CYS B CA  1 
ATOM   2333 C C   . CYS B 1 14  ? -4.29100  13.58600  0.62600   1.000 35.32000 ? 16  CYS B C   1 
ATOM   2334 O O   . CYS B 1 14  ? -3.53500  13.59500  1.59700   1.000 34.84000 ? 16  CYS B O   1 
ATOM   2335 C CB  . CYS B 1 14  ? -5.50500  11.50900  1.16700   1.000 32.01000 ? 16  CYS B CB  1 
ATOM   2336 S SG  . CYS B 1 14  ? -7.05300  10.70700  1.42200   1.000 36.30000 ? 16  CYS B SG  1 
ATOM   2337 N N   . MET B 1 15  ? -3.93500  14.08700  -0.54900  1.000 35.39000 ? 17  MET B N   1 
ATOM   2338 C CA  . MET B 1 15  ? -2.55900  14.48200  -0.81600  1.000 35.86000 ? 17  MET B CA  1 
ATOM   2339 C C   . MET B 1 15  ? -2.31700  15.93200  -0.40300  1.000 37.32000 ? 17  MET B C   1 
ATOM   2340 O O   . MET B 1 15  ? -3.07100  16.82800  -0.78800  1.000 35.13000 ? 17  MET B O   1 
ATOM   2341 C CB  . MET B 1 15  ? -2.23500  14.28200  -2.29500  1.000 32.85000 ? 17  MET B CB  1 
ATOM   2342 C CG  . MET B 1 15  ? -2.28400  12.81900  -2.75200  1.000 32.67000 ? 17  MET B CG  1 
ATOM   2343 S SD  . MET B 1 15  ? -1.34800  11.69900  -1.65700  1.000 33.43000 ? 17  MET B SD  1 
ATOM   2344 C CE  . MET B 1 15  ? 0.28800   12.42200  -1.73000  1.000 33.10000 ? 17  MET B CE  1 
ATOM   2345 N N   . VAL B 1 16  ? -1.28300  16.16300  0.36700   1.000 35.59000 ? 18  VAL B N   1 
ATOM   2346 C CA  . VAL B 1 16  ? -0.90700  17.47600  0.82600   1.000 35.98000 ? 18  VAL B CA  1 
ATOM   2347 C C   . VAL B 1 16  ? 0.55300   17.71000  0.67800   1.000 38.01000 ? 18  VAL B C   1 
ATOM   2348 O O   . VAL B 1 16  ? 1.28600   16.81500  0.47700   1.000 39.28000 ? 18  VAL B O   1 
ATOM   2349 C CB  . VAL B 1 16  ? -1.28200  17.70900  2.28500   1.000 36.44000 ? 18  VAL B CB  1 
ATOM   2350 C CG1 . VAL B 1 16  ? -2.73300  17.47200  2.54000   1.000 36.18000 ? 18  VAL B CG1 1 
ATOM   2351 C CG2 . VAL B 1 16  ? -0.48800  16.84100  3.19900   1.000 34.11000 ? 18  VAL B CG2 1 
ATOM   2352 N N   . GLN B 1 17  ? 0.95700   18.94300  0.79000   1.000 40.44000 ? 19  GLN B N   1 
ATOM   2353 C CA  . GLN B 1 17  ? 2.35100   19.35200  0.73200   1.000 43.13000 ? 19  GLN B CA  1 
ATOM   2354 C C   . GLN B 1 17  ? 2.91500   19.61200  2.13700   1.000 43.97000 ? 19  GLN B C   1 
ATOM   2355 O O   . GLN B 1 17  ? 2.30100   20.21700  2.93000   1.000 44.34000 ? 19  GLN B O   1 
ATOM   2356 C CB  . GLN B 1 17  ? 2.48400   20.58900  -0.12500  1.000 44.92000 ? 19  GLN B CB  1 
ATOM   2357 C CG  . GLN B 1 17  ? 3.85900   21.19500  -0.23700  1.000 50.19000 ? 19  GLN B CG  1 
ATOM   2358 C CD  . GLN B 1 17  ? 3.90700   22.39100  -1.13400  1.000 48.85000 ? 19  GLN B CD  1 
ATOM   2359 O OE1 . GLN B 1 17  ? 4.78500   22.55000  -1.88800  1.000 56.64000 ? 19  GLN B OE1 1 
ATOM   2360 N NE2 . GLN B 1 17  ? 2.95500   23.20900  -1.03700  1.000 54.01000 ? 19  GLN B NE2 1 
ATOM   2361 N N   . VAL B 1 18  ? 4.08100   19.09800  2.42600   1.000 43.26000 ? 20  VAL B N   1 
ATOM   2362 C CA  . VAL B 1 18  ? 4.71500   19.27400  3.69600   1.000 42.97000 ? 20  VAL B CA  1 
ATOM   2363 C C   . VAL B 1 18  ? 6.07600   19.88400  3.54000   1.000 46.95000 ? 20  VAL B C   1 
ATOM   2364 O O   . VAL B 1 18  ? 6.86800   19.45000  2.75400   1.000 44.40000 ? 20  VAL B O   1 
ATOM   2365 C CB  . VAL B 1 18  ? 4.85600   17.98900  4.45400   1.000 40.93000 ? 20  VAL B CB  1 
ATOM   2366 C CG1 . VAL B 1 18  ? 5.49100   18.23500  5.78300   1.000 38.75000 ? 20  VAL B CG1 1 
ATOM   2367 C CG2 . VAL B 1 18  ? 3.53900   17.32400  4.60800   1.000 33.08000 ? 20  VAL B CG2 1 
ATOM   2368 N N   . THR B 1 19  ? 6.31500   20.91400  4.32400   1.000 48.75000 ? 21  THR B N   1 
ATOM   2369 C CA  . THR B 1 19  ? 7.55400   21.65400  4.28600   1.000 50.30000 ? 21  THR B CA  1 
ATOM   2370 C C   . THR B 1 19  ? 8.19800   21.84600  5.65500   1.000 51.40000 ? 21  THR B C   1 
ATOM   2371 O O   . THR B 1 19  ? 7.57000   22.20100  6.58900   1.000 47.57000 ? 21  THR B O   1 
ATOM   2372 C CB  . THR B 1 19  ? 7.35000   23.02500  3.62600   1.000 50.27000 ? 21  THR B CB  1 
ATOM   2373 O OG1 . THR B 1 19  ? 6.93300   22.88200  2.28600   1.000 51.34000 ? 21  THR B OG1 1 
ATOM   2374 C CG2 . THR B 1 19  ? 8.58000   23.79700  3.62300   1.000 52.35000 ? 21  THR B CG2 1 
ATOM   2375 N N   . CYS B 1 20  ? 9.47200   21.57600  5.71600   1.000 51.61000 ? 22  CYS B N   1 
ATOM   2376 C CA  . CYS B 1 20  ? 10.21500  21.79400  6.88600   1.000 52.98000 ? 22  CYS B CA  1 
ATOM   2377 C C   . CYS B 1 20  ? 11.42400  22.48700  6.38200   1.000 53.21000 ? 22  CYS B C   1 
ATOM   2378 O O   . CYS B 1 20  ? 12.16200  21.92900  5.65600   1.000 53.70000 ? 22  CYS B O   1 
ATOM   2379 C CB  . CYS B 1 20  ? 10.55600  20.51200  7.53000   1.000 49.87000 ? 22  CYS B CB  1 
ATOM   2380 S SG  . CYS B 1 20  ? 11.12000  20.70000  9.16400   1.000 58.15000 ? 22  CYS B SG  1 
ATOM   2381 N N   . GLY B 1 21  ? 11.60700  23.72500  6.79100   1.000 54.24000 ? 23  GLY B N   1 
ATOM   2382 C CA  . GLY B 1 21  ? 12.73100  24.54200  6.36800   1.000 55.74000 ? 23  GLY B CA  1 
ATOM   2383 C C   . GLY B 1 21  ? 12.79000  24.67600  4.85900   1.000 59.10000 ? 23  GLY B C   1 
ATOM   2384 O O   . GLY B 1 21  ? 11.88000  25.21900  4.21800   1.000 61.89000 ? 23  GLY B O   1 
ATOM   2385 N N   . THR B 1 22  ? 13.88200  24.17900  4.27800   1.000 57.26000 ? 24  THR B N   1 
ATOM   2386 C CA  . THR B 1 22  ? 14.10400  24.23400  2.84000   1.000 58.67000 ? 24  THR B CA  1 
ATOM   2387 C C   . THR B 1 22  ? 13.56800  23.01200  2.09700   1.000 59.56000 ? 24  THR B C   1 
ATOM   2388 O O   . THR B 1 22  ? 13.58300  23.00400  0.86100   1.000 57.45000 ? 24  THR B O   1 
ATOM   2389 C CB  . THR B 1 22  ? 15.60600  24.38100  2.55300   1.000 59.67000 ? 24  THR B CB  1 
ATOM   2390 O OG1 . THR B 1 22  ? 15.81700  24.51300  1.14200   1.000 67.26000 ? 24  THR B OG1 1 
ATOM   2391 C CG2 . THR B 1 22  ? 16.36400  23.16100  3.05400   1.000 58.29000 ? 24  THR B CG2 1 
ATOM   2392 N N   . THR B 1 23  ? 13.09700  21.99000  2.81000   1.000 59.15000 ? 25  THR B N   1 
ATOM   2393 C CA  . THR B 1 23  ? 12.69700  20.72400  2.20500   1.000 57.94000 ? 25  THR B CA  1 
ATOM   2394 C C   . THR B 1 23  ? 11.18400  20.66100  2.04900   1.000 52.14000 ? 25  THR B C   1 
ATOM   2395 O O   . THR B 1 23  ? 10.44200  20.94600  2.99800   1.000 51.64000 ? 25  THR B O   1 
ATOM   2396 C CB  . THR B 1 23  ? 13.18000  19.54200  3.04600   1.000 58.50000 ? 25  THR B CB  1 
ATOM   2397 O OG1 . THR B 1 23  ? 14.59400  19.64900  3.25800   1.000 60.89000 ? 25  THR B OG1 1 
ATOM   2398 C CG2 . THR B 1 23  ? 12.87000  18.21900  2.34100   1.000 54.69000 ? 25  THR B CG2 1 
ATOM   2399 N N   . THR B 1 24  ? 10.73700  20.26000  0.85900   1.000 52.01000 ? 26  THR B N   1 
ATOM   2400 C CA  . THR B 1 24  ? 9.32400   20.10500  0.52800   1.000 51.04000 ? 26  THR B CA  1 
ATOM   2401 C C   . THR B 1 24  ? 9.08100   18.74400  -0.11100  1.000 48.53000 ? 26  THR B C   1 
ATOM   2402 O O   . THR B 1 24  ? 9.82500   18.33200  -1.01000  1.000 46.36000 ? 26  THR B O   1 
ATOM   2403 C CB  . THR B 1 24  ? 8.85900   21.18600  -0.44600  1.000 53.65000 ? 26  THR B CB  1 
ATOM   2404 O OG1 . THR B 1 24  ? 9.29500   22.46500  0.01900   1.000 62.87000 ? 26  THR B OG1 1 
ATOM   2405 C CG2 . THR B 1 24  ? 7.34500   21.17300  -0.57500  1.000 50.85000 ? 26  THR B CG2 1 
ATOM   2406 N N   . LEU B 1 25  ? 8.02400   18.06500  0.33000   1.000 44.24000 ? 27  LEU B N   1 
ATOM   2407 C CA  . LEU B 1 25  ? 7.64500   16.77700  -0.24400  1.000 39.58000 ? 27  LEU B CA  1 
ATOM   2408 C C   . LEU B 1 25  ? 6.15400   16.55500  0.00300   1.000 37.87000 ? 27  LEU B C   1 
ATOM   2409 O O   . LEU B 1 25  ? 5.45600   17.42000  0.53800   1.000 36.46000 ? 27  LEU B O   1 
ATOM   2410 C CB  . LEU B 1 25  ? 8.50700   15.63800  0.32700   1.000 38.74000 ? 27  LEU B CB  1 
ATOM   2411 C CG  . LEU B 1 25  ? 8.86200   15.59100  1.81800   1.000 38.30000 ? 27  LEU B CG  1 
ATOM   2412 C CD1 . LEU B 1 25  ? 7.64300   15.26600  2.69300   1.000 36.52000 ? 27  LEU B CD1 1 
ATOM   2413 C CD2 . LEU B 1 25  ? 9.99700   14.58600  2.06600   1.000 36.57000 ? 27  LEU B CD2 1 
ATOM   2414 N N   . ASN B 1 26  ? 5.65500   15.41100  -0.40600  1.000 35.21000 ? 28  ASN B N   1 
ATOM   2415 C CA  . ASN B 1 26  ? 4.27600   15.02600  -0.25400  1.000 34.65000 ? 28  ASN B CA  1 
ATOM   2416 C C   . ASN B 1 26  ? 3.90000   14.31200  1.03400   1.000 33.15000 ? 28  ASN B C   1 
ATOM   2417 O O   . ASN B 1 26  ? 4.65200   13.58800  1.56800   1.000 29.64000 ? 28  ASN B O   1 
ATOM   2418 C CB  . ASN B 1 26  ? 3.82600   14.14200  -1.41000  1.000 32.94000 ? 28  ASN B CB  1 
ATOM   2419 C CG  . ASN B 1 26  ? 4.15600   14.69600  -2.73400  1.000 36.31000 ? 28  ASN B CG  1 
ATOM   2420 O OD1 . ASN B 1 26  ? 3.50900   15.53200  -3.21200  1.000 41.66000 ? 28  ASN B OD1 1 
ATOM   2421 N ND2 . ASN B 1 26  ? 5.13600   14.17000  -3.33800  1.000 36.36000 ? 28  ASN B ND2 1 
ATOM   2422 N N   . GLY B 1 27  ? 2.68300   14.52500  1.44300   1.000 30.80000 ? 29  GLY B N   1 
ATOM   2423 C CA  . GLY B 1 27  ? 2.11200   13.91500  2.60000   1.000 31.34000 ? 29  GLY B CA  1 
ATOM   2424 C C   . GLY B 1 27  ? 0.73200   13.35200  2.42000   1.000 31.33000 ? 29  GLY B C   1 
ATOM   2425 O O   . GLY B 1 27  ? 0.03000   13.76800  1.58700   1.000 32.77000 ? 29  GLY B O   1 
ATOM   2426 N N   . LEU B 1 28  ? 0.37500   12.39700  3.24100   1.000 30.73000 ? 30  LEU B N   1 
ATOM   2427 C CA  . LEU B 1 28  ? -0.90500  11.74900  3.22000   1.000 33.51000 ? 30  LEU B CA  1 
ATOM   2428 C C   . LEU B 1 28  ? -1.72800  12.12100  4.42600   1.000 35.99000 ? 30  LEU B C   1 
ATOM   2429 O O   . LEU B 1 28  ? -1.39700  11.77100  5.51800   1.000 34.67000 ? 30  LEU B O   1 
ATOM   2430 C CB  . LEU B 1 28  ? -0.73300  10.24200  3.18500   1.000 29.66000 ? 30  LEU B CB  1 
ATOM   2431 C CG  . LEU B 1 28  ? -1.99900  9.48300   2.88400   1.000 30.00000 ? 30  LEU B CG  1 
ATOM   2432 C CD1 . LEU B 1 28  ? -2.48100  9.64300   1.45900   1.000 26.61000 ? 30  LEU B CD1 1 
ATOM   2433 C CD2 . LEU B 1 28  ? -1.88000  8.05200   3.20000   1.000 29.80000 ? 30  LEU B CD2 1 
ATOM   2434 N N   . TRP B 1 29  ? -2.82400  12.78600  4.17900   1.000 33.17000 ? 31  TRP B N   1 
ATOM   2435 C CA  . TRP B 1 29  ? -3.69900  13.28400  5.19500   1.000 34.86000 ? 31  TRP B CA  1 
ATOM   2436 C C   . TRP B 1 29  ? -4.91000  12.45200  5.38900   1.000 36.08000 ? 31  TRP B C   1 
ATOM   2437 O O   . TRP B 1 29  ? -5.75600  12.39700  4.58000   1.000 33.94000 ? 31  TRP B O   1 
ATOM   2438 C CB  . TRP B 1 29  ? -4.05800  14.72900  4.82800   1.000 36.82000 ? 31  TRP B CB  1 
ATOM   2439 C CG  . TRP B 1 29  ? -4.95400  15.51900  5.75600   1.000 41.62000 ? 31  TRP B CG  1 
ATOM   2440 C CD1 . TRP B 1 29  ? -5.08500  15.37400  7.05400   1.000 38.79000 ? 31  TRP B CD1 1 
ATOM   2441 C CD2 . TRP B 1 29  ? -5.80700  16.58800  5.39500   1.000 41.55000 ? 31  TRP B CD2 1 
ATOM   2442 N NE1 . TRP B 1 29  ? -5.97000  16.23400  7.54100   1.000 42.46000 ? 31  TRP B NE1 1 
ATOM   2443 C CE2 . TRP B 1 29  ? -6.42700  17.01100  6.53500   1.000 42.76000 ? 31  TRP B CE2 1 
ATOM   2444 C CE3 . TRP B 1 29  ? -6.10200  17.21900  4.21100   1.000 41.25000 ? 31  TRP B CE3 1 
ATOM   2445 C CZ2 . TRP B 1 29  ? -7.31900  18.01200  6.53700   1.000 41.96000 ? 31  TRP B CZ2 1 
ATOM   2446 C CZ3 . TRP B 1 29  ? -6.98400  18.21200  4.21700   1.000 43.09000 ? 31  TRP B CZ3 1 
ATOM   2447 C CH2 . TRP B 1 29  ? -7.58900  18.60100  5.36100   1.000 45.31000 ? 31  TRP B CH2 1 
ATOM   2448 N N   . LEU B 1 30  ? -4.96100  11.78200  6.49600   1.000 34.00000 ? 32  LEU B N   1 
ATOM   2449 C CA  . LEU B 1 30  ? -6.05000  10.94200  6.84300   1.000 32.80000 ? 32  LEU B CA  1 
ATOM   2450 C C   . LEU B 1 30  ? -6.50400  11.29900  8.26500   1.000 37.42000 ? 32  LEU B C   1 
ATOM   2451 O O   . LEU B 1 30  ? -5.76200  11.29700  9.15900   1.000 33.95000 ? 32  LEU B O   1 
ATOM   2452 C CB  . LEU B 1 30  ? -5.61500  9.49800   6.73800   1.000 32.86000 ? 32  LEU B CB  1 
ATOM   2453 C CG  . LEU B 1 30  ? -4.98600  8.96700   5.48200   1.000 32.01000 ? 32  LEU B CG  1 
ATOM   2454 C CD1 . LEU B 1 30  ? -4.42600  7.59400   5.70500   1.000 28.35000 ? 32  LEU B CD1 1 
ATOM   2455 C CD2 . LEU B 1 30  ? -5.93000  8.99800   4.32300   1.000 32.32000 ? 32  LEU B CD2 1 
ATOM   2456 N N   . ASP B 1 31  ? -7.77000  11.59700  8.43100   1.000 39.16000 ? 33  ASP B N   1 
ATOM   2457 C CA  . ASP B 1 31  ? -8.30100  12.03700  9.67600   1.000 37.28000 ? 33  ASP B CA  1 
ATOM   2458 C C   . ASP B 1 31  ? -7.51900  13.28000  10.03200  1.000 39.28000 ? 33  ASP B C   1 
ATOM   2459 O O   . ASP B 1 31  ? -7.38200  14.13700  9.23300   1.000 40.63000 ? 33  ASP B O   1 
ATOM   2460 C CB  . ASP B 1 31  ? -8.22800  10.96700  10.72600  1.000 37.87000 ? 33  ASP B CB  1 
ATOM   2461 C CG  . ASP B 1 31  ? -8.94600  9.72800   10.33200  1.000 44.70000 ? 33  ASP B CG  1 
ATOM   2462 O OD1 . ASP B 1 31  ? -10.10100 9.80900   10.04600  1.000 43.54000 ? 33  ASP B OD1 1 
ATOM   2463 O OD2 . ASP B 1 31  ? -8.34600  8.64900   10.31900  1.000 50.44000 ? 33  ASP B OD2 1 
ATOM   2464 N N   . ASP B 1 32  ? -6.99200  13.34200  11.22500  1.000 37.86000 ? 34  ASP B N   1 
ATOM   2465 C CA  . ASP B 1 32  ? -6.25200  14.48500  11.69300  1.000 42.17000 ? 34  ASP B CA  1 
ATOM   2466 C C   . ASP B 1 32  ? -4.76000  14.32200  11.76000  1.000 40.86000 ? 34  ASP B C   1 
ATOM   2467 O O   . ASP B 1 32  ? -4.11000  14.97000  12.49900  1.000 40.38000 ? 34  ASP B O   1 
ATOM   2468 C CB  . ASP B 1 32  ? -6.79900  14.96700  13.01900  1.000 41.90000 ? 34  ASP B CB  1 
ATOM   2469 C CG  . ASP B 1 32  ? -6.67900  13.97800  14.07900  1.000 46.82000 ? 34  ASP B CG  1 
ATOM   2470 O OD1 . ASP B 1 32  ? -6.35700  12.86300  13.83600  1.000 47.52000 ? 34  ASP B OD1 1 
ATOM   2471 O OD2 . ASP B 1 32  ? -6.89700  14.31400  15.19200  1.000 50.96000 ? 34  ASP B OD2 1 
ATOM   2472 N N   . VAL B 1 33  ? -4.25100  13.41100  10.97700  1.000 39.28000 ? 35  VAL B N   1 
ATOM   2473 C CA  . VAL B 1 33  ? -2.83200  13.07300  10.91600  1.000 35.02000 ? 35  VAL B CA  1 
ATOM   2474 C C   . VAL B 1 33  ? -2.36300  13.14300  9.47100   1.000 35.32000 ? 35  VAL B C   1 
ATOM   2475 O O   . VAL B 1 33  ? -3.02700  12.61700  8.56800   1.000 33.67000 ? 35  VAL B O   1 
ATOM   2476 C CB  . VAL B 1 33  ? -2.54400  11.67000  11.49000  1.000 34.42000 ? 35  VAL B CB  1 
ATOM   2477 C CG1 . VAL B 1 33  ? -1.05300  11.38600  11.46700  1.000 33.13000 ? 35  VAL B CG1 1 
ATOM   2478 C CG2 . VAL B 1 33  ? -3.09100  11.54700  12.91200  1.000 37.01000 ? 35  VAL B CG2 1 
ATOM   2479 N N   . VAL B 1 34  ? -1.21600  13.78700  9.25800   1.000 34.36000 ? 36  VAL B N   1 
ATOM   2480 C CA  . VAL B 1 34  ? -0.51100  13.77100  7.98200   1.000 35.48000 ? 36  VAL B CA  1 
ATOM   2481 C C   . VAL B 1 34  ? 0.71200   12.87000  8.11300   1.000 35.77000 ? 36  VAL B C   1 
ATOM   2482 O O   . VAL B 1 34  ? 1.52300   13.03300  9.03600   1.000 33.79000 ? 36  VAL B O   1 
ATOM   2483 C CB  . VAL B 1 34  ? -0.11000  15.18500  7.53200   1.000 35.70000 ? 36  VAL B CB  1 
ATOM   2484 C CG1 . VAL B 1 34  ? 0.76400   15.11400  6.27500   1.000 31.75000 ? 36  VAL B CG1 1 
ATOM   2485 C CG2 . VAL B 1 34  ? -1.36400  16.05000  7.29100   1.000 32.22000 ? 36  VAL B CG2 1 
ATOM   2486 N N   . TYR B 1 35  ? 0.84200   11.93200  7.17900   1.000 31.97000 ? 37  TYR B N   1 
ATOM   2487 C CA  . TYR B 1 35  ? 1.93800   10.96900  7.15100   1.000 34.54000 ? 37  TYR B CA  1 
ATOM   2488 C C   . TYR B 1 35  ? 2.91800   11.32600  6.03100   1.000 33.57000 ? 37  TYR B C   1 
ATOM   2489 O O   . TYR B 1 35  ? 2.48600   11.58300  4.90100   1.000 32.75000 ? 37  TYR B O   1 
ATOM   2490 C CB  . TYR B 1 35  ? 1.38700   9.55700   6.93300   1.000 31.31000 ? 37  TYR B CB  1 
ATOM   2491 C CG  . TYR B 1 35  ? 0.36900   9.11000   7.94300   1.000 34.63000 ? 37  TYR B CG  1 
ATOM   2492 C CD1 . TYR B 1 35  ? -0.96100  9.47400   7.83200   1.000 34.37000 ? 37  TYR B CD1 1 
ATOM   2493 C CD2 . TYR B 1 35  ? 0.74100   8.31000   9.02000   1.000 35.90000 ? 37  TYR B CD2 1 
ATOM   2494 C CE1 . TYR B 1 35  ? -1.91200  9.04600   8.77800   1.000 35.79000 ? 37  TYR B CE1 1 
ATOM   2495 C CE2 . TYR B 1 35  ? -0.19600  7.88800   9.96500   1.000 33.03000 ? 37  TYR B CE2 1 
ATOM   2496 C CZ  . TYR B 1 35  ? -1.50700  8.25900   9.84400   1.000 34.71000 ? 37  TYR B CZ  1 
ATOM   2497 O OH  . TYR B 1 35  ? -2.41400  7.82900   10.78500  1.000 36.86000 ? 37  TYR B OH  1 
ATOM   2498 N N   . CYS B 1 36  ? 4.21400   11.31300  6.32400   1.000 29.94000 ? 38  CYS B N   1 
ATOM   2499 C CA  . CYS B 1 36  ? 5.19700   11.64500  5.28800   1.000 33.41000 ? 38  CYS B CA  1 
ATOM   2500 C C   . CYS B 1 36  ? 6.54900   11.04300  5.66100   1.000 32.14000 ? 38  CYS B C   1 
ATOM   2501 O O   . CYS B 1 36  ? 6.74500   10.58700  6.79800   1.000 31.58000 ? 38  CYS B O   1 
ATOM   2502 C CB  . CYS B 1 36  ? 5.29800   13.16700  5.08300   1.000 35.73000 ? 38  CYS B CB  1 
ATOM   2503 S SG  . CYS B 1 36  ? 6.10600   14.06800  6.42100   1.000 41.79000 ? 38  CYS B SG  1 
ATOM   2504 N N   . PRO B 1 37  ? 7.48400   11.01500  4.75600   1.000 35.20000 ? 39  PRO B N   1 
ATOM   2505 C CA  . PRO B 1 37  ? 8.80300   10.49200  5.04400   1.000 34.80000 ? 39  PRO B CA  1 
ATOM   2506 C C   . PRO B 1 37  ? 9.53800   11.33300  6.07300   1.000 36.59000 ? 39  PRO B C   1 
ATOM   2507 O O   . PRO B 1 37  ? 9.53000   12.48000  5.96000   1.000 35.82000 ? 39  PRO B O   1 
ATOM   2508 C CB  . PRO B 1 37  ? 9.49500   10.59300  3.70200   1.000 35.54000 ? 39  PRO B CB  1 
ATOM   2509 C CG  . PRO B 1 37  ? 8.41000   10.64600  2.71800   1.000 33.98000 ? 39  PRO B CG  1 
ATOM   2510 C CD  . PRO B 1 37  ? 7.37600   11.43200  3.36800   1.000 31.99000 ? 39  PRO B CD  1 
ATOM   2511 N N   . ARG B 1 38  ? 10.17300  10.72200  7.03700   1.000 34.58000 ? 40  ARG B N   1 
ATOM   2512 C CA  . ARG B 1 38  ? 10.86300  11.43600  8.06600   1.000 37.37000 ? 40  ARG B CA  1 
ATOM   2513 C C   . ARG B 1 38  ? 11.97700  12.24700  7.54300   1.000 41.13000 ? 40  ARG B C   1 
ATOM   2514 O O   . ARG B 1 38  ? 12.31300  13.18100  8.14000   1.000 41.78000 ? 40  ARG B O   1 
ATOM   2515 C CB  . ARG B 1 38  ? 11.34200  10.55300  9.20300   1.000 36.20000 ? 40  ARG B CB  1 
ATOM   2516 C CG  . ARG B 1 38  ? 12.43000  9.60300   8.87200   1.000 37.77000 ? 40  ARG B CG  1 
ATOM   2517 C CD  . ARG B 1 38  ? 12.91900  8.80700   10.05200  1.000 40.25000 ? 40  ARG B CD  1 
ATOM   2518 N NE  . ARG B 1 38  ? 13.98300  7.92100   9.67800   1.000 39.29000 ? 40  ARG B NE  1 
ATOM   2519 C CZ  . ARG B 1 38  ? 14.58400  7.10900   10.50100  1.000 39.86000 ? 40  ARG B CZ  1 
ATOM   2520 N NH1 . ARG B 1 38  ? 14.25300  7.05300   11.74400  1.000 37.95000 ? 40  ARG B NH1 1 
ATOM   2521 N NH2 . ARG B 1 38  ? 15.53000  6.36000   10.07200  1.000 40.70000 ? 40  ARG B NH2 1 
ATOM   2522 N N   . HIS B 1 39  ? 12.54600  11.89100  6.42500   1.000 40.01000 ? 41  HIS B N   1 
ATOM   2523 C CA  . HIS B 1 39  ? 13.67400  12.68900  5.95200   1.000 47.36000 ? 41  HIS B CA  1 
ATOM   2524 C C   . HIS B 1 39  ? 13.27200  14.10900  5.54400   1.000 47.55000 ? 41  HIS B C   1 
ATOM   2525 O O   . HIS B 1 39  ? 14.14100  14.88400  5.13400   1.000 50.12000 ? 41  HIS B O   1 
ATOM   2526 C CB  . HIS B 1 39  ? 14.44800  11.96000  4.82300   1.000 49.45000 ? 41  HIS B CB  1 
ATOM   2527 C CG  . HIS B 1 39  ? 13.71600  11.79800  3.51700   1.000 51.58000 ? 41  HIS B CG  1 
ATOM   2528 N ND1 . HIS B 1 39  ? 13.37700  12.86000  2.70100   1.000 53.86000 ? 41  HIS B ND1 1 
ATOM   2529 C CD2 . HIS B 1 39  ? 13.35000  10.67900  2.83600   1.000 53.37000 ? 41  HIS B CD2 1 
ATOM   2530 C CE1 . HIS B 1 39  ? 12.78500  12.40600  1.60600   1.000 52.82000 ? 41  HIS B CE1 1 
ATOM   2531 N NE2 . HIS B 1 39  ? 12.75500  11.08500  1.66300   1.000 48.73000 ? 41  HIS B NE2 1 
ATOM   2532 N N   . VAL B 1 40  ? 12.00200  14.49300  5.70500   1.000 42.32000 ? 42  VAL B N   1 
ATOM   2533 C CA  . VAL B 1 40  ? 11.61800  15.90000  5.59000   1.000 44.36000 ? 42  VAL B CA  1 
ATOM   2534 C C   . VAL B 1 40  ? 12.32900  16.77600  6.62900   1.000 48.96000 ? 42  VAL B C   1 
ATOM   2535 O O   . VAL B 1 40  ? 12.41900  17.99200  6.44700   1.000 45.56000 ? 42  VAL B O   1 
ATOM   2536 C CB  . VAL B 1 40  ? 10.08100  16.04700  5.70600   1.000 42.66000 ? 42  VAL B CB  1 
ATOM   2537 C CG1 . VAL B 1 40  ? 9.60500   15.68900  7.10800   1.000 38.64000 ? 42  VAL B CG1 1 
ATOM   2538 C CG2 . VAL B 1 40  ? 9.62300   17.46400  5.32600   1.000 42.98000 ? 42  VAL B CG2 1 
ATOM   2539 N N   . ILE B 1 41  ? 12.82900  16.19600  7.72200   1.000 46.15000 ? 43  ILE B N   1 
ATOM   2540 C CA  . ILE B 1 41  ? 13.50000  16.99000  8.75400   1.000 53.31000 ? 43  ILE B CA  1 
ATOM   2541 C C   . ILE B 1 41  ? 15.01500  16.94700  8.58000   1.000 57.29000 ? 43  ILE B C   1 
ATOM   2542 O O   . ILE B 1 41  ? 15.76600  17.25900  9.51300   1.000 65.57000 ? 43  ILE B O   1 
ATOM   2543 C CB  . ILE B 1 41  ? 13.12200  16.52800  10.17700  1.000 52.42000 ? 43  ILE B CB  1 
ATOM   2544 C CG1 . ILE B 1 41  ? 13.68600  15.12900  10.46300  1.000 51.73000 ? 43  ILE B CG1 1 
ATOM   2545 C CG2 . ILE B 1 41  ? 11.61200  16.59700  10.40800  1.000 48.36000 ? 43  ILE B CG2 1 
ATOM   2546 C CD1 . ILE B 1 41  ? 13.49400  14.69000  11.88600  1.000 52.72000 ? 43  ILE B CD1 1 
ATOM   2547 N N   . CYS B 1 42  ? 15.47700  16.57300  7.39100   1.000 60.08000 ? 44  CYS B N   1 
ATOM   2548 C CA  . CYS B 1 42  ? 16.90500  16.51100  7.10800   1.000 61.55000 ? 44  CYS B CA  1 
ATOM   2549 C C   . CYS B 1 42  ? 17.38400  17.80700  6.47800   1.000 66.66000 ? 44  CYS B C   1 
ATOM   2550 O O   . CYS B 1 42  ? 16.67100  18.42200  5.67900   1.000 69.36000 ? 44  CYS B O   1 
ATOM   2551 C CB  . CYS B 1 42  ? 17.22400  15.34700  6.17700   1.000 61.01000 ? 44  CYS B CB  1 
ATOM   2552 S SG  . CYS B 1 42  ? 17.59700  13.84700  7.06100   1.000 78.70000 ? 44  CYS B SG  1 
ATOM   2553 N N   . THR B 1 43  ? 18.60500  18.20100  6.83000   1.000 73.36000 ? 45  THR B N   1 
ATOM   2554 C CA  . THR B 1 43  ? 19.22300  19.42300  6.32500   1.000 74.95000 ? 45  THR B CA  1 
ATOM   2555 C C   . THR B 1 43  ? 19.63100  19.29300  4.85500   1.000 74.18000 ? 45  THR B C   1 
ATOM   2556 O O   . THR B 1 43  ? 20.81800  19.24500  4.52500   1.000 73.35000 ? 45  THR B O   1 
ATOM   2557 C CB  . THR B 1 43  ? 20.45000  19.79100  7.16700   1.000 74.23000 ? 45  THR B CB  1 
ATOM   2558 O OG1 . THR B 1 43  ? 21.52400  18.88400  6.87600   1.000 79.46000 ? 45  THR B OG1 1 
ATOM   2559 C CG2 . THR B 1 43  ? 20.11100  19.70700  8.65100   1.000 67.47000 ? 45  THR B CG2 1 
ATOM   2560 N N   . ASN B 1 49  ? 24.65200  11.14800  7.41800   1.000 71.68000 ? 51  ASN B N   1 
ATOM   2561 C CA  . ASN B 1 49  ? 24.29300  10.21700  8.48700   1.000 74.05000 ? 51  ASN B CA  1 
ATOM   2562 C C   . ASN B 1 49  ? 23.59500  10.92000  9.66900   1.000 76.69000 ? 51  ASN B C   1 
ATOM   2563 O O   . ASN B 1 49  ? 24.19900  11.09400  10.73700  1.000 76.58000 ? 51  ASN B O   1 
ATOM   2564 C CB  . ASN B 1 49  ? 25.54500  9.47500   8.96800   1.000 75.40000 ? 51  ASN B CB  1 
ATOM   2565 C CG  . ASN B 1 49  ? 25.23800  8.41200   10.01400  1.000 77.21000 ? 51  ASN B CG  1 
ATOM   2566 O OD1 . ASN B 1 49  ? 24.83200  7.29400   9.68400   1.000 73.56000 ? 51  ASN B OD1 1 
ATOM   2567 N ND2 . ASN B 1 49  ? 25.44200  8.75800   11.28500  1.000 79.35000 ? 51  ASN B ND2 1 
ATOM   2568 N N   . PRO B 1 50  ? 22.33300  11.31900  9.48100   1.000 75.55000 ? 52  PRO B N   1 
ATOM   2569 C CA  . PRO B 1 50  ? 21.60900  12.02800  10.54300  1.000 76.55000 ? 52  PRO B CA  1 
ATOM   2570 C C   . PRO B 1 50  ? 20.99900  11.11200  11.59400  1.000 76.54000 ? 52  PRO B C   1 
ATOM   2571 O O   . PRO B 1 50  ? 20.54400  9.99900   11.31300  1.000 75.16000 ? 52  PRO B O   1 
ATOM   2572 C CB  . PRO B 1 50  ? 20.50300  12.76900  9.77800   1.000 73.74000 ? 52  PRO B CB  1 
ATOM   2573 C CG  . PRO B 1 50  ? 20.23400  11.90000  8.60300   1.000 70.02000 ? 52  PRO B CG  1 
ATOM   2574 C CD  . PRO B 1 50  ? 21.59600  11.36100  8.20400   1.000 74.57000 ? 52  PRO B CD  1 
ATOM   2575 N N   . ASN B 1 51  ? 20.97600  11.62800  12.82300  1.000 79.15000 ? 53  ASN B N   1 
ATOM   2576 C CA  . ASN B 1 51  ? 20.25300  11.02400  13.93800  1.000 76.44000 ? 53  ASN B CA  1 
ATOM   2577 C C   . ASN B 1 51  ? 18.84500  11.61300  13.94100  1.000 75.92000 ? 53  ASN B C   1 
ATOM   2578 O O   . ASN B 1 51  ? 18.65600  12.79200  14.26100  1.000 74.70000 ? 53  ASN B O   1 
ATOM   2579 C CB  . ASN B 1 51  ? 20.99200  11.29000  15.25300  1.000 75.18000 ? 53  ASN B CB  1 
ATOM   2580 C CG  . ASN B 1 51  ? 20.21000  10.84800  16.49300  1.000 76.68000 ? 53  ASN B CG  1 
ATOM   2581 O OD1 . ASN B 1 51  ? 19.08100  11.27600  16.72400  1.000 82.02000 ? 53  ASN B OD1 1 
ATOM   2582 N ND2 . ASN B 1 51  ? 20.82900  10.00400  17.30700  1.000 75.02000 ? 53  ASN B ND2 1 
ATOM   2583 N N   . TYR B 1 52  ? 17.85300  10.79800  13.57400  1.000 72.34000 ? 54  TYR B N   1 
ATOM   2584 C CA  . TYR B 1 52  ? 16.48100  11.28300  13.52000  1.000 66.64000 ? 54  TYR B CA  1 
ATOM   2585 C C   . TYR B 1 52  ? 15.83300  11.35500  14.89500  1.000 70.90000 ? 54  TYR B C   1 
ATOM   2586 O O   . TYR B 1 52  ? 14.82900  12.05800  15.05600  1.000 67.37000 ? 54  TYR B O   1 
ATOM   2587 C CB  . TYR B 1 52  ? 15.64600  10.39800  12.59600  1.000 56.07000 ? 54  TYR B CB  1 
ATOM   2588 C CG  . TYR B 1 52  ? 15.96900  10.55300  11.12300  1.000 55.08000 ? 54  TYR B CG  1 
ATOM   2589 C CD1 . TYR B 1 52  ? 15.45000  11.60800  10.39400  1.000 49.53000 ? 54  TYR B CD1 1 
ATOM   2590 C CD2 . TYR B 1 52  ? 16.78200  9.63500   10.46300  1.000 52.22000 ? 54  TYR B CD2 1 
ATOM   2591 C CE1 . TYR B 1 52  ? 15.73200  11.75400  9.05200   1.000 55.69000 ? 54  TYR B CE1 1 
ATOM   2592 C CE2 . TYR B 1 52  ? 17.06800  9.76900   9.11100   1.000 52.77000 ? 54  TYR B CE2 1 
ATOM   2593 C CZ  . TYR B 1 52  ? 16.53500  10.83600  8.40900   1.000 54.86000 ? 54  TYR B CZ  1 
ATOM   2594 O OH  . TYR B 1 52  ? 16.78600  10.99500  7.06100   1.000 55.06000 ? 54  TYR B OH  1 
ATOM   2595 N N   . GLU B 1 53  ? 16.37900  10.64200  15.88300  1.000 75.01000 ? 55  GLU B N   1 
ATOM   2596 C CA  . GLU B 1 53  ? 15.91900  10.80200  17.26100  1.000 77.07000 ? 55  GLU B CA  1 
ATOM   2597 C C   . GLU B 1 53  ? 16.15800  12.22700  17.75400  1.000 75.45000 ? 55  GLU B C   1 
ATOM   2598 O O   . GLU B 1 53  ? 15.24600  12.87700  18.28300  1.000 75.18000 ? 55  GLU B O   1 
ATOM   2599 C CB  . GLU B 1 53  ? 16.62800  9.79000   18.16800  1.000 73.37000 ? 55  GLU B CB  1 
ATOM   2600 N N   . ASP B 1 54  ? 17.38700  12.72600  17.57800  1.000 76.77000 ? 56  ASP B N   1 
ATOM   2601 C CA  . ASP B 1 54  ? 17.73500  14.08800  17.98000  1.000 76.76000 ? 56  ASP B CA  1 
ATOM   2602 C C   . ASP B 1 54  ? 16.93000  15.11500  17.19600  1.000 74.21000 ? 56  ASP B C   1 
ATOM   2603 O O   . ASP B 1 54  ? 16.20100  15.92800  17.77500  1.000 72.57000 ? 56  ASP B O   1 
ATOM   2604 C CB  . ASP B 1 54  ? 19.23600  14.33300  17.76700  1.000 79.52000 ? 56  ASP B CB  1 
ATOM   2605 C CG  . ASP B 1 54  ? 20.06400  14.06100  19.00800  1.000 82.15000 ? 56  ASP B CG  1 
ATOM   2606 O OD1 . ASP B 1 54  ? 19.61700  14.42800  20.11500  1.000 84.31000 ? 56  ASP B OD1 1 
ATOM   2607 O OD2 . ASP B 1 54  ? 21.17600  13.49900  18.87100  1.000 83.22000 ? 56  ASP B OD2 1 
ATOM   2608 N N   . LEU B 1 55  ? 17.06300  15.08500  15.86300  1.000 73.17000 ? 57  LEU B N   1 
ATOM   2609 C CA  . LEU B 1 55  ? 16.53200  16.13900  15.00500  1.000 71.16000 ? 57  LEU B CA  1 
ATOM   2610 C C   . LEU B 1 55  ? 15.06600  16.45000  15.29800  1.000 72.93000 ? 57  LEU B C   1 
ATOM   2611 O O   . LEU B 1 55  ? 14.64000  17.60400  15.16600  1.000 73.78000 ? 57  LEU B O   1 
ATOM   2612 C CB  . LEU B 1 55  ? 16.70900  15.74200  13.53400  1.000 69.68000 ? 57  LEU B CB  1 
ATOM   2613 C CG  . LEU B 1 55  ? 18.14000  15.64500  12.98500  1.000 68.64000 ? 57  LEU B CG  1 
ATOM   2614 C CD1 . LEU B 1 55  ? 18.15500  15.10100  11.55600  1.000 66.33000 ? 57  LEU B CD1 1 
ATOM   2615 C CD2 . LEU B 1 55  ? 18.84300  16.99300  13.04200  1.000 70.16000 ? 57  LEU B CD2 1 
ATOM   2616 N N   . LEU B 1 56  ? 14.28900  15.44800  15.72500  1.000 71.85000 ? 58  LEU B N   1 
ATOM   2617 C CA  . LEU B 1 56  ? 12.85400  15.60800  15.93200  1.000 67.25000 ? 58  LEU B CA  1 
ATOM   2618 C C   . LEU B 1 56  ? 12.51200  16.09800  17.33500  1.000 71.40000 ? 58  LEU B C   1 
ATOM   2619 O O   . LEU B 1 56  ? 11.48400  16.76300  17.51900  1.000 69.81000 ? 58  LEU B O   1 
ATOM   2620 C CB  . LEU B 1 56  ? 12.13700  14.28200  15.64300  1.000 67.67000 ? 58  LEU B CB  1 
ATOM   2621 C CG  . LEU B 1 56  ? 10.61200  14.22900  15.46800  1.000 65.82000 ? 58  LEU B CG  1 
ATOM   2622 C CD1 . LEU B 1 56  ? 9.88000   14.27000  16.81100  1.000 69.34000 ? 58  LEU B CD1 1 
ATOM   2623 C CD2 . LEU B 1 56  ? 10.13300  15.33900  14.53600  1.000 61.32000 ? 58  LEU B CD2 1 
ATOM   2624 N N   . ILE B 1 57  ? 13.34100  15.77800  18.33400  1.000 72.63000 ? 59  ILE B N   1 
ATOM   2625 C CA  . ILE B 1 57  ? 13.17900  16.39300  19.64800  1.000 71.58000 ? 59  ILE B CA  1 
ATOM   2626 C C   . ILE B 1 57  ? 13.40900  17.89600  19.55400  1.000 71.72000 ? 59  ILE B C   1 
ATOM   2627 O O   . ILE B 1 57  ? 12.69500  18.69200  20.17700  1.000 70.58000 ? 59  ILE B O   1 
ATOM   2628 C CB  . ILE B 1 57  ? 14.12500  15.73300  20.67000  1.000 72.37000 ? 59  ILE B CB  1 
ATOM   2629 N N   . ARG B 1 58  ? 14.40300  18.30900  18.75700  1.000 71.02000 ? 60  ARG B N   1 
ATOM   2630 C CA  . ARG B 1 58  ? 14.67200  19.72700  18.53500  1.000 73.28000 ? 60  ARG B CA  1 
ATOM   2631 C C   . ARG B 1 58  ? 13.56400  20.41400  17.74000  1.000 76.57000 ? 60  ARG B C   1 
ATOM   2632 O O   . ARG B 1 58  ? 13.45100  21.64700  17.79100  1.000 75.88000 ? 60  ARG B O   1 
ATOM   2633 C CB  . ARG B 1 58  ? 16.01400  19.89700  17.81100  1.000 72.93000 ? 60  ARG B CB  1 
ATOM   2634 N N   . LYS B 1 59  ? 12.75600  19.65300  17.00400  1.000 73.42000 ? 61  LYS B N   1 
ATOM   2635 C CA  . LYS B 1 59  ? 11.66500  20.23800  16.24200  1.000 69.28000 ? 61  LYS B CA  1 
ATOM   2636 C C   . LYS B 1 59  ? 10.52300  20.63900  17.16300  1.000 66.35000 ? 61  LYS B C   1 
ATOM   2637 O O   . LYS B 1 59  ? 10.31400  20.05500  18.23000  1.000 69.84000 ? 61  LYS B O   1 
ATOM   2638 C CB  . LYS B 1 59  ? 11.14700  19.25500  15.18800  1.000 65.69000 ? 61  LYS B CB  1 
ATOM   2639 C CG  . LYS B 1 59  ? 12.11200  18.98600  14.04400  1.000 65.91000 ? 61  LYS B CG  1 
ATOM   2640 C CD  . LYS B 1 59  ? 12.12900  20.12500  13.03600  1.000 63.55000 ? 61  LYS B CD  1 
ATOM   2641 C CE  . LYS B 1 59  ? 13.47900  20.22800  12.34300  1.000 67.04000 ? 61  LYS B CE  1 
ATOM   2642 N NZ  . LYS B 1 59  ? 13.60900  21.49700  11.56500  1.000 68.83000 ? 61  LYS B NZ  1 
ATOM   2643 N N   . SER B 1 60  ? 9.78300   21.65200  16.73500  1.000 61.41000 ? 62  SER B N   1 
ATOM   2644 C CA  . SER B 1 60  ? 8.50800   22.00300  17.33400  1.000 62.31000 ? 62  SER B CA  1 
ATOM   2645 C C   . SER B 1 60  ? 7.47600   22.15100  16.21900  1.000 62.00000 ? 62  SER B C   1 
ATOM   2646 O O   . SER B 1 60  ? 7.80600   22.11500  15.02800  1.000 59.49000 ? 62  SER B O   1 
ATOM   2647 C CB  . SER B 1 60  ? 8.61900   23.28500  18.16700  1.000 65.49000 ? 62  SER B CB  1 
ATOM   2648 O OG  . SER B 1 60  ? 8.47600   24.42600  17.34700  1.000 67.11000 ? 62  SER B OG  1 
ATOM   2649 N N   . ASN B 1 61  ? 6.21300   22.33000  16.62100  1.000 58.75000 ? 63  ASN B N   1 
ATOM   2650 C CA  . ASN B 1 61  ? 5.10900   22.31200  15.66300  1.000 56.74000 ? 63  ASN B CA  1 
ATOM   2651 C C   . ASN B 1 61  ? 5.25300   23.39900  14.60100  1.000 58.85000 ? 63  ASN B C   1 
ATOM   2652 O O   . ASN B 1 61  ? 4.99100   23.15800  13.41600  1.000 56.63000 ? 63  ASN B O   1 
ATOM   2653 C CB  . ASN B 1 61  ? 3.78500   22.45800  16.40500  1.000 51.70000 ? 63  ASN B CB  1 
ATOM   2654 C CG  . ASN B 1 61  ? 3.43200   21.22200  17.19500  1.000 55.61000 ? 63  ASN B CG  1 
ATOM   2655 O OD1 . ASN B 1 61  ? 3.99600   20.14500  16.97400  1.000 58.14000 ? 63  ASN B OD1 1 
ATOM   2656 N ND2 . ASN B 1 61  ? 2.49600   21.36200  18.12100  1.000 51.04000 ? 63  ASN B ND2 1 
ATOM   2657 N N   . HIS B 1 62  ? 5.67400   24.60100  14.99900  1.000 60.92000 ? 64  HIS B N   1 
ATOM   2658 C CA  . HIS B 1 62  ? 5.80200   25.69400  14.04000  1.000 60.99000 ? 64  HIS B CA  1 
ATOM   2659 C C   . HIS B 1 62  ? 6.89900   25.45400  13.00900  1.000 56.43000 ? 64  HIS B C   1 
ATOM   2660 O O   . HIS B 1 62  ? 7.06900   26.28200  12.10900  1.000 58.82000 ? 64  HIS B O   1 
ATOM   2661 C CB  . HIS B 1 62  ? 6.05900   27.01900  14.77100  1.000 60.96000 ? 64  HIS B CB  1 
ATOM   2662 C CG  . HIS B 1 62  ? 7.28600   27.01100  15.63000  1.000 58.01000 ? 64  HIS B CG  1 
ATOM   2663 N ND1 . HIS B 1 62  ? 8.55800   26.91000  15.10800  1.000 59.20000 ? 64  HIS B ND1 1 
ATOM   2664 C CD2 . HIS B 1 62  ? 7.43700   27.10700  16.97300  1.000 58.33000 ? 64  HIS B CD2 1 
ATOM   2665 C CE1 . HIS B 1 62  ? 9.44000   26.92600  16.09400  1.000 60.12000 ? 64  HIS B CE1 1 
ATOM   2666 N NE2 . HIS B 1 62  ? 8.78700   27.04800  17.23500  1.000 60.76000 ? 64  HIS B NE2 1 
ATOM   2667 N N   . ASN B 1 63  ? 7.64600   24.35600  13.11700  1.000 57.92000 ? 65  ASN B N   1 
ATOM   2668 C CA  . ASN B 1 63  ? 8.65900   24.03500  12.12100  1.000 56.59000 ? 65  ASN B CA  1 
ATOM   2669 C C   . ASN B 1 63  ? 8.06900   23.39500  10.85700  1.000 55.69000 ? 65  ASN B C   1 
ATOM   2670 O O   . ASN B 1 63  ? 8.74400   23.36000  9.82000   1.000 55.40000 ? 65  ASN B O   1 
ATOM   2671 C CB  . ASN B 1 63  ? 9.71100   23.10800  12.73900  1.000 58.54000 ? 65  ASN B CB  1 
ATOM   2672 C CG  . ASN B 1 63  ? 10.66800  23.84000  13.69000  1.000 65.58000 ? 65  ASN B CG  1 
ATOM   2673 O OD1 . ASN B 1 63  ? 10.60000  23.67800  14.91000  1.000 65.04000 ? 65  ASN B OD1 1 
ATOM   2674 N ND2 . ASN B 1 63  ? 11.57000  24.63600  13.12700  1.000 63.51000 ? 65  ASN B ND2 1 
ATOM   2675 N N   . PHE B 1 64  ? 6.83900   22.89100  10.91100  1.000 53.16000 ? 66  PHE B N   1 
ATOM   2676 C CA  . PHE B 1 64  ? 6.22400   22.17400  9.79500   1.000 54.53000 ? 66  PHE B CA  1 
ATOM   2677 C C   . PHE B 1 64  ? 5.13800   23.02200  9.16100   1.000 53.77000 ? 66  PHE B C   1 
ATOM   2678 O O   . PHE B 1 64  ? 4.24300   23.51800  9.85700   1.000 53.33000 ? 66  PHE B O   1 
ATOM   2679 C CB  . PHE B 1 64  ? 5.61600   20.84900  10.25700  1.000 51.88000 ? 66  PHE B CB  1 
ATOM   2680 C CG  . PHE B 1 64  ? 6.59900   19.92800  10.88800  1.000 48.62000 ? 66  PHE B CG  1 
ATOM   2681 C CD1 . PHE B 1 64  ? 7.40600   19.11500  10.11100  1.000 48.51000 ? 66  PHE B CD1 1 
ATOM   2682 C CD2 . PHE B 1 64  ? 6.73700   19.89400  12.26000  1.000 50.17000 ? 66  PHE B CD2 1 
ATOM   2683 C CE1 . PHE B 1 64  ? 8.33000   18.27500  10.70300  1.000 49.83000 ? 66  PHE B CE1 1 
ATOM   2684 C CE2 . PHE B 1 64  ? 7.64600   19.06100  12.86100  1.000 52.26000 ? 66  PHE B CE2 1 
ATOM   2685 C CZ  . PHE B 1 64  ? 8.44800   18.24900  12.08700  1.000 54.11000 ? 66  PHE B CZ  1 
ATOM   2686 N N   . LEU B 1 65  ? 5.18600   23.16700  7.84100   1.000 52.69000 ? 67  LEU B N   1 
ATOM   2687 C CA  . LEU B 1 65  ? 4.14900   23.88700  7.12000   1.000 55.61000 ? 67  LEU B CA  1 
ATOM   2688 C C   . LEU B 1 65  ? 3.41100   22.91000  6.21800   1.000 53.53000 ? 67  LEU B C   1 
ATOM   2689 O O   . LEU B 1 65  ? 3.97900   22.40200  5.23600   1.000 52.51000 ? 67  LEU B O   1 
ATOM   2690 C CB  . LEU B 1 65  ? 4.72600   25.05600  6.32600   1.000 52.94000 ? 67  LEU B CB  1 
ATOM   2691 C CG  . LEU B 1 65  ? 3.70300   25.64900  5.36000   1.000 57.82000 ? 67  LEU B CG  1 
ATOM   2692 C CD1 . LEU B 1 65  ? 2.71400   26.45600  6.18900   1.000 60.27000 ? 67  LEU B CD1 1 
ATOM   2693 C CD2 . LEU B 1 65  ? 4.36400   26.54300  4.32400   1.000 59.74000 ? 67  LEU B CD2 1 
ATOM   2694 N N   . VAL B 1 66  ? 2.15200   22.64700  6.53700   1.000 50.91000 ? 68  VAL B N   1 
ATOM   2695 C CA  . VAL B 1 66  ? 1.30700   21.73900  5.79000   1.000 49.15000 ? 68  VAL B CA  1 
ATOM   2696 C C   . VAL B 1 66  ? 0.31900   22.56400  4.97400   1.000 52.05000 ? 68  VAL B C   1 
ATOM   2697 O O   . VAL B 1 66  ? -0.28200  23.51000  5.50200   1.000 51.16000 ? 68  VAL B O   1 
ATOM   2698 C CB  . VAL B 1 66  ? 0.57900   20.76600  6.72500   1.000 48.39000 ? 68  VAL B CB  1 
ATOM   2699 C CG1 . VAL B 1 66  ? -0.27200  19.81700  5.92500   1.000 44.67000 ? 68  VAL B CG1 1 
ATOM   2700 C CG2 . VAL B 1 66  ? 1.58100   20.00100  7.58400   1.000 47.08000 ? 68  VAL B CG2 1 
ATOM   2701 N N   . GLN B 1 67  ? 0.16500   22.22800  3.69700   1.000 49.48000 ? 69  GLN B N   1 
ATOM   2702 C CA  . GLN B 1 67  ? -0.76500  22.92700  2.81500   1.000 52.46000 ? 69  GLN B CA  1 
ATOM   2703 C C   . GLN B 1 67  ? -1.63300  21.91200  2.08700   1.000 49.15000 ? 69  GLN B C   1 
ATOM   2704 O O   . GLN B 1 67  ? -1.12000  21.07100  1.33800   1.000 45.00000 ? 69  GLN B O   1 
ATOM   2705 C CB  . GLN B 1 67  ? -0.02500  23.81200  1.81200   1.000 55.49000 ? 69  GLN B CB  1 
ATOM   2706 C CG  . GLN B 1 67  ? 0.32500   25.20700  2.32400   1.000 59.42000 ? 69  GLN B CG  1 
ATOM   2707 C CD  . GLN B 1 67  ? 1.37800   25.88500  1.45900   1.000 64.48000 ? 69  GLN B CD  1 
ATOM   2708 O OE1 . GLN B 1 67  ? 2.55700   25.93800  1.81700   1.000 61.36000 ? 69  GLN B OE1 1 
ATOM   2709 N NE2 . GLN B 1 67  ? 0.95500   26.40000  0.30800   1.000 68.62000 ? 69  GLN B NE2 1 
ATOM   2710 N N   . ALA B 1 68  ? -2.94000  21.99600  2.31400   1.000 48.88000 ? 70  ALA B N   1 
ATOM   2711 C CA  . ALA B 1 68  ? -3.94500  21.21400  1.59500   1.000 49.15000 ? 70  ALA B CA  1 
ATOM   2712 C C   . ALA B 1 68  ? -4.50300  22.13100  0.51700   1.000 52.63000 ? 70  ALA B C   1 
ATOM   2713 O O   . ALA B 1 68  ? -5.48800  22.84100  0.73000   1.000 56.68000 ? 70  ALA B O   1 
ATOM   2714 C CB  . ALA B 1 68  ? -5.04200  20.71400  2.53100   1.000 45.79000 ? 70  ALA B CB  1 
ATOM   2715 N N   . GLY B 1 69  ? -3.86400  22.10900  -0.65200  1.000 50.09000 ? 71  GLY B N   1 
ATOM   2716 C CA  . GLY B 1 69  ? -4.18300  23.04500  -1.70700  1.000 55.34000 ? 71  GLY B CA  1 
ATOM   2717 C C   . GLY B 1 69  ? -3.86200  24.45200  -1.26000  1.000 60.63000 ? 71  GLY B C   1 
ATOM   2718 O O   . GLY B 1 69  ? -2.69300  24.80000  -1.07400  1.000 61.25000 ? 71  GLY B O   1 
ATOM   2719 N N   . ASN B 1 70  ? -4.90000  25.26200  -1.06100  1.000 63.66000 ? 72  ASN B N   1 
ATOM   2720 C CA  . ASN B 1 70  ? -4.69700  26.61100  -0.55000  1.000 64.59000 ? 72  ASN B CA  1 
ATOM   2721 C C   . ASN B 1 70  ? -4.50700  26.61700  0.96100   1.000 66.03000 ? 72  ASN B C   1 
ATOM   2722 O O   . ASN B 1 70  ? -3.56100  27.23300  1.47200   1.000 69.41000 ? 72  ASN B O   1 
ATOM   2723 C CB  . ASN B 1 70  ? -5.88100  27.48900  -0.93700  1.000 64.82000 ? 72  ASN B CB  1 
ATOM   2724 C CG  . ASN B 1 70  ? -5.94600  27.73100  -2.41800  1.000 68.64000 ? 72  ASN B CG  1 
ATOM   2725 O OD1 . ASN B 1 70  ? -4.91300  27.92300  -3.07000  1.000 67.20000 ? 72  ASN B OD1 1 
ATOM   2726 N ND2 . ASN B 1 70  ? -7.15600  27.70400  -2.97200  1.000 68.31000 ? 72  ASN B ND2 1 
ATOM   2727 N N   . VAL B 1 71  ? -5.37800  25.91000  1.67700   1.000 64.35000 ? 73  VAL B N   1 
ATOM   2728 C CA  . VAL B 1 71  ? -5.42400  25.98400  3.13100   1.000 60.71000 ? 73  VAL B CA  1 
ATOM   2729 C C   . VAL B 1 71  ? -4.10400  25.51600  3.73000   1.000 60.76000 ? 73  VAL B C   1 
ATOM   2730 O O   . VAL B 1 71  ? -3.57000  24.46000  3.36100   1.000 57.97000 ? 73  VAL B O   1 
ATOM   2731 C CB  . VAL B 1 71  ? -6.59900  25.14500  3.65100   1.000 59.32000 ? 73  VAL B CB  1 
ATOM   2732 C CG1 . VAL B 1 71  ? -6.58100  25.09100  5.15900   1.000 59.66000 ? 73  VAL B CG1 1 
ATOM   2733 C CG2 . VAL B 1 71  ? -7.92000  25.70100  3.12400   1.000 63.13000 ? 73  VAL B CG2 1 
ATOM   2734 N N   . GLN B 1 72  ? -3.56200  26.30600  4.65800   1.000 58.03000 ? 74  GLN B N   1 
ATOM   2735 C CA  . GLN B 1 72  ? -2.51700  25.81300  5.54000   1.000 55.76000 ? 74  GLN B CA  1 
ATOM   2736 C C   . GLN B 1 72  ? -3.16900  25.06700  6.69900   1.000 55.79000 ? 74  GLN B C   1 
ATOM   2737 O O   . GLN B 1 72  ? -4.16200  25.53400  7.26600   1.000 58.38000 ? 74  GLN B O   1 
ATOM   2738 C CB  . GLN B 1 72  ? -1.64600  26.96100  6.05600   1.000 58.27000 ? 74  GLN B CB  1 
ATOM   2739 N N   . LEU B 1 73  ? -2.64600  23.88700  7.01600   1.000 50.62000 ? 75  LEU B N   1 
ATOM   2740 C CA  . LEU B 1 73  ? -3.07500  23.17400  8.21000   1.000 53.68000 ? 75  LEU B CA  1 
ATOM   2741 C C   . LEU B 1 73  ? -2.10600  23.46200  9.34700   1.000 51.25000 ? 75  LEU B C   1 
ATOM   2742 O O   . LEU B 1 73  ? -0.90400  23.62500  9.13400   1.000 53.02000 ? 75  LEU B O   1 
ATOM   2743 C CB  . LEU B 1 73  ? -3.15100  21.66700  7.96200   1.000 50.96000 ? 75  LEU B CB  1 
ATOM   2744 C CG  . LEU B 1 73  ? -3.92300  21.22600  6.72500   1.000 49.74000 ? 75  LEU B CG  1 
ATOM   2745 C CD1 . LEU B 1 73  ? -3.87300  19.71600  6.59200   1.000 46.84000 ? 75  LEU B CD1 1 
ATOM   2746 C CD2 . LEU B 1 73  ? -5.35800  21.70800  6.80000   1.000 51.72000 ? 75  LEU B CD2 1 
ATOM   2747 N N   . ARG B 1 74  ? -2.63300  23.52200  10.56500  1.000 53.80000 ? 76  ARG B N   1 
ATOM   2748 C CA  . ARG B 1 74  ? -1.82400  23.83700  11.73700  1.000 55.76000 ? 76  ARG B CA  1 
ATOM   2749 C C   . ARG B 1 74  ? -1.37000  22.54200  12.40300  1.000 49.83000 ? 76  ARG B C   1 
ATOM   2750 O O   . ARG B 1 74  ? -2.20300  21.74400  12.84800  1.000 50.16000 ? 76  ARG B O   1 
ATOM   2751 C CB  . ARG B 1 74  ? -2.60500  24.71000  12.72400  1.000 56.71000 ? 76  ARG B CB  1 
ATOM   2752 N N   . VAL B 1 75  ? -0.05700  22.33500  12.46800  1.000 45.49000 ? 77  VAL B N   1 
ATOM   2753 C CA  . VAL B 1 75  ? 0.47300   21.16800  13.16500  1.000 47.47000 ? 77  VAL B CA  1 
ATOM   2754 C C   . VAL B 1 75  ? 0.33700   21.39900  14.66500  1.000 50.26000 ? 77  VAL B C   1 
ATOM   2755 O O   . VAL B 1 75  ? 0.84800   22.39100  15.20100  1.000 49.93000 ? 77  VAL B O   1 
ATOM   2756 C CB  . VAL B 1 75  ? 1.93200   20.90300  12.76300  1.000 47.88000 ? 77  VAL B CB  1 
ATOM   2757 N N   . ILE B 1 76  ? -0.37200  20.49700  15.35400  1.000 46.38000 ? 78  ILE B N   1 
ATOM   2758 C CA  . ILE B 1 76  ? -0.57700  20.56600  16.79100  1.000 47.20000 ? 78  ILE B CA  1 
ATOM   2759 C C   . ILE B 1 76  ? 0.08800   19.40800  17.52500  1.000 51.19000 ? 78  ILE B C   1 
ATOM   2760 O O   . ILE B 1 76  ? -0.13600  19.21700  18.71900  1.000 49.49000 ? 78  ILE B O   1 
ATOM   2761 C CB  . ILE B 1 76  ? -2.07700  20.63600  17.14200  1.000 51.38000 ? 78  ILE B CB  1 
ATOM   2762 C CG1 . ILE B 1 76  ? -2.73600  19.26300  16.94300  1.000 51.63000 ? 78  ILE B CG1 1 
ATOM   2763 C CG2 . ILE B 1 76  ? -2.75800  21.74800  16.33300  1.000 48.31000 ? 78  ILE B CG2 1 
ATOM   2764 C CD1 . ILE B 1 76  ? -4.24100  19.23700  17.18500  1.000 43.99000 ? 78  ILE B CD1 1 
ATOM   2765 N N   . GLY B 1 77  ? 0.91500   18.63800  16.83000  1.000 48.01000 ? 79  GLY B N   1 
ATOM   2766 C CA  . GLY B 1 77  ? 1.63500   17.54300  17.44100  1.000 45.27000 ? 79  GLY B CA  1 
ATOM   2767 C C   . GLY B 1 77  ? 2.45100   16.82700  16.39000  1.000 49.04000 ? 79  GLY B C   1 
ATOM   2768 O O   . GLY B 1 77  ? 2.09500   16.84900  15.20400  1.000 45.05000 ? 79  GLY B O   1 
ATOM   2769 N N   . HIS B 1 78  ? 3.55400   16.20700  16.80100  1.000 45.58000 ? 80  HIS B N   1 
ATOM   2770 C CA  . HIS B 1 78  ? 4.35400   15.43200  15.87300  1.000 47.12000 ? 80  HIS B CA  1 
ATOM   2771 C C   . HIS B 1 78  ? 4.93300   14.23200  16.59900  1.000 53.55000 ? 80  HIS B C   1 
ATOM   2772 O O   . HIS B 1 78  ? 5.18700   14.27100  17.80700  1.000 49.04000 ? 80  HIS B O   1 
ATOM   2773 C CB  . HIS B 1 78  ? 5.46900   16.26900  15.23900  1.000 47.68000 ? 80  HIS B CB  1 
ATOM   2774 C CG  . HIS B 1 78  ? 6.39300   16.90200  16.23100  1.000 57.98000 ? 80  HIS B CG  1 
ATOM   2775 N ND1 . HIS B 1 78  ? 6.17000   18.15300  16.76700  1.000 60.58000 ? 80  HIS B ND1 1 
ATOM   2776 C CD2 . HIS B 1 78  ? 7.54700   16.45800  16.78400  1.000 58.84000 ? 80  HIS B CD2 1 
ATOM   2777 C CE1 . HIS B 1 78  ? 7.14700   18.45300  17.60500  1.000 60.60000 ? 80  HIS B CE1 1 
ATOM   2778 N NE2 . HIS B 1 78  ? 7.99500   17.44000  17.63500  1.000 63.71000 ? 80  HIS B NE2 1 
ATOM   2779 N N   . SER B 1 79  ? 5.12500   13.15900  15.84400  1.000 47.89000 ? 81  SER B N   1 
ATOM   2780 C CA  . SER B 1 79  ? 5.72500   11.94800  16.37000  1.000 43.94000 ? 81  SER B CA  1 
ATOM   2781 C C   . SER B 1 79  ? 6.28900   11.15900  15.19800  1.000 46.87000 ? 81  SER B C   1 
ATOM   2782 O O   . SER B 1 79  ? 5.98300   11.43100  14.03200  1.000 43.51000 ? 81  SER B O   1 
ATOM   2783 C CB  . SER B 1 79  ? 4.71000   11.13700  17.19100  1.000 44.29000 ? 81  SER B CB  1 
ATOM   2784 O OG  . SER B 1 79  ? 4.05700   10.14200  16.43000  1.000 49.62000 ? 81  SER B OG  1 
ATOM   2785 N N   . MET B 1 80  ? 7.15200   10.20400  15.51900  1.000 42.79000 ? 82  MET B N   1 
ATOM   2786 C CA  . MET B 1 80  ? 7.78900   9.37200   14.51700  1.000 43.46000 ? 82  MET B CA  1 
ATOM   2787 C C   . MET B 1 80  ? 7.33400   7.93200   14.70200  1.000 41.37000 ? 82  MET B C   1 
ATOM   2788 O O   . MET B 1 80  ? 7.13300   7.47800   15.83100  1.000 43.11000 ? 82  MET B O   1 
ATOM   2789 C CB  . MET B 1 80  ? 9.31100   9.47600   14.62500  1.000 41.82000 ? 82  MET B CB  1 
ATOM   2790 C CG  . MET B 1 80  ? 10.02300  9.33500   13.30600  1.000 40.47000 ? 82  MET B CG  1 
ATOM   2791 S SD  . MET B 1 80  ? 11.78100  9.54800   13.52500  1.000 60.12000 ? 82  MET B SD  1 
ATOM   2792 C CE  . MET B 1 80  ? 12.21900  7.90300   14.11000  1.000 46.55000 ? 82  MET B CE  1 
ATOM   2793 N N   . GLN B 1 81  ? 7.12700   7.22700   13.59400  1.000 35.21000 ? 83  GLN B N   1 
ATOM   2794 C CA  . GLN B 1 81  ? 6.94000   5.77600   13.62600  1.000 35.96000 ? 83  GLN B CA  1 
ATOM   2795 C C   . GLN B 1 81  ? 7.86600   5.19800   12.56300  1.000 35.34000 ? 83  GLN B C   1 
ATOM   2796 O O   . GLN B 1 81  ? 7.59500   5.31100   11.36200  1.000 33.09000 ? 83  GLN B O   1 
ATOM   2797 C CB  . GLN B 1 81  ? 5.49100   5.36600   13.39000  1.000 40.87000 ? 83  GLN B CB  1 
ATOM   2798 C CG  . GLN B 1 81  ? 5.34400   3.84700   13.30100  1.000 42.18000 ? 83  GLN B CG  1 
ATOM   2799 C CD  . GLN B 1 81  ? 3.91800   3.41000   13.14900  1.000 46.90000 ? 83  GLN B CD  1 
ATOM   2800 O OE1 . GLN B 1 81  ? 3.08400   4.15300   12.62600  1.000 47.07000 ? 83  GLN B OE1 1 
ATOM   2801 N NE2 . GLN B 1 81  ? 3.61600   2.20100   13.61900  1.000 48.49000 ? 83  GLN B NE2 1 
ATOM   2802 N N   . ASN B 1 82  ? 8.98500   4.62700   13.00200  1.000 34.43000 ? 84  ASN B N   1 
ATOM   2803 C CA  . ASN B 1 82  ? 9.98500   4.07700   12.08000  1.000 32.91000 ? 84  ASN B CA  1 
ATOM   2804 C C   . ASN B 1 82  ? 10.37800  5.20700   11.12900  1.000 33.25000 ? 84  ASN B C   1 
ATOM   2805 O O   . ASN B 1 82  ? 10.69100  6.31000   11.60400  1.000 33.03000 ? 84  ASN B O   1 
ATOM   2806 C CB  . ASN B 1 82  ? 9.41000   2.82200   11.42600  1.000 30.63000 ? 84  ASN B CB  1 
ATOM   2807 C CG  . ASN B 1 82  ? 9.15000   1.71400   12.43100  1.000 34.90000 ? 84  ASN B CG  1 
ATOM   2808 O OD1 . ASN B 1 82  ? 9.93900   1.49400   13.35900  1.000 37.71000 ? 84  ASN B OD1 1 
ATOM   2809 N ND2 . ASN B 1 82  ? 8.05200   1.01500   12.26200  1.000 29.69000 ? 84  ASN B ND2 1 
ATOM   2810 N N   . CYS B 1 83  ? 10.29100  5.02300   9.81300   1.000 27.54000 ? 85  CYS B N   1 
ATOM   2811 C CA  . CYS B 1 83  ? 10.74600  6.03500   8.87300   1.000 33.68000 ? 85  CYS B CA  1 
ATOM   2812 C C   . CYS B 1 83  ? 9.65600   6.98500   8.38900   1.000 32.93000 ? 85  CYS B C   1 
ATOM   2813 O O   . CYS B 1 83  ? 9.89900   7.74800   7.44900   1.000 35.45000 ? 85  CYS B O   1 
ATOM   2814 C CB  . CYS B 1 83  ? 11.42300  5.36300   7.67700   1.000 36.52000 ? 85  CYS B CB  1 
ATOM   2815 S SG  . CYS B 1 83  ? 12.94300  4.45500   8.18200   1.000 57.68000 ? 85  CYS B SG  1 
ATOM   2816 N N   . VAL B 1 84  ? 8.48400   7.00500   9.00600   1.000 30.80000 ? 86  VAL B N   1 
ATOM   2817 C CA  . VAL B 1 84  ? 7.49200   8.00700   8.63800   1.000 34.20000 ? 86  VAL B CA  1 
ATOM   2818 C C   . VAL B 1 84  ? 7.22800   8.92600   9.82000   1.000 34.69000 ? 86  VAL B C   1 
ATOM   2819 O O   . VAL B 1 84  ? 7.15800   8.49600   10.98000  1.000 34.78000 ? 86  VAL B O   1 
ATOM   2820 C CB  . VAL B 1 84  ? 6.16500   7.42300   8.08200   1.000 36.95000 ? 86  VAL B CB  1 
ATOM   2821 C CG1 . VAL B 1 84  ? 6.43700   6.52400   6.87600   1.000 32.44000 ? 86  VAL B CG1 1 
ATOM   2822 C CG2 . VAL B 1 84  ? 5.36200   6.72800   9.13200   1.000 37.30000 ? 86  VAL B CG2 1 
ATOM   2823 N N   . LEU B 1 85  ? 7.12400   10.20300  9.50200   1.000 35.57000 ? 87  LEU B N   1 
ATOM   2824 C CA  . LEU B 1 85  ? 6.69500   11.24400  10.40700  1.000 34.45000 ? 87  LEU B CA  1 
ATOM   2825 C C   . LEU B 1 85  ? 5.17500   11.34600  10.40500  1.000 38.06000 ? 87  LEU B C   1 
ATOM   2826 O O   . LEU B 1 85  ? 4.53600   11.33100  9.34600   1.000 34.00000 ? 87  LEU B O   1 
ATOM   2827 C CB  . LEU B 1 85  ? 7.32400   12.55800  9.95800   1.000 33.67000 ? 87  LEU B CB  1 
ATOM   2828 C CG  . LEU B 1 85  ? 6.94500   13.83400  10.67700  1.000 40.05000 ? 87  LEU B CG  1 
ATOM   2829 C CD1 . LEU B 1 85  ? 7.28800   13.74200  12.17400  1.000 43.05000 ? 87  LEU B CD1 1 
ATOM   2830 C CD2 . LEU B 1 85  ? 7.70500   14.96500  9.99500   1.000 40.60000 ? 87  LEU B CD2 1 
ATOM   2831 N N   . LYS B 1 86  ? 4.59900   11.44900  11.59500  1.000 34.64000 ? 88  LYS B N   1 
ATOM   2832 C CA  . LYS B 1 86  ? 3.16100   11.55900  11.79100  1.000 36.96000 ? 88  LYS B CA  1 
ATOM   2833 C C   . LYS B 1 86  ? 2.88700   12.92500  12.40500  1.000 41.31000 ? 88  LYS B C   1 
ATOM   2834 O O   . LYS B 1 86  ? 3.22200   13.16300  13.56900  1.000 43.76000 ? 88  LYS B O   1 
ATOM   2835 C CB  . LYS B 1 86  ? 2.64200   10.42300  12.67100  1.000 35.91000 ? 88  LYS B CB  1 
ATOM   2836 C CG  . LYS B 1 86  ? 2.52100   9.09100   11.92900  1.000 40.45000 ? 88  LYS B CG  1 
ATOM   2837 C CD  . LYS B 1 86  ? 2.38900   7.86400   12.84500  1.000 42.39000 ? 88  LYS B CD  1 
ATOM   2838 C CE  . LYS B 1 86  ? 1.49000   8.09900   14.03100  1.000 47.77000 ? 88  LYS B CE  1 
ATOM   2839 N NZ  . LYS B 1 86  ? 1.33200   6.83200   14.80900  1.000 56.20000 ? 88  LYS B NZ  1 
ATOM   2840 N N   . LEU B 1 87  ? 2.32800   13.83300  11.60700  1.000 38.29000 ? 89  LEU B N   1 
ATOM   2841 C CA  . LEU B 1 87  ? 2.06000   15.20100  12.02300  1.000 37.26000 ? 89  LEU B CA  1 
ATOM   2842 C C   . LEU B 1 87  ? 0.57900   15.32100  12.33700  1.000 38.72000 ? 89  LEU B C   1 
ATOM   2843 O O   . LEU B 1 87  ? -0.25000  15.30000  11.42200  1.000 38.44000 ? 89  LEU B O   1 
ATOM   2844 C CB  . LEU B 1 87  ? 2.44400   16.19700  10.93400  1.000 35.40000 ? 89  LEU B CB  1 
ATOM   2845 C CG  . LEU B 1 87  ? 3.87900   16.22400  10.42500  1.000 36.90000 ? 89  LEU B CG  1 
ATOM   2846 C CD1 . LEU B 1 87  ? 3.97700   17.20900  9.27100   1.000 37.11000 ? 89  LEU B CD1 1 
ATOM   2847 C CD2 . LEU B 1 87  ? 4.81200   16.61900  11.55900  1.000 42.89000 ? 89  LEU B CD2 1 
ATOM   2848 N N   . LYS B 1 88  ? 0.24600   15.46000  13.62100  1.000 39.36000 ? 90  LYS B N   1 
ATOM   2849 C CA  . LYS B 1 88  ? -1.14400  15.70400  14.00600  1.000 42.57000 ? 90  LYS B CA  1 
ATOM   2850 C C   . LYS B 1 88  ? -1.51700  17.14700  13.66800  1.000 43.26000 ? 90  LYS B C   1 
ATOM   2851 O O   . LYS B 1 88  ? -0.76200  18.08000  13.96200  1.000 44.31000 ? 90  LYS B O   1 
ATOM   2852 C CB  . LYS B 1 88  ? -1.35100  15.41700  15.49800  1.000 44.42000 ? 90  LYS B CB  1 
ATOM   2853 C CG  . LYS B 1 88  ? -2.75700  15.72800  16.00300  1.000 48.18000 ? 90  LYS B CG  1 
ATOM   2854 C CD  . LYS B 1 88  ? -3.40800  14.52900  16.68600  1.000 55.10000 ? 90  LYS B CD  1 
ATOM   2855 C CE  . LYS B 1 88  ? -3.82300  13.48100  15.65900  1.000 49.32000 ? 90  LYS B CE  1 
ATOM   2856 N NZ  . LYS B 1 88  ? -4.81000  12.44900  16.13600  1.000 53.87000 ? 90  LYS B NZ  1 
ATOM   2857 N N   . VAL B 1 89  ? -2.66300  17.32800  13.01400  1.000 43.37000 ? 91  VAL B N   1 
ATOM   2858 C CA  . VAL B 1 89  ? -3.09000  18.63800  12.54800  1.000 44.00000 ? 91  VAL B CA  1 
ATOM   2859 C C   . VAL B 1 89  ? -4.44000  18.98500  13.18100  1.000 48.65000 ? 91  VAL B C   1 
ATOM   2860 O O   . VAL B 1 89  ? -5.12500  18.14100  13.76700  1.000 45.15000 ? 91  VAL B O   1 
ATOM   2861 C CB  . VAL B 1 89  ? -3.16200  18.71900  11.01000  1.000 44.02000 ? 91  VAL B CB  1 
ATOM   2862 C CG1 . VAL B 1 89  ? -1.76900  18.67100  10.42300  1.000 43.43000 ? 91  VAL B CG1 1 
ATOM   2863 C CG2 . VAL B 1 89  ? -4.03500  17.59400  10.45500  1.000 42.40000 ? 91  VAL B CG2 1 
ATOM   2864 N N   . ASP B 1 90  ? -4.81600  20.25800  13.03500  1.000 52.19000 ? 92  ASP B N   1 
ATOM   2865 C CA  . ASP B 1 90  ? -6.00200  20.78700  13.70600  1.000 54.89000 ? 92  ASP B CA  1 
ATOM   2866 C C   . ASP B 1 90  ? -7.29000  20.15600  13.18100  1.000 57.67000 ? 92  ASP B C   1 
ATOM   2867 O O   . ASP B 1 90  ? -8.22500  19.91600  13.95600  1.000 62.39000 ? 92  ASP B O   1 
ATOM   2868 C CB  . ASP B 1 90  ? -6.04900  22.30800  13.53400  1.000 56.53000 ? 92  ASP B CB  1 
ATOM   2869 C CG  . ASP B 1 90  ? -6.02200  22.72500  12.06800  1.000 62.27000 ? 92  ASP B CG  1 
ATOM   2870 O OD1 . ASP B 1 90  ? -6.97800  22.40100  11.34300  1.000 65.43000 ? 92  ASP B OD1 1 
ATOM   2871 O OD2 . ASP B 1 90  ? -5.04100  23.34900  11.61900  1.000 64.33000 ? 92  ASP B OD2 1 
ATOM   2872 N N   . THR B 1 91  ? -7.37000  19.89100  11.87400  1.000 54.66000 ? 93  THR B N   1 
ATOM   2873 C CA  . THR B 1 91  ? -8.62300  19.48800  11.24100  1.000 54.70000 ? 93  THR B CA  1 
ATOM   2874 C C   . THR B 1 91  ? -8.53400  18.09200  10.64300  1.000 50.46000 ? 93  THR B C   1 
ATOM   2875 O O   . THR B 1 91  ? -7.50500  17.70600  10.08200  1.000 47.32000 ? 93  THR B O   1 
ATOM   2876 C CB  . THR B 1 91  ? -9.03600  20.45400  10.12500  1.000 59.14000 ? 93  THR B CB  1 
ATOM   2877 O OG1 . THR B 1 91  ? -8.81000  21.80300  10.54800  1.000 63.56000 ? 93  THR B OG1 1 
ATOM   2878 C CG2 . THR B 1 91  ? -10.52300 20.27300  9.80100   1.000 56.00000 ? 93  THR B CG2 1 
ATOM   2879 N N   . ALA B 1 92  ? -9.63600  17.35200  10.74800  1.000 50.69000 ? 94  ALA B N   1 
ATOM   2880 C CA  . ALA B 1 92  ? -9.76000  16.07200  10.07300  1.000 48.11000 ? 94  ALA B CA  1 
ATOM   2881 C C   . ALA B 1 92  ? -9.98300  16.29400  8.58400   1.000 47.36000 ? 94  ALA B C   1 
ATOM   2882 O O   . ALA B 1 92  ? -10.64000 17.25700  8.17900   1.000 48.22000 ? 94  ALA B O   1 
ATOM   2883 C CB  . ALA B 1 92  ? -10.92000 15.27100  10.66800  1.000 46.07000 ? 94  ALA B CB  1 
ATOM   2884 N N   . ASN B 1 93  ? -9.41900  15.42100  7.76400   1.000 41.90000 ? 95  ASN B N   1 
ATOM   2885 C CA  . ASN B 1 93  ? -9.69200  15.51500  6.33800   1.000 38.77000 ? 95  ASN B CA  1 
ATOM   2886 C C   . ASN B 1 93  ? -11.11900 15.07700  6.08800   1.000 38.08000 ? 95  ASN B C   1 
ATOM   2887 O O   . ASN B 1 93  ? -11.45400 13.90200  6.33300   1.000 39.12000 ? 95  ASN B O   1 
ATOM   2888 C CB  . ASN B 1 93  ? -8.71300  14.66500  5.54000   1.000 39.89000 ? 95  ASN B CB  1 
ATOM   2889 C CG  . ASN B 1 93  ? -8.90000  14.81000  4.04100   1.000 39.24000 ? 95  ASN B CG  1 
ATOM   2890 O OD1 . ASN B 1 93  ? -9.79000  15.52400  3.57000   1.000 42.44000 ? 95  ASN B OD1 1 
ATOM   2891 N ND2 . ASN B 1 93  ? -8.04700  14.14600  3.28200   1.000 37.74000 ? 95  ASN B ND2 1 
ATOM   2892 N N   . PRO B 1 94  ? -12.01800 15.95000  5.62600   1.000 37.52000 ? 96  PRO B N   1 
ATOM   2893 C CA  . PRO B 1 94  ? -13.37900 15.50500  5.33400   1.000 38.52000 ? 96  PRO B CA  1 
ATOM   2894 C C   . PRO B 1 94  ? -13.44500 14.53600  4.16500   1.000 39.41000 ? 96  PRO B C   1 
ATOM   2895 O O   . PRO B 1 94  ? -14.47400 13.87900  3.99200   1.000 41.08000 ? 96  PRO B O   1 
ATOM   2896 C CB  . PRO B 1 94  ? -14.13100 16.80500  5.03500   1.000 39.75000 ? 96  PRO B CB  1 
ATOM   2897 C CG  . PRO B 1 94  ? -13.08900 17.74700  4.56000   1.000 39.34000 ? 96  PRO B CG  1 
ATOM   2898 C CD  . PRO B 1 94  ? -11.80200 17.36400  5.25400   1.000 35.79000 ? 96  PRO B CD  1 
ATOM   2899 N N   . LYS B 1 95  ? -12.37400 14.39600  3.38700   1.000 38.72000 ? 97  LYS B N   1 
ATOM   2900 C CA  . LYS B 1 95  ? -12.37200 13.50100  2.23800   1.000 42.41000 ? 97  LYS B CA  1 
ATOM   2901 C C   . LYS B 1 95  ? -11.69900 12.17300  2.53500   1.000 40.37000 ? 97  LYS B C   1 
ATOM   2902 O O   . LYS B 1 95  ? -11.40900 11.41800  1.60100   1.000 38.99000 ? 97  LYS B O   1 
ATOM   2903 C CB  . LYS B 1 95  ? -11.69300 14.16900  1.04600   1.000 37.24000 ? 97  LYS B CB  1 
ATOM   2904 C CG  . LYS B 1 95  ? -12.33900 15.47100  0.61500   1.000 41.19000 ? 97  LYS B CG  1 
ATOM   2905 C CD  . LYS B 1 95  ? -11.65200 15.99300  -0.63000  1.000 43.70000 ? 97  LYS B CD  1 
ATOM   2906 C CE  . LYS B 1 95  ? -11.74700 17.50200  -0.72100  1.000 51.87000 ? 97  LYS B CE  1 
ATOM   2907 N NZ  . LYS B 1 95  ? -11.93500 17.96200  -2.12500  1.000 62.20000 ? 97  LYS B NZ  1 
ATOM   2908 N N   . THR B 1 96  ? -11.44700 11.87800  3.80900   1.000 37.01000 ? 98  THR B N   1 
ATOM   2909 C CA  . THR B 1 96  ? -10.80400 10.63800  4.21300   1.000 37.09000 ? 98  THR B CA  1 
ATOM   2910 C C   . THR B 1 96  ? -11.64200 9.45200   3.75200   1.000 38.02000 ? 98  THR B C   1 
ATOM   2911 O O   . THR B 1 96  ? -12.80700 9.34600   4.14700   1.000 38.79000 ? 98  THR B O   1 
ATOM   2912 C CB  . THR B 1 96  ? -10.63000 10.59500  5.73800   1.000 40.38000 ? 98  THR B CB  1 
ATOM   2913 O OG1 . THR B 1 96  ? -9.90200  11.75000  6.16900   1.000 36.76000 ? 98  THR B OG1 1 
ATOM   2914 C CG2 . THR B 1 96  ? -9.90000  9.32700   6.17700   1.000 34.61000 ? 98  THR B CG2 1 
ATOM   2915 N N   . PRO B 1 97  ? -11.10500 8.55800   2.93000   1.000 38.60000 ? 99  PRO B N   1 
ATOM   2916 C CA  . PRO B 1 97  ? -11.85000 7.35100   2.55100   1.000 36.13000 ? 99  PRO B CA  1 
ATOM   2917 C C   . PRO B 1 97  ? -11.79400 6.32000   3.66800   1.000 35.12000 ? 99  PRO B C   1 
ATOM   2918 O O   . PRO B 1 97  ? -11.05100 6.46200   4.63500   1.000 32.96000 ? 99  PRO B O   1 
ATOM   2919 C CB  . PRO B 1 97  ? -11.09300 6.85700   1.31400   1.000 37.54000 ? 99  PRO B CB  1 
ATOM   2920 C CG  . PRO B 1 97  ? -9.66700  7.28000   1.58200   1.000 35.43000 ? 99  PRO B CG  1 
ATOM   2921 C CD  . PRO B 1 97  ? -9.75300  8.58800   2.34300   1.000 36.93000 ? 99  PRO B CD  1 
ATOM   2922 N N   . LYS B 1 98  ? -12.58800 5.26400   3.51700   1.000 33.57000 ? 100 LYS B N   1 
ATOM   2923 C CA  . LYS B 1 98  ? -12.33400 4.05900   4.29300   1.000 36.98000 ? 100 LYS B CA  1 
ATOM   2924 C C   . LYS B 1 98  ? -11.00000 3.48000   3.85100   1.000 37.11000 ? 100 LYS B C   1 
ATOM   2925 O O   . LYS B 1 98  ? -10.72400 3.37000   2.64900   1.000 34.80000 ? 100 LYS B O   1 
ATOM   2926 C CB  . LYS B 1 98  ? -13.44600 3.02900   4.09900   1.000 36.57000 ? 100 LYS B CB  1 
ATOM   2927 N N   . TYR B 1 99  ? -10.15800 3.12900   4.81800   1.000 33.70000 ? 101 TYR B N   1 
ATOM   2928 C CA  . TYR B 1 99  ? -8.79700  2.75800   4.46400   1.000 33.03000 ? 101 TYR B CA  1 
ATOM   2929 C C   . TYR B 1 99  ? -8.20500  1.86000   5.54000   1.000 35.12000 ? 101 TYR B C   1 
ATOM   2930 O O   . TYR B 1 99  ? -8.66700  1.84000   6.68400   1.000 33.39000 ? 101 TYR B O   1 
ATOM   2931 C CB  . TYR B 1 99  ? -7.91000  4.00000   4.25700   1.000 30.45000 ? 101 TYR B CB  1 
ATOM   2932 C CG  . TYR B 1 99  ? -7.40200  4.57900   5.55500   1.000 31.36000 ? 101 TYR B CG  1 
ATOM   2933 C CD1 . TYR B 1 99  ? -6.19600  4.14900   6.10700   1.000 30.02000 ? 101 TYR B CD1 1 
ATOM   2934 C CD2 . TYR B 1 99  ? -8.13500  5.54800   6.24200   1.000 32.69000 ? 101 TYR B CD2 1 
ATOM   2935 C CE1 . TYR B 1 99  ? -5.74300  4.64800   7.30400   1.000 30.29000 ? 101 TYR B CE1 1 
ATOM   2936 C CE2 . TYR B 1 99  ? -7.68400  6.06300   7.44300   1.000 33.79000 ? 101 TYR B CE2 1 
ATOM   2937 C CZ  . TYR B 1 99  ? -6.48600  5.60700   7.97300   1.000 33.47000 ? 101 TYR B CZ  1 
ATOM   2938 O OH  . TYR B 1 99  ? -6.02600  6.10900   9.17600   1.000 38.66000 ? 101 TYR B OH  1 
ATOM   2939 N N   . LYS B 1 100 ? -7.13800  1.15000   5.14700   1.000 34.05000 ? 102 LYS B N   1 
ATOM   2940 C CA  . LYS B 1 100 ? -6.32800  0.28700   6.00000   1.000 33.18000 ? 102 LYS B CA  1 
ATOM   2941 C C   . LYS B 1 100 ? -4.86500  0.43600   5.56800   1.000 29.94000 ? 102 LYS B C   1 
ATOM   2942 O O   . LYS B 1 100 ? -4.57900  0.67500   4.39400   1.000 26.66000 ? 102 LYS B O   1 
ATOM   2943 C CB  . LYS B 1 100 ? -6.74900  -1.19900  5.87500   1.000 34.73000 ? 102 LYS B CB  1 
ATOM   2944 C CG  . LYS B 1 100 ? -7.96700  -1.66000  6.71100   1.000 51.97000 ? 102 LYS B CG  1 
ATOM   2945 C CD  . LYS B 1 100 ? -9.35200  -1.18600  6.15900   1.000 53.14000 ? 102 LYS B CD  1 
ATOM   2946 C CE  . LYS B 1 100 ? -10.48600 -1.23300  7.21200   1.000 53.37000 ? 102 LYS B CE  1 
ATOM   2947 N NZ  . LYS B 1 100 ? -10.67300 -2.58100  7.85600   1.000 59.84000 ? 102 LYS B NZ  1 
ATOM   2948 N N   . PHE B 1 101 ? -3.94200  0.28800   6.52300   1.000 29.32000 ? 103 PHE B N   1 
ATOM   2949 C CA  . PHE B 1 101 ? -2.51700  0.15800   6.20500   1.000 27.02000 ? 103 PHE B CA  1 
ATOM   2950 C C   . PHE B 1 101 ? -2.17400  -1.32500  6.08200   1.000 29.98000 ? 103 PHE B C   1 
ATOM   2951 O O   . PHE B 1 101 ? -2.46600  -2.10700  6.99100   1.000 31.31000 ? 103 PHE B O   1 
ATOM   2952 C CB  . PHE B 1 101 ? -1.64900  0.79400   7.29100   1.000 31.32000 ? 103 PHE B CB  1 
ATOM   2953 C CG  . PHE B 1 101 ? -1.71900  2.29200   7.34500   1.000 30.07000 ? 103 PHE B CG  1 
ATOM   2954 C CD1 . PHE B 1 101 ? -2.23200  3.02500   6.27900   1.000 29.29000 ? 103 PHE B CD1 1 
ATOM   2955 C CD2 . PHE B 1 101 ? -1.25200  2.97000   8.46900   1.000 27.64000 ? 103 PHE B CD2 1 
ATOM   2956 C CE1 . PHE B 1 101 ? -2.28800  4.40900   6.32100   1.000 28.33000 ? 103 PHE B CE1 1 
ATOM   2957 C CE2 . PHE B 1 101 ? -1.29300  4.36500   8.53300   1.000 29.39000 ? 103 PHE B CE2 1 
ATOM   2958 C CZ  . PHE B 1 101 ? -1.80400  5.09100   7.45600   1.000 33.01000 ? 103 PHE B CZ  1 
ATOM   2959 N N   . VAL B 1 102 ? -1.57100  -1.71900  4.95500   1.000 29.65000 ? 104 VAL B N   1 
ATOM   2960 C CA  . VAL B 1 102 ? -1.15500  -3.10200  4.75600   1.000 28.86000 ? 104 VAL B CA  1 
ATOM   2961 C C   . VAL B 1 102 ? 0.28000   -3.12200  4.22500   1.000 30.66000 ? 104 VAL B C   1 
ATOM   2962 O O   . VAL B 1 102 ? 0.77900   -2.14900  3.66300   1.000 30.65000 ? 104 VAL B O   1 
ATOM   2963 C CB  . VAL B 1 102 ? -2.08200  -3.88700  3.80200   1.000 29.68000 ? 104 VAL B CB  1 
ATOM   2964 C CG1 . VAL B 1 102 ? -3.53800  -3.67100  4.16100   1.000 27.12000 ? 104 VAL B CG1 1 
ATOM   2965 C CG2 . VAL B 1 102 ? -1.82300  -3.48400  2.37600   1.000 30.42000 ? 104 VAL B CG2 1 
ATOM   2966 N N   . ARG B 1 103 ? 0.93600   -4.26000  4.43000   1.000 29.07000 ? 105 ARG B N   1 
ATOM   2967 C CA  . ARG B 1 103 ? 2.27300   -4.51800  3.89900   1.000 34.35000 ? 105 ARG B CA  1 
ATOM   2968 C C   . ARG B 1 103 ? 2.17800   -5.60700  2.84500   1.000 31.39000 ? 105 ARG B C   1 
ATOM   2969 O O   . ARG B 1 103 ? 1.64100   -6.68400  3.11900   1.000 32.63000 ? 105 ARG B O   1 
ATOM   2970 C CB  . ARG B 1 103 ? 3.23600   -4.95400  5.00800   1.000 31.10000 ? 105 ARG B CB  1 
ATOM   2971 C CG  . ARG B 1 103 ? 4.66300   -5.23300  4.51100   1.000 30.64000 ? 105 ARG B CG  1 
ATOM   2972 C CD  . ARG B 1 103 ? 5.65900   -5.17600  5.65700   1.000 32.75000 ? 105 ARG B CD  1 
ATOM   2973 N NE  . ARG B 1 103 ? 7.02200   -5.47500  5.20600   1.000 32.22000 ? 105 ARG B NE  1 
ATOM   2974 C CZ  . ARG B 1 103 ? 7.92300   -4.55300  4.88900   1.000 32.12000 ? 105 ARG B CZ  1 
ATOM   2975 N NH1 . ARG B 1 103 ? 7.61100   -3.26400  4.97100   1.000 28.34000 ? 105 ARG B NH1 1 
ATOM   2976 N NH2 . ARG B 1 103 ? 9.14700   -4.91900  4.50400   1.000 28.65000 ? 105 ARG B NH2 1 
ATOM   2977 N N   . ILE B 1 104 ? 2.71900   -5.34500  1.65500   1.000 27.46000 ? 106 ILE B N   1 
ATOM   2978 C CA  . ILE B 1 104 ? 2.66300   -6.33000  0.57400   1.000 33.56000 ? 106 ILE B CA  1 
ATOM   2979 C C   . ILE B 1 104 ? 3.97900   -7.08500  0.48200   1.000 38.26000 ? 106 ILE B C   1 
ATOM   2980 O O   . ILE B 1 104 ? 4.94100   -6.76400  1.19100   1.000 32.35000 ? 106 ILE B O   1 
ATOM   2981 C CB  . ILE B 1 104 ? 2.32700   -5.66800  -0.77500  1.000 33.95000 ? 106 ILE B CB  1 
ATOM   2982 C CG1 . ILE B 1 104 ? 3.29800   -4.51300  -1.06300  1.000 32.37000 ? 106 ILE B CG1 1 
ATOM   2983 C CG2 . ILE B 1 104 ? 0.85900   -5.24800  -0.79600  1.000 34.22000 ? 106 ILE B CG2 1 
ATOM   2984 C CD1 . ILE B 1 104 ? 3.39400   -4.14100  -2.52800  1.000 36.02000 ? 106 ILE B CD1 1 
ATOM   2985 N N   . GLN B 1 105 ? 4.02300   -8.08800  -0.38900  1.000 38.10000 ? 107 GLN B N   1 
ATOM   2986 C CA  . GLN B 1 105 ? 5.19400   -8.92100  -0.61100  1.000 37.81000 ? 107 GLN B CA  1 
ATOM   2987 C C   . GLN B 1 105 ? 5.67100   -8.76700  -2.06500  1.000 35.86000 ? 107 GLN B C   1 
ATOM   2988 O O   . GLN B 1 105 ? 4.90400   -8.37300  -2.93200  1.000 33.60000 ? 107 GLN B O   1 
ATOM   2989 C CB  . GLN B 1 105 ? 4.87800   -10.39600 -0.34100  1.000 43.86000 ? 107 GLN B CB  1 
ATOM   2990 C CG  . GLN B 1 105 ? 4.50700   -10.71400 1.09000   1.000 51.38000 ? 107 GLN B CG  1 
ATOM   2991 C CD  . GLN B 1 105 ? 3.31300   -11.64100 1.14600   1.000 60.10000 ? 107 GLN B CD  1 
ATOM   2992 O OE1 . GLN B 1 105 ? 3.41100   -12.81700 0.79200   1.000 66.93000 ? 107 GLN B OE1 1 
ATOM   2993 N NE2 . GLN B 1 105 ? 2.16800   -11.11200 1.56800   1.000 61.03000 ? 107 GLN B NE2 1 
ATOM   2994 N N   . PRO B 1 106 ? 6.95200   -9.08200  -2.31600  1.000 34.32000 ? 108 PRO B N   1 
ATOM   2995 C CA  . PRO B 1 106 ? 7.43100   -9.03100  -3.71200  1.000 36.02000 ? 108 PRO B CA  1 
ATOM   2996 C C   . PRO B 1 106 ? 6.50000   -9.79100  -4.62800  1.000 33.50000 ? 108 PRO B C   1 
ATOM   2997 O O   . PRO B 1 106 ? 5.95200   -10.83100 -4.26400  1.000 31.86000 ? 108 PRO B O   1 
ATOM   2998 C CB  . PRO B 1 106 ? 8.81100   -9.70300  -3.62000  1.000 33.76000 ? 108 PRO B CB  1 
ATOM   2999 C CG  . PRO B 1 106 ? 9.26400   -9.44500  -2.26000  1.000 38.13000 ? 108 PRO B CG  1 
ATOM   3000 C CD  . PRO B 1 106 ? 8.02300   -9.44000  -1.38300  1.000 39.68000 ? 108 PRO B CD  1 
ATOM   3001 N N   . GLY B 1 107 ? 6.29800   -9.24800  -5.83000  1.000 35.20000 ? 109 GLY B N   1 
ATOM   3002 C CA  . GLY B 1 107 ? 5.40100   -9.82900  -6.79400  1.000 31.55000 ? 109 GLY B CA  1 
ATOM   3003 C C   . GLY B 1 107 ? 3.97800   -9.31300  -6.74800  1.000 32.94000 ? 109 GLY B C   1 
ATOM   3004 O O   . GLY B 1 107 ? 3.23800   -9.51700  -7.71200  1.000 32.60000 ? 109 GLY B O   1 
ATOM   3005 N N   . GLN B 1 108 ? 3.55200   -8.68800  -5.65600  1.000 32.77000 ? 110 GLN B N   1 
ATOM   3006 C CA  . GLN B 1 108 ? 2.19900   -8.14500  -5.62000  1.000 28.32000 ? 110 GLN B CA  1 
ATOM   3007 C C   . GLN B 1 108 ? 2.18700   -6.77800  -6.29300  1.000 29.99000 ? 110 GLN B C   1 
ATOM   3008 O O   . GLN B 1 108 ? 3.20800   -6.09100  -6.36500  1.000 32.11000 ? 110 GLN B O   1 
ATOM   3009 C CB  . GLN B 1 108 ? 1.67300   -8.06700  -4.18100  1.000 33.81000 ? 110 GLN B CB  1 
ATOM   3010 C CG  . GLN B 1 108 ? 1.58200   -9.45600  -3.49100  1.000 36.58000 ? 110 GLN B CG  1 
ATOM   3011 C CD  . GLN B 1 108 ? 0.97700   -9.42900  -2.08800  1.000 40.58000 ? 110 GLN B CD  1 
ATOM   3012 O OE1 . GLN B 1 108 ? 1.41000   -8.69100  -1.22300  1.000 40.98000 ? 110 GLN B OE1 1 
ATOM   3013 N NE2 . GLN B 1 108 ? -0.01400  -10.27200 -1.86100  1.000 54.87000 ? 110 GLN B NE2 1 
ATOM   3014 N N   . THR B 1 109 ? 1.02800   -6.40500  -6.82700  1.000 33.69000 ? 111 THR B N   1 
ATOM   3015 C CA  . THR B 1 109 ? 0.88300   -5.19700  -7.62600  1.000 30.53000 ? 111 THR B CA  1 
ATOM   3016 C C   . THR B 1 109 ? 0.08500   -4.14200  -6.87200  1.000 28.83000 ? 111 THR B C   1 
ATOM   3017 O O   . THR B 1 109 ? -0.65400  -4.44200  -5.93400  1.000 28.67000 ? 111 THR B O   1 
ATOM   3018 C CB  . THR B 1 109 ? 0.19500   -5.50200  -8.96300  1.000 35.07000 ? 111 THR B CB  1 
ATOM   3019 O OG1 . THR B 1 109 ? -0.98300  -6.27300  -8.71000  1.000 33.92000 ? 111 THR B OG1 1 
ATOM   3020 C CG2 . THR B 1 109 ? 1.13800   -6.27400  -9.89400  1.000 34.95000 ? 111 THR B CG2 1 
ATOM   3021 N N   . PHE B 1 110 ? 0.24900   -2.89300  -7.29200  1.000 28.85000 ? 112 PHE B N   1 
ATOM   3022 C CA  . PHE B 1 110 ? -0.46100  -1.77400  -6.68900  1.000 29.17000 ? 112 PHE B CA  1 
ATOM   3023 C C   . PHE B 1 110 ? -0.35700  -0.59100  -7.63500  1.000 28.66000 ? 112 PHE B C   1 
ATOM   3024 O O   . PHE B 1 110 ? 0.43200   -0.60200  -8.57700  1.000 27.07000 ? 112 PHE B O   1 
ATOM   3025 C CB  . PHE B 1 110 ? 0.07900   -1.41900  -5.29100  1.000 24.38000 ? 112 PHE B CB  1 
ATOM   3026 C CG  . PHE B 1 110 ? 1.56700   -1.07000  -5.25600  1.000 29.85000 ? 112 PHE B CG  1 
ATOM   3027 C CD1 . PHE B 1 110 ? 2.52400   -2.06800  -5.24000  1.000 27.32000 ? 112 PHE B CD1 1 
ATOM   3028 C CD2 . PHE B 1 110 ? 1.99400   0.25100   -5.20800  1.000 27.98000 ? 112 PHE B CD2 1 
ATOM   3029 C CE1 . PHE B 1 110 ? 3.88400   -1.76500  -5.19000  1.000 30.28000 ? 112 PHE B CE1 1 
ATOM   3030 C CE2 . PHE B 1 110 ? 3.36000   0.56400   -5.15900  1.000 29.11000 ? 112 PHE B CE2 1 
ATOM   3031 C CZ  . PHE B 1 110 ? 4.29800   -0.44500  -5.14700  1.000 31.48000 ? 112 PHE B CZ  1 
ATOM   3032 N N   . SER B 1 111 ? -1.19400  0.41000   -7.39200  1.000 27.65000 ? 113 SER B N   1 
ATOM   3033 C CA  . SER B 1 111 ? -1.16500  1.66000   -8.13500  1.000 27.42000 ? 113 SER B CA  1 
ATOM   3034 C C   . SER B 1 111 ? -0.41900  2.70600   -7.32600  1.000 27.22000 ? 113 SER B C   1 
ATOM   3035 O O   . SER B 1 111 ? -0.52900  2.74900   -6.09600  1.000 26.32000 ? 113 SER B O   1 
ATOM   3036 C CB  . SER B 1 111 ? -2.58600  2.16100   -8.42300  1.000 27.73000 ? 113 SER B CB  1 
ATOM   3037 O OG  . SER B 1 111 ? -3.33500  1.21800   -9.17000  1.000 27.91000 ? 113 SER B OG  1 
ATOM   3038 N N   . VAL B 1 112 ? 0.32800   3.55600   -8.01500  1.000 26.35000 ? 114 VAL B N   1 
ATOM   3039 C CA  . VAL B 1 112 ? 0.97700   4.70300   -7.40500  1.000 26.44000 ? 114 VAL B CA  1 
ATOM   3040 C C   . VAL B 1 112 ? 0.34400   5.95700   -7.97300  1.000 29.17000 ? 114 VAL B C   1 
ATOM   3041 O O   . VAL B 1 112 ? 0.15300   6.06400   -9.19300  1.000 31.22000 ? 114 VAL B O   1 
ATOM   3042 C CB  . VAL B 1 112 ? 2.49500   4.68800   -7.65800  1.000 31.17000 ? 114 VAL B CB  1 
ATOM   3043 C CG1 . VAL B 1 112 ? 3.14300   5.98900   -7.18200  1.000 30.18000 ? 114 VAL B CG1 1 
ATOM   3044 C CG2 . VAL B 1 112 ? 3.13900   3.47800   -6.96900  1.000 29.04000 ? 114 VAL B CG2 1 
ATOM   3045 N N   . LEU B 1 113 ? 0.00500   6.89600   -7.09700  1.000 27.16000 ? 115 LEU B N   1 
ATOM   3046 C CA  . LEU B 1 113 ? -0.38600  8.25500   -7.46800  1.000 26.07000 ? 115 LEU B CA  1 
ATOM   3047 C C   . LEU B 1 113 ? 0.83400   9.15600   -7.30900  1.000 32.02000 ? 115 LEU B C   1 
ATOM   3048 O O   . LEU B 1 113 ? 1.12500   9.62300   -6.19900  1.000 31.22000 ? 115 LEU B O   1 
ATOM   3049 C CB  . LEU B 1 113 ? -1.53800  8.75300   -6.59700  1.000 26.94000 ? 115 LEU B CB  1 
ATOM   3050 C CG  . LEU B 1 113 ? -2.04900  10.16600  -6.90600  1.000 29.56000 ? 115 LEU B CG  1 
ATOM   3051 C CD1 . LEU B 1 113 ? -2.60300  10.20500  -8.33200  1.000 27.73000 ? 115 LEU B CD1 1 
ATOM   3052 C CD2 . LEU B 1 113 ? -3.12800  10.60600  -5.90700  1.000 26.78000 ? 115 LEU B CD2 1 
ATOM   3053 N N   . ALA B 1 114 ? 1.53400   9.40800   -8.42100  1.000 26.35000 ? 116 ALA B N   1 
ATOM   3054 C CA  . ALA B 1 114 ? 2.68200   10.30100  -8.42900  1.000 32.18000 ? 116 ALA B CA  1 
ATOM   3055 C C   . ALA B 1 114 ? 2.22900   11.74100  -8.21900  1.000 36.83000 ? 116 ALA B C   1 
ATOM   3056 O O   . ALA B 1 114 ? 1.30200   12.21000  -8.88300  1.000 33.59000 ? 116 ALA B O   1 
ATOM   3057 C CB  . ALA B 1 114 ? 3.44100   10.17000  -9.74900  1.000 32.03000 ? 116 ALA B CB  1 
ATOM   3058 N N   . CYS B 1 115 ? 2.87400   12.44600  -7.28700  1.000 38.26000 ? 117 CYS B N   1 
ATOM   3059 C CA  . CYS B 1 115 ? 2.47800   13.80500  -6.94000  1.000 39.79000 ? 117 CYS B CA  1 
ATOM   3060 C C   . CYS B 1 115 ? 3.68800   14.73000  -6.94300  1.000 43.51000 ? 117 CYS B C   1 
ATOM   3061 O O   . CYS B 1 115 ? 4.82300   14.30500  -6.70300  1.000 41.62000 ? 117 CYS B O   1 
ATOM   3062 C CB  . CYS B 1 115 ? 1.79200   13.86500  -5.56900  1.000 39.54000 ? 117 CYS B CB  1 
ATOM   3063 S SG  . CYS B 1 115 ? 0.29000   12.86400  -5.39100  1.000 37.54000 ? 117 CYS B SG  1 
ATOM   3064 N N   . TYR B 1 116 ? 3.43800   16.00900  -7.22400  1.000 46.31000 ? 118 TYR B N   1 
ATOM   3065 C CA  . TYR B 1 116 ? 4.47900   17.03200  -7.20500  1.000 49.99000 ? 118 TYR B CA  1 
ATOM   3066 C C   . TYR B 1 116 ? 4.03500   18.12700  -6.24800  1.000 46.42000 ? 118 TYR B C   1 
ATOM   3067 O O   . TYR B 1 116 ? 3.04100   18.81100  -6.50600  1.000 49.11000 ? 118 TYR B O   1 
ATOM   3068 C CB  . TYR B 1 116 ? 4.74200   17.59600  -8.60100  1.000 50.96000 ? 118 TYR B CB  1 
ATOM   3069 N N   . ASN B 1 117 ? 4.75900   18.26700  -5.14000  1.000 48.34000 ? 119 ASN B N   1 
ATOM   3070 C CA  . ASN B 1 117 ? 4.52100   19.31600  -4.15200  1.000 50.06000 ? 119 ASN B CA  1 
ATOM   3071 C C   . ASN B 1 117 ? 3.06200   19.33000  -3.70400  1.000 48.73000 ? 119 ASN B C   1 
ATOM   3072 O O   . ASN B 1 117 ? 2.38800   20.36300  -3.71900  1.000 53.42000 ? 119 ASN B O   1 
ATOM   3073 C CB  . ASN B 1 117 ? 4.94800   20.68200  -4.69400  1.000 54.45000 ? 119 ASN B CB  1 
ATOM   3074 N N   . GLY B 1 118 ? 2.57100   18.15800  -3.29800  1.000 44.50000 ? 120 GLY B N   1 
ATOM   3075 C CA  . GLY B 1 118 ? 1.20600   18.00900  -2.83200  1.000 41.02000 ? 120 GLY B CA  1 
ATOM   3076 C C   . GLY B 1 118 ? 0.15300   17.85900  -3.91200  1.000 43.13000 ? 120 GLY B C   1 
ATOM   3077 O O   . GLY B 1 118 ? -1.02200  17.68400  -3.58200  1.000 41.72000 ? 120 GLY B O   1 
ATOM   3078 N N   . SER B 1 119 ? 0.52100   17.91300  -5.18500  1.000 41.79000 ? 121 SER B N   1 
ATOM   3079 C CA  . SER B 1 119 ? -0.46500  17.94800  -6.25700  1.000 43.07000 ? 121 SER B CA  1 
ATOM   3080 C C   . SER B 1 119 ? -0.37800  16.69700  -7.12600  1.000 40.88000 ? 121 SER B C   1 
ATOM   3081 O O   . SER B 1 119 ? 0.67600   16.45600  -7.74400  1.000 42.30000 ? 121 SER B O   1 
ATOM   3082 C CB  . SER B 1 119 ? -0.25900  19.19300  -7.10800  1.000 44.88000 ? 121 SER B CB  1 
ATOM   3083 O OG  . SER B 1 119 ? -0.65300  18.91700  -8.43100  1.000 50.53000 ? 121 SER B OG  1 
ATOM   3084 N N   . PRO B 1 120 ? -1.43000  15.87900  -7.19300  1.000 40.62000 ? 122 PRO B N   1 
ATOM   3085 C CA  . PRO B 1 120 ? -1.38400  14.67000  -8.03200  1.000 39.92000 ? 122 PRO B CA  1 
ATOM   3086 C C   . PRO B 1 120 ? -1.08500  14.97800  -9.49300  1.000 38.63000 ? 122 PRO B C   1 
ATOM   3087 O O   . PRO B 1 120 ? -1.65400  15.89000  -10.09700 1.000 39.66000 ? 122 PRO B O   1 
ATOM   3088 C CB  . PRO B 1 120 ? -2.78400  14.06000  -7.86500  1.000 36.89000 ? 122 PRO B CB  1 
ATOM   3089 C CG  . PRO B 1 120 ? -3.56900  15.04600  -7.05700  1.000 39.72000 ? 122 PRO B CG  1 
ATOM   3090 C CD  . PRO B 1 120 ? -2.61900  15.89500  -6.32000  1.000 38.56000 ? 122 PRO B CD  1 
ATOM   3091 N N   . SER B 1 121 ? -0.19200  14.17700  -10.06200 1.000 35.14000 ? 123 SER B N   1 
ATOM   3092 C CA  . SER B 1 121 ? 0.29500   14.35200  -11.42200 1.000 36.89000 ? 123 SER B CA  1 
ATOM   3093 C C   . SER B 1 121 ? -0.08100  13.20900  -12.34800 1.000 34.41000 ? 123 SER B C   1 
ATOM   3094 O O   . SER B 1 121 ? -0.41600  13.44800  -13.50600 1.000 32.54000 ? 123 SER B O   1 
ATOM   3095 C CB  . SER B 1 121 ? 1.82200   14.51500  -11.40300 1.000 37.82000 ? 123 SER B CB  1 
ATOM   3096 O OG  . SER B 1 121 ? 2.31700   14.78500  -12.70000 1.000 47.01000 ? 123 SER B OG  1 
ATOM   3097 N N   . GLY B 1 122 ? -0.03300  11.96700  -11.87500 1.000 33.55000 ? 124 GLY B N   1 
ATOM   3098 C CA  . GLY B 1 122 ? -0.41300  10.84100  -12.71300 1.000 29.33000 ? 124 GLY B CA  1 
ATOM   3099 C C   . GLY B 1 122 ? -0.52400  9.60400   -11.86400 1.000 33.32000 ? 124 GLY B C   1 
ATOM   3100 O O   . GLY B 1 122 ? -0.17700  9.60900   -10.67400 1.000 30.32000 ? 124 GLY B O   1 
ATOM   3101 N N   . VAL B 1 123 ? -1.01700  8.52800   -12.46900 1.000 29.57000 ? 125 VAL B N   1 
ATOM   3102 C CA  . VAL B 1 123 ? -1.23700  7.28600   -11.74200 1.000 30.07000 ? 125 VAL B CA  1 
ATOM   3103 C C   . VAL B 1 123 ? -0.76900  6.12700   -12.61800 1.000 34.09000 ? 125 VAL B C   1 
ATOM   3104 O O   . VAL B 1 123 ? -0.93200  6.14900   -13.84200 1.000 30.35000 ? 125 VAL B O   1 
ATOM   3105 C CB  . VAL B 1 123 ? -2.71700  7.15600   -11.29300 1.000 32.42000 ? 125 VAL B CB  1 
ATOM   3106 C CG1 . VAL B 1 123 ? -3.64400  7.09500   -12.48200 1.000 35.01000 ? 125 VAL B CG1 1 
ATOM   3107 C CG2 . VAL B 1 123 ? -2.92700  5.97100   -10.33300 1.000 28.43000 ? 125 VAL B CG2 1 
ATOM   3108 N N   . TYR B 1 124 ? -0.11500  5.13900   -12.00600 1.000 31.68000 ? 126 TYR B N   1 
ATOM   3109 C CA  . TYR B 1 124 ? 0.35500   4.01100   -12.79700 1.000 31.94000 ? 126 TYR B CA  1 
ATOM   3110 C C   . TYR B 1 124 ? 0.33800   2.76100   -11.93600 1.000 29.84000 ? 126 TYR B C   1 
ATOM   3111 O O   . TYR B 1 124 ? 0.32300   2.83100   -10.71100 1.000 29.87000 ? 126 TYR B O   1 
ATOM   3112 C CB  . TYR B 1 124 ? 1.75000   4.27900   -13.38000 1.000 34.42000 ? 126 TYR B CB  1 
ATOM   3113 C CG  . TYR B 1 124 ? 2.83300   4.56900   -12.35600 1.000 35.21000 ? 126 TYR B CG  1 
ATOM   3114 C CD1 . TYR B 1 124 ? 3.10000   5.86700   -11.93700 1.000 36.04000 ? 126 TYR B CD1 1 
ATOM   3115 C CD2 . TYR B 1 124 ? 3.61700   3.53800   -11.83900 1.000 40.58000 ? 126 TYR B CD2 1 
ATOM   3116 C CE1 . TYR B 1 124 ? 4.13600   6.12800   -10.99600 1.000 40.35000 ? 126 TYR B CE1 1 
ATOM   3117 C CE2 . TYR B 1 124 ? 4.64600   3.78900   -10.92000 1.000 42.69000 ? 126 TYR B CE2 1 
ATOM   3118 C CZ  . TYR B 1 124 ? 4.89500   5.07900   -10.49600 1.000 42.79000 ? 126 TYR B CZ  1 
ATOM   3119 O OH  . TYR B 1 124 ? 5.90700   5.29700   -9.57000  1.000 41.49000 ? 126 TYR B OH  1 
ATOM   3120 N N   . GLN B 1 125 ? 0.35200   1.61200   -12.59400 1.000 32.21000 ? 127 GLN B N   1 
ATOM   3121 C CA  . GLN B 1 125 ? 0.29900   0.32300   -11.92300 1.000 33.80000 ? 127 GLN B CA  1 
ATOM   3122 C C   . GLN B 1 125 ? 1.70400   -0.27200  -11.87500 1.000 35.70000 ? 127 GLN B C   1 
ATOM   3123 O O   . GLN B 1 125 ? 2.42700   -0.23300  -12.87500 1.000 35.68000 ? 127 GLN B O   1 
ATOM   3124 C CB  . GLN B 1 125 ? -0.68500  -0.60700  -12.65000 1.000 34.56000 ? 127 GLN B CB  1 
ATOM   3125 C CG  . GLN B 1 125 ? -0.87500  -1.98400  -12.01900 1.000 36.50000 ? 127 GLN B CG  1 
ATOM   3126 C CD  . GLN B 1 125 ? -1.85200  -2.02100  -10.84200 1.000 37.77000 ? 127 GLN B CD  1 
ATOM   3127 O OE1 . GLN B 1 125 ? -2.28800  -0.98300  -10.31700 1.000 35.86000 ? 127 GLN B OE1 1 
ATOM   3128 N NE2 . GLN B 1 125 ? -2.21700  -3.23500  -10.43000 1.000 36.48000 ? 127 GLN B NE2 1 
ATOM   3129 N N   . CYS B 1 126 ? 2.07700   -0.80900  -10.69500 1.000 29.35000 ? 128 CYS B N   1 
ATOM   3130 C CA  . CYS B 1 126 ? 3.42000   -1.25600  -10.31400 1.000 34.38000 ? 128 CYS B CA  1 
ATOM   3131 C C   . CYS B 1 126 ? 3.36600   -2.69300  -9.86500  1.000 35.29000 ? 128 CYS B C   1 
ATOM   3132 O O   . CYS B 1 126 ? 2.34000   -3.15500  -9.38500  1.000 32.64000 ? 128 CYS B O   1 
ATOM   3133 C CB  . CYS B 1 126 ? 3.98200   -0.57200  -9.02600  1.000 32.24000 ? 128 CYS B CB  1 
ATOM   3134 S SG  . CYS B 1 126 ? 4.34400   1.05200   -9.10700  1.000 52.30000 ? 128 CYS B SG  1 
ATOM   3135 N N   . ALA B 1 127 ? 4.53700   -3.32300  -9.81600  1.000 37.05000 ? 129 ALA B N   1 
ATOM   3136 C CA  . ALA B 1 127 ? 4.74000   -4.48000  -8.96100  1.000 35.03000 ? 129 ALA B CA  1 
ATOM   3137 C C   . ALA B 1 127 ? 5.91900   -4.22200  -8.02300  1.000 36.36000 ? 129 ALA B C   1 
ATOM   3138 O O   . ALA B 1 127 ? 6.88300   -3.53700  -8.37000  1.000 34.32000 ? 129 ALA B O   1 
ATOM   3139 C CB  . ALA B 1 127 ? 4.98300   -5.76200  -9.76800  1.000 36.02000 ? 129 ALA B CB  1 
ATOM   3140 N N   . MET B 1 128 ? 5.82100   -4.75800  -6.81700  1.000 32.61000 ? 130 MET B N   1 
ATOM   3141 C CA  . MET B 1 128 ? 6.99000   -4.84100  -5.95300  1.000 35.30000 ? 130 MET B CA  1 
ATOM   3142 C C   . MET B 1 128 ? 7.94100   -5.88100  -6.54100  1.000 33.42000 ? 130 MET B C   1 
ATOM   3143 O O   . MET B 1 128 ? 7.59100   -7.06300  -6.62400  1.000 31.56000 ? 130 MET B O   1 
ATOM   3144 C CB  . MET B 1 128 ? 6.55100   -5.20100  -4.53700  1.000 34.52000 ? 130 MET B CB  1 
ATOM   3145 C CG  . MET B 1 128 ? 7.67000   -5.40900  -3.51100  1.000 41.17000 ? 130 MET B CG  1 
ATOM   3146 S SD  . MET B 1 128 ? 8.45300   -3.88400  -2.97700  1.000 43.69000 ? 130 MET B SD  1 
ATOM   3147 C CE  . MET B 1 128 ? 7.13100   -3.03900  -2.13800  1.000 36.41000 ? 130 MET B CE  1 
ATOM   3148 N N   . ARG B 1 129 ? 9.11700   -5.43800  -7.00900  1.000 35.39000 ? 131 ARG B N   1 
ATOM   3149 C CA  . ARG B 1 129 ? 10.10100  -6.35400  -7.58600  1.000 34.24000 ? 131 ARG B CA  1 
ATOM   3150 C C   . ARG B 1 129 ? 10.62700  -7.29900  -6.50500  1.000 36.35000 ? 131 ARG B C   1 
ATOM   3151 O O   . ARG B 1 129 ? 10.54700  -7.00000  -5.30800  1.000 33.70000 ? 131 ARG B O   1 
ATOM   3152 C CB  . ARG B 1 129 ? 11.26600  -5.58800  -8.21800  1.000 34.51000 ? 131 ARG B CB  1 
ATOM   3153 C CG  . ARG B 1 129 ? 10.90900  -4.55200  -9.28500  1.000 38.06000 ? 131 ARG B CG  1 
ATOM   3154 C CD  . ARG B 1 129 ? 10.12300  -5.13600  -10.45300 1.000 36.73000 ? 131 ARG B CD  1 
ATOM   3155 N NE  . ARG B 1 129 ? 10.69400  -6.39800  -10.92600 1.000 38.53000 ? 131 ARG B NE  1 
ATOM   3156 C CZ  . ARG B 1 129 ? 10.10600  -7.17400  -11.82800 1.000 38.90000 ? 131 ARG B CZ  1 
ATOM   3157 N NH1 . ARG B 1 129 ? 8.94400   -6.79700  -12.35600 1.000 34.61000 ? 131 ARG B NH1 1 
ATOM   3158 N NH2 . ARG B 1 129 ? 10.67300  -8.31800  -12.20500 1.000 34.96000 ? 131 ARG B NH2 1 
ATOM   3159 N N   . PRO B 1 130 ? 11.13200  -8.47500  -6.90000  1.000 34.22000 ? 132 PRO B N   1 
ATOM   3160 C CA  . PRO B 1 130 ? 11.71600  -9.39300  -5.89800  1.000 34.92000 ? 132 PRO B CA  1 
ATOM   3161 C C   . PRO B 1 130 ? 12.89300  -8.79600  -5.13000  1.000 34.20000 ? 132 PRO B C   1 
ATOM   3162 O O   . PRO B 1 130 ? 13.15200  -9.21500  -3.99600  1.000 35.13000 ? 132 PRO B O   1 
ATOM   3163 C CB  . PRO B 1 130 ? 12.15100  -10.59800 -6.74300  1.000 41.39000 ? 132 PRO B CB  1 
ATOM   3164 C CG  . PRO B 1 130 ? 11.25300  -10.55000 -7.95100  1.000 40.85000 ? 132 PRO B CG  1 
ATOM   3165 C CD  . PRO B 1 130 ? 11.02900  -9.09200  -8.23200  1.000 36.44000 ? 132 PRO B CD  1 
ATOM   3166 N N   . ASN B 1 131 ? 13.59800  -7.81800  -5.68400  1.000 33.96000 ? 133 ASN B N   1 
ATOM   3167 C CA  . ASN B 1 131 ? 14.63700  -7.12500  -4.92600  1.000 37.36000 ? 133 ASN B CA  1 
ATOM   3168 C C   . ASN B 1 131 ? 14.09000  -5.94600  -4.13300  1.000 37.45000 ? 133 ASN B C   1 
ATOM   3169 O O   . ASN B 1 131 ? 14.87000  -5.07900  -3.71800  1.000 35.02000 ? 133 ASN B O   1 
ATOM   3170 C CB  . ASN B 1 131 ? 15.76400  -6.65800  -5.85500  1.000 35.15000 ? 133 ASN B CB  1 
ATOM   3171 C CG  . ASN B 1 131 ? 15.33200  -5.56200  -6.81000  1.000 38.85000 ? 133 ASN B CG  1 
ATOM   3172 O OD1 . ASN B 1 131 ? 14.17500  -5.13700  -6.81800  1.000 35.90000 ? 133 ASN B OD1 1 
ATOM   3173 N ND2 . ASN B 1 131 ? 16.26900  -5.09500  -7.62700  1.000 40.61000 ? 133 ASN B ND2 1 
ATOM   3174 N N   . PHE B 1 132 ? 12.76600  -5.87600  -3.96700  1.000 33.99000 ? 134 PHE B N   1 
ATOM   3175 C CA  . PHE B 1 132 ? 12.06800  -4.93800  -3.09600  1.000 33.99000 ? 134 PHE B CA  1 
ATOM   3176 C C   . PHE B 1 132 ? 12.06800  -3.50600  -3.60500  1.000 37.77000 ? 134 PHE B C   1 
ATOM   3177 O O   . PHE B 1 132 ? 11.71000  -2.59000  -2.85800  1.000 41.31000 ? 134 PHE B O   1 
ATOM   3178 C CB  . PHE B 1 132 ? 12.62900  -4.97800  -1.67000  1.000 32.49000 ? 134 PHE B CB  1 
ATOM   3179 C CG  . PHE B 1 132 ? 12.25100  -6.22400  -0.91600  1.000 33.25000 ? 134 PHE B CG  1 
ATOM   3180 C CD1 . PHE B 1 132 ? 10.96400  -6.38100  -0.43600  1.000 37.58000 ? 134 PHE B CD1 1 
ATOM   3181 C CD2 . PHE B 1 132 ? 13.16600  -7.24700  -0.72100  1.000 37.54000 ? 134 PHE B CD2 1 
ATOM   3182 C CE1 . PHE B 1 132 ? 10.59300  -7.51800  0.24300   1.000 38.37000 ? 134 PHE B CE1 1 
ATOM   3183 C CE2 . PHE B 1 132 ? 12.80000  -8.40300  -0.04100  1.000 38.78000 ? 134 PHE B CE2 1 
ATOM   3184 C CZ  . PHE B 1 132 ? 11.50300  -8.53200  0.44500   1.000 40.36000 ? 134 PHE B CZ  1 
ATOM   3185 N N   . THR B 1 133 ? 12.45300  -3.26500  -4.84900  1.000 32.17000 ? 135 THR B N   1 
ATOM   3186 C CA  . THR B 1 133 ? 12.33900  -1.93200  -5.41600  1.000 31.28000 ? 135 THR B CA  1 
ATOM   3187 C C   . THR B 1 133 ? 11.11400  -1.86600  -6.32200  1.000 38.46000 ? 135 THR B C   1 
ATOM   3188 O O   . THR B 1 133 ? 10.45900  -2.87300  -6.60700  1.000 35.99000 ? 135 THR B O   1 
ATOM   3189 C CB  . THR B 1 133 ? 13.59200  -1.55600  -6.20700  1.000 36.68000 ? 135 THR B CB  1 
ATOM   3190 O OG1 . THR B 1 133 ? 13.62500  -2.32600  -7.41300  1.000 34.25000 ? 135 THR B OG1 1 
ATOM   3191 C CG2 . THR B 1 133 ? 14.87400  -1.82000  -5.36400  1.000 35.59000 ? 135 THR B CG2 1 
ATOM   3192 N N   . ILE B 1 134 ? 10.80700  -0.65000  -6.76800  1.000 37.15000 ? 136 ILE B N   1 
ATOM   3193 C CA  . ILE B 1 134 ? 9.70500   -0.37000  -7.67700  1.000 36.97000 ? 136 ILE B CA  1 
ATOM   3194 C C   . ILE B 1 134 ? 10.30100  0.23100   -8.93900  1.000 41.80000 ? 136 ILE B C   1 
ATOM   3195 O O   . ILE B 1 134 ? 11.02100  1.23400   -8.86800  1.000 40.51000 ? 136 ILE B O   1 
ATOM   3196 C CB  . ILE B 1 134 ? 8.68500   0.59900   -7.06000  1.000 39.55000 ? 136 ILE B CB  1 
ATOM   3197 C CG1 . ILE B 1 134 ? 8.05500   -0.01000  -5.81300  1.000 42.20000 ? 136 ILE B CG1 1 
ATOM   3198 C CG2 . ILE B 1 134 ? 7.60800   0.91700   -8.06600  1.000 43.17000 ? 136 ILE B CG2 1 
ATOM   3199 C CD1 . ILE B 1 134 ? 7.39600   -1.33600  -6.07000  1.000 40.96000 ? 136 ILE B CD1 1 
ATOM   3200 N N   . LYS B 1 135 ? 10.01800  -0.37300  -10.08500 1.000 39.69000 ? 137 LYS B N   1 
ATOM   3201 C CA  . LYS B 1 135 ? 10.35700  0.25200   -11.36100 1.000 48.78000 ? 137 LYS B CA  1 
ATOM   3202 C C   . LYS B 1 135 ? 9.25800   1.26800   -11.63000 1.000 46.78000 ? 137 LYS B C   1 
ATOM   3203 O O   . LYS B 1 135 ? 8.18300   0.94500   -12.13100 1.000 54.69000 ? 137 LYS B O   1 
ATOM   3204 C CB  . LYS B 1 135 ? 10.47000  -0.78400  -12.47200 1.000 43.02000 ? 137 LYS B CB  1 
ATOM   3205 N N   . GLY B 1 136 ? 9.51600   2.52100   -11.23600 1.000 49.50000 ? 138 GLY B N   1 
ATOM   3206 C CA  . GLY B 1 136 ? 8.54800   3.58400   -11.37000 1.000 53.12000 ? 138 GLY B CA  1 
ATOM   3207 C C   . GLY B 1 136 ? 9.14800   4.76500   -12.10800 1.000 58.37000 ? 138 GLY B C   1 
ATOM   3208 O O   . GLY B 1 136 ? 10.34800  4.80300   -12.41500 1.000 62.34000 ? 138 GLY B O   1 
ATOM   3209 N N   . SER B 1 137 ? 8.30800   5.75900   -12.29600 1.000 62.11000 ? 139 SER B N   1 
ATOM   3210 C CA  . SER B 1 137 ? 8.74800   6.99500   -12.87400 1.000 63.11000 ? 139 SER B CA  1 
ATOM   3211 C C   . SER B 1 137 ? 8.39500   8.05200   -11.91600 1.000 68.10000 ? 139 SER B C   1 
ATOM   3212 O O   . SER B 1 137 ? 7.25100   8.48400   -11.81500 1.000 64.08000 ? 139 SER B O   1 
ATOM   3213 C CB  . SER B 1 137 ? 8.02500   7.29800   -14.11700 1.000 69.04000 ? 139 SER B CB  1 
ATOM   3214 O OG  . SER B 1 137 ? 8.44900   8.53900   -14.60700 1.000 73.77000 ? 139 SER B OG  1 
ATOM   3215 N N   . PHE B 1 138 ? 9.40200   8.48900   -11.20700 1.000 69.97000 ? 140 PHE B N   1 
ATOM   3216 C CA  . PHE B 1 138 ? 9.18100   9.51000   -10.25000 1.000 66.95000 ? 140 PHE B CA  1 
ATOM   3217 C C   . PHE B 1 138 ? 9.86200   10.74400  -10.68700 1.000 73.98000 ? 140 PHE B C   1 
ATOM   3218 O O   . PHE B 1 138 ? 11.00000  10.74800  -11.08900 1.000 78.11000 ? 140 PHE B O   1 
ATOM   3219 C CB  . PHE B 1 138 ? 9.52400   9.07900   -8.87600  1.000 62.95000 ? 140 PHE B CB  1 
ATOM   3220 C CG  . PHE B 1 138 ? 8.47800   8.26200   -8.27800  1.000 60.01000 ? 140 PHE B CG  1 
ATOM   3221 C CD1 . PHE B 1 138 ? 7.18100   8.63800   -8.40200  1.000 56.50000 ? 140 PHE B CD1 1 
ATOM   3222 C CD2 . PHE B 1 138 ? 8.77700   7.09700   -7.67700  1.000 55.75000 ? 140 PHE B CD2 1 
ATOM   3223 C CE1 . PHE B 1 138 ? 6.20800   7.91100   -7.86400  1.000 51.58000 ? 140 PHE B CE1 1 
ATOM   3224 C CE2 . PHE B 1 138 ? 7.79300   6.34700   -7.11800  1.000 54.69000 ? 140 PHE B CE2 1 
ATOM   3225 C CZ  . PHE B 1 138 ? 6.51500   6.77300   -7.19900  1.000 54.61000 ? 140 PHE B CZ  1 
ATOM   3226 N N   . LEU B 1 139 ? 9.08200   11.78800  -10.66600 1.000 73.46000 ? 141 LEU B N   1 
ATOM   3227 C CA  . LEU B 1 139 ? 9.45400   13.06900  -11.08800 1.000 71.70000 ? 141 LEU B CA  1 
ATOM   3228 C C   . LEU B 1 139 ? 10.15900  13.72100  -9.95900  1.000 69.45000 ? 141 LEU B C   1 
ATOM   3229 O O   . LEU B 1 139 ? 10.33100  13.17100  -8.92300  1.000 66.94000 ? 141 LEU B O   1 
ATOM   3230 C CB  . LEU B 1 139 ? 8.14900   13.77500  -11.38100 1.000 69.34000 ? 141 LEU B CB  1 
ATOM   3231 C CG  . LEU B 1 139 ? 7.00600   13.59900  -10.37400 1.000 61.71000 ? 141 LEU B CG  1 
ATOM   3232 C CD1 . LEU B 1 139 ? 6.74000   14.84200  -9.58400  1.000 61.30000 ? 141 LEU B CD1 1 
ATOM   3233 C CD2 . LEU B 1 139 ? 5.71300   13.25600  -11.04000 1.000 53.69000 ? 141 LEU B CD2 1 
ATOM   3234 N N   . ALA B 1 140 ? 10.56500  14.94900  -10.16400 1.000 73.53000 ? 142 ALA B N   1 
ATOM   3235 C CA  . ALA B 1 140 ? 11.19300  15.71500  -9.13700  1.000 73.41000 ? 142 ALA B CA  1 
ATOM   3236 C C   . ALA B 1 140 ? 10.10700  15.85800  -8.10500  1.000 75.27000 ? 142 ALA B C   1 
ATOM   3237 O O   . ALA B 1 140 ? 8.95100   15.86500  -8.43300  1.000 82.62000 ? 142 ALA B O   1 
ATOM   3238 C CB  . ALA B 1 140 ? 11.57200  17.07300  -9.67700  1.000 71.75000 ? 142 ALA B CB  1 
ATOM   3239 N N   . GLY B 1 141 ? 10.48100  15.90600  -6.86100  1.000 68.24000 ? 143 GLY B N   1 
ATOM   3240 C CA  . GLY B 1 141 ? 9.53000   16.06600  -5.80000  1.000 61.73000 ? 143 GLY B CA  1 
ATOM   3241 C C   . GLY B 1 141 ? 8.41100   15.08800  -5.67300  1.000 54.97000 ? 143 GLY B C   1 
ATOM   3242 O O   . GLY B 1 141 ? 7.35000   15.50000  -5.33700  1.000 51.99000 ? 143 GLY B O   1 
ATOM   3243 N N   . SER B 1 142 ? 8.63900   13.82000  -5.93000  1.000 51.95000 ? 144 SER B N   1 
ATOM   3244 C CA  . SER B 1 142 ? 7.57500   12.84500  -5.77100  1.000 46.98000 ? 144 SER B CA  1 
ATOM   3245 C C   . SER B 1 142 ? 7.63000   12.06900  -4.47400  1.000 40.67000 ? 144 SER B C   1 
ATOM   3246 O O   . SER B 1 142 ? 6.82400   11.26400  -4.23700  1.000 37.33000 ? 144 SER B O   1 
ATOM   3247 C CB  . SER B 1 142 ? 7.46500   11.94300  -6.97700  1.000 51.61000 ? 144 SER B CB  1 
ATOM   3248 O OG  . SER B 1 142 ? 8.55800   11.10200  -7.07900  1.000 56.74000 ? 144 SER B OG  1 
ATOM   3249 N N   . CYS B 1 143 ? 8.60300   12.37000  -3.64200  1.000 42.04000 ? 145 CYS B N   1 
ATOM   3250 C CA  . CYS B 1 143 ? 8.80200   11.75600  -2.35000  1.000 37.57000 ? 145 CYS B CA  1 
ATOM   3251 C C   . CYS B 1 143 ? 7.58700   11.88900  -1.53000  1.000 29.28000 ? 145 CYS B C   1 
ATOM   3252 O O   . CYS B 1 143 ? 7.02300   12.89800  -1.49800  1.000 33.54000 ? 145 CYS B O   1 
ATOM   3253 C CB  . CYS B 1 143 ? 9.83200   12.52300  -1.59900  1.000 42.33000 ? 145 CYS B CB  1 
ATOM   3254 S SG  . CYS B 1 143 ? 11.31000  11.68600  -1.31600  1.000 68.52000 ? 145 CYS B SG  1 
ATOM   3255 N N   . GLY B 1 144 ? 7.21800   10.82900  -0.84700  1.000 33.24000 ? 146 GLY B N   1 
ATOM   3256 C CA  . GLY B 1 144 ? 5.97400   10.87800  -0.10700  1.000 32.47000 ? 146 GLY B CA  1 
ATOM   3257 C C   . GLY B 1 144 ? 4.73900   10.42900  -0.87000  1.000 32.92000 ? 146 GLY B C   1 
ATOM   3258 O O   . GLY B 1 144 ? 3.68600   10.26000  -0.24400  1.000 30.26000 ? 146 GLY B O   1 
ATOM   3259 N N   . SER B 1 145 ? 4.82800   10.24800  -2.19400  1.000 33.40000 ? 147 SER B N   1 
ATOM   3260 C CA  . SER B 1 145 ? 3.73900   9.65700   -2.97700  1.000 30.44000 ? 147 SER B CA  1 
ATOM   3261 C C   . SER B 1 145 ? 3.44200   8.24900   -2.47700  1.000 31.49000 ? 147 SER B C   1 
ATOM   3262 O O   . SER B 1 145 ? 4.33400   7.53900   -1.99800  1.000 28.60000 ? 147 SER B O   1 
ATOM   3263 C CB  . SER B 1 145 ? 4.10600   9.58400   -4.46900  1.000 34.77000 ? 147 SER B CB  1 
ATOM   3264 O OG  . SER B 1 145 ? 4.29100   10.86300  -5.05500  1.000 38.22000 ? 147 SER B OG  1 
ATOM   3265 N N   . VAL B 1 146 ? 2.18700   7.81800   -2.62300  1.000 27.62000 ? 148 VAL B N   1 
ATOM   3266 C CA  . VAL B 1 146 ? 1.78600   6.55600   -2.01600  1.000 28.15000 ? 148 VAL B CA  1 
ATOM   3267 C C   . VAL B 1 146 ? 1.28500   5.57200   -3.05900  1.000 29.41000 ? 148 VAL B C   1 
ATOM   3268 O O   . VAL B 1 146 ? 0.73800   5.93900   -4.11400  1.000 27.75000 ? 148 VAL B O   1 
ATOM   3269 C CB  . VAL B 1 146 ? 0.71100   6.74100   -0.92000  1.000 30.62000 ? 148 VAL B CB  1 
ATOM   3270 C CG1 . VAL B 1 146 ? 1.29100   7.52200   0.28600   1.000 30.88000 ? 148 VAL B CG1 1 
ATOM   3271 C CG2 . VAL B 1 146 ? -0.51500  7.39700   -1.49700  1.000 29.82000 ? 148 VAL B CG2 1 
ATOM   3272 N N   . GLY B 1 147 ? 1.44600   4.29300   -2.72500  1.000 28.66000 ? 149 GLY B N   1 
ATOM   3273 C CA  . GLY B 1 147 ? 0.88600   3.19400   -3.47900  1.000 26.40000 ? 149 GLY B CA  1 
ATOM   3274 C C   . GLY B 1 147 ? -0.27200  2.57300   -2.70800  1.000 28.28000 ? 149 GLY B C   1 
ATOM   3275 O O   . GLY B 1 147 ? -0.32000  2.64300   -1.47200  1.000 28.05000 ? 149 GLY B O   1 
ATOM   3276 N N   . PHE B 1 148 ? -1.20100  1.96200   -3.44500  1.000 26.36000 ? 150 PHE B N   1 
ATOM   3277 C CA  . PHE B 1 148 ? -2.45500  1.51600   -2.84400  1.000 27.25000 ? 150 PHE B CA  1 
ATOM   3278 C C   . PHE B 1 148 ? -3.14400  0.51500   -3.76100  1.000 29.32000 ? 150 PHE B C   1 
ATOM   3279 O O   . PHE B 1 148 ? -2.91400  0.49300   -4.96600  1.000 26.96000 ? 150 PHE B O   1 
ATOM   3280 C CB  . PHE B 1 148 ? -3.41100  2.69100   -2.58900  1.000 26.03000 ? 150 PHE B CB  1 
ATOM   3281 C CG  . PHE B 1 148 ? -3.75100  3.45900   -3.82900  1.000 26.36000 ? 150 PHE B CG  1 
ATOM   3282 C CD1 . PHE B 1 148 ? -2.86600  4.40700   -4.33900  1.000 28.85000 ? 150 PHE B CD1 1 
ATOM   3283 C CD2 . PHE B 1 148 ? -4.93900  3.22000   -4.50800  1.000 30.10000 ? 150 PHE B CD2 1 
ATOM   3284 C CE1 . PHE B 1 148 ? -3.16100  5.11300   -5.50600  1.000 29.57000 ? 150 PHE B CE1 1 
ATOM   3285 C CE2 . PHE B 1 148 ? -5.24800  3.92500   -5.67300  1.000 28.75000 ? 150 PHE B CE2 1 
ATOM   3286 C CZ  . PHE B 1 148 ? -4.36000  4.86300   -6.17800  1.000 28.63000 ? 150 PHE B CZ  1 
ATOM   3287 N N   . ASN B 1 149 ? -3.98600  -0.31400  -3.16000  1.000 28.22000 ? 151 ASN B N   1 
ATOM   3288 C CA  . ASN B 1 149 ? -5.00900  -1.05500  -3.87700  1.000 28.03000 ? 151 ASN B CA  1 
ATOM   3289 C C   . ASN B 1 149 ? -6.35300  -0.58600  -3.36800  1.000 30.51000 ? 151 ASN B C   1 
ATOM   3290 O O   . ASN B 1 149 ? -6.46300  -0.05600  -2.26100  1.000 32.44000 ? 151 ASN B O   1 
ATOM   3291 C CB  . ASN B 1 149 ? -4.86800  -2.56400  -3.68400  1.000 27.27000 ? 151 ASN B CB  1 
ATOM   3292 C CG  . ASN B 1 149 ? -3.66100  -3.12100  -4.41500  1.000 31.80000 ? 151 ASN B CG  1 
ATOM   3293 O OD1 . ASN B 1 149 ? -3.73900  -3.42000  -5.59600  1.000 35.23000 ? 151 ASN B OD1 1 
ATOM   3294 N ND2 . ASN B 1 149 ? -2.53200  -3.22400  -3.72300  1.000 30.03000 ? 151 ASN B ND2 1 
ATOM   3295 N N   . ILE B 1 150 ? -7.38200  -0.77500  -4.18200  1.000 33.92000 ? 152 ILE B N   1 
ATOM   3296 C CA  . ILE B 1 150 ? -8.74900  -0.44200  -3.80100  1.000 35.79000 ? 152 ILE B CA  1 
ATOM   3297 C C   . ILE B 1 150 ? -9.57600  -1.70800  -3.92000  1.000 42.11000 ? 152 ILE B C   1 
ATOM   3298 O O   . ILE B 1 150 ? -9.55200  -2.37000  -4.96400  1.000 44.00000 ? 152 ILE B O   1 
ATOM   3299 C CB  . ILE B 1 150 ? -9.33900  0.67700   -4.68100  1.000 38.58000 ? 152 ILE B CB  1 
ATOM   3300 C CG1 . ILE B 1 150 ? -8.55900  1.98100   -4.47400  1.000 36.19000 ? 152 ILE B CG1 1 
ATOM   3301 C CG2 . ILE B 1 150 ? -10.83600 0.85100   -4.38800  1.000 39.44000 ? 152 ILE B CG2 1 
ATOM   3302 C CD1 . ILE B 1 150 ? -9.22200  3.20900   -5.01400  1.000 40.37000 ? 152 ILE B CD1 1 
ATOM   3303 N N   . ASP B 1 151 ? -10.25600 -2.02400  -2.87300  1.000 44.11000 ? 153 ASP B N   1 
ATOM   3304 C CA  . ASP B 1 151 ? -11.10100 -3.13000  -2.89000  1.000 50.92000 ? 153 ASP B CA  1 
ATOM   3305 C C   . ASP B 1 151 ? -12.41500 -2.77300  -2.26200  1.000 54.72000 ? 153 ASP B C   1 
ATOM   3306 O O   . ASP B 1 151 ? -12.48100 -2.55700  -1.09800  1.000 58.53000 ? 153 ASP B O   1 
ATOM   3307 C CB  . ASP B 1 151 ? -10.43400 -4.25100  -2.17600  1.000 54.89000 ? 153 ASP B CB  1 
ATOM   3308 C CG  . ASP B 1 151 ? -10.19200 -3.97600  -0.71500  1.000 60.48000 ? 153 ASP B CG  1 
ATOM   3309 O OD1 . ASP B 1 151 ? -9.17400  -3.38300  -0.30200  1.000 58.13000 ? 153 ASP B OD1 1 
ATOM   3310 O OD2 . ASP B 1 151 ? -11.01600 -4.45800  0.06000   1.000 69.95000 ? 153 ASP B OD2 1 
ATOM   3311 N N   . TYR B 1 152 ? -13.47800 -2.75500  -3.03600  1.000 58.50000 ? 154 TYR B N   1 
ATOM   3312 C CA  . TYR B 1 152 ? -14.78900 -2.44500  -2.50000  1.000 61.25000 ? 154 TYR B CA  1 
ATOM   3313 C C   . TYR B 1 152 ? -14.96700 -1.07600  -1.88400  1.000 60.81000 ? 154 TYR B C   1 
ATOM   3314 O O   . TYR B 1 152 ? -15.55100 -0.93700  -0.85400  1.000 64.80000 ? 154 TYR B O   1 
ATOM   3315 C CB  . TYR B 1 152 ? -15.11700 -3.51900  -1.44700  1.000 65.53000 ? 154 TYR B CB  1 
ATOM   3316 N N   . ASP B 1 153 ? -14.42500 -0.05600  -2.50100  1.000 61.89000 ? 155 ASP B N   1 
ATOM   3317 C CA  . ASP B 1 153 ? -14.52700 1.30300   -1.95800  1.000 61.32000 ? 155 ASP B CA  1 
ATOM   3318 C C   . ASP B 1 153 ? -13.61900 1.50400   -0.73800  1.000 53.47000 ? 155 ASP B C   1 
ATOM   3319 O O   . ASP B 1 153 ? -13.66300 2.51900   -0.13400  1.000 52.60000 ? 155 ASP B O   1 
ATOM   3320 C CB  . ASP B 1 153 ? -15.96900 1.73000   -1.64700  1.000 63.13000 ? 155 ASP B CB  1 
ATOM   3321 C CG  . ASP B 1 153 ? -16.80100 2.03300   -2.90500  1.000 69.12000 ? 155 ASP B CG  1 
ATOM   3322 O OD1 . ASP B 1 153 ? -16.30200 2.69500   -3.82200  1.000 62.51000 ? 155 ASP B OD1 1 
ATOM   3323 O OD2 . ASP B 1 153 ? -17.97900 1.63300   -2.95800  1.000 70.39000 ? 155 ASP B OD2 1 
ATOM   3324 N N   . CYS B 1 154 ? -12.79100 0.53300   -0.41500  1.000 48.27000 ? 156 CYS B N   1 
ATOM   3325 C CA  . CYS B 1 154 ? -11.85000 0.61500   0.68000   1.000 43.48000 ? 156 CYS B CA  1 
ATOM   3326 C C   . CYS B 1 154 ? -10.40900 0.67700   0.14000   1.000 37.28000 ? 156 CYS B C   1 
ATOM   3327 O O   . CYS B 1 154 ? -10.02900 -0.13300  -0.59400  1.000 36.69000 ? 156 CYS B O   1 
ATOM   3328 C CB  . CYS B 1 154 ? -12.06500 -0.56200  1.60100   1.000 49.66000 ? 156 CYS B CB  1 
ATOM   3329 S SG  . CYS B 1 154 ? -10.80200 -1.00700  2.80200   1.000 57.30000 ? 156 CYS B SG  1 
ATOM   3330 N N   . VAL B 1 155 ? -9.66100  1.68100   0.52400   1.000 34.01000 ? 157 VAL B N   1 
ATOM   3331 C CA  . VAL B 1 155 ? -8.28400  1.90100   0.07800   1.000 33.25000 ? 157 VAL B CA  1 
ATOM   3332 C C   . VAL B 1 155 ? -7.31300  1.16100   0.99900   1.000 31.19000 ? 157 VAL B C   1 
ATOM   3333 O O   . VAL B 1 155 ? -7.28000  1.40900   2.20500   1.000 31.00000 ? 157 VAL B O   1 
ATOM   3334 C CB  . VAL B 1 155 ? -7.94600  3.40000   0.04600   1.000 31.95000 ? 157 VAL B CB  1 
ATOM   3335 C CG1 . VAL B 1 155 ? -6.54500  3.63100   -0.60500  1.000 26.94000 ? 157 VAL B CG1 1 
ATOM   3336 C CG2 . VAL B 1 155 ? -9.04600  4.17500   -0.68600  1.000 34.94000 ? 157 VAL B CG2 1 
ATOM   3337 N N   . SER B 1 156 ? -6.48600  0.29300   0.43000   1.000 30.62000 ? 158 SER B N   1 
ATOM   3338 C CA  . SER B 1 156 ? -5.38900  -0.35000  1.15500   1.000 28.84000 ? 158 SER B CA  1 
ATOM   3339 C C   . SER B 1 156 ? -4.07600  0.33300   0.78000   1.000 26.55000 ? 158 SER B C   1 
ATOM   3340 O O   . SER B 1 156 ? -3.52400  0.08200   -0.28700  1.000 29.11000 ? 158 SER B O   1 
ATOM   3341 C CB  . SER B 1 156 ? -5.34400  -1.84200  0.83900   1.000 32.37000 ? 158 SER B CB  1 
ATOM   3342 O OG  . SER B 1 156 ? -6.33300  -2.53800  1.57900   1.000 38.82000 ? 158 SER B OG  1 
ATOM   3343 N N   . PHE B 1 157 ? -3.56500  1.17900   1.67300   1.000 28.78000 ? 159 PHE B N   1 
ATOM   3344 C CA  . PHE B 1 157 ? -2.28400  1.85300   1.45500   1.000 27.53000 ? 159 PHE B CA  1 
ATOM   3345 C C   . PHE B 1 157 ? -1.14100  0.89400   1.79100   1.000 26.52000 ? 159 PHE B C   1 
ATOM   3346 O O   . PHE B 1 157 ? -1.06500  0.38000   2.91400   1.000 28.65000 ? 159 PHE B O   1 
ATOM   3347 C CB  . PHE B 1 157 ? -2.19000  3.11200   2.32300   1.000 27.78000 ? 159 PHE B CB  1 
ATOM   3348 C CG  . PHE B 1 157 ? -3.11900  4.23700   1.90300   1.000 26.36000 ? 159 PHE B CG  1 
ATOM   3349 C CD1 . PHE B 1 157 ? -2.85700  5.00000   0.76500   1.000 24.64000 ? 159 PHE B CD1 1 
ATOM   3350 C CD2 . PHE B 1 157 ? -4.23100  4.54600   2.66000   1.000 26.62000 ? 159 PHE B CD2 1 
ATOM   3351 C CE1 . PHE B 1 157 ? -3.70000  6.04200   0.38900   1.000 25.06000 ? 159 PHE B CE1 1 
ATOM   3352 C CE2 . PHE B 1 157 ? -5.09600  5.58700   2.28000   1.000 27.73000 ? 159 PHE B CE2 1 
ATOM   3353 C CZ  . PHE B 1 157 ? -4.82000  6.33600   1.15600   1.000 22.47000 ? 159 PHE B CZ  1 
ATOM   3354 N N   . CYS B 1 158 ? -0.24800  0.66000   0.82600   1.000 25.67000 ? 160 CYS B N   1 
ATOM   3355 C CA  . CYS B 1 158 ? 0.82100   -0.32100  0.96700   1.000 26.75000 ? 160 CYS B CA  1 
ATOM   3356 C C   . CYS B 1 158 ? 2.21800   0.25800   0.79200   1.000 28.47000 ? 160 CYS B C   1 
ATOM   3357 O O   . CYS B 1 158 ? 3.20300   -0.41100  1.14800   1.000 29.71000 ? 160 CYS B O   1 
ATOM   3358 C CB  . CYS B 1 158 ? 0.62800   -1.47800  -0.03500  1.000 27.19000 ? 160 CYS B CB  1 
ATOM   3359 S SG  . CYS B 1 158 ? 0.66300   -1.01400  -1.81000  1.000 29.44000 ? 160 CYS B SG  1 
ATOM   3360 N N   . TYR B 1 159 ? 2.35100   1.48700   0.30600   1.000 27.41000 ? 161 TYR B N   1 
ATOM   3361 C CA  . TYR B 1 159 ? 3.67000   1.96600   -0.06200  1.000 27.02000 ? 161 TYR B CA  1 
ATOM   3362 C C   . TYR B 1 159 ? 3.73700   3.47400   0.07500   1.000 26.52000 ? 161 TYR B C   1 
ATOM   3363 O O   . TYR B 1 159 ? 2.79200   4.17100   -0.28700  1.000 28.45000 ? 161 TYR B O   1 
ATOM   3364 C CB  . TYR B 1 159 ? 4.00100   1.56500   -1.50500  1.000 26.31000 ? 161 TYR B CB  1 
ATOM   3365 C CG  . TYR B 1 159 ? 5.34300   2.04600   -2.02200  1.000 29.84000 ? 161 TYR B CG  1 
ATOM   3366 C CD1 . TYR B 1 159 ? 6.50400   1.31600   -1.78000  1.000 26.53000 ? 161 TYR B CD1 1 
ATOM   3367 C CD2 . TYR B 1 159 ? 5.44900   3.21200   -2.77600  1.000 30.21000 ? 161 TYR B CD2 1 
ATOM   3368 C CE1 . TYR B 1 159 ? 7.72900   1.73700   -2.26700  1.000 30.32000 ? 161 TYR B CE1 1 
ATOM   3369 C CE2 . TYR B 1 159 ? 6.69400   3.63600   -3.28700  1.000 29.42000 ? 161 TYR B CE2 1 
ATOM   3370 C CZ  . TYR B 1 159 ? 7.82000   2.89500   -3.02400  1.000 30.26000 ? 161 TYR B CZ  1 
ATOM   3371 O OH  . TYR B 1 159 ? 9.06600   3.29800   -3.49600  1.000 33.59000 ? 161 TYR B OH  1 
ATOM   3372 N N   . MET B 1 160 ? 4.86400   3.97400   0.56300   1.000 27.45000 ? 162 MET B N   1 
ATOM   3373 C CA  . MET B 1 160 ? 5.16500   5.39700   0.49100   1.000 27.65000 ? 162 MET B CA  1 
ATOM   3374 C C   . MET B 1 160 ? 6.55900   5.56500   -0.09200  1.000 29.20000 ? 162 MET B C   1 
ATOM   3375 O O   . MET B 1 160 ? 7.50500   4.92800   0.37700   1.000 29.51000 ? 162 MET B O   1 
ATOM   3376 C CB  . MET B 1 160 ? 5.09900   6.07500   1.86400   1.000 28.53000 ? 162 MET B CB  1 
ATOM   3377 C CG  . MET B 1 160 ? 5.59800   7.52200   1.83800   1.000 29.71000 ? 162 MET B CG  1 
ATOM   3378 S SD  . MET B 1 160 ? 5.31300   8.35100   3.41300   1.000 38.30000 ? 162 MET B SD  1 
ATOM   3379 C CE  . MET B 1 160 ? 3.54800   8.68200   3.28600   1.000 34.96000 ? 162 MET B CE  1 
ATOM   3380 N N   . HIS B 1 161 ? 6.68300   6.44300   -1.08000  1.000 25.94000 ? 163 HIS B N   1 
ATOM   3381 C CA  . HIS B 1 161 ? 7.93600   6.59900   -1.79200  1.000 32.26000 ? 163 HIS B CA  1 
ATOM   3382 C C   . HIS B 1 161 ? 8.92700   7.41200   -0.96400  1.000 33.45000 ? 163 HIS B C   1 
ATOM   3383 O O   . HIS B 1 161 ? 8.58400   8.48000   -0.43600  1.000 29.45000 ? 163 HIS B O   1 
ATOM   3384 C CB  . HIS B 1 161 ? 7.70000   7.27600   -3.14200  1.000 31.35000 ? 163 HIS B CB  1 
ATOM   3385 C CG  . HIS B 1 161 ? 8.95400   7.46400   -3.93500  1.000 39.21000 ? 163 HIS B CG  1 
ATOM   3386 N ND1 . HIS B 1 161 ? 9.37800   8.69700   -4.38600  1.000 44.76000 ? 163 HIS B ND1 1 
ATOM   3387 C CD2 . HIS B 1 161 ? 9.89200   6.57400   -4.33900  1.000 41.48000 ? 163 HIS B CD2 1 
ATOM   3388 C CE1 . HIS B 1 161 ? 10.52000  8.55800   -5.03500  1.000 42.03000 ? 163 HIS B CE1 1 
ATOM   3389 N NE2 . HIS B 1 161 ? 10.85500  7.28100   -5.02100  1.000 43.03000 ? 163 HIS B NE2 1 
ATOM   3390 N N   . HIS B 1 162 ? 10.16900  6.92400   -0.88300  1.000 31.52000 ? 164 HIS B N   1 
ATOM   3391 C CA  . HIS B 1 162 ? 11.22400  7.65900   -0.18700  1.000 37.16000 ? 164 HIS B CA  1 
ATOM   3392 C C   . HIS B 1 162 ? 12.38000  8.06700   -1.09500  1.000 39.34000 ? 164 HIS B C   1 
ATOM   3393 O O   . HIS B 1 162 ? 12.84200  9.21000   -1.00800  1.000 42.07000 ? 164 HIS B O   1 
ATOM   3394 C CB  . HIS B 1 162 ? 11.77100  6.83800   1.00400   1.000 31.66000 ? 164 HIS B CB  1 
ATOM   3395 C CG  . HIS B 1 162 ? 10.83300  6.74900   2.16300   1.000 31.71000 ? 164 HIS B CG  1 
ATOM   3396 N ND1 . HIS B 1 162 ? 11.13500  7.25300   3.41400   1.000 31.85000 ? 164 HIS B ND1 1 
ATOM   3397 C CD2 . HIS B 1 162 ? 9.59100   6.21300   2.26900   1.000 31.26000 ? 164 HIS B CD2 1 
ATOM   3398 C CE1 . HIS B 1 162 ? 10.12400  7.02800   4.23300   1.000 34.26000 ? 164 HIS B CE1 1 
ATOM   3399 N NE2 . HIS B 1 162 ? 9.17300   6.39300   3.56400   1.000 32.38000 ? 164 HIS B NE2 1 
ATOM   3400 N N   . MET B 1 163 ? 12.88700  7.17300   -1.94700  1.000 36.19000 ? 165 MET B N   1 
ATOM   3401 C CA  . MET B 1 163 ? 14.20600  7.39800   -2.53400  1.000 41.18000 ? 165 MET B CA  1 
ATOM   3402 C C   . MET B 1 163 ? 14.30300  6.85200   -3.95400  1.000 40.59000 ? 165 MET B C   1 
ATOM   3403 O O   . MET B 1 163 ? 13.72500  5.81400   -4.27500  1.000 38.70000 ? 165 MET B O   1 
ATOM   3404 C CB  . MET B 1 163 ? 15.30900  6.71800   -1.71400  1.000 40.26000 ? 165 MET B CB  1 
ATOM   3405 C CG  . MET B 1 163 ? 15.30100  6.99900   -0.23900  1.000 49.41000 ? 165 MET B CG  1 
ATOM   3406 S SD  . MET B 1 163 ? 16.39900  5.88600   0.65200   1.000 62.71000 ? 165 MET B SD  1 
ATOM   3407 C CE  . MET B 1 163 ? 16.53300  4.51100   -0.47200  1.000 45.67000 ? 165 MET B CE  1 
ATOM   3408 N N   . GLU B 1 164 ? 15.10200  7.52600   -4.77900  1.000 41.95000 ? 166 GLU B N   1 
ATOM   3409 C CA  . GLU B 1 164 ? 15.55000  6.97400   -6.05400  1.000 46.82000 ? 166 GLU B CA  1 
ATOM   3410 C C   . GLU B 1 164 ? 16.91900  6.32900   -5.87100  1.000 45.37000 ? 166 GLU B C   1 
ATOM   3411 O O   . GLU B 1 164 ? 17.83300  6.94800   -5.32300  1.000 44.80000 ? 166 GLU B O   1 
ATOM   3412 C CB  . GLU B 1 164 ? 15.62000  8.05800   -7.13400  1.000 46.70000 ? 166 GLU B CB  1 
ATOM   3413 N N   . LEU B 1 165 ? 17.05100  5.12000   -6.33100  1.000 45.71000 ? 167 LEU B N   1 
ATOM   3414 C CA  . LEU B 1 165 ? 18.29100  4.42100   -6.34100  1.000 49.78000 ? 167 LEU B CA  1 
ATOM   3415 C C   . LEU B 1 165 ? 19.02100  4.79600   -7.63800  1.000 55.84000 ? 167 LEU B C   1 
ATOM   3416 O O   . LEU B 1 165 ? 18.43500  5.13600   -8.61300  1.000 51.33000 ? 167 LEU B O   1 
ATOM   3417 C CB  . LEU B 1 165 ? 18.13200  2.93600   -6.15500  1.000 48.47000 ? 167 LEU B CB  1 
ATOM   3418 C CG  . LEU B 1 165 ? 17.55400  2.51600   -4.83000  1.000 45.24000 ? 167 LEU B CG  1 
ATOM   3419 C CD1 . LEU B 1 165 ? 17.31100  1.05100   -4.72200  1.000 43.88000 ? 167 LEU B CD1 1 
ATOM   3420 C CD2 . LEU B 1 165 ? 18.43700  2.92700   -3.71500  1.000 48.36000 ? 167 LEU B CD2 1 
ATOM   3421 N N   . PRO B 1 166 ? 20.38800  4.67900   -7.57200  1.000 56.47000 ? 168 PRO B N   1 
ATOM   3422 C CA  . PRO B 1 166 ? 21.12300  5.17300   -8.72500  1.000 58.71000 ? 168 PRO B CA  1 
ATOM   3423 C C   . PRO B 1 166 ? 20.79300  4.54300   -10.01000 1.000 61.35000 ? 168 PRO B C   1 
ATOM   3424 O O   . PRO B 1 166 ? 20.96100  5.15100   -11.02200 1.000 62.94000 ? 168 PRO B O   1 
ATOM   3425 C CB  . PRO B 1 166 ? 22.55400  4.89500   -8.36300  1.000 60.46000 ? 168 PRO B CB  1 
ATOM   3426 C CG  . PRO B 1 166 ? 22.49200  3.72800   -7.49500  1.000 60.04000 ? 168 PRO B CG  1 
ATOM   3427 C CD  . PRO B 1 166 ? 21.42800  4.14000   -6.59700  1.000 54.23000 ? 168 PRO B CD  1 
ATOM   3428 N N   . THR B 1 167 ? 20.32000  3.33600   -9.95200  1.000 60.87000 ? 169 THR B N   1 
ATOM   3429 C CA  . THR B 1 167 ? 19.94200  2.59500   -11.08600 1.000 54.14000 ? 169 THR B CA  1 
ATOM   3430 C C   . THR B 1 167 ? 18.62100  3.07500   -11.71800 1.000 57.79000 ? 169 THR B C   1 
ATOM   3431 O O   . THR B 1 167 ? 18.20300  2.58000   -12.71000 1.000 56.66000 ? 169 THR B O   1 
ATOM   3432 C CB  . THR B 1 167 ? 19.93500  1.14300   -10.69400 1.000 55.74000 ? 169 THR B CB  1 
ATOM   3433 O OG1 . THR B 1 167 ? 19.71700  0.37500   -11.83200 1.000 61.18000 ? 169 THR B OG1 1 
ATOM   3434 C CG2 . THR B 1 167 ? 18.90000  0.85400   -9.75900  1.000 54.43000 ? 169 THR B CG2 1 
ATOM   3435 N N   . GLY B 1 168 ? 17.96000  4.02300   -11.11400 1.000 55.43000 ? 170 GLY B N   1 
ATOM   3436 C CA  . GLY B 1 168 ? 16.70600  4.53800   -11.61500 1.000 51.25000 ? 170 GLY B CA  1 
ATOM   3437 C C   . GLY B 1 168 ? 15.39500  4.06500   -11.00100 1.000 55.19000 ? 170 GLY B C   1 
ATOM   3438 O O   . GLY B 1 168 ? 14.39100  4.64100   -11.22500 1.000 55.27000 ? 170 GLY B O   1 
ATOM   3439 N N   . VAL B 1 169 ? 15.44300  3.01000   -10.21900 1.000 54.12000 ? 171 VAL B N   1 
ATOM   3440 C CA  . VAL B 1 169 ? 14.33500  2.42400   -9.51500  1.000 46.60000 ? 171 VAL B CA  1 
ATOM   3441 C C   . VAL B 1 169 ? 14.13500  3.13200   -8.23000  1.000 46.22000 ? 171 VAL B C   1 
ATOM   3442 O O   . VAL B 1 169 ? 14.90400  3.94500   -7.90100  1.000 45.06000 ? 171 VAL B O   1 
ATOM   3443 C CB  . VAL B 1 169 ? 14.52000  0.96200   -9.31700  1.000 42.48000 ? 171 VAL B CB  1 
ATOM   3444 C CG1 . VAL B 1 169 ? 14.68800  0.33300   -10.65400 1.000 46.29000 ? 171 VAL B CG1 1 
ATOM   3445 C CG2 . VAL B 1 169 ? 15.66700  0.69800   -8.42100  1.000 38.67000 ? 171 VAL B CG2 1 
ATOM   3446 N N   . HIS B 1 170 ? 13.08100  2.80400   -7.53100  1.000 41.61000 ? 172 HIS B N   1 
ATOM   3447 C CA  . HIS B 1 170 ? 12.63900  3.52900   -6.34600  1.000 42.23000 ? 172 HIS B CA  1 
ATOM   3448 C C   . HIS B 1 170 ? 12.49600  2.60500   -5.14400  1.000 36.46000 ? 172 HIS B C   1 
ATOM   3449 O O   . HIS B 1 170 ? 12.26300  1.39800   -5.27700  1.000 33.39000 ? 172 HIS B O   1 
ATOM   3450 C CB  . HIS B 1 170 ? 11.32100  4.25400   -6.63100  1.000 43.95000 ? 172 HIS B CB  1 
ATOM   3451 C CG  . HIS B 1 170 ? 11.35500  5.04800   -7.90100  1.000 54.93000 ? 172 HIS B CG  1 
ATOM   3452 N ND1 . HIS B 1 170 ? 11.97300  6.27900   -7.99300  1.000 56.76000 ? 172 HIS B ND1 1 
ATOM   3453 C CD2 . HIS B 1 170 ? 10.90000  4.76200   -9.14600  1.000 56.01000 ? 172 HIS B CD2 1 
ATOM   3454 C CE1 . HIS B 1 170 ? 11.87700  6.72700   -9.23200  1.000 58.30000 ? 172 HIS B CE1 1 
ATOM   3455 N NE2 . HIS B 1 170 ? 11.23100  5.82600   -9.95200  1.000 60.57000 ? 172 HIS B NE2 1 
ATOM   3456 N N   . ALA B 1 171 ? 12.66000  3.19400   -3.96000  1.000 34.60000 ? 173 ALA B N   1 
ATOM   3457 C CA  . ALA B 1 171 ? 12.65300  2.48500   -2.69100  1.000 32.39000 ? 173 ALA B CA  1 
ATOM   3458 C C   . ALA B 1 171 ? 11.77500  3.24500   -1.70500  1.000 31.46000 ? 173 ALA B C   1 
ATOM   3459 O O   . ALA B 1 171 ? 11.73300  4.47800   -1.72400  1.000 31.18000 ? 173 ALA B O   1 
ATOM   3460 C CB  . ALA B 1 171 ? 14.07700  2.33200   -2.12700  1.000 35.69000 ? 173 ALA B CB  1 
ATOM   3461 N N   . GLY B 1 172 ? 11.06600  2.50700   -0.86300  1.000 25.65000 ? 174 GLY B N   1 
ATOM   3462 C CA  . GLY B 1 172 ? 10.09900  3.12000   0.01900   1.000 27.86000 ? 174 GLY B CA  1 
ATOM   3463 C C   . GLY B 1 172 ? 9.75500   2.19800   1.16500   1.000 29.66000 ? 174 GLY B C   1 
ATOM   3464 O O   . GLY B 1 172 ? 10.35000  1.13100   1.33200   1.000 27.24000 ? 174 GLY B O   1 
ATOM   3465 N N   . THR B 1 173 ? 8.77100   2.62800   1.95000   1.000 25.05000 ? 175 THR B N   1 
ATOM   3466 C CA  . THR B 1 173 ? 8.34400   1.94800   3.16000   1.000 28.38000 ? 175 THR B CA  1 
ATOM   3467 C C   . THR B 1 173 ? 6.86000   1.58200   3.05100   1.000 28.69000 ? 175 THR B C   1 
ATOM   3468 O O   . THR B 1 173 ? 6.15800   2.00200   2.12900   1.000 28.58000 ? 175 THR B O   1 
ATOM   3469 C CB  . THR B 1 173 ? 8.56700   2.84000   4.38700   1.000 27.67000 ? 175 THR B CB  1 
ATOM   3470 O OG1 . THR B 1 173 ? 7.68900   3.96500   4.28700   1.000 28.07000 ? 175 THR B OG1 1 
ATOM   3471 C CG2 . THR B 1 173 ? 9.99000   3.35700   4.41800   1.000 29.82000 ? 175 THR B CG2 1 
ATOM   3472 N N   . ASP B 1 174 ? 6.37900   0.78400   4.00000   1.000 27.87000 ? 176 ASP B N   1 
ATOM   3473 C CA  . ASP B 1 174 ? 4.93900   0.69800   4.15400   1.000 28.62000 ? 176 ASP B CA  1 
ATOM   3474 C C   . ASP B 1 174 ? 4.47300   1.94700   4.90400   1.000 29.03000 ? 176 ASP B C   1 
ATOM   3475 O O   . ASP B 1 174 ? 5.27000   2.84100   5.21800   1.000 28.80000 ? 176 ASP B O   1 
ATOM   3476 C CB  . ASP B 1 174 ? 4.54800   -0.62500  4.81900   1.000 28.40000 ? 176 ASP B CB  1 
ATOM   3477 C CG  . ASP B 1 174 ? 5.14300   -0.80800  6.22000   1.000 31.92000 ? 176 ASP B CG  1 
ATOM   3478 O OD1 . ASP B 1 174 ? 5.40100   0.18600   6.92500   1.000 27.10000 ? 176 ASP B OD1 1 
ATOM   3479 O OD2 . ASP B 1 174 ? 5.30400   -1.97400  6.63200   1.000 31.47000 ? 176 ASP B OD2 1 
ATOM   3480 N N   . LEU B 1 175 ? 3.18000   2.04100   5.19300   1.000 24.05000 ? 177 LEU B N   1 
ATOM   3481 C CA  . LEU B 1 175 ? 2.70300   3.27200   5.82100   1.000 28.22000 ? 177 LEU B CA  1 
ATOM   3482 C C   . LEU B 1 175 ? 2.98700   3.31000   7.32300   1.000 32.01000 ? 177 LEU B C   1 
ATOM   3483 O O   . LEU B 1 175 ? 2.76100   4.34000   7.96800   1.000 31.20000 ? 177 LEU B O   1 
ATOM   3484 C CB  . LEU B 1 175 ? 1.20900   3.47300   5.52600   1.000 27.60000 ? 177 LEU B CB  1 
ATOM   3485 C CG  . LEU B 1 175 ? 0.90800   4.35900   4.29600   1.000 27.52000 ? 177 LEU B CG  1 
ATOM   3486 C CD1 . LEU B 1 175 ? 1.23600   5.82600   4.56300   1.000 30.22000 ? 177 LEU B CD1 1 
ATOM   3487 C CD2 . LEU B 1 175 ? 1.67600   3.90500   3.05600   1.000 27.42000 ? 177 LEU B CD2 1 
ATOM   3488 N N   . GLU B 1 176 ? 3.51100   2.22900   7.88500   1.000 33.67000 ? 178 GLU B N   1 
ATOM   3489 C CA  . GLU B 1 176 ? 4.05600   2.22500   9.23200   1.000 33.96000 ? 178 GLU B CA  1 
ATOM   3490 C C   . GLU B 1 176 ? 5.56100   2.48700   9.26100   1.000 34.14000 ? 178 GLU B C   1 
ATOM   3491 O O   . GLU B 1 176 ? 6.18800   2.29300   10.30900  1.000 32.79000 ? 178 GLU B O   1 
ATOM   3492 C CB  . GLU B 1 176 ? 3.73000   0.89300   9.90500   1.000 34.58000 ? 178 GLU B CB  1 
ATOM   3493 C CG  . GLU B 1 176 ? 2.25500   0.70600   10.08000  1.000 39.07000 ? 178 GLU B CG  1 
ATOM   3494 C CD  . GLU B 1 176 ? 1.88700   -0.55900  10.82900  1.000 46.16000 ? 178 GLU B CD  1 
ATOM   3495 O OE1 . GLU B 1 176 ? 0.74200   -0.63200  11.29100  1.000 49.88000 ? 178 GLU B OE1 1 
ATOM   3496 O OE2 . GLU B 1 176 ? 2.72500   -1.47900  10.94800  1.000 54.48000 ? 178 GLU B OE2 1 
ATOM   3497 N N   . GLY B 1 177 ? 6.14900   2.91400   8.13800   1.000 32.60000 ? 179 GLY B N   1 
ATOM   3498 C CA  . GLY B 1 177 ? 7.55400   3.31800   8.08100   1.000 30.91000 ? 179 GLY B CA  1 
ATOM   3499 C C   . GLY B 1 177 ? 8.56900   2.19600   8.00700   1.000 29.88000 ? 179 GLY B C   1 
ATOM   3500 O O   . GLY B 1 177 ? 9.76900   2.45600   8.14700   1.000 27.94000 ? 179 GLY B O   1 
ATOM   3501 N N   . ASN B 1 178 ? 8.14500   0.95600   7.80100   1.000 30.84000 ? 180 ASN B N   1 
ATOM   3502 C CA  . ASN B 1 178 ? 9.08800   -0.13800  7.61900   1.000 28.52000 ? 180 ASN B CA  1 
ATOM   3503 C C   . ASN B 1 178 ? 9.52400   -0.19600  6.15900   1.000 31.05000 ? 180 ASN B C   1 
ATOM   3504 O O   . ASN B 1 178 ? 8.68300   -0.28100  5.24900   1.000 26.10000 ? 180 ASN B O   1 
ATOM   3505 C CB  . ASN B 1 178 ? 8.46800   -1.46400  8.05200   1.000 27.61000 ? 180 ASN B CB  1 
ATOM   3506 C CG  . ASN B 1 178 ? 7.88300   -1.40200  9.45800   1.000 33.40000 ? 180 ASN B CG  1 
ATOM   3507 O OD1 . ASN B 1 178 ? 8.61300   -1.30600  10.46100  1.000 31.22000 ? 180 ASN B OD1 1 
ATOM   3508 N ND2 . ASN B 1 178 ? 6.56300   -1.45700  9.54100   1.000 31.34000 ? 180 ASN B ND2 1 
ATOM   3509 N N   . PHE B 1 179 ? 10.83500  -0.15500  5.94300   1.000 28.81000 ? 181 PHE B N   1 
ATOM   3510 C CA  . PHE B 1 179 ? 11.35100  -0.19100  4.58600   1.000 29.59000 ? 181 PHE B CA  1 
ATOM   3511 C C   . PHE B 1 179 ? 11.02000  -1.52000  3.93800   1.000 28.33000 ? 181 PHE B C   1 
ATOM   3512 O O   . PHE B 1 179 ? 10.96800  -2.56700  4.59400   1.000 24.41000 ? 181 PHE B O   1 
ATOM   3513 C CB  . PHE B 1 179 ? 12.86500  0.06100   4.56700   1.000 30.43000 ? 181 PHE B CB  1 
ATOM   3514 C CG  . PHE B 1 179 ? 13.22000  1.42000   4.05300   1.000 32.21000 ? 181 PHE B CG  1 
ATOM   3515 C CD1 . PHE B 1 179 ? 13.24400  1.67800   2.68300   1.000 28.91000 ? 181 PHE B CD1 1 
ATOM   3516 C CD2 . PHE B 1 179 ? 13.47100  2.46400   4.94100   1.000 34.78000 ? 181 PHE B CD2 1 
ATOM   3517 C CE1 . PHE B 1 179 ? 13.50800  2.94800   2.20500   1.000 29.74000 ? 181 PHE B CE1 1 
ATOM   3518 C CE2 . PHE B 1 179 ? 13.76200  3.73100   4.47200   1.000 35.06000 ? 181 PHE B CE2 1 
ATOM   3519 C CZ  . PHE B 1 179 ? 13.77100  3.97500   3.09700   1.000 33.47000 ? 181 PHE B CZ  1 
ATOM   3520 N N   . TYR B 1 180 ? 10.88100  -1.46800  2.65300   1.000 26.62000 ? 182 TYR B N   1 
ATOM   3521 C CA  . TYR B 1 180 ? 10.74500  -2.61600  1.83200   1.000 28.06000 ? 182 TYR B CA  1 
ATOM   3522 C C   . TYR B 1 180 ? 12.16400  -2.70800  1.28600   1.000 29.00000 ? 182 TYR B C   1 
ATOM   3523 O O   . TYR B 1 180 ? 12.63500  -1.86400  0.63000   1.000 26.13000 ? 182 TYR B O   1 
ATOM   3524 C CB  . TYR B 1 180 ? 9.72700   -2.45100  0.69300   1.000 29.55000 ? 182 TYR B CB  1 
ATOM   3525 C CG  . TYR B 1 180 ? 8.25500   -2.50000  1.02300   1.000 25.46000 ? 182 TYR B CG  1 
ATOM   3526 C CD1 . TYR B 1 180 ? 7.63400   -3.65800  1.27700   1.000 25.32000 ? 182 TYR B CD1 1 
ATOM   3527 C CD2 . TYR B 1 180 ? 7.50000   -1.36600  1.04100   1.000 28.59000 ? 182 TYR B CD2 1 
ATOM   3528 C CE1 . TYR B 1 180 ? 6.31700   -3.71000  1.53800   1.000 28.57000 ? 182 TYR B CE1 1 
ATOM   3529 C CE2 . TYR B 1 180 ? 6.18400   -1.40400  1.30800   1.000 26.08000 ? 182 TYR B CE2 1 
ATOM   3530 C CZ  . TYR B 1 180 ? 5.59500   -2.58600  1.55100   1.000 27.18000 ? 182 TYR B CZ  1 
ATOM   3531 O OH  . TYR B 1 180 ? 4.31200   -2.63600  1.84100   1.000 30.59000 ? 182 TYR B OH  1 
ATOM   3532 N N   . GLY B 1 181 ? 12.83200  -3.77800  1.59100   1.000 28.86000 ? 183 GLY B N   1 
ATOM   3533 C CA  . GLY B 1 181 ? 14.17600  -4.00000  1.16600   1.000 27.72000 ? 183 GLY B CA  1 
ATOM   3534 C C   . GLY B 1 181 ? 15.25100  -3.49300  2.09200   1.000 30.19000 ? 183 GLY B C   1 
ATOM   3535 O O   . GLY B 1 181 ? 15.00100  -2.79400  2.98200   1.000 25.33000 ? 183 GLY B O   1 
ATOM   3536 N N   . PRO B 1 182 ? 16.51900  -3.92300  1.77400   1.000 28.85000 ? 184 PRO B N   1 
ATOM   3537 C CA  . PRO B 1 182 ? 17.59200  -3.50800  2.67700   1.000 30.75000 ? 184 PRO B CA  1 
ATOM   3538 C C   . PRO B 1 182 ? 18.16200  -2.14200  2.39300   1.000 33.13000 ? 184 PRO B C   1 
ATOM   3539 O O   . PRO B 1 182 ? 19.26600  -1.98100  2.01900   1.000 35.21000 ? 184 PRO B O   1 
ATOM   3540 C CB  . PRO B 1 182 ? 18.61800  -4.55000  2.43600   1.000 28.93000 ? 184 PRO B CB  1 
ATOM   3541 C CG  . PRO B 1 182 ? 18.59500  -4.71200  1.02200   1.000 32.22000 ? 184 PRO B CG  1 
ATOM   3542 C CD  . PRO B 1 182 ? 17.17400  -4.72600  0.65700   1.000 27.77000 ? 184 PRO B CD  1 
ATOM   3543 N N   . PHE B 1 183 ? 17.36500  -1.13200  2.61200   1.000 33.68000 ? 185 PHE B N   1 
ATOM   3544 C CA  . PHE B 1 183 ? 17.70000  0.25200   2.37600   1.000 33.96000 ? 185 PHE B CA  1 
ATOM   3545 C C   . PHE B 1 183 ? 17.48400  1.08100   3.60600   1.000 34.85000 ? 185 PHE B C   1 
ATOM   3546 O O   . PHE B 1 183 ? 16.75500  0.70300   4.43800   1.000 35.91000 ? 185 PHE B O   1 
ATOM   3547 C CB  . PHE B 1 183 ? 16.88600  0.81600   1.21200   1.000 33.26000 ? 185 PHE B CB  1 
ATOM   3548 C CG  . PHE B 1 183 ? 16.82400  -0.07400  0.02300   1.000 33.90000 ? 185 PHE B CG  1 
ATOM   3549 C CD1 . PHE B 1 183 ? 17.91900  -0.33800  -0.71000  1.000 36.04000 ? 185 PHE B CD1 1 
ATOM   3550 C CD2 . PHE B 1 183 ? 15.67500  -0.67100  -0.31700  1.000 29.53000 ? 185 PHE B CD2 1 
ATOM   3551 C CE1 . PHE B 1 183 ? 17.86000  -1.18900  -1.76800  1.000 40.03000 ? 185 PHE B CE1 1 
ATOM   3552 C CE2 . PHE B 1 183 ? 15.59200  -1.51000  -1.35300  1.000 29.85000 ? 185 PHE B CE2 1 
ATOM   3553 C CZ  . PHE B 1 183 ? 16.67400  -1.77600  -2.09200  1.000 32.53000 ? 185 PHE B CZ  1 
ATOM   3554 N N   . VAL B 1 184 ? 18.15500  2.20100   3.70400   1.000 33.73000 ? 186 VAL B N   1 
ATOM   3555 C CA  . VAL B 1 184 ? 18.05100  3.09700   4.81200   1.000 36.39000 ? 186 VAL B CA  1 
ATOM   3556 C C   . VAL B 1 184 ? 17.84900  4.50400   4.34300   1.000 40.62000 ? 186 VAL B C   1 
ATOM   3557 O O   . VAL B 1 184 ? 18.31500  4.84100   3.32700   1.000 42.03000 ? 186 VAL B O   1 
ATOM   3558 C CB  . VAL B 1 184 ? 19.28500  3.05500   5.70000   1.000 40.85000 ? 186 VAL B CB  1 
ATOM   3559 C CG1 . VAL B 1 184 ? 19.48500  1.69300   6.22300   1.000 38.11000 ? 186 VAL B CG1 1 
ATOM   3560 C CG2 . VAL B 1 184 ? 20.50800  3.49700   4.97000   1.000 40.60000 ? 186 VAL B CG2 1 
ATOM   3561 N N   . ASP B 1 185 ? 17.17300  5.33500   5.10200   1.000 41.33000 ? 187 ASP B N   1 
ATOM   3562 C CA  . ASP B 1 185 ? 16.96000  6.70500   4.69800   1.000 45.64000 ? 187 ASP B CA  1 
ATOM   3563 C C   . ASP B 1 185 ? 18.08500  7.63800   5.09000   1.000 50.99000 ? 187 ASP B C   1 
ATOM   3564 O O   . ASP B 1 185 ? 17.94000  8.43100   5.92900   1.000 55.24000 ? 187 ASP B O   1 
ATOM   3565 C CB  . ASP B 1 185 ? 15.62600  7.23200   5.18400   1.000 42.31000 ? 187 ASP B CB  1 
ATOM   3566 C CG  . ASP B 1 185 ? 15.43500  7.09000   6.63900   1.000 43.56000 ? 187 ASP B CG  1 
ATOM   3567 O OD1 . ASP B 1 185 ? 16.20300  6.41700   7.27400   1.000 45.51000 ? 187 ASP B OD1 1 
ATOM   3568 O OD2 . ASP B 1 185 ? 14.49300  7.61900   7.15400   1.000 41.69000 ? 187 ASP B OD2 1 
ATOM   3569 N N   . ARG B 1 186 ? 19.20300  7.50200   4.43400   1.000 56.49000 ? 188 ARG B N   1 
ATOM   3570 C CA  . ARG B 1 186 ? 20.37800  8.29400   4.63500   1.000 60.44000 ? 188 ARG B CA  1 
ATOM   3571 C C   . ARG B 1 186 ? 21.16400  8.28500   3.39200   1.000 63.95000 ? 188 ARG B C   1 
ATOM   3572 O O   . ARG B 1 186 ? 20.95400  7.47500   2.54100   1.000 62.09000 ? 188 ARG B O   1 
ATOM   3573 C CB  . ARG B 1 186 ? 21.22000  7.74100   5.69700   1.000 61.83000 ? 188 ARG B CB  1 
ATOM   3574 C CG  . ARG B 1 186 ? 20.82300  8.29000   7.02200   1.000 65.29000 ? 188 ARG B CG  1 
ATOM   3575 C CD  . ARG B 1 186 ? 21.86500  8.07000   8.08300   1.000 70.75000 ? 188 ARG B CD  1 
ATOM   3576 N NE  . ARG B 1 186 ? 22.69200  6.91300   7.81500   1.000 68.96000 ? 188 ARG B NE  1 
ATOM   3577 C CZ  . ARG B 1 186 ? 22.29800  5.67900   7.93600   1.000 62.41000 ? 188 ARG B CZ  1 
ATOM   3578 N NH1 . ARG B 1 186 ? 21.09400  5.42900   8.32500   1.000 62.80000 ? 188 ARG B NH1 1 
ATOM   3579 N NH2 . ARG B 1 186 ? 23.13100  4.72200   7.67400   1.000 58.58000 ? 188 ARG B NH2 1 
ATOM   3580 N N   . GLN B 1 187 ? 22.08500  9.21800   3.27500   1.000 72.43000 ? 189 GLN B N   1 
ATOM   3581 C CA  . GLN B 1 187 ? 22.87300  9.31300   2.06200   1.000 69.82000 ? 189 GLN B CA  1 
ATOM   3582 C C   . GLN B 1 187 ? 24.10800  8.41600   1.98400   1.000 70.34000 ? 189 GLN B C   1 
ATOM   3583 O O   . GLN B 1 187 ? 25.19800  8.87400   1.75200   1.000 70.88000 ? 189 GLN B O   1 
ATOM   3584 C CB  . GLN B 1 187 ? 23.24100  10.76600  1.86800   1.000 71.43000 ? 189 GLN B CB  1 
ATOM   3585 N N   . THR B 1 188 ? 23.90900  7.13200   2.16100   1.000 66.18000 ? 190 THR B N   1 
ATOM   3586 C CA  . THR B 1 188 ? 24.95700  6.17700   2.09400   1.000 65.01000 ? 190 THR B CA  1 
ATOM   3587 C C   . THR B 1 188 ? 24.86600  5.80900   0.67800   1.000 64.92000 ? 190 THR B C   1 
ATOM   3588 O O   . THR B 1 188 ? 23.97000  6.23000   0.01500   1.000 67.65000 ? 190 THR B O   1 
ATOM   3589 C CB  . THR B 1 188 ? 24.64700  4.92200   2.94600   1.000 65.31000 ? 190 THR B CB  1 
ATOM   3590 O OG1 . THR B 1 188 ? 24.58400  5.26600   4.32100   1.000 68.52000 ? 190 THR B OG1 1 
ATOM   3591 C CG2 . THR B 1 188 ? 25.72000  3.90500   2.84300   1.000 61.14000 ? 190 THR B CG2 1 
ATOM   3592 N N   . ALA B 1 189 ? 25.79600  5.02900   0.20400   1.000 65.07000 ? 191 ALA B N   1 
ATOM   3593 C CA  . ALA B 1 189 ? 25.73800  4.55500   -1.14200  1.000 65.22000 ? 191 ALA B CA  1 
ATOM   3594 C C   . ALA B 1 189 ? 24.98000  3.24600   -0.99800  1.000 62.14000 ? 191 ALA B C   1 
ATOM   3595 O O   . ALA B 1 189 ? 25.29300  2.43500   -0.17800  1.000 59.26000 ? 191 ALA B O   1 
ATOM   3596 C CB  . ALA B 1 189 ? 27.12200  4.33400   -1.67600  1.000 64.31000 ? 191 ALA B CB  1 
ATOM   3597 N N   . GLN B 1 190 ? 23.95100  3.08600   -1.79100  1.000 58.62000 ? 192 GLN B N   1 
ATOM   3598 C CA  . GLN B 1 190 ? 23.06700  1.93600   -1.78900  1.000 53.69000 ? 192 GLN B CA  1 
ATOM   3599 C C   . GLN B 1 190 ? 22.71800  1.59400   -3.22200  1.000 54.15000 ? 192 GLN B C   1 
ATOM   3600 O O   . GLN B 1 190 ? 22.63400  2.47500   -4.08400  1.000 53.71000 ? 192 GLN B O   1 
ATOM   3601 C CB  . GLN B 1 190 ? 21.78900  2.19300   -0.99600  1.000 50.30000 ? 192 GLN B CB  1 
ATOM   3602 C CG  . GLN B 1 190 ? 21.88500  3.34400   -0.03200  1.000 51.40000 ? 192 GLN B CG  1 
ATOM   3603 C CD  . GLN B 1 190 ? 20.67100  3.43100   0.84700   1.000 46.49000 ? 192 GLN B CD  1 
ATOM   3604 O OE1 . GLN B 1 190 ? 20.30200  2.44700   1.48600   1.000 37.89000 ? 192 GLN B OE1 1 
ATOM   3605 N NE2 . GLN B 1 190 ? 20.05900  4.60200   0.91400   1.000 43.72000 ? 192 GLN B NE2 1 
ATOM   3606 N N   . ALA B 1 191 ? 22.51600  0.30800   -3.46900  1.000 54.67000 ? 193 ALA B N   1 
ATOM   3607 C CA  . ALA B 1 191 ? 22.16500  -0.15300  -4.79900  1.000 51.20000 ? 193 ALA B CA  1 
ATOM   3608 C C   . ALA B 1 191 ? 21.15500  -1.28100  -4.68900  1.000 44.07000 ? 193 ALA B C   1 
ATOM   3609 O O   . ALA B 1 191 ? 21.16000  -2.04900  -3.72800  1.000 45.48000 ? 193 ALA B O   1 
ATOM   3610 C CB  . ALA B 1 191 ? 23.40600  -0.62200  -5.57300  1.000 50.54000 ? 193 ALA B CB  1 
ATOM   3611 N N   . ALA B 1 192 ? 20.28900  -1.37900  -5.68500  1.000 47.35000 ? 194 ALA B N   1 
ATOM   3612 C CA  . ALA B 1 192 ? 19.38000  -2.51000  -5.72400  1.000 49.94000 ? 194 ALA B CA  1 
ATOM   3613 C C   . ALA B 1 192 ? 20.18100  -3.78100  -5.96100  1.000 49.22000 ? 194 ALA B C   1 
ATOM   3614 O O   . ALA B 1 192 ? 21.10700  -3.80500  -6.77500  1.000 50.27000 ? 194 ALA B O   1 
ATOM   3615 C CB  . ALA B 1 192 ? 18.33000  -2.32600  -6.82600  1.000 42.18000 ? 194 ALA B CB  1 
ATOM   3616 N N   . GLY B 1 193 ? 19.75700  -4.85000  -5.35500  1.000 47.81000 ? 195 GLY B N   1 
ATOM   3617 C CA  . GLY B 1 193 ? 20.35700  -6.11400  -5.60500  1.000 43.91000 ? 195 GLY B CA  1 
ATOM   3618 C C   . GLY B 1 193 ? 19.89700  -6.52700  -6.98600  1.000 49.86000 ? 195 GLY B C   1 
ATOM   3619 O O   . GLY B 1 193 ? 19.10100  -5.88700  -7.62600  1.000 45.91000 ? 195 GLY B O   1 
ATOM   3620 N N   . THR B 1 194 ? 20.46400  -7.60100  -7.46500  1.000 46.10000 ? 196 THR B N   1 
ATOM   3621 C CA  . THR B 1 194 ? 20.12300  -8.10500  -8.75200  1.000 48.20000 ? 196 THR B CA  1 
ATOM   3622 C C   . THR B 1 194 ? 18.67100  -8.54500  -8.69600  1.000 50.98000 ? 196 THR B C   1 
ATOM   3623 O O   . THR B 1 194 ? 18.27700  -9.17300  -7.78100  1.000 52.22000 ? 196 THR B O   1 
ATOM   3624 C CB  . THR B 1 194 ? 21.08900  -9.21600  -9.13100  1.000 54.41000 ? 196 THR B CB  1 
ATOM   3625 O OG1 . THR B 1 194 ? 20.62100  -9.84700  -10.29900 1.000 57.83000 ? 196 THR B OG1 1 
ATOM   3626 C CG2 . THR B 1 194 ? 21.11700  -10.18300 -8.06300  1.000 53.43000 ? 196 THR B CG2 1 
ATOM   3627 N N   . ASP B 1 195 ? 17.89600  -8.18300  -9.68600  1.000 46.75000 ? 197 ASP B N   1 
ATOM   3628 C CA  . ASP B 1 195 ? 16.48500  -8.49900  -9.74300  1.000 47.23000 ? 197 ASP B CA  1 
ATOM   3629 C C   . ASP B 1 195 ? 16.18700  -9.75000  -10.49700 1.000 50.17000 ? 197 ASP B C   1 
ATOM   3630 O O   . ASP B 1 195 ? 17.00500  -10.21600 -11.22000 1.000 51.93000 ? 197 ASP B O   1 
ATOM   3631 C CB  . ASP B 1 195 ? 15.70400  -7.36400  -10.39200 1.000 42.46000 ? 197 ASP B CB  1 
ATOM   3632 C CG  . ASP B 1 195 ? 14.24700  -7.31800  -9.94400  1.000 44.25000 ? 197 ASP B CG  1 
ATOM   3633 O OD1 . ASP B 1 195 ? 13.89000  -7.89200  -8.91700  1.000 39.70000 ? 197 ASP B OD1 1 
ATOM   3634 O OD2 . ASP B 1 195 ? 13.47000  -6.70400  -10.63800 1.000 42.51000 ? 197 ASP B OD2 1 
ATOM   3635 N N   . THR B 1 196 ? 15.01000  -10.28600 -10.31500 1.000 43.63000 ? 198 THR B N   1 
ATOM   3636 C CA  . THR B 1 196 ? 14.58000  -11.46600 -10.99300 1.000 46.58000 ? 198 THR B CA  1 
ATOM   3637 C C   . THR B 1 196 ? 13.18300  -11.34500 -11.53600 1.000 46.14000 ? 198 THR B C   1 
ATOM   3638 O O   . THR B 1 196 ? 12.46000  -10.52500 -11.10700 1.000 44.42000 ? 198 THR B O   1 
ATOM   3639 C CB  . THR B 1 196 ? 14.70600  -12.69500 -10.12000 1.000 49.03000 ? 198 THR B CB  1 
ATOM   3640 O OG1 . THR B 1 196 ? 14.08800  -12.49700 -8.88000  1.000 47.84000 ? 198 THR B OG1 1 
ATOM   3641 C CG2 . THR B 1 196 ? 16.10800  -12.94300 -9.84100  1.000 54.09000 ? 198 THR B CG2 1 
ATOM   3642 N N   . THR B 1 197 ? 12.83200  -12.15900 -12.50500 1.000 45.72000 ? 199 THR B N   1 
ATOM   3643 C CA  . THR B 1 197 ? 11.48200  -12.13300 -13.05200 1.000 44.04000 ? 199 THR B CA  1 
ATOM   3644 C C   . THR B 1 197 ? 10.52400  -12.87400 -12.12500 1.000 42.64000 ? 199 THR B C   1 
ATOM   3645 O O   . THR B 1 197 ? 10.88800  -13.88600 -11.51900 1.000 43.58000 ? 199 THR B O   1 
ATOM   3646 C CB  . THR B 1 197 ? 11.47600  -12.75700 -14.44600 1.000 45.16000 ? 199 THR B CB  1 
ATOM   3647 O OG1 . THR B 1 197 ? 12.41000  -12.05400 -15.26300 1.000 41.55000 ? 199 THR B OG1 1 
ATOM   3648 C CG2 . THR B 1 197 ? 10.10100  -12.64900 -15.08400 1.000 41.38000 ? 199 THR B CG2 1 
ATOM   3649 N N   . ILE B 1 198 ? 9.30000   -12.35400 -12.00600 1.000 39.67000 ? 200 ILE B N   1 
ATOM   3650 C CA  . ILE B 1 198 ? 8.30200   -12.88900 -11.08200 1.000 37.58000 ? 200 ILE B CA  1 
ATOM   3651 C C   . ILE B 1 198 ? 7.55000   -14.01400 -11.78900 1.000 37.30000 ? 200 ILE B C   1 
ATOM   3652 O O   . ILE B 1 198 ? 6.55800   -13.77700 -12.47800 1.000 36.16000 ? 200 ILE B O   1 
ATOM   3653 C CB  . ILE B 1 198 ? 7.34400   -11.80400 -10.58500 1.000 36.35000 ? 200 ILE B CB  1 
ATOM   3654 C CG1 . ILE B 1 198 ? 8.12400   -10.59500 -10.05700 1.000 38.05000 ? 200 ILE B CG1 1 
ATOM   3655 C CG2 . ILE B 1 198 ? 6.42300   -12.38400 -9.52100  1.000 33.12000 ? 200 ILE B CG2 1 
ATOM   3656 C CD1 . ILE B 1 198 ? 7.40000   -9.25400  -10.23600 1.000 35.27000 ? 200 ILE B CD1 1 
ATOM   3657 N N   . THR B 1 199 ? 7.97400   -15.25100 -11.52600 1.000 41.51000 ? 201 THR B N   1 
ATOM   3658 C CA  . THR B 1 199 ? 7.52200   -16.41600 -12.28500 1.000 40.81000 ? 201 THR B CA  1 
ATOM   3659 C C   . THR B 1 199 ? 6.01200   -16.59900 -12.21300 1.000 38.87000 ? 201 THR B C   1 
ATOM   3660 O O   . THR B 1 199 ? 5.35000   -16.79300 -13.23900 1.000 38.75000 ? 201 THR B O   1 
ATOM   3661 C CB  . THR B 1 199 ? 8.24500   -17.66500 -11.76900 1.000 41.22000 ? 201 THR B CB  1 
ATOM   3662 O OG1 . THR B 1 199 ? 9.65000   -17.41300 -11.78700 1.000 47.38000 ? 201 THR B OG1 1 
ATOM   3663 C CG2 . THR B 1 199 ? 7.94400   -18.88600 -12.63300 1.000 40.19000 ? 201 THR B CG2 1 
ATOM   3664 N N   . VAL B 1 200 ? 5.44100   -16.55700 -11.00200 1.000 38.71000 ? 202 VAL B N   1 
ATOM   3665 C CA  . VAL B 1 200 ? 4.00400   -16.81300 -10.86600 1.000 34.56000 ? 202 VAL B CA  1 
ATOM   3666 C C   . VAL B 1 200 ? 3.17900   -15.77800 -11.63100 1.000 35.83000 ? 202 VAL B C   1 
ATOM   3667 O O   . VAL B 1 200 ? 2.05900   -16.06900 -12.07700 1.000 35.72000 ? 202 VAL B O   1 
ATOM   3668 C CB  . VAL B 1 200 ? 3.61200   -16.87500 -9.37400  1.000 39.52000 ? 202 VAL B CB  1 
ATOM   3669 C CG1 . VAL B 1 200 ? 3.71300   -15.49600 -8.74400  1.000 39.99000 ? 202 VAL B CG1 1 
ATOM   3670 C CG2 . VAL B 1 200 ? 2.21200   -17.48100 -9.18900  1.000 40.14000 ? 202 VAL B CG2 1 
ATOM   3671 N N   . ASN B 1 201 ? 3.71700   -14.57300 -11.83200 1.000 35.81000 ? 203 ASN B N   1 
ATOM   3672 C CA  . ASN B 1 201 ? 2.99600   -13.56800 -12.60800 1.000 34.99000 ? 203 ASN B CA  1 
ATOM   3673 C C   . ASN B 1 201 ? 3.11600   -13.81700 -14.10800 1.000 34.36000 ? 203 ASN B C   1 
ATOM   3674 O O   . ASN B 1 201 ? 2.15700   -13.58300 -14.85300 1.000 29.57000 ? 203 ASN B O   1 
ATOM   3675 C CB  . ASN B 1 201 ? 3.50000   -12.16700 -12.26600 1.000 30.19000 ? 203 ASN B CB  1 
ATOM   3676 C CG  . ASN B 1 201 ? 3.10200   -11.72200 -10.86000 1.000 36.74000 ? 203 ASN B CG  1 
ATOM   3677 O OD1 . ASN B 1 201 ? 2.34200   -12.40400 -10.14700 1.000 33.70000 ? 203 ASN B OD1 1 
ATOM   3678 N ND2 . ASN B 1 201 ? 3.62600   -10.57100 -10.45200 1.000 34.10000 ? 203 ASN B ND2 1 
ATOM   3679 N N   . VAL B 1 202 ? 4.27800   -14.26800 -14.57800 1.000 33.85000 ? 204 VAL B N   1 
ATOM   3680 C CA  . VAL B 1 202 ? 4.38600   -14.67800 -15.97800 1.000 35.02000 ? 204 VAL B CA  1 
ATOM   3681 C C   . VAL B 1 202 ? 3.37600   -15.78200 -16.27500 1.000 36.01000 ? 204 VAL B C   1 
ATOM   3682 O O   . VAL B 1 202 ? 2.63000   -15.71600 -17.25800 1.000 36.06000 ? 204 VAL B O   1 
ATOM   3683 C CB  . VAL B 1 202 ? 5.82200   -15.12100 -16.30800 1.000 38.58000 ? 204 VAL B CB  1 
ATOM   3684 C CG1 . VAL B 1 202 ? 5.92500   -15.56400 -17.76300 1.000 37.89000 ? 204 VAL B CG1 1 
ATOM   3685 C CG2 . VAL B 1 202 ? 6.80800   -13.99200 -16.03100 1.000 38.61000 ? 204 VAL B CG2 1 
ATOM   3686 N N   . LEU B 1 203 ? 3.30600   -16.79100 -15.39600 1.000 34.18000 ? 205 LEU B N   1 
ATOM   3687 C CA  . LEU B 1 203 ? 2.35500   -17.88000 -15.60700 1.000 35.59000 ? 205 LEU B CA  1 
ATOM   3688 C C   . LEU B 1 203 ? 0.93000   -17.35300 -15.67400 1.000 36.87000 ? 205 LEU B C   1 
ATOM   3689 O O   . LEU B 1 203 ? 0.16200   -17.72100 -16.57300 1.000 37.05000 ? 205 LEU B O   1 
ATOM   3690 C CB  . LEU B 1 203 ? 2.49900   -18.94000 -14.50700 1.000 35.02000 ? 205 LEU B CB  1 
ATOM   3691 C CG  . LEU B 1 203 ? 3.82000   -19.73500 -14.57000 1.000 37.00000 ? 205 LEU B CG  1 
ATOM   3692 C CD1 . LEU B 1 203 ? 4.01400   -20.57600 -13.30600 1.000 36.70000 ? 205 LEU B CD1 1 
ATOM   3693 C CD2 . LEU B 1 203 ? 3.90800   -20.61400 -15.83000 1.000 36.45000 ? 205 LEU B CD2 1 
ATOM   3694 N N   . ALA B 1 204 ? 0.56200   -16.46200 -14.74500 1.000 34.93000 ? 206 ALA B N   1 
ATOM   3695 C CA  . ALA B 1 204 ? -0.78000  -15.87900 -14.75900 1.000 35.82000 ? 206 ALA B CA  1 
ATOM   3696 C C   . ALA B 1 204 ? -1.04700  -15.14600 -16.06300 1.000 37.18000 ? 206 ALA B C   1 
ATOM   3697 O O   . ALA B 1 204 ? -2.15500  -15.19600 -16.60200 1.000 39.54000 ? 206 ALA B O   1 
ATOM   3698 C CB  . ALA B 1 204 ? -0.96500  -14.92700 -13.57500 1.000 37.25000 ? 206 ALA B CB  1 
ATOM   3699 N N   . TRP B 1 205 ? -0.03800  -14.45900 -16.58400 1.000 38.34000 ? 207 TRP B N   1 
ATOM   3700 C CA  . TRP B 1 205 ? -0.19800  -13.72000 -17.83000 1.000 39.72000 ? 207 TRP B CA  1 
ATOM   3701 C C   . TRP B 1 205 ? -0.28700  -14.65400 -19.03700 1.000 41.05000 ? 207 TRP B C   1 
ATOM   3702 O O   . TRP B 1 205 ? -0.95200  -14.32400 -20.02800 1.000 39.83000 ? 207 TRP B O   1 
ATOM   3703 C CB  . TRP B 1 205 ? 0.96600   -12.74000 -17.96200 1.000 40.43000 ? 207 TRP B CB  1 
ATOM   3704 C CG  . TRP B 1 205 ? 0.96100   -11.89700 -19.18000 1.000 43.80000 ? 207 TRP B CG  1 
ATOM   3705 C CD1 . TRP B 1 205 ? 0.16000   -10.81200 -19.43600 1.000 48.52000 ? 207 TRP B CD1 1 
ATOM   3706 C CD2 . TRP B 1 205 ? 1.83300   -12.02400 -20.29400 1.000 47.65000 ? 207 TRP B CD2 1 
ATOM   3707 N NE1 . TRP B 1 205 ? 0.47600   -10.27000 -20.65400 1.000 49.51000 ? 207 TRP B NE1 1 
ATOM   3708 C CE2 . TRP B 1 205 ? 1.49900   -10.99800 -21.20600 1.000 48.81000 ? 207 TRP B CE2 1 
ATOM   3709 C CE3 . TRP B 1 205 ? 2.85900   -12.91500 -20.62300 1.000 48.19000 ? 207 TRP B CE3 1 
ATOM   3710 C CZ2 . TRP B 1 205 ? 2.14700   -10.84600 -22.42400 1.000 54.85000 ? 207 TRP B CZ2 1 
ATOM   3711 C CZ3 . TRP B 1 205 ? 3.50200   -12.76100 -21.83300 1.000 54.22000 ? 207 TRP B CZ3 1 
ATOM   3712 C CH2 . TRP B 1 205 ? 3.14900   -11.73000 -22.71800 1.000 55.55000 ? 207 TRP B CH2 1 
ATOM   3713 N N   . LEU B 1 206 ? 0.36800   -15.81900 -18.98000 1.000 37.04000 ? 208 LEU B N   1 
ATOM   3714 C CA  . LEU B 1 206 ? 0.15600   -16.82700 -20.01800 1.000 41.13000 ? 208 LEU B CA  1 
ATOM   3715 C C   . LEU B 1 206 ? -1.25400  -17.41200 -19.94500 1.000 42.08000 ? 208 LEU B C   1 
ATOM   3716 O O   . LEU B 1 206 ? -1.84600  -17.74100 -20.98000 1.000 42.12000 ? 208 LEU B O   1 
ATOM   3717 C CB  . LEU B 1 206 ? 1.20000   -17.93600 -19.90800 1.000 36.87000 ? 208 LEU B CB  1 
ATOM   3718 C CG  . LEU B 1 206 ? 2.64100   -17.51800 -20.19400 1.000 39.11000 ? 208 LEU B CG  1 
ATOM   3719 C CD1 . LEU B 1 206 ? 3.62400   -18.66400 -19.87700 1.000 39.84000 ? 208 LEU B CD1 1 
ATOM   3720 C CD2 . LEU B 1 206 ? 2.81700   -17.01100 -21.63500 1.000 36.42000 ? 208 LEU B CD2 1 
ATOM   3721 N N   . TYR B 1 207 ? -1.81600  -17.51800 -18.75500 1.000 36.83000 ? 209 TYR B N   1 
ATOM   3722 C CA  . TYR B 1 207 ? -3.15800  -17.98500 -18.60400 1.000 44.11000 ? 209 TYR B CA  1 
ATOM   3723 C C   . TYR B 1 207 ? -4.10400  -16.97000 -19.23900 1.000 47.87000 ? 209 TYR B C   1 
ATOM   3724 O O   . TYR B 1 207 ? -5.00100  -17.31900 -19.94000 1.000 47.06000 ? 209 TYR B O   1 
ATOM   3725 C CB  . TYR B 1 207 ? -3.52200  -18.26800 -17.17100 1.000 40.25000 ? 209 TYR B CB  1 
ATOM   3726 C CG  . TYR B 1 207 ? -3.13700  -19.63500 -16.68200 1.000 43.97000 ? 209 TYR B CG  1 
ATOM   3727 C CD1 . TYR B 1 207 ? -3.78700  -20.78500 -17.12200 1.000 46.12000 ? 209 TYR B CD1 1 
ATOM   3728 C CD2 . TYR B 1 207 ? -2.17000  -19.78500 -15.76000 1.000 39.83000 ? 209 TYR B CD2 1 
ATOM   3729 C CE1 . TYR B 1 207 ? -3.43500  -22.01200 -16.65600 1.000 44.29000 ? 209 TYR B CE1 1 
ATOM   3730 C CE2 . TYR B 1 207 ? -1.81800  -20.99800 -15.30300 1.000 42.60000 ? 209 TYR B CE2 1 
ATOM   3731 C CZ  . TYR B 1 207 ? -2.44200  -22.11400 -15.75200 1.000 44.44000 ? 209 TYR B CZ  1 
ATOM   3732 O OH  . TYR B 1 207 ? -2.04100  -23.27300 -15.27800 1.000 40.95000 ? 209 TYR B OH  1 
ATOM   3733 N N   . ALA B 1 208 ? -3.85100  -15.70400 -19.00800 1.000 44.54000 ? 210 ALA B N   1 
ATOM   3734 C CA  . ALA B 1 208 ? -4.64500  -14.66100 -19.56000 1.000 46.65000 ? 210 ALA B CA  1 
ATOM   3735 C C   . ALA B 1 208 ? -4.56000  -14.71100 -21.06200 1.000 47.65000 ? 210 ALA B C   1 
ATOM   3736 O O   . ALA B 1 208 ? -5.47900  -14.45100 -21.70500 1.000 49.70000 ? 210 ALA B O   1 
ATOM   3737 C CB  . ALA B 1 208 ? -4.18800  -13.34100 -19.03600 1.000 46.35000 ? 210 ALA B CB  1 
ATOM   3738 N N   . ALA B 1 209 ? -3.41300  -15.02000 -21.59200 1.000 46.34000 ? 211 ALA B N   1 
ATOM   3739 C CA  . ALA B 1 209 ? -3.24600  -15.13100 -23.03800 1.000 49.22000 ? 211 ALA B CA  1 
ATOM   3740 C C   . ALA B 1 209 ? -4.08400  -16.26800 -23.60500 1.000 49.74000 ? 211 ALA B C   1 
ATOM   3741 O O   . ALA B 1 209 ? -4.70300  -16.12100 -24.66200 1.000 53.08000 ? 211 ALA B O   1 
ATOM   3742 C CB  . ALA B 1 209 ? -1.77400  -15.33800 -23.37800 1.000 48.47000 ? 211 ALA B CB  1 
ATOM   3743 N N   . VAL B 1 210 ? -4.11400  -17.40500 -22.90700 1.000 50.16000 ? 212 VAL B N   1 
ATOM   3744 C CA  . VAL B 1 210 ? -4.97500  -18.51900 -23.29700 1.000 53.57000 ? 212 VAL B CA  1 
ATOM   3745 C C   . VAL B 1 210 ? -6.44500  -18.11200 -23.23800 1.000 55.15000 ? 212 VAL B C   1 
ATOM   3746 O O   . VAL B 1 210 ? -7.22300  -18.39900 -24.15600 1.000 55.97000 ? 212 VAL B O   1 
ATOM   3747 C CB  . VAL B 1 210 ? -4.70000  -19.74100 -22.40400 1.000 48.54000 ? 212 VAL B CB  1 
ATOM   3748 C CG1 . VAL B 1 210 ? -5.82500  -20.75900 -22.55300 1.000 51.17000 ? 212 VAL B CG1 1 
ATOM   3749 C CG2 . VAL B 1 210 ? -3.34300  -20.34800 -22.74200 1.000 45.90000 ? 212 VAL B CG2 1 
ATOM   3750 N N   . ILE B 1 211 ? -6.84800  -17.46100 -22.14100 1.000 51.96000 ? 213 ILE B N   1 
ATOM   3751 C CA  . ILE B 1 211 ? -8.22400  -16.98300 -21.99200 1.000 54.19000 ? 213 ILE B CA  1 
ATOM   3752 C C   . ILE B 1 211 ? -8.58300  -16.02000 -23.11400 1.000 56.51000 ? 213 ILE B C   1 
ATOM   3753 O O   . ILE B 1 211 ? -9.74600  -15.92900 -23.52300 1.000 60.65000 ? 213 ILE B O   1 
ATOM   3754 C CB  . ILE B 1 211 ? -8.41000  -16.33900 -20.60100 1.000 54.67000 ? 213 ILE B CB  1 
ATOM   3755 C CG1 . ILE B 1 211 ? -8.27900  -17.39900 -19.50700 1.000 53.81000 ? 213 ILE B CG1 1 
ATOM   3756 C CG2 . ILE B 1 211 ? -9.74800  -15.63200 -20.49300 1.000 56.88000 ? 213 ILE B CG2 1 
ATOM   3757 C CD1 . ILE B 1 211 ? -8.44300  -16.85700 -18.10300 1.000 52.41000 ? 213 ILE B CD1 1 
ATOM   3758 N N   . ASN B 1 212 ? -7.59400  -15.32000 -23.65400 1.000 58.56000 ? 214 ASN B N   1 
ATOM   3759 C CA  . ASN B 1 212 ? -7.77700  -14.37800 -24.74800 1.000 62.77000 ? 214 ASN B CA  1 
ATOM   3760 C C   . ASN B 1 212 ? -7.62400  -15.01600 -26.13200 1.000 62.43000 ? 214 ASN B C   1 
ATOM   3761 O O   . ASN B 1 212 ? -7.59400  -14.29400 -27.13400 1.000 62.49000 ? 214 ASN B O   1 
ATOM   3762 C CB  . ASN B 1 212 ? -6.78100  -13.22300 -24.60000 1.000 62.85000 ? 214 ASN B CB  1 
ATOM   3763 C CG  . ASN B 1 212 ? -7.35300  -11.90300 -25.05000 1.000 71.05000 ? 214 ASN B CG  1 
ATOM   3764 O OD1 . ASN B 1 212 ? -6.88000  -11.30900 -26.02300 1.000 75.50000 ? 214 ASN B OD1 1 
ATOM   3765 N ND2 . ASN B 1 212 ? -8.38800  -11.43400 -24.35300 1.000 67.71000 ? 214 ASN B ND2 1 
ATOM   3766 N N   . GLY B 1 213 ? -7.51700  -16.34000 -26.21300 1.000 58.77000 ? 215 GLY B N   1 
ATOM   3767 C CA  . GLY B 1 213 ? -7.43900  -17.01800 -27.49200 1.000 57.95000 ? 215 GLY B CA  1 
ATOM   3768 C C   . GLY B 1 213 ? -6.05100  -17.22900 -28.05200 1.000 60.70000 ? 215 GLY B C   1 
ATOM   3769 O O   . GLY B 1 213 ? -5.92500  -17.67600 -29.19800 1.000 60.90000 ? 215 GLY B O   1 
ATOM   3770 N N   . ASP B 1 214 ? -5.00700  -16.90900 -27.32200 1.000 61.00000 ? 216 ASP B N   1 
ATOM   3771 C CA  . ASP B 1 214 ? -3.68000  -17.11200 -27.81100 1.000 59.97000 ? 216 ASP B CA  1 
ATOM   3772 C C   . ASP B 1 214 ? -3.28500  -18.44400 -27.26000 1.000 61.04000 ? 216 ASP B C   1 
ATOM   3773 O O   . ASP B 1 214 ? -3.23200  -18.61200 -26.08200 1.000 60.29000 ? 216 ASP B O   1 
ATOM   3774 C CB  . ASP B 1 214 ? -2.78000  -16.05300 -27.26700 1.000 62.36000 ? 216 ASP B CB  1 
ATOM   3775 C CG  . ASP B 1 214 ? -2.21300  -15.16700 -28.32100 1.000 68.20000 ? 216 ASP B CG  1 
ATOM   3776 O OD1 . ASP B 1 214 ? -2.12000  -15.55000 -29.47200 1.000 72.00000 ? 216 ASP B OD1 1 
ATOM   3777 O OD2 . ASP B 1 214 ? -1.81800  -14.07000 -27.99600 1.000 70.59000 ? 216 ASP B OD2 1 
ATOM   3778 N N   . ARG B 1 215 ? -3.03600  -19.40000 -28.13200 1.000 56.83000 ? 217 ARG B N   1 
ATOM   3779 C CA  . ARG B 1 215 ? -2.71700  -20.73800 -27.74300 1.000 52.60000 ? 217 ARG B CA  1 
ATOM   3780 C C   . ARG B 1 215 ? -1.51100  -21.39500 -28.37200 1.000 54.10000 ? 217 ARG B C   1 
ATOM   3781 O O   . ARG B 1 215 ? -1.28000  -22.53300 -28.14200 1.000 53.67000 ? 217 ARG B O   1 
ATOM   3782 C CB  . ARG B 1 215 ? -3.96100  -21.60400 -27.96500 1.000 57.81000 ? 217 ARG B CB  1 
ATOM   3783 C CG  . ARG B 1 215 ? -5.21000  -21.04000 -27.32300 1.000 58.58000 ? 217 ARG B CG  1 
ATOM   3784 C CD  . ARG B 1 215 ? -6.40000  -21.96800 -27.28900 1.000 64.11000 ? 217 ARG B CD  1 
ATOM   3785 N NE  . ARG B 1 215 ? -6.07400  -23.26300 -26.72300 1.000 66.11000 ? 217 ARG B NE  1 
ATOM   3786 C CZ  . ARG B 1 215 ? -6.63400  -23.81300 -25.65900 1.000 63.10000 ? 217 ARG B CZ  1 
ATOM   3787 N NH1 . ARG B 1 215 ? -6.24200  -25.00800 -25.28100 1.000 56.82000 ? 217 ARG B NH1 1 
ATOM   3788 N NH2 . ARG B 1 215 ? -7.58700  -23.19200 -25.00600 1.000 63.48000 ? 217 ARG B NH2 1 
ATOM   3789 N N   . TRP B 1 216 ? -0.74700  -20.67700 -29.15900 1.000 52.75000 ? 218 TRP B N   1 
ATOM   3790 C CA  . TRP B 1 216 ? 0.37200   -21.25400 -29.84200 1.000 50.46000 ? 218 TRP B CA  1 
ATOM   3791 C C   . TRP B 1 216 ? 1.46500   -21.80300 -28.98900 1.000 53.46000 ? 218 TRP B C   1 
ATOM   3792 O O   . TRP B 1 216 ? 2.10800   -22.71800 -29.37000 1.000 51.58000 ? 218 TRP B O   1 
ATOM   3793 C CB  . TRP B 1 216 ? 0.93000   -20.32700 -30.88000 1.000 55.09000 ? 218 TRP B CB  1 
ATOM   3794 C CG  . TRP B 1 216 ? 1.56500   -19.19500 -30.40000 1.000 55.90000 ? 218 TRP B CG  1 
ATOM   3795 C CD1 . TRP B 1 216 ? 1.03700   -18.00400 -30.27900 1.000 58.79000 ? 218 TRP B CD1 1 
ATOM   3796 C CD2 . TRP B 1 216 ? 2.89600   -19.08900 -29.96600 1.000 58.81000 ? 218 TRP B CD2 1 
ATOM   3797 N NE1 . TRP B 1 216 ? 1.92900   -17.12700 -29.79200 1.000 58.63000 ? 218 TRP B NE1 1 
ATOM   3798 C CE2 . TRP B 1 216 ? 3.09300   -17.77700 -29.58600 1.000 58.50000 ? 218 TRP B CE2 1 
ATOM   3799 C CE3 . TRP B 1 216 ? 3.94300   -19.98200 -29.84500 1.000 56.11000 ? 218 TRP B CE3 1 
ATOM   3800 C CZ2 . TRP B 1 216 ? 4.26000   -17.33400 -29.12000 1.000 60.11000 ? 218 TRP B CZ2 1 
ATOM   3801 C CZ3 . TRP B 1 216 ? 5.07600   -19.54700 -29.38000 1.000 57.32000 ? 218 TRP B CZ3 1 
ATOM   3802 C CH2 . TRP B 1 216 ? 5.25300   -18.22900 -29.03700 1.000 63.22000 ? 218 TRP B CH2 1 
ATOM   3803 N N   . PHE B 1 217 ? 1.71500   -21.18600 -27.86200 1.000 50.60000 ? 219 PHE B N   1 
ATOM   3804 C CA  . PHE B 1 217 ? 2.74700   -21.60200 -26.96500 1.000 47.30000 ? 219 PHE B CA  1 
ATOM   3805 C C   . PHE B 1 217 ? 2.41300   -22.84100 -26.20000 1.000 46.04000 ? 219 PHE B C   1 
ATOM   3806 O O   . PHE B 1 217 ? 3.25000   -23.37400 -25.60600 1.000 48.39000 ? 219 PHE B O   1 
ATOM   3807 C CB  . PHE B 1 217 ? 3.14600   -20.48600 -26.03000 1.000 49.28000 ? 219 PHE B CB  1 
ATOM   3808 C CG  . PHE B 1 217 ? 2.01700   -19.93300 -25.26300 1.000 48.13000 ? 219 PHE B CG  1 
ATOM   3809 C CD1 . PHE B 1 217 ? 1.62500   -20.50000 -24.10500 1.000 44.99000 ? 219 PHE B CD1 1 
ATOM   3810 C CD2 . PHE B 1 217 ? 1.33400   -18.85700 -25.73100 1.000 48.35000 ? 219 PHE B CD2 1 
ATOM   3811 C CE1 . PHE B 1 217 ? 0.58700   -19.99200 -23.40900 1.000 42.82000 ? 219 PHE B CE1 1 
ATOM   3812 C CE2 . PHE B 1 217 ? 0.28900   -18.34600 -25.05100 1.000 47.11000 ? 219 PHE B CE2 1 
ATOM   3813 C CZ  . PHE B 1 217 ? -0.08400  -18.92000 -23.88900 1.000 47.45000 ? 219 PHE B CZ  1 
ATOM   3814 N N   . LEU B 1 218 ? 1.18800   -23.26400 -26.23700 1.000 45.50000 ? 220 LEU B N   1 
ATOM   3815 C CA  . LEU B 1 218 ? 0.78700   -24.42800 -25.54200 1.000 46.24000 ? 220 LEU B CA  1 
ATOM   3816 C C   . LEU B 1 218 ? 1.37700   -25.64100 -26.17500 1.000 50.67000 ? 220 LEU B C   1 
ATOM   3817 O O   . LEU B 1 218 ? 1.46600   -25.72700 -27.34200 1.000 51.39000 ? 220 LEU B O   1 
ATOM   3818 C CB  . LEU B 1 218 ? -0.69600  -24.53700 -25.53200 1.000 47.08000 ? 220 LEU B CB  1 
ATOM   3819 C CG  . LEU B 1 218 ? -1.46100  -23.51100 -24.73400 1.000 48.60000 ? 220 LEU B CG  1 
ATOM   3820 C CD1 . LEU B 1 218 ? -2.89400  -23.80600 -24.94900 1.000 54.41000 ? 220 LEU B CD1 1 
ATOM   3821 C CD2 . LEU B 1 218 ? -1.16800  -23.54400 -23.27200 1.000 43.05000 ? 220 LEU B CD2 1 
ATOM   3822 N N   . ASN B 1 219 ? 1.78100   -26.58000 -25.37000 1.000 51.50000 ? 221 ASN B N   1 
ATOM   3823 C CA  . ASN B 1 219 ? 2.36300   -27.80200 -25.87200 1.000 50.49000 ? 221 ASN B CA  1 
ATOM   3824 C C   . ASN B 1 219 ? 1.85600   -29.04200 -25.17500 1.000 47.61000 ? 221 ASN B C   1 
ATOM   3825 O O   . ASN B 1 219 ? 1.11800   -28.95500 -24.27600 1.000 46.55000 ? 221 ASN B O   1 
ATOM   3826 C CB  . ASN B 1 219 ? 3.86700   -27.71300 -25.96000 1.000 47.79000 ? 221 ASN B CB  1 
ATOM   3827 C CG  . ASN B 1 219 ? 4.52800   -27.62300 -24.65000 1.000 44.97000 ? 221 ASN B CG  1 
ATOM   3828 O OD1 . ASN B 1 219 ? 4.00600   -28.00100 -23.67500 1.000 50.16000 ? 221 ASN B OD1 1 
ATOM   3829 N ND2 . ASN B 1 219 ? 5.70000   -27.14100 -24.65000 1.000 48.45000 ? 221 ASN B ND2 1 
ATOM   3830 N N   . ARG B 1 220 ? 2.21200   -30.19600 -25.67300 1.000 49.24000 ? 222 ARG B N   1 
ATOM   3831 C CA  . ARG B 1 220 ? 1.79000   -31.46300 -25.11200 1.000 50.42000 ? 222 ARG B CA  1 
ATOM   3832 C C   . ARG B 1 220 ? 2.43700   -31.93400 -23.80800 1.000 47.90000 ? 222 ARG B C   1 
ATOM   3833 O O   . ARG B 1 220 ? 1.94100   -32.77900 -23.15300 1.000 47.92000 ? 222 ARG B O   1 
ATOM   3834 C CB  . ARG B 1 220 ? 1.87900   -32.53700 -26.17100 1.000 50.19000 ? 222 ARG B CB  1 
ATOM   3835 C CG  . ARG B 1 220 ? 3.18600   -33.25200 -26.21300 1.000 47.94000 ? 222 ARG B CG  1 
ATOM   3836 C CD  . ARG B 1 220 ? 3.40300   -34.03300 -27.46200 1.000 50.10000 ? 222 ARG B CD  1 
ATOM   3837 N NE  . ARG B 1 220 ? 2.33800   -34.92600 -27.75500 1.000 49.81000 ? 222 ARG B NE  1 
ATOM   3838 C CZ  . ARG B 1 220 ? 1.74300   -34.97900 -28.90700 1.000 49.32000 ? 222 ARG B CZ  1 
ATOM   3839 N NH1 . ARG B 1 220 ? 2.13400   -34.19600 -29.87400 1.000 52.62000 ? 222 ARG B NH1 1 
ATOM   3840 N NH2 . ARG B 1 220 ? 0.78900   -35.83000 -29.09500 1.000 44.47000 ? 222 ARG B NH2 1 
ATOM   3841 N N   . PHE B 1 221 ? 3.57300   -31.39000 -23.49400 1.000 47.96000 ? 223 PHE B N   1 
ATOM   3842 C CA  . PHE B 1 221 ? 4.34700   -31.77300 -22.35600 1.000 47.29000 ? 223 PHE B CA  1 
ATOM   3843 C C   . PHE B 1 221 ? 4.04000   -31.24100 -20.96400 1.000 53.86000 ? 223 PHE B C   1 
ATOM   3844 O O   . PHE B 1 221 ? 3.29900   -30.31400 -20.80400 1.000 49.99000 ? 223 PHE B O   1 
ATOM   3845 C CB  . PHE B 1 221 ? 5.79800   -31.57500 -22.72600 1.000 48.86000 ? 223 PHE B CB  1 
ATOM   3846 C CG  . PHE B 1 221 ? 6.16000   -32.19800 -24.05000 1.000 48.24000 ? 223 PHE B CG  1 
ATOM   3847 C CD1 . PHE B 1 221 ? 6.09900   -33.54000 -24.22400 1.000 44.72000 ? 223 PHE B CD1 1 
ATOM   3848 C CD2 . PHE B 1 221 ? 6.51700   -31.43400 -25.12100 1.000 46.44000 ? 223 PHE B CD2 1 
ATOM   3849 C CE1 . PHE B 1 221 ? 6.39300   -34.10400 -25.42200 1.000 45.58000 ? 223 PHE B CE1 1 
ATOM   3850 C CE2 . PHE B 1 221 ? 6.82200   -32.00200 -26.31400 1.000 43.61000 ? 223 PHE B CE2 1 
ATOM   3851 C CZ  . PHE B 1 221 ? 6.76200   -33.33200 -26.46500 1.000 44.99000 ? 223 PHE B CZ  1 
ATOM   3852 N N   . THR B 1 222 ? 4.60000   -31.90000 -19.96700 1.000 53.54000 ? 224 THR B N   1 
ATOM   3853 C CA  . THR B 1 222 ? 4.55900   -31.47000 -18.57800 1.000 51.52000 ? 224 THR B CA  1 
ATOM   3854 C C   . THR B 1 222 ? 5.99200   -31.46600 -18.06000 1.000 52.14000 ? 224 THR B C   1 
ATOM   3855 O O   . THR B 1 222 ? 6.87400   -32.12100 -18.62100 1.000 54.47000 ? 224 THR B O   1 
ATOM   3856 C CB  . THR B 1 222 ? 3.64800   -32.38800 -17.73400 1.000 53.03000 ? 224 THR B CB  1 
ATOM   3857 O OG1 . THR B 1 222 ? 2.28200   -32.10400 -18.03500 1.000 53.20000 ? 224 THR B OG1 1 
ATOM   3858 C CG2 . THR B 1 222 ? 3.83900   -32.19900 -16.23100 1.000 53.94000 ? 224 THR B CG2 1 
ATOM   3859 N N   . THR B 1 223 ? 6.24100   -30.67400 -17.02100 1.000 50.46000 ? 225 THR B N   1 
ATOM   3860 C CA  . THR B 1 223 ? 7.52600   -30.69000 -16.34000 1.000 50.29000 ? 225 THR B CA  1 
ATOM   3861 C C   . THR B 1 223 ? 7.28300   -30.87300 -14.84700 1.000 51.36000 ? 225 THR B C   1 
ATOM   3862 O O   . THR B 1 223 ? 6.14100   -30.87900 -14.37700 1.000 51.78000 ? 225 THR B O   1 
ATOM   3863 C CB  . THR B 1 223 ? 8.33800   -29.41300 -16.64400 1.000 51.81000 ? 225 THR B CB  1 
ATOM   3864 O OG1 . THR B 1 223 ? 9.67700   -29.54700 -16.14600 1.000 55.75000 ? 225 THR B OG1 1 
ATOM   3865 C CG2 . THR B 1 223 ? 7.68800   -28.18500 -16.03600 1.000 49.19000 ? 225 THR B CG2 1 
ATOM   3866 N N   . THR B 1 224 ? 8.34600   -30.96700 -14.11600 1.000 51.02000 ? 226 THR B N   1 
ATOM   3867 C CA  . THR B 1 224 ? 8.27100   -31.07600 -12.70600 1.000 56.44000 ? 226 THR B CA  1 
ATOM   3868 C C   . THR B 1 224 ? 8.69700   -29.76500 -12.10900 1.000 55.33000 ? 226 THR B C   1 
ATOM   3869 O O   . THR B 1 224 ? 9.37500   -28.99700 -12.72700 1.000 50.58000 ? 226 THR B O   1 
ATOM   3870 C CB  . THR B 1 224 ? 9.20600   -32.13700 -12.14200 1.000 55.62000 ? 226 THR B CB  1 
ATOM   3871 O OG1 . THR B 1 224 ? 10.55200  -31.74700 -12.35200 1.000 54.94000 ? 226 THR B OG1 1 
ATOM   3872 C CG2 . THR B 1 224 ? 8.95500   -33.40700 -12.77400 1.000 56.51000 ? 226 THR B CG2 1 
ATOM   3873 N N   . LEU B 1 225 ? 8.29800   -29.56700 -10.86900 1.000 55.84000 ? 227 LEU B N   1 
ATOM   3874 C CA  . LEU B 1 225 ? 8.63300   -28.35400 -10.17300 1.000 57.10000 ? 227 LEU B CA  1 
ATOM   3875 C C   . LEU B 1 225 ? 10.10800  -28.23200 -10.09700 1.000 58.03000 ? 227 LEU B C   1 
ATOM   3876 O O   . LEU B 1 225 ? 10.63000  -27.18300 -10.32500 1.000 59.34000 ? 227 LEU B O   1 
ATOM   3877 C CB  . LEU B 1 225 ? 8.04900   -28.38400 -8.79400  1.000 59.22000 ? 227 LEU B CB  1 
ATOM   3878 C CG  . LEU B 1 225 ? 7.75700   -27.08200 -8.09800  1.000 58.09000 ? 227 LEU B CG  1 
ATOM   3879 C CD1 . LEU B 1 225 ? 7.10700   -26.15700 -9.08000  1.000 57.33000 ? 227 LEU B CD1 1 
ATOM   3880 C CD2 . LEU B 1 225 ? 6.81200   -27.35200 -6.96800  1.000 54.98000 ? 227 LEU B CD2 1 
ATOM   3881 N N   . ASN B 1 226 ? 10.78400  -29.31900 -9.80100  1.000 57.44000 ? 228 ASN B N   1 
ATOM   3882 C CA  . ASN B 1 226 ? 12.21700  -29.27900 -9.75200  1.000 58.58000 ? 228 ASN B CA  1 
ATOM   3883 C C   . ASN B 1 226 ? 12.91200  -29.01100 -11.07700 1.000 60.45000 ? 228 ASN B C   1 
ATOM   3884 O O   . ASN B 1 226 ? 13.78400  -28.20500 -11.13300 1.000 60.74000 ? 228 ASN B O   1 
ATOM   3885 C CB  . ASN B 1 226 ? 12.78800  -30.53800 -9.13000  1.000 62.27000 ? 228 ASN B CB  1 
ATOM   3886 C CG  . ASN B 1 226 ? 11.86100  -31.16400 -8.14200  1.000 65.43000 ? 228 ASN B CG  1 
ATOM   3887 O OD1 . ASN B 1 226 ? 10.67400  -31.29900 -8.40600  1.000 69.84000 ? 228 ASN B OD1 1 
ATOM   3888 N ND2 . ASN B 1 226 ? 12.37200  -31.53100 -7.02100  1.000 68.37000 ? 228 ASN B ND2 1 
ATOM   3889 N N   . ASP B 1 227 ? 12.50400  -29.67300 -12.14000 1.000 57.41000 ? 229 ASP B N   1 
ATOM   3890 C CA  . ASP B 1 227 ? 13.14100  -29.49100 -13.40700 1.000 58.52000 ? 229 ASP B CA  1 
ATOM   3891 C C   . ASP B 1 227 ? 12.94600  -28.08500 -13.81200 1.000 56.66000 ? 229 ASP B C   1 
ATOM   3892 O O   . ASP B 1 227 ? 13.79100  -27.52200 -14.39500 1.000 57.19000 ? 229 ASP B O   1 
ATOM   3893 C CB  . ASP B 1 227 ? 12.58600  -30.41300 -14.49300 1.000 64.70000 ? 229 ASP B CB  1 
ATOM   3894 C CG  . ASP B 1 227 ? 12.99800  -31.88600 -14.32900 1.000 66.76000 ? 229 ASP B CG  1 
ATOM   3895 O OD1 . ASP B 1 227 ? 14.17200  -32.15200 -14.13500 1.000 73.59000 ? 229 ASP B OD1 1 
ATOM   3896 O OD2 . ASP B 1 227 ? 12.14900  -32.75400 -14.41500 1.000 64.65000 ? 229 ASP B OD2 1 
ATOM   3897 N N   . PHE B 1 228 ? 11.79100  -27.54200 -13.54600 1.000 53.72000 ? 230 PHE B N   1 
ATOM   3898 C CA  . PHE B 1 228 ? 11.51000  -26.16700 -13.91600 1.000 56.31000 ? 230 PHE B CA  1 
ATOM   3899 C C   . PHE B 1 228 ? 12.36000  -25.14900 -13.21800 1.000 54.35000 ? 230 PHE B C   1 
ATOM   3900 O O   . PHE B 1 228 ? 12.88300  -24.28000 -13.79400 1.000 57.77000 ? 230 PHE B O   1 
ATOM   3901 C CB  . PHE B 1 228 ? 10.04900  -25.84800 -13.68900 1.000 52.57000 ? 230 PHE B CB  1 
ATOM   3902 C CG  . PHE B 1 228 ? 9.70300   -24.45400 -14.00300 1.000 50.08000 ? 230 PHE B CG  1 
ATOM   3903 C CD1 . PHE B 1 228 ? 9.57600   -24.05900 -15.26500 1.000 50.55000 ? 230 PHE B CD1 1 
ATOM   3904 C CD2 . PHE B 1 228 ? 9.54500   -23.55100 -13.02200 1.000 51.68000 ? 230 PHE B CD2 1 
ATOM   3905 C CE1 . PHE B 1 228 ? 9.27200   -22.78000 -15.58100 1.000 51.41000 ? 230 PHE B CE1 1 
ATOM   3906 C CE2 . PHE B 1 228 ? 9.25000   -22.26500 -13.30700 1.000 53.23000 ? 230 PHE B CE2 1 
ATOM   3907 C CZ  . PHE B 1 228 ? 9.12000   -21.87000 -14.60300 1.000 55.11000 ? 230 PHE B CZ  1 
ATOM   3908 N N   . ASN B 1 229 ? 12.54300  -25.31400 -11.95700 1.000 55.77000 ? 231 ASN B N   1 
ATOM   3909 C CA  . ASN B 1 229 ? 13.26500  -24.32100 -11.17000 1.000 58.96000 ? 231 ASN B CA  1 
ATOM   3910 C C   . ASN B 1 229 ? 14.73600  -24.24500 -11.55400 1.000 59.00000 ? 231 ASN B C   1 
ATOM   3911 O O   . ASN B 1 229 ? 15.36900  -23.19700 -11.36700 1.000 59.27000 ? 231 ASN B O   1 
ATOM   3912 C CB  . ASN B 1 229 ? 13.08800  -24.62200 -9.68500  1.000 55.36000 ? 231 ASN B CB  1 
ATOM   3913 C CG  . ASN B 1 229 ? 11.75800  -24.12400 -9.16700  1.000 53.66000 ? 231 ASN B CG  1 
ATOM   3914 O OD1 . ASN B 1 229 ? 11.24700  -23.11600 -9.64900  1.000 53.01000 ? 231 ASN B OD1 1 
ATOM   3915 N ND2 . ASN B 1 229 ? 11.18200  -24.82900 -8.20100  1.000 53.74000 ? 231 ASN B ND2 1 
ATOM   3916 N N   . LEU B 1 230 ? 15.28900  -25.32500 -12.11400 1.000 61.19000 ? 232 LEU B N   1 
ATOM   3917 C CA  . LEU B 1 230 ? 16.65500  -25.26800 -12.62500 1.000 58.77000 ? 232 LEU B CA  1 
ATOM   3918 C C   . LEU B 1 230 ? 16.72500  -24.43200 -13.89600 1.000 60.34000 ? 232 LEU B C   1 
ATOM   3919 O O   . LEU B 1 230 ? 17.65800  -23.63800 -14.08100 1.000 59.82000 ? 232 LEU B O   1 
ATOM   3920 C CB  . LEU B 1 230 ? 17.17500  -26.68400 -12.86900 1.000 63.05000 ? 232 LEU B CB  1 
ATOM   3921 N N   . VAL B 1 231 ? 15.73600  -24.59400 -14.77900 1.000 62.95000 ? 233 VAL B N   1 
ATOM   3922 C CA  . VAL B 1 231 ? 15.60800  -23.70300 -15.92900 1.000 59.11000 ? 233 VAL B CA  1 
ATOM   3923 C C   . VAL B 1 231 ? 15.38500  -22.27100 -15.45800 1.000 59.87000 ? 233 VAL B C   1 
ATOM   3924 O O   . VAL B 1 231 ? 15.98800  -21.32500 -15.98400 1.000 59.81000 ? 233 VAL B O   1 
ATOM   3925 C CB  . VAL B 1 231 ? 14.46500  -24.18600 -16.84300 1.000 60.73000 ? 233 VAL B CB  1 
ATOM   3926 C CG1 . VAL B 1 231 ? 14.46500  -23.41700 -18.16300 1.000 57.92000 ? 233 VAL B CG1 1 
ATOM   3927 C CG2 . VAL B 1 231 ? 14.57100  -25.68700 -17.07300 1.000 60.55000 ? 233 VAL B CG2 1 
ATOM   3928 N N   . ALA B 1 232 ? 14.54600  -22.10900 -14.45500 1.000 59.96000 ? 234 ALA B N   1 
ATOM   3929 C CA  . ALA B 1 232 ? 14.20300  -20.79900 -13.92100 1.000 59.16000 ? 234 ALA B CA  1 
ATOM   3930 C C   . ALA B 1 232 ? 15.39200  -20.10000 -13.36200 1.000 61.33000 ? 234 ALA B C   1 
ATOM   3931 O O   . ALA B 1 232 ? 15.64400  -18.97600 -13.65800 1.000 59.97000 ? 234 ALA B O   1 
ATOM   3932 C CB  . ALA B 1 232 ? 13.18100  -20.96800 -12.83200 1.000 54.52000 ? 234 ALA B CB  1 
ATOM   3933 N N   . MET B 1 233 ? 16.15200  -20.82300 -12.58900 1.000 62.52000 ? 235 MET B N   1 
ATOM   3934 C CA  . MET B 1 233 ? 17.32000  -20.28200 -12.00000 1.000 65.60000 ? 235 MET B CA  1 
ATOM   3935 C C   . MET B 1 233 ? 18.30600  -19.87200 -13.09000 1.000 66.05000 ? 235 MET B C   1 
ATOM   3936 O O   . MET B 1 233 ? 18.94600  -18.86600 -12.96200 1.000 69.38000 ? 235 MET B O   1 
ATOM   3937 C CB  . MET B 1 233 ? 17.88600  -21.25200 -10.98700 1.000 67.19000 ? 235 MET B CB  1 
ATOM   3938 N N   . LYS B 1 234 ? 18.42800  -20.63500 -14.15700 1.000 63.25000 ? 236 LYS B N   1 
ATOM   3939 C CA  . LYS B 1 234 ? 19.34000  -20.26900 -15.21800 1.000 63.56000 ? 236 LYS B CA  1 
ATOM   3940 C C   . LYS B 1 234 ? 18.95700  -19.01900 -15.96200 1.000 62.99000 ? 236 LYS B C   1 
ATOM   3941 O O   . LYS B 1 234 ? 19.77800  -18.38900 -16.54200 1.000 64.93000 ? 236 LYS B O   1 
ATOM   3942 C CB  . LYS B 1 234 ? 19.63100  -21.43000 -16.17600 1.000 67.07000 ? 236 LYS B CB  1 
ATOM   3943 N N   . TYR B 1 235 ? 17.69100  -18.68500 -15.97300 1.000 62.61000 ? 237 TYR B N   1 
ATOM   3944 C CA  . TYR B 1 235 ? 17.21100  -17.49600 -16.65200 1.000 58.82000 ? 237 TYR B CA  1 
ATOM   3945 C C   . TYR B 1 235 ? 16.87700  -16.26300 -15.79500 1.000 58.85000 ? 237 TYR B C   1 
ATOM   3946 O O   . TYR B 1 235 ? 16.29000  -15.34900 -16.27600 1.000 58.78000 ? 237 TYR B O   1 
ATOM   3947 C CB  . TYR B 1 235 ? 16.05300  -17.87200 -17.51800 1.000 61.91000 ? 237 TYR B CB  1 
ATOM   3948 C CG  . TYR B 1 235 ? 16.45200  -18.64700 -18.71200 1.000 63.01000 ? 237 TYR B CG  1 
ATOM   3949 C CD1 . TYR B 1 235 ? 16.90100  -17.99700 -19.80400 1.000 65.55000 ? 237 TYR B CD1 1 
ATOM   3950 C CD2 . TYR B 1 235 ? 16.40200  -19.99800 -18.74100 1.000 61.10000 ? 237 TYR B CD2 1 
ATOM   3951 C CE1 . TYR B 1 235 ? 17.29200  -18.66200 -20.90900 1.000 69.40000 ? 237 TYR B CE1 1 
ATOM   3952 C CE2 . TYR B 1 235 ? 16.79800  -20.68000 -19.85200 1.000 63.10000 ? 237 TYR B CE2 1 
ATOM   3953 C CZ  . TYR B 1 235 ? 17.23200  -19.98800 -20.93900 1.000 68.58000 ? 237 TYR B CZ  1 
ATOM   3954 O OH  . TYR B 1 235 ? 17.63900  -20.56000 -22.10300 1.000 72.78000 ? 237 TYR B OH  1 
ATOM   3955 N N   . ASN B 1 236 ? 17.27100  -16.27000 -14.54100 1.000 57.29000 ? 238 ASN B N   1 
ATOM   3956 C CA  . ASN B 1 236 ? 17.00800  -15.20300 -13.57200 1.000 57.28000 ? 238 ASN B CA  1 
ATOM   3957 C C   . ASN B 1 236 ? 15.50400  -15.04000 -13.34000 1.000 58.66000 ? 238 ASN B C   1 
ATOM   3958 O O   . ASN B 1 236 ? 14.94200  -13.94300 -13.44000 1.000 50.28000 ? 238 ASN B O   1 
ATOM   3959 C CB  . ASN B 1 236 ? 17.65200  -13.88200 -14.00200 1.000 56.83000 ? 238 ASN B CB  1 
ATOM   3960 C CG  . ASN B 1 236 ? 19.13500  -13.82200 -13.67900 1.000 65.48000 ? 238 ASN B CG  1 
ATOM   3961 O OD1 . ASN B 1 236 ? 19.96200  -13.65400 -14.57200 1.000 65.53000 ? 238 ASN B OD1 1 
ATOM   3962 N ND2 . ASN B 1 236 ? 19.47900  -13.96800 -12.40000 1.000 61.64000 ? 238 ASN B ND2 1 
ATOM   3963 N N   . TYR B 1 237 ? 14.85500  -16.16200 -13.04000 1.000 53.60000 ? 239 TYR B N   1 
ATOM   3964 C CA  . TYR B 1 237 ? 13.44400  -16.21900 -12.70600 1.000 51.16000 ? 239 TYR B CA  1 
ATOM   3965 C C   . TYR B 1 237 ? 13.32300  -16.65100 -11.25700 1.000 52.00000 ? 239 TYR B C   1 
ATOM   3966 O O   . TYR B 1 237 ? 14.06500  -17.52800 -10.80300 1.000 53.48000 ? 239 TYR B O   1 
ATOM   3967 C CB  . TYR B 1 237 ? 12.69700  -17.21500 -13.60100 1.000 48.37000 ? 239 TYR B CB  1 
ATOM   3968 C CG  . TYR B 1 237 ? 12.02500  -16.62100 -14.81500 1.000 44.37000 ? 239 TYR B CG  1 
ATOM   3969 C CD1 . TYR B 1 237 ? 12.76200  -15.98700 -15.80700 1.000 42.80000 ? 239 TYR B CD1 1 
ATOM   3970 C CD2 . TYR B 1 237 ? 10.64900  -16.71900 -14.98300 1.000 42.59000 ? 239 TYR B CD2 1 
ATOM   3971 C CE1 . TYR B 1 237 ? 12.14400  -15.45100 -16.92200 1.000 42.93000 ? 239 TYR B CE1 1 
ATOM   3972 C CE2 . TYR B 1 237 ? 10.02300  -16.19000 -16.09200 1.000 39.57000 ? 239 TYR B CE2 1 
ATOM   3973 C CZ  . TYR B 1 237 ? 10.77100  -15.55800 -17.06100 1.000 41.96000 ? 239 TYR B CZ  1 
ATOM   3974 O OH  . TYR B 1 237 ? 10.14500  -15.03600 -18.16800 1.000 43.24000 ? 239 TYR B OH  1 
ATOM   3975 N N   . GLU B 1 238 ? 12.39600  -16.03500 -10.53200 1.000 47.01000 ? 240 GLU B N   1 
ATOM   3976 C CA  . GLU B 1 238 ? 12.14500  -16.47200 -9.17300  1.000 50.43000 ? 240 GLU B CA  1 
ATOM   3977 C C   . GLU B 1 238 ? 11.75600  -17.95100 -9.18300  1.000 52.63000 ? 240 GLU B C   1 
ATOM   3978 O O   . GLU B 1 238 ? 11.17300  -18.44000 -10.15400 1.000 51.35000 ? 240 GLU B O   1 
ATOM   3979 C CB  . GLU B 1 238 ? 11.03900  -15.63500 -8.53200  1.000 47.59000 ? 240 GLU B CB  1 
ATOM   3980 C CG  . GLU B 1 238 ? 11.49300  -14.26400 -8.05000  1.000 50.60000 ? 240 GLU B CG  1 
ATOM   3981 C CD  . GLU B 1 238 ? 12.56900  -14.34100 -6.96200  1.000 54.98000 ? 240 GLU B CD  1 
ATOM   3982 O OE1 . GLU B 1 238 ? 13.70800  -13.88100 -7.21000  1.000 49.87000 ? 240 GLU B OE1 1 
ATOM   3983 O OE2 . GLU B 1 238 ? 12.26500  -14.85000 -5.85700  1.000 53.61000 ? 240 GLU B OE2 1 
ATOM   3984 N N   . PRO B 1 239 ? 12.10500  -18.69400 -8.13700  1.000 53.16000 ? 241 PRO B N   1 
ATOM   3985 C CA  . PRO B 1 239 ? 11.67000  -20.09200 -8.05700  1.000 49.98000 ? 241 PRO B CA  1 
ATOM   3986 C C   . PRO B 1 239 ? 10.17600  -20.20300 -7.79400  1.000 51.74000 ? 241 PRO B C   1 
ATOM   3987 O O   . PRO B 1 239 ? 9.55000   -19.32700 -7.19300  1.000 50.64000 ? 241 PRO B O   1 
ATOM   3988 C CB  . PRO B 1 239 ? 12.48800  -20.65200 -6.88700  1.000 53.32000 ? 241 PRO B CB  1 
ATOM   3989 C CG  . PRO B 1 239 ? 12.95800  -19.44700 -6.12600  1.000 52.32000 ? 241 PRO B CG  1 
ATOM   3990 C CD  . PRO B 1 239 ? 13.11600  -18.35800 -7.12100  1.000 49.50000 ? 241 PRO B CD  1 
ATOM   3991 N N   . LEU B 1 240 ? 9.57500   -21.28400 -8.22700  1.000 52.47000 ? 242 LEU B N   1 
ATOM   3992 C CA  . LEU B 1 240 ? 8.16700   -21.51200 -8.05500  1.000 49.35000 ? 242 LEU B CA  1 
ATOM   3993 C C   . LEU B 1 240 ? 7.88000   -22.48300 -6.94600  1.000 49.54000 ? 242 LEU B C   1 
ATOM   3994 O O   . LEU B 1 240 ? 8.51700   -23.48600 -6.82000  1.000 50.25000 ? 242 LEU B O   1 
ATOM   3995 C CB  . LEU B 1 240 ? 7.56100   -21.98700 -9.36100  1.000 50.40000 ? 242 LEU B CB  1 
ATOM   3996 C CG  . LEU B 1 240 ? 6.05400   -22.05100 -9.48400  1.000 50.09000 ? 242 LEU B CG  1 
ATOM   3997 C CD1 . LEU B 1 240 ? 5.48900   -20.70100 -9.75600  1.000 46.27000 ? 242 LEU B CD1 1 
ATOM   3998 C CD2 . LEU B 1 240 ? 5.64600   -22.93100 -10.60600 1.000 53.77000 ? 242 LEU B CD2 1 
ATOM   3999 N N   . THR B 1 241 ? 6.90700   -22.15800 -6.13500  1.000 47.44000 ? 243 THR B N   1 
ATOM   4000 C CA  . THR B 1 241 ? 6.57600   -22.92800 -4.97800  1.000 49.84000 ? 243 THR B CA  1 
ATOM   4001 C C   . THR B 1 241 ? 5.26000   -23.57300 -5.08000  1.000 53.46000 ? 243 THR B C   1 
ATOM   4002 O O   . THR B 1 241 ? 4.52300   -23.26300 -5.92300  1.000 53.37000 ? 243 THR B O   1 
ATOM   4003 C CB  . THR B 1 241 ? 6.52900   -22.04000 -3.72900  1.000 51.76000 ? 243 THR B CB  1 
ATOM   4004 O OG1 . THR B 1 241 ? 5.38200   -21.22300 -3.75500  1.000 49.60000 ? 243 THR B OG1 1 
ATOM   4005 C CG2 . THR B 1 241 ? 7.71400   -21.15600 -3.67400  1.000 49.90000 ? 243 THR B CG2 1 
ATOM   4006 N N   . GLN B 1 242 ? 4.98700   -24.48600 -4.19300  1.000 53.16000 ? 244 GLN B N   1 
ATOM   4007 C CA  . GLN B 1 242 ? 3.72400   -25.14600 -4.16900  1.000 56.30000 ? 244 GLN B CA  1 
ATOM   4008 C C   . GLN B 1 242 ? 2.65200   -24.12300 -3.89800  1.000 57.65000 ? 244 GLN B C   1 
ATOM   4009 O O   . GLN B 1 242 ? 1.54900   -24.28400 -4.29800  1.000 55.99000 ? 244 GLN B O   1 
ATOM   4010 C CB  . GLN B 1 242 ? 3.69200   -26.22300 -3.13000  1.000 60.72000 ? 244 GLN B CB  1 
ATOM   4011 C CG  . GLN B 1 242 ? 3.34000   -27.58300 -3.66400  1.000 65.30000 ? 244 GLN B CG  1 
ATOM   4012 C CD  . GLN B 1 242 ? 2.00000   -27.64700 -4.31100  1.000 62.67000 ? 244 GLN B CD  1 
ATOM   4013 O OE1 . GLN B 1 242 ? 1.05400   -27.08600 -3.84200  1.000 65.50000 ? 244 GLN B OE1 1 
ATOM   4014 N NE2 . GLN B 1 242 ? 1.92700   -28.34200 -5.37500  1.000 64.82000 ? 244 GLN B NE2 1 
ATOM   4015 N N   . ASP B 1 243 ? 2.98500   -23.09200 -3.16600  1.000 58.16000 ? 245 ASP B N   1 
ATOM   4016 C CA  . ASP B 1 243 ? 2.03200   -22.05100 -2.87900  1.000 60.55000 ? 245 ASP B CA  1 
ATOM   4017 C C   . ASP B 1 243 ? 1.64000   -21.38800 -4.17800  1.000 55.66000 ? 245 ASP B C   1 
ATOM   4018 O O   . ASP B 1 243 ? 0.51200   -21.06900 -4.37400  1.000 56.10000 ? 245 ASP B O   1 
ATOM   4019 C CB  . ASP B 1 243 ? 2.58500   -21.04000 -1.88400  1.000 61.50000 ? 245 ASP B CB  1 
ATOM   4020 N N   . HIS B 1 244 ? 2.59300   -21.18300 -5.04400  1.000 52.71000 ? 246 HIS B N   1 
ATOM   4021 C CA  . HIS B 1 244 ? 2.30600   -20.58800 -6.32700  1.000 53.04000 ? 246 HIS B CA  1 
ATOM   4022 C C   . HIS B 1 244 ? 1.41100   -21.46800 -7.15000  1.000 52.43000 ? 246 HIS B C   1 
ATOM   4023 O O   . HIS B 1 244 ? 0.47700   -21.03600 -7.72800  1.000 49.94000 ? 246 HIS B O   1 
ATOM   4024 C CB  . HIS B 1 244 ? 3.57300   -20.36300 -7.06800  1.000 49.18000 ? 246 HIS B CB  1 
ATOM   4025 C CG  . HIS B 1 244 ? 4.43700   -19.33400 -6.45000  1.000 49.23000 ? 246 HIS B CG  1 
ATOM   4026 N ND1 . HIS B 1 244 ? 5.79400   -19.34800 -6.55700  1.000 49.67000 ? 246 HIS B ND1 1 
ATOM   4027 C CD2 . HIS B 1 244 ? 4.13300   -18.26300 -5.70600  1.000 48.39000 ? 246 HIS B CD2 1 
ATOM   4028 C CE1 . HIS B 1 244 ? 6.29100   -18.31800 -5.92300  1.000 49.89000 ? 246 HIS B CE1 1 
ATOM   4029 N NE2 . HIS B 1 244 ? 5.30100   -17.64100 -5.40100  1.000 46.64000 ? 246 HIS B NE2 1 
ATOM   4030 N N   . VAL B 1 245 ? 1.67500   -22.74200 -7.12900  1.000 51.29000 ? 247 VAL B N   1 
ATOM   4031 C CA  . VAL B 1 245 ? 0.88500   -23.65200 -7.87400  1.000 51.99000 ? 247 VAL B CA  1 
ATOM   4032 C C   . VAL B 1 245 ? -0.52000  -23.64600 -7.40200  1.000 51.73000 ? 247 VAL B C   1 
ATOM   4033 O O   . VAL B 1 245 ? -1.42000  -23.61900 -8.16000  1.000 53.98000 ? 247 VAL B O   1 
ATOM   4034 C CB  . VAL B 1 245 ? 1.49900   -25.03800 -7.84500  1.000 49.94000 ? 247 VAL B CB  1 
ATOM   4035 C CG1 . VAL B 1 245 ? 0.64800   -26.00200 -8.58700  1.000 52.03000 ? 247 VAL B CG1 1 
ATOM   4036 C CG2 . VAL B 1 245 ? 2.85000   -25.01200 -8.48700  1.000 51.12000 ? 247 VAL B CG2 1 
ATOM   4037 N N   . ASP B 1 246 ? -0.69600  -23.62800 -6.11400  1.000 57.54000 ? 248 ASP B N   1 
ATOM   4038 C CA  . ASP B 1 246 ? -2.02100  -23.59900 -5.53800  1.000 56.08000 ? 248 ASP B CA  1 
ATOM   4039 C C   . ASP B 1 246 ? -2.71100  -22.32000 -5.92200  1.000 54.03000 ? 248 ASP B C   1 
ATOM   4040 O O   . ASP B 1 246 ? -3.84400  -22.33400 -6.25400  1.000 53.45000 ? 248 ASP B O   1 
ATOM   4041 C CB  . ASP B 1 246 ? -1.98000  -23.73900 -4.03500  1.000 59.58000 ? 248 ASP B CB  1 
ATOM   4042 C CG  . ASP B 1 246 ? -1.72500  -25.13000 -3.58600  1.000 62.42000 ? 248 ASP B CG  1 
ATOM   4043 O OD1 . ASP B 1 246 ? -1.82700  -26.06500 -4.37200  1.000 64.33000 ? 248 ASP B OD1 1 
ATOM   4044 O OD2 . ASP B 1 246 ? -1.41700  -25.29500 -2.42100  1.000 68.13000 ? 248 ASP B OD2 1 
ATOM   4045 N N   . ILE B 1 247 ? -1.99400  -21.22700 -5.91000  1.000 52.05000 ? 249 ILE B N   1 
ATOM   4046 C CA  . ILE B 1 247 ? -2.56400  -19.95100 -6.24400  1.000 53.63000 ? 249 ILE B CA  1 
ATOM   4047 C C   . ILE B 1 247 ? -3.13200  -19.94600 -7.64600  1.000 54.15000 ? 249 ILE B C   1 
ATOM   4048 O O   . ILE B 1 247 ? -4.15100  -19.34800 -7.89300  1.000 53.82000 ? 249 ILE B O   1 
ATOM   4049 C CB  . ILE B 1 247 ? -1.50900  -18.85500 -6.14600  1.000 56.03000 ? 249 ILE B CB  1 
ATOM   4050 C CG1 . ILE B 1 247 ? -1.18500  -18.61400 -4.71400  1.000 58.73000 ? 249 ILE B CG1 1 
ATOM   4051 C CG2 . ILE B 1 247 ? -2.03000  -17.54200 -6.62700  1.000 56.21000 ? 249 ILE B CG2 1 
ATOM   4052 C CD1 . ILE B 1 247 ? -2.40600  -18.30400 -3.90300  1.000 57.57000 ? 249 ILE B CD1 1 
ATOM   4053 N N   . LEU B 1 248 ? -2.46200  -20.61200 -8.54900  1.000 48.26000 ? 250 LEU B N   1 
ATOM   4054 C CA  . LEU B 1 248 ? -2.89400  -20.64100 -9.90700  1.000 49.20000 ? 250 LEU B CA  1 
ATOM   4055 C C   . LEU B 1 248 ? -3.99600  -21.62100 -10.21700 1.000 50.83000 ? 250 LEU B C   1 
ATOM   4056 O O   . LEU B 1 248 ? -4.45700  -21.64700 -11.29700 1.000 48.64000 ? 250 LEU B O   1 
ATOM   4057 C CB  . LEU B 1 248 ? -1.71200  -20.89000 -10.79900 1.000 42.24000 ? 250 LEU B CB  1 
ATOM   4058 C CG  . LEU B 1 248 ? -0.74600  -19.75100 -10.90300 1.000 43.15000 ? 250 LEU B CG  1 
ATOM   4059 C CD1 . LEU B 1 248 ? 0.61600   -20.18300 -11.28700 1.000 39.20000 ? 250 LEU B CD1 1 
ATOM   4060 C CD2 . LEU B 1 248 ? -1.23600  -18.68900 -11.81100 1.000 41.40000 ? 250 LEU B CD2 1 
ATOM   4061 N N   . GLY B 1 249 ? -4.44500  -22.39400 -9.25400  1.000 49.30000 ? 251 GLY B N   1 
ATOM   4062 C CA  . GLY B 1 249 ? -5.45400  -23.40700 -9.51100  1.000 52.26000 ? 251 GLY B CA  1 
ATOM   4063 C C   . GLY B 1 249 ? -6.74100  -22.96900 -10.15100 1.000 52.14000 ? 251 GLY B C   1 
ATOM   4064 O O   . GLY B 1 249 ? -7.25200  -23.63700 -11.01100 1.000 53.39000 ? 251 GLY B O   1 
ATOM   4065 N N   . PRO B 1 250 ? -7.24500  -21.81700 -9.78400  1.000 52.65000 ? 252 PRO B N   1 
ATOM   4066 C CA  . PRO B 1 250 ? -8.45800  -21.35300 -10.39900 1.000 51.53000 ? 252 PRO B CA  1 
ATOM   4067 C C   . PRO B 1 250 ? -8.24100  -21.18800 -11.85000 1.000 51.77000 ? 252 PRO B C   1 
ATOM   4068 O O   . PRO B 1 250 ? -9.09600  -21.52800 -12.57400 1.000 54.19000 ? 252 PRO B O   1 
ATOM   4069 C CB  . PRO B 1 250 ? -8.67800  -20.02300 -9.74300  1.000 53.08000 ? 252 PRO B CB  1 
ATOM   4070 C CG  . PRO B 1 250 ? -8.16000  -20.21100 -8.40200  1.000 48.13000 ? 252 PRO B CG  1 
ATOM   4071 C CD  . PRO B 1 250 ? -7.05500  -21.20100 -8.48000  1.000 52.05000 ? 252 PRO B CD  1 
ATOM   4072 N N   . LEU B 1 251 ? -7.12700  -20.66500 -12.26800 1.000 52.41000 ? 253 LEU B N   1 
ATOM   4073 C CA  . LEU B 1 251 ? -6.85000  -20.52400 -13.67000 1.000 50.27000 ? 253 LEU B CA  1 
ATOM   4074 C C   . LEU B 1 251 ? -6.66600  -21.84200 -14.41200 1.000 47.82000 ? 253 LEU B C   1 
ATOM   4075 O O   . LEU B 1 251 ? -6.96100  -21.93900 -15.54600 1.000 46.86000 ? 253 LEU B O   1 
ATOM   4076 C CB  . LEU B 1 251 ? -5.70000  -19.59000 -13.89600 1.000 48.61000 ? 253 LEU B CB  1 
ATOM   4077 C CG  . LEU B 1 251 ? -5.90000  -18.12600 -13.53500 1.000 49.46000 ? 253 LEU B CG  1 
ATOM   4078 C CD1 . LEU B 1 251 ? -4.63300  -17.35200 -13.62200 1.000 44.61000 ? 253 LEU B CD1 1 
ATOM   4079 C CD2 . LEU B 1 251 ? -6.95500  -17.47200 -14.34900 1.000 46.38000 ? 253 LEU B CD2 1 
ATOM   4080 N N   . SER B 1 252 ? -6.07500  -22.81400 -13.74900 1.000 49.75000 ? 254 SER B N   1 
ATOM   4081 C CA  . SER B 1 252 ? -5.85100  -24.12900 -14.28600 1.000 48.10000 ? 254 SER B CA  1 
ATOM   4082 C C   . SER B 1 252 ? -7.17400  -24.79700 -14.48200 1.000 52.01000 ? 254 SER B C   1 
ATOM   4083 O O   . SER B 1 252 ? -7.41600  -25.40100 -15.47600 1.000 50.59000 ? 254 SER B O   1 
ATOM   4084 C CB  . SER B 1 252 ? -4.97700  -24.92300 -13.34900 1.000 50.84000 ? 254 SER B CB  1 
ATOM   4085 O OG  . SER B 1 252 ? -4.89800  -26.26200 -13.69700 1.000 52.52000 ? 254 SER B OG  1 
ATOM   4086 N N   . ALA B 1 253 ? -8.04400  -24.65000 -13.51300 1.000 51.88000 ? 255 ALA B N   1 
ATOM   4087 C CA  . ALA B 1 253 ? -9.36700  -25.20000 -13.61400 1.000 52.31000 ? 255 ALA B CA  1 
ATOM   4088 C C   . ALA B 1 253 ? -10.13900 -24.52800 -14.73200 1.000 52.70000 ? 255 ALA B C   1 
ATOM   4089 O O   . ALA B 1 253 ? -10.80800 -25.15700 -15.49200 1.000 54.30000 ? 255 ALA B O   1 
ATOM   4090 C CB  . ALA B 1 253 ? -10.09200 -25.04300 -12.31800 1.000 46.80000 ? 255 ALA B CB  1 
ATOM   4091 N N   . GLN B 1 254 ? -10.01200 -23.23400 -14.82900 1.000 53.60000 ? 256 GLN B N   1 
ATOM   4092 C CA  . GLN B 1 254 ? -10.70300 -22.48800 -15.83800 1.000 55.18000 ? 256 GLN B CA  1 
ATOM   4093 C C   . GLN B 1 254 ? -10.30400 -22.83300 -17.24400 1.000 54.40000 ? 256 GLN B C   1 
ATOM   4094 O O   . GLN B 1 254 ? -11.10600 -22.78100 -18.11900 1.000 51.59000 ? 256 GLN B O   1 
ATOM   4095 C CB  . GLN B 1 254 ? -10.57500 -21.00900 -15.58500 1.000 53.80000 ? 256 GLN B CB  1 
ATOM   4096 C CG  . GLN B 1 254 ? -11.10100 -20.15500 -16.70900 1.000 58.78000 ? 256 GLN B CG  1 
ATOM   4097 C CD  . GLN B 1 254 ? -11.20500 -18.69700 -16.37000 1.000 67.01000 ? 256 GLN B CD  1 
ATOM   4098 O OE1 . GLN B 1 254 ? -11.52400 -17.87500 -17.22200 1.000 69.44000 ? 256 GLN B OE1 1 
ATOM   4099 N NE2 . GLN B 1 254 ? -10.96400 -18.36400 -15.11500 1.000 66.63000 ? 256 GLN B NE2 1 
ATOM   4100 N N   . THR B 1 255 ? -9.04300  -23.11400 -17.45300 1.000 50.90000 ? 257 THR B N   1 
ATOM   4101 C CA  . THR B 1 255 ? -8.56600  -23.39200 -18.77700 1.000 49.89000 ? 257 THR B CA  1 
ATOM   4102 C C   . THR B 1 255 ? -8.23100  -24.79800 -19.11600 1.000 49.73000 ? 257 THR B C   1 
ATOM   4103 O O   . THR B 1 255 ? -7.96200  -25.06700 -20.22100 1.000 51.05000 ? 257 THR B O   1 
ATOM   4104 C CB  . THR B 1 255 ? -7.31600  -22.56200 -19.05900 1.000 50.07000 ? 257 THR B CB  1 
ATOM   4105 O OG1 . THR B 1 255 ? -6.29000  -22.93500 -18.16300 1.000 47.07000 ? 257 THR B OG1 1 
ATOM   4106 C CG2 . THR B 1 255 ? -7.58900  -21.18400 -18.86100 1.000 46.69000 ? 257 THR B CG2 1 
ATOM   4107 N N   . GLY B 1 256 ? -8.25600  -25.70000 -18.17600 1.000 45.49000 ? 258 GLY B N   1 
ATOM   4108 C CA  . GLY B 1 256 ? -7.83000  -27.05600 -18.45600 1.000 46.81000 ? 258 GLY B CA  1 
ATOM   4109 C C   . GLY B 1 256 ? -6.34100  -27.23100 -18.68700 1.000 53.16000 ? 258 GLY B C   1 
ATOM   4110 O O   . GLY B 1 256 ? -5.91400  -28.31500 -19.09500 1.000 48.96000 ? 258 GLY B O   1 
ATOM   4111 N N   . ILE B 1 257 ? -5.52900  -26.20500 -18.43900 1.000 49.81000 ? 259 ILE B N   1 
ATOM   4112 C CA  . ILE B 1 257 ? -4.08000  -26.31300 -18.54500 1.000 46.89000 ? 259 ILE B CA  1 
ATOM   4113 C C   . ILE B 1 257 ? -3.52000  -26.37700 -17.13300 1.000 47.88000 ? 259 ILE B C   1 
ATOM   4114 O O   . ILE B 1 257 ? -3.61100  -25.40200 -16.37800 1.000 47.15000 ? 259 ILE B O   1 
ATOM   4115 C CB  . ILE B 1 257 ? -3.47500  -25.14500 -19.33000 1.000 44.65000 ? 259 ILE B CB  1 
ATOM   4116 C CG1 . ILE B 1 257 ? -4.12700  -25.06000 -20.70500 1.000 50.02000 ? 259 ILE B CG1 1 
ATOM   4117 C CG2 . ILE B 1 257 ? -1.96100  -25.31500 -19.44300 1.000 44.93000 ? 259 ILE B CG2 1 
ATOM   4118 C CD1 . ILE B 1 257 ? -4.19800  -23.67000 -21.23700 1.000 51.73000 ? 259 ILE B CD1 1 
ATOM   4119 N N   . ALA B 1 258 ? -2.93400  -27.51800 -16.77400 1.000 48.53000 ? 260 ALA B N   1 
ATOM   4120 C CA  . ALA B 1 258 ? -2.33000  -27.66300 -15.45600 1.000 46.48000 ? 260 ALA B CA  1 
ATOM   4121 C C   . ALA B 1 258 ? -1.09800  -26.77300 -15.33600 1.000 46.79000 ? 260 ALA B C   1 
ATOM   4122 O O   . ALA B 1 258 ? -0.44700  -26.43800 -16.33000 1.000 43.93000 ? 260 ALA B O   1 
ATOM   4123 C CB  . ALA B 1 258 ? -1.96000  -29.12400 -15.20200 1.000 43.43000 ? 260 ALA B CB  1 
ATOM   4124 N N   . VAL B 1 259 ? -0.77400  -26.38800 -14.10000 1.000 44.49000 ? 261 VAL B N   1 
ATOM   4125 C CA  . VAL B 1 259 ? 0.30600   -25.42700 -13.89000 1.000 45.22000 ? 261 VAL B CA  1 
ATOM   4126 C C   . VAL B 1 259 ? 1.62600   -25.97000 -14.42900 1.000 45.40000 ? 261 VAL B C   1 
ATOM   4127 O O   . VAL B 1 259 ? 2.36600   -25.26800 -15.12900 1.000 44.90000 ? 261 VAL B O   1 
ATOM   4128 C CB  . VAL B 1 259 ? 0.41600   -25.04900 -12.40300 1.000 45.34000 ? 261 VAL B CB  1 
ATOM   4129 C CG1 . VAL B 1 259 ? 1.62600   -24.15600 -12.19700 1.000 44.57000 ? 261 VAL B CG1 1 
ATOM   4130 C CG2 . VAL B 1 259 ? -0.86900  -24.36300 -11.94500 1.000 45.62000 ? 261 VAL B CG2 1 
ATOM   4131 N N   . LEU B 1 260 ? 1.94100   -27.23400 -14.11800 1.000 44.03000 ? 262 LEU B N   1 
ATOM   4132 C CA  . LEU B 1 260 ? 3.18600   -27.82100 -14.60800 1.000 43.46000 ? 262 LEU B CA  1 
ATOM   4133 C C   . LEU B 1 260 ? 3.18000   -28.06100 -16.11800 1.000 44.32000 ? 262 LEU B C   1 
ATOM   4134 O O   . LEU B 1 260 ? 4.25500   -28.27500 -16.70000 1.000 44.70000 ? 262 LEU B O   1 
ATOM   4135 C CB  . LEU B 1 260 ? 3.49900   -29.13000 -13.86400 1.000 43.06000 ? 262 LEU B CB  1 
ATOM   4136 C CG  . LEU B 1 260 ? 3.77000   -29.01400 -12.34900 1.000 47.81000 ? 262 LEU B CG  1 
ATOM   4137 C CD1 . LEU B 1 260 ? 3.97900   -30.38200 -11.68900 1.000 48.60000 ? 262 LEU B CD1 1 
ATOM   4138 C CD2 . LEU B 1 260 ? 4.94300   -28.09700 -12.04400 1.000 47.95000 ? 262 LEU B CD2 1 
ATOM   4139 N N   . ASP B 1 261 ? 2.01300   -28.03200 -16.76800 1.000 41.94000 ? 263 ASP B N   1 
ATOM   4140 C CA  . ASP B 1 261 ? 1.98500   -28.05500 -18.23300 1.000 47.05000 ? 263 ASP B CA  1 
ATOM   4141 C C   . ASP B 1 261 ? 2.23100   -26.65700 -18.80200 1.000 43.01000 ? 263 ASP B C   1 
ATOM   4142 O O   . ASP B 1 261 ? 2.98700   -26.49900 -19.76400 1.000 40.74000 ? 263 ASP B O   1 
ATOM   4143 C CB  . ASP B 1 261 ? 0.65600   -28.64000 -18.72000 1.000 49.56000 ? 263 ASP B CB  1 
ATOM   4144 C CG  . ASP B 1 261 ? 0.47300   -28.56400 -20.25600 1.000 57.40000 ? 263 ASP B CG  1 
ATOM   4145 O OD1 . ASP B 1 261 ? 1.45700   -28.38900 -21.02800 1.000 59.40000 ? 263 ASP B OD1 1 
ATOM   4146 O OD2 . ASP B 1 261 ? -0.69100  -28.69500 -20.69500 1.000 62.49000 ? 263 ASP B OD2 1 
ATOM   4147 N N   . MET B 1 262 ? 1.62200   -25.63100 -18.19700 1.000 43.98000 ? 264 MET B N   1 
ATOM   4148 C CA  . MET B 1 262 ? 1.99500   -24.25800 -18.51200 1.000 40.89000 ? 264 MET B CA  1 
ATOM   4149 C C   . MET B 1 262 ? 3.47300   -23.99500 -18.23400 1.000 42.86000 ? 264 MET B C   1 
ATOM   4150 O O   . MET B 1 262 ? 4.10800   -23.23600 -18.97500 1.000 41.75000 ? 264 MET B O   1 
ATOM   4151 C CB  . MET B 1 262 ? 1.10900   -23.29200 -17.72400 1.000 41.17000 ? 264 MET B CB  1 
ATOM   4152 C CG  . MET B 1 262 ? 1.09400   -21.86800 -18.26800 1.000 39.81000 ? 264 MET B CG  1 
ATOM   4153 S SD  . MET B 1 262 ? 0.41500   -21.71800 -19.94400 1.000 40.06000 ? 264 MET B SD  1 
ATOM   4154 C CE  . MET B 1 262 ? -1.28100  -21.31800 -19.56800 1.000 40.92000 ? 264 MET B CE  1 
ATOM   4155 N N   . CYS B 1 263 ? 4.02800   -24.62900 -17.22300 1.000 41.83000 ? 265 CYS B N   1 
ATOM   4156 C CA  . CYS B 1 263 ? 5.42600   -24.48400 -16.91700 1.000 44.07000 ? 265 CYS B CA  1 
ATOM   4157 C C   . CYS B 1 263 ? 6.29400   -24.99100 -18.05100 1.000 44.87000 ? 265 CYS B C   1 
ATOM   4158 O O   . CYS B 1 263 ? 7.33100   -24.45700 -18.32400 1.000 43.07000 ? 265 CYS B O   1 
ATOM   4159 C CB  . CYS B 1 263 ? 5.80500   -25.14500 -15.62100 1.000 43.56000 ? 265 CYS B CB  1 
ATOM   4160 S SG  . CYS B 1 263 ? 5.39700   -24.21100 -14.17900 1.000 45.63000 ? 265 CYS B SG  1 
ATOM   4161 N N   . ALA B 1 264 ? 5.84400   -26.05200 -18.67800 1.000 43.95000 ? 266 ALA B N   1 
ATOM   4162 C CA  . ALA B 1 264 ? 6.53400   -26.61300 -19.80100 1.000 47.81000 ? 266 ALA B CA  1 
ATOM   4163 C C   . ALA B 1 264 ? 6.51800   -25.61500 -20.91500 1.000 45.34000 ? 266 ALA B C   1 
ATOM   4164 O O   . ALA B 1 264 ? 7.49900   -25.41300 -21.53400 1.000 50.46000 ? 266 ALA B O   1 
ATOM   4165 C CB  . ALA B 1 264 ? 5.91100   -27.91100 -20.21300 1.000 50.36000 ? 266 ALA B CB  1 
ATOM   4166 N N   . SER B 1 265 ? 5.40500   -24.95100 -21.11900 1.000 44.11000 ? 267 SER B N   1 
ATOM   4167 C CA  . SER B 1 265 ? 5.31900   -23.94800 -22.12200 1.000 43.77000 ? 267 SER B CA  1 
ATOM   4168 C C   . SER B 1 265 ? 6.28600   -22.88000 -21.81300 1.000 44.08000 ? 267 SER B C   1 
ATOM   4169 O O   . SER B 1 265 ? 6.91400   -22.43300 -22.66200 1.000 43.97000 ? 267 SER B O   1 
ATOM   4170 C CB  . SER B 1 265 ? 3.97300   -23.35000 -22.16100 1.000 41.84000 ? 267 SER B CB  1 
ATOM   4171 O OG  . SER B 1 265 ? 3.12900   -24.16800 -22.83200 1.000 47.25000 ? 267 SER B OG  1 
ATOM   4172 N N   . LEU B 1 266 ? 6.38700   -22.48200 -20.56700 1.000 44.68000 ? 268 LEU B N   1 
ATOM   4173 C CA  . LEU B 1 266 ? 7.31100   -21.46300 -20.16400 1.000 44.06000 ? 268 LEU B CA  1 
ATOM   4174 C C   . LEU B 1 266 ? 8.74500   -21.84200 -20.33000 1.000 45.07000 ? 268 LEU B C   1 
ATOM   4175 O O   . LEU B 1 266 ? 9.50600   -21.06000 -20.74600 1.000 46.20000 ? 268 LEU B O   1 
ATOM   4176 C CB  . LEU B 1 266 ? 7.04000   -20.99200 -18.76200 1.000 42.93000 ? 268 LEU B CB  1 
ATOM   4177 C CG  . LEU B 1 266 ? 7.82500   -19.81900 -18.22500 1.000 41.44000 ? 268 LEU B CG  1 
ATOM   4178 C CD1 . LEU B 1 266 ? 7.85900   -18.68100 -19.16700 1.000 38.70000 ? 268 LEU B CD1 1 
ATOM   4179 C CD2 . LEU B 1 266 ? 7.31600   -19.34800 -16.90600 1.000 41.21000 ? 268 LEU B CD2 1 
ATOM   4180 N N   . LYS B 1 267 ? 9.09500   -23.07100 -20.03100 1.000 48.53000 ? 269 LYS B N   1 
ATOM   4181 C CA  . LYS B 1 267 ? 10.46100  -23.52600 -20.20500 1.000 51.37000 ? 269 LYS B CA  1 
ATOM   4182 C C   . LYS B 1 267 ? 10.88400  -23.38100 -21.63300 1.000 53.70000 ? 269 LYS B C   1 
ATOM   4183 O O   . LYS B 1 267 ? 11.94800  -22.93300 -21.90600 1.000 56.65000 ? 269 LYS B O   1 
ATOM   4184 C CB  . LYS B 1 267 ? 10.55100  -24.98900 -19.96000 1.000 54.39000 ? 269 LYS B CB  1 
ATOM   4185 C CG  . LYS B 1 267 ? 10.74800  -25.42900 -18.55100 1.000 57.52000 ? 269 LYS B CG  1 
ATOM   4186 C CD  . LYS B 1 267 ? 10.91300  -26.93400 -18.51900 1.000 58.74000 ? 269 LYS B CD  1 
ATOM   4187 C CE  . LYS B 1 267 ? 12.02600  -27.37200 -19.43500 1.000 61.52000 ? 269 LYS B CE  1 
ATOM   4188 N NZ  . LYS B 1 267 ? 12.65900  -28.65200 -19.02900 1.000 66.70000 ? 269 LYS B NZ  1 
ATOM   4189 N N   . GLU B 1 268 ? 10.01900  -23.76600 -22.54100 1.000 52.72000 ? 270 GLU B N   1 
ATOM   4190 C CA  . GLU B 1 268 ? 10.26700  -23.66400 -23.94600 1.000 55.66000 ? 270 GLU B CA  1 
ATOM   4191 C C   . GLU B 1 268 ? 10.38400  -22.24900 -24.45100 1.000 58.73000 ? 270 GLU B C   1 
ATOM   4192 O O   . GLU B 1 268 ? 11.15000  -21.99500 -25.31800 1.000 58.13000 ? 270 GLU B O   1 
ATOM   4193 C CB  . GLU B 1 268 ? 9.27900   -24.47300 -24.75000 1.000 59.18000 ? 270 GLU B CB  1 
ATOM   4194 C CG  . GLU B 1 268 ? 9.46400   -25.96900 -24.62700 1.000 61.75000 ? 270 GLU B CG  1 
ATOM   4195 C CD  . GLU B 1 268 ? 10.85700  -26.41200 -24.97000 1.000 67.47000 ? 270 GLU B CD  1 
ATOM   4196 O OE1 . GLU B 1 268 ? 11.44500  -27.17400 -24.20700 1.000 67.03000 ? 270 GLU B OE1 1 
ATOM   4197 O OE2 . GLU B 1 268 ? 11.37900  -25.98900 -26.00100 1.000 68.43000 ? 270 GLU B OE2 1 
ATOM   4198 N N   . LEU B 1 269 ? 9.59300   -21.33400 -23.92600 1.000 55.11000 ? 271 LEU B N   1 
ATOM   4199 C CA  . LEU B 1 269 ? 9.68900   -19.96000 -24.32300 1.000 54.27000 ? 271 LEU B CA  1 
ATOM   4200 C C   . LEU B 1 269 ? 11.01500  -19.38200 -23.93400 1.000 57.59000 ? 271 LEU B C   1 
ATOM   4201 O O   . LEU B 1 269 ? 11.59800  -18.64800 -24.65000 1.000 60.84000 ? 271 LEU B O   1 
ATOM   4202 C CB  . LEU B 1 269 ? 8.59200   -19.14200 -23.72900 1.000 53.11000 ? 271 LEU B CB  1 
ATOM   4203 C CG  . LEU B 1 269 ? 7.26800   -19.43600 -24.33600 1.000 51.28000 ? 271 LEU B CG  1 
ATOM   4204 C CD1 . LEU B 1 269 ? 6.17900   -18.68600 -23.65700 1.000 51.01000 ? 271 LEU B CD1 1 
ATOM   4205 C CD2 . LEU B 1 269 ? 7.38100   -19.02400 -25.75600 1.000 57.71000 ? 271 LEU B CD2 1 
ATOM   4206 N N   . LEU B 1 270 ? 11.47700  -19.71600 -22.76000 1.000 55.19000 ? 272 LEU B N   1 
ATOM   4207 C CA  . LEU B 1 270 ? 12.74100  -19.23300 -22.28300 1.000 56.41000 ? 272 LEU B CA  1 
ATOM   4208 C C   . LEU B 1 270 ? 13.94300  -19.77700 -23.03100 1.000 64.20000 ? 272 LEU B C   1 
ATOM   4209 O O   . LEU B 1 270 ? 14.88600  -19.07400 -23.29700 1.000 61.77000 ? 272 LEU B O   1 
ATOM   4210 C CB  . LEU B 1 270 ? 12.90000  -19.55600 -20.83400 1.000 55.21000 ? 272 LEU B CB  1 
ATOM   4211 C CG  . LEU B 1 270 ? 11.94800  -18.90000 -19.87000 1.000 52.66000 ? 272 LEU B CG  1 
ATOM   4212 C CD1 . LEU B 1 270 ? 12.15800  -19.43500 -18.48200 1.000 50.65000 ? 272 LEU B CD1 1 
ATOM   4213 C CD2 . LEU B 1 270 ? 12.06200  -17.40500 -19.95200 1.000 49.82000 ? 272 LEU B CD2 1 
ATOM   4214 N N   . GLN B 1 271 ? 13.90600  -21.06400 -23.31100 1.000 64.08000 ? 273 GLN B N   1 
ATOM   4215 C CA  . GLN B 1 271 ? 14.95900  -21.71500 -24.02200 1.000 64.04000 ? 273 GLN B CA  1 
ATOM   4216 C C   . GLN B 1 271 ? 15.01300  -21.30500 -25.45000 1.000 64.83000 ? 273 GLN B C   1 
ATOM   4217 O O   . GLN B 1 271 ? 16.03900  -21.01000 -25.95700 1.000 65.83000 ? 273 GLN B O   1 
ATOM   4218 C CB  . GLN B 1 271 ? 14.82500  -23.21000 -23.88000 1.000 62.65000 ? 273 GLN B CB  1 
ATOM   4219 C CG  . GLN B 1 271 ? 15.42000  -23.75700 -22.61000 1.000 58.40000 ? 273 GLN B CG  1 
ATOM   4220 C CD  . GLN B 1 271 ? 14.91200  -25.12200 -22.24100 1.000 62.14000 ? 273 GLN B CD  1 
ATOM   4221 O OE1 . GLN B 1 271 ? 14.12400  -25.69400 -22.93800 1.000 66.08000 ? 273 GLN B OE1 1 
ATOM   4222 N NE2 . GLN B 1 271 ? 15.37200  -25.64600 -21.14400 1.000 57.23000 ? 273 GLN B NE2 1 
ATOM   4223 N N   . ASN B 1 272 ? 13.87600  -21.24900 -26.09000 1.000 65.24000 ? 274 ASN B N   1 
ATOM   4224 C CA  . ASN B 1 272 ? 13.82600  -20.93200 -27.49800 1.000 67.39000 ? 274 ASN B CA  1 
ATOM   4225 C C   . ASN B 1 272 ? 13.28000  -19.61300 -28.04700 1.000 69.48000 ? 274 ASN B C   1 
ATOM   4226 O O   . ASN B 1 272 ? 13.46900  -19.36000 -29.20300 1.000 70.71000 ? 274 ASN B O   1 
ATOM   4227 C CB  . ASN B 1 272 ? 13.24200  -22.12900 -28.23300 1.000 68.96000 ? 274 ASN B CB  1 
ATOM   4228 C CG  . ASN B 1 272 ? 13.75500  -23.44400 -27.69100 1.000 70.27000 ? 274 ASN B CG  1 
ATOM   4229 O OD1 . ASN B 1 272 ? 14.88400  -23.54500 -27.29400 1.000 71.53000 ? 274 ASN B OD1 1 
ATOM   4230 N ND2 . ASN B 1 272 ? 12.91700  -24.44000 -27.65400 1.000 71.32000 ? 274 ASN B ND2 1 
ATOM   4231 N N   . GLY B 1 273 ? 12.62300  -18.77300 -27.25900 1.000 65.52000 ? 275 GLY B N   1 
ATOM   4232 C CA  . GLY B 1 273 ? 12.15500  -17.49600 -27.76000 1.000 62.01000 ? 275 GLY B CA  1 
ATOM   4233 C C   . GLY B 1 273 ? 10.79600  -17.41700 -28.39000 1.000 70.10000 ? 275 GLY B C   1 
ATOM   4234 O O   . GLY B 1 273 ? 10.23700  -18.41800 -28.69800 1.000 70.39000 ? 275 GLY B O   1 
ATOM   4235 N N   . MET B 1 274 ? 10.25100  -16.21900 -28.55500 1.000 70.99000 ? 276 MET B N   1 
ATOM   4236 C CA  . MET B 1 274 ? 8.94500   -16.06900 -29.17000 1.000 74.05000 ? 276 MET B CA  1 
ATOM   4237 C C   . MET B 1 274 ? 8.98000   -16.39000 -30.62800 1.000 74.86000 ? 276 MET B C   1 
ATOM   4238 O O   . MET B 1 274 ? 7.99800   -16.77400 -31.21600 1.000 75.41000 ? 276 MET B O   1 
ATOM   4239 C CB  . MET B 1 274 ? 8.30200   -14.70900 -28.92800 1.000 77.35000 ? 276 MET B CB  1 
ATOM   4240 C CG  . MET B 1 274 ? 7.04900   -14.70900 -28.06700 1.000 70.50000 ? 276 MET B CG  1 
ATOM   4241 S SD  . MET B 1 274 ? 7.28200   -14.05400 -26.44600 1.000 76.77000 ? 276 MET B SD  1 
ATOM   4242 C CE  . MET B 1 274 ? 8.67400   -14.99600 -25.91600 1.000 66.55000 ? 276 MET B CE  1 
ATOM   4243 N N   . ASN B 1 275 ? 10.12900  -16.19700 -31.22500 1.000 77.43000 ? 277 ASN B N   1 
ATOM   4244 C CA  . ASN B 1 275 ? 10.28200  -16.52000 -32.62600 1.000 78.66000 ? 277 ASN B CA  1 
ATOM   4245 C C   . ASN B 1 275 ? 9.32700   -15.88200 -33.60800 1.000 76.91000 ? 277 ASN B C   1 
ATOM   4246 O O   . ASN B 1 275 ? 8.75000   -16.52500 -34.43300 1.000 77.80000 ? 277 ASN B O   1 
ATOM   4247 C CB  . ASN B 1 275 ? 10.24300  -18.01900 -32.75300 1.000 78.84000 ? 277 ASN B CB  1 
ATOM   4248 C CG  . ASN B 1 275 ? 10.56700  -18.48800 -34.11500 1.000 80.87000 ? 277 ASN B CG  1 
ATOM   4249 O OD1 . ASN B 1 275 ? 10.14100  -19.53900 -34.50800 1.000 80.23000 ? 277 ASN B OD1 1 
ATOM   4250 N ND2 . ASN B 1 275 ? 11.34000  -17.70700 -34.84200 1.000 79.00000 ? 277 ASN B ND2 1 
ATOM   4251 N N   . GLY B 1 276 ? 9.15300   -14.59200 -33.49300 1.000 79.05000 ? 278 GLY B N   1 
ATOM   4252 C CA  . GLY B 1 276 ? 8.30600   -13.88200 -34.41900 1.000 79.15000 ? 278 GLY B CA  1 
ATOM   4253 C C   . GLY B 1 276 ? 6.85900   -13.89700 -34.08800 1.000 78.77000 ? 278 GLY B C   1 
ATOM   4254 O O   . GLY B 1 276 ? 6.04900   -13.27400 -34.75600 1.000 78.44000 ? 278 GLY B O   1 
ATOM   4255 N N   . ARG B 1 277 ? 6.53300   -14.63200 -33.04500 1.000 79.52000 ? 279 ARG B N   1 
ATOM   4256 C CA  . ARG B 1 277 ? 5.18500   -14.66600 -32.60400 1.000 74.80000 ? 279 ARG B CA  1 
ATOM   4257 C C   . ARG B 1 277 ? 5.19300   -13.78200 -31.37500 1.000 74.00000 ? 279 ARG B C   1 
ATOM   4258 O O   . ARG B 1 277 ? 6.21200   -13.50100 -30.81900 1.000 73.50000 ? 279 ARG B O   1 
ATOM   4259 C CB  . ARG B 1 277 ? 4.74800   -16.09400 -32.34900 1.000 70.58000 ? 279 ARG B CB  1 
ATOM   4260 N N   . THR B 1 278 ? 4.03700   -13.32000 -30.98900 1.000 75.05000 ? 280 THR B N   1 
ATOM   4261 C CA  . THR B 1 278 ? 3.87800   -12.47800 -29.84500 1.000 73.96000 ? 280 THR B CA  1 
ATOM   4262 C C   . THR B 1 278 ? 2.82200   -13.18000 -29.04400 1.000 73.50000 ? 280 THR B C   1 
ATOM   4263 O O   . THR B 1 278 ? 2.11300   -14.03200 -29.56500 1.000 68.52000 ? 280 THR B O   1 
ATOM   4264 C CB  . THR B 1 278 ? 3.34700   -11.09900 -30.23900 1.000 74.20000 ? 280 THR B CB  1 
ATOM   4265 O OG1 . THR B 1 278 ? 1.99000   -11.18300 -30.66500 1.000 74.00000 ? 280 THR B OG1 1 
ATOM   4266 C CG2 . THR B 1 278 ? 4.12100   -10.57400 -31.32700 1.000 72.19000 ? 280 THR B CG2 1 
ATOM   4267 N N   . ILE B 1 279 ? 2.72000   -12.81700 -27.78400 1.000 73.07000 ? 281 ILE B N   1 
ATOM   4268 C CA  . ILE B 1 279 ? 1.73300   -13.43200 -26.96500 1.000 67.83000 ? 281 ILE B CA  1 
ATOM   4269 C C   . ILE B 1 279 ? 0.53700   -12.56300 -26.85900 1.000 69.66000 ? 281 ILE B C   1 
ATOM   4270 O O   . ILE B 1 279 ? -0.41600  -12.86500 -27.53700 1.000 79.10000 ? 281 ILE B O   1 
ATOM   4271 C CB  . ILE B 1 279 ? 2.28100   -13.84500 -25.62800 1.000 65.51000 ? 281 ILE B CB  1 
ATOM   4272 C CG1 . ILE B 1 279 ? 3.44500   -14.79600 -25.86900 1.000 64.05000 ? 281 ILE B CG1 1 
ATOM   4273 C CG2 . ILE B 1 279 ? 1.17200   -14.40100 -24.77100 1.000 58.05000 ? 281 ILE B CG2 1 
ATOM   4274 C CD1 . ILE B 1 279 ? 3.32000   -16.17500 -25.31000 1.000 57.41000 ? 281 ILE B CD1 1 
ATOM   4275 N N   . LEU B 1 280 ? 0.54300   -11.51000 -26.08100 1.000 67.05000 ? 282 LEU B N   1 
ATOM   4276 C CA  . LEU B 1 280 ? -0.65600  -10.68800 -26.01000 1.000 69.69000 ? 282 LEU B CA  1 
ATOM   4277 C C   . LEU B 1 280 ? -0.51000  -9.41300  -26.76200 1.000 71.10000 ? 282 LEU B C   1 
ATOM   4278 O O   . LEU B 1 280 ? -1.37100  -8.60100  -26.78500 1.000 76.13000 ? 282 LEU B O   1 
ATOM   4279 C CB  . LEU B 1 280 ? -1.04500  -10.40700 -24.58300 1.000 68.51000 ? 282 LEU B CB  1 
ATOM   4280 C CG  . LEU B 1 280 ? -2.07300  -11.35200 -24.05000 1.000 62.57000 ? 282 LEU B CG  1 
ATOM   4281 C CD1 . LEU B 1 280 ? -2.03200  -11.36400 -22.56300 1.000 56.20000 ? 282 LEU B CD1 1 
ATOM   4282 C CD2 . LEU B 1 280 ? -3.42000  -10.95800 -24.52200 1.000 61.40000 ? 282 LEU B CD2 1 
ATOM   4283 N N   . GLY B 1 281 ? 0.62100   -9.25700  -27.38500 1.000 73.55000 ? 283 GLY B N   1 
ATOM   4284 C CA  . GLY B 1 281 ? 0.92000   -8.08300  -28.12000 1.000 76.13000 ? 283 GLY B CA  1 
ATOM   4285 C C   . GLY B 1 281 ? 2.21300   -7.65700  -27.51700 1.000 78.47000 ? 283 GLY B C   1 
ATOM   4286 O O   . GLY B 1 281 ? 2.45700   -6.47700  -27.24700 1.000 81.11000 ? 283 GLY B O   1 
ATOM   4287 N N   . SER B 1 282 ? 3.04700   -8.63100  -27.26000 1.000 73.56000 ? 284 SER B N   1 
ATOM   4288 C CA  . SER B 1 282 ? 4.29700   -8.33200  -26.70700 1.000 73.00000 ? 284 SER B CA  1 
ATOM   4289 C C   . SER B 1 282 ? 5.15300   -9.41200  -27.14700 1.000 74.43000 ? 284 SER B C   1 
ATOM   4290 O O   . SER B 1 282 ? 4.70100   -10.45500 -27.52700 1.000 74.27000 ? 284 SER B O   1 
ATOM   4291 C CB  . SER B 1 282 ? 4.25300   -8.30400  -25.21100 1.000 72.02000 ? 284 SER B CB  1 
ATOM   4292 O OG  . SER B 1 282 ? 5.55600   -8.37100  -24.70000 1.000 72.00000 ? 284 SER B OG  1 
ATOM   4293 N N   . ALA B 1 283 ? 6.41200   -9.12400  -27.11600 1.000 73.52000 ? 285 ALA B N   1 
ATOM   4294 C CA  . ALA B 1 283 ? 7.37200   -10.08700 -27.49200 1.000 73.72000 ? 285 ALA B CA  1 
ATOM   4295 C C   . ALA B 1 283 ? 8.24300   -10.42800 -26.33900 1.000 71.25000 ? 285 ALA B C   1 
ATOM   4296 O O   . ALA B 1 283 ? 9.19400   -11.15400 -26.48800 1.000 73.84000 ? 285 ALA B O   1 
ATOM   4297 C CB  . ALA B 1 283 ? 8.17000   -9.60100  -28.67200 1.000 71.96000 ? 285 ALA B CB  1 
ATOM   4298 N N   . LEU B 1 284 ? 7.90800   -9.89900  -25.18100 1.000 71.56000 ? 286 LEU B N   1 
ATOM   4299 C CA  . LEU B 1 284 ? 8.60400   -10.15400 -23.96300 1.000 70.11000 ? 286 LEU B CA  1 
ATOM   4300 C C   . LEU B 1 284 ? 7.46300   -10.55400 -23.05500 1.000 60.89000 ? 286 LEU B C   1 
ATOM   4301 O O   . LEU B 1 284 ? 6.37000   -10.19300 -23.29100 1.000 62.59000 ? 286 LEU B O   1 
ATOM   4302 C CB  . LEU B 1 284 ? 9.34500   -8.91900  -23.49300 1.000 67.30000 ? 286 LEU B CB  1 
ATOM   4303 N N   . LEU B 1 285 ? 7.74400   -11.32200 -22.04700 1.000 59.02000 ? 287 LEU B N   1 
ATOM   4304 C CA  . LEU B 1 285 ? 6.74700   -11.82500 -21.17500 1.000 57.51000 ? 287 LEU B CA  1 
ATOM   4305 C C   . LEU B 1 285 ? 6.55700   -10.92400 -19.98600 1.000 55.60000 ? 287 LEU B C   1 
ATOM   4306 O O   . LEU B 1 285 ? 7.46500   -10.66500 -19.27400 1.000 55.21000 ? 287 LEU B O   1 
ATOM   4307 C CB  . LEU B 1 285 ? 7.24000   -13.15800 -20.70600 1.000 55.48000 ? 287 LEU B CB  1 
ATOM   4308 C CG  . LEU B 1 285 ? 7.70600   -14.12300 -21.77500 1.000 54.72000 ? 287 LEU B CG  1 
ATOM   4309 C CD1 . LEU B 1 285 ? 8.89600   -14.89800 -21.34000 1.000 49.57000 ? 287 LEU B CD1 1 
ATOM   4310 C CD2 . LEU B 1 285 ? 6.59900   -15.05700 -22.09900 1.000 54.37000 ? 287 LEU B CD2 1 
ATOM   4311 N N   . GLU B 1 286 ? 5.34900   -10.46900 -19.79500 1.000 50.38000 ? 288 GLU B N   1 
ATOM   4312 C CA  . GLU B 1 286 ? 4.98900   -9.60100  -18.70800 1.000 48.38000 ? 288 GLU B CA  1 
ATOM   4313 C C   . GLU B 1 286 ? 4.97100   -10.25500 -17.36400 1.000 42.84000 ? 288 GLU B C   1 
ATOM   4314 O O   . GLU B 1 286 ? 4.45700   -11.28400 -17.23600 1.000 40.61000 ? 288 GLU B O   1 
ATOM   4315 C CB  . GLU B 1 286 ? 3.61900   -9.07300  -18.99200 1.000 45.28000 ? 288 GLU B CB  1 
ATOM   4316 C CG  . GLU B 1 286 ? 3.06900   -8.16000  -17.94700 1.000 49.35000 ? 288 GLU B CG  1 
ATOM   4317 C CD  . GLU B 1 286 ? 3.83500   -6.87600  -17.84800 1.000 50.26000 ? 288 GLU B CD  1 
ATOM   4318 O OE1 . GLU B 1 286 ? 4.19200   -6.33300  -18.85100 1.000 51.45000 ? 288 GLU B OE1 1 
ATOM   4319 O OE2 . GLU B 1 286 ? 4.08500   -6.44200  -16.76900 1.000 49.68000 ? 288 GLU B OE2 1 
ATOM   4320 N N   . ASP B 1 287 ? 5.53800   -9.61200  -16.35900 1.000 42.54000 ? 289 ASP B N   1 
ATOM   4321 C CA  . ASP B 1 287 ? 5.54900   -10.17500 -15.00900 1.000 36.96000 ? 289 ASP B CA  1 
ATOM   4322 C C   . ASP B 1 287 ? 4.97500   -9.23000  -13.95000 1.000 36.81000 ? 289 ASP B C   1 
ATOM   4323 O O   . ASP B 1 287 ? 5.19700   -9.43700  -12.75000 1.000 36.36000 ? 289 ASP B O   1 
ATOM   4324 C CB  . ASP B 1 287 ? 6.95800   -10.63500 -14.62500 1.000 40.62000 ? 289 ASP B CB  1 
ATOM   4325 C CG  . ASP B 1 287 ? 7.89600   -9.48900  -14.25100 1.000 39.50000 ? 289 ASP B CG  1 
ATOM   4326 O OD1 . ASP B 1 287 ? 7.60700   -8.30600  -14.52800 1.000 41.12000 ? 289 ASP B OD1 1 
ATOM   4327 O OD2 . ASP B 1 287 ? 8.96200   -9.80100  -13.69900 1.000 38.37000 ? 289 ASP B OD2 1 
ATOM   4328 N N   . GLU B 1 288 ? 4.22600   -8.21200  -14.35400 1.000 37.99000 ? 290 GLU B N   1 
ATOM   4329 C CA  . GLU B 1 288 ? 3.56600   -7.32200  -13.40600 1.000 39.67000 ? 290 GLU B CA  1 
ATOM   4330 C C   . GLU B 1 288 ? 2.04300   -7.46100  -13.44500 1.000 41.04000 ? 290 GLU B C   1 
ATOM   4331 O O   . GLU B 1 288 ? 1.32200   -6.49700  -13.17300 1.000 40.69000 ? 290 GLU B O   1 
ATOM   4332 C CB  . GLU B 1 288 ? 4.00400   -5.87400  -13.64600 1.000 41.82000 ? 290 GLU B CB  1 
ATOM   4333 C CG  . GLU B 1 288 ? 5.51600   -5.65800  -13.49500 1.000 44.40000 ? 290 GLU B CG  1 
ATOM   4334 C CD  . GLU B 1 288 ? 5.93100   -4.26400  -12.97400 1.000 46.68000 ? 290 GLU B CD  1 
ATOM   4335 O OE1 . GLU B 1 288 ? 5.17200   -3.28500  -13.13800 1.000 50.40000 ? 290 GLU B OE1 1 
ATOM   4336 O OE2 . GLU B 1 288 ? 7.05800   -4.15600  -12.43200 1.000 44.53000 ? 290 GLU B OE2 1 
ATOM   4337 N N   . PHE B 1 289 ? 1.54200   -8.65700  -13.77700 1.000 37.73000 ? 291 PHE B N   1 
ATOM   4338 C CA  . PHE B 1 289 ? 0.14700   -9.04500  -13.57000 1.000 37.29000 ? 291 PHE B CA  1 
ATOM   4339 C C   . PHE B 1 289 ? 0.09800   -10.23300 -12.62200 1.000 38.86000 ? 291 PHE B C   1 
ATOM   4340 O O   . PHE B 1 289 ? 0.65000   -11.29500 -12.93200 1.000 38.54000 ? 291 PHE B O   1 
ATOM   4341 C CB  . PHE B 1 289 ? -0.53300  -9.45600  -14.87200 1.000 41.75000 ? 291 PHE B CB  1 
ATOM   4342 C CG  . PHE B 1 289 ? -1.08600  -8.32800  -15.66800 1.000 45.55000 ? 291 PHE B CG  1 
ATOM   4343 C CD1 . PHE B 1 289 ? -2.28000  -7.72700  -15.30700 1.000 45.81000 ? 291 PHE B CD1 1 
ATOM   4344 C CD2 . PHE B 1 289 ? -0.44000  -7.90900  -16.82400 1.000 50.43000 ? 291 PHE B CD2 1 
ATOM   4345 C CE1 . PHE B 1 289 ? -2.81100  -6.69800  -16.06600 1.000 53.99000 ? 291 PHE B CE1 1 
ATOM   4346 C CE2 . PHE B 1 289 ? -0.96500  -6.88600  -17.59600 1.000 54.37000 ? 291 PHE B CE2 1 
ATOM   4347 C CZ  . PHE B 1 289 ? -2.15400  -6.27900  -17.22000 1.000 52.28000 ? 291 PHE B CZ  1 
ATOM   4348 N N   . THR B 1 290 ? -0.61900  -10.09100 -11.56000 1.000 35.84000 ? 292 THR B N   1 
ATOM   4349 C CA  . THR B 1 290 ? -0.78400  -11.15300 -10.66300 1.000 37.25000 ? 292 THR B CA  1 
ATOM   4350 C C   . THR B 1 290 ? -1.93600  -12.06900 -11.05800 1.000 37.41000 ? 292 THR B C   1 
ATOM   4351 O O   . THR B 1 290 ? -2.73900  -11.73300 -11.82400 1.000 36.61000 ? 292 THR B O   1 
ATOM   4352 C CB  . THR B 1 290 ? -0.99100  -10.66200 -9.23800  1.000 41.29000 ? 292 THR B CB  1 
ATOM   4353 O OG1 . THR B 1 290 ? -2.30400  -10.25000 -9.09400  1.000 36.00000 ? 292 THR B OG1 1 
ATOM   4354 C CG2 . THR B 1 290 ? -0.12800  -9.56900  -8.92700  1.000 37.29000 ? 292 THR B CG2 1 
ATOM   4355 N N   . PRO B 1 291 ? -1.94200  -13.28100 -10.41500 1.000 38.52000 ? 293 PRO B N   1 
ATOM   4356 C CA  . PRO B 1 291 ? -3.07100  -14.15200 -10.72800 1.000 41.53000 ? 293 PRO B CA  1 
ATOM   4357 C C   . PRO B 1 291 ? -4.37200  -13.48300 -10.40400 1.000 45.78000 ? 293 PRO B C   1 
ATOM   4358 O O   . PRO B 1 291 ? -5.29000  -13.56000 -11.13200 1.000 47.71000 ? 293 PRO B O   1 
ATOM   4359 C CB  . PRO B 1 291 ? -2.89400  -15.29800 -9.79100  1.000 40.83000 ? 293 PRO B CB  1 
ATOM   4360 C CG  . PRO B 1 291 ? -1.49100  -15.45200 -9.68200  1.000 43.05000 ? 293 PRO B CG  1 
ATOM   4361 C CD  . PRO B 1 291 ? -0.96200  -14.10300 -9.59300  1.000 37.09000 ? 293 PRO B CD  1 
ATOM   4362 N N   . PHE B 1 292 ? -4.40900  -12.78100 -9.30200  1.000 50.58000 ? 294 PHE B N   1 
ATOM   4363 C CA  . PHE B 1 292 ? -5.57200  -12.06200 -8.88000  1.000 49.08000 ? 294 PHE B CA  1 
ATOM   4364 C C   . PHE B 1 292 ? -5.93100  -11.03200 -9.89000  1.000 46.51000 ? 294 PHE B C   1 
ATOM   4365 O O   . PHE B 1 292 ? -7.03400  -10.91500 -10.21300 1.000 49.67000 ? 294 PHE B O   1 
ATOM   4366 C CB  . PHE B 1 292 ? -5.28500  -11.41300 -7.56000  1.000 49.14000 ? 294 PHE B CB  1 
ATOM   4367 C CG  . PHE B 1 292 ? -6.48900  -11.12900 -6.75700  1.000 59.52000 ? 294 PHE B CG  1 
ATOM   4368 C CD1 . PHE B 1 292 ? -7.42000  -10.24200 -7.19200  1.000 61.12000 ? 294 PHE B CD1 1 
ATOM   4369 C CD2 . PHE B 1 292 ? -6.68000  -11.75200 -5.54600  1.000 60.71000 ? 294 PHE B CD2 1 
ATOM   4370 C CE1 . PHE B 1 292 ? -8.53800  -9.97100  -6.45800  1.000 61.87000 ? 294 PHE B CE1 1 
ATOM   4371 C CE2 . PHE B 1 292 ? -7.78700  -11.49800 -4.80500  1.000 66.93000 ? 294 PHE B CE2 1 
ATOM   4372 C CZ  . PHE B 1 292 ? -8.72200  -10.59300 -5.26300  1.000 65.53000 ? 294 PHE B CZ  1 
ATOM   4373 N N   . ASP B 1 293 ? -4.96800  -10.33200 -10.42800 1.000 44.38000 ? 295 ASP B N   1 
ATOM   4374 C CA  . ASP B 1 293 ? -5.23100  -9.31000  -11.39200 1.000 43.55000 ? 295 ASP B CA  1 
ATOM   4375 C C   . ASP B 1 293 ? -5.92700  -9.92700  -12.57000 1.000 48.64000 ? 295 ASP B C   1 
ATOM   4376 O O   . ASP B 1 293 ? -6.80100  -9.35800  -13.08900 1.000 49.52000 ? 295 ASP B O   1 
ATOM   4377 C CB  . ASP B 1 293 ? -3.94800  -8.62100  -11.86200 1.000 39.69000 ? 295 ASP B CB  1 
ATOM   4378 C CG  . ASP B 1 293 ? -3.29800  -7.77600  -10.82300 1.000 43.12000 ? 295 ASP B CG  1 
ATOM   4379 O OD1 . ASP B 1 293 ? -3.94400  -7.38100  -9.89500  1.000 45.87000 ? 295 ASP B OD1 1 
ATOM   4380 O OD2 . ASP B 1 293 ? -2.13400  -7.51700  -10.91700 1.000 39.53000 ? 295 ASP B OD2 1 
ATOM   4381 N N   . VAL B 1 294 ? -5.52200  -11.11400 -12.97300 1.000 51.62000 ? 296 VAL B N   1 
ATOM   4382 C CA  . VAL B 1 294 ? -6.09400  -11.76100 -14.15000 1.000 53.92000 ? 296 VAL B CA  1 
ATOM   4383 C C   . VAL B 1 294 ? -7.52500  -12.20700 -13.87100 1.000 52.66000 ? 296 VAL B C   1 
ATOM   4384 O O   . VAL B 1 294 ? -8.41700  -12.01200 -14.70000 1.000 56.43000 ? 296 VAL B O   1 
ATOM   4385 C CB  . VAL B 1 294 ? -5.20200  -12.94000 -14.59500 1.000 49.20000 ? 296 VAL B CB  1 
ATOM   4386 C CG1 . VAL B 1 294 ? -5.90700  -13.77100 -15.66300 1.000 50.90000 ? 296 VAL B CG1 1 
ATOM   4387 C CG2 . VAL B 1 294 ? -3.84200  -12.43900 -15.09700 1.000 45.19000 ? 296 VAL B CG2 1 
ATOM   4388 N N   . VAL B 1 295 ? -7.76600  -12.80500 -12.70000 1.000 56.77000 ? 297 VAL B N   1 
ATOM   4389 C CA  . VAL B 1 295 ? -9.12300  -13.22100 -12.33300 1.000 59.21000 ? 297 VAL B CA  1 
ATOM   4390 C C   . VAL B 1 295 ? -10.08300 -12.04300 -12.41800 1.000 58.95000 ? 297 VAL B C   1 
ATOM   4391 O O   . VAL B 1 295 ? -11.25000 -12.19700 -12.80500 1.000 66.70000 ? 297 VAL B O   1 
ATOM   4392 C CB  . VAL B 1 295 ? -9.12900  -13.86700 -10.93100 1.000 58.13000 ? 297 VAL B CB  1 
ATOM   4393 C CG1 . VAL B 1 295 ? -10.52400 -14.36900 -10.58000 1.000 60.72000 ? 297 VAL B CG1 1 
ATOM   4394 C CG2 . VAL B 1 295 ? -8.13600  -15.02400 -10.86800 1.000 55.99000 ? 297 VAL B CG2 1 
ATOM   4395 N N   . ARG B 1 296 ? -9.60800  -10.84600 -12.08600 1.000 58.85000 ? 298 ARG B N   1 
ATOM   4396 C CA  . ARG B 1 296 ? -10.40400 -9.62900  -12.20700 1.000 59.96000 ? 298 ARG B CA  1 
ATOM   4397 C C   . ARG B 1 296 ? -10.15500 -8.96300  -13.55400 1.000 59.48000 ? 298 ARG B C   1 
ATOM   4398 O O   . ARG B 1 296 ? -10.32300 -9.58400  -14.60500 1.000 66.35000 ? 298 ARG B O   1 
ATOM   4399 C CB  . ARG B 1 296 ? -10.08000 -8.65600  -11.06600 1.000 56.74000 ? 298 ARG B CB  1 
HETATM 4400 C C10 . FNO C 2 .   ? -22.73400 -3.10300  -29.27900 1.000 62.09000 ? 301 FNO A C10 1 
HETATM 4401 C C13 . FNO C 2 .   ? -22.56700 -0.56400  -30.12600 1.000 58.48000 ? 301 FNO A C13 1 
HETATM 4402 C C15 . FNO C 2 .   ? -22.54900 -2.34100  -26.96800 1.000 61.39000 ? 301 FNO A C15 1 
HETATM 4403 C C17 . FNO C 2 .   ? -20.21700 -4.91000  -33.70900 1.000 61.10000 ? 301 FNO A C17 1 
HETATM 4404 C C20 . FNO C 2 .   ? -19.21300 -4.18600  -34.59500 1.000 59.07000 ? 301 FNO A C20 1 
HETATM 4405 C C21 . FNO C 2 .   ? -20.78800 -6.25800  -34.08200 1.000 59.40000 ? 301 FNO A C21 1 
HETATM 4406 C C06 . FNO C 2 .   ? -22.91500 -4.10400  -31.59600 1.000 65.59000 ? 301 FNO A C06 1 
HETATM 4407 C C07 . FNO C 2 .   ? -22.77600 -2.90000  -30.63400 1.000 62.67000 ? 301 FNO A C07 1 
HETATM 4408 C C08 . FNO C 2 .   ? -21.63400 -4.95400  -31.68900 1.000 65.30000 ? 301 FNO A C08 1 
HETATM 4409 C C09 . FNO C 2 .   ? -22.58600 -2.06800  -28.33400 1.000 59.48000 ? 301 FNO A C09 1 
HETATM 4410 C C11 . FNO C 2 .   ? -22.52700 -0.81100  -28.72800 1.000 56.55000 ? 301 FNO A C11 1 
HETATM 4411 C C12 . FNO C 2 .   ? -22.67600 -1.58600  -31.06400 1.000 58.88000 ? 301 FNO A C12 1 
HETATM 4412 C C14 . FNO C 2 .   ? -20.61200 -4.35300  -32.61800 1.000 61.22000 ? 301 FNO A C14 1 
HETATM 4413 C C16 . FNO C 2 .   ? -22.40800 0.20000   -27.73400 1.000 53.45000 ? 301 FNO A C16 1 
HETATM 4414 C C18 . FNO C 2 .   ? -22.41900 -1.38900  -25.99900 1.000 55.89000 ? 301 FNO A C18 1 
HETATM 4415 C C19 . FNO C 2 .   ? -22.32600 -0.08600  -26.39200 1.000 56.34000 ? 301 FNO A C19 1 
HETATM 4416 O O01 . FNO C 2 .   ? -23.21800 -3.67700  -32.85000 1.000 63.57000 ? 301 FNO A O01 1 
HETATM 4417 O O02 . FNO C 2 .   ? -22.82100 -4.18300  -28.91400 1.000 68.42000 ? 301 FNO A O02 1 
HETATM 4418 O O03 . FNO C 2 .   ? -22.64900 -3.63700  -26.58000 1.000 68.84000 ? 301 FNO A O03 1 
HETATM 4419 O O04 . FNO C 2 .   ? -22.47200 0.53100   -30.50000 1.000 57.55000 ? 301 FNO A O04 1 
HETATM 4420 O O05 . FNO C 2 .   ? -22.33200 1.50500   -28.04500 1.000 49.06000 ? 301 FNO A O05 1 
HETATM 4421 O O   . HOH D 3 .   ? 18.32100  -1.11800  -43.87900 1.000 41.77000 ? 401 HOH A O   1 
HETATM 4422 O O   . HOH D 3 .   ? 18.00700  5.61700   -46.93800 1.000 35.99000 ? 402 HOH A O   1 
HETATM 4423 O O   . HOH D 3 .   ? 22.72500  15.92800  -35.12200 1.000 38.48000 ? 403 HOH A O   1 
HETATM 4424 O O   . HOH D 3 .   ? 18.53300  10.57700  -51.54800 1.000 40.40000 ? 404 HOH A O   1 
HETATM 4425 O O   . HOH D 3 .   ? 21.47200  2.31200   -33.73000 1.000 38.84000 ? 405 HOH A O   1 
HETATM 4426 O O   . HOH D 3 .   ? 16.57900  19.04700  -37.20000 1.000 45.18000 ? 406 HOH A O   1 
HETATM 4427 O O   . HOH D 3 .   ? -23.09400 19.45200  -20.12900 1.000 38.49000 ? 407 HOH A O   1 
HETATM 4428 O O   . HOH D 3 .   ? -11.73400 21.27100  -12.41100 1.000 41.67000 ? 408 HOH A O   1 
HETATM 4429 O O   . HOH D 3 .   ? 5.36000   -0.88500  -37.48400 1.000 40.30000 ? 409 HOH A O   1 
HETATM 4430 O O   . HOH D 3 .   ? 1.70300   10.89300  -41.67700 1.000 40.53000 ? 410 HOH A O   1 
HETATM 4431 O O   . HOH D 3 .   ? -15.32900 15.47800  -27.76400 1.000 33.00000 ? 411 HOH A O   1 
HETATM 4432 O O   . HOH D 3 .   ? -17.66400 7.29000   -39.16300 1.000 38.56000 ? 412 HOH A O   1 
HETATM 4433 O O   . HOH D 3 .   ? 20.75300  5.34700   -40.77800 1.000 34.64000 ? 413 HOH A O   1 
HETATM 4434 O O   . HOH D 3 .   ? -15.84000 15.27200  -10.39300 1.000 36.94000 ? 414 HOH A O   1 
HETATM 4435 O O   . HOH D 3 .   ? 15.88200  0.01500   -42.14600 1.000 36.13000 ? 415 HOH A O   1 
HETATM 4436 O O   . HOH D 3 .   ? -8.40700  15.45300  -24.44800 1.000 38.03000 ? 416 HOH A O   1 
HETATM 4437 O O   . HOH D 3 .   ? -0.47900  22.66600  -39.65900 1.000 45.09000 ? 417 HOH A O   1 
HETATM 4438 O O   . HOH D 3 .   ? 1.72100   12.76000  -32.05200 1.000 31.89000 ? 418 HOH A O   1 
HETATM 4439 O O   . HOH D 3 .   ? -1.98200  12.61900  -22.93700 1.000 35.22000 ? 419 HOH A O   1 
HETATM 4440 O O   . HOH D 3 .   ? -4.28000  2.59700   -28.30200 1.000 32.46000 ? 420 HOH A O   1 
HETATM 4441 O O   . HOH D 3 .   ? -15.36500 6.96100   -17.98100 1.000 24.24000 ? 421 HOH A O   1 
HETATM 4442 O O   . HOH D 3 .   ? 19.12700  9.96300   -47.44800 1.000 34.57000 ? 422 HOH A O   1 
HETATM 4443 O O   . HOH D 3 .   ? 15.76600  12.04700  -51.20300 1.000 37.79000 ? 423 HOH A O   1 
HETATM 4444 O O   . HOH D 3 .   ? -29.37600 2.94600   -14.68800 1.000 39.71000 ? 424 HOH A O   1 
HETATM 4445 O O   . HOH D 3 .   ? 13.22800  14.67300  -48.82800 1.000 41.77000 ? 425 HOH A O   1 
HETATM 4446 O O   . HOH D 3 .   ? -12.96500 4.97400   -33.15300 1.000 29.65000 ? 426 HOH A O   1 
HETATM 4447 O O   . HOH D 3 .   ? -22.45200 17.19400  -27.12700 1.000 37.56000 ? 427 HOH A O   1 
HETATM 4448 O O   . HOH D 3 .   ? 6.18000   7.57200   -28.09600 1.000 34.48000 ? 428 HOH A O   1 
HETATM 4449 O O   . HOH D 3 .   ? 21.31900  1.07800   -43.77000 1.000 35.65000 ? 429 HOH A O   1 
HETATM 4450 O O   . HOH D 3 .   ? 4.06600   10.07800  -37.39200 1.000 32.44000 ? 430 HOH A O   1 
HETATM 4451 O O   . HOH D 3 .   ? -20.36400 9.32700   -36.48600 1.000 35.50000 ? 431 HOH A O   1 
HETATM 4452 O O   . HOH D 3 .   ? -28.05400 11.55100  -35.10600 1.000 35.25000 ? 432 HOH A O   1 
HETATM 4453 O O   . HOH D 3 .   ? 1.28000   9.32000   -22.77900 1.000 41.84000 ? 433 HOH A O   1 
HETATM 4454 O O   . HOH D 3 .   ? -23.88100 18.36600  -33.92200 1.000 50.30000 ? 434 HOH A O   1 
HETATM 4455 O O   . HOH D 3 .   ? 8.22500   12.19700  -48.10800 1.000 39.09000 ? 435 HOH A O   1 
HETATM 4456 O O   . HOH D 3 .   ? -33.15500 14.33900  -30.98500 1.000 39.46000 ? 436 HOH A O   1 
HETATM 4457 O O   . HOH D 3 .   ? -12.32600 10.26500  -38.33700 1.000 42.79000 ? 437 HOH A O   1 
HETATM 4458 O O   . HOH D 3 .   ? -31.68000 -4.71900  -36.53400 1.000 45.24000 ? 438 HOH A O   1 
HETATM 4459 O O   . HOH D 3 .   ? 20.14300  8.38700   -45.70600 1.000 37.35000 ? 439 HOH A O   1 
HETATM 4460 O O   . HOH D 3 .   ? -22.10700 13.70700  -7.96300  1.000 37.86000 ? 440 HOH A O   1 
HETATM 4461 O O   . HOH D 3 .   ? 16.81500  7.95900   -53.18000 1.000 39.88000 ? 441 HOH A O   1 
HETATM 4462 O O   . HOH D 3 .   ? -24.48900 10.65800  -6.33700  1.000 55.77000 ? 442 HOH A O   1 
HETATM 4463 O O   . HOH D 3 .   ? -11.01100 6.19700   -6.26200  1.000 36.09000 ? 443 HOH A O   1 
HETATM 4464 O O   . HOH D 3 .   ? 16.65300  17.81500  -39.50800 1.000 37.99000 ? 444 HOH A O   1 
HETATM 4465 O O   . HOH D 3 .   ? -27.35700 15.29500  -34.91100 1.000 41.00000 ? 445 HOH A O   1 
HETATM 4466 O O   . HOH D 3 .   ? -37.44800 15.76600  -25.26800 1.000 46.25000 ? 446 HOH A O   1 
HETATM 4467 O O   . HOH D 3 .   ? 2.04900   9.21800   -20.30900 1.000 46.05000 ? 447 HOH A O   1 
HETATM 4468 O O   . HOH D 3 .   ? 3.56000   1.36500   -28.07900 1.000 47.55000 ? 448 HOH A O   1 
HETATM 4469 O O   . HOH D 3 .   ? 0.57200   12.59100  -34.77300 1.000 40.62000 ? 449 HOH A O   1 
HETATM 4470 O O   . HOH D 3 .   ? 20.79800  -0.30700  -22.64400 1.000 53.37000 ? 450 HOH A O   1 
HETATM 4471 O O   . HOH D 3 .   ? 21.56600  -0.28500  -33.81400 1.000 38.75000 ? 451 HOH A O   1 
HETATM 4472 O O   . HOH D 3 .   ? -15.00500 12.12900  -7.13200  1.000 49.96000 ? 452 HOH A O   1 
HETATM 4473 O O   . HOH D 3 .   ? -12.52100 8.40100   -41.04600 1.000 46.48000 ? 453 HOH A O   1 
HETATM 4474 O O   . HOH D 3 .   ? 1.04400   10.87000  -36.50100 1.000 46.61000 ? 454 HOH A O   1 
HETATM 4475 O O   . HOH D 3 .   ? 20.80500  2.60700   -41.69000 1.000 37.60000 ? 455 HOH A O   1 
HETATM 4476 O O   . HOH E 3 .   ? 1.24200   24.20400  8.37100   1.000 52.56000 ? 301 HOH B O   1 
HETATM 4477 O O   . HOH E 3 .   ? 15.43000  14.36300  2.55400   1.000 50.61000 ? 302 HOH B O   1 
HETATM 4478 O O   . HOH E 3 .   ? 11.04200  -1.01700  11.22200  1.000 33.79000 ? 303 HOH B O   1 
HETATM 4479 O O   . HOH E 3 .   ? 2.41400   -12.19000 -7.55900  1.000 40.35000 ? 304 HOH B O   1 
HETATM 4480 O O   . HOH E 3 .   ? 1.21000   0.01700   5.04800   1.000 30.02000 ? 305 HOH B O   1 
HETATM 4481 O O   . HOH E 3 .   ? -1.53800  -5.29100  -12.13900 1.000 40.24000 ? 306 HOH B O   1 
HETATM 4482 O O   . HOH E 3 .   ? 0.30300   9.91400   -3.71100  1.000 35.11000 ? 307 HOH B O   1 
HETATM 4483 O O   . HOH E 3 .   ? -10.48800 11.46500  -0.91900  1.000 44.91000 ? 308 HOH B O   1 
HETATM 4484 O O   . HOH E 3 .   ? -3.11800  -4.45800  -8.25400  1.000 35.28000 ? 309 HOH B O   1 
HETATM 4485 O O   . HOH E 3 .   ? 2.35100   5.56300   10.50000  1.000 41.21000 ? 310 HOH B O   1 
HETATM 4486 O O   . HOH E 3 .   ? 3.75400   -2.99800  8.57600   1.000 39.22000 ? 311 HOH B O   1 
HETATM 4487 O O   . HOH E 3 .   ? 9.60300   -7.41700  3.61300   1.000 39.47000 ? 312 HOH B O   1 
HETATM 4488 O O   . HOH E 3 .   ? -4.84600  8.93500   10.42500  1.000 35.48000 ? 313 HOH B O   1 
HETATM 4489 O O   . HOH E 3 .   ? 17.52800  -5.21700  -3.15800  1.000 38.42000 ? 314 HOH B O   1 
HETATM 4490 O O   . HOH E 3 .   ? -8.53400  14.16300  -11.22600 1.000 33.60000 ? 315 HOH B O   1 
HETATM 4491 O O   . HOH E 3 .   ? 15.73600  -3.09900  -9.44800  1.000 40.27000 ? 316 HOH B O   1 
HETATM 4492 O O   . HOH E 3 .   ? 12.05400  -5.97400  3.06800   1.000 31.50000 ? 317 HOH B O   1 
HETATM 4493 O O   . HOH E 3 .   ? -2.42300  -2.47300  -1.07000  1.000 30.01000 ? 318 HOH B O   1 
HETATM 4494 O O   . HOH E 3 .   ? -4.644    0.301     9.201     1.000 31.74000 ? 319 HOH B O   1 
HETATM 4495 O O   . HOH E 3 .   ? 11.46800  -0.26000  -1.35500  1.000 26.97000 ? 320 HOH B O   1 
HETATM 4496 O O   . HOH E 3 .   ? 2.34700   -10.75200 -15.49300 1.000 34.40000 ? 321 HOH B O   1 
HETATM 4497 O O   . HOH E 3 .   ? 10.62400  -32.10100 -16.96200 1.000 46.25000 ? 322 HOH B O   1 
HETATM 4498 O O   . HOH E 3 .   ? 7.18400   -7.88700  2.53800   1.000 39.16000 ? 323 HOH B O   1 
HETATM 4499 O O   . HOH E 3 .   ? 8.65500   0.88300   15.85100  1.000 40.06000 ? 324 HOH B O   1 
HETATM 4500 O O   . HOH E 3 .   ? 15.28800  -9.30500  -2.07400  1.000 40.37000 ? 325 HOH B O   1 
HETATM 4501 O O   . HOH E 3 .   ? 12.58600  9.00100   5.24300   1.000 33.86000 ? 326 HOH B O   1 
HETATM 4502 O O   . HOH E 3 .   ? -1.61100  -7.12100  -5.08800  1.000 39.85000 ? 327 HOH B O   1 
HETATM 4503 O O   . HOH E 3 .   ? -0.30100  -6.26800  6.27200   1.000 38.30000 ? 328 HOH B O   1 
HETATM 4504 O O   . HOH E 3 .   ? -11.23400 3.33700   7.60700   1.000 36.10000 ? 329 HOH B O   1 
HETATM 4505 O O   . HOH E 3 .   ? 7.37200   -16.58900 -8.69100  1.000 43.57000 ? 330 HOH B O   1 
HETATM 4506 O O   . HOH E 3 .   ? -14.20000 5.29600   0.96800   1.000 41.39000 ? 331 HOH B O   1 
HETATM 4507 O O   . HOH E 3 .   ? 16.08200  3.42100   7.61100   1.000 36.79000 ? 332 HOH B O   1 
HETATM 4508 O O   . HOH E 3 .   ? 9.11000   3.75800   15.93200  1.000 42.60000 ? 333 HOH B O   1 
HETATM 4509 O O   . HOH E 3 .   ? -12.73900 4.21700   -6.21100  1.000 46.19000 ? 334 HOH B O   1 
HETATM 4510 O O   . HOH E 3 .   ? 11.95900  -6.16500  5.95100   1.000 39.67000 ? 335 HOH B O   1 
# 
