data_9MQL
# 
_entry.id   9MQL 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9MQL         pdb_00009mql 10.2210/pdb9mql/pdb 
WWPDB D_1000291542 ?            ?                   
EMDB  EMD-48528    ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-02-12 ? 
2 'EM metadata'     1 0 2025-02-12 ? 
3 'Half map'        1 0 2025-02-12 1 
4 'Half map'        1 0 2025-02-12 2 
5 Image             1 0 2025-02-12 ? 
6 'Primary map'     1 0 2025-02-12 ? 
7 'Structure model' 1 1 2025-03-12 ? 
8 'EM metadata'     1 1 2025-03-12 ? 
# 
loop_
_pdbx_audit_revision_details.ordinal 
_pdbx_audit_revision_details.revision_ordinal 
_pdbx_audit_revision_details.data_content_type 
_pdbx_audit_revision_details.provider 
_pdbx_audit_revision_details.type 
_pdbx_audit_revision_details.description 
_pdbx_audit_revision_details.details 
1 1 'Structure model' repository 'Initial release' ? ? 
2 2 'EM metadata'     repository 'Initial release' ? ? 
3 3 'Half map'        repository 'Initial release' ? ? 
4 4 'Half map'        repository 'Initial release' ? ? 
5 5 Image             repository 'Initial release' ? ? 
6 6 'Primary map'     repository 'Initial release' ? ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 7 'Structure model' 'Data collection'      
2 7 'Structure model' 'Source and taxonomy'  
3 7 'Structure model' 'Structure summary'    
4 8 'EM metadata'     'Experimental summary' 
5 8 'EM metadata'     'Source and taxonomy'  
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1  7 'Structure model' em_admin                         
2  7 'Structure model' em_entity_assembly               
3  7 'Structure model' em_entity_assembly_naturalsource 
4  7 'Structure model' em_entity_assembly_recombinant   
5  7 'Structure model' entity_src_gen                   
6  8 'EM metadata'     em_admin                         
7  8 'EM metadata'     em_entity_assembly               
8  8 'EM metadata'     em_entity_assembly_naturalsource 
9  8 'EM metadata'     em_entity_assembly_recombinant   
10 8 'EM metadata'     entity_src_gen                   
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1  7 'Structure model' '_em_admin.last_update'                          
2  7 'Structure model' '_em_entity_assembly.name'                       
3  7 'Structure model' '_em_entity_assembly_naturalsource.ncbi_tax_id'  
4  7 'Structure model' '_em_entity_assembly_naturalsource.organism'     
5  7 'Structure model' '_em_entity_assembly_recombinant.ncbi_tax_id'    
6  7 'Structure model' '_em_entity_assembly_recombinant.organism'       
7  7 'Structure model' '_entity_src_gen.gene_src_common_name'           
8  7 'Structure model' '_entity_src_gen.host_org_common_name'           
9  7 'Structure model' '_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id' 
10 7 'Structure model' '_entity_src_gen.pdbx_gene_src_scientific_name'  
11 7 'Structure model' '_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id' 
12 7 'Structure model' '_entity_src_gen.pdbx_host_org_scientific_name'  
13 8 'EM metadata'     '_em_admin.last_update'                          
14 8 'EM metadata'     '_em_entity_assembly.name'                       
15 8 'EM metadata'     '_em_entity_assembly_naturalsource.ncbi_tax_id'  
16 8 'EM metadata'     '_em_entity_assembly_naturalsource.organism'     
17 8 'EM metadata'     '_em_entity_assembly_recombinant.ncbi_tax_id'    
18 8 'EM metadata'     '_em_entity_assembly_recombinant.organism'       
19 8 'EM metadata'     '_entity_src_gen.gene_src_common_name'           
20 8 'EM metadata'     '_entity_src_gen.host_org_common_name'           
21 8 'EM metadata'     '_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id' 
22 8 'EM metadata'     '_entity_src_gen.pdbx_gene_src_scientific_name'  
23 8 'EM metadata'     '_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id' 
24 8 'EM metadata'     '_entity_src_gen.pdbx_host_org_scientific_name'  
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  ? 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9MQL 
_pdbx_database_status.recvd_initial_deposition_date   2025-01-03 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.details 
_pdbx_database_related.db_id 
_pdbx_database_related.content_type 
PDB  .                                                                                                        9MQK      
unspecified            
EMDB .                                                                                                        EMD-48527 
'other EM volume'      
EMDB 'Locally-Refined Inactive Kappa-Opioid Receptor with Nb6M, NabFab, and isoquinuclidine compound #020_E1' EMD-48528 
'associated EM volume' 
# 
loop_
_pdbx_contact_author.id 
_pdbx_contact_author.email 
_pdbx_contact_author.name_first 
_pdbx_contact_author.name_last 
_pdbx_contact_author.name_mi 
_pdbx_contact_author.role 
_pdbx_contact_author.identifier_ORCID 
4 aashish.manglik@ucsf.edu Aashish Manglik  ?  'principal investigator/group leader' 0000-0002-7173-3741 
5 bshoichet@gmail.com      Brian   Shoichet K. 'principal investigator/group leader' 0000-0002-6098-7367 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Kim, J.Y.'       1 ? 
'Vigneron, S.F.'  2 ? 
'Billesbolle, C.' 3 ? 
'Manglik, A.'     4 ? 
'Shoichet, B.K.'  5 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Biorxiv 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2692-8205 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     
;Docking 14 million virtual isoquinuclidines against the mu and kappa opioid receptors reveals dual antagonists-inverse agonists with reduced withdrawal effects.
;
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1101/2025.01.09.632033 
_citation.pdbx_database_id_PubMed   39868130 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Vigneron, S.F.'  1  0000-0003-2671-3044 
primary 'Ohno, S.'        2  0000-0002-2414-5066 
primary 'Braz, J.'        3  ?                   
primary 'Kim, J.Y.'       4  0000-0002-6816-5958 
primary 'Kweon, O.S.'     5  0000-0001-6588-3420 
primary 'Webb, C.'        6  0000-0003-2784-0408 
primary 'Billesbolle, C.' 7  0000-0001-8084-1552 
primary 'Bhardwaj, K.'    8  0009-0000-1769-0210 
primary 'Irwin, J.'       9  0000-0002-1195-6417 
primary 'Manglik, A.'     10 0000-0002-7173-3741 
primary 'Basbaum, A.I.'   11 0000-0002-1710-6333 
primary 'Ellman, J.A.'    12 0000-0001-9320-5512 
primary 'Shoichet, B.K.'  13 0000-0002-6098-7367 
# 
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 'Kappa-Opioid Receptor' 43626.902 1 ? ? ? ? 
2 non-polymer syn 
;methyl (1S,3R,4S,6S,8M)-2-[(1-ethyl-1H-pyrazol-4-yl)methyl]-8-(3-hydroxyphenyl)-3,4-dimethyl-2-azabicyclo[2.2.2]oct-7-ene-6-carboxylate
;
395.495   1 ? ? ? ? 
# 
_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       
;DYKDDDDAMESPIQIFRGDPGPTCSPSACLLPNSSSWFPNWAESDSNGSVGSEDQQLESAHISPAIPVIITAVYSVVFVV
GLVGNSLVMFVIIRYTKMKTATNIYIFNLALADALVTTTMPFQSAVYLMNSWPFGDVLCKIVISIDYYNMFTSIFTLTMM
SVDRYIAVCHPVKALDFRTPLKAKIINICIWLLASSVGISAIVLGGTKVREDVDVIECSLQFPDDEYSWWDLFMKICVFV
FAFVIPVLIIIVCYTLMILRLKSVRLLSGSREKDRNLRRITKLVLVVVAVFIICWTPIHIFILVEALGSTSHSTAALSSY
YFCIALGYTNSSLNPVLYAFLDENFKRCFRDFCFPIKMRMERQSTNRVRNTVQDPASMRDVGGMNKPV
;
_entity_poly.pdbx_seq_one_letter_code_can   
;DYKDDDDAMESPIQIFRGDPGPTCSPSACLLPNSSSWFPNWAESDSNGSVGSEDQQLESAHISPAIPVIITAVYSVVFVV
GLVGNSLVMFVIIRYTKMKTATNIYIFNLALADALVTTTMPFQSAVYLMNSWPFGDVLCKIVISIDYYNMFTSIFTLTMM
SVDRYIAVCHPVKALDFRTPLKAKIINICIWLLASSVGISAIVLGGTKVREDVDVIECSLQFPDDEYSWWDLFMKICVFV
FAFVIPVLIIIVCYTLMILRLKSVRLLSGSREKDRNLRRITKLVLVVVAVFIICWTPIHIFILVEALGSTSHSTAALSSY
YFCIALGYTNSSLNPVLYAFLDENFKRCFRDFCFPIKMRMERQSTNRVRNTVQDPASMRDVGGMNKPV
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
_pdbx_entity_nonpoly.entity_id   2 
_pdbx_entity_nonpoly.name        
;methyl (1S,3R,4S,6S,8M)-2-[(1-ethyl-1H-pyrazol-4-yl)methyl]-8-(3-hydroxyphenyl)-3,4-dimethyl-2-azabicyclo[2.2.2]oct-7-ene-6-carboxylate
;
_pdbx_entity_nonpoly.comp_id     A1BNM 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   ASP n 
1 2   TYR n 
1 3   LYS n 
1 4   ASP n 
1 5   ASP n 
1 6   ASP n 
1 7   ASP n 
1 8   ALA n 
1 9   MET n 
1 10  GLU n 
1 11  SER n 
1 12  PRO n 
1 13  ILE n 
1 14  GLN n 
1 15  ILE n 
1 16  PHE n 
1 17  ARG n 
1 18  GLY n 
1 19  ASP n 
1 20  PRO n 
1 21  GLY n 
1 22  PRO n 
1 23  THR n 
1 24  CYS n 
1 25  SER n 
1 26  PRO n 
1 27  SER n 
1 28  ALA n 
1 29  CYS n 
1 30  LEU n 
1 31  LEU n 
1 32  PRO n 
1 33  ASN n 
1 34  SER n 
1 35  SER n 
1 36  SER n 
1 37  TRP n 
1 38  PHE n 
1 39  PRO n 
1 40  ASN n 
1 41  TRP n 
1 42  ALA n 
1 43  GLU n 
1 44  SER n 
1 45  ASP n 
1 46  SER n 
1 47  ASN n 
1 48  GLY n 
1 49  SER n 
1 50  VAL n 
1 51  GLY n 
1 52  SER n 
1 53  GLU n 
1 54  ASP n 
1 55  GLN n 
1 56  GLN n 
1 57  LEU n 
1 58  GLU n 
1 59  SER n 
1 60  ALA n 
1 61  HIS n 
1 62  ILE n 
1 63  SER n 
1 64  PRO n 
1 65  ALA n 
1 66  ILE n 
1 67  PRO n 
1 68  VAL n 
1 69  ILE n 
1 70  ILE n 
1 71  THR n 
1 72  ALA n 
1 73  VAL n 
1 74  TYR n 
1 75  SER n 
1 76  VAL n 
1 77  VAL n 
1 78  PHE n 
1 79  VAL n 
1 80  VAL n 
1 81  GLY n 
1 82  LEU n 
1 83  VAL n 
1 84  GLY n 
1 85  ASN n 
1 86  SER n 
1 87  LEU n 
1 88  VAL n 
1 89  MET n 
1 90  PHE n 
1 91  VAL n 
1 92  ILE n 
1 93  ILE n 
1 94  ARG n 
1 95  TYR n 
1 96  THR n 
1 97  LYS n 
1 98  MET n 
1 99  LYS n 
1 100 THR n 
1 101 ALA n 
1 102 THR n 
1 103 ASN n 
1 104 ILE n 
1 105 TYR n 
1 106 ILE n 
1 107 PHE n 
1 108 ASN n 
1 109 LEU n 
1 110 ALA n 
1 111 LEU n 
1 112 ALA n 
1 113 ASP n 
1 114 ALA n 
1 115 LEU n 
1 116 VAL n 
1 117 THR n 
1 118 THR n 
1 119 THR n 
1 120 MET n 
1 121 PRO n 
1 122 PHE n 
1 123 GLN n 
1 124 SER n 
1 125 ALA n 
1 126 VAL n 
1 127 TYR n 
1 128 LEU n 
1 129 MET n 
1 130 ASN n 
1 131 SER n 
1 132 TRP n 
1 133 PRO n 
1 134 PHE n 
1 135 GLY n 
1 136 ASP n 
1 137 VAL n 
1 138 LEU n 
1 139 CYS n 
1 140 LYS n 
1 141 ILE n 
1 142 VAL n 
1 143 ILE n 
1 144 SER n 
1 145 ILE n 
1 146 ASP n 
1 147 TYR n 
1 148 TYR n 
1 149 ASN n 
1 150 MET n 
1 151 PHE n 
1 152 THR n 
1 153 SER n 
1 154 ILE n 
1 155 PHE n 
1 156 THR n 
1 157 LEU n 
1 158 THR n 
1 159 MET n 
1 160 MET n 
1 161 SER n 
1 162 VAL n 
1 163 ASP n 
1 164 ARG n 
1 165 TYR n 
1 166 ILE n 
1 167 ALA n 
1 168 VAL n 
1 169 CYS n 
1 170 HIS n 
1 171 PRO n 
1 172 VAL n 
1 173 LYS n 
1 174 ALA n 
1 175 LEU n 
1 176 ASP n 
1 177 PHE n 
1 178 ARG n 
1 179 THR n 
1 180 PRO n 
1 181 LEU n 
1 182 LYS n 
1 183 ALA n 
1 184 LYS n 
1 185 ILE n 
1 186 ILE n 
1 187 ASN n 
1 188 ILE n 
1 189 CYS n 
1 190 ILE n 
1 191 TRP n 
1 192 LEU n 
1 193 LEU n 
1 194 ALA n 
1 195 SER n 
1 196 SER n 
1 197 VAL n 
1 198 GLY n 
1 199 ILE n 
1 200 SER n 
1 201 ALA n 
1 202 ILE n 
1 203 VAL n 
1 204 LEU n 
1 205 GLY n 
1 206 GLY n 
1 207 THR n 
1 208 LYS n 
1 209 VAL n 
1 210 ARG n 
1 211 GLU n 
1 212 ASP n 
1 213 VAL n 
1 214 ASP n 
1 215 VAL n 
1 216 ILE n 
1 217 GLU n 
1 218 CYS n 
1 219 SER n 
1 220 LEU n 
1 221 GLN n 
1 222 PHE n 
1 223 PRO n 
1 224 ASP n 
1 225 ASP n 
1 226 GLU n 
1 227 TYR n 
1 228 SER n 
1 229 TRP n 
1 230 TRP n 
1 231 ASP n 
1 232 LEU n 
1 233 PHE n 
1 234 MET n 
1 235 LYS n 
1 236 ILE n 
1 237 CYS n 
1 238 VAL n 
1 239 PHE n 
1 240 VAL n 
1 241 PHE n 
1 242 ALA n 
1 243 PHE n 
1 244 VAL n 
1 245 ILE n 
1 246 PRO n 
1 247 VAL n 
1 248 LEU n 
1 249 ILE n 
1 250 ILE n 
1 251 ILE n 
1 252 VAL n 
1 253 CYS n 
1 254 TYR n 
1 255 THR n 
1 256 LEU n 
1 257 MET n 
1 258 ILE n 
1 259 LEU n 
1 260 ARG n 
1 261 LEU n 
1 262 LYS n 
1 263 SER n 
1 264 VAL n 
1 265 ARG n 
1 266 LEU n 
1 267 LEU n 
1 268 SER n 
1 269 GLY n 
1 270 SER n 
1 271 ARG n 
1 272 GLU n 
1 273 LYS n 
1 274 ASP n 
1 275 ARG n 
1 276 ASN n 
1 277 LEU n 
1 278 ARG n 
1 279 ARG n 
1 280 ILE n 
1 281 THR n 
1 282 LYS n 
1 283 LEU n 
1 284 VAL n 
1 285 LEU n 
1 286 VAL n 
1 287 VAL n 
1 288 VAL n 
1 289 ALA n 
1 290 VAL n 
1 291 PHE n 
1 292 ILE n 
1 293 ILE n 
1 294 CYS n 
1 295 TRP n 
1 296 THR n 
1 297 PRO n 
1 298 ILE n 
1 299 HIS n 
1 300 ILE n 
1 301 PHE n 
1 302 ILE n 
1 303 LEU n 
1 304 VAL n 
1 305 GLU n 
1 306 ALA n 
1 307 LEU n 
1 308 GLY n 
1 309 SER n 
1 310 THR n 
1 311 SER n 
1 312 HIS n 
1 313 SER n 
1 314 THR n 
1 315 ALA n 
1 316 ALA n 
1 317 LEU n 
1 318 SER n 
1 319 SER n 
1 320 TYR n 
1 321 TYR n 
1 322 PHE n 
1 323 CYS n 
1 324 ILE n 
1 325 ALA n 
1 326 LEU n 
1 327 GLY n 
1 328 TYR n 
1 329 THR n 
1 330 ASN n 
1 331 SER n 
1 332 SER n 
1 333 LEU n 
1 334 ASN n 
1 335 PRO n 
1 336 VAL n 
1 337 LEU n 
1 338 TYR n 
1 339 ALA n 
1 340 PHE n 
1 341 LEU n 
1 342 ASP n 
1 343 GLU n 
1 344 ASN n 
1 345 PHE n 
1 346 LYS n 
1 347 ARG n 
1 348 CYS n 
1 349 PHE n 
1 350 ARG n 
1 351 ASP n 
1 352 PHE n 
1 353 CYS n 
1 354 PHE n 
1 355 PRO n 
1 356 ILE n 
1 357 LYS n 
1 358 MET n 
1 359 ARG n 
1 360 MET n 
1 361 GLU n 
1 362 ARG n 
1 363 GLN n 
1 364 SER n 
1 365 THR n 
1 366 ASN n 
1 367 ARG n 
1 368 VAL n 
1 369 ARG n 
1 370 ASN n 
1 371 THR n 
1 372 VAL n 
1 373 GLN n 
1 374 ASP n 
1 375 PRO n 
1 376 ALA n 
1 377 SER n 
1 378 MET n 
1 379 ARG n 
1 380 ASP n 
1 381 VAL n 
1 382 GLY n 
1 383 GLY n 
1 384 MET n 
1 385 ASN n 
1 386 LYS n 
1 387 PRO n 
1 388 VAL n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   388 
_entity_src_gen.gene_src_common_name               'house mouse' 
_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      'Mus musculus' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     10090 
_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               'house mouse' 
_entity_src_gen.pdbx_host_org_scientific_name      'Mus musculus' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     10090 
_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 
A1BNM non-polymer         . 
;methyl (1S,3R,4S,6S,8M)-2-[(1-ethyl-1H-pyrazol-4-yl)methyl]-8-(3-hydroxyphenyl)-3,4-dimethyl-2-azabicyclo[2.2.2]oct-7-ene-6-carboxylate
;
? 'C23 H29 N3 O3'  395.495 
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 
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 
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   ASP 1   -7  ?   ?   ?   A . n 
A 1 2   TYR 2   -6  ?   ?   ?   A . n 
A 1 3   LYS 3   -5  ?   ?   ?   A . n 
A 1 4   ASP 4   -4  ?   ?   ?   A . n 
A 1 5   ASP 5   -3  ?   ?   ?   A . n 
A 1 6   ASP 6   -2  ?   ?   ?   A . n 
A 1 7   ASP 7   -1  ?   ?   ?   A . n 
A 1 8   ALA 8   0   ?   ?   ?   A . n 
A 1 9   MET 9   1   ?   ?   ?   A . n 
A 1 10  GLU 10  2   ?   ?   ?   A . n 
A 1 11  SER 11  3   ?   ?   ?   A . n 
A 1 12  PRO 12  4   ?   ?   ?   A . n 
A 1 13  ILE 13  5   ?   ?   ?   A . n 
A 1 14  GLN 14  6   ?   ?   ?   A . n 
A 1 15  ILE 15  7   ?   ?   ?   A . n 
A 1 16  PHE 16  8   ?   ?   ?   A . n 
A 1 17  ARG 17  9   ?   ?   ?   A . n 
A 1 18  GLY 18  10  ?   ?   ?   A . n 
A 1 19  ASP 19  11  ?   ?   ?   A . n 
A 1 20  PRO 20  12  ?   ?   ?   A . n 
A 1 21  GLY 21  13  ?   ?   ?   A . n 
A 1 22  PRO 22  14  ?   ?   ?   A . n 
A 1 23  THR 23  15  ?   ?   ?   A . n 
A 1 24  CYS 24  16  ?   ?   ?   A . n 
A 1 25  SER 25  17  ?   ?   ?   A . n 
A 1 26  PRO 26  18  ?   ?   ?   A . n 
A 1 27  SER 27  19  ?   ?   ?   A . n 
A 1 28  ALA 28  20  ?   ?   ?   A . n 
A 1 29  CYS 29  21  ?   ?   ?   A . n 
A 1 30  LEU 30  22  ?   ?   ?   A . n 
A 1 31  LEU 31  23  ?   ?   ?   A . n 
A 1 32  PRO 32  24  ?   ?   ?   A . n 
A 1 33  ASN 33  25  ?   ?   ?   A . n 
A 1 34  SER 34  26  ?   ?   ?   A . n 
A 1 35  SER 35  27  ?   ?   ?   A . n 
A 1 36  SER 36  28  ?   ?   ?   A . n 
A 1 37  TRP 37  29  ?   ?   ?   A . n 
A 1 38  PHE 38  30  ?   ?   ?   A . n 
A 1 39  PRO 39  31  ?   ?   ?   A . n 
A 1 40  ASN 40  32  ?   ?   ?   A . n 
A 1 41  TRP 41  33  ?   ?   ?   A . n 
A 1 42  ALA 42  34  ?   ?   ?   A . n 
A 1 43  GLU 43  35  ?   ?   ?   A . n 
A 1 44  SER 44  36  ?   ?   ?   A . n 
A 1 45  ASP 45  37  ?   ?   ?   A . n 
A 1 46  SER 46  38  ?   ?   ?   A . n 
A 1 47  ASN 47  39  ?   ?   ?   A . n 
A 1 48  GLY 48  40  ?   ?   ?   A . n 
A 1 49  SER 49  41  ?   ?   ?   A . n 
A 1 50  VAL 50  42  ?   ?   ?   A . n 
A 1 51  GLY 51  43  ?   ?   ?   A . n 
A 1 52  SER 52  44  ?   ?   ?   A . n 
A 1 53  GLU 53  45  ?   ?   ?   A . n 
A 1 54  ASP 54  46  ?   ?   ?   A . n 
A 1 55  GLN 55  47  ?   ?   ?   A . n 
A 1 56  GLN 56  48  ?   ?   ?   A . n 
A 1 57  LEU 57  49  ?   ?   ?   A . n 
A 1 58  GLU 58  50  ?   ?   ?   A . n 
A 1 59  SER 59  51  ?   ?   ?   A . n 
A 1 60  ALA 60  52  ?   ?   ?   A . n 
A 1 61  HIS 61  53  ?   ?   ?   A . n 
A 1 62  ILE 62  54  ?   ?   ?   A . n 
A 1 63  SER 63  55  ?   ?   ?   A . n 
A 1 64  PRO 64  56  ?   ?   ?   A . n 
A 1 65  ALA 65  57  57  ALA ALA A . n 
A 1 66  ILE 66  58  58  ILE ILE A . n 
A 1 67  PRO 67  59  59  PRO PRO A . n 
A 1 68  VAL 68  60  60  VAL VAL A . n 
A 1 69  ILE 69  61  61  ILE ILE A . n 
A 1 70  ILE 70  62  62  ILE ILE A . n 
A 1 71  THR 71  63  63  THR THR A . n 
A 1 72  ALA 72  64  64  ALA ALA A . n 
A 1 73  VAL 73  65  65  VAL VAL A . n 
A 1 74  TYR 74  66  66  TYR TYR A . n 
A 1 75  SER 75  67  67  SER SER A . n 
A 1 76  VAL 76  68  68  VAL VAL A . n 
A 1 77  VAL 77  69  69  VAL VAL A . n 
A 1 78  PHE 78  70  70  PHE PHE A . n 
A 1 79  VAL 79  71  71  VAL VAL A . n 
A 1 80  VAL 80  72  72  VAL VAL A . n 
A 1 81  GLY 81  73  73  GLY GLY A . n 
A 1 82  LEU 82  74  74  LEU LEU A . n 
A 1 83  VAL 83  75  75  VAL VAL A . n 
A 1 84  GLY 84  76  76  GLY GLY A . n 
A 1 85  ASN 85  77  77  ASN ASN A . n 
A 1 86  SER 86  78  78  SER SER A . n 
A 1 87  LEU 87  79  79  LEU LEU A . n 
A 1 88  VAL 88  80  80  VAL VAL A . n 
A 1 89  MET 89  81  81  MET MET A . n 
A 1 90  PHE 90  82  82  PHE PHE A . n 
A 1 91  VAL 91  83  83  VAL VAL A . n 
A 1 92  ILE 92  84  84  ILE ILE A . n 
A 1 93  ILE 93  85  85  ILE ILE A . n 
A 1 94  ARG 94  86  86  ARG ARG A . n 
A 1 95  TYR 95  87  87  TYR TYR A . n 
A 1 96  THR 96  88  88  THR THR A . n 
A 1 97  LYS 97  89  89  LYS LYS A . n 
A 1 98  MET 98  90  90  MET MET A . n 
A 1 99  LYS 99  91  91  LYS LYS A . n 
A 1 100 THR 100 92  92  THR THR A . n 
A 1 101 ALA 101 93  93  ALA ALA A . n 
A 1 102 THR 102 94  94  THR THR A . n 
A 1 103 ASN 103 95  95  ASN ASN A . n 
A 1 104 ILE 104 96  96  ILE ILE A . n 
A 1 105 TYR 105 97  97  TYR TYR A . n 
A 1 106 ILE 106 98  98  ILE ILE A . n 
A 1 107 PHE 107 99  99  PHE PHE A . n 
A 1 108 ASN 108 100 100 ASN ASN A . n 
A 1 109 LEU 109 101 101 LEU LEU A . n 
A 1 110 ALA 110 102 102 ALA ALA A . n 
A 1 111 LEU 111 103 103 LEU LEU A . n 
A 1 112 ALA 112 104 104 ALA ALA A . n 
A 1 113 ASP 113 105 105 ASP ASP A . n 
A 1 114 ALA 114 106 106 ALA ALA A . n 
A 1 115 LEU 115 107 107 LEU LEU A . n 
A 1 116 VAL 116 108 108 VAL VAL A . n 
A 1 117 THR 117 109 109 THR THR A . n 
A 1 118 THR 118 110 110 THR THR A . n 
A 1 119 THR 119 111 111 THR THR A . n 
A 1 120 MET 120 112 112 MET MET A . n 
A 1 121 PRO 121 113 113 PRO PRO A . n 
A 1 122 PHE 122 114 114 PHE PHE A . n 
A 1 123 GLN 123 115 115 GLN GLN A . n 
A 1 124 SER 124 116 116 SER SER A . n 
A 1 125 ALA 125 117 117 ALA ALA A . n 
A 1 126 VAL 126 118 118 VAL VAL A . n 
A 1 127 TYR 127 119 119 TYR TYR A . n 
A 1 128 LEU 128 120 120 LEU LEU A . n 
A 1 129 MET 129 121 121 MET MET A . n 
A 1 130 ASN 130 122 122 ASN ASN A . n 
A 1 131 SER 131 123 123 SER SER A . n 
A 1 132 TRP 132 124 124 TRP TRP A . n 
A 1 133 PRO 133 125 125 PRO PRO A . n 
A 1 134 PHE 134 126 126 PHE PHE A . n 
A 1 135 GLY 135 127 127 GLY GLY A . n 
A 1 136 ASP 136 128 128 ASP ASP A . n 
A 1 137 VAL 137 129 129 VAL VAL A . n 
A 1 138 LEU 138 130 130 LEU LEU A . n 
A 1 139 CYS 139 131 131 CYS CYS A . n 
A 1 140 LYS 140 132 132 LYS LYS A . n 
A 1 141 ILE 141 133 133 ILE ILE A . n 
A 1 142 VAL 142 134 134 VAL VAL A . n 
A 1 143 ILE 143 135 135 ILE ILE A . n 
A 1 144 SER 144 136 136 SER SER A . n 
A 1 145 ILE 145 137 137 ILE ILE A . n 
A 1 146 ASP 146 138 138 ASP ASP A . n 
A 1 147 TYR 147 139 139 TYR TYR A . n 
A 1 148 TYR 148 140 140 TYR TYR A . n 
A 1 149 ASN 149 141 141 ASN ASN A . n 
A 1 150 MET 150 142 142 MET MET A . n 
A 1 151 PHE 151 143 143 PHE PHE A . n 
A 1 152 THR 152 144 144 THR THR A . n 
A 1 153 SER 153 145 145 SER SER A . n 
A 1 154 ILE 154 146 146 ILE ILE A . n 
A 1 155 PHE 155 147 147 PHE PHE A . n 
A 1 156 THR 156 148 148 THR THR A . n 
A 1 157 LEU 157 149 149 LEU LEU A . n 
A 1 158 THR 158 150 150 THR THR A . n 
A 1 159 MET 159 151 151 MET MET A . n 
A 1 160 MET 160 152 152 MET MET A . n 
A 1 161 SER 161 153 153 SER SER A . n 
A 1 162 VAL 162 154 154 VAL VAL A . n 
A 1 163 ASP 163 155 155 ASP ASP A . n 
A 1 164 ARG 164 156 156 ARG ARG A . n 
A 1 165 TYR 165 157 157 TYR TYR A . n 
A 1 166 ILE 166 158 158 ILE ILE A . n 
A 1 167 ALA 167 159 159 ALA ALA A . n 
A 1 168 VAL 168 160 160 VAL VAL A . n 
A 1 169 CYS 169 161 161 CYS CYS A . n 
A 1 170 HIS 170 162 162 HIS HIS A . n 
A 1 171 PRO 171 163 163 PRO PRO A . n 
A 1 172 VAL 172 164 164 VAL VAL A . n 
A 1 173 LYS 173 165 165 LYS LYS A . n 
A 1 174 ALA 174 166 166 ALA ALA A . n 
A 1 175 LEU 175 167 167 LEU LEU A . n 
A 1 176 ASP 176 168 168 ASP ASP A . n 
A 1 177 PHE 177 169 169 PHE PHE A . n 
A 1 178 ARG 178 170 170 ARG ARG A . n 
A 1 179 THR 179 171 171 THR THR A . n 
A 1 180 PRO 180 172 172 PRO PRO A . n 
A 1 181 LEU 181 173 173 LEU LEU A . n 
A 1 182 LYS 182 174 174 LYS LYS A . n 
A 1 183 ALA 183 175 175 ALA ALA A . n 
A 1 184 LYS 184 176 176 LYS LYS A . n 
A 1 185 ILE 185 177 177 ILE ILE A . n 
A 1 186 ILE 186 178 178 ILE ILE A . n 
A 1 187 ASN 187 179 179 ASN ASN A . n 
A 1 188 ILE 188 180 180 ILE ILE A . n 
A 1 189 CYS 189 181 181 CYS CYS A . n 
A 1 190 ILE 190 182 182 ILE ILE A . n 
A 1 191 TRP 191 183 183 TRP TRP A . n 
A 1 192 LEU 192 184 184 LEU LEU A . n 
A 1 193 LEU 193 185 185 LEU LEU A . n 
A 1 194 ALA 194 186 186 ALA ALA A . n 
A 1 195 SER 195 187 187 SER SER A . n 
A 1 196 SER 196 188 188 SER SER A . n 
A 1 197 VAL 197 189 189 VAL VAL A . n 
A 1 198 GLY 198 190 190 GLY GLY A . n 
A 1 199 ILE 199 191 191 ILE ILE A . n 
A 1 200 SER 200 192 192 SER SER A . n 
A 1 201 ALA 201 193 193 ALA ALA A . n 
A 1 202 ILE 202 194 194 ILE ILE A . n 
A 1 203 VAL 203 195 195 VAL VAL A . n 
A 1 204 LEU 204 196 196 LEU LEU A . n 
A 1 205 GLY 205 197 197 GLY GLY A . n 
A 1 206 GLY 206 198 198 GLY GLY A . n 
A 1 207 THR 207 199 199 THR THR A . n 
A 1 208 LYS 208 200 200 LYS LYS A . n 
A 1 209 VAL 209 201 201 VAL VAL A . n 
A 1 210 ARG 210 202 202 ARG ARG A . n 
A 1 211 GLU 211 203 203 GLU GLU A . n 
A 1 212 ASP 212 204 204 ASP ASP A . n 
A 1 213 VAL 213 205 205 VAL VAL A . n 
A 1 214 ASP 214 206 206 ASP ASP A . n 
A 1 215 VAL 215 207 207 VAL VAL A . n 
A 1 216 ILE 216 208 208 ILE ILE A . n 
A 1 217 GLU 217 209 209 GLU GLU A . n 
A 1 218 CYS 218 210 210 CYS CYS A . n 
A 1 219 SER 219 211 211 SER SER A . n 
A 1 220 LEU 220 212 212 LEU LEU A . n 
A 1 221 GLN 221 213 213 GLN GLN A . n 
A 1 222 PHE 222 214 214 PHE PHE A . n 
A 1 223 PRO 223 215 215 PRO PRO A . n 
A 1 224 ASP 224 216 216 ASP ASP A . n 
A 1 225 ASP 225 217 217 ASP ASP A . n 
A 1 226 GLU 226 218 218 GLU GLU A . n 
A 1 227 TYR 227 219 219 TYR TYR A . n 
A 1 228 SER 228 220 220 SER SER A . n 
A 1 229 TRP 229 221 221 TRP TRP A . n 
A 1 230 TRP 230 222 222 TRP TRP A . n 
A 1 231 ASP 231 223 223 ASP ASP A . n 
A 1 232 LEU 232 224 224 LEU LEU A . n 
A 1 233 PHE 233 225 225 PHE PHE A . n 
A 1 234 MET 234 226 226 MET MET A . n 
A 1 235 LYS 235 227 227 LYS LYS A . n 
A 1 236 ILE 236 228 228 ILE ILE A . n 
A 1 237 CYS 237 229 229 CYS CYS A . n 
A 1 238 VAL 238 230 230 VAL VAL A . n 
A 1 239 PHE 239 231 231 PHE PHE A . n 
A 1 240 VAL 240 232 232 VAL VAL A . n 
A 1 241 PHE 241 233 233 PHE PHE A . n 
A 1 242 ALA 242 234 234 ALA ALA A . n 
A 1 243 PHE 243 235 235 PHE PHE A . n 
A 1 244 VAL 244 236 236 VAL VAL A . n 
A 1 245 ILE 245 237 237 ILE ILE A . n 
A 1 246 PRO 246 238 238 PRO PRO A . n 
A 1 247 VAL 247 239 239 VAL VAL A . n 
A 1 248 LEU 248 240 240 LEU LEU A . n 
A 1 249 ILE 249 241 241 ILE ILE A . n 
A 1 250 ILE 250 242 242 ILE ILE A . n 
A 1 251 ILE 251 243 243 ILE ILE A . n 
A 1 252 VAL 252 244 244 VAL VAL A . n 
A 1 253 CYS 253 245 245 CYS CYS A . n 
A 1 254 TYR 254 246 246 TYR TYR A . n 
A 1 255 THR 255 247 247 THR THR A . n 
A 1 256 LEU 256 248 248 LEU LEU A . n 
A 1 257 MET 257 249 249 MET MET A . n 
A 1 258 ILE 258 250 250 ILE ILE A . n 
A 1 259 LEU 259 251 251 LEU LEU A . n 
A 1 260 ARG 260 252 252 ARG ARG A . n 
A 1 261 LEU 261 253 253 LEU LEU A . n 
A 1 262 LYS 262 254 254 LYS LYS A . n 
A 1 263 SER 263 255 255 SER SER A . n 
A 1 264 VAL 264 256 256 VAL VAL A . n 
A 1 265 ARG 265 257 257 ARG ARG A . n 
A 1 266 LEU 266 258 258 LEU LEU A . n 
A 1 267 LEU 267 259 259 LEU LEU A . n 
A 1 268 SER 268 260 260 SER SER A . n 
A 1 269 GLY 269 261 261 GLY GLY A . n 
A 1 270 SER 270 262 262 SER SER A . n 
A 1 271 ARG 271 263 263 ARG ARG A . n 
A 1 272 GLU 272 264 264 GLU GLU A . n 
A 1 273 LYS 273 265 265 LYS LYS A . n 
A 1 274 ASP 274 266 266 ASP ASP A . n 
A 1 275 ARG 275 267 267 ARG ARG A . n 
A 1 276 ASN 276 268 268 ASN ASN A . n 
A 1 277 LEU 277 269 269 LEU LEU A . n 
A 1 278 ARG 278 270 270 ARG ARG A . n 
A 1 279 ARG 279 271 271 ARG ARG A . n 
A 1 280 ILE 280 272 272 ILE ILE A . n 
A 1 281 THR 281 273 273 THR THR A . n 
A 1 282 LYS 282 274 274 LYS LYS A . n 
A 1 283 LEU 283 275 275 LEU LEU A . n 
A 1 284 VAL 284 276 276 VAL VAL A . n 
A 1 285 LEU 285 277 277 LEU LEU A . n 
A 1 286 VAL 286 278 278 VAL VAL A . n 
A 1 287 VAL 287 279 279 VAL VAL A . n 
A 1 288 VAL 288 280 280 VAL VAL A . n 
A 1 289 ALA 289 281 281 ALA ALA A . n 
A 1 290 VAL 290 282 282 VAL VAL A . n 
A 1 291 PHE 291 283 283 PHE PHE A . n 
A 1 292 ILE 292 284 284 ILE ILE A . n 
A 1 293 ILE 293 285 285 ILE ILE A . n 
A 1 294 CYS 294 286 286 CYS CYS A . n 
A 1 295 TRP 295 287 287 TRP TRP A . n 
A 1 296 THR 296 288 288 THR THR A . n 
A 1 297 PRO 297 289 289 PRO PRO A . n 
A 1 298 ILE 298 290 290 ILE ILE A . n 
A 1 299 HIS 299 291 291 HIS HIS A . n 
A 1 300 ILE 300 292 292 ILE ILE A . n 
A 1 301 PHE 301 293 293 PHE PHE A . n 
A 1 302 ILE 302 294 294 ILE ILE A . n 
A 1 303 LEU 303 295 295 LEU LEU A . n 
A 1 304 VAL 304 296 296 VAL VAL A . n 
A 1 305 GLU 305 297 297 GLU GLU A . n 
A 1 306 ALA 306 298 298 ALA ALA A . n 
A 1 307 LEU 307 299 299 LEU LEU A . n 
A 1 308 GLY 308 300 300 GLY GLY A . n 
A 1 309 SER 309 301 ?   ?   ?   A . n 
A 1 310 THR 310 302 ?   ?   ?   A . n 
A 1 311 SER 311 303 ?   ?   ?   A . n 
A 1 312 HIS 312 304 ?   ?   ?   A . n 
A 1 313 SER 313 305 ?   ?   ?   A . n 
A 1 314 THR 314 306 ?   ?   ?   A . n 
A 1 315 ALA 315 307 307 ALA ALA A . n 
A 1 316 ALA 316 308 308 ALA ALA A . n 
A 1 317 LEU 317 309 309 LEU LEU A . n 
A 1 318 SER 318 310 310 SER SER A . n 
A 1 319 SER 319 311 311 SER SER A . n 
A 1 320 TYR 320 312 312 TYR TYR A . n 
A 1 321 TYR 321 313 313 TYR TYR A . n 
A 1 322 PHE 322 314 314 PHE PHE A . n 
A 1 323 CYS 323 315 315 CYS CYS A . n 
A 1 324 ILE 324 316 316 ILE ILE A . n 
A 1 325 ALA 325 317 317 ALA ALA A . n 
A 1 326 LEU 326 318 318 LEU LEU A . n 
A 1 327 GLY 327 319 319 GLY GLY A . n 
A 1 328 TYR 328 320 320 TYR TYR A . n 
A 1 329 THR 329 321 321 THR THR A . n 
A 1 330 ASN 330 322 322 ASN ASN A . n 
A 1 331 SER 331 323 323 SER SER A . n 
A 1 332 SER 332 324 324 SER SER A . n 
A 1 333 LEU 333 325 325 LEU LEU A . n 
A 1 334 ASN 334 326 326 ASN ASN A . n 
A 1 335 PRO 335 327 327 PRO PRO A . n 
A 1 336 VAL 336 328 328 VAL VAL A . n 
A 1 337 LEU 337 329 329 LEU LEU A . n 
A 1 338 TYR 338 330 330 TYR TYR A . n 
A 1 339 ALA 339 331 331 ALA ALA A . n 
A 1 340 PHE 340 332 332 PHE PHE A . n 
A 1 341 LEU 341 333 333 LEU LEU A . n 
A 1 342 ASP 342 334 334 ASP ASP A . n 
A 1 343 GLU 343 335 335 GLU GLU A . n 
A 1 344 ASN 344 336 336 ASN ASN A . n 
A 1 345 PHE 345 337 337 PHE PHE A . n 
A 1 346 LYS 346 338 338 LYS LYS A . n 
A 1 347 ARG 347 339 339 ARG ARG A . n 
A 1 348 CYS 348 340 340 CYS CYS A . n 
A 1 349 PHE 349 341 341 PHE PHE A . n 
A 1 350 ARG 350 342 342 ARG ARG A . n 
A 1 351 ASP 351 343 343 ASP ASP A . n 
A 1 352 PHE 352 344 344 PHE PHE A . n 
A 1 353 CYS 353 345 345 CYS CYS A . n 
A 1 354 PHE 354 346 346 PHE PHE A . n 
A 1 355 PRO 355 347 347 PRO PRO A . n 
A 1 356 ILE 356 348 ?   ?   ?   A . n 
A 1 357 LYS 357 349 ?   ?   ?   A . n 
A 1 358 MET 358 350 ?   ?   ?   A . n 
A 1 359 ARG 359 351 ?   ?   ?   A . n 
A 1 360 MET 360 352 ?   ?   ?   A . n 
A 1 361 GLU 361 353 ?   ?   ?   A . n 
A 1 362 ARG 362 354 ?   ?   ?   A . n 
A 1 363 GLN 363 355 ?   ?   ?   A . n 
A 1 364 SER 364 356 ?   ?   ?   A . n 
A 1 365 THR 365 357 ?   ?   ?   A . n 
A 1 366 ASN 366 358 ?   ?   ?   A . n 
A 1 367 ARG 367 359 ?   ?   ?   A . n 
A 1 368 VAL 368 360 ?   ?   ?   A . n 
A 1 369 ARG 369 361 ?   ?   ?   A . n 
A 1 370 ASN 370 362 ?   ?   ?   A . n 
A 1 371 THR 371 363 ?   ?   ?   A . n 
A 1 372 VAL 372 364 ?   ?   ?   A . n 
A 1 373 GLN 373 365 ?   ?   ?   A . n 
A 1 374 ASP 374 366 ?   ?   ?   A . n 
A 1 375 PRO 375 367 ?   ?   ?   A . n 
A 1 376 ALA 376 368 ?   ?   ?   A . n 
A 1 377 SER 377 369 ?   ?   ?   A . n 
A 1 378 MET 378 370 ?   ?   ?   A . n 
A 1 379 ARG 379 371 ?   ?   ?   A . n 
A 1 380 ASP 380 372 ?   ?   ?   A . n 
A 1 381 VAL 381 373 ?   ?   ?   A . n 
A 1 382 GLY 382 374 ?   ?   ?   A . n 
A 1 383 GLY 383 375 ?   ?   ?   A . n 
A 1 384 MET 384 376 ?   ?   ?   A . n 
A 1 385 ASN 385 377 ?   ?   ?   A . n 
A 1 386 LYS 386 378 ?   ?   ?   A . n 
A 1 387 PRO 387 379 ?   ?   ?   A . n 
A 1 388 VAL 388 380 ?   ?   ?   A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1BNM 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1BNM 
_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        ? 
# 
_pdbx_nonpoly_scheme.asym_id         B 
_pdbx_nonpoly_scheme.entity_id       2 
_pdbx_nonpoly_scheme.mon_id          A1BNM 
_pdbx_nonpoly_scheme.ndb_seq_num     1 
_pdbx_nonpoly_scheme.pdb_seq_num     401 
_pdbx_nonpoly_scheme.auth_seq_num    1 
_pdbx_nonpoly_scheme.pdb_mon_id      A1BNM 
_pdbx_nonpoly_scheme.auth_mon_id     A1 
_pdbx_nonpoly_scheme.pdb_strand_id   A 
_pdbx_nonpoly_scheme.pdb_ins_code    . 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9MQL 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     1.00 
_cell.length_a_esd                 ? 
_cell.length_b                     1.00 
_cell.length_b_esd                 ? 
_cell.length_c                     1.00 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        ? 
_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                         9MQL 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                1 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9MQL 
_exptl.crystals_number            ? 
_exptl.details                    ? 
_exptl.method                     'ELECTRON MICROSCOPY' 
_exptl.method_details             ? 
# 
_refine.pdbx_refine_id                           'ELECTRON MICROSCOPY' 
_refine.entry_id                                 9MQL 
_refine.pdbx_diffrn_id                           ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             ? 
_refine.ls_d_res_high                            . 
_refine.ls_percent_reflns_obs                    ? 
_refine.ls_R_factor_obs                          ? 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       ? 
_refine.ls_R_factor_R_free                       ? 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 ? 
_refine.ls_number_reflns_R_free                  ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.B_iso_mean                               ? 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.solvent_model_details                    ? 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.pdbx_ls_cross_valid_method               ? 
_refine.details                                  ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
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 
'ELECTRON MICROSCOPY' ? 0.002 ? 2360 ? f_bond_d           ? ? 
'ELECTRON MICROSCOPY' ? 0.473 ? 3219 ? f_angle_d          ? ? 
'ELECTRON MICROSCOPY' ? 7.376 ? 322  ? f_dihedral_angle_d ? ? 
'ELECTRON MICROSCOPY' ? 0.037 ? 394  ? f_chiral_restr     ? ? 
'ELECTRON MICROSCOPY' ? 0.003 ? 380  ? f_plane_restr      ? ? 
# 
_struct.entry_id                     9MQL 
_struct.title                        
'Locally-Refined Inactive Kappa-Opioid Receptor with Nb6M, NabFab, and isoquinuclidine compound #020_E1' 
_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        9MQL 
_struct_keywords.text            
'G-protein coupled receptor, Kappa-opioid, isoquinuclidine, antagonist, nanobodies, fabs, MEMBRANE PROTEIN' 
_struct_keywords.pdbx_keywords   'MEMBRANE PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    PDB 
_struct_ref.db_code                    9MQL 
_struct_ref.pdbx_db_accession          9MQL 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   ? 
_struct_ref.pdbx_align_begin           1 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9MQL 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 388 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             9MQL 
_struct_ref_seq.db_align_beg                  -7 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  380 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       -7 
_struct_ref_seq.pdbx_auth_seq_align_end       380 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'electron microscopy' 
_pdbx_struct_assembly_auth_evidence.details                'not applicable' 
# 
_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]         1.0 
_pdbx_struct_oper_list.matrix[1][2]         0.0 
_pdbx_struct_oper_list.matrix[1][3]         0.0 
_pdbx_struct_oper_list.vector[1]            0.0 
_pdbx_struct_oper_list.matrix[2][1]         0.0 
_pdbx_struct_oper_list.matrix[2][2]         1.0 
_pdbx_struct_oper_list.matrix[2][3]         0.0 
_pdbx_struct_oper_list.vector[2]            0.0 
_pdbx_struct_oper_list.matrix[3][1]         0.0 
_pdbx_struct_oper_list.matrix[3][2]         0.0 
_pdbx_struct_oper_list.matrix[3][3]         1.0 
_pdbx_struct_oper_list.vector[3]            0.0 
# 
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 PRO A 67  ? TYR A 95  ? PRO A 59  TYR A 87  1 ? 29 
HELX_P HELX_P2  AA2 THR A 100 ? THR A 119 ? THR A 92  THR A 111 1 ? 20 
HELX_P HELX_P3  AA3 THR A 119 ? SER A 124 ? THR A 111 SER A 116 1 ? 6  
HELX_P HELX_P4  AA4 SER A 124 ? MET A 129 ? SER A 116 MET A 121 1 ? 6  
HELX_P HELX_P5  AA5 GLY A 135 ? HIS A 170 ? GLY A 127 HIS A 162 1 ? 36 
HELX_P HELX_P6  AA6 HIS A 170 ? ARG A 178 ? HIS A 162 ARG A 170 1 ? 9  
HELX_P HELX_P7  AA7 THR A 179 ? LEU A 204 ? THR A 171 LEU A 196 1 ? 26 
HELX_P HELX_P8  AA8 SER A 228 ? PHE A 243 ? SER A 220 PHE A 235 1 ? 16 
HELX_P HELX_P9  AA9 PHE A 243 ? LEU A 266 ? PHE A 235 LEU A 258 1 ? 24 
HELX_P HELX_P10 AB1 SER A 270 ? GLY A 308 ? SER A 262 GLY A 300 1 ? 39 
HELX_P HELX_P11 AB2 ALA A 316 ? ASP A 342 ? ALA A 308 ASP A 334 1 ? 27 
HELX_P HELX_P12 AB3 ASP A 342 ? PHE A 354 ? ASP A 334 PHE A 346 1 ? 13 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_struct_conn.id                            disulf1 
_struct_conn.conn_type_id                  disulf 
_struct_conn.pdbx_leaving_atom_flag        ? 
_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            139 
_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           A 
_struct_conn.ptnr2_label_comp_id           CYS 
_struct_conn.ptnr2_label_seq_id            218 
_struct_conn.ptnr2_label_atom_id           SG 
_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             131 
_struct_conn.ptnr2_auth_asym_id            A 
_struct_conn.ptnr2_auth_comp_id            CYS 
_struct_conn.ptnr2_auth_seq_id             210 
_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               2.030 
_struct_conn.pdbx_value_order              ? 
_struct_conn.pdbx_role                     ? 
# 
_struct_conn_type.id          disulf 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
_pdbx_modification_feature.ordinal                            1 
_pdbx_modification_feature.label_comp_id                      CYS 
_pdbx_modification_feature.label_asym_id                      A 
_pdbx_modification_feature.label_seq_id                       139 
_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      218 
_pdbx_modification_feature.modified_residue_label_alt_id      ? 
_pdbx_modification_feature.auth_comp_id                       CYS 
_pdbx_modification_feature.auth_asym_id                       A 
_pdbx_modification_feature.auth_seq_id                        131 
_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       210 
_pdbx_modification_feature.modified_residue_PDB_ins_code      ? 
_pdbx_modification_feature.modified_residue_symmetry          1_555 
_pdbx_modification_feature.comp_id_linking_atom               SG 
_pdbx_modification_feature.modified_residue_id_linking_atom   SG 
_pdbx_modification_feature.modified_residue_id                . 
_pdbx_modification_feature.ref_pcm_id                         . 
_pdbx_modification_feature.ref_comp_id                        . 
_pdbx_modification_feature.type                               None 
_pdbx_modification_feature.category                           'Disulfide bridge' 
# 
_struct_sheet.id               AA1 
_struct_sheet.type             ? 
_struct_sheet.number_strands   2 
_struct_sheet.details          ? 
# 
_struct_sheet_order.sheet_id     AA1 
_struct_sheet_order.range_id_1   1 
_struct_sheet_order.range_id_2   2 
_struct_sheet_order.offset       ? 
_struct_sheet_order.sense        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 GLY A 205 ? VAL A 209 ? GLY A 197 VAL A 201 
AA1 2 ILE A 216 ? LEU A 220 ? ILE A 208 LEU A 212 
# 
_pdbx_struct_sheet_hbond.sheet_id                AA1 
_pdbx_struct_sheet_hbond.range_id_1              1 
_pdbx_struct_sheet_hbond.range_id_2              2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id   N 
_pdbx_struct_sheet_hbond.range_1_label_comp_id   LYS 
_pdbx_struct_sheet_hbond.range_1_label_asym_id   A 
_pdbx_struct_sheet_hbond.range_1_label_seq_id    208 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code    ? 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id    N 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id    LYS 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id    A 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id     200 
_pdbx_struct_sheet_hbond.range_2_label_atom_id   O 
_pdbx_struct_sheet_hbond.range_2_label_comp_id   GLU 
_pdbx_struct_sheet_hbond.range_2_label_asym_id   A 
_pdbx_struct_sheet_hbond.range_2_label_seq_id    217 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code    ? 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id    O 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id    GLU 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id    A 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id     209 
# 
_pdbx_entry_details.entry_id                   9MQL 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 VAL A 71  ? ? -90.17  -60.79 
2 1 ARG A 170 ? ? -89.69  30.28  
3 1 TYR A 219 ? ? 39.02   37.19  
4 1 SER A 220 ? ? -136.85 -69.53 
5 1 PHE A 235 ? ? -120.17 -52.92 
# 
_em_3d_fitting.id                1 
_em_3d_fitting.entry_id          9MQL 
_em_3d_fitting.method            ? 
_em_3d_fitting.target_criteria   ? 
_em_3d_fitting.details           ? 
_em_3d_fitting.overall_b_value   ? 
_em_3d_fitting.ref_space         ? 
_em_3d_fitting.ref_protocol      ? 
# 
_em_3d_reconstruction.entry_id                    9MQL 
_em_3d_reconstruction.id                          1 
_em_3d_reconstruction.method                      ? 
_em_3d_reconstruction.algorithm                   'FOURIER SPACE' 
_em_3d_reconstruction.citation_id                 ? 
_em_3d_reconstruction.details                     ? 
_em_3d_reconstruction.resolution                  2.96 
_em_3d_reconstruction.resolution_method           'FSC 0.143 CUT-OFF' 
_em_3d_reconstruction.magnification_calibration   ? 
_em_3d_reconstruction.nominal_pixel_size          ? 
_em_3d_reconstruction.actual_pixel_size           ? 
_em_3d_reconstruction.num_particles               98518 
_em_3d_reconstruction.euler_angles_details        ? 
_em_3d_reconstruction.num_class_averages          ? 
_em_3d_reconstruction.refinement_type             ? 
_em_3d_reconstruction.image_processing_id         1 
_em_3d_reconstruction.symmetry_type               POINT 
# 
_em_buffer.id            1 
_em_buffer.specimen_id   1 
_em_buffer.name          ? 
_em_buffer.details       ? 
_em_buffer.pH            7.5 
# 
_em_entity_assembly.id                   1 
_em_entity_assembly.parent_id            0 
_em_entity_assembly.source               RECOMBINANT 
_em_entity_assembly.type                 COMPLEX 
_em_entity_assembly.name                 'Mouse Kappa-Opioid Receptor' 
_em_entity_assembly.details              ? 
_em_entity_assembly.synonym              ? 
_em_entity_assembly.oligomeric_details   ? 
_em_entity_assembly.entity_id_list       1 
# 
_em_imaging.entry_id                        9MQL 
_em_imaging.id                              1 
_em_imaging.astigmatism                     ? 
_em_imaging.electron_beam_tilt_params       ? 
_em_imaging.residual_tilt                   ? 
_em_imaging.microscope_model                'FEI TALOS ARCTICA' 
_em_imaging.specimen_holder_type            ? 
_em_imaging.specimen_holder_model           'FEI TITAN KRIOS AUTOGRID HOLDER' 
_em_imaging.details                         ? 
_em_imaging.date                            ? 
_em_imaging.accelerating_voltage            200 
_em_imaging.illumination_mode               OTHER 
_em_imaging.mode                            'BRIGHT FIELD' 
_em_imaging.nominal_cs                      ? 
_em_imaging.nominal_defocus_min             800 
_em_imaging.nominal_defocus_max             2100 
_em_imaging.calibrated_defocus_min          ? 
_em_imaging.calibrated_defocus_max          ? 
_em_imaging.tilt_angle_min                  ? 
_em_imaging.tilt_angle_max                  ? 
_em_imaging.nominal_magnification           ? 
_em_imaging.calibrated_magnification        ? 
_em_imaging.electron_source                 'FIELD EMISSION GUN' 
_em_imaging.citation_id                     ? 
_em_imaging.temperature                     ? 
_em_imaging.detector_distance               ? 
_em_imaging.recording_temperature_minimum   ? 
_em_imaging.recording_temperature_maximum   ? 
_em_imaging.alignment_procedure             BASIC 
_em_imaging.c2_aperture_diameter            ? 
_em_imaging.specimen_id                     1 
_em_imaging.cryogen                         NITROGEN 
# 
_em_sample_support.id               1 
_em_sample_support.film_material    ? 
_em_sample_support.method           ? 
_em_sample_support.grid_material    GOLD 
_em_sample_support.grid_mesh_size   ? 
_em_sample_support.grid_type        'UltrAuFoil R1.2/1.3' 
_em_sample_support.details          ? 
_em_sample_support.specimen_id      1 
_em_sample_support.citation_id      ? 
# 
_em_vitrification.entry_id              9MQL 
_em_vitrification.id                    1 
_em_vitrification.specimen_id           1 
_em_vitrification.cryogen_name          ETHANE 
_em_vitrification.humidity              ? 
_em_vitrification.temp                  ? 
_em_vitrification.chamber_temperature   ? 
_em_vitrification.instrument            'FEI VITROBOT MARK IV' 
_em_vitrification.method                ? 
_em_vitrification.time_resolved_state   ? 
_em_vitrification.citation_id           ? 
_em_vitrification.details               ? 
# 
_em_experiment.entry_id                9MQL 
_em_experiment.id                      1 
_em_experiment.reconstruction_method   'SINGLE PARTICLE' 
_em_experiment.aggregation_state       PARTICLE 
_em_experiment.entity_assembly_id      1 
# 
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 ASP -7  ? A ASP 1   
2   1 Y 1 A TYR -6  ? A TYR 2   
3   1 Y 1 A LYS -5  ? A LYS 3   
4   1 Y 1 A ASP -4  ? A ASP 4   
5   1 Y 1 A ASP -3  ? A ASP 5   
6   1 Y 1 A ASP -2  ? A ASP 6   
7   1 Y 1 A ASP -1  ? A ASP 7   
8   1 Y 1 A ALA 0   ? A ALA 8   
9   1 Y 1 A MET 1   ? A MET 9   
10  1 Y 1 A GLU 2   ? A GLU 10  
11  1 Y 1 A SER 3   ? A SER 11  
12  1 Y 1 A PRO 4   ? A PRO 12  
13  1 Y 1 A ILE 5   ? A ILE 13  
14  1 Y 1 A GLN 6   ? A GLN 14  
15  1 Y 1 A ILE 7   ? A ILE 15  
16  1 Y 1 A PHE 8   ? A PHE 16  
17  1 Y 1 A ARG 9   ? A ARG 17  
18  1 Y 1 A GLY 10  ? A GLY 18  
19  1 Y 1 A ASP 11  ? A ASP 19  
20  1 Y 1 A PRO 12  ? A PRO 20  
21  1 Y 1 A GLY 13  ? A GLY 21  
22  1 Y 1 A PRO 14  ? A PRO 22  
23  1 Y 1 A THR 15  ? A THR 23  
24  1 Y 1 A CYS 16  ? A CYS 24  
25  1 Y 1 A SER 17  ? A SER 25  
26  1 Y 1 A PRO 18  ? A PRO 26  
27  1 Y 1 A SER 19  ? A SER 27  
28  1 Y 1 A ALA 20  ? A ALA 28  
29  1 Y 1 A CYS 21  ? A CYS 29  
30  1 Y 1 A LEU 22  ? A LEU 30  
31  1 Y 1 A LEU 23  ? A LEU 31  
32  1 Y 1 A PRO 24  ? A PRO 32  
33  1 Y 1 A ASN 25  ? A ASN 33  
34  1 Y 1 A SER 26  ? A SER 34  
35  1 Y 1 A SER 27  ? A SER 35  
36  1 Y 1 A SER 28  ? A SER 36  
37  1 Y 1 A TRP 29  ? A TRP 37  
38  1 Y 1 A PHE 30  ? A PHE 38  
39  1 Y 1 A PRO 31  ? A PRO 39  
40  1 Y 1 A ASN 32  ? A ASN 40  
41  1 Y 1 A TRP 33  ? A TRP 41  
42  1 Y 1 A ALA 34  ? A ALA 42  
43  1 Y 1 A GLU 35  ? A GLU 43  
44  1 Y 1 A SER 36  ? A SER 44  
45  1 Y 1 A ASP 37  ? A ASP 45  
46  1 Y 1 A SER 38  ? A SER 46  
47  1 Y 1 A ASN 39  ? A ASN 47  
48  1 Y 1 A GLY 40  ? A GLY 48  
49  1 Y 1 A SER 41  ? A SER 49  
50  1 Y 1 A VAL 42  ? A VAL 50  
51  1 Y 1 A GLY 43  ? A GLY 51  
52  1 Y 1 A SER 44  ? A SER 52  
53  1 Y 1 A GLU 45  ? A GLU 53  
54  1 Y 1 A ASP 46  ? A ASP 54  
55  1 Y 1 A GLN 47  ? A GLN 55  
56  1 Y 1 A GLN 48  ? A GLN 56  
57  1 Y 1 A LEU 49  ? A LEU 57  
58  1 Y 1 A GLU 50  ? A GLU 58  
59  1 Y 1 A SER 51  ? A SER 59  
60  1 Y 1 A ALA 52  ? A ALA 60  
61  1 Y 1 A HIS 53  ? A HIS 61  
62  1 Y 1 A ILE 54  ? A ILE 62  
63  1 Y 1 A SER 55  ? A SER 63  
64  1 Y 1 A PRO 56  ? A PRO 64  
65  1 Y 1 A SER 301 ? A SER 309 
66  1 Y 1 A THR 302 ? A THR 310 
67  1 Y 1 A SER 303 ? A SER 311 
68  1 Y 1 A HIS 304 ? A HIS 312 
69  1 Y 1 A SER 305 ? A SER 313 
70  1 Y 1 A THR 306 ? A THR 314 
71  1 Y 1 A ILE 348 ? A ILE 356 
72  1 Y 1 A LYS 349 ? A LYS 357 
73  1 Y 1 A MET 350 ? A MET 358 
74  1 Y 1 A ARG 351 ? A ARG 359 
75  1 Y 1 A MET 352 ? A MET 360 
76  1 Y 1 A GLU 353 ? A GLU 361 
77  1 Y 1 A ARG 354 ? A ARG 362 
78  1 Y 1 A GLN 355 ? A GLN 363 
79  1 Y 1 A SER 356 ? A SER 364 
80  1 Y 1 A THR 357 ? A THR 365 
81  1 Y 1 A ASN 358 ? A ASN 366 
82  1 Y 1 A ARG 359 ? A ARG 367 
83  1 Y 1 A VAL 360 ? A VAL 368 
84  1 Y 1 A ARG 361 ? A ARG 369 
85  1 Y 1 A ASN 362 ? A ASN 370 
86  1 Y 1 A THR 363 ? A THR 371 
87  1 Y 1 A VAL 364 ? A VAL 372 
88  1 Y 1 A GLN 365 ? A GLN 373 
89  1 Y 1 A ASP 366 ? A ASP 374 
90  1 Y 1 A PRO 367 ? A PRO 375 
91  1 Y 1 A ALA 368 ? A ALA 376 
92  1 Y 1 A SER 369 ? A SER 377 
93  1 Y 1 A MET 370 ? A MET 378 
94  1 Y 1 A ARG 371 ? A ARG 379 
95  1 Y 1 A ASP 372 ? A ASP 380 
96  1 Y 1 A VAL 373 ? A VAL 381 
97  1 Y 1 A GLY 374 ? A GLY 382 
98  1 Y 1 A GLY 375 ? A GLY 383 
99  1 Y 1 A MET 376 ? A MET 384 
100 1 Y 1 A ASN 377 ? A ASN 385 
101 1 Y 1 A LYS 378 ? A LYS 386 
102 1 Y 1 A PRO 379 ? A PRO 387 
103 1 Y 1 A VAL 380 ? A VAL 388 
# 
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 
A1BNM C01  C N N 1   
A1BNM C02  C N R 2   
A1BNM C04  C N S 3   
A1BNM C05  C N N 4   
A1BNM C06  C N N 5   
A1BNM C07  C N S 6   
A1BNM C08  C N N 7   
A1BNM C09  C N S 8   
A1BNM C10  C N N 9   
A1BNM C12  C N N 10  
A1BNM C14  C N N 11  
A1BNM C15  C Y N 12  
A1BNM C16  C Y N 13  
A1BNM C17  C Y N 14  
A1BNM C18  C Y N 15  
A1BNM C19  C Y N 16  
A1BNM C21  C Y N 17  
A1BNM C22  C N N 18  
A1BNM C23  C Y N 19  
A1BNM C24  C Y N 20  
A1BNM C27  C Y N 21  
A1BNM C28  C N N 22  
A1BNM C29  C N N 23  
A1BNM N03  N N N 24  
A1BNM N25  N Y N 25  
A1BNM N26  N Y N 26  
A1BNM O11  O N N 27  
A1BNM O13  O N N 28  
A1BNM O20  O N N 29  
A1BNM H1   H N N 30  
A1BNM H2   H N N 31  
A1BNM H3   H N N 32  
A1BNM H4   H N N 33  
A1BNM H5   H N N 34  
A1BNM H6   H N N 35  
A1BNM H7   H N N 36  
A1BNM H8   H N N 37  
A1BNM H9   H N N 38  
A1BNM H10  H N N 39  
A1BNM H11  H N N 40  
A1BNM H12  H N N 41  
A1BNM H13  H N N 42  
A1BNM H14  H N N 43  
A1BNM H15  H N N 44  
A1BNM H16  H N N 45  
A1BNM H17  H N N 46  
A1BNM H18  H N N 47  
A1BNM H19  H N N 48  
A1BNM H20  H N N 49  
A1BNM H21  H N N 50  
A1BNM H22  H N N 51  
A1BNM H23  H N N 52  
A1BNM H24  H N N 53  
A1BNM H25  H N N 54  
A1BNM H26  H N N 55  
A1BNM H27  H N N 56  
A1BNM H28  H N N 57  
A1BNM H30  H N N 58  
ALA   N    N N N 59  
ALA   CA   C N S 60  
ALA   C    C N N 61  
ALA   O    O N N 62  
ALA   CB   C N N 63  
ALA   OXT  O N N 64  
ALA   H    H N N 65  
ALA   H2   H N N 66  
ALA   HA   H N N 67  
ALA   HB1  H N N 68  
ALA   HB2  H N N 69  
ALA   HB3  H N N 70  
ALA   HXT  H N N 71  
ARG   N    N N N 72  
ARG   CA   C N S 73  
ARG   C    C N N 74  
ARG   O    O N N 75  
ARG   CB   C N N 76  
ARG   CG   C N N 77  
ARG   CD   C N N 78  
ARG   NE   N N N 79  
ARG   CZ   C N N 80  
ARG   NH1  N N N 81  
ARG   NH2  N N N 82  
ARG   OXT  O N N 83  
ARG   H    H N N 84  
ARG   H2   H N N 85  
ARG   HA   H N N 86  
ARG   HB2  H N N 87  
ARG   HB3  H N N 88  
ARG   HG2  H N N 89  
ARG   HG3  H N N 90  
ARG   HD2  H N N 91  
ARG   HD3  H N N 92  
ARG   HE   H N N 93  
ARG   HH11 H N N 94  
ARG   HH12 H N N 95  
ARG   HH21 H N N 96  
ARG   HH22 H N N 97  
ARG   HXT  H N N 98  
ASN   N    N N N 99  
ASN   CA   C N S 100 
ASN   C    C N N 101 
ASN   O    O N N 102 
ASN   CB   C N N 103 
ASN   CG   C N N 104 
ASN   OD1  O N N 105 
ASN   ND2  N N N 106 
ASN   OXT  O N N 107 
ASN   H    H N N 108 
ASN   H2   H N N 109 
ASN   HA   H N N 110 
ASN   HB2  H N N 111 
ASN   HB3  H N N 112 
ASN   HD21 H N N 113 
ASN   HD22 H N N 114 
ASN   HXT  H N N 115 
ASP   N    N N N 116 
ASP   CA   C N S 117 
ASP   C    C N N 118 
ASP   O    O N N 119 
ASP   CB   C N N 120 
ASP   CG   C N N 121 
ASP   OD1  O N N 122 
ASP   OD2  O N N 123 
ASP   OXT  O N N 124 
ASP   H    H N N 125 
ASP   H2   H N N 126 
ASP   HA   H N N 127 
ASP   HB2  H N N 128 
ASP   HB3  H N N 129 
ASP   HD2  H N N 130 
ASP   HXT  H N N 131 
CYS   N    N N N 132 
CYS   CA   C N R 133 
CYS   C    C N N 134 
CYS   O    O N N 135 
CYS   CB   C N N 136 
CYS   SG   S N N 137 
CYS   OXT  O N N 138 
CYS   H    H N N 139 
CYS   H2   H N N 140 
CYS   HA   H N N 141 
CYS   HB2  H N N 142 
CYS   HB3  H N N 143 
CYS   HG   H N N 144 
CYS   HXT  H N N 145 
GLN   N    N N N 146 
GLN   CA   C N S 147 
GLN   C    C N N 148 
GLN   O    O N N 149 
GLN   CB   C N N 150 
GLN   CG   C N N 151 
GLN   CD   C N N 152 
GLN   OE1  O N N 153 
GLN   NE2  N N N 154 
GLN   OXT  O N N 155 
GLN   H    H N N 156 
GLN   H2   H N N 157 
GLN   HA   H N N 158 
GLN   HB2  H N N 159 
GLN   HB3  H N N 160 
GLN   HG2  H N N 161 
GLN   HG3  H N N 162 
GLN   HE21 H N N 163 
GLN   HE22 H N N 164 
GLN   HXT  H N N 165 
GLU   N    N N N 166 
GLU   CA   C N S 167 
GLU   C    C N N 168 
GLU   O    O N N 169 
GLU   CB   C N N 170 
GLU   CG   C N N 171 
GLU   CD   C N N 172 
GLU   OE1  O N N 173 
GLU   OE2  O N N 174 
GLU   OXT  O N N 175 
GLU   H    H N N 176 
GLU   H2   H N N 177 
GLU   HA   H N N 178 
GLU   HB2  H N N 179 
GLU   HB3  H N N 180 
GLU   HG2  H N N 181 
GLU   HG3  H N N 182 
GLU   HE2  H N N 183 
GLU   HXT  H N N 184 
GLY   N    N N N 185 
GLY   CA   C N N 186 
GLY   C    C N N 187 
GLY   O    O N N 188 
GLY   OXT  O N N 189 
GLY   H    H N N 190 
GLY   H2   H N N 191 
GLY   HA2  H N N 192 
GLY   HA3  H N N 193 
GLY   HXT  H N N 194 
HIS   N    N N N 195 
HIS   CA   C N S 196 
HIS   C    C N N 197 
HIS   O    O N N 198 
HIS   CB   C N N 199 
HIS   CG   C Y N 200 
HIS   ND1  N Y N 201 
HIS   CD2  C Y N 202 
HIS   CE1  C Y N 203 
HIS   NE2  N Y N 204 
HIS   OXT  O N N 205 
HIS   H    H N N 206 
HIS   H2   H N N 207 
HIS   HA   H N N 208 
HIS   HB2  H N N 209 
HIS   HB3  H N N 210 
HIS   HD1  H N N 211 
HIS   HD2  H N N 212 
HIS   HE1  H N N 213 
HIS   HE2  H N N 214 
HIS   HXT  H N N 215 
ILE   N    N N N 216 
ILE   CA   C N S 217 
ILE   C    C N N 218 
ILE   O    O N N 219 
ILE   CB   C N S 220 
ILE   CG1  C N N 221 
ILE   CG2  C N N 222 
ILE   CD1  C N N 223 
ILE   OXT  O N N 224 
ILE   H    H N N 225 
ILE   H2   H N N 226 
ILE   HA   H N N 227 
ILE   HB   H N N 228 
ILE   HG12 H N N 229 
ILE   HG13 H N N 230 
ILE   HG21 H N N 231 
ILE   HG22 H N N 232 
ILE   HG23 H N N 233 
ILE   HD11 H N N 234 
ILE   HD12 H N N 235 
ILE   HD13 H N N 236 
ILE   HXT  H N N 237 
LEU   N    N N N 238 
LEU   CA   C N S 239 
LEU   C    C N N 240 
LEU   O    O N N 241 
LEU   CB   C N N 242 
LEU   CG   C N N 243 
LEU   CD1  C N N 244 
LEU   CD2  C N N 245 
LEU   OXT  O N N 246 
LEU   H    H N N 247 
LEU   H2   H N N 248 
LEU   HA   H N N 249 
LEU   HB2  H N N 250 
LEU   HB3  H N N 251 
LEU   HG   H N N 252 
LEU   HD11 H N N 253 
LEU   HD12 H N N 254 
LEU   HD13 H N N 255 
LEU   HD21 H N N 256 
LEU   HD22 H N N 257 
LEU   HD23 H N N 258 
LEU   HXT  H N N 259 
LYS   N    N N N 260 
LYS   CA   C N S 261 
LYS   C    C N N 262 
LYS   O    O N N 263 
LYS   CB   C N N 264 
LYS   CG   C N N 265 
LYS   CD   C N N 266 
LYS   CE   C N N 267 
LYS   NZ   N N N 268 
LYS   OXT  O N N 269 
LYS   H    H N N 270 
LYS   H2   H N N 271 
LYS   HA   H N N 272 
LYS   HB2  H N N 273 
LYS   HB3  H N N 274 
LYS   HG2  H N N 275 
LYS   HG3  H N N 276 
LYS   HD2  H N N 277 
LYS   HD3  H N N 278 
LYS   HE2  H N N 279 
LYS   HE3  H N N 280 
LYS   HZ1  H N N 281 
LYS   HZ2  H N N 282 
LYS   HZ3  H N N 283 
LYS   HXT  H N N 284 
MET   N    N N N 285 
MET   CA   C N S 286 
MET   C    C N N 287 
MET   O    O N N 288 
MET   CB   C N N 289 
MET   CG   C N N 290 
MET   SD   S N N 291 
MET   CE   C N N 292 
MET   OXT  O N N 293 
MET   H    H N N 294 
MET   H2   H N N 295 
MET   HA   H N N 296 
MET   HB2  H N N 297 
MET   HB3  H N N 298 
MET   HG2  H N N 299 
MET   HG3  H N N 300 
MET   HE1  H N N 301 
MET   HE2  H N N 302 
MET   HE3  H N N 303 
MET   HXT  H N N 304 
PHE   N    N N N 305 
PHE   CA   C N S 306 
PHE   C    C N N 307 
PHE   O    O N N 308 
PHE   CB   C N N 309 
PHE   CG   C Y N 310 
PHE   CD1  C Y N 311 
PHE   CD2  C Y N 312 
PHE   CE1  C Y N 313 
PHE   CE2  C Y N 314 
PHE   CZ   C Y N 315 
PHE   OXT  O N N 316 
PHE   H    H N N 317 
PHE   H2   H N N 318 
PHE   HA   H N N 319 
PHE   HB2  H N N 320 
PHE   HB3  H N N 321 
PHE   HD1  H N N 322 
PHE   HD2  H N N 323 
PHE   HE1  H N N 324 
PHE   HE2  H N N 325 
PHE   HZ   H N N 326 
PHE   HXT  H N N 327 
PRO   N    N N N 328 
PRO   CA   C N S 329 
PRO   C    C N N 330 
PRO   O    O N N 331 
PRO   CB   C N N 332 
PRO   CG   C N N 333 
PRO   CD   C N N 334 
PRO   OXT  O N N 335 
PRO   H    H N N 336 
PRO   HA   H N N 337 
PRO   HB2  H N N 338 
PRO   HB3  H N N 339 
PRO   HG2  H N N 340 
PRO   HG3  H N N 341 
PRO   HD2  H N N 342 
PRO   HD3  H N N 343 
PRO   HXT  H N N 344 
SER   N    N N N 345 
SER   CA   C N S 346 
SER   C    C N N 347 
SER   O    O N N 348 
SER   CB   C N N 349 
SER   OG   O N N 350 
SER   OXT  O N N 351 
SER   H    H N N 352 
SER   H2   H N N 353 
SER   HA   H N N 354 
SER   HB2  H N N 355 
SER   HB3  H N N 356 
SER   HG   H N N 357 
SER   HXT  H N N 358 
THR   N    N N N 359 
THR   CA   C N S 360 
THR   C    C N N 361 
THR   O    O N N 362 
THR   CB   C N R 363 
THR   OG1  O N N 364 
THR   CG2  C N N 365 
THR   OXT  O N N 366 
THR   H    H N N 367 
THR   H2   H N N 368 
THR   HA   H N N 369 
THR   HB   H N N 370 
THR   HG1  H N N 371 
THR   HG21 H N N 372 
THR   HG22 H N N 373 
THR   HG23 H N N 374 
THR   HXT  H N N 375 
TRP   N    N N N 376 
TRP   CA   C N S 377 
TRP   C    C N N 378 
TRP   O    O N N 379 
TRP   CB   C N N 380 
TRP   CG   C Y N 381 
TRP   CD1  C Y N 382 
TRP   CD2  C Y N 383 
TRP   NE1  N Y N 384 
TRP   CE2  C Y N 385 
TRP   CE3  C Y N 386 
TRP   CZ2  C Y N 387 
TRP   CZ3  C Y N 388 
TRP   CH2  C Y N 389 
TRP   OXT  O N N 390 
TRP   H    H N N 391 
TRP   H2   H N N 392 
TRP   HA   H N N 393 
TRP   HB2  H N N 394 
TRP   HB3  H N N 395 
TRP   HD1  H N N 396 
TRP   HE1  H N N 397 
TRP   HE3  H N N 398 
TRP   HZ2  H N N 399 
TRP   HZ3  H N N 400 
TRP   HH2  H N N 401 
TRP   HXT  H N N 402 
TYR   N    N N N 403 
TYR   CA   C N S 404 
TYR   C    C N N 405 
TYR   O    O N N 406 
TYR   CB   C N N 407 
TYR   CG   C Y N 408 
TYR   CD1  C Y N 409 
TYR   CD2  C Y N 410 
TYR   CE1  C Y N 411 
TYR   CE2  C Y N 412 
TYR   CZ   C Y N 413 
TYR   OH   O N N 414 
TYR   OXT  O N N 415 
TYR   H    H N N 416 
TYR   H2   H N N 417 
TYR   HA   H N N 418 
TYR   HB2  H N N 419 
TYR   HB3  H N N 420 
TYR   HD1  H N N 421 
TYR   HD2  H N N 422 
TYR   HE1  H N N 423 
TYR   HE2  H N N 424 
TYR   HH   H N N 425 
TYR   HXT  H N N 426 
VAL   N    N N N 427 
VAL   CA   C N S 428 
VAL   C    C N N 429 
VAL   O    O N N 430 
VAL   CB   C N N 431 
VAL   CG1  C N N 432 
VAL   CG2  C N N 433 
VAL   OXT  O N N 434 
VAL   H    H N N 435 
VAL   H2   H N N 436 
VAL   HA   H N N 437 
VAL   HB   H N N 438 
VAL   HG11 H N N 439 
VAL   HG12 H N N 440 
VAL   HG13 H N N 441 
VAL   HG21 H N N 442 
VAL   HG22 H N N 443 
VAL   HG23 H N N 444 
VAL   HXT  H N N 445 
# 
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 
A1BNM C12 O11  sing N N 1   
A1BNM O11 C10  sing N N 2   
A1BNM O13 C10  doub N N 3   
A1BNM C10 C09  sing N N 4   
A1BNM C17 C16  doub Y N 5   
A1BNM C17 C18  sing Y N 6   
A1BNM C16 C15  sing Y N 7   
A1BNM C09 C08  sing N N 8   
A1BNM C09 C04  sing N N 9   
A1BNM C08 C07  sing N N 10  
A1BNM C05 C04  sing N N 11  
A1BNM C05 C06  doub N N 12  
A1BNM C04 N03  sing N N 13  
A1BNM C06 C15  sing N N 14  
A1BNM C06 C07  sing N N 15  
A1BNM C18 C19  doub Y N 16  
A1BNM C15 C21  doub Y N 17  
A1BNM C07 C14  sing N N 18  
A1BNM C07 C02  sing N N 19  
A1BNM C28 N25  sing N N 20  
A1BNM C28 C29  sing N N 21  
A1BNM N03 C02  sing N N 22  
A1BNM N03 C22  sing N N 23  
A1BNM C24 N25  sing Y N 24  
A1BNM C24 C23  doub Y N 25  
A1BNM C21 C19  sing Y N 26  
A1BNM C19 O20  sing N N 27  
A1BNM N25 N26  sing Y N 28  
A1BNM C02 C01  sing N N 29  
A1BNM C23 C22  sing N N 30  
A1BNM C23 C27  sing Y N 31  
A1BNM N26 C27  doub Y N 32  
A1BNM C01 H1   sing N N 33  
A1BNM C01 H2   sing N N 34  
A1BNM C01 H3   sing N N 35  
A1BNM C02 H4   sing N N 36  
A1BNM C04 H5   sing N N 37  
A1BNM C05 H6   sing N N 38  
A1BNM C08 H7   sing N N 39  
A1BNM C08 H8   sing N N 40  
A1BNM C09 H9   sing N N 41  
A1BNM C12 H10  sing N N 42  
A1BNM C12 H11  sing N N 43  
A1BNM C12 H12  sing N N 44  
A1BNM C14 H13  sing N N 45  
A1BNM C14 H14  sing N N 46  
A1BNM C14 H15  sing N N 47  
A1BNM C16 H16  sing N N 48  
A1BNM C17 H17  sing N N 49  
A1BNM C18 H18  sing N N 50  
A1BNM C21 H19  sing N N 51  
A1BNM C22 H20  sing N N 52  
A1BNM C22 H21  sing N N 53  
A1BNM C24 H22  sing N N 54  
A1BNM C27 H23  sing N N 55  
A1BNM C28 H24  sing N N 56  
A1BNM C28 H25  sing N N 57  
A1BNM C29 H26  sing N N 58  
A1BNM C29 H27  sing N N 59  
A1BNM C29 H28  sing N N 60  
A1BNM O20 H30  sing N N 61  
ALA   N   CA   sing N N 62  
ALA   N   H    sing N N 63  
ALA   N   H2   sing N N 64  
ALA   CA  C    sing N N 65  
ALA   CA  CB   sing N N 66  
ALA   CA  HA   sing N N 67  
ALA   C   O    doub N N 68  
ALA   C   OXT  sing N N 69  
ALA   CB  HB1  sing N N 70  
ALA   CB  HB2  sing N N 71  
ALA   CB  HB3  sing N N 72  
ALA   OXT HXT  sing N N 73  
ARG   N   CA   sing N N 74  
ARG   N   H    sing N N 75  
ARG   N   H2   sing N N 76  
ARG   CA  C    sing N N 77  
ARG   CA  CB   sing N N 78  
ARG   CA  HA   sing N N 79  
ARG   C   O    doub N N 80  
ARG   C   OXT  sing N N 81  
ARG   CB  CG   sing N N 82  
ARG   CB  HB2  sing N N 83  
ARG   CB  HB3  sing N N 84  
ARG   CG  CD   sing N N 85  
ARG   CG  HG2  sing N N 86  
ARG   CG  HG3  sing N N 87  
ARG   CD  NE   sing N N 88  
ARG   CD  HD2  sing N N 89  
ARG   CD  HD3  sing N N 90  
ARG   NE  CZ   sing N N 91  
ARG   NE  HE   sing N N 92  
ARG   CZ  NH1  sing N N 93  
ARG   CZ  NH2  doub N N 94  
ARG   NH1 HH11 sing N N 95  
ARG   NH1 HH12 sing N N 96  
ARG   NH2 HH21 sing N N 97  
ARG   NH2 HH22 sing N N 98  
ARG   OXT HXT  sing N N 99  
ASN   N   CA   sing N N 100 
ASN   N   H    sing N N 101 
ASN   N   H2   sing N N 102 
ASN   CA  C    sing N N 103 
ASN   CA  CB   sing N N 104 
ASN   CA  HA   sing N N 105 
ASN   C   O    doub N N 106 
ASN   C   OXT  sing N N 107 
ASN   CB  CG   sing N N 108 
ASN   CB  HB2  sing N N 109 
ASN   CB  HB3  sing N N 110 
ASN   CG  OD1  doub N N 111 
ASN   CG  ND2  sing N N 112 
ASN   ND2 HD21 sing N N 113 
ASN   ND2 HD22 sing N N 114 
ASN   OXT HXT  sing N N 115 
ASP   N   CA   sing N N 116 
ASP   N   H    sing N N 117 
ASP   N   H2   sing N N 118 
ASP   CA  C    sing N N 119 
ASP   CA  CB   sing N N 120 
ASP   CA  HA   sing N N 121 
ASP   C   O    doub N N 122 
ASP   C   OXT  sing N N 123 
ASP   CB  CG   sing N N 124 
ASP   CB  HB2  sing N N 125 
ASP   CB  HB3  sing N N 126 
ASP   CG  OD1  doub N N 127 
ASP   CG  OD2  sing N N 128 
ASP   OD2 HD2  sing N N 129 
ASP   OXT HXT  sing N N 130 
CYS   N   CA   sing N N 131 
CYS   N   H    sing N N 132 
CYS   N   H2   sing N N 133 
CYS   CA  C    sing N N 134 
CYS   CA  CB   sing N N 135 
CYS   CA  HA   sing N N 136 
CYS   C   O    doub N N 137 
CYS   C   OXT  sing N N 138 
CYS   CB  SG   sing N N 139 
CYS   CB  HB2  sing N N 140 
CYS   CB  HB3  sing N N 141 
CYS   SG  HG   sing N N 142 
CYS   OXT HXT  sing N N 143 
GLN   N   CA   sing N N 144 
GLN   N   H    sing N N 145 
GLN   N   H2   sing N N 146 
GLN   CA  C    sing N N 147 
GLN   CA  CB   sing N N 148 
GLN   CA  HA   sing N N 149 
GLN   C   O    doub N N 150 
GLN   C   OXT  sing N N 151 
GLN   CB  CG   sing N N 152 
GLN   CB  HB2  sing N N 153 
GLN   CB  HB3  sing N N 154 
GLN   CG  CD   sing N N 155 
GLN   CG  HG2  sing N N 156 
GLN   CG  HG3  sing N N 157 
GLN   CD  OE1  doub N N 158 
GLN   CD  NE2  sing N N 159 
GLN   NE2 HE21 sing N N 160 
GLN   NE2 HE22 sing N N 161 
GLN   OXT HXT  sing N N 162 
GLU   N   CA   sing N N 163 
GLU   N   H    sing N N 164 
GLU   N   H2   sing N N 165 
GLU   CA  C    sing N N 166 
GLU   CA  CB   sing N N 167 
GLU   CA  HA   sing N N 168 
GLU   C   O    doub N N 169 
GLU   C   OXT  sing N N 170 
GLU   CB  CG   sing N N 171 
GLU   CB  HB2  sing N N 172 
GLU   CB  HB3  sing N N 173 
GLU   CG  CD   sing N N 174 
GLU   CG  HG2  sing N N 175 
GLU   CG  HG3  sing N N 176 
GLU   CD  OE1  doub N N 177 
GLU   CD  OE2  sing N N 178 
GLU   OE2 HE2  sing N N 179 
GLU   OXT HXT  sing N N 180 
GLY   N   CA   sing N N 181 
GLY   N   H    sing N N 182 
GLY   N   H2   sing N N 183 
GLY   CA  C    sing N N 184 
GLY   CA  HA2  sing N N 185 
GLY   CA  HA3  sing N N 186 
GLY   C   O    doub N N 187 
GLY   C   OXT  sing N N 188 
GLY   OXT HXT  sing N N 189 
HIS   N   CA   sing N N 190 
HIS   N   H    sing N N 191 
HIS   N   H2   sing N N 192 
HIS   CA  C    sing N N 193 
HIS   CA  CB   sing N N 194 
HIS   CA  HA   sing N N 195 
HIS   C   O    doub N N 196 
HIS   C   OXT  sing N N 197 
HIS   CB  CG   sing N N 198 
HIS   CB  HB2  sing N N 199 
HIS   CB  HB3  sing N N 200 
HIS   CG  ND1  sing Y N 201 
HIS   CG  CD2  doub Y N 202 
HIS   ND1 CE1  doub Y N 203 
HIS   ND1 HD1  sing N N 204 
HIS   CD2 NE2  sing Y N 205 
HIS   CD2 HD2  sing N N 206 
HIS   CE1 NE2  sing Y N 207 
HIS   CE1 HE1  sing N N 208 
HIS   NE2 HE2  sing N N 209 
HIS   OXT HXT  sing N N 210 
ILE   N   CA   sing N N 211 
ILE   N   H    sing N N 212 
ILE   N   H2   sing N N 213 
ILE   CA  C    sing N N 214 
ILE   CA  CB   sing N N 215 
ILE   CA  HA   sing N N 216 
ILE   C   O    doub N N 217 
ILE   C   OXT  sing N N 218 
ILE   CB  CG1  sing N N 219 
ILE   CB  CG2  sing N N 220 
ILE   CB  HB   sing N N 221 
ILE   CG1 CD1  sing N N 222 
ILE   CG1 HG12 sing N N 223 
ILE   CG1 HG13 sing N N 224 
ILE   CG2 HG21 sing N N 225 
ILE   CG2 HG22 sing N N 226 
ILE   CG2 HG23 sing N N 227 
ILE   CD1 HD11 sing N N 228 
ILE   CD1 HD12 sing N N 229 
ILE   CD1 HD13 sing N N 230 
ILE   OXT HXT  sing N N 231 
LEU   N   CA   sing N N 232 
LEU   N   H    sing N N 233 
LEU   N   H2   sing N N 234 
LEU   CA  C    sing N N 235 
LEU   CA  CB   sing N N 236 
LEU   CA  HA   sing N N 237 
LEU   C   O    doub N N 238 
LEU   C   OXT  sing N N 239 
LEU   CB  CG   sing N N 240 
LEU   CB  HB2  sing N N 241 
LEU   CB  HB3  sing N N 242 
LEU   CG  CD1  sing N N 243 
LEU   CG  CD2  sing N N 244 
LEU   CG  HG   sing N N 245 
LEU   CD1 HD11 sing N N 246 
LEU   CD1 HD12 sing N N 247 
LEU   CD1 HD13 sing N N 248 
LEU   CD2 HD21 sing N N 249 
LEU   CD2 HD22 sing N N 250 
LEU   CD2 HD23 sing N N 251 
LEU   OXT HXT  sing N N 252 
LYS   N   CA   sing N N 253 
LYS   N   H    sing N N 254 
LYS   N   H2   sing N N 255 
LYS   CA  C    sing N N 256 
LYS   CA  CB   sing N N 257 
LYS   CA  HA   sing N N 258 
LYS   C   O    doub N N 259 
LYS   C   OXT  sing N N 260 
LYS   CB  CG   sing N N 261 
LYS   CB  HB2  sing N N 262 
LYS   CB  HB3  sing N N 263 
LYS   CG  CD   sing N N 264 
LYS   CG  HG2  sing N N 265 
LYS   CG  HG3  sing N N 266 
LYS   CD  CE   sing N N 267 
LYS   CD  HD2  sing N N 268 
LYS   CD  HD3  sing N N 269 
LYS   CE  NZ   sing N N 270 
LYS   CE  HE2  sing N N 271 
LYS   CE  HE3  sing N N 272 
LYS   NZ  HZ1  sing N N 273 
LYS   NZ  HZ2  sing N N 274 
LYS   NZ  HZ3  sing N N 275 
LYS   OXT HXT  sing N N 276 
MET   N   CA   sing N N 277 
MET   N   H    sing N N 278 
MET   N   H2   sing N N 279 
MET   CA  C    sing N N 280 
MET   CA  CB   sing N N 281 
MET   CA  HA   sing N N 282 
MET   C   O    doub N N 283 
MET   C   OXT  sing N N 284 
MET   CB  CG   sing N N 285 
MET   CB  HB2  sing N N 286 
MET   CB  HB3  sing N N 287 
MET   CG  SD   sing N N 288 
MET   CG  HG2  sing N N 289 
MET   CG  HG3  sing N N 290 
MET   SD  CE   sing N N 291 
MET   CE  HE1  sing N N 292 
MET   CE  HE2  sing N N 293 
MET   CE  HE3  sing N N 294 
MET   OXT HXT  sing N N 295 
PHE   N   CA   sing N N 296 
PHE   N   H    sing N N 297 
PHE   N   H2   sing N N 298 
PHE   CA  C    sing N N 299 
PHE   CA  CB   sing N N 300 
PHE   CA  HA   sing N N 301 
PHE   C   O    doub N N 302 
PHE   C   OXT  sing N N 303 
PHE   CB  CG   sing N N 304 
PHE   CB  HB2  sing N N 305 
PHE   CB  HB3  sing N N 306 
PHE   CG  CD1  doub Y N 307 
PHE   CG  CD2  sing Y N 308 
PHE   CD1 CE1  sing Y N 309 
PHE   CD1 HD1  sing N N 310 
PHE   CD2 CE2  doub Y N 311 
PHE   CD2 HD2  sing N N 312 
PHE   CE1 CZ   doub Y N 313 
PHE   CE1 HE1  sing N N 314 
PHE   CE2 CZ   sing Y N 315 
PHE   CE2 HE2  sing N N 316 
PHE   CZ  HZ   sing N N 317 
PHE   OXT HXT  sing N N 318 
PRO   N   CA   sing N N 319 
PRO   N   CD   sing N N 320 
PRO   N   H    sing N N 321 
PRO   CA  C    sing N N 322 
PRO   CA  CB   sing N N 323 
PRO   CA  HA   sing N N 324 
PRO   C   O    doub N N 325 
PRO   C   OXT  sing N N 326 
PRO   CB  CG   sing N N 327 
PRO   CB  HB2  sing N N 328 
PRO   CB  HB3  sing N N 329 
PRO   CG  CD   sing N N 330 
PRO   CG  HG2  sing N N 331 
PRO   CG  HG3  sing N N 332 
PRO   CD  HD2  sing N N 333 
PRO   CD  HD3  sing N N 334 
PRO   OXT HXT  sing N N 335 
SER   N   CA   sing N N 336 
SER   N   H    sing N N 337 
SER   N   H2   sing N N 338 
SER   CA  C    sing N N 339 
SER   CA  CB   sing N N 340 
SER   CA  HA   sing N N 341 
SER   C   O    doub N N 342 
SER   C   OXT  sing N N 343 
SER   CB  OG   sing N N 344 
SER   CB  HB2  sing N N 345 
SER   CB  HB3  sing N N 346 
SER   OG  HG   sing N N 347 
SER   OXT HXT  sing N N 348 
THR   N   CA   sing N N 349 
THR   N   H    sing N N 350 
THR   N   H2   sing N N 351 
THR   CA  C    sing N N 352 
THR   CA  CB   sing N N 353 
THR   CA  HA   sing N N 354 
THR   C   O    doub N N 355 
THR   C   OXT  sing N N 356 
THR   CB  OG1  sing N N 357 
THR   CB  CG2  sing N N 358 
THR   CB  HB   sing N N 359 
THR   OG1 HG1  sing N N 360 
THR   CG2 HG21 sing N N 361 
THR   CG2 HG22 sing N N 362 
THR   CG2 HG23 sing N N 363 
THR   OXT HXT  sing N N 364 
TRP   N   CA   sing N N 365 
TRP   N   H    sing N N 366 
TRP   N   H2   sing N N 367 
TRP   CA  C    sing N N 368 
TRP   CA  CB   sing N N 369 
TRP   CA  HA   sing N N 370 
TRP   C   O    doub N N 371 
TRP   C   OXT  sing N N 372 
TRP   CB  CG   sing N N 373 
TRP   CB  HB2  sing N N 374 
TRP   CB  HB3  sing N N 375 
TRP   CG  CD1  doub Y N 376 
TRP   CG  CD2  sing Y N 377 
TRP   CD1 NE1  sing Y N 378 
TRP   CD1 HD1  sing N N 379 
TRP   CD2 CE2  doub Y N 380 
TRP   CD2 CE3  sing Y N 381 
TRP   NE1 CE2  sing Y N 382 
TRP   NE1 HE1  sing N N 383 
TRP   CE2 CZ2  sing Y N 384 
TRP   CE3 CZ3  doub Y N 385 
TRP   CE3 HE3  sing N N 386 
TRP   CZ2 CH2  doub Y N 387 
TRP   CZ2 HZ2  sing N N 388 
TRP   CZ3 CH2  sing Y N 389 
TRP   CZ3 HZ3  sing N N 390 
TRP   CH2 HH2  sing N N 391 
TRP   OXT HXT  sing N N 392 
TYR   N   CA   sing N N 393 
TYR   N   H    sing N N 394 
TYR   N   H2   sing N N 395 
TYR   CA  C    sing N N 396 
TYR   CA  CB   sing N N 397 
TYR   CA  HA   sing N N 398 
TYR   C   O    doub N N 399 
TYR   C   OXT  sing N N 400 
TYR   CB  CG   sing N N 401 
TYR   CB  HB2  sing N N 402 
TYR   CB  HB3  sing N N 403 
TYR   CG  CD1  doub Y N 404 
TYR   CG  CD2  sing Y N 405 
TYR   CD1 CE1  sing Y N 406 
TYR   CD1 HD1  sing N N 407 
TYR   CD2 CE2  doub Y N 408 
TYR   CD2 HD2  sing N N 409 
TYR   CE1 CZ   doub Y N 410 
TYR   CE1 HE1  sing N N 411 
TYR   CE2 CZ   sing Y N 412 
TYR   CE2 HE2  sing N N 413 
TYR   CZ  OH   sing N N 414 
TYR   OH  HH   sing N N 415 
TYR   OXT HXT  sing N N 416 
VAL   N   CA   sing N N 417 
VAL   N   H    sing N N 418 
VAL   N   H2   sing N N 419 
VAL   CA  C    sing N N 420 
VAL   CA  CB   sing N N 421 
VAL   CA  HA   sing N N 422 
VAL   C   O    doub N N 423 
VAL   C   OXT  sing N N 424 
VAL   CB  CG1  sing N N 425 
VAL   CB  CG2  sing N N 426 
VAL   CB  HB   sing N N 427 
VAL   CG1 HG11 sing N N 428 
VAL   CG1 HG12 sing N N 429 
VAL   CG1 HG13 sing N N 430 
VAL   CG2 HG21 sing N N 431 
VAL   CG2 HG22 sing N N 432 
VAL   CG2 HG23 sing N N 433 
VAL   OXT HXT  sing N N 434 
# 
_em_admin.current_status     REL 
_em_admin.deposition_date    2025-01-03 
_em_admin.deposition_site    RCSB 
_em_admin.entry_id           9MQL 
_em_admin.last_update        2025-03-12 
_em_admin.map_release_date   2025-02-12 
_em_admin.title              
'Locally-Refined Inactive Kappa-Opioid Receptor with Nb6M, NabFab, and isoquinuclidine compound #020_E1' 
# 
_em_ctf_correction.details                  ? 
_em_ctf_correction.em_image_processing_id   1 
_em_ctf_correction.id                       1 
_em_ctf_correction.type                     'PHASE FLIPPING ONLY' 
# 
_em_entity_assembly_molwt.entity_assembly_id   1 
_em_entity_assembly_molwt.experimental_flag    NO 
_em_entity_assembly_molwt.id                   1 
_em_entity_assembly_molwt.units                MEGADALTONS 
_em_entity_assembly_molwt.value                46 
# 
_em_entity_assembly_naturalsource.cell                 ? 
_em_entity_assembly_naturalsource.cellular_location    ? 
_em_entity_assembly_naturalsource.entity_assembly_id   1 
_em_entity_assembly_naturalsource.id                   2 
_em_entity_assembly_naturalsource.ncbi_tax_id          10090 
_em_entity_assembly_naturalsource.organism             'Mus musculus' 
_em_entity_assembly_naturalsource.organelle            ? 
_em_entity_assembly_naturalsource.organ                ? 
_em_entity_assembly_naturalsource.strain               ? 
_em_entity_assembly_naturalsource.tissue               ? 
_em_entity_assembly_naturalsource.details              ? 
# 
_em_entity_assembly_recombinant.cell                 ? 
_em_entity_assembly_recombinant.entity_assembly_id   1 
_em_entity_assembly_recombinant.id                   2 
_em_entity_assembly_recombinant.ncbi_tax_id          10090 
_em_entity_assembly_recombinant.organism             'Mus musculus' 
_em_entity_assembly_recombinant.plasmid              ? 
_em_entity_assembly_recombinant.strain               ? 
# 
_em_image_processing.details              ? 
_em_image_processing.id                   1 
_em_image_processing.image_recording_id   1 
# 
_em_image_recording.average_exposure_time               ? 
_em_image_recording.avg_electron_dose_per_subtomogram   ? 
_em_image_recording.avg_electron_dose_per_image         64.1 
_em_image_recording.details                             ? 
_em_image_recording.detector_mode                       ? 
_em_image_recording.film_or_detector_model              'GATAN K3 BIOQUANTUM (6k x 4k)' 
_em_image_recording.id                                  1 
_em_image_recording.imaging_id                          1 
_em_image_recording.num_diffraction_images              ? 
_em_image_recording.num_grids_imaged                    ? 
_em_image_recording.num_real_images                     ? 
# 
_em_imaging_optics.chr_aberration_corrector   ? 
_em_imaging_optics.energyfilter_lower         ? 
_em_imaging_optics.energyfilter_slit_width    ? 
_em_imaging_optics.energyfilter_name          ? 
_em_imaging_optics.energyfilter_upper         ? 
_em_imaging_optics.id                         1 
_em_imaging_optics.imaging_id                 1 
_em_imaging_optics.phase_plate                OTHER 
_em_imaging_optics.sph_aberration_corrector   ? 
_em_imaging_optics.details                    ? 
# 
loop_
_em_software.category 
_em_software.details 
_em_software.id 
_em_software.image_processing_id 
_em_software.fitting_id 
_em_software.imaging_id 
_em_software.name 
_em_software.version 
'PARTICLE SELECTION'       ? 1  1 ? ? ?      ?            
'MODEL REFINEMENT'         ? 2  ? ? ? PHENIX 1.21.1_5286: 
'IMAGE ACQUISITION'        ? 3  1 ? 1 ?      ?            
MASKING                    ? 4  1 1 1 ?      ?            
'CTF CORRECTION'           ? 5  1 ? ? ?      ?            
'LAYERLINE INDEXING'       ? 6  1 1 1 ?      ?            
'DIFFRACTION INDEXING'     ? 7  1 1 1 ?      ?            
'MODEL FITTING'            ? 8  1 1 1 ?      ?            
OTHER                      ? 9  1 1 1 ?      ?            
'INITIAL EULER ASSIGNMENT' ? 10 1 ? ? ?      ?            
'FINAL EULER ASSIGNMENT'   ? 11 1 ? ? ?      ?            
CLASSIFICATION             ? 12 1 ? ? ?      ?            
RECONSTRUCTION             ? 13 1 ? ? ?      ?            
# 
_em_specimen.concentration           ? 
_em_specimen.details                 ? 
_em_specimen.embedding_applied       NO 
_em_specimen.experiment_id           1 
_em_specimen.id                      1 
_em_specimen.shadowing_applied       NO 
_em_specimen.staining_applied        NO 
_em_specimen.vitrification_applied   YES 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'Defense Advanced Research Projects Agency (DARPA)'                                        'United States' HR0011-19-2-0020 1 
'National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)' 'United States' R35GM122481      2 
'National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)' 'United States' R35GM122473      3 
# 
_atom_sites.entry_id                    9MQL 
_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]   1.000000 
_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]   1.000000 
_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]   1.000000 
_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 
C 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . ALA   A 1 65  ? 181.494 149.596 177.585 1.00 106.04 ? 57  ALA   A N   1 
ATOM   2    C CA  . ALA   A 1 65  ? 180.193 149.843 178.193 1.00 113.24 ? 57  ALA   A CA  1 
ATOM   3    C C   . ALA   A 1 65  ? 179.802 151.312 178.078 1.00 114.14 ? 57  ALA   A C   1 
ATOM   4    O O   . ALA   A 1 65  ? 180.412 152.178 178.704 1.00 110.28 ? 57  ALA   A O   1 
ATOM   5    C CB  . ALA   A 1 65  ? 180.198 149.409 179.650 1.00 108.10 ? 57  ALA   A CB  1 
ATOM   6    N N   . ILE   A 1 66  ? 178.779 151.585 177.274 1.00 114.50 ? 58  ILE   A N   1 
ATOM   7    C CA  . ILE   A 1 66  ? 178.277 152.943 177.086 1.00 113.98 ? 58  ILE   A CA  1 
ATOM   8    C C   . ILE   A 1 66  ? 176.752 152.899 177.151 1.00 113.91 ? 58  ILE   A C   1 
ATOM   9    O O   . ILE   A 1 66  ? 176.104 152.322 176.266 1.00 113.47 ? 58  ILE   A O   1 
ATOM   10   C CB  . ILE   A 1 66  ? 178.796 153.548 175.770 1.00 114.28 ? 58  ILE   A CB  1 
ATOM   11   C CG1 . ILE   A 1 66  ? 178.096 154.873 175.464 1.00 108.10 ? 58  ILE   A CG1 1 
ATOM   12   C CG2 . ILE   A 1 66  ? 178.679 152.553 174.616 1.00 113.07 ? 58  ILE   A CG2 1 
ATOM   13   C CD1 . ILE   A 1 66  ? 178.330 155.944 176.508 1.00 103.68 ? 58  ILE   A CD1 1 
ATOM   14   N N   . PRO   A 1 67  ? 176.139 153.477 178.188 1.00 113.14 ? 59  PRO   A N   1 
ATOM   15   C CA  . PRO   A 1 67  ? 174.697 153.271 178.398 1.00 107.23 ? 59  PRO   A CA  1 
ATOM   16   C C   . PRO   A 1 67  ? 173.800 153.979 177.396 1.00 103.29 ? 59  PRO   A C   1 
ATOM   17   O O   . PRO   A 1 67  ? 172.618 153.628 177.308 1.00 95.25  ? 59  PRO   A O   1 
ATOM   18   C CB  . PRO   A 1 67  ? 174.470 153.813 179.816 1.00 103.66 ? 59  PRO   A CB  1 
ATOM   19   C CG  . PRO   A 1 67  ? 175.567 154.803 180.015 1.00 108.95 ? 59  PRO   A CG  1 
ATOM   20   C CD  . PRO   A 1 67  ? 176.754 154.245 179.285 1.00 112.99 ? 59  PRO   A CD  1 
ATOM   21   N N   . VAL   A 1 68  ? 174.303 154.960 176.643 1.00 107.61 ? 60  VAL   A N   1 
ATOM   22   C CA  . VAL   A 1 68  ? 173.402 155.767 175.827 1.00 104.68 ? 60  VAL   A CA  1 
ATOM   23   C C   . VAL   A 1 68  ? 172.965 155.051 174.556 1.00 95.57  ? 60  VAL   A C   1 
ATOM   24   O O   . VAL   A 1 68  ? 172.026 155.505 173.897 1.00 88.53  ? 60  VAL   A O   1 
ATOM   25   C CB  . VAL   A 1 68  ? 174.037 157.126 175.472 1.00 103.28 ? 60  VAL   A CB  1 
ATOM   26   C CG1 . VAL   A 1 68  ? 174.275 157.948 176.731 1.00 99.13  ? 60  VAL   A CG1 1 
ATOM   27   C CG2 . VAL   A 1 68  ? 175.318 156.934 174.685 1.00 105.99 ? 60  VAL   A CG2 1 
ATOM   28   N N   . ILE   A 1 69  ? 173.597 153.933 174.196 1.00 93.89  ? 61  ILE   A N   1 
ATOM   29   C CA  . ILE   A 1 69  ? 173.239 153.254 172.952 1.00 93.47  ? 61  ILE   A CA  1 
ATOM   30   C C   . ILE   A 1 69  ? 171.871 152.591 173.078 1.00 89.84  ? 61  ILE   A C   1 
ATOM   31   O O   . ILE   A 1 69  ? 170.926 152.926 172.352 1.00 87.46  ? 61  ILE   A O   1 
ATOM   32   C CB  . ILE   A 1 69  ? 174.324 152.234 172.561 1.00 97.17  ? 61  ILE   A CB  1 
ATOM   33   C CG1 . ILE   A 1 69  ? 175.589 152.958 172.095 1.00 105.83 ? 61  ILE   A CG1 1 
ATOM   34   C CG2 . ILE   A 1 69  ? 173.812 151.304 171.472 1.00 97.29  ? 61  ILE   A CG2 1 
ATOM   35   C CD1 . ILE   A 1 69  ? 176.667 152.031 171.575 1.00 109.22 ? 61  ILE   A CD1 1 
ATOM   36   N N   . ILE   A 1 70  ? 171.746 151.639 174.005 1.00 90.54  ? 62  ILE   A N   1 
ATOM   37   C CA  . ILE   A 1 70  ? 170.477 150.939 174.169 1.00 84.53  ? 62  ILE   A CA  1 
ATOM   38   C C   . ILE   A 1 70  ? 169.414 151.874 174.734 1.00 81.25  ? 62  ILE   A C   1 
ATOM   39   O O   . ILE   A 1 70  ? 168.230 151.745 174.405 1.00 76.24  ? 62  ILE   A O   1 
ATOM   40   C CB  . ILE   A 1 70  ? 170.673 149.681 175.036 1.00 77.93  ? 62  ILE   A CB  1 
ATOM   41   C CG1 . ILE   A 1 70  ? 171.566 148.679 174.304 1.00 74.92  ? 62  ILE   A CG1 1 
ATOM   42   C CG2 . ILE   A 1 70  ? 169.344 149.028 175.357 1.00 69.82  ? 62  ILE   A CG2 1 
ATOM   43   C CD1 . ILE   A 1 70  ? 171.834 147.411 175.078 1.00 73.15  ? 62  ILE   A CD1 1 
ATOM   44   N N   . THR   A 1 71  ? 169.807 152.836 175.573 1.00 82.36  ? 63  THR   A N   1 
ATOM   45   C CA  . THR   A 1 71  ? 168.844 153.817 176.069 1.00 74.21  ? 63  THR   A CA  1 
ATOM   46   C C   . THR   A 1 71  ? 168.319 154.701 174.941 1.00 77.09  ? 63  THR   A C   1 
ATOM   47   O O   . THR   A 1 71  ? 167.125 155.018 174.898 1.00 75.92  ? 63  THR   A O   1 
ATOM   48   C CB  . THR   A 1 71  ? 169.477 154.668 177.168 1.00 74.16  ? 63  THR   A CB  1 
ATOM   49   O OG1 . THR   A 1 71  ? 170.011 153.812 178.185 1.00 80.87  ? 63  THR   A OG1 1 
ATOM   50   C CG2 . THR   A 1 71  ? 168.441 155.589 177.788 1.00 68.81  ? 63  THR   A CG2 1 
ATOM   51   N N   . ALA   A 1 72  ? 169.194 155.106 174.017 1.00 81.02  ? 64  ALA   A N   1 
ATOM   52   C CA  . ALA   A 1 72  ? 168.749 155.874 172.860 1.00 80.44  ? 64  ALA   A CA  1 
ATOM   53   C C   . ALA   A 1 72  ? 167.839 155.042 171.967 1.00 73.86  ? 64  ALA   A C   1 
ATOM   54   O O   . ALA   A 1 72  ? 166.854 155.555 171.425 1.00 67.43  ? 64  ALA   A O   1 
ATOM   55   C CB  . ALA   A 1 72  ? 169.953 156.386 172.072 1.00 79.57  ? 64  ALA   A CB  1 
ATOM   56   N N   . VAL   A 1 73  ? 168.159 153.757 171.799 1.00 71.95  ? 65  VAL   A N   1 
ATOM   57   C CA  . VAL   A 1 73  ? 167.281 152.872 171.037 1.00 70.63  ? 65  VAL   A CA  1 
ATOM   58   C C   . VAL   A 1 73  ? 165.912 152.786 171.700 1.00 70.02  ? 65  VAL   A C   1 
ATOM   59   O O   . VAL   A 1 73  ? 164.872 152.845 171.030 1.00 68.81  ? 65  VAL   A O   1 
ATOM   60   C CB  . VAL   A 1 73  ? 167.929 151.483 170.883 1.00 68.93  ? 65  VAL   A CB  1 
ATOM   61   C CG1 . VAL   A 1 73  ? 166.901 150.458 170.436 1.00 60.21  ? 65  VAL   A CG1 1 
ATOM   62   C CG2 . VAL   A 1 73  ? 169.083 151.547 169.899 1.00 73.59  ? 65  VAL   A CG2 1 
ATOM   63   N N   . TYR   A 1 74  ? 165.891 152.655 173.028 1.00 71.92  ? 66  TYR   A N   1 
ATOM   64   C CA  . TYR   A 1 74  ? 164.629 152.581 173.756 1.00 66.34  ? 66  TYR   A CA  1 
ATOM   65   C C   . TYR   A 1 74  ? 163.823 153.863 173.603 1.00 67.12  ? 66  TYR   A C   1 
ATOM   66   O O   . TYR   A 1 74  ? 162.602 153.815 173.437 1.00 66.40  ? 66  TYR   A O   1 
ATOM   67   C CB  . TYR   A 1 74  ? 164.888 152.290 175.234 1.00 64.68  ? 66  TYR   A CB  1 
ATOM   68   C CG  . TYR   A 1 74  ? 165.138 150.832 175.546 1.00 67.58  ? 66  TYR   A CG  1 
ATOM   69   C CD1 . TYR   A 1 74  ? 164.534 149.828 174.804 1.00 69.03  ? 66  TYR   A CD1 1 
ATOM   70   C CD2 . TYR   A 1 74  ? 165.967 150.461 176.595 1.00 64.94  ? 66  TYR   A CD2 1 
ATOM   71   C CE1 . TYR   A 1 74  ? 164.757 148.496 175.091 1.00 66.17  ? 66  TYR   A CE1 1 
ATOM   72   C CE2 . TYR   A 1 74  ? 166.193 149.133 176.891 1.00 65.96  ? 66  TYR   A CE2 1 
ATOM   73   C CZ  . TYR   A 1 74  ? 165.587 148.155 176.136 1.00 68.98  ? 66  TYR   A CZ  1 
ATOM   74   O OH  . TYR   A 1 74  ? 165.814 146.830 176.427 1.00 69.50  ? 66  TYR   A OH  1 
ATOM   75   N N   . SER   A 1 75  ? 164.486 155.021 173.667 1.00 65.43  ? 67  SER   A N   1 
ATOM   76   C CA  . SER   A 1 75  ? 163.778 156.291 173.504 1.00 59.43  ? 67  SER   A CA  1 
ATOM   77   C C   . SER   A 1 75  ? 163.234 156.450 172.088 1.00 60.53  ? 67  SER   A C   1 
ATOM   78   O O   . SER   A 1 75  ? 162.103 156.922 171.895 1.00 60.91  ? 67  SER   A O   1 
ATOM   79   C CB  . SER   A 1 75  ? 164.705 157.453 173.855 1.00 61.52  ? 67  SER   A CB  1 
ATOM   80   O OG  . SER   A 1 75  ? 165.353 157.228 175.094 1.00 67.68  ? 67  SER   A OG  1 
ATOM   81   N N   . VAL   A 1 76  ? 164.028 156.063 171.087 1.00 61.12  ? 68  VAL   A N   1 
ATOM   82   C CA  . VAL   A 1 76  ? 163.574 156.127 169.702 1.00 59.42  ? 68  VAL   A CA  1 
ATOM   83   C C   . VAL   A 1 76  ? 162.354 155.242 169.507 1.00 58.81  ? 68  VAL   A C   1 
ATOM   84   O O   . VAL   A 1 76  ? 161.387 155.633 168.846 1.00 54.81  ? 68  VAL   A O   1 
ATOM   85   C CB  . VAL   A 1 76  ? 164.718 155.740 168.746 1.00 64.32  ? 68  VAL   A CB  1 
ATOM   86   C CG1 . VAL   A 1 76  ? 164.172 155.387 167.371 1.00 61.27  ? 68  VAL   A CG1 1 
ATOM   87   C CG2 . VAL   A 1 76  ? 165.729 156.871 168.649 1.00 69.43  ? 68  VAL   A CG2 1 
ATOM   88   N N   . VAL   A 1 77  ? 162.377 154.036 170.077 1.00 64.53  ? 69  VAL   A N   1 
ATOM   89   C CA  . VAL   A 1 77  ? 161.193 153.183 170.035 1.00 59.79  ? 69  VAL   A CA  1 
ATOM   90   C C   . VAL   A 1 77  ? 160.024 153.878 170.721 1.00 51.41  ? 69  VAL   A C   1 
ATOM   91   O O   . VAL   A 1 77  ? 158.966 154.085 170.118 1.00 50.27  ? 69  VAL   A O   1 
ATOM   92   C CB  . VAL   A 1 77  ? 161.492 151.815 170.676 1.00 57.16  ? 69  VAL   A CB  1 
ATOM   93   C CG1 . VAL   A 1 77  ? 160.201 151.060 170.944 1.00 50.45  ? 69  VAL   A CG1 1 
ATOM   94   C CG2 . VAL   A 1 77  ? 162.412 151.002 169.782 1.00 54.83  ? 69  VAL   A CG2 1 
ATOM   95   N N   . PHE   A 1 78  ? 160.246 154.340 171.955 1.00 52.18  ? 70  PHE   A N   1 
ATOM   96   C CA  . PHE   A 1 78  ? 159.202 154.931 172.785 1.00 56.97  ? 70  PHE   A CA  1 
ATOM   97   C C   . PHE   A 1 78  ? 158.476 156.063 172.077 1.00 56.50  ? 70  PHE   A C   1 
ATOM   98   O O   . PHE   A 1 78  ? 157.270 156.246 172.273 1.00 54.74  ? 70  PHE   A O   1 
ATOM   99   C CB  . PHE   A 1 78  ? 159.832 155.421 174.094 1.00 54.13  ? 70  PHE   A CB  1 
ATOM   100  C CG  . PHE   A 1 78  ? 158.896 156.185 174.988 1.00 54.31  ? 70  PHE   A CG  1 
ATOM   101  C CD1 . PHE   A 1 78  ? 157.676 155.652 175.363 1.00 55.18  ? 70  PHE   A CD1 1 
ATOM   102  C CD2 . PHE   A 1 78  ? 159.255 157.432 175.476 1.00 51.32  ? 70  PHE   A CD2 1 
ATOM   103  C CE1 . PHE   A 1 78  ? 156.825 156.355 176.195 1.00 53.71  ? 70  PHE   A CE1 1 
ATOM   104  C CE2 . PHE   A 1 78  ? 158.409 158.139 176.306 1.00 51.41  ? 70  PHE   A CE2 1 
ATOM   105  C CZ  . PHE   A 1 78  ? 157.193 157.600 176.666 1.00 52.11  ? 70  PHE   A CZ  1 
ATOM   106  N N   . VAL   A 1 79  ? 159.184 156.829 171.251 1.00 53.50  ? 71  VAL   A N   1 
ATOM   107  C CA  . VAL   A 1 79  ? 158.536 157.923 170.534 1.00 48.54  ? 71  VAL   A CA  1 
ATOM   108  C C   . VAL   A 1 79  ? 157.997 157.449 169.187 1.00 51.13  ? 71  VAL   A C   1 
ATOM   109  O O   . VAL   A 1 79  ? 156.787 157.522 168.927 1.00 51.35  ? 71  VAL   A O   1 
ATOM   110  C CB  . VAL   A 1 79  ? 159.497 159.110 170.352 1.00 48.21  ? 71  VAL   A CB  1 
ATOM   111  C CG1 . VAL   A 1 79  ? 158.803 160.238 169.613 1.00 50.03  ? 71  VAL   A CG1 1 
ATOM   112  C CG2 . VAL   A 1 79  ? 160.002 159.588 171.701 1.00 49.32  ? 71  VAL   A CG2 1 
ATOM   113  N N   . VAL   A 1 80  ? 158.893 156.970 168.320 1.00 55.83  ? 72  VAL   A N   1 
ATOM   114  C CA  . VAL   A 1 80  ? 158.542 156.727 166.925 1.00 55.76  ? 72  VAL   A CA  1 
ATOM   115  C C   . VAL   A 1 80  ? 157.537 155.588 166.796 1.00 53.10  ? 72  VAL   A C   1 
ATOM   116  O O   . VAL   A 1 80  ? 156.574 155.687 166.029 1.00 51.84  ? 72  VAL   A O   1 
ATOM   117  C CB  . VAL   A 1 80  ? 159.818 156.462 166.103 1.00 60.30  ? 72  VAL   A CB  1 
ATOM   118  C CG1 . VAL   A 1 80  ? 159.521 155.570 164.906 1.00 54.29  ? 72  VAL   A CG1 1 
ATOM   119  C CG2 . VAL   A 1 80  ? 160.435 157.775 165.653 1.00 61.04  ? 72  VAL   A CG2 1 
ATOM   120  N N   . GLY   A 1 81  ? 157.753 154.477 167.507 1.00 50.84  ? 73  GLY   A N   1 
ATOM   121  C CA  . GLY   A 1 81  ? 156.821 153.368 167.403 1.00 49.35  ? 73  GLY   A CA  1 
ATOM   122  C C   . GLY   A 1 81  ? 155.439 153.732 167.905 1.00 48.94  ? 73  GLY   A C   1 
ATOM   123  O O   . GLY   A 1 81  ? 154.431 153.357 167.302 1.00 53.89  ? 73  GLY   A O   1 
ATOM   124  N N   . LEU   A 1 82  ? 155.373 154.476 169.011 1.00 43.84  ? 74  LEU   A N   1 
ATOM   125  C CA  . LEU   A 1 82  ? 154.088 154.945 169.516 1.00 42.58  ? 74  LEU   A CA  1 
ATOM   126  C C   . LEU   A 1 82  ? 153.379 155.801 168.477 1.00 42.38  ? 74  LEU   A C   1 
ATOM   127  O O   . LEU   A 1 82  ? 152.197 155.586 168.182 1.00 44.87  ? 74  LEU   A O   1 
ATOM   128  C CB  . LEU   A 1 82  ? 154.292 155.727 170.815 1.00 46.15  ? 74  LEU   A CB  1 
ATOM   129  C CG  . LEU   A 1 82  ? 153.102 155.946 171.757 1.00 42.18  ? 74  LEU   A CG  1 
ATOM   130  C CD1 . LEU   A 1 82  ? 152.266 157.146 171.340 1.00 39.23  ? 74  LEU   A CD1 1 
ATOM   131  C CD2 . LEU   A 1 82  ? 152.240 154.698 171.839 1.00 42.74  ? 74  LEU   A CD2 1 
ATOM   132  N N   . VAL   A 1 83  ? 154.094 156.768 167.895 1.00 43.79  ? 75  VAL   A N   1 
ATOM   133  C CA  . VAL   A 1 83  ? 153.466 157.663 166.924 1.00 42.14  ? 75  VAL   A CA  1 
ATOM   134  C C   . VAL   A 1 83  ? 152.994 156.886 165.700 1.00 40.62  ? 75  VAL   A C   1 
ATOM   135  O O   . VAL   A 1 83  ? 151.870 157.080 165.219 1.00 41.71  ? 75  VAL   A O   1 
ATOM   136  C CB  . VAL   A 1 83  ? 154.431 158.800 166.540 1.00 40.30  ? 75  VAL   A CB  1 
ATOM   137  C CG1 . VAL   A 1 83  ? 153.846 159.634 165.415 1.00 37.87  ? 75  VAL   A CG1 1 
ATOM   138  C CG2 . VAL   A 1 83  ? 154.717 159.674 167.747 1.00 43.76  ? 75  VAL   A CG2 1 
ATOM   139  N N   . GLY   A 1 84  ? 153.834 155.985 165.188 1.00 36.51  ? 76  GLY   A N   1 
ATOM   140  C CA  . GLY   A 1 84  ? 153.468 155.240 163.994 1.00 33.40  ? 76  GLY   A CA  1 
ATOM   141  C C   . GLY   A 1 84  ? 152.299 154.299 164.211 1.00 37.18  ? 76  GLY   A C   1 
ATOM   142  O O   . GLY   A 1 84  ? 151.389 154.225 163.381 1.00 41.55  ? 76  GLY   A O   1 
ATOM   143  N N   . ASN   A 1 85  ? 152.304 153.564 165.326 1.00 35.48  ? 77  ASN   A N   1 
ATOM   144  C CA  . ASN   A 1 85  ? 151.200 152.654 165.604 1.00 32.09  ? 77  ASN   A CA  1 
ATOM   145  C C   . ASN   A 1 85  ? 149.910 153.417 165.877 1.00 38.15  ? 77  ASN   A C   1 
ATOM   146  O O   . ASN   A 1 85  ? 148.827 152.975 165.475 1.00 39.54  ? 77  ASN   A O   1 
ATOM   147  C CB  . ASN   A 1 85  ? 151.560 151.745 166.776 1.00 35.07  ? 77  ASN   A CB  1 
ATOM   148  C CG  . ASN   A 1 85  ? 152.770 150.880 166.486 1.00 44.78  ? 77  ASN   A CG  1 
ATOM   149  O OD1 . ASN   A 1 85  ? 152.753 150.055 165.574 1.00 47.77  ? 77  ASN   A OD1 1 
ATOM   150  N ND2 . ASN   A 1 85  ? 153.831 151.068 167.259 1.00 47.82  ? 77  ASN   A ND2 1 
ATOM   151  N N   . SER   A 1 86  ? 150.002 154.567 166.552 1.00 38.54  ? 78  SER   A N   1 
ATOM   152  C CA  . SER   A 1 86  ? 148.818 155.393 166.753 1.00 34.86  ? 78  SER   A CA  1 
ATOM   153  C C   . SER   A 1 86  ? 148.264 155.884 165.424 1.00 36.68  ? 78  SER   A C   1 
ATOM   154  O O   . SER   A 1 86  ? 147.045 155.891 165.217 1.00 41.45  ? 78  SER   A O   1 
ATOM   155  C CB  . SER   A 1 86  ? 149.154 156.571 167.665 1.00 39.16  ? 78  SER   A CB  1 
ATOM   156  O OG  . SER   A 1 86  ? 149.665 156.120 168.905 1.00 44.60  ? 78  SER   A OG  1 
ATOM   157  N N   . LEU   A 1 87  ? 149.145 156.294 164.508 1.00 36.21  ? 79  LEU   A N   1 
ATOM   158  C CA  . LEU   A 1 87  ? 148.696 156.712 163.185 1.00 37.34  ? 79  LEU   A CA  1 
ATOM   159  C C   . LEU   A 1 87  ? 148.025 155.564 162.443 1.00 40.45  ? 79  LEU   A C   1 
ATOM   160  O O   . LEU   A 1 87  ? 146.989 155.756 161.796 1.00 48.79  ? 79  LEU   A O   1 
ATOM   161  C CB  . LEU   A 1 87  ? 149.876 157.254 162.379 1.00 39.17  ? 79  LEU   A CB  1 
ATOM   162  C CG  . LEU   A 1 87  ? 149.575 157.825 160.992 1.00 46.27  ? 79  LEU   A CG  1 
ATOM   163  C CD1 . LEU   A 1 87  ? 148.307 158.659 161.006 1.00 49.82  ? 79  LEU   A CD1 1 
ATOM   164  C CD2 . LEU   A 1 87  ? 150.749 158.643 160.487 1.00 55.76  ? 79  LEU   A CD2 1 
ATOM   165  N N   . VAL   A 1 88  ? 148.602 154.364 162.523 1.00 37.16  ? 80  VAL   A N   1 
ATOM   166  C CA  . VAL   A 1 88  ? 148.021 153.208 161.841 1.00 34.61  ? 80  VAL   A CA  1 
ATOM   167  C C   . VAL   A 1 88  ? 146.627 152.915 162.385 1.00 39.94  ? 80  VAL   A C   1 
ATOM   168  O O   . VAL   A 1 88  ? 145.671 152.714 161.624 1.00 40.82  ? 80  VAL   A O   1 
ATOM   169  C CB  . VAL   A 1 88  ? 148.949 151.987 161.976 1.00 31.94  ? 80  VAL   A CB  1 
ATOM   170  C CG1 . VAL   A 1 88  ? 148.191 150.705 161.687 1.00 33.67  ? 80  VAL   A CG1 1 
ATOM   171  C CG2 . VAL   A 1 88  ? 150.142 152.123 161.051 1.00 32.92  ? 80  VAL   A CG2 1 
ATOM   172  N N   . MET   A 1 89  ? 146.491 152.890 163.714 1.00 38.15  ? 81  MET   A N   1 
ATOM   173  C CA  . MET   A 1 89  ? 145.192 152.608 164.318 1.00 34.44  ? 81  MET   A CA  1 
ATOM   174  C C   . MET   A 1 89  ? 144.169 153.679 163.963 1.00 37.38  ? 81  MET   A C   1 
ATOM   175  O O   . MET   A 1 89  ? 143.019 153.363 163.632 1.00 38.92  ? 81  MET   A O   1 
ATOM   176  C CB  . MET   A 1 89  ? 145.331 152.484 165.834 1.00 33.33  ? 81  MET   A CB  1 
ATOM   177  C CG  . MET   A 1 89  ? 146.189 151.321 166.289 1.00 32.22  ? 81  MET   A CG  1 
ATOM   178  S SD  . MET   A 1 89  ? 146.166 151.107 168.076 1.00 42.68  ? 81  MET   A SD  1 
ATOM   179  C CE  . MET   A 1 89  ? 147.489 152.207 168.563 1.00 40.94  ? 81  MET   A CE  1 
ATOM   180  N N   . PHE   A 1 90  ? 144.570 154.952 164.021 1.00 36.69  ? 82  PHE   A N   1 
ATOM   181  C CA  . PHE   A 1 90  ? 143.656 156.034 163.677 1.00 36.55  ? 82  PHE   A CA  1 
ATOM   182  C C   . PHE   A 1 90  ? 143.204 155.934 162.229 1.00 39.16  ? 82  PHE   A C   1 
ATOM   183  O O   . PHE   A 1 90  ? 142.021 156.118 161.925 1.00 41.68  ? 82  PHE   A O   1 
ATOM   184  C CB  . PHE   A 1 90  ? 144.327 157.384 163.934 1.00 39.89  ? 82  PHE   A CB  1 
ATOM   185  C CG  . PHE   A 1 90  ? 143.601 158.548 163.325 1.00 48.22  ? 82  PHE   A CG  1 
ATOM   186  C CD1 . PHE   A 1 90  ? 142.508 159.107 163.962 1.00 46.28  ? 82  PHE   A CD1 1 
ATOM   187  C CD2 . PHE   A 1 90  ? 144.011 159.086 162.118 1.00 44.73  ? 82  PHE   A CD2 1 
ATOM   188  C CE1 . PHE   A 1 90  ? 141.838 160.174 163.407 1.00 44.06  ? 82  PHE   A CE1 1 
ATOM   189  C CE2 . PHE   A 1 90  ? 143.342 160.152 161.559 1.00 42.82  ? 82  PHE   A CE2 1 
ATOM   190  C CZ  . PHE   A 1 90  ? 142.256 160.697 162.205 1.00 42.41  ? 82  PHE   A CZ  1 
ATOM   191  N N   . VAL   A 1 91  ? 144.135 155.647 161.319 1.00 42.34  ? 83  VAL   A N   1 
ATOM   192  C CA  . VAL   A 1 91  ? 143.797 155.571 159.905 1.00 43.79  ? 83  VAL   A CA  1 
ATOM   193  C C   . VAL   A 1 91  ? 142.855 154.403 159.640 1.00 43.33  ? 83  VAL   A C   1 
ATOM   194  O O   . VAL   A 1 91  ? 141.892 154.527 158.874 1.00 45.61  ? 83  VAL   A O   1 
ATOM   195  C CB  . VAL   A 1 91  ? 145.083 155.480 159.065 1.00 41.26  ? 83  VAL   A CB  1 
ATOM   196  C CG1 . VAL   A 1 91  ? 144.795 154.858 157.735 1.00 45.44  ? 83  VAL   A CG1 1 
ATOM   197  C CG2 . VAL   A 1 91  ? 145.692 156.857 158.881 1.00 43.23  ? 83  VAL   A CG2 1 
ATOM   198  N N   . ILE   A 1 92  ? 143.108 153.254 160.272 1.00 43.58  ? 84  ILE   A N   1 
ATOM   199  C CA  . ILE   A 1 92  ? 142.229 152.102 160.083 1.00 40.95  ? 84  ILE   A CA  1 
ATOM   200  C C   . ILE   A 1 92  ? 140.836 152.391 160.630 1.00 41.54  ? 84  ILE   A C   1 
ATOM   201  O O   . ILE   A 1 92  ? 139.825 152.057 160.000 1.00 43.31  ? 84  ILE   A O   1 
ATOM   202  C CB  . ILE   A 1 92  ? 142.842 150.844 160.726 1.00 39.07  ? 84  ILE   A CB  1 
ATOM   203  C CG1 . ILE   A 1 92  ? 144.088 150.406 159.958 1.00 36.26  ? 84  ILE   A CG1 1 
ATOM   204  C CG2 . ILE   A 1 92  ? 141.829 149.713 160.765 1.00 37.93  ? 84  ILE   A CG2 1 
ATOM   205  C CD1 . ILE   A 1 92  ? 144.921 149.387 160.690 1.00 36.08  ? 84  ILE   A CD1 1 
ATOM   206  N N   . ILE   A 1 93  ? 140.756 153.017 161.807 1.00 42.88  ? 85  ILE   A N   1 
ATOM   207  C CA  . ILE   A 1 93  ? 139.457 153.290 162.416 1.00 40.79  ? 85  ILE   A CA  1 
ATOM   208  C C   . ILE   A 1 93  ? 138.675 154.313 161.598 1.00 40.47  ? 85  ILE   A C   1 
ATOM   209  O O   . ILE   A 1 93  ? 137.466 154.164 161.386 1.00 45.80  ? 85  ILE   A O   1 
ATOM   210  C CB  . ILE   A 1 93  ? 139.640 153.753 163.872 1.00 32.59  ? 85  ILE   A CB  1 
ATOM   211  C CG1 . ILE   A 1 93  ? 139.930 152.561 164.780 1.00 28.56  ? 85  ILE   A CG1 1 
ATOM   212  C CG2 . ILE   A 1 93  ? 138.409 154.492 164.362 1.00 32.02  ? 85  ILE   A CG2 1 
ATOM   213  C CD1 . ILE   A 1 93  ? 140.157 152.943 166.221 1.00 34.62  ? 85  ILE   A CD1 1 
ATOM   214  N N   . ARG   A 1 94  ? 139.349 155.360 161.119 1.00 40.61  ? 86  ARG   A N   1 
ATOM   215  C CA  . ARG   A 1 94  ? 138.647 156.481 160.500 1.00 44.74  ? 86  ARG   A CA  1 
ATOM   216  C C   . ARG   A 1 94  ? 138.145 156.129 159.105 1.00 48.29  ? 86  ARG   A C   1 
ATOM   217  O O   . ARG   A 1 94  ? 136.954 156.266 158.808 1.00 51.11  ? 86  ARG   A O   1 
ATOM   218  C CB  . ARG   A 1 94  ? 139.565 157.703 160.449 1.00 51.42  ? 86  ARG   A CB  1 
ATOM   219  C CG  . ARG   A 1 94  ? 139.162 158.735 159.411 1.00 57.39  ? 86  ARG   A CG  1 
ATOM   220  C CD  . ARG   A 1 94  ? 139.584 160.131 159.825 1.00 62.80  ? 86  ARG   A CD  1 
ATOM   221  N NE  . ARG   A 1 94  ? 138.586 160.770 160.673 1.00 67.10  ? 86  ARG   A NE  1 
ATOM   222  C CZ  . ARG   A 1 94  ? 138.410 162.080 160.766 1.00 69.81  ? 86  ARG   A CZ  1 
ATOM   223  N NH1 . ARG   A 1 94  ? 139.153 162.928 160.073 1.00 67.46  ? 86  ARG   A NH1 1 
ATOM   224  N NH2 . ARG   A 1 94  ? 137.466 162.552 161.574 1.00 73.25  ? 86  ARG   A NH2 1 
ATOM   225  N N   . TYR   A 1 95  ? 139.041 155.676 158.232 1.00 52.83  ? 87  TYR   A N   1 
ATOM   226  C CA  . TYR   A 1 95  ? 138.707 155.490 156.826 1.00 51.01  ? 87  TYR   A CA  1 
ATOM   227  C C   . TYR   A 1 95  ? 137.930 154.195 156.634 1.00 55.31  ? 87  TYR   A C   1 
ATOM   228  O O   . TYR   A 1 95  ? 138.407 153.116 156.998 1.00 58.91  ? 87  TYR   A O   1 
ATOM   229  C CB  . TYR   A 1 95  ? 139.973 155.485 155.972 1.00 55.77  ? 87  TYR   A CB  1 
ATOM   230  C CG  . TYR   A 1 95  ? 140.712 156.804 155.948 1.00 61.25  ? 87  TYR   A CG  1 
ATOM   231  C CD1 . TYR   A 1 95  ? 141.492 157.208 157.023 1.00 59.63  ? 87  TYR   A CD1 1 
ATOM   232  C CD2 . TYR   A 1 95  ? 140.630 157.646 154.849 1.00 64.77  ? 87  TYR   A CD2 1 
ATOM   233  C CE1 . TYR   A 1 95  ? 142.168 158.411 157.004 1.00 63.65  ? 87  TYR   A CE1 1 
ATOM   234  C CE2 . TYR   A 1 95  ? 141.303 158.851 154.820 1.00 71.45  ? 87  TYR   A CE2 1 
ATOM   235  C CZ  . TYR   A 1 95  ? 142.070 159.229 155.900 1.00 75.02  ? 87  TYR   A CZ  1 
ATOM   236  O OH  . TYR   A 1 95  ? 142.743 160.429 155.879 1.00 81.73  ? 87  TYR   A OH  1 
ATOM   237  N N   . THR   A 1 96  ? 136.730 154.305 156.059 1.00 59.67  ? 88  THR   A N   1 
ATOM   238  C CA  . THR   A 1 96  ? 135.962 153.123 155.688 1.00 62.93  ? 88  THR   A CA  1 
ATOM   239  C C   . THR   A 1 96  ? 136.609 152.373 154.531 1.00 61.10  ? 88  THR   A C   1 
ATOM   240  O O   . THR   A 1 96  ? 136.356 151.176 154.357 1.00 57.13  ? 88  THR   A O   1 
ATOM   241  C CB  . THR   A 1 96  ? 134.529 153.530 155.327 1.00 64.93  ? 88  THR   A CB  1 
ATOM   242  O OG1 . THR   A 1 96  ? 133.991 154.349 156.372 1.00 62.28  ? 88  THR   A OG1 1 
ATOM   243  C CG2 . THR   A 1 96  ? 133.638 152.307 155.157 1.00 64.35  ? 88  THR   A CG2 1 
ATOM   244  N N   . LYS   A 1 97  ? 137.458 153.049 153.756 1.00 61.95  ? 89  LYS   A N   1 
ATOM   245  C CA  . LYS   A 1 97  ? 138.128 152.405 152.633 1.00 65.44  ? 89  LYS   A CA  1 
ATOM   246  C C   . LYS   A 1 97  ? 139.024 151.263 153.097 1.00 63.52  ? 89  LYS   A C   1 
ATOM   247  O O   . LYS   A 1 97  ? 139.072 150.205 152.459 1.00 64.73  ? 89  LYS   A O   1 
ATOM   248  C CB  . LYS   A 1 97  ? 138.939 153.441 151.853 1.00 66.55  ? 89  LYS   A CB  1 
ATOM   249  C CG  . LYS   A 1 97  ? 140.088 152.867 151.045 1.00 67.36  ? 89  LYS   A CG  1 
ATOM   250  C CD  . LYS   A 1 97  ? 140.961 153.972 150.477 1.00 73.02  ? 89  LYS   A CD  1 
ATOM   251  C CE  . LYS   A 1 97  ? 141.660 154.743 151.583 1.00 72.49  ? 89  LYS   A CE  1 
ATOM   252  N NZ  . LYS   A 1 97  ? 142.576 155.786 151.045 1.00 82.18  ? 89  LYS   A NZ  1 
ATOM   253  N N   . MET   A 1 98  ? 139.734 151.451 154.209 1.00 60.09  ? 90  MET   A N   1 
ATOM   254  C CA  . MET   A 1 98  ? 140.720 150.483 154.668 1.00 58.34  ? 90  MET   A CA  1 
ATOM   255  C C   . MET   A 1 98  ? 140.215 149.639 155.834 1.00 56.91  ? 90  MET   A C   1 
ATOM   256  O O   . MET   A 1 98  ? 140.993 149.263 156.713 1.00 53.69  ? 90  MET   A O   1 
ATOM   257  C CB  . MET   A 1 98  ? 142.021 151.179 155.056 1.00 54.44  ? 90  MET   A CB  1 
ATOM   258  C CG  . MET   A 1 98  ? 142.537 152.164 154.033 1.00 62.91  ? 90  MET   A CG  1 
ATOM   259  S SD  . MET   A 1 98  ? 144.331 152.116 153.954 1.00 76.80  ? 90  MET   A SD  1 
ATOM   260  C CE  . MET   A 1 98  ? 144.735 152.104 155.688 1.00 52.67  ? 90  MET   A CE  1 
ATOM   261  N N   . LYS   A 1 99  ? 138.919 149.330 155.860 1.00 57.71  ? 91  LYS   A N   1 
ATOM   262  C CA  . LYS   A 1 99  ? 138.364 148.444 156.883 1.00 52.92  ? 91  LYS   A CA  1 
ATOM   263  C C   . LYS   A 1 99  ? 138.232 147.044 156.291 1.00 57.78  ? 91  LYS   A C   1 
ATOM   264  O O   . LYS   A 1 99  ? 137.150 146.580 155.927 1.00 62.50  ? 91  LYS   A O   1 
ATOM   265  C CB  . LYS   A 1 99  ? 137.033 148.978 157.395 1.00 57.01  ? 91  LYS   A CB  1 
ATOM   266  C CG  . LYS   A 1 99  ? 137.175 150.160 158.338 1.00 54.22  ? 91  LYS   A CG  1 
ATOM   267  C CD  . LYS   A 1 99  ? 135.831 150.604 158.878 1.00 55.46  ? 91  LYS   A CD  1 
ATOM   268  C CE  . LYS   A 1 99  ? 135.977 151.822 159.767 1.00 51.22  ? 91  LYS   A CE  1 
ATOM   269  N NZ  . LYS   A 1 99  ? 134.660 152.292 160.272 1.00 63.68  ? 91  LYS   A NZ  1 
ATOM   270  N N   . THR   A 1 100 ? 139.371 146.363 156.196 1.00 54.40  ? 92  THR   A N   1 
ATOM   271  C CA  . THR   A 1 100 ? 139.452 145.006 155.681 1.00 49.15  ? 92  THR   A CA  1 
ATOM   272  C C   . THR   A 1 100 ? 139.991 144.082 156.765 1.00 48.90  ? 92  THR   A C   1 
ATOM   273  O O   . THR   A 1 100 ? 140.578 144.531 157.753 1.00 51.75  ? 92  THR   A O   1 
ATOM   274  C CB  . THR   A 1 100 ? 140.343 144.934 154.433 1.00 48.03  ? 92  THR   A CB  1 
ATOM   275  O OG1 . THR   A 1 100 ? 141.699 145.213 154.795 1.00 50.12  ? 92  THR   A OG1 1 
ATOM   276  C CG2 . THR   A 1 100 ? 139.890 145.950 153.401 1.00 45.09  ? 92  THR   A CG2 1 
ATOM   277  N N   . ALA   A 1 101 ? 139.785 142.776 156.570 1.00 43.12  ? 93  ALA   A N   1 
ATOM   278  C CA  . ALA   A 1 101 ? 140.139 141.803 157.602 1.00 41.34  ? 93  ALA   A CA  1 
ATOM   279  C C   . ALA   A 1 101 ? 141.632 141.831 157.905 1.00 44.17  ? 93  ALA   A C   1 
ATOM   280  O O   . ALA   A 1 101 ? 142.042 141.860 159.074 1.00 50.95  ? 93  ALA   A O   1 
ATOM   281  C CB  . ALA   A 1 101 ? 139.702 140.404 157.171 1.00 48.25  ? 93  ALA   A CB  1 
ATOM   282  N N   . THR   A 1 102 ? 142.464 141.828 156.861 1.00 42.21  ? 94  THR   A N   1 
ATOM   283  C CA  . THR   A 1 102 ? 143.904 141.928 157.074 1.00 40.38  ? 94  THR   A CA  1 
ATOM   284  C C   . THR   A 1 102 ? 144.259 143.240 157.759 1.00 40.54  ? 94  THR   A C   1 
ATOM   285  O O   . THR   A 1 102 ? 145.163 143.286 158.601 1.00 45.14  ? 94  THR   A O   1 
ATOM   286  C CB  . THR   A 1 102 ? 144.648 141.790 155.745 1.00 40.06  ? 94  THR   A CB  1 
ATOM   287  O OG1 . THR   A 1 102 ? 146.022 142.154 155.924 1.00 39.84  ? 94  THR   A OG1 1 
ATOM   288  C CG2 . THR   A 1 102 ? 144.022 142.674 154.676 1.00 41.32  ? 94  THR   A CG2 1 
ATOM   289  N N   . ASN   A 1 103 ? 143.536 144.313 157.435 1.00 38.18  ? 95  ASN   A N   1 
ATOM   290  C CA  . ASN   A 1 103 ? 143.761 145.579 158.119 1.00 33.76  ? 95  ASN   A CA  1 
ATOM   291  C C   . ASN   A 1 103 ? 143.298 145.527 159.568 1.00 36.01  ? 95  ASN   A C   1 
ATOM   292  O O   . ASN   A 1 103 ? 143.880 146.201 160.420 1.00 40.76  ? 95  ASN   A O   1 
ATOM   293  C CB  . ASN   A 1 103 ? 143.068 146.713 157.369 1.00 36.20  ? 95  ASN   A CB  1 
ATOM   294  C CG  . ASN   A 1 103 ? 143.925 147.276 156.257 1.00 45.12  ? 95  ASN   A CG  1 
ATOM   295  O OD1 . ASN   A 1 103 ? 144.990 146.743 155.950 1.00 45.39  ? 95  ASN   A OD1 1 
ATOM   296  N ND2 . ASN   A 1 103 ? 143.467 148.357 155.647 1.00 54.32  ? 95  ASN   A ND2 1 
ATOM   297  N N   . ILE   A 1 104 ? 142.271 144.733 159.877 1.00 36.28  ? 96  ILE   A N   1 
ATOM   298  C CA  . ILE   A 1 104 ? 141.866 144.563 161.271 1.00 36.40  ? 96  ILE   A CA  1 
ATOM   299  C C   . ILE   A 1 104 ? 142.949 143.830 162.057 1.00 37.85  ? 96  ILE   A C   1 
ATOM   300  O O   . ILE   A 1 104 ? 143.271 144.195 163.198 1.00 43.43  ? 96  ILE   A O   1 
ATOM   301  C CB  . ILE   A 1 104 ? 140.512 143.836 161.350 1.00 37.39  ? 96  ILE   A CB  1 
ATOM   302  C CG1 . ILE   A 1 104 ? 139.421 144.664 160.670 1.00 41.27  ? 96  ILE   A CG1 1 
ATOM   303  C CG2 . ILE   A 1 104 ? 140.131 143.568 162.790 1.00 41.66  ? 96  ILE   A CG2 1 
ATOM   304  C CD1 . ILE   A 1 104 ? 139.323 146.082 161.178 1.00 44.74  ? 96  ILE   A CD1 1 
ATOM   305  N N   . TYR   A 1 105 ? 143.530 142.786 161.464 1.00 33.62  ? 97  TYR   A N   1 
ATOM   306  C CA  . TYR   A 1 105 ? 144.639 142.103 162.125 1.00 32.79  ? 97  TYR   A CA  1 
ATOM   307  C C   . TYR   A 1 105 ? 145.836 143.034 162.293 1.00 34.19  ? 97  TYR   A C   1 
ATOM   308  O O   . TYR   A 1 105 ? 146.524 143.001 163.322 1.00 34.12  ? 97  TYR   A O   1 
ATOM   309  C CB  . TYR   A 1 105 ? 145.035 140.860 161.336 1.00 35.76  ? 97  TYR   A CB  1 
ATOM   310  C CG  . TYR   A 1 105 ? 143.938 139.833 161.184 1.00 35.36  ? 97  TYR   A CG  1 
ATOM   311  C CD1 . TYR   A 1 105 ? 143.254 139.349 162.288 1.00 37.64  ? 97  TYR   A CD1 1 
ATOM   312  C CD2 . TYR   A 1 105 ? 143.597 139.337 159.935 1.00 35.86  ? 97  TYR   A CD2 1 
ATOM   313  C CE1 . TYR   A 1 105 ? 142.254 138.410 162.150 1.00 39.18  ? 97  TYR   A CE1 1 
ATOM   314  C CE2 . TYR   A 1 105 ? 142.599 138.399 159.788 1.00 37.67  ? 97  TYR   A CE2 1 
ATOM   315  C CZ  . TYR   A 1 105 ? 141.931 137.938 160.898 1.00 41.48  ? 97  TYR   A CZ  1 
ATOM   316  O OH  . TYR   A 1 105 ? 140.935 137.001 160.754 1.00 49.35  ? 97  TYR   A OH  1 
ATOM   317  N N   . ILE   A 1 106 ? 146.103 143.868 161.286 1.00 35.29  ? 98  ILE   A N   1 
ATOM   318  C CA  . ILE   A 1 106 ? 147.168 144.861 161.393 1.00 31.28  ? 98  ILE   A CA  1 
ATOM   319  C C   . ILE   A 1 106 ? 146.866 145.848 162.514 1.00 33.68  ? 98  ILE   A C   1 
ATOM   320  O O   . ILE   A 1 106 ? 147.770 146.297 163.227 1.00 35.51  ? 98  ILE   A O   1 
ATOM   321  C CB  . ILE   A 1 106 ? 147.364 145.570 160.039 1.00 34.65  ? 98  ILE   A CB  1 
ATOM   322  C CG1 . ILE   A 1 106 ? 148.148 144.675 159.081 1.00 34.44  ? 98  ILE   A CG1 1 
ATOM   323  C CG2 . ILE   A 1 106 ? 148.066 146.903 160.214 1.00 39.97  ? 98  ILE   A CG2 1 
ATOM   324  C CD1 . ILE   A 1 106 ? 148.166 145.179 157.661 1.00 40.51  ? 98  ILE   A CD1 1 
ATOM   325  N N   . PHE   A 1 107 ? 145.591 146.203 162.683 1.00 36.10  ? 99  PHE   A N   1 
ATOM   326  C CA  . PHE   A 1 107 ? 145.189 147.058 163.795 1.00 35.12  ? 99  PHE   A CA  1 
ATOM   327  C C   . PHE   A 1 107 ? 145.505 146.401 165.130 1.00 35.28  ? 99  PHE   A C   1 
ATOM   328  O O   . PHE   A 1 107 ? 145.986 147.062 166.055 1.00 36.41  ? 99  PHE   A O   1 
ATOM   329  C CB  . PHE   A 1 107 ? 143.695 147.378 163.695 1.00 32.60  ? 99  PHE   A CB  1 
ATOM   330  C CG  . PHE   A 1 107 ? 143.166 148.208 164.837 1.00 38.89  ? 99  PHE   A CG  1 
ATOM   331  C CD1 . PHE   A 1 107 ? 142.770 147.614 166.026 1.00 38.39  ? 99  PHE   A CD1 1 
ATOM   332  C CD2 . PHE   A 1 107 ? 143.056 149.581 164.716 1.00 39.93  ? 99  PHE   A CD2 1 
ATOM   333  C CE1 . PHE   A 1 107 ? 142.289 148.375 167.071 1.00 32.20  ? 99  PHE   A CE1 1 
ATOM   334  C CE2 . PHE   A 1 107 ? 142.571 150.343 165.758 1.00 34.96  ? 99  PHE   A CE2 1 
ATOM   335  C CZ  . PHE   A 1 107 ? 142.187 149.740 166.935 1.00 33.35  ? 99  PHE   A CZ  1 
ATOM   336  N N   . ASN   A 1 108 ? 145.221 145.105 165.253 1.00 34.20  ? 100 ASN   A N   1 
ATOM   337  C CA  . ASN   A 1 108 ? 145.549 144.398 166.491 1.00 32.49  ? 100 ASN   A CA  1 
ATOM   338  C C   . ASN   A 1 108 ? 147.054 144.391 166.740 1.00 32.71  ? 100 ASN   A C   1 
ATOM   339  O O   . ASN   A 1 108 ? 147.512 144.596 167.874 1.00 37.07  ? 100 ASN   A O   1 
ATOM   340  C CB  . ASN   A 1 108 ? 145.010 142.971 166.440 1.00 33.76  ? 100 ASN   A CB  1 
ATOM   341  C CG  . ASN   A 1 108 ? 144.825 142.372 167.814 1.00 42.01  ? 100 ASN   A CG  1 
ATOM   342  O OD1 . ASN   A 1 108 ? 144.287 143.015 168.713 1.00 47.06  ? 100 ASN   A OD1 1 
ATOM   343  N ND2 . ASN   A 1 108 ? 145.270 141.134 167.987 1.00 44.53  ? 100 ASN   A ND2 1 
ATOM   344  N N   . LEU   A 1 109 ? 147.837 144.155 165.686 1.00 35.60  ? 101 LEU   A N   1 
ATOM   345  C CA  . LEU   A 1 109 ? 149.292 144.177 165.812 1.00 35.81  ? 101 LEU   A CA  1 
ATOM   346  C C   . LEU   A 1 109 ? 149.788 145.545 166.265 1.00 35.87  ? 101 LEU   A C   1 
ATOM   347  O O   . LEU   A 1 109 ? 150.648 145.645 167.150 1.00 38.54  ? 101 LEU   A O   1 
ATOM   348  C CB  . LEU   A 1 109 ? 149.930 143.796 164.477 1.00 36.53  ? 101 LEU   A CB  1 
ATOM   349  C CG  . LEU   A 1 109 ? 151.109 142.828 164.484 1.00 37.21  ? 101 LEU   A CG  1 
ATOM   350  C CD1 . LEU   A 1 109 ? 150.707 141.504 165.098 1.00 35.70  ? 101 LEU   A CD1 1 
ATOM   351  C CD2 . LEU   A 1 109 ? 151.617 142.630 163.069 1.00 39.88  ? 101 LEU   A CD2 1 
ATOM   352  N N   . ALA   A 1 110 ? 149.252 146.611 165.668 1.00 35.82  ? 102 ALA   A N   1 
ATOM   353  C CA  . ALA   A 1 110 ? 149.645 147.963 166.045 1.00 34.66  ? 102 ALA   A CA  1 
ATOM   354  C C   . ALA   A 1 110 ? 149.228 148.283 167.473 1.00 35.23  ? 102 ALA   A C   1 
ATOM   355  O O   . ALA   A 1 110 ? 149.952 148.977 168.192 1.00 39.93  ? 102 ALA   A O   1 
ATOM   356  C CB  . ALA   A 1 110 ? 149.043 148.974 165.071 1.00 35.53  ? 102 ALA   A CB  1 
ATOM   357  N N   . LEU   A 1 111 ? 148.060 147.798 167.896 1.00 35.24  ? 103 LEU   A N   1 
ATOM   358  C CA  . LEU   A 1 111 ? 147.624 148.001 169.274 1.00 36.65  ? 103 LEU   A CA  1 
ATOM   359  C C   . LEU   A 1 111 ? 148.592 147.351 170.252 1.00 38.15  ? 103 LEU   A C   1 
ATOM   360  O O   . LEU   A 1 111 ? 148.992 147.964 171.250 1.00 42.09  ? 103 LEU   A O   1 
ATOM   361  C CB  . LEU   A 1 111 ? 146.213 147.443 169.460 1.00 35.62  ? 103 LEU   A CB  1 
ATOM   362  C CG  . LEU   A 1 111 ? 145.672 147.360 170.887 1.00 34.81  ? 103 LEU   A CG  1 
ATOM   363  C CD1 . LEU   A 1 111 ? 145.598 148.740 171.515 1.00 37.16  ? 103 LEU   A CD1 1 
ATOM   364  C CD2 . LEU   A 1 111 ? 144.310 146.693 170.898 1.00 35.40  ? 103 LEU   A CD2 1 
ATOM   365  N N   . ALA   A 1 112 ? 148.991 146.109 169.972 1.00 38.27  ? 104 ALA   A N   1 
ATOM   366  C CA  . ALA   A 1 112 ? 149.952 145.437 170.843 1.00 32.32  ? 104 ALA   A CA  1 
ATOM   367  C C   . ALA   A 1 112 ? 151.288 146.173 170.864 1.00 35.51  ? 104 ALA   A C   1 
ATOM   368  O O   . ALA   A 1 112 ? 151.888 146.360 171.931 1.00 39.62  ? 104 ALA   A O   1 
ATOM   369  C CB  . ALA   A 1 112 ? 150.143 143.989 170.398 1.00 38.16  ? 104 ALA   A CB  1 
ATOM   370  N N   . ASP   A 1 113 ? 151.764 146.606 169.694 1.00 37.69  ? 105 ASP   A N   1 
ATOM   371  C CA  . ASP   A 1 113 ? 153.049 147.297 169.625 1.00 36.11  ? 105 ASP   A CA  1 
ATOM   372  C C   . ASP   A 1 113 ? 153.009 148.631 170.362 1.00 38.68  ? 105 ASP   A C   1 
ATOM   373  O O   . ASP   A 1 113 ? 153.985 149.012 171.018 1.00 42.77  ? 105 ASP   A O   1 
ATOM   374  C CB  . ASP   A 1 113 ? 153.457 147.500 168.168 1.00 42.85  ? 105 ASP   A CB  1 
ATOM   375  C CG  . ASP   A 1 113 ? 153.872 146.207 167.495 1.00 56.13  ? 105 ASP   A CG  1 
ATOM   376  O OD1 . ASP   A 1 113 ? 154.051 145.197 168.206 1.00 60.20  ? 105 ASP   A OD1 1 
ATOM   377  O OD2 . ASP   A 1 113 ? 154.020 146.202 166.255 1.00 57.50  ? 105 ASP   A OD2 1 
ATOM   378  N N   . ALA   A 1 114 ? 151.899 149.363 170.255 1.00 41.02  ? 106 ALA   A N   1 
ATOM   379  C CA  . ALA   A 1 114 ? 151.775 150.629 170.967 1.00 38.64  ? 106 ALA   A CA  1 
ATOM   380  C C   . ALA   A 1 114 ? 151.671 150.409 172.469 1.00 38.36  ? 106 ALA   A C   1 
ATOM   381  O O   . ALA   A 1 114 ? 152.199 151.204 173.255 1.00 37.77  ? 106 ALA   A O   1 
ATOM   382  C CB  . ALA   A 1 114 ? 150.565 151.405 170.452 1.00 34.69  ? 106 ALA   A CB  1 
ATOM   383  N N   . LEU   A 1 115 ? 150.987 149.342 172.889 1.00 38.75  ? 107 LEU   A N   1 
ATOM   384  C CA  . LEU   A 1 115 ? 150.910 149.036 174.313 1.00 35.49  ? 107 LEU   A CA  1 
ATOM   385  C C   . LEU   A 1 115 ? 152.281 148.697 174.881 1.00 38.94  ? 107 LEU   A C   1 
ATOM   386  O O   . LEU   A 1 115 ? 152.632 149.141 175.979 1.00 43.14  ? 107 LEU   A O   1 
ATOM   387  C CB  . LEU   A 1 115 ? 149.932 147.888 174.553 1.00 38.92  ? 107 LEU   A CB  1 
ATOM   388  C CG  . LEU   A 1 115 ? 148.468 148.284 174.743 1.00 33.26  ? 107 LEU   A CG  1 
ATOM   389  C CD1 . LEU   A 1 115 ? 147.590 147.048 174.817 1.00 31.82  ? 107 LEU   A CD1 1 
ATOM   390  C CD2 . LEU   A 1 115 ? 148.307 149.137 175.987 1.00 30.19  ? 107 LEU   A CD2 1 
ATOM   391  N N   . VAL   A 1 116 ? 153.074 147.907 174.150 1.00 42.83  ? 108 VAL   A N   1 
ATOM   392  C CA  . VAL   A 1 116 ? 154.402 147.559 174.645 1.00 43.46  ? 108 VAL   A CA  1 
ATOM   393  C C   . VAL   A 1 116 ? 155.356 148.745 174.586 1.00 40.60  ? 108 VAL   A C   1 
ATOM   394  O O   . VAL   A 1 116 ? 156.389 148.739 175.263 1.00 43.49  ? 108 VAL   A O   1 
ATOM   395  C CB  . VAL   A 1 116 ? 154.981 146.360 173.870 1.00 43.86  ? 108 VAL   A CB  1 
ATOM   396  C CG1 . VAL   A 1 116 ? 155.696 146.824 172.616 1.00 39.18  ? 108 VAL   A CG1 1 
ATOM   397  C CG2 . VAL   A 1 116 ? 155.920 145.561 174.756 1.00 47.63  ? 108 VAL   A CG2 1 
ATOM   398  N N   . THR   A 1 117 ? 155.035 149.768 173.792 1.00 46.65  ? 109 THR   A N   1 
ATOM   399  C CA  . THR   A 1 117 ? 155.927 150.915 173.656 1.00 45.84  ? 109 THR   A CA  1 
ATOM   400  C C   . THR   A 1 117 ? 155.870 151.814 174.886 1.00 47.53  ? 109 THR   A C   1 
ATOM   401  O O   . THR   A 1 117 ? 156.890 152.381 175.297 1.00 48.80  ? 109 THR   A O   1 
ATOM   402  C CB  . THR   A 1 117 ? 155.571 151.695 172.388 1.00 45.41  ? 109 THR   A CB  1 
ATOM   403  O OG1 . THR   A 1 117 ? 156.138 151.039 171.248 1.00 45.25  ? 109 THR   A OG1 1 
ATOM   404  C CG2 . THR   A 1 117 ? 156.093 153.115 172.453 1.00 46.45  ? 109 THR   A CG2 1 
ATOM   405  N N   . THR   A 1 118 ? 154.691 151.935 175.502 1.00 48.36  ? 110 THR   A N   1 
ATOM   406  C CA  . THR   A 1 118 ? 154.530 152.823 176.650 1.00 46.65  ? 110 THR   A CA  1 
ATOM   407  C C   . THR   A 1 118 ? 155.417 152.408 177.820 1.00 46.88  ? 110 THR   A C   1 
ATOM   408  O O   . THR   A 1 118 ? 155.775 153.245 178.655 1.00 49.26  ? 110 THR   A O   1 
ATOM   409  C CB  . THR   A 1 118 ? 153.061 152.854 177.076 1.00 41.46  ? 110 THR   A CB  1 
ATOM   410  O OG1 . THR   A 1 118 ? 152.238 153.090 175.928 1.00 42.01  ? 110 THR   A OG1 1 
ATOM   411  C CG2 . THR   A 1 118 ? 152.814 153.961 178.086 1.00 49.82  ? 110 THR   A CG2 1 
ATOM   412  N N   . THR   A 1 119 ? 155.797 151.135 177.889 1.00 43.40  ? 111 THR   A N   1 
ATOM   413  C CA  . THR   A 1 119 ? 156.624 150.625 178.973 1.00 39.75  ? 111 THR   A CA  1 
ATOM   414  C C   . THR   A 1 119 ? 158.116 150.756 178.694 1.00 41.86  ? 111 THR   A C   1 
ATOM   415  O O   . THR   A 1 119 ? 158.926 150.279 179.494 1.00 42.66  ? 111 THR   A O   1 
ATOM   416  C CB  . THR   A 1 119 ? 156.279 149.160 179.256 1.00 43.80  ? 111 THR   A CB  1 
ATOM   417  O OG1 . THR   A 1 119 ? 156.791 148.334 178.204 1.00 49.87  ? 111 THR   A OG1 1 
ATOM   418  C CG2 . THR   A 1 119 ? 154.775 148.978 179.347 1.00 43.40  ? 111 THR   A CG2 1 
ATOM   419  N N   . MET   A 1 120 ? 158.494 151.379 177.579 1.00 42.20  ? 112 MET   A N   1 
ATOM   420  C CA  . MET   A 1 120 ? 159.912 151.538 177.265 1.00 42.68  ? 112 MET   A CA  1 
ATOM   421  C C   . MET   A 1 120 ? 160.686 152.348 178.301 1.00 42.25  ? 112 MET   A C   1 
ATOM   422  O O   . MET   A 1 120 ? 161.802 151.928 178.653 1.00 42.98  ? 112 MET   A O   1 
ATOM   423  C CB  . MET   A 1 120 ? 160.067 152.150 175.867 1.00 45.81  ? 112 MET   A CB  1 
ATOM   424  C CG  . MET   A 1 120 ? 160.005 151.138 174.735 1.00 50.31  ? 112 MET   A CG  1 
ATOM   425  S SD  . MET   A 1 120 ? 160.964 149.648 175.063 1.00 60.56  ? 112 MET   A SD  1 
ATOM   426  C CE  . MET   A 1 120 ? 159.661 148.472 175.409 1.00 51.36  ? 112 MET   A CE  1 
ATOM   427  N N   . PRO   A 1 121 ? 160.201 153.491 178.804 1.00 40.34  ? 113 PRO   A N   1 
ATOM   428  C CA  . PRO   A 1 121 ? 160.957 154.181 179.863 1.00 38.05  ? 113 PRO   A CA  1 
ATOM   429  C C   . PRO   A 1 121 ? 161.142 153.345 181.115 1.00 40.27  ? 113 PRO   A C   1 
ATOM   430  O O   . PRO   A 1 121 ? 162.158 153.495 181.804 1.00 40.68  ? 113 PRO   A O   1 
ATOM   431  C CB  . PRO   A 1 121 ? 160.117 155.437 180.137 1.00 33.73  ? 113 PRO   A CB  1 
ATOM   432  C CG  . PRO   A 1 121 ? 158.774 155.134 179.586 1.00 37.48  ? 113 PRO   A CG  1 
ATOM   433  C CD  . PRO   A 1 121 ? 159.021 154.273 178.398 1.00 41.75  ? 113 PRO   A CD  1 
ATOM   434  N N   . PHE   A 1 122 ? 160.187 152.469 181.437 1.00 39.53  ? 114 PHE   A N   1 
ATOM   435  C CA  . PHE   A 1 122 ? 160.352 151.585 182.585 1.00 34.61  ? 114 PHE   A CA  1 
ATOM   436  C C   . PHE   A 1 122 ? 161.341 150.466 182.293 1.00 42.23  ? 114 PHE   A C   1 
ATOM   437  O O   . PHE   A 1 122 ? 162.062 150.026 183.195 1.00 45.51  ? 114 PHE   A O   1 
ATOM   438  C CB  . PHE   A 1 122 ? 159.000 151.005 183.000 1.00 35.12  ? 114 PHE   A CB  1 
ATOM   439  C CG  . PHE   A 1 122 ? 157.940 152.043 183.224 1.00 36.00  ? 114 PHE   A CG  1 
ATOM   440  C CD1 . PHE   A 1 122 ? 157.824 152.679 184.447 1.00 35.91  ? 114 PHE   A CD1 1 
ATOM   441  C CD2 . PHE   A 1 122 ? 157.061 152.385 182.213 1.00 39.34  ? 114 PHE   A CD2 1 
ATOM   442  C CE1 . PHE   A 1 122 ? 156.852 153.635 184.656 1.00 38.43  ? 114 PHE   A CE1 1 
ATOM   443  C CE2 . PHE   A 1 122 ? 156.088 153.340 182.416 1.00 39.04  ? 114 PHE   A CE2 1 
ATOM   444  C CZ  . PHE   A 1 122 ? 155.983 153.965 183.639 1.00 39.94  ? 114 PHE   A CZ  1 
ATOM   445  N N   . GLN   A 1 123 ? 161.384 149.989 181.047 1.00 49.05  ? 115 GLN   A N   1 
ATOM   446  C CA  . GLN   A 1 123 ? 162.331 148.940 180.683 1.00 47.32  ? 115 GLN   A CA  1 
ATOM   447  C C   . GLN   A 1 123 ? 163.770 149.430 180.782 1.00 50.04  ? 115 GLN   A C   1 
ATOM   448  O O   . GLN   A 1 123 ? 164.651 148.699 181.246 1.00 59.20  ? 115 GLN   A O   1 
ATOM   449  C CB  . GLN   A 1 123 ? 162.036 148.437 179.270 1.00 50.97  ? 115 GLN   A CB  1 
ATOM   450  C CG  . GLN   A 1 123 ? 160.817 147.541 179.166 1.00 54.23  ? 115 GLN   A CG  1 
ATOM   451  C CD  . GLN   A 1 123 ? 160.913 146.327 180.063 1.00 59.64  ? 115 GLN   A CD  1 
ATOM   452  O OE1 . GLN   A 1 123 ? 160.027 146.068 180.871 1.00 53.15  ? 115 GLN   A OE1 1 
ATOM   453  N NE2 . GLN   A 1 123 ? 161.992 145.570 179.919 1.00 69.26  ? 115 GLN   A NE2 1 
ATOM   454  N N   . SER   A 1 124 ? 164.028 150.664 180.348 1.00 48.43  ? 116 SER   A N   1 
ATOM   455  C CA  . SER   A 1 124 ? 165.389 151.184 180.307 1.00 48.42  ? 116 SER   A CA  1 
ATOM   456  C C   . SER   A 1 124 ? 165.973 151.447 181.687 1.00 50.84  ? 116 SER   A C   1 
ATOM   457  O O   . SER   A 1 124 ? 167.186 151.651 181.793 1.00 58.64  ? 116 SER   A O   1 
ATOM   458  C CB  . SER   A 1 124 ? 165.431 152.468 179.478 1.00 50.26  ? 116 SER   A CB  1 
ATOM   459  O OG  . SER   A 1 124 ? 164.489 153.412 179.954 1.00 53.55  ? 116 SER   A OG  1 
ATOM   460  N N   . ALA   A 1 125 ? 165.152 151.457 182.739 1.00 47.43  ? 117 ALA   A N   1 
ATOM   461  C CA  . ALA   A 1 125 ? 165.679 151.691 184.079 1.00 47.49  ? 117 ALA   A CA  1 
ATOM   462  C C   . ALA   A 1 125 ? 166.493 150.503 184.572 1.00 54.46  ? 117 ALA   A C   1 
ATOM   463  O O   . ALA   A 1 125 ? 167.540 150.682 185.204 1.00 58.32  ? 117 ALA   A O   1 
ATOM   464  C CB  . ALA   A 1 125 ? 164.540 151.998 185.046 1.00 46.19  ? 117 ALA   A CB  1 
ATOM   465  N N   . VAL   A 1 126 ? 166.030 149.281 184.298 1.00 55.14  ? 118 VAL   A N   1 
ATOM   466  C CA  . VAL   A 1 126 ? 166.760 148.091 184.719 1.00 60.73  ? 118 VAL   A CA  1 
ATOM   467  C C   . VAL   A 1 126 ? 168.056 147.904 183.949 1.00 62.44  ? 118 VAL   A C   1 
ATOM   468  O O   . VAL   A 1 126 ? 168.849 147.021 184.291 1.00 67.16  ? 118 VAL   A O   1 
ATOM   469  C CB  . VAL   A 1 126 ? 165.886 146.828 184.577 1.00 66.04  ? 118 VAL   A CB  1 
ATOM   470  C CG1 . VAL   A 1 126 ? 164.485 147.094 185.098 1.00 58.24  ? 118 VAL   A CG1 1 
ATOM   471  C CG2 . VAL   A 1 126 ? 165.852 146.359 183.135 1.00 62.19  ? 118 VAL   A CG2 1 
ATOM   472  N N   . TYR   A 1 127 ? 168.284 148.703 182.910 1.00 59.67  ? 119 TYR   A N   1 
ATOM   473  C CA  . TYR   A 1 127 ? 169.547 148.713 182.188 1.00 64.12  ? 119 TYR   A CA  1 
ATOM   474  C C   . TYR   A 1 127 ? 170.434 149.884 182.589 1.00 63.80  ? 119 TYR   A C   1 
ATOM   475  O O   . TYR   A 1 127 ? 171.660 149.746 182.613 1.00 67.77  ? 119 TYR   A O   1 
ATOM   476  C CB  . TYR   A 1 127 ? 169.280 148.725 180.674 1.00 65.43  ? 119 TYR   A CB  1 
ATOM   477  C CG  . TYR   A 1 127 ? 170.429 149.188 179.802 1.00 74.12  ? 119 TYR   A CG  1 
ATOM   478  C CD1 . TYR   A 1 127 ? 171.211 148.268 179.120 1.00 77.07  ? 119 TYR   A CD1 1 
ATOM   479  C CD2 . TYR   A 1 127 ? 170.683 150.541 179.595 1.00 76.73  ? 119 TYR   A CD2 1 
ATOM   480  C CE1 . TYR   A 1 127 ? 172.252 148.675 178.313 1.00 81.67  ? 119 TYR   A CE1 1 
ATOM   481  C CE2 . TYR   A 1 127 ? 171.723 150.957 178.785 1.00 82.07  ? 119 TYR   A CE2 1 
ATOM   482  C CZ  . TYR   A 1 127 ? 172.501 150.019 178.144 1.00 83.27  ? 119 TYR   A CZ  1 
ATOM   483  O OH  . TYR   A 1 127 ? 173.535 150.420 177.330 1.00 85.88  ? 119 TYR   A OH  1 
ATOM   484  N N   . LEU   A 1 128 ? 169.838 151.035 182.901 1.00 61.31  ? 120 LEU   A N   1 
ATOM   485  C CA  . LEU   A 1 128 ? 170.621 152.184 183.345 1.00 58.85  ? 120 LEU   A CA  1 
ATOM   486  C C   . LEU   A 1 128 ? 171.103 152.005 184.780 1.00 62.90  ? 120 LEU   A C   1 
ATOM   487  O O   . LEU   A 1 128 ? 172.259 152.304 185.098 1.00 68.38  ? 120 LEU   A O   1 
ATOM   488  C CB  . LEU   A 1 128 ? 169.790 153.461 183.215 1.00 59.61  ? 120 LEU   A CB  1 
ATOM   489  C CG  . LEU   A 1 128 ? 169.700 154.099 181.829 1.00 60.57  ? 120 LEU   A CG  1 
ATOM   490  C CD1 . LEU   A 1 128 ? 168.513 155.041 181.765 1.00 54.25  ? 120 LEU   A CD1 1 
ATOM   491  C CD2 . LEU   A 1 128 ? 170.984 154.838 181.499 1.00 69.03  ? 120 LEU   A CD2 1 
ATOM   492  N N   . MET   A 1 129 ? 170.229 151.517 185.662 1.00 64.63  ? 121 MET   A N   1 
ATOM   493  C CA  . MET   A 1 129 ? 170.538 151.402 187.081 1.00 65.03  ? 121 MET   A CA  1 
ATOM   494  C C   . MET   A 1 129 ? 170.583 149.968 187.587 1.00 65.91  ? 121 MET   A C   1 
ATOM   495  O O   . MET   A 1 129 ? 171.025 149.749 188.721 1.00 63.73  ? 121 MET   A O   1 
ATOM   496  C CB  . MET   A 1 129 ? 169.516 152.187 187.915 1.00 61.58  ? 121 MET   A CB  1 
ATOM   497  C CG  . MET   A 1 129 ? 169.114 153.523 187.322 1.00 60.54  ? 121 MET   A CG  1 
ATOM   498  S SD  . MET   A 1 129 ? 167.434 153.990 187.774 1.00 75.50  ? 121 MET   A SD  1 
ATOM   499  C CE  . MET   A 1 129 ? 167.258 153.149 189.344 1.00 52.34  ? 121 MET   A CE  1 
ATOM   500  N N   . ASN   A 1 130 ? 170.138 148.996 186.790 1.00 67.74  ? 122 ASN   A N   1 
ATOM   501  C CA  . ASN   A 1 130 ? 170.115 147.587 187.187 1.00 69.29  ? 122 ASN   A CA  1 
ATOM   502  C C   . ASN   A 1 130 ? 169.309 147.378 188.468 1.00 70.74  ? 122 ASN   A C   1 
ATOM   503  O O   . ASN   A 1 130 ? 169.696 146.611 189.351 1.00 72.46  ? 122 ASN   A O   1 
ATOM   504  C CB  . ASN   A 1 130 ? 171.532 147.031 187.337 1.00 77.91  ? 122 ASN   A CB  1 
ATOM   505  C CG  . ASN   A 1 130 ? 171.732 145.736 186.577 1.00 85.96  ? 122 ASN   A CG  1 
ATOM   506  O OD1 . ASN   A 1 130 ? 171.067 144.736 186.845 1.00 91.99  ? 122 ASN   A OD1 1 
ATOM   507  N ND2 . ASN   A 1 130 ? 172.651 145.749 185.618 1.00 82.04  ? 122 ASN   A ND2 1 
ATOM   508  N N   . SER   A 1 131 ? 168.178 148.072 188.571 1.00 68.30  ? 123 SER   A N   1 
ATOM   509  C CA  . SER   A 1 131 ? 167.275 147.919 189.703 1.00 60.98  ? 123 SER   A CA  1 
ATOM   510  C C   . SER   A 1 131 ? 165.886 148.365 189.274 1.00 58.86  ? 123 SER   A C   1 
ATOM   511  O O   . SER   A 1 131 ? 165.721 149.051 188.263 1.00 60.48  ? 123 SER   A O   1 
ATOM   512  C CB  . SER   A 1 131 ? 167.751 148.720 190.919 1.00 55.86  ? 123 SER   A CB  1 
ATOM   513  O OG  . SER   A 1 131 ? 168.740 148.008 191.641 1.00 56.28  ? 123 SER   A OG  1 
ATOM   514  N N   . TRP   A 1 132 ? 164.886 147.966 190.059 1.00 51.68  ? 124 TRP   A N   1 
ATOM   515  C CA  . TRP   A 1 132 ? 163.497 148.310 189.768 1.00 43.68  ? 124 TRP   A CA  1 
ATOM   516  C C   . TRP   A 1 132 ? 162.970 149.279 190.817 1.00 44.38  ? 124 TRP   A C   1 
ATOM   517  O O   . TRP   A 1 132 ? 162.654 148.864 191.942 1.00 43.40  ? 124 TRP   A O   1 
ATOM   518  C CB  . TRP   A 1 132 ? 162.628 147.051 189.719 1.00 43.62  ? 124 TRP   A CB  1 
ATOM   519  C CG  . TRP   A 1 132 ? 161.225 147.323 189.291 1.00 37.41  ? 124 TRP   A CG  1 
ATOM   520  C CD1 . TRP   A 1 132 ? 160.132 147.429 190.095 1.00 36.29  ? 124 TRP   A CD1 1 
ATOM   521  C CD2 . TRP   A 1 132 ? 160.762 147.536 187.953 1.00 36.73  ? 124 TRP   A CD2 1 
ATOM   522  N NE1 . TRP   A 1 132 ? 159.014 147.690 189.342 1.00 37.63  ? 124 TRP   A NE1 1 
ATOM   523  C CE2 . TRP   A 1 132 ? 159.376 147.761 188.023 1.00 33.81  ? 124 TRP   A CE2 1 
ATOM   524  C CE3 . TRP   A 1 132 ? 161.385 147.556 186.704 1.00 42.44  ? 124 TRP   A CE3 1 
ATOM   525  C CZ2 . TRP   A 1 132 ? 158.602 148.002 186.893 1.00 33.40  ? 124 TRP   A CZ2 1 
ATOM   526  C CZ3 . TRP   A 1 132 ? 160.615 147.796 185.583 1.00 40.38  ? 124 TRP   A CZ3 1 
ATOM   527  C CH2 . TRP   A 1 132 ? 159.239 148.015 185.684 1.00 34.23  ? 124 TRP   A CH2 1 
ATOM   528  N N   . PRO   A 1 133 ? 162.865 150.572 190.510 1.00 41.54  ? 125 PRO   A N   1 
ATOM   529  C CA  . PRO   A 1 133 ? 162.323 151.544 191.475 1.00 35.17  ? 125 PRO   A CA  1 
ATOM   530  C C   . PRO   A 1 133 ? 160.842 151.872 191.313 1.00 37.84  ? 125 PRO   A C   1 
ATOM   531  O O   . PRO   A 1 133 ? 160.372 152.795 191.985 1.00 46.34  ? 125 PRO   A O   1 
ATOM   532  C CB  . PRO   A 1 133 ? 163.172 152.783 191.176 1.00 34.24  ? 125 PRO   A CB  1 
ATOM   533  C CG  . PRO   A 1 133 ? 163.412 152.704 189.703 1.00 34.38  ? 125 PRO   A CG  1 
ATOM   534  C CD  . PRO   A 1 133 ? 163.441 151.237 189.329 1.00 39.24  ? 125 PRO   A CD  1 
ATOM   535  N N   . PHE   A 1 134 ? 160.106 151.163 190.457 1.00 35.67  ? 126 PHE   A N   1 
ATOM   536  C CA  . PHE   A 1 134 ? 158.748 151.560 190.107 1.00 33.82  ? 126 PHE   A CA  1 
ATOM   537  C C   . PHE   A 1 134 ? 157.664 150.855 190.914 1.00 40.89  ? 126 PHE   A C   1 
ATOM   538  O O   . PHE   A 1 134 ? 156.492 151.227 190.795 1.00 43.78  ? 126 PHE   A O   1 
ATOM   539  C CB  . PHE   A 1 134 ? 158.502 151.327 188.614 1.00 33.43  ? 126 PHE   A CB  1 
ATOM   540  C CG  . PHE   A 1 134 ? 159.462 152.058 187.727 1.00 33.83  ? 126 PHE   A CG  1 
ATOM   541  C CD1 . PHE   A 1 134 ? 159.381 153.431 187.583 1.00 36.57  ? 126 PHE   A CD1 1 
ATOM   542  C CD2 . PHE   A 1 134 ? 160.444 151.375 187.038 1.00 36.76  ? 126 PHE   A CD2 1 
ATOM   543  C CE1 . PHE   A 1 134 ? 160.265 154.108 186.769 1.00 35.48  ? 126 PHE   A CE1 1 
ATOM   544  C CE2 . PHE   A 1 134 ? 161.326 152.045 186.223 1.00 35.74  ? 126 PHE   A CE2 1 
ATOM   545  C CZ  . PHE   A 1 134 ? 161.238 153.413 186.088 1.00 34.59  ? 126 PHE   A CZ  1 
ATOM   546  N N   . GLY   A 1 135 ? 158.009 149.863 191.723 1.00 37.00  ? 127 GLY   A N   1 
ATOM   547  C CA  . GLY   A 1 135 ? 157.057 149.255 192.629 1.00 36.24  ? 127 GLY   A CA  1 
ATOM   548  C C   . GLY   A 1 135 ? 156.419 147.992 192.071 1.00 47.42  ? 127 GLY   A C   1 
ATOM   549  O O   . GLY   A 1 135 ? 156.564 147.631 190.899 1.00 50.78  ? 127 GLY   A O   1 
ATOM   550  N N   . ASP   A 1 136 ? 155.667 147.330 192.956 1.00 47.49  ? 128 ASP   A N   1 
ATOM   551  C CA  . ASP   A 1 136 ? 155.141 146.000 192.667 1.00 44.78  ? 128 ASP   A CA  1 
ATOM   552  C C   . ASP   A 1 136 ? 154.021 146.039 191.633 1.00 44.86  ? 128 ASP   A C   1 
ATOM   553  O O   . ASP   A 1 136 ? 153.978 145.199 190.728 1.00 48.23  ? 128 ASP   A O   1 
ATOM   554  C CB  . ASP   A 1 136 ? 154.655 145.350 193.961 1.00 48.96  ? 128 ASP   A CB  1 
ATOM   555  C CG  . ASP   A 1 136 ? 154.701 143.841 193.908 1.00 59.32  ? 128 ASP   A CG  1 
ATOM   556  O OD1 . ASP   A 1 136 ? 154.562 143.284 192.801 1.00 59.04  ? 128 ASP   A OD1 1 
ATOM   557  O OD2 . ASP   A 1 136 ? 154.879 143.210 194.971 1.00 60.87  ? 128 ASP   A OD2 1 
ATOM   558  N N   . VAL   A 1 137 ? 153.094 146.991 191.759 1.00 43.93  ? 129 VAL   A N   1 
ATOM   559  C CA  . VAL   A 1 137 ? 151.985 147.067 190.812 1.00 38.73  ? 129 VAL   A CA  1 
ATOM   560  C C   . VAL   A 1 137 ? 152.495 147.398 189.415 1.00 43.24  ? 129 VAL   A C   1 
ATOM   561  O O   . VAL   A 1 137 ? 152.046 146.815 188.419 1.00 46.86  ? 129 VAL   A O   1 
ATOM   562  C CB  . VAL   A 1 137 ? 150.940 148.088 191.292 1.00 41.12  ? 129 VAL   A CB  1 
ATOM   563  C CG1 . VAL   A 1 137 ? 149.790 148.172 190.306 1.00 41.42  ? 129 VAL   A CG1 1 
ATOM   564  C CG2 . VAL   A 1 137 ? 150.433 147.714 192.673 1.00 40.86  ? 129 VAL   A CG2 1 
ATOM   565  N N   . LEU   A 1 138 ? 153.434 148.340 189.316 1.00 44.45  ? 130 LEU   A N   1 
ATOM   566  C CA  . LEU   A 1 138 ? 154.012 148.667 188.018 1.00 40.47  ? 130 LEU   A CA  1 
ATOM   567  C C   . LEU   A 1 138 ? 154.796 147.491 187.452 1.00 38.72  ? 130 LEU   A C   1 
ATOM   568  O O   . LEU   A 1 138 ? 154.775 147.256 186.239 1.00 42.69  ? 130 LEU   A O   1 
ATOM   569  C CB  . LEU   A 1 138 ? 154.896 149.908 188.130 1.00 37.29  ? 130 LEU   A CB  1 
ATOM   570  C CG  . LEU   A 1 138 ? 154.219 151.211 187.705 1.00 34.77  ? 130 LEU   A CG  1 
ATOM   571  C CD1 . LEU   A 1 138 ? 155.125 152.401 187.952 1.00 40.67  ? 130 LEU   A CD1 1 
ATOM   572  C CD2 . LEU   A 1 138 ? 153.810 151.146 186.245 1.00 34.70  ? 130 LEU   A CD2 1 
ATOM   573  N N   . CYS   A 1 139 ? 155.492 146.738 188.309 1.00 36.96  ? 131 CYS   A N   1 
ATOM   574  C CA  . CYS   A 1 139 ? 156.170 145.533 187.838 1.00 41.14  ? 131 CYS   A CA  1 
ATOM   575  C C   . CYS   A 1 139 ? 155.176 144.530 187.265 1.00 41.18  ? 131 CYS   A C   1 
ATOM   576  O O   . CYS   A 1 139 ? 155.412 143.946 186.198 1.00 42.54  ? 131 CYS   A O   1 
ATOM   577  C CB  . CYS   A 1 139 ? 156.970 144.906 188.979 1.00 43.12  ? 131 CYS   A CB  1 
ATOM   578  S SG  . CYS   A 1 139 ? 157.632 143.264 188.628 1.00 60.72  ? 131 CYS   A SG  1 
ATOM   579  N N   . LYS   A 1 140 ? 154.055 144.324 187.960 1.00 41.87  ? 132 LYS   A N   1 
ATOM   580  C CA  . LYS   A 1 140 ? 153.024 143.412 187.475 1.00 38.03  ? 132 LYS   A CA  1 
ATOM   581  C C   . LYS   A 1 140 ? 152.490 143.863 186.123 1.00 39.55  ? 132 LYS   A C   1 
ATOM   582  O O   . LYS   A 1 140 ? 152.360 143.060 185.190 1.00 44.25  ? 132 LYS   A O   1 
ATOM   583  C CB  . LYS   A 1 140 ? 151.883 143.329 188.490 1.00 35.20  ? 132 LYS   A CB  1 
ATOM   584  C CG  . LYS   A 1 140 ? 152.155 142.451 189.694 1.00 39.84  ? 132 LYS   A CG  1 
ATOM   585  C CD  . LYS   A 1 140 ? 151.104 142.675 190.769 1.00 41.93  ? 132 LYS   A CD  1 
ATOM   586  C CE  . LYS   A 1 140 ? 150.986 141.482 191.700 1.00 42.09  ? 132 LYS   A CE  1 
ATOM   587  N NZ  . LYS   A 1 140 ? 152.270 141.159 192.374 1.00 46.31  ? 132 LYS   A NZ  1 
ATOM   588  N N   . ILE   A 1 141 ? 152.182 145.156 186.002 1.00 37.57  ? 133 ILE   A N   1 
ATOM   589  C CA  . ILE   A 1 141 ? 151.627 145.684 184.759 1.00 38.43  ? 133 ILE   A CA  1 
ATOM   590  C C   . ILE   A 1 141 ? 152.625 145.532 183.618 1.00 40.90  ? 133 ILE   A C   1 
ATOM   591  O O   . ILE   A 1 141 ? 152.260 145.147 182.501 1.00 38.61  ? 133 ILE   A O   1 
ATOM   592  C CB  . ILE   A 1 141 ? 151.197 147.151 184.952 1.00 38.26  ? 133 ILE   A CB  1 
ATOM   593  C CG1 . ILE   A 1 141 ? 149.810 147.216 185.591 1.00 39.66  ? 133 ILE   A CG1 1 
ATOM   594  C CG2 . ILE   A 1 141 ? 151.209 147.900 183.630 1.00 39.62  ? 133 ILE   A CG2 1 
ATOM   595  C CD1 . ILE   A 1 141 ? 149.645 148.348 186.575 1.00 38.47  ? 133 ILE   A CD1 1 
ATOM   596  N N   . VAL   A 1 142 ? 153.901 145.823 183.880 1.00 40.23  ? 134 VAL   A N   1 
ATOM   597  C CA  . VAL   A 1 142 ? 154.919 145.739 182.839 1.00 37.28  ? 134 VAL   A CA  1 
ATOM   598  C C   . VAL   A 1 142 ? 155.107 144.299 182.373 1.00 41.38  ? 134 VAL   A C   1 
ATOM   599  O O   . VAL   A 1 142 ? 155.186 144.030 181.167 1.00 43.95  ? 134 VAL   A O   1 
ATOM   600  C CB  . VAL   A 1 142 ? 156.236 146.354 183.346 1.00 36.65  ? 134 VAL   A CB  1 
ATOM   601  C CG1 . VAL   A 1 142 ? 157.406 145.833 182.546 1.00 43.04  ? 134 VAL   A CG1 1 
ATOM   602  C CG2 . VAL   A 1 142 ? 156.170 147.870 183.272 1.00 34.03  ? 134 VAL   A CG2 1 
ATOM   603  N N   . ILE   A 1 143 ? 155.183 143.351 183.312 1.00 42.54  ? 135 ILE   A N   1 
ATOM   604  C CA  . ILE   A 1 143 ? 155.345 141.949 182.928 1.00 39.01  ? 135 ILE   A CA  1 
ATOM   605  C C   . ILE   A 1 143 ? 154.137 141.471 182.131 1.00 39.03  ? 135 ILE   A C   1 
ATOM   606  O O   . ILE   A 1 143 ? 154.276 140.770 181.116 1.00 43.64  ? 135 ILE   A O   1 
ATOM   607  C CB  . ILE   A 1 143 ? 155.584 141.074 184.172 1.00 40.60  ? 135 ILE   A CB  1 
ATOM   608  C CG1 . ILE   A 1 143 ? 156.910 141.435 184.837 1.00 43.92  ? 135 ILE   A CG1 1 
ATOM   609  C CG2 . ILE   A 1 143 ? 155.585 139.605 183.800 1.00 39.96  ? 135 ILE   A CG2 1 
ATOM   610  C CD1 . ILE   A 1 143 ? 157.203 140.616 186.070 1.00 41.05  ? 135 ILE   A CD1 1 
ATOM   611  N N   . SER   A 1 144 ? 152.933 141.840 182.578 1.00 40.63  ? 136 SER   A N   1 
ATOM   612  C CA  . SER   A 1 144 ? 151.729 141.434 181.864 1.00 43.12  ? 136 SER   A CA  1 
ATOM   613  C C   . SER   A 1 144 ? 151.706 142.008 180.456 1.00 42.44  ? 136 SER   A C   1 
ATOM   614  O O   . SER   A 1 144 ? 151.331 141.316 179.505 1.00 44.89  ? 136 SER   A O   1 
ATOM   615  C CB  . SER   A 1 144 ? 150.488 141.868 182.640 1.00 43.41  ? 136 SER   A CB  1 
ATOM   616  O OG  . SER   A 1 144 ? 149.311 141.354 182.042 1.00 49.12  ? 136 SER   A OG  1 
ATOM   617  N N   . ILE   A 1 145 ? 152.110 143.271 180.301 1.00 43.23  ? 137 ILE   A N   1 
ATOM   618  C CA  . ILE   A 1 145 ? 152.135 143.890 178.978 1.00 44.49  ? 137 ILE   A CA  1 
ATOM   619  C C   . ILE   A 1 145 ? 153.150 143.194 178.081 1.00 44.61  ? 137 ILE   A C   1 
ATOM   620  O O   . ILE   A 1 145 ? 152.891 142.959 176.895 1.00 47.85  ? 137 ILE   A O   1 
ATOM   621  C CB  . ILE   A 1 145 ? 152.417 145.399 179.101 1.00 43.98  ? 137 ILE   A CB  1 
ATOM   622  C CG1 . ILE   A 1 145 ? 151.120 146.158 179.380 1.00 46.53  ? 137 ILE   A CG1 1 
ATOM   623  C CG2 . ILE   A 1 145 ? 153.081 145.932 177.844 1.00 43.90  ? 137 ILE   A CG2 1 
ATOM   624  C CD1 . ILE   A 1 145 ? 151.322 147.624 179.675 1.00 46.88  ? 137 ILE   A CD1 1 
ATOM   625  N N   . ASP   A 1 146 ? 154.319 142.851 178.628 1.00 42.27  ? 138 ASP   A N   1 
ATOM   626  C CA  . ASP   A 1 146 ? 155.333 142.166 177.831 1.00 42.98  ? 138 ASP   A CA  1 
ATOM   627  C C   . ASP   A 1 146 ? 154.821 140.822 177.325 1.00 42.82  ? 138 ASP   A C   1 
ATOM   628  O O   . ASP   A 1 146 ? 154.953 140.497 176.137 1.00 45.04  ? 138 ASP   A O   1 
ATOM   629  C CB  . ASP   A 1 146 ? 156.609 141.978 178.652 1.00 48.99  ? 138 ASP   A CB  1 
ATOM   630  C CG  . ASP   A 1 146 ? 157.358 143.275 178.873 1.00 57.76  ? 138 ASP   A CG  1 
ATOM   631  O OD1 . ASP   A 1 146 ? 157.146 144.227 178.094 1.00 62.64  ? 138 ASP   A OD1 1 
ATOM   632  O OD2 . ASP   A 1 146 ? 158.161 143.342 179.826 1.00 55.70  ? 138 ASP   A OD2 1 
ATOM   633  N N   . TYR   A 1 147 ? 154.221 140.028 178.216 1.00 41.45  ? 139 TYR   A N   1 
ATOM   634  C CA  . TYR   A 1 147 ? 153.728 138.717 177.799 1.00 37.80  ? 139 TYR   A CA  1 
ATOM   635  C C   . TYR   A 1 147 ? 152.550 138.845 176.839 1.00 39.18  ? 139 TYR   A C   1 
ATOM   636  O O   . TYR   A 1 147 ? 152.432 138.067 175.880 1.00 42.26  ? 139 TYR   A O   1 
ATOM   637  C CB  . TYR   A 1 147 ? 153.353 137.884 179.023 1.00 37.35  ? 139 TYR   A CB  1 
ATOM   638  C CG  . TYR   A 1 147 ? 154.530 137.149 179.621 1.00 39.74  ? 139 TYR   A CG  1 
ATOM   639  C CD1 . TYR   A 1 147 ? 155.037 136.007 179.020 1.00 40.00  ? 139 TYR   A CD1 1 
ATOM   640  C CD2 . TYR   A 1 147 ? 155.143 137.605 180.778 1.00 42.98  ? 139 TYR   A CD2 1 
ATOM   641  C CE1 . TYR   A 1 147 ? 156.116 135.336 179.558 1.00 41.03  ? 139 TYR   A CE1 1 
ATOM   642  C CE2 . TYR   A 1 147 ? 156.222 136.940 181.324 1.00 39.34  ? 139 TYR   A CE2 1 
ATOM   643  C CZ  . TYR   A 1 147 ? 156.704 135.806 180.709 1.00 41.93  ? 139 TYR   A CZ  1 
ATOM   644  O OH  . TYR   A 1 147 ? 157.779 135.139 181.249 1.00 49.28  ? 139 TYR   A OH  1 
ATOM   645  N N   . TYR   A 1 148 ? 151.674 139.826 177.075 1.00 40.76  ? 140 TYR   A N   1 
ATOM   646  C CA  . TYR   A 1 148 ? 150.571 140.087 176.159 1.00 39.18  ? 140 TYR   A CA  1 
ATOM   647  C C   . TYR   A 1 148 ? 151.088 140.405 174.767 1.00 40.24  ? 140 TYR   A C   1 
ATOM   648  O O   . TYR   A 1 148 ? 150.595 139.866 173.773 1.00 45.50  ? 140 TYR   A O   1 
ATOM   649  C CB  . TYR   A 1 148 ? 149.727 141.248 176.681 1.00 39.88  ? 140 TYR   A CB  1 
ATOM   650  C CG  . TYR   A 1 148 ? 148.454 140.845 177.380 1.00 43.51  ? 140 TYR   A CG  1 
ATOM   651  C CD1 . TYR   A 1 148 ? 147.505 140.061 176.743 1.00 45.41  ? 140 TYR   A CD1 1 
ATOM   652  C CD2 . TYR   A 1 148 ? 148.193 141.266 178.675 1.00 43.83  ? 140 TYR   A CD2 1 
ATOM   653  C CE1 . TYR   A 1 148 ? 146.337 139.700 177.381 1.00 50.39  ? 140 TYR   A CE1 1 
ATOM   654  C CE2 . TYR   A 1 148 ? 147.031 140.911 179.320 1.00 46.92  ? 140 TYR   A CE2 1 
ATOM   655  C CZ  . TYR   A 1 148 ? 146.106 140.129 178.670 1.00 50.76  ? 140 TYR   A CZ  1 
ATOM   656  O OH  . TYR   A 1 148 ? 144.945 139.776 179.315 1.00 57.18  ? 140 TYR   A OH  1 
ATOM   657  N N   . ASN   A 1 149 ? 152.084 141.286 174.677 1.00 39.83  ? 141 ASN   A N   1 
ATOM   658  C CA  . ASN   A 1 149 ? 152.648 141.636 173.379 1.00 42.13  ? 141 ASN   A CA  1 
ATOM   659  C C   . ASN   A 1 149 ? 153.253 140.415 172.703 1.00 41.40  ? 141 ASN   A C   1 
ATOM   660  O O   . ASN   A 1 149 ? 152.980 140.145 171.527 1.00 43.33  ? 141 ASN   A O   1 
ATOM   661  C CB  . ASN   A 1 149 ? 153.693 142.739 173.544 1.00 41.38  ? 141 ASN   A CB  1 
ATOM   662  C CG  . ASN   A 1 149 ? 154.713 142.747 172.425 1.00 42.73  ? 141 ASN   A CG  1 
ATOM   663  O OD1 . ASN   A 1 149 ? 155.836 142.276 172.592 1.00 46.78  ? 141 ASN   A OD1 1 
ATOM   664  N ND2 . ASN   A 1 149 ? 154.326 143.284 171.275 1.00 42.55  ? 141 ASN   A ND2 1 
ATOM   665  N N   . MET   A 1 150 ? 154.048 139.639 173.447 1.00 40.25  ? 142 MET   A N   1 
ATOM   666  C CA  . MET   A 1 150 ? 154.723 138.492 172.849 1.00 37.94  ? 142 MET   A CA  1 
ATOM   667  C C   . MET   A 1 150 ? 153.724 137.490 172.286 1.00 41.61  ? 142 MET   A C   1 
ATOM   668  O O   . MET   A 1 150 ? 153.888 137.000 171.163 1.00 47.19  ? 142 MET   A O   1 
ATOM   669  C CB  . MET   A 1 150 ? 155.627 137.808 173.871 1.00 40.63  ? 142 MET   A CB  1 
ATOM   670  C CG  . MET   A 1 150 ? 156.454 136.680 173.272 1.00 48.22  ? 142 MET   A CG  1 
ATOM   671  S SD  . MET   A 1 150 ? 157.411 135.761 174.487 1.00 65.42  ? 142 MET   A SD  1 
ATOM   672  C CE  . MET   A 1 150 ? 157.430 136.932 175.833 1.00 50.40  ? 142 MET   A CE  1 
ATOM   673  N N   . PHE   A 1 151 ? 152.682 137.163 173.053 1.00 40.33  ? 143 PHE   A N   1 
ATOM   674  C CA  . PHE   A 1 151 ? 151.737 136.157 172.578 1.00 39.17  ? 143 PHE   A CA  1 
ATOM   675  C C   . PHE   A 1 151 ? 150.824 136.711 171.490 1.00 39.85  ? 143 PHE   A C   1 
ATOM   676  O O   . PHE   A 1 151 ? 150.571 136.038 170.480 1.00 41.77  ? 143 PHE   A O   1 
ATOM   677  C CB  . PHE   A 1 151 ? 150.922 135.611 173.749 1.00 41.42  ? 143 PHE   A CB  1 
ATOM   678  C CG  . PHE   A 1 151 ? 151.627 134.533 174.518 1.00 47.57  ? 143 PHE   A CG  1 
ATOM   679  C CD1 . PHE   A 1 151 ? 152.542 134.855 175.504 1.00 43.97  ? 143 PHE   A CD1 1 
ATOM   680  C CD2 . PHE   A 1 151 ? 151.388 133.199 174.244 1.00 50.52  ? 143 PHE   A CD2 1 
ATOM   681  C CE1 . PHE   A 1 151 ? 153.197 133.867 176.209 1.00 45.91  ? 143 PHE   A CE1 1 
ATOM   682  C CE2 . PHE   A 1 151 ? 152.042 132.206 174.946 1.00 48.55  ? 143 PHE   A CE2 1 
ATOM   683  C CZ  . PHE   A 1 151 ? 152.947 132.542 175.930 1.00 48.79  ? 143 PHE   A CZ  1 
ATOM   684  N N   . THR   A 1 152 ? 150.324 137.936 171.671 1.00 41.46  ? 144 THR   A N   1 
ATOM   685  C CA  . THR   A 1 152 ? 149.367 138.503 170.732 1.00 40.84  ? 144 THR   A CA  1 
ATOM   686  C C   . THR   A 1 152 ? 149.998 138.749 169.370 1.00 41.40  ? 144 THR   A C   1 
ATOM   687  O O   . THR   A 1 152 ? 149.356 138.519 168.342 1.00 39.67  ? 144 THR   A O   1 
ATOM   688  C CB  . THR   A 1 152 ? 148.786 139.798 171.299 1.00 38.72  ? 144 THR   A CB  1 
ATOM   689  O OG1 . THR   A 1 152 ? 148.138 139.523 172.546 1.00 47.58  ? 144 THR   A OG1 1 
ATOM   690  C CG2 . THR   A 1 152 ? 147.774 140.398 170.339 1.00 40.12  ? 144 THR   A CG2 1 
ATOM   691  N N   . SER   A 1 153 ? 151.250 139.216 169.333 1.00 42.14  ? 145 SER   A N   1 
ATOM   692  C CA  . SER   A 1 153 ? 151.887 139.481 168.048 1.00 36.17  ? 145 SER   A CA  1 
ATOM   693  C C   . SER   A 1 153 ? 151.985 138.211 167.213 1.00 35.38  ? 145 SER   A C   1 
ATOM   694  O O   . SER   A 1 153 ? 151.603 138.194 166.037 1.00 38.88  ? 145 SER   A O   1 
ATOM   695  C CB  . SER   A 1 153 ? 153.270 140.093 168.267 1.00 35.41  ? 145 SER   A CB  1 
ATOM   696  O OG  . SER   A 1 153 ? 153.173 141.339 168.934 1.00 41.67  ? 145 SER   A OG  1 
ATOM   697  N N   . ILE   A 1 154 ? 152.470 137.125 167.815 1.00 36.13  ? 146 ILE   A N   1 
ATOM   698  C CA  . ILE   A 1 154 ? 152.657 135.892 167.060 1.00 36.23  ? 146 ILE   A CA  1 
ATOM   699  C C   . ILE   A 1 154 ? 151.312 135.270 166.695 1.00 39.77  ? 146 ILE   A C   1 
ATOM   700  O O   . ILE   A 1 154 ? 151.147 134.731 165.593 1.00 38.46  ? 146 ILE   A O   1 
ATOM   701  C CB  . ILE   A 1 154 ? 153.568 134.916 167.831 1.00 35.82  ? 146 ILE   A CB  1 
ATOM   702  C CG1 . ILE   A 1 154 ? 153.986 133.756 166.929 1.00 35.62  ? 146 ILE   A CG1 1 
ATOM   703  C CG2 . ILE   A 1 154 ? 152.901 134.402 169.095 1.00 37.77  ? 146 ILE   A CG2 1 
ATOM   704  C CD1 . ILE   A 1 154 ? 154.830 134.168 165.750 1.00 37.83  ? 146 ILE   A CD1 1 
ATOM   705  N N   . PHE   A 1 155 ? 150.321 135.348 167.590 1.00 39.91  ? 147 PHE   A N   1 
ATOM   706  C CA  . PHE   A 1 155 ? 149.010 134.796 167.256 1.00 32.66  ? 147 PHE   A CA  1 
ATOM   707  C C   . PHE   A 1 155 ? 148.347 135.579 166.128 1.00 32.26  ? 147 PHE   A C   1 
ATOM   708  O O   . PHE   A 1 155 ? 147.738 134.989 165.227 1.00 35.99  ? 147 PHE   A O   1 
ATOM   709  C CB  . PHE   A 1 155 ? 148.119 134.770 168.497 1.00 39.13  ? 147 PHE   A CB  1 
ATOM   710  C CG  . PHE   A 1 155 ? 148.519 133.733 169.509 1.00 47.26  ? 147 PHE   A CG  1 
ATOM   711  C CD1 . PHE   A 1 155 ? 149.412 132.729 169.177 1.00 47.23  ? 147 PHE   A CD1 1 
ATOM   712  C CD2 . PHE   A 1 155 ? 147.999 133.760 170.791 1.00 48.93  ? 147 PHE   A CD2 1 
ATOM   713  C CE1 . PHE   A 1 155 ? 149.781 131.775 170.105 1.00 47.07  ? 147 PHE   A CE1 1 
ATOM   714  C CE2 . PHE   A 1 155 ? 148.364 132.809 171.723 1.00 43.70  ? 147 PHE   A CE2 1 
ATOM   715  C CZ  . PHE   A 1 155 ? 149.256 131.816 171.379 1.00 44.86  ? 147 PHE   A CZ  1 
ATOM   716  N N   . THR   A 1 156 ? 148.460 136.909 166.153 1.00 33.25  ? 148 THR   A N   1 
ATOM   717  C CA  . THR   A 1 156 ? 147.881 137.724 165.094 1.00 31.17  ? 148 THR   A CA  1 
ATOM   718  C C   . THR   A 1 156 ? 148.596 137.495 163.771 1.00 30.67  ? 148 THR   A C   1 
ATOM   719  O O   . THR   A 1 156 ? 147.961 137.489 162.714 1.00 33.44  ? 148 THR   A O   1 
ATOM   720  C CB  . THR   A 1 156 ? 147.925 139.201 165.483 1.00 33.40  ? 148 THR   A CB  1 
ATOM   721  O OG1 . THR   A 1 156 ? 147.350 139.370 166.784 1.00 38.52  ? 148 THR   A OG1 1 
ATOM   722  C CG2 . THR   A 1 156 ? 147.145 140.038 164.487 1.00 33.75  ? 148 THR   A CG2 1 
ATOM   723  N N   . LEU   A 1 157 ? 149.917 137.304 163.803 1.00 33.30  ? 149 LEU   A N   1 
ATOM   724  C CA  . LEU   A 1 157 ? 150.635 136.980 162.574 1.00 27.86  ? 149 LEU   A CA  1 
ATOM   725  C C   . LEU   A 1 157 ? 150.217 135.620 162.029 1.00 30.36  ? 149 LEU   A C   1 
ATOM   726  O O   . LEU   A 1 157 ? 150.084 135.448 160.811 1.00 32.21  ? 149 LEU   A O   1 
ATOM   727  C CB  . LEU   A 1 157 ? 152.140 137.025 162.818 1.00 28.24  ? 149 LEU   A CB  1 
ATOM   728  C CG  . LEU   A 1 157 ? 152.707 138.426 163.037 1.00 30.87  ? 149 LEU   A CG  1 
ATOM   729  C CD1 . LEU   A 1 157 ? 154.145 138.340 163.484 1.00 34.99  ? 149 LEU   A CD1 1 
ATOM   730  C CD2 . LEU   A 1 157 ? 152.584 139.259 161.776 1.00 32.36  ? 149 LEU   A CD2 1 
ATOM   731  N N   . THR   A 1 158 ? 150.007 134.641 162.911 1.00 30.09  ? 150 THR   A N   1 
ATOM   732  C CA  . THR   A 1 158 ? 149.525 133.337 162.464 1.00 27.94  ? 150 THR   A CA  1 
ATOM   733  C C   . THR   A 1 158 ? 148.149 133.452 161.822 1.00 31.84  ? 150 THR   A C   1 
ATOM   734  O O   . THR   A 1 158 ? 147.884 132.835 160.783 1.00 36.23  ? 150 THR   A O   1 
ATOM   735  C CB  . THR   A 1 158 ? 149.487 132.360 163.638 1.00 27.71  ? 150 THR   A CB  1 
ATOM   736  O OG1 . THR   A 1 158 ? 150.764 132.337 164.284 1.00 33.66  ? 150 THR   A OG1 1 
ATOM   737  C CG2 . THR   A 1 158 ? 149.147 130.961 163.156 1.00 26.70  ? 150 THR   A CG2 1 
ATOM   738  N N   . MET   A 1 159 ? 147.259 134.243 162.424 1.00 33.66  ? 151 MET   A N   1 
ATOM   739  C CA  . MET   A 1 159 ? 145.936 134.426 161.838 1.00 33.08  ? 151 MET   A CA  1 
ATOM   740  C C   . MET   A 1 159 ? 145.997 135.203 160.528 1.00 32.80  ? 151 MET   A C   1 
ATOM   741  O O   . MET   A 1 159 ? 145.205 134.938 159.621 1.00 37.06  ? 151 MET   A O   1 
ATOM   742  C CB  . MET   A 1 159 ? 145.007 135.117 162.834 1.00 35.73  ? 151 MET   A CB  1 
ATOM   743  C CG  . MET   A 1 159 ? 144.446 134.191 163.908 1.00 39.60  ? 151 MET   A CG  1 
ATOM   744  S SD  . MET   A 1 159 ? 143.592 132.691 163.357 1.00 71.17  ? 151 MET   A SD  1 
ATOM   745  C CE  . MET   A 1 159 ? 142.731 133.231 161.877 1.00 41.99  ? 151 MET   A CE  1 
ATOM   746  N N   . MET   A 1 160 ? 146.927 136.153 160.406 1.00 32.95  ? 152 MET   A N   1 
ATOM   747  C CA  . MET   A 1 160 ? 147.132 136.833 159.131 1.00 32.31  ? 152 MET   A CA  1 
ATOM   748  C C   . MET   A 1 160 ? 147.582 135.856 158.056 1.00 34.19  ? 152 MET   A C   1 
ATOM   749  O O   . MET   A 1 160 ? 147.106 135.909 156.916 1.00 39.74  ? 152 MET   A O   1 
ATOM   750  C CB  . MET   A 1 160 ? 148.167 137.946 159.286 1.00 33.42  ? 152 MET   A CB  1 
ATOM   751  C CG  . MET   A 1 160 ? 147.642 139.203 159.929 1.00 32.38  ? 152 MET   A CG  1 
ATOM   752  S SD  . MET   A 1 160 ? 148.939 140.353 160.418 1.00 58.59  ? 152 MET   A SD  1 
ATOM   753  C CE  . MET   A 1 160 ? 149.573 140.846 158.821 1.00 43.40  ? 152 MET   A CE  1 
ATOM   754  N N   . SER   A 1 161 ? 148.510 134.962 158.400 1.00 31.19  ? 153 SER   A N   1 
ATOM   755  C CA  . SER   A 1 161 ? 148.968 133.964 157.441 1.00 31.37  ? 153 SER   A CA  1 
ATOM   756  C C   . SER   A 1 161 ? 147.833 133.034 157.034 1.00 36.61  ? 153 SER   A C   1 
ATOM   757  O O   . SER   A 1 161 ? 147.695 132.691 155.854 1.00 39.96  ? 153 SER   A O   1 
ATOM   758  C CB  . SER   A 1 161 ? 150.131 133.170 158.030 1.00 33.03  ? 153 SER   A CB  1 
ATOM   759  O OG  . SER   A 1 161 ? 151.104 134.037 158.582 1.00 39.51  ? 153 SER   A OG  1 
ATOM   760  N N   . VAL   A 1 162 ? 147.007 132.619 157.996 1.00 36.72  ? 154 VAL   A N   1 
ATOM   761  C CA  . VAL   A 1 162 ? 145.877 131.748 157.681 1.00 32.96  ? 154 VAL   A CA  1 
ATOM   762  C C   . VAL   A 1 162 ? 144.873 132.470 156.789 1.00 36.83  ? 154 VAL   A C   1 
ATOM   763  O O   . VAL   A 1 162 ? 144.334 131.886 155.841 1.00 43.28  ? 154 VAL   A O   1 
ATOM   764  C CB  . VAL   A 1 162 ? 145.225 131.234 158.977 1.00 32.54  ? 154 VAL   A CB  1 
ATOM   765  C CG1 . VAL   A 1 162 ? 143.913 130.531 158.672 1.00 30.55  ? 154 VAL   A CG1 1 
ATOM   766  C CG2 . VAL   A 1 162 ? 146.173 130.299 159.706 1.00 32.24  ? 154 VAL   A CG2 1 
ATOM   767  N N   . ASP   A 1 163 ? 144.600 133.745 157.078 1.00 36.91  ? 155 ASP   A N   1 
ATOM   768  C CA  . ASP   A 1 163 ? 143.683 134.522 156.251 1.00 36.58  ? 155 ASP   A CA  1 
ATOM   769  C C   . ASP   A 1 163 ? 144.209 134.670 154.830 1.00 41.04  ? 155 ASP   A C   1 
ATOM   770  O O   . ASP   A 1 163 ? 143.451 134.540 153.862 1.00 44.76  ? 155 ASP   A O   1 
ATOM   771  C CB  . ASP   A 1 163 ? 143.455 135.894 156.883 1.00 40.37  ? 155 ASP   A CB  1 
ATOM   772  C CG  . ASP   A 1 163 ? 142.353 136.676 156.201 1.00 55.45  ? 155 ASP   A CG  1 
ATOM   773  O OD1 . ASP   A 1 163 ? 142.641 137.352 155.192 1.00 59.54  ? 155 ASP   A OD1 1 
ATOM   774  O OD2 . ASP   A 1 163 ? 141.201 136.623 156.679 1.00 62.74  ? 155 ASP   A OD2 1 
ATOM   775  N N   . ARG   A 1 164 ? 145.508 134.943 154.684 1.00 40.64  ? 156 ARG   A N   1 
ATOM   776  C CA  . ARG   A 1 164 ? 146.099 135.042 153.354 1.00 38.75  ? 156 ARG   A CA  1 
ATOM   777  C C   . ARG   A 1 164 ? 146.025 133.709 152.621 1.00 36.51  ? 156 ARG   A C   1 
ATOM   778  O O   . ARG   A 1 164 ? 145.750 133.670 151.416 1.00 38.79  ? 156 ARG   A O   1 
ATOM   779  C CB  . ARG   A 1 164 ? 147.546 135.519 153.459 1.00 35.97  ? 156 ARG   A CB  1 
ATOM   780  C CG  . ARG   A 1 164 ? 147.702 136.982 153.833 1.00 35.89  ? 156 ARG   A CG  1 
ATOM   781  C CD  . ARG   A 1 164 ? 147.399 137.900 152.662 1.00 43.58  ? 156 ARG   A CD  1 
ATOM   782  N NE  . ARG   A 1 164 ? 146.022 138.378 152.669 1.00 45.13  ? 156 ARG   A NE  1 
ATOM   783  C CZ  . ARG   A 1 164 ? 145.378 138.815 151.596 1.00 47.69  ? 156 ARG   A CZ  1 
ATOM   784  N NH1 . ARG   A 1 164 ? 145.956 138.847 150.408 1.00 46.78  ? 156 ARG   A NH1 1 
ATOM   785  N NH2 . ARG   A 1 164 ? 144.121 139.231 151.719 1.00 55.55  ? 156 ARG   A NH2 1 
ATOM   786  N N   . TYR   A 1 165 ? 146.273 132.605 153.330 1.00 35.65  ? 157 TYR   A N   1 
ATOM   787  C CA  . TYR   A 1 165 ? 146.185 131.290 152.705 1.00 34.88  ? 157 TYR   A CA  1 
ATOM   788  C C   . TYR   A 1 165 ? 144.769 130.998 152.232 1.00 39.75  ? 157 TYR   A C   1 
ATOM   789  O O   . TYR   A 1 165 ? 144.572 130.445 151.146 1.00 43.44  ? 157 TYR   A O   1 
ATOM   790  C CB  . TYR   A 1 165 ? 146.654 130.210 153.679 1.00 36.98  ? 157 TYR   A CB  1 
ATOM   791  C CG  . TYR   A 1 165 ? 146.238 128.815 153.278 1.00 37.70  ? 157 TYR   A CG  1 
ATOM   792  C CD1 . TYR   A 1 165 ? 146.898 128.140 152.265 1.00 42.12  ? 157 TYR   A CD1 1 
ATOM   793  C CD2 . TYR   A 1 165 ? 145.185 128.175 153.913 1.00 43.22  ? 157 TYR   A CD2 1 
ATOM   794  C CE1 . TYR   A 1 165 ? 146.520 126.868 151.893 1.00 44.95  ? 157 TYR   A CE1 1 
ATOM   795  C CE2 . TYR   A 1 165 ? 144.800 126.903 153.546 1.00 47.17  ? 157 TYR   A CE2 1 
ATOM   796  C CZ  . TYR   A 1 165 ? 145.471 126.255 152.536 1.00 44.23  ? 157 TYR   A CZ  1 
ATOM   797  O OH  . TYR   A 1 165 ? 145.095 124.986 152.166 1.00 50.86  ? 157 TYR   A OH  1 
ATOM   798  N N   . ILE   A 1 166 ? 143.770 131.351 153.041 1.00 43.71  ? 158 ILE   A N   1 
ATOM   799  C CA  . ILE   A 1 166 ? 142.384 131.142 152.637 1.00 42.07  ? 158 ILE   A CA  1 
ATOM   800  C C   . ILE   A 1 166 ? 142.046 132.009 151.431 1.00 42.39  ? 158 ILE   A C   1 
ATOM   801  O O   . ILE   A 1 166 ? 141.379 131.558 150.494 1.00 50.80  ? 158 ILE   A O   1 
ATOM   802  C CB  . ILE   A 1 166 ? 141.436 131.411 153.819 1.00 47.03  ? 158 ILE   A CB  1 
ATOM   803  C CG1 . ILE   A 1 166 ? 141.604 130.333 154.888 1.00 51.00  ? 158 ILE   A CG1 1 
ATOM   804  C CG2 . ILE   A 1 166 ? 139.993 131.461 153.352 1.00 52.97  ? 158 ILE   A CG2 1 
ATOM   805  C CD1 . ILE   A 1 166 ? 141.063 130.729 156.238 1.00 58.47  ? 158 ILE   A CD1 1 
ATOM   806  N N   . ALA   A 1 167 ? 142.508 133.261 151.429 1.00 42.49  ? 159 ALA   A N   1 
ATOM   807  C CA  . ALA   A 1 167 ? 142.221 134.154 150.312 1.00 40.79  ? 159 ALA   A CA  1 
ATOM   808  C C   . ALA   A 1 167 ? 142.864 133.660 149.022 1.00 43.40  ? 159 ALA   A C   1 
ATOM   809  O O   . ALA   A 1 167 ? 142.284 133.799 147.939 1.00 46.94  ? 159 ALA   A O   1 
ATOM   810  C CB  . ALA   A 1 167 ? 142.698 135.569 150.638 1.00 43.47  ? 159 ALA   A CB  1 
ATOM   811  N N   . VAL   A 1 168 ? 144.063 133.087 149.114 1.00 45.88  ? 160 VAL   A N   1 
ATOM   812  C CA  . VAL   A 1 168 ? 144.796 132.699 147.913 1.00 40.00  ? 160 VAL   A CA  1 
ATOM   813  C C   . VAL   A 1 168 ? 144.333 131.340 147.401 1.00 41.84  ? 160 VAL   A C   1 
ATOM   814  O O   . VAL   A 1 168 ? 144.044 131.176 146.210 1.00 43.41  ? 160 VAL   A O   1 
ATOM   815  C CB  . VAL   A 1 168 ? 146.310 132.710 148.188 1.00 32.88  ? 160 VAL   A CB  1 
ATOM   816  C CG1 . VAL   A 1 168 ? 147.060 132.032 147.058 1.00 35.09  ? 160 VAL   A CG1 1 
ATOM   817  C CG2 . VAL   A 1 168 ? 146.801 134.134 148.376 1.00 35.20  ? 160 VAL   A CG2 1 
ATOM   818  N N   . CYS   A 1 169 ? 144.250 130.345 148.284 1.00 42.20  ? 161 CYS   A N   1 
ATOM   819  C CA  . CYS   A 1 169 ? 144.017 128.969 147.867 1.00 46.33  ? 161 CYS   A CA  1 
ATOM   820  C C   . CYS   A 1 169 ? 142.558 128.537 147.934 1.00 52.88  ? 161 CYS   A C   1 
ATOM   821  O O   . CYS   A 1 169 ? 142.194 127.555 147.279 1.00 54.09  ? 161 CYS   A O   1 
ATOM   822  C CB  . CYS   A 1 169 ? 144.857 128.011 148.719 1.00 46.28  ? 161 CYS   A CB  1 
ATOM   823  S SG  . CYS   A 1 169 ? 146.640 128.271 148.601 1.00 50.23  ? 161 CYS   A SG  1 
ATOM   824  N N   . HIS   A 1 170 ? 141.719 129.226 148.704 1.00 53.81  ? 162 HIS   A N   1 
ATOM   825  C CA  . HIS   A 1 170 ? 140.303 128.881 148.840 1.00 52.93  ? 162 HIS   A CA  1 
ATOM   826  C C   . HIS   A 1 170 ? 139.451 130.134 148.685 1.00 57.53  ? 162 HIS   A C   1 
ATOM   827  O O   . HIS   A 1 170 ? 138.837 130.607 149.649 1.00 63.05  ? 162 HIS   A O   1 
ATOM   828  C CB  . HIS   A 1 170 ? 140.035 128.201 150.183 1.00 55.67  ? 162 HIS   A CB  1 
ATOM   829  C CG  . HIS   A 1 170 ? 140.926 127.030 150.456 1.00 57.31  ? 162 HIS   A CG  1 
ATOM   830  N ND1 . HIS   A 1 170 ? 140.692 125.779 149.928 1.00 64.66  ? 162 HIS   A ND1 1 
ATOM   831  C CD2 . HIS   A 1 170 ? 142.052 126.920 151.199 1.00 56.76  ? 162 HIS   A CD2 1 
ATOM   832  C CE1 . HIS   A 1 170 ? 141.636 124.949 150.335 1.00 65.65  ? 162 HIS   A CE1 1 
ATOM   833  N NE2 . HIS   A 1 170 ? 142.473 125.616 151.107 1.00 61.54  ? 162 HIS   A NE2 1 
ATOM   834  N N   . PRO   A 1 171 ? 139.389 130.702 147.476 1.00 53.03  ? 163 PRO   A N   1 
ATOM   835  C CA  . PRO   A 1 171 ? 138.584 131.917 147.283 1.00 55.89  ? 163 PRO   A CA  1 
ATOM   836  C C   . PRO   A 1 171 ? 137.089 131.695 147.437 1.00 69.89  ? 163 PRO   A C   1 
ATOM   837  O O   . PRO   A 1 171 ? 136.357 132.670 147.646 1.00 75.62  ? 163 PRO   A O   1 
ATOM   838  C CB  . PRO   A 1 171 ? 138.937 132.346 145.854 1.00 57.06  ? 163 PRO   A CB  1 
ATOM   839  C CG  . PRO   A 1 171 ? 139.324 131.082 145.178 1.00 59.49  ? 163 PRO   A CG  1 
ATOM   840  C CD  . PRO   A 1 171 ? 140.004 130.242 146.219 1.00 54.91  ? 163 PRO   A CD  1 
ATOM   841  N N   . VAL   A 1 172 ? 136.610 130.454 147.330 1.00 72.78  ? 164 VAL   A N   1 
ATOM   842  C CA  . VAL   A 1 172 ? 135.176 130.199 147.439 1.00 72.40  ? 164 VAL   A CA  1 
ATOM   843  C C   . VAL   A 1 172 ? 134.697 130.396 148.875 1.00 76.63  ? 164 VAL   A C   1 
ATOM   844  O O   . VAL   A 1 172 ? 133.605 130.926 149.111 1.00 79.88  ? 164 VAL   A O   1 
ATOM   845  C CB  . VAL   A 1 172 ? 134.842 128.794 146.901 1.00 75.26  ? 164 VAL   A CB  1 
ATOM   846  C CG1 . VAL   A 1 172 ? 135.596 127.715 147.671 1.00 71.78  ? 164 VAL   A CG1 1 
ATOM   847  C CG2 . VAL   A 1 172 ? 133.342 128.546 146.945 1.00 73.49  ? 164 VAL   A CG2 1 
ATOM   848  N N   . LYS   A 1 173 ? 135.500 129.978 149.854 1.00 70.05  ? 165 LYS   A N   1 
ATOM   849  C CA  . LYS   A 1 173 ? 135.149 130.127 151.261 1.00 69.05  ? 165 LYS   A CA  1 
ATOM   850  C C   . LYS   A 1 173 ? 135.561 131.481 151.824 1.00 72.62  ? 165 LYS   A C   1 
ATOM   851  O O   . LYS   A 1 173 ? 134.939 131.970 152.778 1.00 77.70  ? 165 LYS   A O   1 
ATOM   852  C CB  . LYS   A 1 173 ? 135.783 128.987 152.070 1.00 68.57  ? 165 LYS   A CB  1 
ATOM   853  C CG  . LYS   A 1 173 ? 136.362 129.375 153.420 1.00 80.95  ? 165 LYS   A CG  1 
ATOM   854  C CD  . LYS   A 1 173 ? 136.751 128.146 154.224 1.00 82.51  ? 165 LYS   A CD  1 
ATOM   855  C CE  . LYS   A 1 173 ? 138.253 127.920 154.198 1.00 79.10  ? 165 LYS   A CE  1 
ATOM   856  N NZ  . LYS   A 1 173 ? 138.627 126.588 154.751 1.00 82.05  ? 165 LYS   A NZ  1 
ATOM   857  N N   . ALA   A 1 174 ? 136.575 132.113 151.227 1.00 67.04  ? 166 ALA   A N   1 
ATOM   858  C CA  . ALA   A 1 174 ? 137.053 133.402 151.709 1.00 70.52  ? 166 ALA   A CA  1 
ATOM   859  C C   . ALA   A 1 174 ? 135.988 134.488 151.640 1.00 75.39  ? 166 ALA   A C   1 
ATOM   860  O O   . ALA   A 1 174 ? 136.087 135.479 152.369 1.00 77.43  ? 166 ALA   A O   1 
ATOM   861  C CB  . ALA   A 1 174 ? 138.286 133.833 150.915 1.00 65.69  ? 166 ALA   A CB  1 
ATOM   862  N N   . LEU   A 1 175 ? 134.980 134.336 150.778 1.00 76.58  ? 167 LEU   A N   1 
ATOM   863  C CA  . LEU   A 1 175 ? 133.909 135.326 150.722 1.00 80.17  ? 167 LEU   A CA  1 
ATOM   864  C C   . LEU   A 1 175 ? 133.147 135.381 152.040 1.00 84.87  ? 167 LEU   A C   1 
ATOM   865  O O   . LEU   A 1 175 ? 132.867 136.464 152.566 1.00 85.51  ? 167 LEU   A O   1 
ATOM   866  C CB  . LEU   A 1 175 ? 132.963 135.009 149.564 1.00 76.32  ? 167 LEU   A CB  1 
ATOM   867  C CG  . LEU   A 1 175 ? 133.460 135.369 148.165 1.00 77.64  ? 167 LEU   A CG  1 
ATOM   868  C CD1 . LEU   A 1 175 ? 132.468 134.908 147.112 1.00 81.77  ? 167 LEU   A CD1 1 
ATOM   869  C CD2 . LEU   A 1 175 ? 133.701 136.865 148.058 1.00 78.16  ? 167 LEU   A CD2 1 
ATOM   870  N N   . ASP   A 1 176 ? 132.801 134.216 152.587 1.00 85.64  ? 168 ASP   A N   1 
ATOM   871  C CA  . ASP   A 1 176 ? 132.116 134.166 153.874 1.00 86.67  ? 168 ASP   A CA  1 
ATOM   872  C C   . ASP   A 1 176 ? 133.078 134.385 155.036 1.00 84.20  ? 168 ASP   A C   1 
ATOM   873  O O   . ASP   A 1 176 ? 132.719 135.032 156.027 1.00 81.33  ? 168 ASP   A O   1 
ATOM   874  C CB  . ASP   A 1 176 ? 131.392 132.829 154.028 1.00 91.93  ? 168 ASP   A CB  1 
ATOM   875  C CG  . ASP   A 1 176 ? 130.420 132.823 155.192 1.00 99.95  ? 168 ASP   A CG  1 
ATOM   876  O OD1 . ASP   A 1 176 ? 130.062 133.916 155.677 1.00 104.43 ? 168 ASP   A OD1 1 
ATOM   877  O OD2 . ASP   A 1 176 ? 130.013 131.722 155.621 1.00 95.62  ? 168 ASP   A OD2 1 
ATOM   878  N N   . PHE   A 1 177 ? 134.300 133.856 154.938 1.00 80.79  ? 169 PHE   A N   1 
ATOM   879  C CA  . PHE   A 1 177 ? 135.201 133.876 156.088 1.00 77.66  ? 169 PHE   A CA  1 
ATOM   880  C C   . PHE   A 1 177 ? 135.758 135.276 156.332 1.00 75.15  ? 169 PHE   A C   1 
ATOM   881  O O   . PHE   A 1 177 ? 135.792 135.745 157.475 1.00 76.32  ? 169 PHE   A O   1 
ATOM   882  C CB  . PHE   A 1 177 ? 136.323 132.850 155.870 1.00 77.92  ? 169 PHE   A CB  1 
ATOM   883  C CG  . PHE   A 1 177 ? 137.120 132.499 157.117 1.00 81.76  ? 169 PHE   A CG  1 
ATOM   884  C CD1 . PHE   A 1 177 ? 137.539 131.194 157.318 1.00 85.65  ? 169 PHE   A CD1 1 
ATOM   885  C CD2 . PHE   A 1 177 ? 137.481 133.452 158.058 1.00 78.66  ? 169 PHE   A CD2 1 
ATOM   886  C CE1 . PHE   A 1 177 ? 138.269 130.845 158.438 1.00 90.79  ? 169 PHE   A CE1 1 
ATOM   887  C CE2 . PHE   A 1 177 ? 138.214 133.108 159.179 1.00 81.21  ? 169 PHE   A CE2 1 
ATOM   888  C CZ  . PHE   A 1 177 ? 138.609 131.803 159.367 1.00 84.67  ? 169 PHE   A CZ  1 
ATOM   889  N N   . ARG   A 1 178 ? 136.149 135.983 155.271 1.00 73.10  ? 170 ARG   A N   1 
ATOM   890  C CA  . ARG   A 1 178 ? 137.011 137.153 155.398 1.00 70.59  ? 170 ARG   A CA  1 
ATOM   891  C C   . ARG   A 1 178 ? 136.240 138.454 155.587 1.00 73.05  ? 170 ARG   A C   1 
ATOM   892  O O   . ARG   A 1 178 ? 136.714 139.515 155.160 1.00 74.68  ? 170 ARG   A O   1 
ATOM   893  C CB  . ARG   A 1 178 ? 137.933 137.252 154.182 1.00 67.98  ? 170 ARG   A CB  1 
ATOM   894  C CG  . ARG   A 1 178 ? 138.826 136.037 153.995 1.00 65.05  ? 170 ARG   A CG  1 
ATOM   895  C CD  . ARG   A 1 178 ? 140.085 136.385 153.225 1.00 60.33  ? 170 ARG   A CD  1 
ATOM   896  N NE  . ARG   A 1 178 ? 140.668 137.646 153.664 1.00 62.33  ? 170 ARG   A NE  1 
ATOM   897  C CZ  . ARG   A 1 178 ? 141.050 138.616 152.846 1.00 62.34  ? 170 ARG   A CZ  1 
ATOM   898  N NH1 . ARG   A 1 178 ? 140.928 138.502 151.535 1.00 60.23  ? 170 ARG   A NH1 1 
ATOM   899  N NH2 . ARG   A 1 178 ? 141.569 139.728 153.357 1.00 61.88  ? 170 ARG   A NH2 1 
ATOM   900  N N   . THR   A 1 179 ? 135.065 138.407 156.209 1.00 69.80  ? 171 THR   A N   1 
ATOM   901  C CA  . THR   A 1 179 ? 134.374 139.635 156.566 1.00 66.25  ? 171 THR   A CA  1 
ATOM   902  C C   . THR   A 1 179 ? 135.080 140.312 157.743 1.00 59.73  ? 171 THR   A C   1 
ATOM   903  O O   . THR   A 1 179 ? 135.620 139.638 158.623 1.00 61.48  ? 171 THR   A O   1 
ATOM   904  C CB  . THR   A 1 179 ? 132.920 139.350 156.929 1.00 70.55  ? 171 THR   A CB  1 
ATOM   905  O OG1 . THR   A 1 179 ? 132.857 138.759 158.232 1.00 72.63  ? 171 THR   A OG1 1 
ATOM   906  C CG2 . THR   A 1 179 ? 132.297 138.402 155.920 1.00 72.01  ? 171 THR   A CG2 1 
ATOM   907  N N   . PRO   A 1 180 ? 135.096 141.647 157.774 1.00 57.89  ? 172 PRO   A N   1 
ATOM   908  C CA  . PRO   A 1 180 ? 135.783 142.346 158.875 1.00 58.16  ? 172 PRO   A CA  1 
ATOM   909  C C   . PRO   A 1 180 ? 135.213 142.044 160.252 1.00 58.02  ? 172 PRO   A C   1 
ATOM   910  O O   . PRO   A 1 180 ? 135.954 142.103 161.241 1.00 60.49  ? 172 PRO   A O   1 
ATOM   911  C CB  . PRO   A 1 180 ? 135.613 143.827 158.509 1.00 61.02  ? 172 PRO   A CB  1 
ATOM   912  C CG  . PRO   A 1 180 ? 135.375 143.832 157.037 1.00 64.88  ? 172 PRO   A CG  1 
ATOM   913  C CD  . PRO   A 1 180 ? 134.608 142.579 156.745 1.00 65.59  ? 172 PRO   A CD  1 
ATOM   914  N N   . LEU   A 1 181 ? 133.916 141.743 160.352 1.00 56.82  ? 173 LEU   A N   1 
ATOM   915  C CA  . LEU   A 1 181 ? 133.334 141.412 161.649 1.00 56.52  ? 173 LEU   A CA  1 
ATOM   916  C C   . LEU   A 1 181 ? 133.959 140.147 162.226 1.00 56.98  ? 173 LEU   A C   1 
ATOM   917  O O   . LEU   A 1 181 ? 134.257 140.079 163.426 1.00 54.00  ? 173 LEU   A O   1 
ATOM   918  C CB  . LEU   A 1 181 ? 131.820 141.254 161.516 1.00 58.97  ? 173 LEU   A CB  1 
ATOM   919  C CG  . LEU   A 1 181 ? 131.038 140.989 162.802 1.00 60.38  ? 173 LEU   A CG  1 
ATOM   920  C CD1 . LEU   A 1 181 ? 131.393 142.015 163.865 1.00 63.11  ? 173 LEU   A CD1 1 
ATOM   921  C CD2 . LEU   A 1 181 ? 129.545 140.995 162.525 1.00 56.92  ? 173 LEU   A CD2 1 
ATOM   922  N N   . LYS   A 1 182 ? 134.163 139.132 161.383 1.00 54.76  ? 174 LYS   A N   1 
ATOM   923  C CA  . LYS   A 1 182 ? 134.857 137.932 161.833 1.00 50.53  ? 174 LYS   A CA  1 
ATOM   924  C C   . LYS   A 1 182 ? 136.292 138.239 162.232 1.00 49.23  ? 174 LYS   A C   1 
ATOM   925  O O   . LYS   A 1 182 ? 136.815 137.631 163.170 1.00 52.13  ? 174 LYS   A O   1 
ATOM   926  C CB  . LYS   A 1 182 ? 134.823 136.861 160.744 1.00 51.94  ? 174 LYS   A CB  1 
ATOM   927  C CG  . LYS   A 1 182 ? 133.423 136.417 160.362 1.00 59.28  ? 174 LYS   A CG  1 
ATOM   928  C CD  . LYS   A 1 182 ? 132.703 135.784 161.539 1.00 61.69  ? 174 LYS   A CD  1 
ATOM   929  C CE  . LYS   A 1 182 ? 133.259 134.404 161.846 1.00 66.31  ? 174 LYS   A CE  1 
ATOM   930  N NZ  . LYS   A 1 182 ? 132.875 133.411 160.806 1.00 77.11  ? 174 LYS   A NZ  1 
ATOM   931  N N   . ALA   A 1 183 ? 136.941 139.176 161.539 1.00 46.59  ? 175 ALA   A N   1 
ATOM   932  C CA  . ALA   A 1 183 ? 138.289 139.577 161.927 1.00 42.28  ? 175 ALA   A CA  1 
ATOM   933  C C   . ALA   A 1 183 ? 138.299 140.212 163.311 1.00 45.24  ? 175 ALA   A C   1 
ATOM   934  O O   . ALA   A 1 183 ? 139.186 139.931 164.124 1.00 48.32  ? 175 ALA   A O   1 
ATOM   935  C CB  . ALA   A 1 183 ? 138.871 140.537 160.891 1.00 45.68  ? 175 ALA   A CB  1 
ATOM   936  N N   . LYS   A 1 184 ? 137.321 141.074 163.599 1.00 46.02  ? 176 LYS   A N   1 
ATOM   937  C CA  . LYS   A 1 184 ? 137.228 141.672 164.928 1.00 44.22  ? 176 LYS   A CA  1 
ATOM   938  C C   . LYS   A 1 184 ? 136.973 140.614 165.994 1.00 44.26  ? 176 LYS   A C   1 
ATOM   939  O O   . LYS   A 1 184 ? 137.579 140.645 167.074 1.00 47.15  ? 176 LYS   A O   1 
ATOM   940  C CB  . LYS   A 1 184 ? 136.124 142.727 164.954 1.00 48.43  ? 176 LYS   A CB  1 
ATOM   941  C CG  . LYS   A 1 184 ? 136.497 144.041 164.300 1.00 55.62  ? 176 LYS   A CG  1 
ATOM   942  C CD  . LYS   A 1 184 ? 135.266 144.899 164.067 1.00 64.93  ? 176 LYS   A CD  1 
ATOM   943  C CE  . LYS   A 1 184 ? 134.480 145.092 165.353 1.00 73.54  ? 176 LYS   A CE  1 
ATOM   944  N NZ  . LYS   A 1 184 ? 133.389 146.092 165.191 1.00 83.93  ? 176 LYS   A NZ  1 
ATOM   945  N N   . ILE   A 1 185 ? 136.075 139.669 165.709 1.00 43.29  ? 177 ILE   A N   1 
ATOM   946  C CA  . ILE   A 1 185 ? 135.785 138.605 166.667 1.00 41.21  ? 177 ILE   A CA  1 
ATOM   947  C C   . ILE   A 1 185 ? 137.032 137.767 166.924 1.00 40.72  ? 177 ILE   A C   1 
ATOM   948  O O   . ILE   A 1 185 ? 137.325 137.394 168.066 1.00 45.63  ? 177 ILE   A O   1 
ATOM   949  C CB  . ILE   A 1 185 ? 134.610 137.745 166.169 1.00 40.16  ? 177 ILE   A CB  1 
ATOM   950  C CG1 . ILE   A 1 185 ? 133.298 138.520 166.294 1.00 44.10  ? 177 ILE   A CG1 1 
ATOM   951  C CG2 . ILE   A 1 185 ? 134.529 136.442 166.945 1.00 35.67  ? 177 ILE   A CG2 1 
ATOM   952  C CD1 . ILE   A 1 185 ? 132.264 138.140 165.259 1.00 49.06  ? 177 ILE   A CD1 1 
ATOM   953  N N   . ILE   A 1 186 ? 137.791 137.468 165.868 1.00 41.68  ? 178 ILE   A N   1 
ATOM   954  C CA  . ILE   A 1 186 ? 139.014 136.690 166.022 1.00 41.85  ? 178 ILE   A CA  1 
ATOM   955  C C   . ILE   A 1 186 ? 140.056 137.475 166.810 1.00 42.18  ? 178 ILE   A C   1 
ATOM   956  O O   . ILE   A 1 186 ? 140.813 136.902 167.598 1.00 47.29  ? 178 ILE   A O   1 
ATOM   957  C CB  . ILE   A 1 186 ? 139.538 136.253 164.641 1.00 36.63  ? 178 ILE   A CB  1 
ATOM   958  C CG1 . ILE   A 1 186 ? 138.786 135.010 164.164 1.00 36.20  ? 178 ILE   A CG1 1 
ATOM   959  C CG2 . ILE   A 1 186 ? 141.032 135.979 164.678 1.00 34.26  ? 178 ILE   A CG2 1 
ATOM   960  C CD1 . ILE   A 1 186 ? 138.971 134.711 162.698 1.00 42.60  ? 178 ILE   A CD1 1 
ATOM   961  N N   . ASN   A 1 187 ? 140.111 138.795 166.619 1.00 40.43  ? 179 ASN   A N   1 
ATOM   962  C CA  . ASN   A 1 187 ? 141.028 139.613 167.409 1.00 41.66  ? 179 ASN   A CA  1 
ATOM   963  C C   . ASN   A 1 187 ? 140.671 139.571 168.891 1.00 44.61  ? 179 ASN   A C   1 
ATOM   964  O O   . ASN   A 1 187 ? 141.555 139.450 169.751 1.00 48.36  ? 179 ASN   A O   1 
ATOM   965  C CB  . ASN   A 1 187 ? 141.017 141.052 166.900 1.00 41.85  ? 179 ASN   A CB  1 
ATOM   966  C CG  . ASN   A 1 187 ? 141.931 141.255 165.716 1.00 41.50  ? 179 ASN   A CG  1 
ATOM   967  O OD1 . ASN   A 1 187 ? 142.553 140.313 165.230 1.00 46.38  ? 179 ASN   A OD1 1 
ATOM   968  N ND2 . ASN   A 1 187 ? 142.018 142.490 165.242 1.00 38.69  ? 179 ASN   A ND2 1 
ATOM   969  N N   . ILE   A 1 188 ? 139.378 139.672 169.207 1.00 46.50  ? 180 ILE   A N   1 
ATOM   970  C CA  . ILE   A 1 188 ? 138.952 139.575 170.602 1.00 43.03  ? 180 ILE   A CA  1 
ATOM   971  C C   . ILE   A 1 188 ? 139.287 138.200 171.167 1.00 45.21  ? 180 ILE   A C   1 
ATOM   972  O O   . ILE   A 1 188 ? 139.746 138.075 172.310 1.00 45.34  ? 180 ILE   A O   1 
ATOM   973  C CB  . ILE   A 1 188 ? 137.452 139.897 170.737 1.00 38.21  ? 180 ILE   A CB  1 
ATOM   974  C CG1 . ILE   A 1 188 ? 137.185 141.369 170.415 1.00 35.74  ? 180 ILE   A CG1 1 
ATOM   975  C CG2 . ILE   A 1 188 ? 136.952 139.559 172.130 1.00 45.68  ? 180 ILE   A CG2 1 
ATOM   976  C CD1 . ILE   A 1 188 ? 135.960 141.599 169.566 1.00 39.11  ? 180 ILE   A CD1 1 
ATOM   977  N N   . CYS   A 1 189 ? 139.070 137.148 170.375 1.00 45.49  ? 181 CYS   A N   1 
ATOM   978  C CA  . CYS   A 1 189 ? 139.389 135.797 170.829 1.00 45.34  ? 181 CYS   A CA  1 
ATOM   979  C C   . CYS   A 1 189 ? 140.886 135.627 171.056 1.00 44.84  ? 181 CYS   A C   1 
ATOM   980  O O   . CYS   A 1 189 ? 141.304 134.923 171.982 1.00 45.73  ? 181 CYS   A O   1 
ATOM   981  C CB  . CYS   A 1 189 ? 138.878 134.772 169.818 1.00 46.92  ? 181 CYS   A CB  1 
ATOM   982  S SG  . CYS   A 1 189 ? 137.079 134.611 169.769 1.00 82.47  ? 181 CYS   A SG  1 
ATOM   983  N N   . ILE   A 1 190 ? 141.709 136.250 170.211 1.00 44.42  ? 182 ILE   A N   1 
ATOM   984  C CA  . ILE   A 1 190 ? 143.156 136.194 170.387 1.00 45.33  ? 182 ILE   A CA  1 
ATOM   985  C C   . ILE   A 1 190 ? 143.563 136.896 171.675 1.00 43.20  ? 182 ILE   A C   1 
ATOM   986  O O   . ILE   A 1 190 ? 144.399 136.393 172.435 1.00 45.89  ? 182 ILE   A O   1 
ATOM   987  C CB  . ILE   A 1 190 ? 143.865 136.805 169.165 1.00 44.01  ? 182 ILE   A CB  1 
ATOM   988  C CG1 . ILE   A 1 190 ? 143.864 135.824 167.995 1.00 42.41  ? 182 ILE   A CG1 1 
ATOM   989  C CG2 . ILE   A 1 190 ? 145.288 137.210 169.511 1.00 42.51  ? 182 ILE   A CG2 1 
ATOM   990  C CD1 . ILE   A 1 190 ? 144.179 136.474 166.673 1.00 39.17  ? 182 ILE   A CD1 1 
ATOM   991  N N   . TRP   A 1 191 ? 142.984 138.069 171.940 1.00 41.88  ? 183 TRP   A N   1 
ATOM   992  C CA  . TRP   A 1 191 ? 143.305 138.776 173.176 1.00 43.45  ? 183 TRP   A CA  1 
ATOM   993  C C   . TRP   A 1 191 ? 142.871 137.975 174.397 1.00 48.38  ? 183 TRP   A C   1 
ATOM   994  O O   . TRP   A 1 191 ? 143.564 137.966 175.421 1.00 49.93  ? 183 TRP   A O   1 
ATOM   995  C CB  . TRP   A 1 191 ? 142.660 140.161 173.179 1.00 40.94  ? 183 TRP   A CB  1 
ATOM   996  C CG  . TRP   A 1 191 ? 143.511 141.208 172.534 1.00 43.42  ? 183 TRP   A CG  1 
ATOM   997  C CD1 . TRP   A 1 191 ? 143.363 141.725 171.284 1.00 44.36  ? 183 TRP   A CD1 1 
ATOM   998  C CD2 . TRP   A 1 191 ? 144.652 141.860 173.106 1.00 42.99  ? 183 TRP   A CD2 1 
ATOM   999  N NE1 . TRP   A 1 191 ? 144.337 142.662 171.040 1.00 44.15  ? 183 TRP   A NE1 1 
ATOM   1000 C CE2 . TRP   A 1 191 ? 145.141 142.762 172.143 1.00 42.81  ? 183 TRP   A CE2 1 
ATOM   1001 C CE3 . TRP   A 1 191 ? 145.305 141.768 174.337 1.00 40.87  ? 183 TRP   A CE3 1 
ATOM   1002 C CZ2 . TRP   A 1 191 ? 146.252 143.569 172.373 1.00 39.72  ? 183 TRP   A CZ2 1 
ATOM   1003 C CZ3 . TRP   A 1 191 ? 146.408 142.569 174.563 1.00 40.32  ? 183 TRP   A CZ3 1 
ATOM   1004 C CH2 . TRP   A 1 191 ? 146.870 143.457 173.587 1.00 37.76  ? 183 TRP   A CH2 1 
ATOM   1005 N N   . LEU   A 1 192 ? 141.723 137.301 174.312 1.00 49.25  ? 184 LEU   A N   1 
ATOM   1006 C CA  . LEU   A 1 192 ? 141.276 136.463 175.421 1.00 44.02  ? 184 LEU   A CA  1 
ATOM   1007 C C   . LEU   A 1 192 ? 142.187 135.255 175.611 1.00 44.96  ? 184 LEU   A C   1 
ATOM   1008 O O   . LEU   A 1 192 ? 142.456 134.848 176.746 1.00 50.39  ? 184 LEU   A O   1 
ATOM   1009 C CB  . LEU   A 1 192 ? 139.832 136.016 175.198 1.00 40.81  ? 184 LEU   A CB  1 
ATOM   1010 C CG  . LEU   A 1 192 ? 138.764 137.108 175.268 1.00 46.02  ? 184 LEU   A CG  1 
ATOM   1011 C CD1 . LEU   A 1 192 ? 137.395 136.537 174.938 1.00 49.57  ? 184 LEU   A CD1 1 
ATOM   1012 C CD2 . LEU   A 1 192 ? 138.758 137.773 176.634 1.00 49.55  ? 184 LEU   A CD2 1 
ATOM   1013 N N   . LEU   A 1 193 ? 142.656 134.658 174.512 1.00 47.19  ? 185 LEU   A N   1 
ATOM   1014 C CA  . LEU   A 1 193 ? 143.535 133.497 174.615 1.00 47.91  ? 185 LEU   A CA  1 
ATOM   1015 C C   . LEU   A 1 193 ? 144.860 133.860 175.270 1.00 54.58  ? 185 LEU   A C   1 
ATOM   1016 O O   . LEU   A 1 193 ? 145.367 133.117 176.118 1.00 57.39  ? 185 LEU   A O   1 
ATOM   1017 C CB  . LEU   A 1 193 ? 143.774 132.896 173.230 1.00 45.11  ? 185 LEU   A CB  1 
ATOM   1018 C CG  . LEU   A 1 193 ? 143.556 131.390 173.085 1.00 48.59  ? 185 LEU   A CG  1 
ATOM   1019 C CD1 . LEU   A 1 193 ? 142.154 131.006 173.530 1.00 50.65  ? 185 LEU   A CD1 1 
ATOM   1020 C CD2 . LEU   A 1 193 ? 143.806 130.952 171.653 1.00 47.38  ? 185 LEU   A CD2 1 
ATOM   1021 N N   . ALA   A 1 194 ? 145.440 134.999 174.885 1.00 53.76  ? 186 ALA   A N   1 
ATOM   1022 C CA  . ALA   A 1 194 ? 146.688 135.444 175.491 1.00 46.35  ? 186 ALA   A CA  1 
ATOM   1023 C C   . ALA   A 1 194 ? 146.502 135.883 176.936 1.00 48.22  ? 186 ALA   A C   1 
ATOM   1024 O O   . ALA   A 1 194 ? 147.492 136.004 177.665 1.00 51.93  ? 186 ALA   A O   1 
ATOM   1025 C CB  . ALA   A 1 194 ? 147.294 136.585 174.674 1.00 44.64  ? 186 ALA   A CB  1 
ATOM   1026 N N   . SER   A 1 195 ? 145.261 136.127 177.365 1.00 47.05  ? 187 SER   A N   1 
ATOM   1027 C CA  . SER   A 1 195 ? 145.006 136.524 178.744 1.00 50.25  ? 187 SER   A CA  1 
ATOM   1028 C C   . SER   A 1 195 ? 145.309 135.409 179.734 1.00 51.37  ? 187 SER   A C   1 
ATOM   1029 O O   . SER   A 1 195 ? 145.450 135.683 180.929 1.00 55.85  ? 187 SER   A O   1 
ATOM   1030 C CB  . SER   A 1 195 ? 143.555 136.977 178.902 1.00 51.26  ? 187 SER   A CB  1 
ATOM   1031 O OG  . SER   A 1 195 ? 143.325 138.185 178.198 1.00 53.10  ? 187 SER   A OG  1 
ATOM   1032 N N   . SER   A 1 196 ? 145.407 134.162 179.269 1.00 46.86  ? 188 SER   A N   1 
ATOM   1033 C CA  . SER   A 1 196 ? 145.802 133.078 180.160 1.00 49.35  ? 188 SER   A CA  1 
ATOM   1034 C C   . SER   A 1 196 ? 147.240 133.243 180.632 1.00 54.68  ? 188 SER   A C   1 
ATOM   1035 O O   . SER   A 1 196 ? 147.641 132.632 181.628 1.00 59.69  ? 188 SER   A O   1 
ATOM   1036 C CB  . SER   A 1 196 ? 145.621 131.732 179.461 1.00 52.07  ? 188 SER   A CB  1 
ATOM   1037 O OG  . SER   A 1 196 ? 146.436 131.645 178.306 1.00 60.87  ? 188 SER   A OG  1 
ATOM   1038 N N   . VAL   A 1 197 ? 148.030 134.056 179.931 1.00 57.28  ? 189 VAL   A N   1 
ATOM   1039 C CA  . VAL   A 1 197 ? 149.409 134.323 180.320 1.00 54.86  ? 189 VAL   A CA  1 
ATOM   1040 C C   . VAL   A 1 197 ? 149.502 135.722 180.916 1.00 53.10  ? 189 VAL   A C   1 
ATOM   1041 O O   . VAL   A 1 197 ? 150.296 135.963 181.831 1.00 58.40  ? 189 VAL   A O   1 
ATOM   1042 C CB  . VAL   A 1 197 ? 150.367 134.165 179.125 1.00 50.44  ? 189 VAL   A CB  1 
ATOM   1043 C CG1 . VAL   A 1 197 ? 151.803 134.076 179.607 1.00 50.57  ? 189 VAL   A CG1 1 
ATOM   1044 C CG2 . VAL   A 1 197 ? 149.997 132.936 178.314 1.00 49.66  ? 189 VAL   A CG2 1 
ATOM   1045 N N   . GLY   A 1 198 ? 148.698 136.654 180.401 1.00 46.85  ? 190 GLY   A N   1 
ATOM   1046 C CA  . GLY   A 1 198 ? 148.707 138.001 180.951 1.00 46.84  ? 190 GLY   A CA  1 
ATOM   1047 C C   . GLY   A 1 198 ? 148.183 138.056 182.375 1.00 54.07  ? 190 GLY   A C   1 
ATOM   1048 O O   . GLY   A 1 198 ? 148.781 138.693 183.247 1.00 58.79  ? 190 GLY   A O   1 
ATOM   1049 N N   . ILE   A 1 199 ? 147.064 137.378 182.634 1.00 53.90  ? 191 ILE   A N   1 
ATOM   1050 C CA  . ILE   A 1 199 ? 146.518 137.344 183.987 1.00 52.72  ? 191 ILE   A CA  1 
ATOM   1051 C C   . ILE   A 1 199 ? 147.436 136.551 184.910 1.00 51.78  ? 191 ILE   A C   1 
ATOM   1052 O O   . ILE   A 1 199 ? 147.595 136.886 186.090 1.00 50.22  ? 191 ILE   A O   1 
ATOM   1053 C CB  . ILE   A 1 199 ? 145.088 136.775 183.970 1.00 52.72  ? 191 ILE   A CB  1 
ATOM   1054 C CG1 . ILE   A 1 199 ? 144.156 137.716 183.207 1.00 52.52  ? 191 ILE   A CG1 1 
ATOM   1055 C CG2 . ILE   A 1 199 ? 144.570 136.564 185.382 1.00 53.46  ? 191 ILE   A CG2 1 
ATOM   1056 C CD1 . ILE   A 1 199 ? 142.748 137.192 183.063 1.00 61.96  ? 191 ILE   A CD1 1 
ATOM   1057 N N   . SER   A 1 200 ? 148.058 135.492 184.388 1.00 52.07  ? 192 SER   A N   1 
ATOM   1058 C CA  . SER   A 1 200 ? 149.022 134.740 185.183 1.00 52.53  ? 192 SER   A CA  1 
ATOM   1059 C C   . SER   A 1 200 ? 150.215 135.606 185.564 1.00 47.01  ? 192 SER   A C   1 
ATOM   1060 O O   . SER   A 1 200 ? 150.727 135.512 186.684 1.00 45.86  ? 192 SER   A O   1 
ATOM   1061 C CB  . SER   A 1 200 ? 149.480 133.500 184.417 1.00 58.31  ? 192 SER   A CB  1 
ATOM   1062 O OG  . SER   A 1 200 ? 148.401 132.910 183.715 1.00 56.32  ? 192 SER   A OG  1 
ATOM   1063 N N   . ALA   A 1 201 ? 150.677 136.452 184.642 1.00 48.29  ? 193 ALA   A N   1 
ATOM   1064 C CA  . ALA   A 1 201 ? 151.774 137.363 184.950 1.00 45.61  ? 193 ALA   A CA  1 
ATOM   1065 C C   . ALA   A 1 201 ? 151.341 138.433 185.943 1.00 45.60  ? 193 ALA   A C   1 
ATOM   1066 O O   . ALA   A 1 201 ? 152.136 138.866 186.784 1.00 46.68  ? 193 ALA   A O   1 
ATOM   1067 C CB  . ALA   A 1 201 ? 152.302 138.002 183.668 1.00 42.10  ? 193 ALA   A CB  1 
ATOM   1068 N N   . ILE   A 1 202 ? 150.088 138.883 185.849 1.00 46.85  ? 194 ILE   A N   1 
ATOM   1069 C CA  . ILE   A 1 202 ? 149.561 139.824 186.834 1.00 44.99  ? 194 ILE   A CA  1 
ATOM   1070 C C   . ILE   A 1 202 ? 149.567 139.197 188.222 1.00 44.08  ? 194 ILE   A C   1 
ATOM   1071 O O   . ILE   A 1 202 ? 149.968 139.829 189.206 1.00 45.28  ? 194 ILE   A O   1 
ATOM   1072 C CB  . ILE   A 1 202 ? 148.148 140.287 186.431 1.00 44.32  ? 194 ILE   A CB  1 
ATOM   1073 C CG1 . ILE   A 1 202 ? 148.220 141.317 185.303 1.00 44.35  ? 194 ILE   A CG1 1 
ATOM   1074 C CG2 . ILE   A 1 202 ? 147.397 140.839 187.633 1.00 46.66  ? 194 ILE   A CG2 1 
ATOM   1075 C CD1 . ILE   A 1 202 ? 148.272 142.753 185.777 1.00 43.78  ? 194 ILE   A CD1 1 
ATOM   1076 N N   . VAL   A 1 203 ? 149.124 137.944 188.321 1.00 46.80  ? 195 VAL   A N   1 
ATOM   1077 C CA  . VAL   A 1 203 ? 149.046 137.276 189.618 1.00 45.23  ? 195 VAL   A CA  1 
ATOM   1078 C C   . VAL   A 1 203 ? 150.441 136.999 190.168 1.00 44.76  ? 195 VAL   A C   1 
ATOM   1079 O O   . VAL   A 1 203 ? 150.731 137.277 191.338 1.00 45.98  ? 195 VAL   A O   1 
ATOM   1080 C CB  . VAL   A 1 203 ? 148.221 135.983 189.501 1.00 44.82  ? 195 VAL   A CB  1 
ATOM   1081 C CG1 . VAL   A 1 203 ? 148.438 135.102 190.719 1.00 43.93  ? 195 VAL   A CG1 1 
ATOM   1082 C CG2 . VAL   A 1 203 ? 146.747 136.308 189.327 1.00 44.23  ? 195 VAL   A CG2 1 
ATOM   1083 N N   . LEU   A 1 204 ? 151.327 136.455 189.334 1.00 46.29  ? 196 LEU   A N   1 
ATOM   1084 C CA  . LEU   A 1 204 ? 152.633 135.988 189.784 1.00 41.47  ? 196 LEU   A CA  1 
ATOM   1085 C C   . LEU   A 1 204 ? 153.699 137.073 189.784 1.00 42.40  ? 196 LEU   A C   1 
ATOM   1086 O O   . LEU   A 1 204 ? 154.669 136.968 190.542 1.00 47.03  ? 196 LEU   A O   1 
ATOM   1087 C CB  . LEU   A 1 204 ? 153.111 134.829 188.907 1.00 39.75  ? 196 LEU   A CB  1 
ATOM   1088 C CG  . LEU   A 1 204 ? 152.339 133.515 188.990 1.00 39.45  ? 196 LEU   A CG  1 
ATOM   1089 C CD1 . LEU   A 1 204 ? 152.835 132.554 187.926 1.00 40.12  ? 196 LEU   A CD1 1 
ATOM   1090 C CD2 . LEU   A 1 204 ? 152.474 132.904 190.370 1.00 42.03  ? 196 LEU   A CD2 1 
ATOM   1091 N N   . GLY   A 1 205 ? 153.554 138.099 188.949 1.00 42.44  ? 197 GLY   A N   1 
ATOM   1092 C CA  . GLY   A 1 205 ? 154.574 139.128 188.877 1.00 43.76  ? 197 GLY   A CA  1 
ATOM   1093 C C   . GLY   A 1 205 ? 154.750 139.843 190.201 1.00 49.17  ? 197 GLY   A C   1 
ATOM   1094 O O   . GLY   A 1 205 ? 153.804 140.025 190.969 1.00 56.55  ? 197 GLY   A O   1 
ATOM   1095 N N   . GLY   A 1 206 ? 155.984 140.241 190.475 1.00 48.95  ? 198 GLY   A N   1 
ATOM   1096 C CA  . GLY   A 1 206 ? 156.281 140.917 191.723 1.00 55.06  ? 198 GLY   A CA  1 
ATOM   1097 C C   . GLY   A 1 206 ? 157.741 141.300 191.786 1.00 60.87  ? 198 GLY   A C   1 
ATOM   1098 O O   . GLY   A 1 206 ? 158.541 140.951 190.913 1.00 61.12  ? 198 GLY   A O   1 
ATOM   1099 N N   . THR   A 1 207 ? 158.076 142.029 192.846 1.00 61.21  ? 199 THR   A N   1 
ATOM   1100 C CA  . THR   A 1 207 ? 159.432 142.497 193.088 1.00 59.56  ? 199 THR   A CA  1 
ATOM   1101 C C   . THR   A 1 207 ? 160.004 141.779 194.301 1.00 58.58  ? 199 THR   A C   1 
ATOM   1102 O O   . THR   A 1 207 ? 159.384 141.767 195.370 1.00 58.70  ? 199 THR   A O   1 
ATOM   1103 C CB  . THR   A 1 207 ? 159.462 144.010 193.311 1.00 56.44  ? 199 THR   A CB  1 
ATOM   1104 O OG1 . THR   A 1 207 ? 158.484 144.370 194.293 1.00 60.05  ? 199 THR   A OG1 1 
ATOM   1105 C CG2 . THR   A 1 207 ? 159.160 144.742 192.019 1.00 50.65  ? 199 THR   A CG2 1 
ATOM   1106 N N   . LYS   A 1 208 ? 161.180 141.182 194.133 1.00 58.47  ? 200 LYS   A N   1 
ATOM   1107 C CA  . LYS   A 1 208 ? 161.881 140.506 195.215 1.00 60.57  ? 200 LYS   A CA  1 
ATOM   1108 C C   . LYS   A 1 208 ? 163.276 141.095 195.337 1.00 63.18  ? 200 LYS   A C   1 
ATOM   1109 O O   . LYS   A 1 208 ? 163.993 141.213 194.338 1.00 59.63  ? 200 LYS   A O   1 
ATOM   1110 C CB  . LYS   A 1 208 ? 161.962 138.997 194.970 1.00 65.49  ? 200 LYS   A CB  1 
ATOM   1111 C CG  . LYS   A 1 208 ? 162.497 138.208 196.152 1.00 68.66  ? 200 LYS   A CG  1 
ATOM   1112 C CD  . LYS   A 1 208 ? 162.805 136.772 195.764 1.00 70.17  ? 200 LYS   A CD  1 
ATOM   1113 C CE  . LYS   A 1 208 ? 163.246 135.960 196.970 1.00 88.93  ? 200 LYS   A CE  1 
ATOM   1114 N NZ  . LYS   A 1 208 ? 164.533 136.454 197.532 1.00 96.12  ? 200 LYS   A NZ  1 
ATOM   1115 N N   . VAL   A 1 209 ? 163.659 141.458 196.554 1.00 69.04  ? 201 VAL   A N   1 
ATOM   1116 C CA  . VAL   A 1 209 ? 164.968 142.049 196.798 1.00 71.97  ? 201 VAL   A CA  1 
ATOM   1117 C C   . VAL   A 1 209 ? 166.023 140.952 196.825 1.00 79.13  ? 201 VAL   A C   1 
ATOM   1118 O O   . VAL   A 1 209 ? 165.758 139.816 197.241 1.00 77.66  ? 201 VAL   A O   1 
ATOM   1119 C CB  . VAL   A 1 209 ? 164.960 142.863 198.104 1.00 69.92  ? 201 VAL   A CB  1 
ATOM   1120 C CG1 . VAL   A 1 209 ? 163.769 143.804 198.127 1.00 65.03  ? 201 VAL   A CG1 1 
ATOM   1121 C CG2 . VAL   A 1 209 ? 164.928 141.945 199.315 1.00 74.07  ? 201 VAL   A CG2 1 
ATOM   1122 N N   . ARG   A 1 210 ? 167.221 141.281 196.352 1.00 85.59  ? 202 ARG   A N   1 
ATOM   1123 C CA  . ARG   A 1 210 ? 168.334 140.344 196.388 1.00 90.09  ? 202 ARG   A CA  1 
ATOM   1124 C C   . ARG   A 1 210 ? 169.038 140.439 197.735 1.00 100.44 ? 202 ARG   A C   1 
ATOM   1125 O O   . ARG   A 1 210 ? 169.404 141.531 198.179 1.00 99.81  ? 202 ARG   A O   1 
ATOM   1126 C CB  . ARG   A 1 210 ? 169.314 140.632 195.252 1.00 89.75  ? 202 ARG   A CB  1 
ATOM   1127 C CG  . ARG   A 1 210 ? 169.072 139.807 194.002 1.00 89.53  ? 202 ARG   A CG  1 
ATOM   1128 C CD  . ARG   A 1 210 ? 169.597 140.516 192.766 1.00 93.18  ? 202 ARG   A CD  1 
ATOM   1129 N NE  . ARG   A 1 210 ? 170.123 139.580 191.779 1.00 104.11 ? 202 ARG   A NE  1 
ATOM   1130 C CZ  . ARG   A 1 210 ? 170.988 139.903 190.827 1.00 107.16 ? 202 ARG   A CZ  1 
ATOM   1131 N NH1 . ARG   A 1 210 ? 171.454 141.136 190.707 1.00 106.28 ? 202 ARG   A NH1 1 
ATOM   1132 N NH2 . ARG   A 1 210 ? 171.395 138.967 189.975 1.00 105.55 ? 202 ARG   A NH2 1 
ATOM   1133 N N   . GLU   A 1 211 ? 169.226 139.290 198.384 1.00 109.00 ? 203 GLU   A N   1 
ATOM   1134 C CA  . GLU   A 1 211 ? 169.817 139.259 199.715 1.00 111.94 ? 203 GLU   A CA  1 
ATOM   1135 C C   . GLU   A 1 211 ? 171.336 139.353 199.698 1.00 111.15 ? 203 GLU   A C   1 
ATOM   1136 O O   . GLU   A 1 211 ? 171.944 139.441 200.769 1.00 109.62 ? 203 GLU   A O   1 
ATOM   1137 C CB  . GLU   A 1 211 ? 169.391 137.983 200.446 1.00 113.79 ? 203 GLU   A CB  1 
ATOM   1138 C CG  . GLU   A 1 211 ? 167.920 137.641 200.283 1.00 115.32 ? 203 GLU   A CG  1 
ATOM   1139 C CD  . GLU   A 1 211 ? 167.329 137.004 201.524 1.00 127.37 ? 203 GLU   A CD  1 
ATOM   1140 O OE1 . GLU   A 1 211 ? 167.951 136.067 202.066 1.00 130.63 ? 203 GLU   A OE1 1 
ATOM   1141 O OE2 . GLU   A 1 211 ? 166.241 137.440 201.957 1.00 132.65 ? 203 GLU   A OE2 1 
ATOM   1142 N N   . ASP   A 1 212 ? 171.961 139.340 198.519 1.00 111.49 ? 204 ASP   A N   1 
ATOM   1143 C CA  . ASP   A 1 212 ? 173.411 139.405 198.418 1.00 112.60 ? 204 ASP   A CA  1 
ATOM   1144 C C   . ASP   A 1 212 ? 173.932 140.716 197.849 1.00 111.67 ? 204 ASP   A C   1 
ATOM   1145 O O   . ASP   A 1 212 ? 175.101 141.042 198.076 1.00 114.03 ? 204 ASP   A O   1 
ATOM   1146 C CB  . ASP   A 1 212 ? 173.938 138.246 197.558 1.00 112.91 ? 204 ASP   A CB  1 
ATOM   1147 C CG  . ASP   A 1 212 ? 173.552 138.379 196.098 1.00 111.68 ? 204 ASP   A CG  1 
ATOM   1148 O OD1 . ASP   A 1 212 ? 172.348 138.274 195.787 1.00 106.28 ? 204 ASP   A OD1 1 
ATOM   1149 O OD2 . ASP   A 1 212 ? 174.455 138.584 195.259 1.00 111.09 ? 204 ASP   A OD2 1 
ATOM   1150 N N   . VAL   A 1 213 ? 173.108 141.473 197.121 1.00 105.46 ? 205 VAL   A N   1 
ATOM   1151 C CA  . VAL   A 1 213 ? 173.537 142.730 196.522 1.00 103.13 ? 205 VAL   A CA  1 
ATOM   1152 C C   . VAL   A 1 213 ? 172.568 143.872 196.781 1.00 103.04 ? 205 VAL   A C   1 
ATOM   1153 O O   . VAL   A 1 213 ? 172.831 144.997 196.351 1.00 105.39 ? 205 VAL   A O   1 
ATOM   1154 C CB  . VAL   A 1 213 ? 173.778 142.576 195.006 1.00 98.83  ? 205 VAL   A CB  1 
ATOM   1155 C CG1 . VAL   A 1 213 ? 175.129 141.928 194.747 1.00 102.66 ? 205 VAL   A CG1 1 
ATOM   1156 C CG2 . VAL   A 1 213 ? 172.664 141.765 194.374 1.00 97.17  ? 205 VAL   A CG2 1 
ATOM   1157 N N   . ASP   A 1 214 ? 171.454 143.625 197.475 1.00 100.68 ? 206 ASP   A N   1 
ATOM   1158 C CA  . ASP   A 1 214 ? 170.445 144.651 197.756 1.00 100.38 ? 206 ASP   A CA  1 
ATOM   1159 C C   . ASP   A 1 214 ? 169.934 145.289 196.464 1.00 93.31  ? 206 ASP   A C   1 
ATOM   1160 O O   . ASP   A 1 214 ? 169.906 146.512 196.313 1.00 92.53  ? 206 ASP   A O   1 
ATOM   1161 C CB  . ASP   A 1 214 ? 170.988 145.711 198.718 1.00 104.53 ? 206 ASP   A CB  1 
ATOM   1162 C CG  . ASP   A 1 214 ? 169.888 146.520 199.381 1.00 108.41 ? 206 ASP   A CG  1 
ATOM   1163 O OD1 . ASP   A 1 214 ? 168.713 146.379 198.979 1.00 100.01 ? 206 ASP   A OD1 1 
ATOM   1164 O OD2 . ASP   A 1 214 ? 170.199 147.300 200.305 1.00 118.33 ? 206 ASP   A OD2 1 
ATOM   1165 N N   . VAL   A 1 215 ? 169.529 144.441 195.524 1.00 86.44  ? 207 VAL   A N   1 
ATOM   1166 C CA  . VAL   A 1 215 ? 169.019 144.870 194.228 1.00 75.76  ? 207 VAL   A CA  1 
ATOM   1167 C C   . VAL   A 1 215 ? 167.591 144.365 194.085 1.00 73.77  ? 207 VAL   A C   1 
ATOM   1168 O O   . VAL   A 1 215 ? 167.332 143.168 194.253 1.00 80.46  ? 207 VAL   A O   1 
ATOM   1169 C CB  . VAL   A 1 215 ? 169.901 144.355 193.076 1.00 79.61  ? 207 VAL   A CB  1 
ATOM   1170 C CG1 . VAL   A 1 215 ? 169.150 144.418 191.757 1.00 76.62  ? 207 VAL   A CG1 1 
ATOM   1171 C CG2 . VAL   A 1 215 ? 171.189 145.155 192.998 1.00 83.22  ? 207 VAL   A CG2 1 
ATOM   1172 N N   . ILE   A 1 216 ? 166.670 145.274 193.782 1.00 67.79  ? 208 ILE   A N   1 
ATOM   1173 C CA  . ILE   A 1 216 ? 165.278 144.904 193.558 1.00 61.76  ? 208 ILE   A CA  1 
ATOM   1174 C C   . ILE   A 1 216 ? 165.128 144.394 192.132 1.00 59.36  ? 208 ILE   A C   1 
ATOM   1175 O O   . ILE   A 1 216 ? 165.561 145.048 191.177 1.00 61.64  ? 208 ILE   A O   1 
ATOM   1176 C CB  . ILE   A 1 216 ? 164.345 146.096 193.823 1.00 54.85  ? 208 ILE   A CB  1 
ATOM   1177 C CG1 . ILE   A 1 216 ? 164.800 146.870 195.060 1.00 55.35  ? 208 ILE   A CG1 1 
ATOM   1178 C CG2 . ILE   A 1 216 ? 162.914 145.618 193.998 1.00 56.95  ? 208 ILE   A CG2 1 
ATOM   1179 C CD1 . ILE   A 1 216 ? 165.433 148.207 194.744 1.00 59.46  ? 208 ILE   A CD1 1 
ATOM   1180 N N   . GLU   A 1 217 ? 164.516 143.224 191.984 1.00 58.94  ? 209 GLU   A N   1 
ATOM   1181 C CA  . GLU   A 1 217 ? 164.337 142.589 190.688 1.00 62.99  ? 209 GLU   A CA  1 
ATOM   1182 C C   . GLU   A 1 217 ? 162.855 142.379 190.413 1.00 65.71  ? 209 GLU   A C   1 
ATOM   1183 O O   . GLU   A 1 217 ? 162.109 141.927 191.286 1.00 69.92  ? 209 GLU   A O   1 
ATOM   1184 C CB  . GLU   A 1 217 ? 165.072 141.247 190.626 1.00 69.85  ? 209 GLU   A CB  1 
ATOM   1185 C CG  . GLU   A 1 217 ? 166.562 141.367 190.364 1.00 80.70  ? 209 GLU   A CG  1 
ATOM   1186 C CD  . GLU   A 1 217 ? 167.040 140.418 189.284 1.00 96.91  ? 209 GLU   A CD  1 
ATOM   1187 O OE1 . GLU   A 1 217 ? 166.186 139.852 188.570 1.00 94.01  ? 209 GLU   A OE1 1 
ATOM   1188 O OE2 . GLU   A 1 217 ? 168.269 140.240 189.149 1.00 102.17 ? 209 GLU   A OE2 1 
ATOM   1189 N N   . CYS   A 1 218 ? 162.436 142.706 189.194 1.00 58.25  ? 210 CYS   A N   1 
ATOM   1190 C CA  . CYS   A 1 218 ? 161.057 142.527 188.755 1.00 52.16  ? 210 CYS   A CA  1 
ATOM   1191 C C   . CYS   A 1 218 ? 160.995 141.290 187.867 1.00 62.31  ? 210 CYS   A C   1 
ATOM   1192 O O   . CYS   A 1 218 ? 161.567 141.275 186.772 1.00 66.18  ? 210 CYS   A O   1 
ATOM   1193 C CB  . CYS   A 1 218 ? 160.563 143.767 188.014 1.00 45.26  ? 210 CYS   A CB  1 
ATOM   1194 S SG  . CYS   A 1 218 ? 158.990 143.570 187.150 1.00 61.19  ? 210 CYS   A SG  1 
ATOM   1195 N N   . SER   A 1 219 ? 160.303 140.256 188.339 1.00 60.92  ? 211 SER   A N   1 
ATOM   1196 C CA  . SER   A 1 219 ? 160.195 139.003 187.603 1.00 58.06  ? 211 SER   A CA  1 
ATOM   1197 C C   . SER   A 1 219 ? 159.030 138.203 188.168 1.00 55.36  ? 211 SER   A C   1 
ATOM   1198 O O   . SER   A 1 219 ? 158.456 138.550 189.201 1.00 56.99  ? 211 SER   A O   1 
ATOM   1199 C CB  . SER   A 1 219 ? 161.497 138.200 187.674 1.00 61.20  ? 211 SER   A CB  1 
ATOM   1200 O OG  . SER   A 1 219 ? 161.911 138.022 189.017 1.00 62.17  ? 211 SER   A OG  1 
ATOM   1201 N N   . LEU   A 1 220 ? 158.687 137.125 187.468 1.00 52.08  ? 212 LEU   A N   1 
ATOM   1202 C CA  . LEU   A 1 220 ? 157.630 136.237 187.932 1.00 49.91  ? 212 LEU   A CA  1 
ATOM   1203 C C   . LEU   A 1 220 ? 158.069 135.502 189.192 1.00 55.30  ? 212 LEU   A C   1 
ATOM   1204 O O   . LEU   A 1 220 ? 159.189 134.992 189.276 1.00 60.32  ? 212 LEU   A O   1 
ATOM   1205 C CB  . LEU   A 1 220 ? 157.259 135.236 186.840 1.00 43.78  ? 212 LEU   A CB  1 
ATOM   1206 C CG  . LEU   A 1 220 ? 156.592 135.824 185.597 1.00 39.58  ? 212 LEU   A CG  1 
ATOM   1207 C CD1 . LEU   A 1 220 ? 156.553 134.802 184.481 1.00 48.62  ? 212 LEU   A CD1 1 
ATOM   1208 C CD2 . LEU   A 1 220 ? 155.194 136.305 185.925 1.00 39.36  ? 212 LEU   A CD2 1 
ATOM   1209 N N   . GLN   A 1 221 ? 157.174 135.445 190.172 1.00 54.15  ? 213 GLN   A N   1 
ATOM   1210 C CA  . GLN   A 1 221 ? 157.473 134.884 191.487 1.00 57.55  ? 213 GLN   A CA  1 
ATOM   1211 C C   . GLN   A 1 221 ? 156.864 133.491 191.588 1.00 63.85  ? 213 GLN   A C   1 
ATOM   1212 O O   . GLN   A 1 221 ? 155.754 133.323 192.101 1.00 62.58  ? 213 GLN   A O   1 
ATOM   1213 C CB  . GLN   A 1 221 ? 156.951 135.795 192.594 1.00 60.28  ? 213 GLN   A CB  1 
ATOM   1214 C CG  . GLN   A 1 221 ? 157.374 137.243 192.456 1.00 54.31  ? 213 GLN   A CG  1 
ATOM   1215 C CD  . GLN   A 1 221 ? 158.799 137.472 192.905 1.00 60.06  ? 213 GLN   A CD  1 
ATOM   1216 O OE1 . GLN   A 1 221 ? 159.083 137.547 194.100 1.00 70.32  ? 213 GLN   A OE1 1 
ATOM   1217 N NE2 . GLN   A 1 221 ? 159.708 137.587 191.945 1.00 57.27  ? 213 GLN   A NE2 1 
ATOM   1218 N N   . PHE   A 1 222 ? 157.593 132.496 191.100 1.00 73.93  ? 214 PHE   A N   1 
ATOM   1219 C CA  . PHE   A 1 222 ? 157.238 131.111 191.344 1.00 77.56  ? 214 PHE   A CA  1 
ATOM   1220 C C   . PHE   A 1 222 ? 157.546 130.749 192.793 1.00 88.19  ? 214 PHE   A C   1 
ATOM   1221 O O   . PHE   A 1 222 ? 158.391 131.383 193.430 1.00 91.38  ? 214 PHE   A O   1 
ATOM   1222 C CB  . PHE   A 1 222 ? 157.998 130.197 190.390 1.00 73.97  ? 214 PHE   A CB  1 
ATOM   1223 C CG  . PHE   A 1 222 ? 157.863 130.585 188.950 1.00 67.77  ? 214 PHE   A CG  1 
ATOM   1224 C CD1 . PHE   A 1 222 ? 156.617 130.661 188.356 1.00 62.19  ? 214 PHE   A CD1 1 
ATOM   1225 C CD2 . PHE   A 1 222 ? 158.980 130.875 188.190 1.00 70.93  ? 214 PHE   A CD2 1 
ATOM   1226 C CE1 . PHE   A 1 222 ? 156.488 131.018 187.032 1.00 59.39  ? 214 PHE   A CE1 1 
ATOM   1227 C CE2 . PHE   A 1 222 ? 158.857 131.234 186.864 1.00 69.86  ? 214 PHE   A CE2 1 
ATOM   1228 C CZ  . PHE   A 1 222 ? 157.609 131.305 186.285 1.00 62.40  ? 214 PHE   A CZ  1 
ATOM   1229 N N   . PRO   A 1 223 ? 156.859 129.751 193.346 1.00 88.43  ? 215 PRO   A N   1 
ATOM   1230 C CA  . PRO   A 1 223 ? 157.104 129.377 194.744 1.00 91.06  ? 215 PRO   A CA  1 
ATOM   1231 C C   . PRO   A 1 223 ? 158.563 129.016 194.981 1.00 99.15  ? 215 PRO   A C   1 
ATOM   1232 O O   . PRO   A 1 223 ? 159.164 128.248 194.227 1.00 98.69  ? 215 PRO   A O   1 
ATOM   1233 C CB  . PRO   A 1 223 ? 156.178 128.172 194.955 1.00 89.91  ? 215 PRO   A CB  1 
ATOM   1234 C CG  . PRO   A 1 223 ? 155.815 127.708 193.575 1.00 86.92  ? 215 PRO   A CG  1 
ATOM   1235 C CD  . PRO   A 1 223 ? 155.778 128.949 192.752 1.00 83.13  ? 215 PRO   A CD  1 
ATOM   1236 N N   . ASP   A 1 224 ? 159.133 129.580 196.049 1.00 105.65 ? 216 ASP   A N   1 
ATOM   1237 C CA  . ASP   A 1 224 ? 160.540 129.350 196.354 1.00 106.19 ? 216 ASP   A CA  1 
ATOM   1238 C C   . ASP   A 1 224 ? 160.806 127.922 196.807 1.00 109.60 ? 216 ASP   A C   1 
ATOM   1239 O O   . ASP   A 1 224 ? 161.971 127.523 196.908 1.00 109.42 ? 216 ASP   A O   1 
ATOM   1240 C CB  . ASP   A 1 224 ? 161.017 130.337 197.421 1.00 105.27 ? 216 ASP   A CB  1 
ATOM   1241 C CG  . ASP   A 1 224 ? 160.914 131.781 196.967 1.00 110.54 ? 216 ASP   A CG  1 
ATOM   1242 O OD1 . ASP   A 1 224 ? 160.479 132.016 195.820 1.00 114.85 ? 216 ASP   A OD1 1 
ATOM   1243 O OD2 . ASP   A 1 224 ? 161.269 132.682 197.757 1.00 104.01 ? 216 ASP   A OD2 1 
ATOM   1244 N N   . ASP   A 1 225 ? 159.755 127.150 197.092 1.00 114.34 ? 217 ASP   A N   1 
ATOM   1245 C CA  . ASP   A 1 225 ? 159.940 125.739 197.410 1.00 119.97 ? 217 ASP   A CA  1 
ATOM   1246 C C   . ASP   A 1 225 ? 160.567 125.002 196.234 1.00 116.36 ? 217 ASP   A C   1 
ATOM   1247 O O   . ASP   A 1 225 ? 161.480 124.188 196.414 1.00 114.69 ? 217 ASP   A O   1 
ATOM   1248 C CB  . ASP   A 1 225 ? 158.595 125.111 197.790 1.00 118.76 ? 217 ASP   A CB  1 
ATOM   1249 C CG  . ASP   A 1 225 ? 158.712 123.642 198.169 1.00 121.73 ? 217 ASP   A CG  1 
ATOM   1250 O OD1 . ASP   A 1 225 ? 157.660 122.981 198.294 1.00 120.13 ? 217 ASP   A OD1 1 
ATOM   1251 O OD2 . ASP   A 1 225 ? 159.842 123.152 198.372 1.00 124.40 ? 217 ASP   A OD2 1 
ATOM   1252 N N   . GLU   A 1 226 ? 160.106 125.336 195.024 1.00 107.35 ? 218 GLU   A N   1 
ATOM   1253 C CA  . GLU   A 1 226 ? 160.693 124.738 193.797 1.00 104.10 ? 218 GLU   A CA  1 
ATOM   1254 C C   . GLU   A 1 226 ? 161.362 125.860 192.986 1.00 103.47 ? 218 GLU   A C   1 
ATOM   1255 O O   . GLU   A 1 226 ? 162.607 125.841 192.881 1.00 106.33 ? 218 GLU   A O   1 
ATOM   1256 C CB  . GLU   A 1 226 ? 159.621 124.014 192.982 1.00 100.80 ? 218 GLU   A CB  1 
ATOM   1257 C CG  . GLU   A 1 226 ? 160.090 123.601 191.590 1.00 101.57 ? 218 GLU   A CG  1 
ATOM   1258 C CD  . GLU   A 1 226 ? 161.086 122.458 191.583 1.00 107.19 ? 218 GLU   A CD  1 
ATOM   1259 O OE1 . GLU   A 1 226 ? 160.884 121.493 192.349 1.00 110.85 ? 218 GLU   A OE1 1 
ATOM   1260 O OE2 . GLU   A 1 226 ? 162.063 122.531 190.811 1.00 102.12 ? 218 GLU   A OE2 1 
ATOM   1261 N N   . TYR   A 1 227 ? 160.569 126.803 192.462 1.00 97.27  ? 219 TYR   A N   1 
ATOM   1262 C CA  . TYR   A 1 227 ? 161.119 127.943 191.678 1.00 92.81  ? 219 TYR   A CA  1 
ATOM   1263 C C   . TYR   A 1 227 ? 162.261 127.449 190.804 1.00 93.06  ? 219 TYR   A C   1 
ATOM   1264 O O   . TYR   A 1 227 ? 163.255 128.190 190.640 1.00 90.21  ? 219 TYR   A O   1 
ATOM   1265 C CB  . TYR   A 1 227 ? 161.658 129.034 192.608 1.00 91.36  ? 219 TYR   A CB  1 
ATOM   1266 C CG  . TYR   A 1 227 ? 161.492 130.473 192.135 1.00 90.12  ? 219 TYR   A CG  1 
ATOM   1267 C CD1 . TYR   A 1 227 ? 161.498 131.522 193.043 1.00 89.68  ? 219 TYR   A CD1 1 
ATOM   1268 C CD2 . TYR   A 1 227 ? 161.353 130.787 190.789 1.00 86.26  ? 219 TYR   A CD2 1 
ATOM   1269 C CE1 . TYR   A 1 227 ? 161.347 132.836 192.636 1.00 87.60  ? 219 TYR   A CE1 1 
ATOM   1270 C CE2 . TYR   A 1 227 ? 161.208 132.099 190.367 1.00 83.23  ? 219 TYR   A CE2 1 
ATOM   1271 C CZ  . TYR   A 1 227 ? 161.202 133.126 191.292 1.00 88.44  ? 219 TYR   A CZ  1 
ATOM   1272 O OH  . TYR   A 1 227 ? 161.063 134.422 190.890 1.00 79.93  ? 219 TYR   A OH  1 
ATOM   1273 N N   . SER   A 1 228 ? 162.149 126.238 190.254 1.00 91.29  ? 220 SER   A N   1 
ATOM   1274 C CA  . SER   A 1 228 ? 163.232 125.807 189.334 1.00 87.59  ? 220 SER   A CA  1 
ATOM   1275 C C   . SER   A 1 228 ? 162.549 125.148 188.139 1.00 86.37  ? 220 SER   A C   1 
ATOM   1276 O O   . SER   A 1 228 ? 162.568 125.740 187.038 1.00 82.38  ? 220 SER   A O   1 
ATOM   1277 C CB  . SER   A 1 228 ? 164.206 124.872 189.997 1.00 89.99  ? 220 SER   A CB  1 
ATOM   1278 O OG  . SER   A 1 228 ? 164.682 125.415 191.221 1.00 92.16  ? 220 SER   A OG  1 
ATOM   1279 N N   . TRP   A 1 229 ? 161.958 123.976 188.366 1.00 88.43  ? 221 TRP   A N   1 
ATOM   1280 C CA  . TRP   A 1 229 ? 161.168 123.378 187.270 1.00 83.88  ? 221 TRP   A CA  1 
ATOM   1281 C C   . TRP   A 1 229 ? 160.199 124.455 186.798 1.00 76.74  ? 221 TRP   A C   1 
ATOM   1282 O O   . TRP   A 1 229 ? 160.005 124.580 185.579 1.00 76.38  ? 221 TRP   A O   1 
ATOM   1283 C CB  . TRP   A 1 229 ? 160.415 122.133 187.753 1.00 88.01  ? 221 TRP   A CB  1 
ATOM   1284 C CG  . TRP   A 1 229 ? 159.235 121.783 186.886 1.00 90.79  ? 221 TRP   A CG  1 
ATOM   1285 C CD1 . TRP   A 1 229 ? 159.261 121.118 185.696 1.00 97.29  ? 221 TRP   A CD1 1 
ATOM   1286 C CD2 . TRP   A 1 229 ? 157.850 122.101 187.139 1.00 90.44  ? 221 TRP   A CD2 1 
ATOM   1287 N NE1 . TRP   A 1 229 ? 157.993 120.991 185.195 1.00 100.74 ? 221 TRP   A NE1 1 
ATOM   1288 C CE2 . TRP   A 1 229 ? 157.108 121.586 186.055 1.00 95.16  ? 221 TRP   A CE2 1 
ATOM   1289 C CE3 . TRP   A 1 229 ? 157.173 122.764 188.167 1.00 88.24  ? 221 TRP   A CE3 1 
ATOM   1290 C CZ2 . TRP   A 1 229 ? 155.724 121.714 185.975 1.00 86.95  ? 221 TRP   A CZ2 1 
ATOM   1291 C CZ3 . TRP   A 1 229 ? 155.804 122.888 188.085 1.00 87.98  ? 221 TRP   A CZ3 1 
ATOM   1292 C CH2 . TRP   A 1 229 ? 155.092 122.375 187.003 1.00 87.29  ? 221 TRP   A CH2 1 
ATOM   1293 N N   . TRP   A 1 230 ? 159.657 125.248 187.732 1.00 78.64  ? 222 TRP   A N   1 
ATOM   1294 C CA  . TRP   A 1 230 ? 158.626 126.234 187.326 1.00 75.62  ? 222 TRP   A CA  1 
ATOM   1295 C C   . TRP   A 1 230 ? 159.196 127.120 186.227 1.00 66.81  ? 222 TRP   A C   1 
ATOM   1296 O O   . TRP   A 1 230 ? 158.544 127.273 185.173 1.00 63.38  ? 222 TRP   A O   1 
ATOM   1297 C CB  . TRP   A 1 230 ? 158.213 127.096 188.523 1.00 79.74  ? 222 TRP   A CB  1 
ATOM   1298 C CG  . TRP   A 1 230 ? 157.354 126.383 189.530 1.00 81.70  ? 222 TRP   A CG  1 
ATOM   1299 C CD1 . TRP   A 1 230 ? 157.737 125.907 190.748 1.00 85.41  ? 222 TRP   A CD1 1 
ATOM   1300 C CD2 . TRP   A 1 230 ? 155.952 126.073 189.400 1.00 81.17  ? 222 TRP   A CD2 1 
ATOM   1301 N NE1 . TRP   A 1 230 ? 156.678 125.317 191.383 1.00 84.01  ? 222 TRP   A NE1 1 
ATOM   1302 C CE2 . TRP   A 1 230 ? 155.570 125.405 190.583 1.00 83.20  ? 222 TRP   A CE2 1 
ATOM   1303 C CE3 . TRP   A 1 230 ? 154.992 126.290 188.407 1.00 83.81  ? 222 TRP   A CE3 1 
ATOM   1304 C CZ2 . TRP   A 1 230 ? 154.269 124.956 190.795 1.00 84.70  ? 222 TRP   A CZ2 1 
ATOM   1305 C CZ3 . TRP   A 1 230 ? 153.706 125.845 188.618 1.00 85.60  ? 222 TRP   A CZ3 1 
ATOM   1306 C CH2 . TRP   A 1 230 ? 153.352 125.188 189.795 1.00 83.95  ? 222 TRP   A CH2 1 
ATOM   1307 N N   . ASP   A 1 231 ? 160.382 127.683 186.470 1.00 68.51  ? 223 ASP   A N   1 
ATOM   1308 C CA  . ASP   A 1 231 ? 160.955 128.603 185.493 1.00 65.00  ? 223 ASP   A CA  1 
ATOM   1309 C C   . ASP   A 1 231 ? 161.296 127.886 184.192 1.00 66.00  ? 223 ASP   A C   1 
ATOM   1310 O O   . ASP   A 1 231 ? 160.982 128.374 183.100 1.00 66.55  ? 223 ASP   A O   1 
ATOM   1311 C CB  . ASP   A 1 231 ? 162.196 129.275 186.079 1.00 71.77  ? 223 ASP   A CB  1 
ATOM   1312 C CG  . ASP   A 1 231 ? 162.858 130.225 185.105 1.00 71.25  ? 223 ASP   A CG  1 
ATOM   1313 O OD1 . ASP   A 1 231 ? 162.225 131.236 184.737 1.00 70.26  ? 223 ASP   A OD1 1 
ATOM   1314 O OD2 . ASP   A 1 231 ? 164.011 129.960 184.709 1.00 72.59  ? 223 ASP   A OD2 1 
ATOM   1315 N N   . LEU   A 1 232 ? 161.940 126.720 184.291 1.00 62.25  ? 224 LEU   A N   1 
ATOM   1316 C CA  . LEU   A 1 232 ? 162.292 125.965 183.092 1.00 51.04  ? 224 LEU   A CA  1 
ATOM   1317 C C   . LEU   A 1 232 ? 161.049 125.519 182.335 1.00 52.74  ? 224 LEU   A C   1 
ATOM   1318 O O   . LEU   A 1 232 ? 160.995 125.612 181.103 1.00 54.78  ? 224 LEU   A O   1 
ATOM   1319 C CB  . LEU   A 1 232 ? 163.154 124.760 183.466 1.00 49.71  ? 224 LEU   A CB  1 
ATOM   1320 C CG  . LEU   A 1 232 ? 163.503 123.792 182.335 1.00 48.33  ? 224 LEU   A CG  1 
ATOM   1321 C CD1 . LEU   A 1 232 ? 164.240 124.511 181.221 1.00 52.73  ? 224 LEU   A CD1 1 
ATOM   1322 C CD2 . LEU   A 1 232 ? 164.332 122.635 182.862 1.00 47.04  ? 224 LEU   A CD2 1 
ATOM   1323 N N   . PHE   A 1 233 ? 160.036 125.034 183.057 1.00 56.87  ? 225 PHE   A N   1 
ATOM   1324 C CA  . PHE   A 1 233 ? 158.803 124.594 182.417 1.00 52.29  ? 225 PHE   A CA  1 
ATOM   1325 C C   . PHE   A 1 233 ? 158.104 125.749 181.717 1.00 50.14  ? 225 PHE   A C   1 
ATOM   1326 O O   . PHE   A 1 233 ? 157.628 125.599 180.587 1.00 52.67  ? 225 PHE   A O   1 
ATOM   1327 C CB  . PHE   A 1 233 ? 157.883 123.955 183.457 1.00 62.64  ? 225 PHE   A CB  1 
ATOM   1328 C CG  . PHE   A 1 233 ? 156.558 123.514 182.910 1.00 64.52  ? 225 PHE   A CG  1 
ATOM   1329 C CD1 . PHE   A 1 233 ? 156.475 122.441 182.040 1.00 61.41  ? 225 PHE   A CD1 1 
ATOM   1330 C CD2 . PHE   A 1 233 ? 155.393 124.165 183.276 1.00 67.11  ? 225 PHE   A CD2 1 
ATOM   1331 C CE1 . PHE   A 1 233 ? 155.256 122.031 181.541 1.00 59.68  ? 225 PHE   A CE1 1 
ATOM   1332 C CE2 . PHE   A 1 233 ? 154.172 123.760 182.779 1.00 68.04  ? 225 PHE   A CE2 1 
ATOM   1333 C CZ  . PHE   A 1 233 ? 154.103 122.691 181.912 1.00 65.37  ? 225 PHE   A CZ  1 
ATOM   1334 N N   . MET   A 1 234 ? 158.034 126.912 182.369 1.00 48.77  ? 226 MET   A N   1 
ATOM   1335 C CA  . MET   A 1 234 ? 157.384 128.059 181.746 1.00 49.29  ? 226 MET   A CA  1 
ATOM   1336 C C   . MET   A 1 234 ? 158.152 128.535 180.523 1.00 49.21  ? 226 MET   A C   1 
ATOM   1337 O O   . MET   A 1 234 ? 157.546 128.889 179.508 1.00 53.51  ? 226 MET   A O   1 
ATOM   1338 C CB  . MET   A 1 234 ? 157.222 129.196 182.752 1.00 51.23  ? 226 MET   A CB  1 
ATOM   1339 C CG  . MET   A 1 234 ? 156.559 130.428 182.160 1.00 52.65  ? 226 MET   A CG  1 
ATOM   1340 S SD  . MET   A 1 234 ? 155.762 131.479 183.384 1.00 74.22  ? 226 MET   A SD  1 
ATOM   1341 C CE  . MET   A 1 234 ? 154.573 132.345 182.363 1.00 47.65  ? 226 MET   A CE  1 
ATOM   1342 N N   . LYS   A 1 235 ? 159.485 128.553 180.595 1.00 44.91  ? 227 LYS   A N   1 
ATOM   1343 C CA  . LYS   A 1 235 ? 160.269 128.971 179.438 1.00 42.42  ? 227 LYS   A CA  1 
ATOM   1344 C C   . LYS   A 1 235 ? 160.084 128.010 178.270 1.00 43.38  ? 227 LYS   A C   1 
ATOM   1345 O O   . LYS   A 1 235 ? 159.922 128.441 177.122 1.00 48.16  ? 227 LYS   A O   1 
ATOM   1346 C CB  . LYS   A 1 235 ? 161.744 129.088 179.819 1.00 43.47  ? 227 LYS   A CB  1 
ATOM   1347 C CG  . LYS   A 1 235 ? 162.062 130.318 180.650 1.00 48.50  ? 227 LYS   A CG  1 
ATOM   1348 C CD  . LYS   A 1 235 ? 163.553 130.467 180.873 1.00 56.68  ? 227 LYS   A CD  1 
ATOM   1349 C CE  . LYS   A 1 235 ? 163.856 131.616 181.820 1.00 64.97  ? 227 LYS   A CE  1 
ATOM   1350 N NZ  . LYS   A 1 235 ? 165.318 131.873 181.934 1.00 67.14  ? 227 LYS   A NZ  1 
ATOM   1351 N N   . ILE   A 1 236 ? 160.085 126.704 178.546 1.00 45.15  ? 228 ILE   A N   1 
ATOM   1352 C CA  . ILE   A 1 236 ? 159.890 125.717 177.486 1.00 40.82  ? 228 ILE   A CA  1 
ATOM   1353 C C   . ILE   A 1 236 ? 158.496 125.845 176.883 1.00 40.56  ? 228 ILE   A C   1 
ATOM   1354 O O   . ILE   A 1 236 ? 158.325 125.785 175.659 1.00 43.40  ? 228 ILE   A O   1 
ATOM   1355 C CB  . ILE   A 1 236 ? 160.153 124.299 178.026 1.00 39.50  ? 228 ILE   A CB  1 
ATOM   1356 C CG1 . ILE   A 1 236 ? 161.643 123.967 177.944 1.00 37.99  ? 228 ILE   A CG1 1 
ATOM   1357 C CG2 . ILE   A 1 236 ? 159.334 123.266 177.268 1.00 40.30  ? 228 ILE   A CG2 1 
ATOM   1358 C CD1 . ILE   A 1 236 ? 162.037 122.751 178.744 1.00 38.50  ? 228 ILE   A CD1 1 
ATOM   1359 N N   . CYS   A 1 237 ? 157.478 126.019 177.730 1.00 41.30  ? 229 CYS   A N   1 
ATOM   1360 C CA  . CYS   A 1 237 ? 156.115 126.157 177.228 1.00 38.26  ? 229 CYS   A CA  1 
ATOM   1361 C C   . CYS   A 1 237 ? 155.957 127.420 176.394 1.00 41.26  ? 229 CYS   A C   1 
ATOM   1362 O O   . CYS   A 1 237 ? 155.295 127.401 175.352 1.00 46.88  ? 229 CYS   A O   1 
ATOM   1363 C CB  . CYS   A 1 237 ? 155.123 126.155 178.390 1.00 40.56  ? 229 CYS   A CB  1 
ATOM   1364 S SG  . CYS   A 1 237 ? 154.732 124.511 179.017 1.00 68.05  ? 229 CYS   A SG  1 
ATOM   1365 N N   . VAL   A 1 238 ? 156.552 128.529 176.838 1.00 41.77  ? 230 VAL   A N   1 
ATOM   1366 C CA  . VAL   A 1 238 ? 156.488 129.764 176.064 1.00 41.28  ? 230 VAL   A CA  1 
ATOM   1367 C C   . VAL   A 1 238 ? 157.167 129.575 174.717 1.00 39.95  ? 230 VAL   A C   1 
ATOM   1368 O O   . VAL   A 1 238 ? 156.625 129.958 173.676 1.00 45.07  ? 230 VAL   A O   1 
ATOM   1369 C CB  . VAL   A 1 238 ? 157.110 130.930 176.857 1.00 40.84  ? 230 VAL   A CB  1 
ATOM   1370 C CG1 . VAL   A 1 238 ? 157.455 132.081 175.929 1.00 40.09  ? 230 VAL   A CG1 1 
ATOM   1371 C CG2 . VAL   A 1 238 ? 156.159 131.394 177.945 1.00 39.51  ? 230 VAL   A CG2 1 
ATOM   1372 N N   . PHE   A 1 239 ? 158.349 128.955 174.712 1.00 39.82  ? 231 PHE   A N   1 
ATOM   1373 C CA  . PHE   A 1 239 ? 159.045 128.690 173.458 1.00 39.49  ? 231 PHE   A CA  1 
ATOM   1374 C C   . PHE   A 1 239 ? 158.176 127.872 172.512 1.00 38.91  ? 231 PHE   A C   1 
ATOM   1375 O O   . PHE   A 1 239 ? 157.976 128.248 171.352 1.00 44.10  ? 231 PHE   A O   1 
ATOM   1376 C CB  . PHE   A 1 239 ? 160.364 127.971 173.744 1.00 42.22  ? 231 PHE   A CB  1 
ATOM   1377 C CG  . PHE   A 1 239 ? 161.148 127.618 172.514 1.00 43.55  ? 231 PHE   A CG  1 
ATOM   1378 C CD1 . PHE   A 1 239 ? 161.716 128.606 171.730 1.00 42.60  ? 231 PHE   A CD1 1 
ATOM   1379 C CD2 . PHE   A 1 239 ? 161.328 126.295 172.151 1.00 39.63  ? 231 PHE   A CD2 1 
ATOM   1380 C CE1 . PHE   A 1 239 ? 162.442 128.281 170.602 1.00 44.34  ? 231 PHE   A CE1 1 
ATOM   1381 C CE2 . PHE   A 1 239 ? 162.053 125.964 171.025 1.00 37.26  ? 231 PHE   A CE2 1 
ATOM   1382 C CZ  . PHE   A 1 239 ? 162.610 126.958 170.249 1.00 43.87  ? 231 PHE   A CZ  1 
ATOM   1383 N N   . VAL   A 1 240 ? 157.616 126.767 173.007 1.00 37.82  ? 232 VAL   A N   1 
ATOM   1384 C CA  . VAL   A 1 240 ? 156.857 125.861 172.149 1.00 37.17  ? 232 VAL   A CA  1 
ATOM   1385 C C   . VAL   A 1 240 ? 155.594 126.535 171.625 1.00 39.46  ? 232 VAL   A C   1 
ATOM   1386 O O   . VAL   A 1 240 ? 155.283 126.458 170.431 1.00 42.09  ? 232 VAL   A O   1 
ATOM   1387 C CB  . VAL   A 1 240 ? 156.531 124.560 172.903 1.00 37.79  ? 232 VAL   A CB  1 
ATOM   1388 C CG1 . VAL   A 1 240 ? 155.524 123.736 172.124 1.00 38.55  ? 232 VAL   A CG1 1 
ATOM   1389 C CG2 . VAL   A 1 240 ? 157.797 123.759 173.144 1.00 38.61  ? 232 VAL   A CG2 1 
ATOM   1390 N N   . PHE   A 1 241 ? 154.850 127.210 172.500 1.00 41.23  ? 233 PHE   A N   1 
ATOM   1391 C CA  . PHE   A 1 241 ? 153.533 127.720 172.145 1.00 41.70  ? 233 PHE   A CA  1 
ATOM   1392 C C   . PHE   A 1 241 ? 153.551 129.125 171.559 1.00 42.73  ? 233 PHE   A C   1 
ATOM   1393 O O   . PHE   A 1 241 ? 152.500 129.603 171.120 1.00 49.59  ? 233 PHE   A O   1 
ATOM   1394 C CB  . PHE   A 1 241 ? 152.615 127.699 173.371 1.00 42.36  ? 233 PHE   A CB  1 
ATOM   1395 C CG  . PHE   A 1 241 ? 152.023 126.352 173.658 1.00 44.82  ? 233 PHE   A CG  1 
ATOM   1396 C CD1 . PHE   A 1 241 ? 150.947 125.885 172.924 1.00 47.89  ? 233 PHE   A CD1 1 
ATOM   1397 C CD2 . PHE   A 1 241 ? 152.546 125.549 174.656 1.00 47.05  ? 233 PHE   A CD2 1 
ATOM   1398 C CE1 . PHE   A 1 241 ? 150.401 124.643 173.183 1.00 57.11  ? 233 PHE   A CE1 1 
ATOM   1399 C CE2 . PHE   A 1 241 ? 152.005 124.307 174.919 1.00 53.05  ? 233 PHE   A CE2 1 
ATOM   1400 C CZ  . PHE   A 1 241 ? 150.931 123.853 174.183 1.00 59.96  ? 233 PHE   A CZ  1 
ATOM   1401 N N   . ALA   A 1 242 ? 154.699 129.801 171.533 1.00 43.27  ? 234 ALA   A N   1 
ATOM   1402 C CA  . ALA   A 1 242 ? 154.779 131.120 170.936 1.00 41.93  ? 234 ALA   A CA  1 
ATOM   1403 C C   . ALA   A 1 242 ? 155.809 131.226 169.825 1.00 40.51  ? 234 ALA   A C   1 
ATOM   1404 O O   . ALA   A 1 242 ? 155.814 132.236 169.114 1.00 44.64  ? 234 ALA   A O   1 
ATOM   1405 C CB  . ALA   A 1 242 ? 155.090 132.177 172.007 1.00 38.06  ? 234 ALA   A CB  1 
ATOM   1406 N N   . PHE   A 1 243 ? 156.687 130.240 169.660 1.00 35.57  ? 235 PHE   A N   1 
ATOM   1407 C CA  . PHE   A 1 243 ? 157.619 130.252 168.543 1.00 34.97  ? 235 PHE   A CA  1 
ATOM   1408 C C   . PHE   A 1 243 ? 157.470 129.047 167.631 1.00 37.83  ? 235 PHE   A C   1 
ATOM   1409 O O   . PHE   A 1 243 ? 157.300 129.216 166.422 1.00 41.90  ? 235 PHE   A O   1 
ATOM   1410 C CB  . PHE   A 1 243 ? 159.063 130.345 169.053 1.00 39.58  ? 235 PHE   A CB  1 
ATOM   1411 C CG  . PHE   A 1 243 ? 160.032 130.833 168.020 1.00 40.59  ? 235 PHE   A CG  1 
ATOM   1412 C CD1 . PHE   A 1 243 ? 159.926 132.114 167.507 1.00 38.92  ? 235 PHE   A CD1 1 
ATOM   1413 C CD2 . PHE   A 1 243 ? 161.042 130.012 167.555 1.00 41.68  ? 235 PHE   A CD2 1 
ATOM   1414 C CE1 . PHE   A 1 243 ? 160.811 132.567 166.554 1.00 41.76  ? 235 PHE   A CE1 1 
ATOM   1415 C CE2 . PHE   A 1 243 ? 161.930 130.461 166.602 1.00 47.75  ? 235 PHE   A CE2 1 
ATOM   1416 C CZ  . PHE   A 1 243 ? 161.814 131.740 166.100 1.00 47.05  ? 235 PHE   A CZ  1 
ATOM   1417 N N   . VAL   A 1 244 ? 157.510 127.830 168.172 1.00 36.70  ? 236 VAL   A N   1 
ATOM   1418 C CA  . VAL   A 1 244 ? 157.641 126.646 167.324 1.00 38.03  ? 236 VAL   A CA  1 
ATOM   1419 C C   . VAL   A 1 244 ? 156.359 126.400 166.536 1.00 39.44  ? 236 VAL   A C   1 
ATOM   1420 O O   . VAL   A 1 244 ? 156.368 126.373 165.300 1.00 42.66  ? 236 VAL   A O   1 
ATOM   1421 C CB  . VAL   A 1 244 ? 158.026 125.418 168.165 1.00 36.30  ? 236 VAL   A CB  1 
ATOM   1422 C CG1 . VAL   A 1 244 ? 158.045 124.175 167.298 1.00 40.16  ? 236 VAL   A CG1 1 
ATOM   1423 C CG2 . VAL   A 1 244 ? 159.377 125.630 168.810 1.00 36.50  ? 236 VAL   A CG2 1 
ATOM   1424 N N   . ILE   A 1 245 ? 155.244 126.195 167.238 1.00 36.16  ? 237 ILE   A N   1 
ATOM   1425 C CA  . ILE   A 1 245 ? 153.995 125.842 166.558 1.00 38.54  ? 237 ILE   A CA  1 
ATOM   1426 C C   . ILE   A 1 245 ? 153.486 126.960 165.652 1.00 39.91  ? 237 ILE   A C   1 
ATOM   1427 O O   . ILE   A 1 245 ? 153.106 126.669 164.504 1.00 42.84  ? 237 ILE   A O   1 
ATOM   1428 C CB  . ILE   A 1 245 ? 152.947 125.382 167.586 1.00 39.02  ? 237 ILE   A CB  1 
ATOM   1429 C CG1 . ILE   A 1 245 ? 153.410 124.093 168.267 1.00 37.93  ? 237 ILE   A CG1 1 
ATOM   1430 C CG2 . ILE   A 1 245 ? 151.602 125.167 166.918 1.00 38.78  ? 237 ILE   A CG2 1 
ATOM   1431 C CD1 . ILE   A 1 245 ? 152.612 123.730 169.496 1.00 43.18  ? 237 ILE   A CD1 1 
ATOM   1432 N N   . PRO   A 1 246 ? 153.416 128.227 166.088 1.00 36.80  ? 238 PRO   A N   1 
ATOM   1433 C CA  . PRO   A 1 246 ? 152.973 129.275 165.152 1.00 33.47  ? 238 PRO   A CA  1 
ATOM   1434 C C   . PRO   A 1 246 ? 153.872 129.428 163.938 1.00 34.69  ? 238 PRO   A C   1 
ATOM   1435 O O   . PRO   A 1 246 ? 153.371 129.661 162.832 1.00 36.17  ? 238 PRO   A O   1 
ATOM   1436 C CB  . PRO   A 1 246 ? 152.971 130.539 166.021 1.00 30.74  ? 238 PRO   A CB  1 
ATOM   1437 C CG  . PRO   A 1 246 ? 152.838 130.049 167.404 1.00 34.46  ? 238 PRO   A CG  1 
ATOM   1438 C CD  . PRO   A 1 246 ? 153.601 128.768 167.446 1.00 36.21  ? 238 PRO   A CD  1 
ATOM   1439 N N   . VAL   A 1 247 ? 155.189 129.300 164.108 1.00 33.74  ? 239 VAL   A N   1 
ATOM   1440 C CA  . VAL   A 1 247 ? 156.088 129.407 162.964 1.00 31.48  ? 239 VAL   A CA  1 
ATOM   1441 C C   . VAL   A 1 247 ? 155.901 128.222 162.027 1.00 31.01  ? 239 VAL   A C   1 
ATOM   1442 O O   . VAL   A 1 247 ? 155.981 128.367 160.805 1.00 36.77  ? 239 VAL   A O   1 
ATOM   1443 C CB  . VAL   A 1 247 ? 157.548 129.551 163.433 1.00 31.01  ? 239 VAL   A CB  1 
ATOM   1444 C CG1 . VAL   A 1 247 ? 158.516 129.087 162.363 1.00 36.64  ? 239 VAL   A CG1 1 
ATOM   1445 C CG2 . VAL   A 1 247 ? 157.834 130.995 163.810 1.00 34.04  ? 239 VAL   A CG2 1 
ATOM   1446 N N   . LEU   A 1 248 ? 155.635 127.035 162.577 1.00 28.16  ? 240 LEU   A N   1 
ATOM   1447 C CA  . LEU   A 1 248 ? 155.335 125.887 161.726 1.00 29.24  ? 240 LEU   A CA  1 
ATOM   1448 C C   . LEU   A 1 248 ? 154.067 126.121 160.915 1.00 31.94  ? 240 LEU   A C   1 
ATOM   1449 O O   . LEU   A 1 248 ? 154.019 125.817 159.715 1.00 36.38  ? 240 LEU   A O   1 
ATOM   1450 C CB  . LEU   A 1 248 ? 155.197 124.625 162.576 1.00 32.96  ? 240 LEU   A CB  1 
ATOM   1451 C CG  . LEU   A 1 248 ? 156.485 123.965 163.065 1.00 34.36  ? 240 LEU   A CG  1 
ATOM   1452 C CD1 . LEU   A 1 248 ? 156.164 122.774 163.948 1.00 29.08  ? 240 LEU   A CD1 1 
ATOM   1453 C CD2 . LEU   A 1 248 ? 157.355 123.550 161.891 1.00 34.38  ? 240 LEU   A CD2 1 
ATOM   1454 N N   . ILE   A 1 249 ? 153.030 126.666 161.555 1.00 32.05  ? 241 ILE   A N   1 
ATOM   1455 C CA  . ILE   A 1 249 ? 151.784 126.950 160.845 1.00 30.59  ? 241 ILE   A CA  1 
ATOM   1456 C C   . ILE   A 1 249 ? 152.020 127.983 159.751 1.00 30.63  ? 241 ILE   A C   1 
ATOM   1457 O O   . ILE   A 1 249 ? 151.521 127.846 158.626 1.00 33.55  ? 241 ILE   A O   1 
ATOM   1458 C CB  . ILE   A 1 249 ? 150.695 127.408 161.832 1.00 30.99  ? 241 ILE   A CB  1 
ATOM   1459 C CG1 . ILE   A 1 249 ? 150.355 126.288 162.813 1.00 33.85  ? 241 ILE   A CG1 1 
ATOM   1460 C CG2 . ILE   A 1 249 ? 149.450 127.844 161.084 1.00 34.78  ? 241 ILE   A CG2 1 
ATOM   1461 C CD1 . ILE   A 1 249 ? 149.680 126.772 164.073 1.00 36.68  ? 241 ILE   A CD1 1 
ATOM   1462 N N   . ILE   A 1 250 ? 152.786 129.031 160.063 1.00 30.14  ? 242 ILE   A N   1 
ATOM   1463 C CA  . ILE   A 1 250 ? 153.090 130.066 159.079 1.00 29.58  ? 242 ILE   A CA  1 
ATOM   1464 C C   . ILE   A 1 250 ? 153.876 129.483 157.912 1.00 31.19  ? 242 ILE   A C   1 
ATOM   1465 O O   . ILE   A 1 250 ? 153.617 129.804 156.747 1.00 36.88  ? 242 ILE   A O   1 
ATOM   1466 C CB  . ILE   A 1 250 ? 153.847 131.228 159.749 1.00 27.51  ? 242 ILE   A CB  1 
ATOM   1467 C CG1 . ILE   A 1 250 ? 152.895 132.065 160.603 1.00 29.30  ? 242 ILE   A CG1 1 
ATOM   1468 C CG2 . ILE   A 1 250 ? 154.535 132.092 158.708 1.00 27.35  ? 242 ILE   A CG2 1 
ATOM   1469 C CD1 . ILE   A 1 250 ? 153.597 133.045 161.511 1.00 29.90  ? 242 ILE   A CD1 1 
ATOM   1470 N N   . ILE   A 1 251 ? 154.852 128.621 158.206 1.00 30.21  ? 243 ILE   A N   1 
ATOM   1471 C CA  . ILE   A 1 251 ? 155.665 128.015 157.158 1.00 27.86  ? 243 ILE   A CA  1 
ATOM   1472 C C   . ILE   A 1 251 ? 154.802 127.162 156.241 1.00 28.11  ? 243 ILE   A C   1 
ATOM   1473 O O   . ILE   A 1 251 ? 154.929 127.226 155.015 1.00 34.86  ? 243 ILE   A O   1 
ATOM   1474 C CB  . ILE   A 1 251 ? 156.813 127.197 157.778 1.00 28.48  ? 243 ILE   A CB  1 
ATOM   1475 C CG1 . ILE   A 1 251 ? 157.936 128.118 158.248 1.00 28.05  ? 243 ILE   A CG1 1 
ATOM   1476 C CG2 . ILE   A 1 251 ? 157.351 126.180 156.785 1.00 27.25  ? 243 ILE   A CG2 1 
ATOM   1477 C CD1 . ILE   A 1 251 ? 158.950 127.429 159.125 1.00 28.40  ? 243 ILE   A CD1 1 
ATOM   1478 N N   . VAL   A 1 252 ? 153.910 126.353 156.816 1.00 26.50  ? 244 VAL   A N   1 
ATOM   1479 C CA  . VAL   A 1 252 ? 153.037 125.515 155.995 1.00 27.42  ? 244 VAL   A CA  1 
ATOM   1480 C C   . VAL   A 1 252 ? 152.134 126.381 155.125 1.00 29.81  ? 244 VAL   A C   1 
ATOM   1481 O O   . VAL   A 1 252 ? 151.999 126.157 153.910 1.00 35.43  ? 244 VAL   A O   1 
ATOM   1482 C CB  . VAL   A 1 252 ? 152.218 124.564 156.887 1.00 26.56  ? 244 VAL   A CB  1 
ATOM   1483 C CG1 . VAL   A 1 252 ? 151.005 124.041 156.137 1.00 28.03  ? 244 VAL   A CG1 1 
ATOM   1484 C CG2 . VAL   A 1 252 ? 153.086 123.418 157.374 1.00 29.76  ? 244 VAL   A CG2 1 
ATOM   1485 N N   . CYS   A 1 253 ? 151.514 127.397 155.733 1.00 29.65  ? 245 CYS   A N   1 
ATOM   1486 C CA  . CYS   A 1 253 ? 150.592 128.254 154.998 1.00 31.73  ? 245 CYS   A CA  1 
ATOM   1487 C C   . CYS   A 1 253 ? 151.295 128.957 153.849 1.00 32.48  ? 245 CYS   A C   1 
ATOM   1488 O O   . CYS   A 1 253 ? 150.775 129.002 152.729 1.00 37.14  ? 245 CYS   A O   1 
ATOM   1489 C CB  . CYS   A 1 253 ? 149.959 129.276 155.942 1.00 31.10  ? 245 CYS   A CB  1 
ATOM   1490 S SG  . CYS   A 1 253 ? 148.687 128.606 157.035 1.00 51.02  ? 245 CYS   A SG  1 
ATOM   1491 N N   . TYR   A 1 254 ? 152.490 129.492 154.095 1.00 29.61  ? 246 TYR   A N   1 
ATOM   1492 C CA  . TYR   A 1 254 ? 153.186 130.224 153.047 1.00 28.71  ? 246 TYR   A CA  1 
ATOM   1493 C C   . TYR   A 1 254 ? 153.818 129.305 152.012 1.00 30.25  ? 246 TYR   A C   1 
ATOM   1494 O O   . TYR   A 1 254 ? 153.958 129.706 150.856 1.00 36.31  ? 246 TYR   A O   1 
ATOM   1495 C CB  . TYR   A 1 254 ? 154.228 131.157 153.656 1.00 31.63  ? 246 TYR   A CB  1 
ATOM   1496 C CG  . TYR   A 1 254 ? 153.701 132.562 153.781 1.00 37.69  ? 246 TYR   A CG  1 
ATOM   1497 C CD1 . TYR   A 1 254 ? 153.578 133.370 152.662 1.00 33.19  ? 246 TYR   A CD1 1 
ATOM   1498 C CD2 . TYR   A 1 254 ? 153.292 133.069 155.005 1.00 39.12  ? 246 TYR   A CD2 1 
ATOM   1499 C CE1 . TYR   A 1 254 ? 153.084 134.647 152.757 1.00 34.39  ? 246 TYR   A CE1 1 
ATOM   1500 C CE2 . TYR   A 1 254 ? 152.795 134.351 155.111 1.00 38.44  ? 246 TYR   A CE2 1 
ATOM   1501 C CZ  . TYR   A 1 254 ? 152.694 135.134 153.982 1.00 41.02  ? 246 TYR   A CZ  1 
ATOM   1502 O OH  . TYR   A 1 254 ? 152.202 136.411 154.071 1.00 42.45  ? 246 TYR   A OH  1 
ATOM   1503 N N   . THR   A 1 255 ? 154.180 128.076 152.380 1.00 29.41  ? 247 THR   A N   1 
ATOM   1504 C CA  . THR   A 1 255 ? 154.615 127.114 151.375 1.00 26.58  ? 247 THR   A CA  1 
ATOM   1505 C C   . THR   A 1 255 ? 153.484 126.809 150.402 1.00 30.32  ? 247 THR   A C   1 
ATOM   1506 O O   . THR   A 1 255 ? 153.675 126.828 149.179 1.00 35.21  ? 247 THR   A O   1 
ATOM   1507 C CB  . THR   A 1 255 ? 155.107 125.834 152.049 1.00 28.95  ? 247 THR   A CB  1 
ATOM   1508 O OG1 . THR   A 1 255 ? 156.232 126.132 152.884 1.00 33.41  ? 247 THR   A OG1 1 
ATOM   1509 C CG2 . THR   A 1 255 ? 155.517 124.808 151.009 1.00 33.05  ? 247 THR   A CG2 1 
ATOM   1510 N N   . LEU   A 1 256 ? 152.285 126.553 150.932 1.00 31.68  ? 248 LEU   A N   1 
ATOM   1511 C CA  . LEU   A 1 256 ? 151.140 126.317 150.056 1.00 31.74  ? 248 LEU   A CA  1 
ATOM   1512 C C   . LEU   A 1 256 ? 150.803 127.561 149.238 1.00 35.69  ? 248 LEU   A C   1 
ATOM   1513 O O   . LEU   A 1 256 ? 150.464 127.462 148.051 1.00 34.76  ? 248 LEU   A O   1 
ATOM   1514 C CB  . LEU   A 1 256 ? 149.934 125.865 150.876 1.00 32.14  ? 248 LEU   A CB  1 
ATOM   1515 C CG  . LEU   A 1 256 ? 150.128 124.565 151.656 1.00 32.70  ? 248 LEU   A CG  1 
ATOM   1516 C CD1 . LEU   A 1 256 ? 148.838 124.152 152.340 1.00 36.47  ? 248 LEU   A CD1 1 
ATOM   1517 C CD2 . LEU   A 1 256 ? 150.631 123.464 150.741 1.00 31.28  ? 248 LEU   A CD2 1 
ATOM   1518 N N   . MET   A 1 257 ? 150.898 128.742 149.855 1.00 37.31  ? 249 MET   A N   1 
ATOM   1519 C CA  . MET   A 1 257 ? 150.618 129.985 149.144 1.00 32.89  ? 249 MET   A CA  1 
ATOM   1520 C C   . MET   A 1 257 ? 151.590 130.198 147.993 1.00 34.83  ? 249 MET   A C   1 
ATOM   1521 O O   . MET   A 1 257 ? 151.186 130.601 146.898 1.00 44.03  ? 249 MET   A O   1 
ATOM   1522 C CB  . MET   A 1 257 ? 150.686 131.166 150.111 1.00 31.65  ? 249 MET   A CB  1 
ATOM   1523 C CG  . MET   A 1 257 ? 149.372 131.881 150.330 1.00 38.47  ? 249 MET   A CG  1 
ATOM   1524 S SD  . MET   A 1 257 ? 149.558 133.258 151.473 1.00 49.71  ? 249 MET   A SD  1 
ATOM   1525 C CE  . MET   A 1 257 ? 149.682 132.389 153.030 1.00 35.06  ? 249 MET   A CE  1 
ATOM   1526 N N   . ILE   A 1 258 ? 152.878 129.944 148.224 1.00 32.01  ? 250 ILE   A N   1 
ATOM   1527 C CA  . ILE   A 1 258 ? 153.879 130.135 147.182 1.00 31.35  ? 250 ILE   A CA  1 
ATOM   1528 C C   . ILE   A 1 258 ? 153.693 129.109 146.074 1.00 36.47  ? 250 ILE   A C   1 
ATOM   1529 O O   . ILE   A 1 258 ? 153.853 129.423 144.889 1.00 46.74  ? 250 ILE   A O   1 
ATOM   1530 C CB  . ILE   A 1 258 ? 155.291 130.083 147.792 1.00 29.27  ? 250 ILE   A CB  1 
ATOM   1531 C CG1 . ILE   A 1 258 ? 155.639 131.432 148.423 1.00 32.06  ? 250 ILE   A CG1 1 
ATOM   1532 C CG2 . ILE   A 1 258 ? 156.324 129.706 146.746 1.00 30.80  ? 250 ILE   A CG2 1 
ATOM   1533 C CD1 . ILE   A 1 258 ? 156.796 131.377 149.388 1.00 29.65  ? 250 ILE   A CD1 1 
ATOM   1534 N N   . LEU   A 1 259 ? 153.338 127.874 146.433 1.00 40.70  ? 251 LEU   A N   1 
ATOM   1535 C CA  . LEU   A 1 259 ? 153.025 126.878 145.413 1.00 41.67  ? 251 LEU   A CA  1 
ATOM   1536 C C   . LEU   A 1 259 ? 151.868 127.343 144.536 1.00 45.02  ? 251 LEU   A C   1 
ATOM   1537 O O   . LEU   A 1 259 ? 151.935 127.266 143.302 1.00 53.72  ? 251 LEU   A O   1 
ATOM   1538 C CB  . LEU   A 1 259 ? 152.695 125.540 146.074 1.00 43.75  ? 251 LEU   A CB  1 
ATOM   1539 C CG  . LEU   A 1 259 ? 153.818 124.511 146.193 1.00 50.48  ? 251 LEU   A CG  1 
ATOM   1540 C CD1 . LEU   A 1 259 ? 153.238 123.109 146.244 1.00 51.80  ? 251 LEU   A CD1 1 
ATOM   1541 C CD2 . LEU   A 1 259 ? 154.802 124.646 145.042 1.00 50.15  ? 251 LEU   A CD2 1 
ATOM   1542 N N   . ARG   A 1 260 ? 150.801 127.845 145.161 1.00 43.59  ? 252 ARG   A N   1 
ATOM   1543 C CA  . ARG   A 1 260 ? 149.652 128.325 144.398 1.00 44.00  ? 252 ARG   A CA  1 
ATOM   1544 C C   . ARG   A 1 260 ? 150.034 129.502 143.509 1.00 47.51  ? 252 ARG   A C   1 
ATOM   1545 O O   . ARG   A 1 260 ? 149.642 129.563 142.339 1.00 53.26  ? 252 ARG   A O   1 
ATOM   1546 C CB  . ARG   A 1 260 ? 148.517 128.716 145.342 1.00 44.38  ? 252 ARG   A CB  1 
ATOM   1547 C CG  . ARG   A 1 260 ? 147.201 128.975 144.637 1.00 40.46  ? 252 ARG   A CG  1 
ATOM   1548 C CD  . ARG   A 1 260 ? 146.363 127.713 144.557 1.00 42.89  ? 252 ARG   A CD  1 
ATOM   1549 N NE  . ARG   A 1 260 ? 145.766 127.541 143.238 1.00 50.60  ? 252 ARG   A NE  1 
ATOM   1550 C CZ  . ARG   A 1 260 ? 144.672 128.164 142.823 1.00 56.74  ? 252 ARG   A CZ  1 
ATOM   1551 N NH1 . ARG   A 1 260 ? 144.026 129.017 143.600 1.00 56.86  ? 252 ARG   A NH1 1 
ATOM   1552 N NH2 . ARG   A 1 260 ? 144.217 127.926 141.597 1.00 58.10  ? 252 ARG   A NH2 1 
ATOM   1553 N N   . LEU   A 1 261 ? 150.804 130.449 144.050 1.00 43.92  ? 253 LEU   A N   1 
ATOM   1554 C CA  . LEU   A 1 261 ? 151.202 131.617 143.271 1.00 42.35  ? 253 LEU   A CA  1 
ATOM   1555 C C   . LEU   A 1 261 ? 152.046 131.217 142.070 1.00 51.46  ? 253 LEU   A C   1 
ATOM   1556 O O   . LEU   A 1 261 ? 151.846 131.730 140.966 1.00 59.43  ? 253 LEU   A O   1 
ATOM   1557 C CB  . LEU   A 1 261 ? 151.963 132.608 144.150 1.00 38.99  ? 253 LEU   A CB  1 
ATOM   1558 C CG  . LEU   A 1 261 ? 151.165 133.385 145.197 1.00 42.36  ? 253 LEU   A CG  1 
ATOM   1559 C CD1 . LEU   A 1 261 ? 151.992 134.539 145.737 1.00 41.37  ? 253 LEU   A CD1 1 
ATOM   1560 C CD2 . LEU   A 1 261 ? 149.852 133.887 144.624 1.00 40.13  ? 253 LEU   A CD2 1 
ATOM   1561 N N   . LYS   A 1 262 ? 152.991 130.295 142.264 1.00 53.67  ? 254 LYS   A N   1 
ATOM   1562 C CA  . LYS   A 1 262 ? 153.815 129.835 141.151 1.00 54.60  ? 254 LYS   A CA  1 
ATOM   1563 C C   . LYS   A 1 262 ? 152.980 129.093 140.116 1.00 60.07  ? 254 LYS   A C   1 
ATOM   1564 O O   . LYS   A 1 262 ? 153.248 129.183 138.913 1.00 66.69  ? 254 LYS   A O   1 
ATOM   1565 C CB  . LYS   A 1 262 ? 154.944 128.945 141.669 1.00 47.39  ? 254 LYS   A CB  1 
ATOM   1566 C CG  . LYS   A 1 262 ? 156.091 129.707 142.307 1.00 50.48  ? 254 LYS   A CG  1 
ATOM   1567 C CD  . LYS   A 1 262 ? 157.190 128.766 142.769 1.00 52.58  ? 254 LYS   A CD  1 
ATOM   1568 C CE  . LYS   A 1 262 ? 158.336 129.530 143.412 1.00 59.92  ? 254 LYS   A CE  1 
ATOM   1569 N NZ  . LYS   A 1 262 ? 159.420 128.624 143.881 1.00 64.67  ? 254 LYS   A NZ  1 
ATOM   1570 N N   . SER   A 1 263 ? 151.968 128.347 140.566 1.00 57.94  ? 255 SER   A N   1 
ATOM   1571 C CA  . SER   A 1 263 ? 151.156 127.565 139.638 1.00 61.03  ? 255 SER   A CA  1 
ATOM   1572 C C   . SER   A 1 263 ? 150.410 128.460 138.652 1.00 69.15  ? 255 SER   A C   1 
ATOM   1573 O O   . SER   A 1 263 ? 150.353 128.166 137.453 1.00 72.32  ? 255 SER   A O   1 
ATOM   1574 C CB  . SER   A 1 263 ? 150.175 126.687 140.415 1.00 60.64  ? 255 SER   A CB  1 
ATOM   1575 O OG  . SER   A 1 263 ? 148.960 126.524 139.704 1.00 63.75  ? 255 SER   A OG  1 
ATOM   1576 N N   . VAL   A 1 264 ? 149.831 129.561 139.138 1.00 69.13  ? 256 VAL   A N   1 
ATOM   1577 C CA  . VAL   A 1 264 ? 148.996 130.413 138.294 1.00 69.01  ? 256 VAL   A CA  1 
ATOM   1578 C C   . VAL   A 1 264 ? 149.702 131.681 137.834 1.00 75.91  ? 256 VAL   A C   1 
ATOM   1579 O O   . VAL   A 1 264 ? 149.103 132.463 137.078 1.00 76.89  ? 256 VAL   A O   1 
ATOM   1580 C CB  . VAL   A 1 264 ? 147.680 130.794 139.007 1.00 65.18  ? 256 VAL   A CB  1 
ATOM   1581 C CG1 . VAL   A 1 264 ? 146.749 129.595 139.086 1.00 62.28  ? 256 VAL   A CG1 1 
ATOM   1582 C CG2 . VAL   A 1 264 ? 147.957 131.362 140.385 1.00 57.83  ? 256 VAL   A CG2 1 
ATOM   1583 N N   . ARG   A 1 265 ? 150.950 131.912 138.256 1.00 76.27  ? 257 ARG   A N   1 
ATOM   1584 C CA  . ARG   A 1 265 ? 151.655 133.135 137.874 1.00 84.23  ? 257 ARG   A CA  1 
ATOM   1585 C C   . ARG   A 1 265 ? 151.831 133.239 136.365 1.00 86.36  ? 257 ARG   A C   1 
ATOM   1586 O O   . ARG   A 1 265 ? 151.862 134.347 135.816 1.00 82.01  ? 257 ARG   A O   1 
ATOM   1587 C CB  . ARG   A 1 265 ? 153.012 133.195 138.581 1.00 76.77  ? 257 ARG   A CB  1 
ATOM   1588 C CG  . ARG   A 1 265 ? 154.165 133.752 137.761 1.00 83.16  ? 257 ARG   A CG  1 
ATOM   1589 C CD  . ARG   A 1 265 ? 155.484 133.562 138.498 1.00 82.11  ? 257 ARG   A CD  1 
ATOM   1590 N NE  . ARG   A 1 265 ? 156.629 134.027 137.725 1.00 84.83  ? 257 ARG   A NE  1 
ATOM   1591 C CZ  . ARG   A 1 265 ? 157.875 133.621 137.921 1.00 74.07  ? 257 ARG   A CZ  1 
ATOM   1592 N NH1 . ARG   A 1 265 ? 158.174 132.734 138.856 1.00 73.30  ? 257 ARG   A NH1 1 
ATOM   1593 N NH2 . ARG   A 1 265 ? 158.847 134.117 137.159 1.00 60.12  ? 257 ARG   A NH2 1 
ATOM   1594 N N   . LEU   A 1 266 ? 151.932 132.100 135.680 1.00 82.92  ? 258 LEU   A N   1 
ATOM   1595 C CA  . LEU   A 1 266 ? 152.170 132.118 134.242 1.00 83.82  ? 258 LEU   A CA  1 
ATOM   1596 C C   . LEU   A 1 266 ? 151.009 132.753 133.485 1.00 78.92  ? 258 LEU   A C   1 
ATOM   1597 O O   . LEU   A 1 266 ? 151.224 133.583 132.594 1.00 69.21  ? 258 LEU   A O   1 
ATOM   1598 C CB  . LEU   A 1 266 ? 152.422 130.696 133.742 1.00 89.72  ? 258 LEU   A CB  1 
ATOM   1599 C CG  . LEU   A 1 266 ? 153.217 129.769 134.666 1.00 78.90  ? 258 LEU   A CG  1 
ATOM   1600 C CD1 . LEU   A 1 266 ? 153.288 128.370 134.080 1.00 74.94  ? 258 LEU   A CD1 1 
ATOM   1601 C CD2 . LEU   A 1 266 ? 154.614 130.314 134.920 1.00 73.44  ? 258 LEU   A CD2 1 
ATOM   1602 N N   . LEU   A 1 267 ? 149.766 132.385 133.827 1.00 90.61  ? 259 LEU   A N   1 
ATOM   1603 C CA  . LEU   A 1 267 ? 148.636 132.725 132.967 1.00 98.49  ? 259 LEU   A CA  1 
ATOM   1604 C C   . LEU   A 1 267 ? 147.419 133.237 133.739 1.00 96.35  ? 259 LEU   A C   1 
ATOM   1605 O O   . LEU   A 1 267 ? 146.298 133.187 133.222 1.00 94.78  ? 259 LEU   A O   1 
ATOM   1606 C CB  . LEU   A 1 267 ? 148.219 131.523 132.111 1.00 98.79  ? 259 LEU   A CB  1 
ATOM   1607 C CG  . LEU   A 1 267 ? 149.319 130.675 131.465 1.00 93.96  ? 259 LEU   A CG  1 
ATOM   1608 C CD1 . LEU   A 1 267 ? 148.762 129.351 130.964 1.00 89.87  ? 259 LEU   A CD1 1 
ATOM   1609 C CD2 . LEU   A 1 267 ? 149.999 131.437 130.336 1.00 87.26  ? 259 LEU   A CD2 1 
ATOM   1610 N N   . SER   A 1 268 ? 147.603 133.734 134.961 1.00 87.63  ? 260 SER   A N   1 
ATOM   1611 C CA  . SER   A 1 268 ? 146.491 134.370 135.657 1.00 94.71  ? 260 SER   A CA  1 
ATOM   1612 C C   . SER   A 1 268 ? 146.152 135.705 134.998 1.00 109.80 ? 260 SER   A C   1 
ATOM   1613 O O   . SER   A 1 268 ? 147.022 136.389 134.450 1.00 112.85 ? 260 SER   A O   1 
ATOM   1614 C CB  . SER   A 1 268 ? 146.818 134.579 137.134 1.00 75.91  ? 260 SER   A CB  1 
ATOM   1615 O OG  . SER   A 1 268 ? 145.643 134.515 137.925 1.00 62.96  ? 260 SER   A OG  1 
ATOM   1616 N N   . GLY   A 1 269 ? 144.872 136.076 135.048 1.00 98.01  ? 261 GLY   A N   1 
ATOM   1617 C CA  . GLY   A 1 269 ? 144.430 137.205 134.252 1.00 93.80  ? 261 GLY   A CA  1 
ATOM   1618 C C   . GLY   A 1 269 ? 143.500 138.225 134.880 1.00 93.73  ? 261 GLY   A C   1 
ATOM   1619 O O   . GLY   A 1 269 ? 143.220 139.254 134.257 1.00 93.34  ? 261 GLY   A O   1 
ATOM   1620 N N   . SER   A 1 270 ? 143.009 137.980 136.096 1.00 92.44  ? 262 SER   A N   1 
ATOM   1621 C CA  . SER   A 1 270 ? 142.137 138.948 136.768 1.00 87.55  ? 262 SER   A CA  1 
ATOM   1622 C C   . SER   A 1 270 ? 143.026 140.021 137.389 1.00 78.55  ? 262 SER   A C   1 
ATOM   1623 O O   . SER   A 1 270 ? 143.346 140.002 138.578 1.00 76.35  ? 262 SER   A O   1 
ATOM   1624 C CB  . SER   A 1 270 ? 141.254 138.261 137.801 1.00 75.16  ? 262 SER   A CB  1 
ATOM   1625 O OG  . SER   A 1 270 ? 140.182 139.103 138.186 1.00 62.96  ? 262 SER   A OG  1 
ATOM   1626 N N   . ARG   A 1 271 ? 143.400 140.994 136.553 1.00 70.17  ? 263 ARG   A N   1 
ATOM   1627 C CA  . ARG   A 1 271 ? 144.551 141.847 136.841 1.00 71.55  ? 263 ARG   A CA  1 
ATOM   1628 C C   . ARG   A 1 271 ? 144.410 142.571 138.175 1.00 70.55  ? 263 ARG   A C   1 
ATOM   1629 O O   . ARG   A 1 271 ? 145.320 142.531 139.011 1.00 72.45  ? 263 ARG   A O   1 
ATOM   1630 C CB  . ARG   A 1 271 ? 144.748 142.848 135.701 1.00 79.95  ? 263 ARG   A CB  1 
ATOM   1631 C CG  . ARG   A 1 271 ? 145.857 142.470 134.730 1.00 76.67  ? 263 ARG   A CG  1 
ATOM   1632 C CD  . ARG   A 1 271 ? 145.323 141.663 133.558 1.00 73.17  ? 263 ARG   A CD  1 
ATOM   1633 N NE  . ARG   A 1 271 ? 146.187 141.764 132.388 1.00 72.16  ? 263 ARG   A NE  1 
ATOM   1634 C CZ  . ARG   A 1 271 ? 146.200 140.892 131.389 1.00 73.08  ? 263 ARG   A CZ  1 
ATOM   1635 N NH1 . ARG   A 1 271 ? 145.402 139.838 131.382 1.00 73.46  ? 263 ARG   A NH1 1 
ATOM   1636 N NH2 . ARG   A 1 271 ? 147.036 141.083 130.373 1.00 72.82  ? 263 ARG   A NH2 1 
ATOM   1637 N N   . GLU   A 1 272 ? 143.274 143.233 138.401 1.00 67.59  ? 264 GLU   A N   1 
ATOM   1638 C CA  . GLU   A 1 272 ? 143.117 144.042 139.607 1.00 66.78  ? 264 GLU   A CA  1 
ATOM   1639 C C   . GLU   A 1 272 ? 143.148 143.181 140.865 1.00 67.60  ? 264 GLU   A C   1 
ATOM   1640 O O   . GLU   A 1 272 ? 143.934 143.436 141.788 1.00 70.65  ? 264 GLU   A O   1 
ATOM   1641 C CB  . GLU   A 1 272 ? 141.815 144.839 139.529 1.00 73.77  ? 264 GLU   A CB  1 
ATOM   1642 C CG  . GLU   A 1 272 ? 141.604 145.809 140.679 1.00 87.02  ? 264 GLU   A CG  1 
ATOM   1643 C CD  . GLU   A 1 272 ? 140.185 146.345 140.738 1.00 94.06  ? 264 GLU   A CD  1 
ATOM   1644 O OE1 . GLU   A 1 272 ? 139.634 146.698 139.674 1.00 92.41  ? 264 GLU   A OE1 1 
ATOM   1645 O OE2 . GLU   A 1 272 ? 139.619 146.410 141.850 1.00 88.66  ? 264 GLU   A OE2 1 
ATOM   1646 N N   . LYS   A 1 273 ? 142.312 142.143 140.912 1.00 65.27  ? 265 LYS   A N   1 
ATOM   1647 C CA  . LYS   A 1 273 ? 142.226 141.318 142.112 1.00 64.80  ? 265 LYS   A CA  1 
ATOM   1648 C C   . LYS   A 1 273 ? 143.493 140.497 142.318 1.00 60.46  ? 265 LYS   A C   1 
ATOM   1649 O O   . LYS   A 1 273 ? 143.956 140.339 143.454 1.00 60.96  ? 265 LYS   A O   1 
ATOM   1650 C CB  . LYS   A 1 273 ? 140.997 140.415 142.035 1.00 68.93  ? 265 LYS   A CB  1 
ATOM   1651 C CG  . LYS   A 1 273 ? 139.783 141.093 141.423 1.00 73.76  ? 265 LYS   A CG  1 
ATOM   1652 C CD  . LYS   A 1 273 ? 138.504 140.357 141.768 1.00 84.27  ? 265 LYS   A CD  1 
ATOM   1653 C CE  . LYS   A 1 273 ? 138.007 140.745 143.152 1.00 94.31  ? 265 LYS   A CE  1 
ATOM   1654 N NZ  . LYS   A 1 273 ? 136.619 140.269 143.400 1.00 104.86 ? 265 LYS   A NZ  1 
ATOM   1655 N N   . ASP   A 1 274 ? 144.067 139.965 141.237 1.00 54.64  ? 266 ASP   A N   1 
ATOM   1656 C CA  . ASP   A 1 274 ? 145.313 139.215 141.360 1.00 52.87  ? 266 ASP   A CA  1 
ATOM   1657 C C   . ASP   A 1 274 ? 146.438 140.103 141.876 1.00 54.14  ? 266 ASP   A C   1 
ATOM   1658 O O   . ASP   A 1 274 ? 147.207 139.697 142.756 1.00 60.03  ? 266 ASP   A O   1 
ATOM   1659 C CB  . ASP   A 1 274 ? 145.682 138.595 140.010 1.00 58.66  ? 266 ASP   A CB  1 
ATOM   1660 C CG  . ASP   A 1 274 ? 146.953 137.774 140.067 1.00 64.74  ? 266 ASP   A CG  1 
ATOM   1661 O OD1 . ASP   A 1 274 ? 148.050 138.357 139.944 1.00 61.75  ? 266 ASP   A OD1 1 
ATOM   1662 O OD2 . ASP   A 1 274 ? 146.854 136.540 140.225 1.00 72.15  ? 266 ASP   A OD2 1 
ATOM   1663 N N   . ARG   A 1 275 ? 146.539 141.326 141.350 1.00 52.81  ? 267 ARG   A N   1 
ATOM   1664 C CA  . ARG   A 1 275 ? 147.563 142.253 141.815 1.00 52.55  ? 267 ARG   A CA  1 
ATOM   1665 C C   . ARG   A 1 275 ? 147.367 142.603 143.283 1.00 53.53  ? 267 ARG   A C   1 
ATOM   1666 O O   . ARG   A 1 275 ? 148.333 142.637 144.056 1.00 51.52  ? 267 ARG   A O   1 
ATOM   1667 C CB  . ARG   A 1 275 ? 147.548 143.514 140.952 1.00 61.36  ? 267 ARG   A CB  1 
ATOM   1668 C CG  . ARG   A 1 275 ? 148.446 144.626 141.452 1.00 66.16  ? 267 ARG   A CG  1 
ATOM   1669 C CD  . ARG   A 1 275 ? 147.825 145.992 141.213 1.00 68.02  ? 267 ARG   A CD  1 
ATOM   1670 N NE  . ARG   A 1 275 ? 147.009 146.018 140.006 1.00 75.33  ? 267 ARG   A NE  1 
ATOM   1671 C CZ  . ARG   A 1 275 ? 146.557 147.125 139.433 1.00 84.35  ? 267 ARG   A CZ  1 
ATOM   1672 N NH1 . ARG   A 1 275 ? 146.838 148.321 139.923 1.00 82.55  ? 267 ARG   A NH1 1 
ATOM   1673 N NH2 . ARG   A 1 275 ? 145.811 147.030 138.336 1.00 82.84  ? 267 ARG   A NH2 1 
ATOM   1674 N N   . ASN   A 1 276 ? 146.120 142.857 143.690 1.00 56.25  ? 268 ASN   A N   1 
ATOM   1675 C CA  . ASN   A 1 276 ? 145.859 143.191 145.086 1.00 53.92  ? 268 ASN   A CA  1 
ATOM   1676 C C   . ASN   A 1 276 ? 146.212 142.028 146.007 1.00 51.87  ? 268 ASN   A C   1 
ATOM   1677 O O   . ASN   A 1 276 ? 146.846 142.222 147.054 1.00 48.93  ? 268 ASN   A O   1 
ATOM   1678 C CB  . ASN   A 1 276 ? 144.396 143.594 145.254 1.00 55.93  ? 268 ASN   A CB  1 
ATOM   1679 C CG  . ASN   A 1 276 ? 144.080 144.920 144.590 1.00 69.21  ? 268 ASN   A CG  1 
ATOM   1680 O OD1 . ASN   A 1 276 ? 144.981 145.687 144.250 1.00 67.65  ? 268 ASN   A OD1 1 
ATOM   1681 N ND2 . ASN   A 1 276 ? 142.797 145.195 144.397 1.00 75.80  ? 268 ASN   A ND2 1 
ATOM   1682 N N   . LEU   A 1 277 ? 145.824 140.809 145.624 1.00 46.61  ? 269 LEU   A N   1 
ATOM   1683 C CA  . LEU   A 1 277 ? 146.132 139.639 146.438 1.00 39.88  ? 269 LEU   A CA  1 
ATOM   1684 C C   . LEU   A 1 277 ? 147.635 139.445 146.568 1.00 43.11  ? 269 LEU   A C   1 
ATOM   1685 O O   . LEU   A 1 277 ? 148.150 139.194 147.665 1.00 45.16  ? 269 LEU   A O   1 
ATOM   1686 C CB  . LEU   A 1 277 ? 145.485 138.397 145.829 1.00 37.84  ? 269 LEU   A CB  1 
ATOM   1687 C CG  . LEU   A 1 277 ? 144.239 137.846 146.518 1.00 41.43  ? 269 LEU   A CG  1 
ATOM   1688 C CD1 . LEU   A 1 277 ? 143.029 138.693 146.176 1.00 49.10  ? 269 LEU   A CD1 1 
ATOM   1689 C CD2 . LEU   A 1 277 ? 144.016 136.403 146.113 1.00 38.09  ? 269 LEU   A CD2 1 
ATOM   1690 N N   . ARG   A 1 278 ? 148.360 139.570 145.454 1.00 40.50  ? 270 ARG   A N   1 
ATOM   1691 C CA  . ARG   A 1 278 ? 149.802 139.366 145.479 1.00 38.55  ? 270 ARG   A CA  1 
ATOM   1692 C C   . ARG   A 1 278 ? 150.527 140.461 146.249 1.00 41.63  ? 270 ARG   A C   1 
ATOM   1693 O O   . ARG   A 1 278 ? 151.585 140.195 146.827 1.00 40.68  ? 270 ARG   A O   1 
ATOM   1694 C CB  . ARG   A 1 278 ? 150.333 139.270 144.049 1.00 41.78  ? 270 ARG   A CB  1 
ATOM   1695 C CG  . ARG   A 1 278 ? 149.976 137.958 143.371 1.00 42.18  ? 270 ARG   A CG  1 
ATOM   1696 C CD  . ARG   A 1 278 ? 150.556 137.848 141.974 1.00 42.71  ? 270 ARG   A CD  1 
ATOM   1697 N NE  . ARG   A 1 278 ? 149.889 136.804 141.205 1.00 45.39  ? 270 ARG   A NE  1 
ATOM   1698 C CZ  . ARG   A 1 278 ? 150.376 135.586 141.012 1.00 48.11  ? 270 ARG   A CZ  1 
ATOM   1699 N NH1 . ARG   A 1 278 ? 151.553 135.228 141.494 1.00 50.05  ? 270 ARG   A NH1 1 
ATOM   1700 N NH2 . ARG   A 1 278 ? 149.662 134.705 140.317 1.00 48.76  ? 270 ARG   A NH2 1 
ATOM   1701 N N   . ARG   A 1 279 ? 149.988 141.680 146.273 1.00 45.96  ? 271 ARG   A N   1 
ATOM   1702 C CA  . ARG   A 1 279 ? 150.591 142.741 147.070 1.00 43.18  ? 271 ARG   A CA  1 
ATOM   1703 C C   . ARG   A 1 279 ? 150.356 142.555 148.566 1.00 43.26  ? 271 ARG   A C   1 
ATOM   1704 O O   . ARG   A 1 279 ? 151.291 142.718 149.362 1.00 42.89  ? 271 ARG   A O   1 
ATOM   1705 C CB  . ARG   A 1 279 ? 150.063 144.103 146.617 1.00 46.70  ? 271 ARG   A CB  1 
ATOM   1706 C CG  . ARG   A 1 279 ? 150.810 144.670 145.423 1.00 55.91  ? 271 ARG   A CG  1 
ATOM   1707 C CD  . ARG   A 1 279 ? 150.317 146.054 145.041 1.00 63.10  ? 271 ARG   A CD  1 
ATOM   1708 N NE  . ARG   A 1 279 ? 150.909 146.503 143.785 1.00 75.71  ? 271 ARG   A NE  1 
ATOM   1709 C CZ  . ARG   A 1 279 ? 150.403 147.457 143.016 1.00 83.28  ? 271 ARG   A CZ  1 
ATOM   1710 N NH1 . ARG   A 1 279 ? 149.292 148.094 143.346 1.00 81.31  ? 271 ARG   A NH1 1 
ATOM   1711 N NH2 . ARG   A 1 279 ? 151.026 147.778 141.887 1.00 86.36  ? 271 ARG   A NH2 1 
ATOM   1712 N N   . ILE   A 1 280 ? 149.132 142.211 148.978 1.00 42.65  ? 272 ILE   A N   1 
ATOM   1713 C CA  . ILE   A 1 280 ? 148.914 141.980 150.406 1.00 40.22  ? 272 ILE   A CA  1 
ATOM   1714 C C   . ILE   A 1 280 ? 149.642 140.736 150.900 1.00 40.53  ? 272 ILE   A C   1 
ATOM   1715 O O   . ILE   A 1 280 ? 150.132 140.730 152.037 1.00 41.38  ? 272 ILE   A O   1 
ATOM   1716 C CB  . ILE   A 1 280 ? 147.421 141.899 150.784 1.00 43.35  ? 272 ILE   A CB  1 
ATOM   1717 C CG1 . ILE   A 1 280 ? 146.568 142.860 149.956 1.00 45.56  ? 272 ILE   A CG1 1 
ATOM   1718 C CG2 . ILE   A 1 280 ? 147.239 142.184 152.266 1.00 47.47  ? 272 ILE   A CG2 1 
ATOM   1719 C CD1 . ILE   A 1 280 ? 147.036 144.309 149.994 1.00 49.94  ? 272 ILE   A CD1 1 
ATOM   1720 N N   . THR   A 1 281 ? 149.724 139.677 150.092 1.00 36.93  ? 273 THR   A N   1 
ATOM   1721 C CA  . THR   A 1 281 ? 150.499 138.507 150.493 1.00 35.29  ? 273 THR   A CA  1 
ATOM   1722 C C   . THR   A 1 281 ? 151.963 138.876 150.710 1.00 36.65  ? 273 THR   A C   1 
ATOM   1723 O O   . THR   A 1 281 ? 152.579 138.463 151.697 1.00 36.42  ? 273 THR   A O   1 
ATOM   1724 C CB  . THR   A 1 281 ? 150.368 137.400 149.444 1.00 40.29  ? 273 THR   A CB  1 
ATOM   1725 O OG1 . THR   A 1 281 ? 148.991 137.032 149.307 1.00 35.05  ? 273 THR   A OG1 1 
ATOM   1726 C CG2 . THR   A 1 281 ? 151.171 136.178 149.855 1.00 41.87  ? 273 THR   A CG2 1 
ATOM   1727 N N   . LYS   A 1 282 ? 152.536 139.646 149.784 1.00 37.05  ? 274 LYS   A N   1 
ATOM   1728 C CA  . LYS   A 1 282 ? 153.873 140.215 149.918 1.00 33.84  ? 274 LYS   A CA  1 
ATOM   1729 C C   . LYS   A 1 282 ? 154.047 140.968 151.231 1.00 34.33  ? 274 LYS   A C   1 
ATOM   1730 O O   . LYS   A 1 282 ? 155.016 140.738 151.963 1.00 37.60  ? 274 LYS   A O   1 
ATOM   1731 C CB  . LYS   A 1 282 ? 154.156 141.152 148.741 1.00 41.21  ? 274 LYS   A CB  1 
ATOM   1732 C CG  . LYS   A 1 282 ? 155.625 141.390 148.422 1.00 41.64  ? 274 LYS   A CG  1 
ATOM   1733 C CD  . LYS   A 1 282 ? 156.520 140.266 148.901 1.00 56.10  ? 274 LYS   A CD  1 
ATOM   1734 C CE  . LYS   A 1 282 ? 157.950 140.489 148.439 1.00 64.95  ? 274 LYS   A CE  1 
ATOM   1735 N NZ  . LYS   A 1 282 ? 158.887 139.458 148.966 1.00 82.70  ? 274 LYS   A NZ  1 
ATOM   1736 N N   . LEU   A 1 283 ? 153.121 141.884 151.523 1.00 35.38  ? 275 LEU   A N   1 
ATOM   1737 C CA  . LEU   A 1 283 ? 153.231 142.698 152.730 1.00 37.01  ? 275 LEU   A CA  1 
ATOM   1738 C C   . LEU   A 1 283 ? 153.201 141.834 153.986 1.00 35.46  ? 275 LEU   A C   1 
ATOM   1739 O O   . LEU   A 1 283 ? 154.022 142.006 154.898 1.00 38.84  ? 275 LEU   A O   1 
ATOM   1740 C CB  . LEU   A 1 283 ? 152.106 143.735 152.761 1.00 39.47  ? 275 LEU   A CB  1 
ATOM   1741 C CG  . LEU   A 1 283 ? 151.664 144.274 154.122 1.00 35.42  ? 275 LEU   A CG  1 
ATOM   1742 C CD1 . LEU   A 1 283 ? 152.692 145.238 154.684 1.00 41.83  ? 275 LEU   A CD1 1 
ATOM   1743 C CD2 . LEU   A 1 283 ? 150.310 144.948 154.007 1.00 42.43  ? 275 LEU   A CD2 1 
ATOM   1744 N N   . VAL   A 1 284 ? 152.261 140.889 154.044 1.00 34.55  ? 276 VAL   A N   1 
ATOM   1745 C CA  . VAL   A 1 284 ? 152.145 140.026 155.216 1.00 31.67  ? 276 VAL   A CA  1 
ATOM   1746 C C   . VAL   A 1 284 ? 153.388 139.159 155.364 1.00 31.77  ? 276 VAL   A C   1 
ATOM   1747 O O   . VAL   A 1 284 ? 153.889 138.950 156.476 1.00 35.26  ? 276 VAL   A O   1 
ATOM   1748 C CB  . VAL   A 1 284 ? 150.862 139.179 155.131 1.00 30.21  ? 276 VAL   A CB  1 
ATOM   1749 C CG1 . VAL   A 1 284 ? 150.795 138.192 156.281 1.00 32.10  ? 276 VAL   A CG1 1 
ATOM   1750 C CG2 . VAL   A 1 284 ? 149.639 140.074 155.133 1.00 34.98  ? 276 VAL   A CG2 1 
ATOM   1751 N N   . LEU   A 1 285 ? 153.908 138.641 154.248 1.00 32.95  ? 277 LEU   A N   1 
ATOM   1752 C CA  . LEU   A 1 285 ? 155.107 137.813 154.300 1.00 32.17  ? 277 LEU   A CA  1 
ATOM   1753 C C   . LEU   A 1 285 ? 156.301 138.604 154.814 1.00 30.98  ? 277 LEU   A C   1 
ATOM   1754 O O   . LEU   A 1 285 ? 157.083 138.099 155.626 1.00 29.82  ? 277 LEU   A O   1 
ATOM   1755 C CB  . LEU   A 1 285 ? 155.406 137.236 152.917 1.00 38.55  ? 277 LEU   A CB  1 
ATOM   1756 C CG  . LEU   A 1 285 ? 156.754 136.536 152.743 1.00 40.65  ? 277 LEU   A CG  1 
ATOM   1757 C CD1 . LEU   A 1 285 ? 156.854 135.331 153.666 1.00 37.44  ? 277 LEU   A CD1 1 
ATOM   1758 C CD2 . LEU   A 1 285 ? 156.966 136.127 151.296 1.00 35.28  ? 277 LEU   A CD2 1 
ATOM   1759 N N   . VAL   A 1 286 ? 156.461 139.844 154.348 1.00 32.51  ? 278 VAL   A N   1 
ATOM   1760 C CA  . VAL   A 1 286 ? 157.580 140.661 154.806 1.00 29.99  ? 278 VAL   A CA  1 
ATOM   1761 C C   . VAL   A 1 286 ? 157.443 140.976 156.291 1.00 30.03  ? 278 VAL   A C   1 
ATOM   1762 O O   . VAL   A 1 286 ? 158.429 140.943 157.037 1.00 29.17  ? 278 VAL   A O   1 
ATOM   1763 C CB  . VAL   A 1 286 ? 157.697 141.940 153.959 1.00 31.59  ? 278 VAL   A CB  1 
ATOM   1764 C CG1 . VAL   A 1 286 ? 158.748 142.866 154.544 1.00 32.20  ? 278 VAL   A CG1 1 
ATOM   1765 C CG2 . VAL   A 1 286 ? 158.050 141.591 152.526 1.00 35.55  ? 278 VAL   A CG2 1 
ATOM   1766 N N   . VAL   A 1 287 ? 156.225 141.281 156.747 1.00 32.93  ? 279 VAL   A N   1 
ATOM   1767 C CA  . VAL   A 1 287 ? 156.020 141.559 158.168 1.00 29.92  ? 279 VAL   A CA  1 
ATOM   1768 C C   . VAL   A 1 287 ? 156.358 140.332 159.009 1.00 30.02  ? 279 VAL   A C   1 
ATOM   1769 O O   . VAL   A 1 287 ? 157.043 140.432 160.037 1.00 31.95  ? 279 VAL   A O   1 
ATOM   1770 C CB  . VAL   A 1 287 ? 154.577 142.037 158.414 1.00 32.87  ? 279 VAL   A CB  1 
ATOM   1771 C CG1 . VAL   A 1 287 ? 154.253 142.015 159.896 1.00 33.36  ? 279 VAL   A CG1 1 
ATOM   1772 C CG2 . VAL   A 1 287 ? 154.378 143.431 157.846 1.00 36.54  ? 279 VAL   A CG2 1 
ATOM   1773 N N   . VAL   A 1 288 ? 155.893 139.156 158.581 1.00 30.20  ? 280 VAL   A N   1 
ATOM   1774 C CA  . VAL   A 1 288 ? 156.163 137.925 159.320 1.00 27.34  ? 280 VAL   A CA  1 
ATOM   1775 C C   . VAL   A 1 288 ? 157.658 137.631 159.347 1.00 32.07  ? 280 VAL   A C   1 
ATOM   1776 O O   . VAL   A 1 288 ? 158.212 137.253 160.387 1.00 35.40  ? 280 VAL   A O   1 
ATOM   1777 C CB  . VAL   A 1 288 ? 155.366 136.755 158.714 1.00 27.79  ? 280 VAL   A CB  1 
ATOM   1778 C CG1 . VAL   A 1 288 ? 155.980 135.428 159.115 1.00 28.32  ? 280 VAL   A CG1 1 
ATOM   1779 C CG2 . VAL   A 1 288 ? 153.912 136.825 159.145 1.00 31.07  ? 280 VAL   A CG2 1 
ATOM   1780 N N   . ALA   A 1 289 ? 158.333 137.795 158.208 1.00 33.51  ? 281 ALA   A N   1 
ATOM   1781 C CA  . ALA   A 1 289 ? 159.770 137.563 158.151 1.00 28.61  ? 281 ALA   A CA  1 
ATOM   1782 C C   . ALA   A 1 289 ? 160.544 138.519 159.044 1.00 31.95  ? 281 ALA   A C   1 
ATOM   1783 O O   . ALA   A 1 289 ? 161.481 138.087 159.720 1.00 34.04  ? 281 ALA   A O   1 
ATOM   1784 C CB  . ALA   A 1 289 ? 160.266 137.680 156.711 1.00 26.34  ? 281 ALA   A CB  1 
ATOM   1785 N N   . VAL   A 1 290 ? 160.174 139.799 159.067 1.00 34.63  ? 282 VAL   A N   1 
ATOM   1786 C CA  . VAL   A 1 290 ? 160.836 140.748 159.955 1.00 30.87  ? 282 VAL   A CA  1 
ATOM   1787 C C   . VAL   A 1 290 ? 160.620 140.361 161.411 1.00 36.31  ? 282 VAL   A C   1 
ATOM   1788 O O   . VAL   A 1 290 ? 161.554 140.405 162.220 1.00 41.05  ? 282 VAL   A O   1 
ATOM   1789 C CB  . VAL   A 1 290 ? 160.346 142.177 159.662 1.00 30.07  ? 282 VAL   A CB  1 
ATOM   1790 C CG1 . VAL   A 1 290 ? 160.758 143.123 160.777 1.00 31.28  ? 282 VAL   A CG1 1 
ATOM   1791 C CG2 . VAL   A 1 290 ? 160.893 142.654 158.330 1.00 34.13  ? 282 VAL   A CG2 1 
ATOM   1792 N N   . PHE   A 1 291 ? 159.394 139.964 161.766 1.00 38.38  ? 283 PHE   A N   1 
ATOM   1793 C CA  . PHE   A 1 291 ? 159.129 139.536 163.137 1.00 38.06  ? 283 PHE   A CA  1 
ATOM   1794 C C   . PHE   A 1 291 ? 159.969 138.322 163.513 1.00 37.21  ? 283 PHE   A C   1 
ATOM   1795 O O   . PHE   A 1 291 ? 160.488 138.242 164.632 1.00 40.55  ? 283 PHE   A O   1 
ATOM   1796 C CB  . PHE   A 1 291 ? 157.643 139.230 163.317 1.00 34.27  ? 283 PHE   A CB  1 
ATOM   1797 C CG  . PHE   A 1 291 ? 157.279 138.767 164.702 1.00 35.48  ? 283 PHE   A CG  1 
ATOM   1798 C CD1 . PHE   A 1 291 ? 156.903 139.678 165.673 1.00 38.48  ? 283 PHE   A CD1 1 
ATOM   1799 C CD2 . PHE   A 1 291 ? 157.296 137.421 165.029 1.00 36.89  ? 283 PHE   A CD2 1 
ATOM   1800 C CE1 . PHE   A 1 291 ? 156.565 139.258 166.944 1.00 37.34  ? 283 PHE   A CE1 1 
ATOM   1801 C CE2 . PHE   A 1 291 ? 156.960 136.997 166.297 1.00 39.13  ? 283 PHE   A CE2 1 
ATOM   1802 C CZ  . PHE   A 1 291 ? 156.593 137.916 167.255 1.00 40.40  ? 283 PHE   A CZ  1 
ATOM   1803 N N   . ILE   A 1 292 ? 160.095 137.359 162.603 1.00 38.98  ? 284 ILE   A N   1 
ATOM   1804 C CA  . ILE   A 1 292 ? 160.821 136.126 162.887 1.00 38.03  ? 284 ILE   A CA  1 
ATOM   1805 C C   . ILE   A 1 292 ? 162.287 136.432 163.165 1.00 41.28  ? 284 ILE   A C   1 
ATOM   1806 O O   . ILE   A 1 292 ? 162.862 135.916 164.128 1.00 44.73  ? 284 ILE   A O   1 
ATOM   1807 C CB  . ILE   A 1 292 ? 160.675 135.114 161.736 1.00 35.70  ? 284 ILE   A CB  1 
ATOM   1808 C CG1 . ILE   A 1 292 ? 159.270 134.513 161.735 1.00 37.86  ? 284 ILE   A CG1 1 
ATOM   1809 C CG2 . ILE   A 1 292 ? 161.712 134.012 161.853 1.00 31.77  ? 284 ILE   A CG2 1 
ATOM   1810 C CD1 . ILE   A 1 292 ? 158.975 133.663 160.523 1.00 43.58  ? 284 ILE   A CD1 1 
ATOM   1811 N N   . ILE   A 1 293 ? 162.904 137.279 162.338 1.00 38.01  ? 285 ILE   A N   1 
ATOM   1812 C CA  . ILE   A 1 293 ? 164.314 137.592 162.545 1.00 40.27  ? 285 ILE   A CA  1 
ATOM   1813 C C   . ILE   A 1 293 ? 164.520 138.533 163.724 1.00 43.34  ? 285 ILE   A C   1 
ATOM   1814 O O   . ILE   A 1 293 ? 165.610 138.561 164.302 1.00 48.49  ? 285 ILE   A O   1 
ATOM   1815 C CB  . ILE   A 1 293 ? 164.948 138.169 161.259 1.00 41.79  ? 285 ILE   A CB  1 
ATOM   1816 C CG1 . ILE   A 1 293 ? 164.633 139.658 161.109 1.00 42.54  ? 285 ILE   A CG1 1 
ATOM   1817 C CG2 . ILE   A 1 293 ? 164.505 137.379 160.037 1.00 40.22  ? 285 ILE   A CG2 1 
ATOM   1818 C CD1 . ILE   A 1 293 ? 165.038 140.234 159.772 1.00 46.05  ? 285 ILE   A CD1 1 
ATOM   1819 N N   . CYS   A 1 294 ? 163.502 139.312 164.100 1.00 41.49  ? 286 CYS   A N   1 
ATOM   1820 C CA  . CYS   A 1 294 ? 163.642 140.175 165.267 1.00 39.34  ? 286 CYS   A CA  1 
ATOM   1821 C C   . CYS   A 1 294 ? 163.488 139.410 166.576 1.00 39.88  ? 286 CYS   A C   1 
ATOM   1822 O O   . CYS   A 1 294 ? 164.167 139.730 167.557 1.00 42.85  ? 286 CYS   A O   1 
ATOM   1823 C CB  . CYS   A 1 294 ? 162.625 141.314 165.207 1.00 44.34  ? 286 CYS   A CB  1 
ATOM   1824 S SG  . CYS   A 1 294 ? 163.232 142.813 164.401 1.00 61.34  ? 286 CYS   A SG  1 
ATOM   1825 N N   . TRP   A 1 295 ? 162.613 138.406 166.616 1.00 41.45  ? 287 TRP   A N   1 
ATOM   1826 C CA  . TRP   A 1 295 ? 162.339 137.677 167.845 1.00 39.10  ? 287 TRP   A CA  1 
ATOM   1827 C C   . TRP   A 1 295 ? 163.018 136.317 167.920 1.00 39.79  ? 287 TRP   A C   1 
ATOM   1828 O O   . TRP   A 1 295 ? 162.883 135.636 168.942 1.00 41.84  ? 287 TRP   A O   1 
ATOM   1829 C CB  . TRP   A 1 295 ? 160.825 137.492 168.020 1.00 38.52  ? 287 TRP   A CB  1 
ATOM   1830 C CG  . TRP   A 1 295 ? 160.160 138.653 168.684 1.00 38.38  ? 287 TRP   A CG  1 
ATOM   1831 C CD1 . TRP   A 1 295 ? 159.719 139.795 168.087 1.00 37.49  ? 287 TRP   A CD1 1 
ATOM   1832 C CD2 . TRP   A 1 295 ? 159.859 138.787 170.077 1.00 37.97  ? 287 TRP   A CD2 1 
ATOM   1833 N NE1 . TRP   A 1 295 ? 159.160 140.632 169.020 1.00 38.52  ? 287 TRP   A NE1 1 
ATOM   1834 C CE2 . TRP   A 1 295 ? 159.234 140.036 170.251 1.00 37.51  ? 287 TRP   A CE2 1 
ATOM   1835 C CE3 . TRP   A 1 295 ? 160.056 137.971 171.194 1.00 39.63  ? 287 TRP   A CE3 1 
ATOM   1836 C CZ2 . TRP   A 1 295 ? 158.806 140.488 171.495 1.00 41.53  ? 287 TRP   A CZ2 1 
ATOM   1837 C CZ3 . TRP   A 1 295 ? 159.631 138.421 172.427 1.00 39.65  ? 287 TRP   A CZ3 1 
ATOM   1838 C CH2 . TRP   A 1 295 ? 159.013 139.668 172.568 1.00 41.66  ? 287 TRP   A CH2 1 
ATOM   1839 N N   . THR   A 1 296 ? 163.720 135.894 166.873 1.00 38.59  ? 288 THR   A N   1 
ATOM   1840 C CA  . THR   A 1 296 ? 164.424 134.614 166.922 1.00 36.55  ? 288 THR   A CA  1 
ATOM   1841 C C   . THR   A 1 296 ? 165.582 134.607 167.913 1.00 39.93  ? 288 THR   A C   1 
ATOM   1842 O O   . THR   A 1 296 ? 165.665 133.662 168.716 1.00 42.28  ? 288 THR   A O   1 
ATOM   1843 C CB  . THR   A 1 296 ? 164.888 134.230 165.512 1.00 40.29  ? 288 THR   A CB  1 
ATOM   1844 O OG1 . THR   A 1 296 ? 163.774 133.736 164.760 1.00 45.91  ? 288 THR   A OG1 1 
ATOM   1845 C CG2 . THR   A 1 296 ? 165.961 133.156 165.574 1.00 38.65  ? 288 THR   A CG2 1 
ATOM   1846 N N   . PRO   A 1 297 ? 166.502 135.586 167.919 1.00 38.73  ? 289 PRO   A N   1 
ATOM   1847 C CA  . PRO   A 1 297 ? 167.646 135.482 168.841 1.00 35.79  ? 289 PRO   A CA  1 
ATOM   1848 C C   . PRO   A 1 297 ? 167.258 135.415 170.308 1.00 35.24  ? 289 PRO   A C   1 
ATOM   1849 O O   . PRO   A 1 297 ? 167.904 134.693 171.076 1.00 37.20  ? 289 PRO   A O   1 
ATOM   1850 C CB  . PRO   A 1 297 ? 168.457 136.748 168.530 1.00 35.32  ? 289 PRO   A CB  1 
ATOM   1851 C CG  . PRO   A 1 297 ? 168.069 137.117 167.155 1.00 35.12  ? 289 PRO   A CG  1 
ATOM   1852 C CD  . PRO   A 1 297 ? 166.620 136.778 167.061 1.00 38.92  ? 289 PRO   A CD  1 
ATOM   1853 N N   . ILE   A 1 298 ? 166.220 136.143 170.724 1.00 37.29  ? 290 ILE   A N   1 
ATOM   1854 C CA  . ILE   A 1 298 ? 165.886 136.190 172.144 1.00 35.53  ? 290 ILE   A CA  1 
ATOM   1855 C C   . ILE   A 1 298 ? 165.322 134.853 172.612 1.00 38.42  ? 290 ILE   A C   1 
ATOM   1856 O O   . ILE   A 1 298 ? 165.637 134.387 173.712 1.00 43.12  ? 290 ILE   A O   1 
ATOM   1857 C CB  . ILE   A 1 298 ? 164.929 137.362 172.438 1.00 36.36  ? 290 ILE   A CB  1 
ATOM   1858 C CG1 . ILE   A 1 298 ? 164.653 137.461 173.939 1.00 41.38  ? 290 ILE   A CG1 1 
ATOM   1859 C CG2 . ILE   A 1 298 ? 163.636 137.237 171.650 1.00 40.17  ? 290 ILE   A CG2 1 
ATOM   1860 C CD1 . ILE   A 1 298 ? 165.900 137.630 174.777 1.00 39.83  ? 290 ILE   A CD1 1 
ATOM   1861 N N   . HIS   A 1 299 ? 164.495 134.206 171.786 1.00 37.92  ? 291 HIS   A N   1 
ATOM   1862 C CA  . HIS   A 1 299 ? 163.949 132.902 172.152 1.00 35.28  ? 291 HIS   A CA  1 
ATOM   1863 C C   . HIS   A 1 299 ? 165.058 131.870 172.310 1.00 39.81  ? 291 HIS   A C   1 
ATOM   1864 O O   . HIS   A 1 299 ? 165.092 131.117 173.292 1.00 46.21  ? 291 HIS   A O   1 
ATOM   1865 C CB  . HIS   A 1 299 ? 162.939 132.446 171.099 1.00 36.50  ? 291 HIS   A CB  1 
ATOM   1866 C CG  . HIS   A 1 299 ? 161.553 132.966 171.320 1.00 43.24  ? 291 HIS   A CG  1 
ATOM   1867 N ND1 . HIS   A 1 299 ? 161.069 134.086 170.681 1.00 42.84  ? 291 HIS   A ND1 1 
ATOM   1868 C CD2 . HIS   A 1 299 ? 160.545 132.512 172.100 1.00 48.50  ? 291 HIS   A CD2 1 
ATOM   1869 C CE1 . HIS   A 1 299 ? 159.823 134.304 171.063 1.00 43.76  ? 291 HIS   A CE1 1 
ATOM   1870 N NE2 . HIS   A 1 299 ? 159.481 133.363 171.924 1.00 46.81  ? 291 HIS   A NE2 1 
ATOM   1871 N N   . ILE   A 1 300 ? 165.985 131.831 171.352 1.00 38.93  ? 292 ILE   A N   1 
ATOM   1872 C CA  . ILE   A 1 300 ? 167.088 130.877 171.414 1.00 38.06  ? 292 ILE   A CA  1 
ATOM   1873 C C   . ILE   A 1 300 ? 167.980 131.169 172.612 1.00 41.76  ? 292 ILE   A C   1 
ATOM   1874 O O   . ILE   A 1 300 ? 168.424 130.249 173.309 1.00 48.61  ? 292 ILE   A O   1 
ATOM   1875 C CB  . ILE   A 1 300 ? 167.883 130.895 170.095 1.00 32.48  ? 292 ILE   A CB  1 
ATOM   1876 C CG1 . ILE   A 1 300 ? 167.031 130.337 168.956 1.00 41.09  ? 292 ILE   A CG1 1 
ATOM   1877 C CG2 . ILE   A 1 300 ? 169.170 130.101 170.232 1.00 25.49  ? 292 ILE   A CG2 1 
ATOM   1878 C CD1 . ILE   A 1 300 ? 167.656 130.511 167.591 1.00 52.46  ? 292 ILE   A CD1 1 
ATOM   1879 N N   . PHE   A 1 301 ? 168.263 132.448 172.869 1.00 37.49  ? 293 PHE   A N   1 
ATOM   1880 C CA  . PHE   A 1 301 ? 169.107 132.797 174.007 1.00 38.00  ? 293 PHE   A CA  1 
ATOM   1881 C C   . PHE   A 1 301 ? 168.454 132.394 175.322 1.00 43.67  ? 293 PHE   A C   1 
ATOM   1882 O O   . PHE   A 1 301 ? 169.121 131.858 176.214 1.00 51.46  ? 293 PHE   A O   1 
ATOM   1883 C CB  . PHE   A 1 301 ? 169.415 134.293 174.001 1.00 42.65  ? 293 PHE   A CB  1 
ATOM   1884 C CG  . PHE   A 1 301 ? 170.466 134.695 174.995 1.00 53.45  ? 293 PHE   A CG  1 
ATOM   1885 C CD1 . PHE   A 1 301 ? 170.120 135.046 176.288 1.00 57.87  ? 293 PHE   A CD1 1 
ATOM   1886 C CD2 . PHE   A 1 301 ? 171.803 134.714 174.637 1.00 57.79  ? 293 PHE   A CD2 1 
ATOM   1887 C CE1 . PHE   A 1 301 ? 171.086 135.409 177.202 1.00 61.57  ? 293 PHE   A CE1 1 
ATOM   1888 C CE2 . PHE   A 1 301 ? 172.773 135.079 175.548 1.00 61.90  ? 293 PHE   A CE2 1 
ATOM   1889 C CZ  . PHE   A 1 301 ? 172.414 135.427 176.832 1.00 62.13  ? 293 PHE   A CZ  1 
ATOM   1890 N N   . ILE   A 1 302 ? 167.152 132.647 175.462 1.00 42.48  ? 294 ILE   A N   1 
ATOM   1891 C CA  . ILE   A 1 302 ? 166.447 132.274 176.684 1.00 42.13  ? 294 ILE   A CA  1 
ATOM   1892 C C   . ILE   A 1 302 ? 166.456 130.762 176.861 1.00 42.58  ? 294 ILE   A C   1 
ATOM   1893 O O   . ILE   A 1 302 ? 166.682 130.253 177.966 1.00 48.39  ? 294 ILE   A O   1 
ATOM   1894 C CB  . ILE   A 1 302 ? 165.015 132.839 176.665 1.00 41.13  ? 294 ILE   A CB  1 
ATOM   1895 C CG1 . ILE   A 1 302 ? 165.036 134.360 176.837 1.00 37.89  ? 294 ILE   A CG1 1 
ATOM   1896 C CG2 . ILE   A 1 302 ? 164.167 132.192 177.741 1.00 44.74  ? 294 ILE   A CG2 1 
ATOM   1897 C CD1 . ILE   A 1 302 ? 165.245 134.820 178.261 1.00 37.86  ? 294 ILE   A CD1 1 
ATOM   1898 N N   . LEU   A 1 303 ? 166.220 130.020 175.776 1.00 41.83  ? 295 LEU   A N   1 
ATOM   1899 C CA  . LEU   A 1 303 ? 166.230 128.562 175.860 1.00 46.09  ? 295 LEU   A CA  1 
ATOM   1900 C C   . LEU   A 1 303 ? 167.607 128.036 176.251 1.00 49.71  ? 295 LEU   A C   1 
ATOM   1901 O O   . LEU   A 1 303 ? 167.719 127.124 177.080 1.00 50.82  ? 295 LEU   A O   1 
ATOM   1902 C CB  . LEU   A 1 303 ? 165.782 127.963 174.528 1.00 49.35  ? 295 LEU   A CB  1 
ATOM   1903 C CG  . LEU   A 1 303 ? 165.401 126.483 174.526 1.00 52.59  ? 295 LEU   A CG  1 
ATOM   1904 C CD1 . LEU   A 1 303 ? 164.059 126.276 175.204 1.00 46.04  ? 295 LEU   A CD1 1 
ATOM   1905 C CD2 . LEU   A 1 303 ? 165.381 125.943 173.106 1.00 48.55  ? 295 LEU   A CD2 1 
ATOM   1906 N N   . VAL   A 1 304 ? 168.668 128.598 175.666 1.00 49.53  ? 296 VAL   A N   1 
ATOM   1907 C CA  . VAL   A 1 304 ? 170.021 128.149 175.981 1.00 50.43  ? 296 VAL   A CA  1 
ATOM   1908 C C   . VAL   A 1 304 ? 170.373 128.473 177.428 1.00 55.69  ? 296 VAL   A C   1 
ATOM   1909 O O   . VAL   A 1 304 ? 170.984 127.658 178.129 1.00 57.62  ? 296 VAL   A O   1 
ATOM   1910 C CB  . VAL   A 1 304 ? 171.030 128.768 174.995 1.00 46.03  ? 296 VAL   A CB  1 
ATOM   1911 C CG1 . VAL   A 1 304 ? 172.453 128.565 175.484 1.00 52.82  ? 296 VAL   A CG1 1 
ATOM   1912 C CG2 . VAL   A 1 304 ? 170.856 128.162 173.615 1.00 44.05  ? 296 VAL   A CG2 1 
ATOM   1913 N N   . GLU   A 1 305 ? 169.994 129.663 177.900 1.00 55.82  ? 297 GLU   A N   1 
ATOM   1914 C CA  . GLU   A 1 305 ? 170.243 130.020 179.293 1.00 58.15  ? 297 GLU   A CA  1 
ATOM   1915 C C   . GLU   A 1 305 ? 169.488 129.099 180.244 1.00 59.21  ? 297 GLU   A C   1 
ATOM   1916 O O   . GLU   A 1 305 ? 170.020 128.702 181.287 1.00 60.45  ? 297 GLU   A O   1 
ATOM   1917 C CB  . GLU   A 1 305 ? 169.855 131.477 179.537 1.00 61.95  ? 297 GLU   A CB  1 
ATOM   1918 C CG  . GLU   A 1 305 ? 170.534 132.110 180.737 1.00 73.35  ? 297 GLU   A CG  1 
ATOM   1919 C CD  . GLU   A 1 305 ? 170.322 133.609 180.798 1.00 84.91  ? 297 GLU   A CD  1 
ATOM   1920 O OE1 . GLU   A 1 305 ? 169.152 134.045 180.795 1.00 89.04  ? 297 GLU   A OE1 1 
ATOM   1921 O OE2 . GLU   A 1 305 ? 171.325 134.351 180.850 1.00 90.33  ? 297 GLU   A OE2 1 
ATOM   1922 N N   . ALA   A 1 306 ? 168.242 128.758 179.909 1.00 56.78  ? 298 ALA   A N   1 
ATOM   1923 C CA  . ALA   A 1 306 ? 167.464 127.868 180.764 1.00 58.61  ? 298 ALA   A CA  1 
ATOM   1924 C C   . ALA   A 1 306 ? 168.051 126.463 180.793 1.00 58.22  ? 298 ALA   A C   1 
ATOM   1925 O O   . ALA   A 1 306 ? 168.136 125.843 181.859 1.00 58.69  ? 298 ALA   A O   1 
ATOM   1926 C CB  . ALA   A 1 306 ? 166.009 127.831 180.298 1.00 54.52  ? 298 ALA   A CB  1 
ATOM   1927 N N   . LEU   A 1 307 ? 168.464 125.942 179.637 1.00 56.39  ? 299 LEU   A N   1 
ATOM   1928 C CA  . LEU   A 1 307 ? 168.970 124.575 179.563 1.00 57.61  ? 299 LEU   A CA  1 
ATOM   1929 C C   . LEU   A 1 307 ? 170.466 124.507 179.859 1.00 64.95  ? 299 LEU   A C   1 
ATOM   1930 O O   . LEU   A 1 307 ? 170.891 123.810 180.786 1.00 67.95  ? 299 LEU   A O   1 
ATOM   1931 C CB  . LEU   A 1 307 ? 168.665 123.977 178.185 1.00 54.67  ? 299 LEU   A CB  1 
ATOM   1932 C CG  . LEU   A 1 307 ? 167.185 123.856 177.820 1.00 54.20  ? 299 LEU   A CG  1 
ATOM   1933 C CD1 . LEU   A 1 307 ? 167.021 123.508 176.351 1.00 51.35  ? 299 LEU   A CD1 1 
ATOM   1934 C CD2 . LEU   A 1 307 ? 166.501 122.824 178.698 1.00 56.62  ? 299 LEU   A CD2 1 
ATOM   1935 N N   . GLY   A 1 308 ? 171.272 125.224 179.083 1.00 65.10  ? 300 GLY   A N   1 
ATOM   1936 C CA  . GLY   A 1 308 ? 172.712 125.209 179.262 1.00 61.96  ? 300 GLY   A CA  1 
ATOM   1937 C C   . GLY   A 1 308 ? 173.187 126.117 180.378 1.00 65.09  ? 300 GLY   A C   1 
ATOM   1938 O O   . GLY   A 1 308 ? 172.795 125.953 181.533 1.00 67.25  ? 300 GLY   A O   1 
ATOM   1939 N N   . ALA   A 1 315 ? 180.501 139.261 177.824 1.00 94.24  ? 307 ALA   A N   1 
ATOM   1940 C CA  . ALA   A 1 315 ? 180.041 139.032 176.460 1.00 97.30  ? 307 ALA   A CA  1 
ATOM   1941 C C   . ALA   A 1 315 ? 178.636 138.440 176.451 1.00 95.15  ? 307 ALA   A C   1 
ATOM   1942 O O   . ALA   A 1 315 ? 177.808 138.795 175.611 1.00 89.50  ? 307 ALA   A O   1 
ATOM   1943 C CB  . ALA   A 1 315 ? 181.008 138.121 175.720 1.00 92.70  ? 307 ALA   A CB  1 
ATOM   1944 N N   . ALA   A 1 316 ? 178.377 137.527 177.390 1.00 97.38  ? 308 ALA   A N   1 
ATOM   1945 C CA  . ALA   A 1 316 ? 177.055 136.919 177.482 1.00 92.84  ? 308 ALA   A CA  1 
ATOM   1946 C C   . ALA   A 1 316 ? 175.990 137.959 177.807 1.00 88.50  ? 308 ALA   A C   1 
ATOM   1947 O O   . ALA   A 1 316 ? 174.911 137.961 177.205 1.00 88.61  ? 308 ALA   A O   1 
ATOM   1948 C CB  . ALA   A 1 316 ? 177.059 135.807 178.530 1.00 91.43  ? 308 ALA   A CB  1 
ATOM   1949 N N   . LEU   A 1 317 ? 176.280 138.859 178.750 1.00 87.60  ? 309 LEU   A N   1 
ATOM   1950 C CA  . LEU   A 1 317 ? 175.324 139.910 179.086 1.00 88.55  ? 309 LEU   A CA  1 
ATOM   1951 C C   . LEU   A 1 317 ? 175.139 140.879 177.925 1.00 85.86  ? 309 LEU   A C   1 
ATOM   1952 O O   . LEU   A 1 317 ? 174.027 141.367 177.687 1.00 84.02  ? 309 LEU   A O   1 
ATOM   1953 C CB  . LEU   A 1 317 ? 175.780 140.653 180.341 1.00 93.14  ? 309 LEU   A CB  1 
ATOM   1954 C CG  . LEU   A 1 317 ? 175.108 140.258 181.658 1.00 100.70 ? 309 LEU   A CG  1 
ATOM   1955 C CD1 . LEU   A 1 317 ? 173.725 140.877 181.757 1.00 93.19  ? 309 LEU   A CD1 1 
ATOM   1956 C CD2 . LEU   A 1 317 ? 175.032 138.745 181.802 1.00 97.11  ? 309 LEU   A CD2 1 
ATOM   1957 N N   . SER   A 1 318 ? 176.218 141.176 177.197 1.00 87.18  ? 310 SER   A N   1 
ATOM   1958 C CA  . SER   A 1 318 ? 176.104 142.042 176.028 1.00 83.20  ? 310 SER   A CA  1 
ATOM   1959 C C   . SER   A 1 318 ? 175.204 141.417 174.970 1.00 75.61  ? 310 SER   A C   1 
ATOM   1960 O O   . SER   A 1 318 ? 174.346 142.096 174.395 1.00 70.89  ? 310 SER   A O   1 
ATOM   1961 C CB  . SER   A 1 318 ? 177.489 142.331 175.452 1.00 87.21  ? 310 SER   A CB  1 
ATOM   1962 O OG  . SER   A 1 318 ? 178.364 142.826 176.450 1.00 89.67  ? 310 SER   A OG  1 
ATOM   1963 N N   . SER   A 1 319 ? 175.380 140.120 174.707 1.00 75.50  ? 311 SER   A N   1 
ATOM   1964 C CA  . SER   A 1 319 ? 174.516 139.436 173.751 1.00 72.03  ? 311 SER   A CA  1 
ATOM   1965 C C   . SER   A 1 319 ? 173.075 139.399 174.242 1.00 68.72  ? 311 SER   A C   1 
ATOM   1966 O O   . SER   A 1 319 ? 172.137 139.569 173.455 1.00 70.63  ? 311 SER   A O   1 
ATOM   1967 C CB  . SER   A 1 319 ? 175.031 138.021 173.495 1.00 72.81  ? 311 SER   A CB  1 
ATOM   1968 O OG  . SER   A 1 319 ? 176.388 138.038 173.091 1.00 78.53  ? 311 SER   A OG  1 
ATOM   1969 N N   . TYR   A 1 320 ? 172.881 139.177 175.543 1.00 64.56  ? 312 TYR   A N   1 
ATOM   1970 C CA  . TYR   A 1 320 ? 171.537 139.163 176.111 1.00 61.75  ? 312 TYR   A CA  1 
ATOM   1971 C C   . TYR   A 1 320 ? 170.837 140.497 175.890 1.00 58.95  ? 312 TYR   A C   1 
ATOM   1972 O O   . TYR   A 1 320 ? 169.697 140.545 175.410 1.00 57.27  ? 312 TYR   A O   1 
ATOM   1973 C CB  . TYR   A 1 320 ? 171.619 138.830 177.601 1.00 66.16  ? 312 TYR   A CB  1 
ATOM   1974 C CG  . TYR   A 1 320 ? 170.310 138.913 178.349 1.00 64.76  ? 312 TYR   A CG  1 
ATOM   1975 C CD1 . TYR   A 1 320 ? 169.188 138.227 177.908 1.00 60.41  ? 312 TYR   A CD1 1 
ATOM   1976 C CD2 . TYR   A 1 320 ? 170.200 139.670 179.506 1.00 65.24  ? 312 TYR   A CD2 1 
ATOM   1977 C CE1 . TYR   A 1 320 ? 167.993 138.300 178.595 1.00 61.75  ? 312 TYR   A CE1 1 
ATOM   1978 C CE2 . TYR   A 1 320 ? 169.010 139.749 180.198 1.00 63.53  ? 312 TYR   A CE2 1 
ATOM   1979 C CZ  . TYR   A 1 320 ? 167.909 139.062 179.739 1.00 66.25  ? 312 TYR   A CZ  1 
ATOM   1980 O OH  . TYR   A 1 320 ? 166.721 139.138 180.427 1.00 70.22  ? 312 TYR   A OH  1 
ATOM   1981 N N   . TYR   A 1 321 ? 171.516 141.597 176.216 1.00 62.12  ? 313 TYR   A N   1 
ATOM   1982 C CA  . TYR   A 1 321 ? 170.894 142.907 176.071 1.00 59.54  ? 313 TYR   A CA  1 
ATOM   1983 C C   . TYR   A 1 321 ? 170.714 143.289 174.608 1.00 56.50  ? 313 TYR   A C   1 
ATOM   1984 O O   . TYR   A 1 321 ? 169.731 143.954 174.265 1.00 54.68  ? 313 TYR   A O   1 
ATOM   1985 C CB  . TYR   A 1 321 ? 171.708 143.963 176.814 1.00 66.11  ? 313 TYR   A CB  1 
ATOM   1986 C CG  . TYR   A 1 321 ? 171.377 144.029 178.286 1.00 75.60  ? 313 TYR   A CG  1 
ATOM   1987 C CD1 . TYR   A 1 321 ? 170.112 144.411 178.713 1.00 77.63  ? 313 TYR   A CD1 1 
ATOM   1988 C CD2 . TYR   A 1 321 ? 172.321 143.700 179.248 1.00 78.32  ? 313 TYR   A CD2 1 
ATOM   1989 C CE1 . TYR   A 1 321 ? 169.798 144.469 180.055 1.00 77.97  ? 313 TYR   A CE1 1 
ATOM   1990 C CE2 . TYR   A 1 321 ? 172.017 143.757 180.593 1.00 85.05  ? 313 TYR   A CE2 1 
ATOM   1991 C CZ  . TYR   A 1 321 ? 170.754 144.142 180.991 1.00 86.23  ? 313 TYR   A CZ  1 
ATOM   1992 O OH  . TYR   A 1 321 ? 170.446 144.199 182.331 1.00 87.49  ? 313 TYR   A OH  1 
ATOM   1993 N N   . PHE   A 1 322 ? 171.631 142.873 173.730 1.00 58.89  ? 314 PHE   A N   1 
ATOM   1994 C CA  . PHE   A 1 322 ? 171.433 143.107 172.304 1.00 53.05  ? 314 PHE   A CA  1 
ATOM   1995 C C   . PHE   A 1 322 ? 170.199 142.374 171.796 1.00 52.75  ? 314 PHE   A C   1 
ATOM   1996 O O   . PHE   A 1 322 ? 169.420 142.928 171.014 1.00 51.48  ? 314 PHE   A O   1 
ATOM   1997 C CB  . PHE   A 1 322 ? 172.671 142.678 171.518 1.00 57.16  ? 314 PHE   A CB  1 
ATOM   1998 C CG  . PHE   A 1 322 ? 172.426 142.523 170.043 1.00 63.93  ? 314 PHE   A CG  1 
ATOM   1999 C CD1 . PHE   A 1 322 ? 172.371 143.632 169.216 1.00 66.40  ? 314 PHE   A CD1 1 
ATOM   2000 C CD2 . PHE   A 1 322 ? 172.251 141.268 169.482 1.00 60.62  ? 314 PHE   A CD2 1 
ATOM   2001 C CE1 . PHE   A 1 322 ? 172.144 143.494 167.861 1.00 56.97  ? 314 PHE   A CE1 1 
ATOM   2002 C CE2 . PHE   A 1 322 ? 172.023 141.125 168.128 1.00 56.72  ? 314 PHE   A CE2 1 
ATOM   2003 C CZ  . PHE   A 1 322 ? 171.971 142.240 167.317 1.00 53.28  ? 314 PHE   A CZ  1 
ATOM   2004 N N   . CYS   A 1 323 ? 170.008 141.124 172.226 1.00 55.40  ? 315 CYS   A N   1 
ATOM   2005 C CA  . CYS   A 1 323 ? 168.823 140.374 171.823 1.00 46.66  ? 315 CYS   A CA  1 
ATOM   2006 C C   . CYS   A 1 323 ? 167.552 141.032 172.344 1.00 44.45  ? 315 CYS   A C   1 
ATOM   2007 O O   . CYS   A 1 323 ? 166.554 141.135 171.618 1.00 46.35  ? 315 CYS   A O   1 
ATOM   2008 C CB  . CYS   A 1 323 ? 168.920 138.933 172.319 1.00 47.61  ? 315 CYS   A CB  1 
ATOM   2009 S SG  . CYS   A 1 323 ? 170.195 137.945 171.507 1.00 66.50  ? 315 CYS   A SG  1 
ATOM   2010 N N   . ILE   A 1 324 ? 167.571 141.486 173.599 1.00 48.23  ? 316 ILE   A N   1 
ATOM   2011 C CA  . ILE   A 1 324 ? 166.398 142.151 174.164 1.00 44.92  ? 316 ILE   A CA  1 
ATOM   2012 C C   . ILE   A 1 324 ? 166.078 143.419 173.382 1.00 45.55  ? 316 ILE   A C   1 
ATOM   2013 O O   . ILE   A 1 324 ? 164.918 143.690 173.052 1.00 48.81  ? 316 ILE   A O   1 
ATOM   2014 C CB  . ILE   A 1 324 ? 166.612 142.453 175.658 1.00 48.82  ? 316 ILE   A CB  1 
ATOM   2015 C CG1 . ILE   A 1 324 ? 166.865 141.161 176.439 1.00 51.82  ? 316 ILE   A CG1 1 
ATOM   2016 C CG2 . ILE   A 1 324 ? 165.417 143.206 176.218 1.00 50.93  ? 316 ILE   A CG2 1 
ATOM   2017 C CD1 . ILE   A 1 324 ? 165.631 140.551 177.053 1.00 52.70  ? 316 ILE   A CD1 1 
ATOM   2018 N N   . ALA   A 1 325 ? 167.103 144.218 173.076 1.00 47.50  ? 317 ALA   A N   1 
ATOM   2019 C CA  . ALA   A 1 325 ? 166.887 145.445 172.318 1.00 45.32  ? 317 ALA   A CA  1 
ATOM   2020 C C   . ALA   A 1 325 ? 166.355 145.149 170.922 1.00 45.59  ? 317 ALA   A C   1 
ATOM   2021 O O   . ALA   A 1 325 ? 165.448 145.834 170.438 1.00 46.02  ? 317 ALA   A O   1 
ATOM   2022 C CB  . ALA   A 1 325 ? 168.184 146.248 172.237 1.00 51.05  ? 317 ALA   A CB  1 
ATOM   2023 N N   . LEU   A 1 326 ? 166.909 144.130 170.260 1.00 45.95  ? 318 LEU   A N   1 
ATOM   2024 C CA  . LEU   A 1 326 ? 166.450 143.772 168.923 1.00 38.68  ? 318 LEU   A CA  1 
ATOM   2025 C C   . LEU   A 1 326 ? 164.999 143.315 168.942 1.00 42.11  ? 318 LEU   A C   1 
ATOM   2026 O O   . LEU   A 1 326 ? 164.239 143.597 168.009 1.00 45.43  ? 318 LEU   A O   1 
ATOM   2027 C CB  . LEU   A 1 326 ? 167.351 142.686 168.339 1.00 36.66  ? 318 LEU   A CB  1 
ATOM   2028 C CG  . LEU   A 1 326 ? 167.024 142.201 166.928 1.00 37.51  ? 318 LEU   A CG  1 
ATOM   2029 C CD1 . LEU   A 1 326 ? 167.310 143.291 165.912 1.00 38.51  ? 318 LEU   A CD1 1 
ATOM   2030 C CD2 . LEU   A 1 326 ? 167.810 140.944 166.604 1.00 36.59  ? 318 LEU   A CD2 1 
ATOM   2031 N N   . GLY   A 1 327 ? 164.597 142.599 169.993 1.00 43.03  ? 319 GLY   A N   1 
ATOM   2032 C CA  . GLY   A 1 327 ? 163.208 142.184 170.099 1.00 38.39  ? 319 GLY   A CA  1 
ATOM   2033 C C   . GLY   A 1 327 ? 162.250 143.355 170.209 1.00 41.98  ? 319 GLY   A C   1 
ATOM   2034 O O   . GLY   A 1 327 ? 161.164 143.337 169.626 1.00 44.85  ? 319 GLY   A O   1 
ATOM   2035 N N   . TYR   A 1 328 ? 162.638 144.390 170.958 1.00 43.27  ? 320 TYR   A N   1 
ATOM   2036 C CA  . TYR   A 1 328 ? 161.755 145.532 171.171 1.00 42.44  ? 320 TYR   A CA  1 
ATOM   2037 C C   . TYR   A 1 328 ? 161.668 146.444 169.954 1.00 45.89  ? 320 TYR   A C   1 
ATOM   2038 O O   . TYR   A 1 328 ? 160.644 147.108 169.761 1.00 49.12  ? 320 TYR   A O   1 
ATOM   2039 C CB  . TYR   A 1 328 ? 162.216 146.335 172.388 1.00 42.77  ? 320 TYR   A CB  1 
ATOM   2040 C CG  . TYR   A 1 328 ? 161.751 145.761 173.704 1.00 45.33  ? 320 TYR   A CG  1 
ATOM   2041 C CD1 . TYR   A 1 328 ? 160.442 145.337 173.873 1.00 49.28  ? 320 TYR   A CD1 1 
ATOM   2042 C CD2 . TYR   A 1 328 ? 162.621 145.640 174.777 1.00 49.38  ? 320 TYR   A CD2 1 
ATOM   2043 C CE1 . TYR   A 1 328 ? 160.013 144.809 175.073 1.00 54.26  ? 320 TYR   A CE1 1 
ATOM   2044 C CE2 . TYR   A 1 328 ? 162.201 145.114 175.980 1.00 52.96  ? 320 TYR   A CE2 1 
ATOM   2045 C CZ  . TYR   A 1 328 ? 160.896 144.700 176.122 1.00 54.19  ? 320 TYR   A CZ  1 
ATOM   2046 O OH  . TYR   A 1 328 ? 160.471 144.175 177.320 1.00 53.88  ? 320 TYR   A OH  1 
ATOM   2047 N N   . THR   A 1 329 ? 162.718 146.502 169.130 1.00 45.02  ? 321 THR   A N   1 
ATOM   2048 C CA  . THR   A 1 329 ? 162.695 147.377 167.963 1.00 44.84  ? 321 THR   A CA  1 
ATOM   2049 C C   . THR   A 1 329 ? 161.681 146.931 166.917 1.00 48.50  ? 321 THR   A C   1 
ATOM   2050 O O   . THR   A 1 329 ? 161.357 147.713 166.018 1.00 52.87  ? 321 THR   A O   1 
ATOM   2051 C CB  . THR   A 1 329 ? 164.080 147.457 167.322 1.00 42.42  ? 321 THR   A CB  1 
ATOM   2052 O OG1 . THR   A 1 329 ? 164.539 146.139 166.999 1.00 47.93  ? 321 THR   A OG1 1 
ATOM   2053 C CG2 . THR   A 1 329 ? 165.065 148.118 168.266 1.00 42.26  ? 321 THR   A CG2 1 
ATOM   2054 N N   . ASN   A 1 330 ? 161.180 145.698 167.008 1.00 48.65  ? 322 ASN   A N   1 
ATOM   2055 C CA  . ASN   A 1 330 ? 160.180 145.235 166.054 1.00 48.71  ? 322 ASN   A CA  1 
ATOM   2056 C C   . ASN   A 1 330 ? 158.881 146.019 166.180 1.00 50.46  ? 322 ASN   A C   1 
ATOM   2057 O O   . ASN   A 1 330 ? 158.129 146.135 165.207 1.00 52.46  ? 322 ASN   A O   1 
ATOM   2058 C CB  . ASN   A 1 330 ? 159.923 143.742 166.249 1.00 46.76  ? 322 ASN   A CB  1 
ATOM   2059 C CG  . ASN   A 1 330 ? 158.913 143.191 165.265 1.00 46.70  ? 322 ASN   A CG  1 
ATOM   2060 O OD1 . ASN   A 1 330 ? 157.849 142.715 165.653 1.00 49.13  ? 322 ASN   A OD1 1 
ATOM   2061 N ND2 . ASN   A 1 330 ? 159.242 143.256 163.982 1.00 48.09  ? 322 ASN   A ND2 1 
ATOM   2062 N N   . SER   A 1 331 ? 158.602 146.566 167.364 1.00 50.36  ? 323 SER   A N   1 
ATOM   2063 C CA  . SER   A 1 331 ? 157.373 147.324 167.568 1.00 50.86  ? 323 SER   A CA  1 
ATOM   2064 C C   . SER   A 1 331 ? 157.369 148.644 166.808 1.00 55.48  ? 323 SER   A C   1 
ATOM   2065 O O   . SER   A 1 331 ? 156.298 149.228 166.616 1.00 56.91  ? 323 SER   A O   1 
ATOM   2066 C CB  . SER   A 1 331 ? 157.161 147.584 169.059 1.00 50.17  ? 323 SER   A CB  1 
ATOM   2067 O OG  . SER   A 1 331 ? 157.430 146.421 169.821 1.00 53.16  ? 323 SER   A OG  1 
ATOM   2068 N N   . SER   A 1 332 ? 158.533 149.124 166.374 1.00 56.73  ? 324 SER   A N   1 
ATOM   2069 C CA  . SER   A 1 332 ? 158.628 150.394 165.668 1.00 51.74  ? 324 SER   A CA  1 
ATOM   2070 C C   . SER   A 1 332 ? 158.772 150.244 164.161 1.00 49.07  ? 324 SER   A C   1 
ATOM   2071 O O   . SER   A 1 332 ? 158.525 151.211 163.434 1.00 51.26  ? 324 SER   A O   1 
ATOM   2072 C CB  . SER   A 1 332 ? 159.813 151.206 166.202 1.00 48.67  ? 324 SER   A CB  1 
ATOM   2073 O OG  . SER   A 1 332 ? 159.818 151.222 167.617 1.00 50.50  ? 324 SER   A OG  1 
ATOM   2074 N N   . LEU   A 1 333 ? 159.164 149.067 163.676 1.00 45.59  ? 325 LEU   A N   1 
ATOM   2075 C CA  . LEU   A 1 333 ? 159.399 148.860 162.254 1.00 42.01  ? 325 LEU   A CA  1 
ATOM   2076 C C   . LEU   A 1 333 ? 158.133 148.530 161.475 1.00 45.59  ? 325 LEU   A C   1 
ATOM   2077 O O   . LEU   A 1 333 ? 158.173 148.522 160.241 1.00 50.26  ? 325 LEU   A O   1 
ATOM   2078 C CB  . LEU   A 1 333 ? 160.425 147.743 162.052 1.00 46.79  ? 325 LEU   A CB  1 
ATOM   2079 C CG  . LEU   A 1 333 ? 161.796 147.956 162.693 1.00 51.41  ? 325 LEU   A CG  1 
ATOM   2080 C CD1 . LEU   A 1 333 ? 162.726 146.802 162.361 1.00 46.91  ? 325 LEU   A CD1 1 
ATOM   2081 C CD2 . LEU   A 1 333 ? 162.397 149.279 162.252 1.00 52.92  ? 325 LEU   A CD2 1 
ATOM   2082 N N   . ASN   A 1 334 ? 157.021 148.242 162.156 1.00 48.36  ? 326 ASN   A N   1 
ATOM   2083 C CA  . ASN   A 1 334 ? 155.794 147.901 161.437 1.00 45.10  ? 326 ASN   A CA  1 
ATOM   2084 C C   . ASN   A 1 334 ? 155.254 149.061 160.607 1.00 44.08  ? 326 ASN   A C   1 
ATOM   2085 O O   . ASN   A 1 334 ? 154.882 148.833 159.442 1.00 48.52  ? 326 ASN   A O   1 
ATOM   2086 C CB  . ASN   A 1 334 ? 154.750 147.365 162.419 1.00 53.35  ? 326 ASN   A CB  1 
ATOM   2087 C CG  . ASN   A 1 334 ? 154.960 145.901 162.747 1.00 55.91  ? 326 ASN   A CG  1 
ATOM   2088 O OD1 . ASN   A 1 334 ? 155.462 145.136 161.925 1.00 50.00  ? 326 ASN   A OD1 1 
ATOM   2089 N ND2 . ASN   A 1 334 ? 154.580 145.506 163.955 1.00 60.43  ? 326 ASN   A ND2 1 
ATOM   2090 N N   . PRO   A 1 335 ? 155.143 150.293 161.121 1.00 42.28  ? 327 PRO   A N   1 
ATOM   2091 C CA  . PRO   A 1 335 ? 154.661 151.377 160.247 1.00 44.99  ? 327 PRO   A CA  1 
ATOM   2092 C C   . PRO   A 1 335 ? 155.613 151.715 159.112 1.00 45.83  ? 327 PRO   A C   1 
ATOM   2093 O O   . PRO   A 1 335 ? 155.157 152.069 158.018 1.00 51.53  ? 327 PRO   A O   1 
ATOM   2094 C CB  . PRO   A 1 335 ? 154.477 152.556 161.213 1.00 40.40  ? 327 PRO   A CB  1 
ATOM   2095 C CG  . PRO   A 1 335 ? 155.329 152.245 162.377 1.00 46.00  ? 327 PRO   A CG  1 
ATOM   2096 C CD  . PRO   A 1 335 ? 155.337 150.758 162.507 1.00 43.80  ? 327 PRO   A CD  1 
ATOM   2097 N N   . VAL   A 1 336 ? 156.924 151.605 159.330 1.00 44.64  ? 328 VAL   A N   1 
ATOM   2098 C CA  . VAL   A 1 336 ? 157.896 151.961 158.301 1.00 45.24  ? 328 VAL   A CA  1 
ATOM   2099 C C   . VAL   A 1 336 ? 157.922 150.870 157.239 1.00 49.04  ? 328 VAL   A C   1 
ATOM   2100 O O   . VAL   A 1 336 ? 158.508 151.046 156.165 1.00 53.93  ? 328 VAL   A O   1 
ATOM   2101 C CB  . VAL   A 1 336 ? 159.297 152.191 158.898 1.00 42.50  ? 328 VAL   A CB  1 
ATOM   2102 C CG1 . VAL   A 1 336 ? 159.195 152.956 160.207 1.00 37.77  ? 328 VAL   A CG1 1 
ATOM   2103 C CG2 . VAL   A 1 336 ? 160.026 150.874 159.090 1.00 47.55  ? 328 VAL   A CG2 1 
ATOM   2104 N N   . LEU   A 1 337 ? 157.294 149.738 157.535 1.00 46.55  ? 329 LEU   A N   1 
ATOM   2105 C CA  . LEU   A 1 337 ? 157.069 148.675 156.565 1.00 43.77  ? 329 LEU   A CA  1 
ATOM   2106 C C   . LEU   A 1 337 ? 155.741 148.818 155.846 1.00 48.12  ? 329 LEU   A C   1 
ATOM   2107 O O   . LEU   A 1 337 ? 155.662 148.553 154.643 1.00 54.18  ? 329 LEU   A O   1 
ATOM   2108 C CB  . LEU   A 1 337 ? 157.122 147.307 157.258 1.00 43.19  ? 329 LEU   A CB  1 
ATOM   2109 C CG  . LEU   A 1 337 ? 158.497 146.691 157.513 1.00 39.91  ? 329 LEU   A CG  1 
ATOM   2110 C CD1 . LEU   A 1 337 ? 158.341 145.277 158.039 1.00 38.78  ? 329 LEU   A CD1 1 
ATOM   2111 C CD2 . LEU   A 1 337 ? 159.340 146.707 156.252 1.00 46.17  ? 329 LEU   A CD2 1 
ATOM   2112 N N   . TYR   A 1 338 ? 154.692 149.225 156.563 1.00 48.33  ? 330 TYR   A N   1 
ATOM   2113 C CA  . TYR   A 1 338 ? 153.401 149.470 155.928 1.00 49.64  ? 330 TYR   A CA  1 
ATOM   2114 C C   . TYR   A 1 338 ? 153.498 150.613 154.926 1.00 54.28  ? 330 TYR   A C   1 
ATOM   2115 O O   . TYR   A 1 338 ? 152.910 150.556 153.840 1.00 61.93  ? 330 TYR   A O   1 
ATOM   2116 C CB  . TYR   A 1 338 ? 152.339 149.779 156.983 1.00 45.20  ? 330 TYR   A CB  1 
ATOM   2117 C CG  . TYR   A 1 338 ? 152.131 148.691 158.010 1.00 45.89  ? 330 TYR   A CG  1 
ATOM   2118 C CD1 . TYR   A 1 338 ? 152.402 147.364 157.714 1.00 47.78  ? 330 TYR   A CD1 1 
ATOM   2119 C CD2 . TYR   A 1 338 ? 151.661 148.996 159.279 1.00 46.29  ? 330 TYR   A CD2 1 
ATOM   2120 C CE1 . TYR   A 1 338 ? 152.213 146.371 158.655 1.00 50.13  ? 330 TYR   A CE1 1 
ATOM   2121 C CE2 . TYR   A 1 338 ? 151.469 148.011 160.225 1.00 47.17  ? 330 TYR   A CE2 1 
ATOM   2122 C CZ  . TYR   A 1 338 ? 151.746 146.702 159.909 1.00 49.01  ? 330 TYR   A CZ  1 
ATOM   2123 O OH  . TYR   A 1 338 ? 151.554 145.721 160.853 1.00 48.79  ? 330 TYR   A OH  1 
ATOM   2124 N N   . ALA   A 1 339 ? 154.239 151.666 155.278 1.00 53.10  ? 331 ALA   A N   1 
ATOM   2125 C CA  . ALA   A 1 339 ? 154.363 152.819 154.396 1.00 57.55  ? 331 ALA   A CA  1 
ATOM   2126 C C   . ALA   A 1 339 ? 155.119 152.495 153.115 1.00 60.53  ? 331 ALA   A C   1 
ATOM   2127 O O   . ALA   A 1 339 ? 155.006 153.243 152.138 1.00 67.80  ? 331 ALA   A O   1 
ATOM   2128 C CB  . ALA   A 1 339 ? 155.056 153.969 155.128 1.00 56.49  ? 331 ALA   A CB  1 
ATOM   2129 N N   . PHE   A 1 340 ? 155.884 151.406 153.094 1.00 59.37  ? 332 PHE   A N   1 
ATOM   2130 C CA  . PHE   A 1 340 ? 156.656 151.030 151.916 1.00 59.92  ? 332 PHE   A CA  1 
ATOM   2131 C C   . PHE   A 1 340 ? 156.055 149.866 151.144 1.00 59.02  ? 332 PHE   A C   1 
ATOM   2132 O O   . PHE   A 1 340 ? 156.308 149.743 149.942 1.00 62.52  ? 332 PHE   A O   1 
ATOM   2133 C CB  . PHE   A 1 340 ? 158.094 150.672 152.310 1.00 60.26  ? 332 PHE   A CB  1 
ATOM   2134 C CG  . PHE   A 1 340 ? 158.931 151.852 152.720 1.00 64.14  ? 332 PHE   A CG  1 
ATOM   2135 C CD1 . PHE   A 1 340 ? 160.251 151.678 153.097 1.00 72.68  ? 332 PHE   A CD1 1 
ATOM   2136 C CD2 . PHE   A 1 340 ? 158.407 153.134 152.716 1.00 67.41  ? 332 PHE   A CD2 1 
ATOM   2137 C CE1 . PHE   A 1 340 ? 161.029 152.756 153.473 1.00 78.67  ? 332 PHE   A CE1 1 
ATOM   2138 C CE2 . PHE   A 1 340 ? 159.179 154.216 153.091 1.00 73.17  ? 332 PHE   A CE2 1 
ATOM   2139 C CZ  . PHE   A 1 340 ? 160.491 154.027 153.469 1.00 78.09  ? 332 PHE   A CZ  1 
ATOM   2140 N N   . LEU   A 1 341 ? 155.269 149.009 151.795 1.00 56.75  ? 333 LEU   A N   1 
ATOM   2141 C CA  . LEU   A 1 341 ? 154.717 147.836 151.133 1.00 58.13  ? 333 LEU   A CA  1 
ATOM   2142 C C   . LEU   A 1 341 ? 153.263 147.996 150.711 1.00 62.84  ? 333 LEU   A C   1 
ATOM   2143 O O   . LEU   A 1 341 ? 152.788 147.208 149.887 1.00 67.75  ? 333 LEU   A O   1 
ATOM   2144 C CB  . LEU   A 1 341 ? 154.832 146.609 152.044 1.00 55.90  ? 333 LEU   A CB  1 
ATOM   2145 C CG  . LEU   A 1 341 ? 156.241 146.096 152.331 1.00 53.45  ? 333 LEU   A CG  1 
ATOM   2146 C CD1 . LEU   A 1 341 ? 156.256 145.336 153.642 1.00 47.85  ? 333 LEU   A CD1 1 
ATOM   2147 C CD2 . LEU   A 1 341 ? 156.733 145.218 151.195 1.00 49.44  ? 333 LEU   A CD2 1 
ATOM   2148 N N   . ASP   A 1 342 ? 152.548 148.980 151.248 1.00 60.92  ? 334 ASP   A N   1 
ATOM   2149 C CA  . ASP   A 1 342 ? 151.141 149.187 150.934 1.00 63.52  ? 334 ASP   A CA  1 
ATOM   2150 C C   . ASP   A 1 342 ? 150.945 150.590 150.381 1.00 68.48  ? 334 ASP   A C   1 
ATOM   2151 O O   . ASP   A 1 342 ? 151.420 151.566 150.971 1.00 67.89  ? 334 ASP   A O   1 
ATOM   2152 C CB  . ASP   A 1 342 ? 150.262 148.975 152.168 1.00 65.29  ? 334 ASP   A CB  1 
ATOM   2153 C CG  . ASP   A 1 342 ? 148.801 148.780 151.814 1.00 74.17  ? 334 ASP   A CG  1 
ATOM   2154 O OD1 . ASP   A 1 342 ? 148.463 148.853 150.614 1.00 78.64  ? 334 ASP   A OD1 1 
ATOM   2155 O OD2 . ASP   A 1 342 ? 147.989 148.550 152.733 1.00 73.19  ? 334 ASP   A OD2 1 
ATOM   2156 N N   . GLU   A 1 343 ? 150.247 150.686 149.248 1.00 74.33  ? 335 GLU   A N   1 
ATOM   2157 C CA  . GLU   A 1 343 ? 149.984 151.987 148.644 1.00 75.43  ? 335 GLU   A CA  1 
ATOM   2158 C C   . GLU   A 1 343 ? 148.901 152.747 149.397 1.00 70.27  ? 335 GLU   A C   1 
ATOM   2159 O O   . GLU   A 1 343 ? 148.995 153.969 149.554 1.00 71.58  ? 335 GLU   A O   1 
ATOM   2160 C CB  . GLU   A 1 343 ? 149.591 151.817 147.177 1.00 80.59  ? 335 GLU   A CB  1 
ATOM   2161 C CG  . GLU   A 1 343 ? 150.752 151.469 146.259 1.00 89.92  ? 335 GLU   A CG  1 
ATOM   2162 C CD  . GLU   A 1 343 ? 151.712 152.629 146.069 1.00 95.81  ? 335 GLU   A CD  1 
ATOM   2163 O OE1 . GLU   A 1 343 ? 151.388 153.550 145.290 1.00 96.54  ? 335 GLU   A OE1 1 
ATOM   2164 O OE2 . GLU   A 1 343 ? 152.790 152.619 146.698 1.00 91.37  ? 335 GLU   A OE2 1 
ATOM   2165 N N   . ASN   A 1 344 ? 147.864 152.046 149.859 1.00 67.65  ? 336 ASN   A N   1 
ATOM   2166 C CA  . ASN   A 1 344 ? 146.781 152.712 150.575 1.00 69.28  ? 336 ASN   A CA  1 
ATOM   2167 C C   . ASN   A 1 344 ? 147.260 153.279 151.906 1.00 65.99  ? 336 ASN   A C   1 
ATOM   2168 O O   . ASN   A 1 344 ? 146.888 154.399 152.280 1.00 64.87  ? 336 ASN   A O   1 
ATOM   2169 C CB  . ASN   A 1 344 ? 145.623 151.740 150.785 1.00 68.91  ? 336 ASN   A CB  1 
ATOM   2170 C CG  . ASN   A 1 344 ? 144.943 151.356 149.490 1.00 78.17  ? 336 ASN   A CG  1 
ATOM   2171 O OD1 . ASN   A 1 344 ? 144.046 152.052 149.017 1.00 81.04  ? 336 ASN   A OD1 1 
ATOM   2172 N ND2 . ASN   A 1 344 ? 145.369 150.243 148.906 1.00 83.82  ? 336 ASN   A ND2 1 
ATOM   2173 N N   . PHE   A 1 345 ? 148.084 152.523 152.635 1.00 65.59  ? 337 PHE   A N   1 
ATOM   2174 C CA  . PHE   A 1 345 ? 148.635 153.028 153.888 1.00 56.01  ? 337 PHE   A CA  1 
ATOM   2175 C C   . PHE   A 1 345 ? 149.520 154.243 153.650 1.00 60.12  ? 337 PHE   A C   1 
ATOM   2176 O O   . PHE   A 1 345 ? 149.472 155.213 154.414 1.00 62.01  ? 337 PHE   A O   1 
ATOM   2177 C CB  . PHE   A 1 345 ? 149.417 151.926 154.603 1.00 53.39  ? 337 PHE   A CB  1 
ATOM   2178 C CG  . PHE   A 1 345 ? 148.627 151.212 155.661 1.00 52.10  ? 337 PHE   A CG  1 
ATOM   2179 C CD1 . PHE   A 1 345 ? 148.171 151.889 156.777 1.00 47.38  ? 337 PHE   A CD1 1 
ATOM   2180 C CD2 . PHE   A 1 345 ? 148.342 149.865 155.541 1.00 53.16  ? 337 PHE   A CD2 1 
ATOM   2181 C CE1 . PHE   A 1 345 ? 147.446 151.238 157.751 1.00 44.34  ? 337 PHE   A CE1 1 
ATOM   2182 C CE2 . PHE   A 1 345 ? 147.615 149.208 156.512 1.00 50.28  ? 337 PHE   A CE2 1 
ATOM   2183 C CZ  . PHE   A 1 345 ? 147.167 149.896 157.618 1.00 47.11  ? 337 PHE   A CZ  1 
ATOM   2184 N N   . LYS   A 1 346 ? 150.335 154.209 152.594 1.00 63.46  ? 338 LYS   A N   1 
ATOM   2185 C CA  . LYS   A 1 346 ? 151.173 155.357 152.262 1.00 64.14  ? 338 LYS   A CA  1 
ATOM   2186 C C   . LYS   A 1 346 ? 150.329 156.578 151.914 1.00 65.38  ? 338 LYS   A C   1 
ATOM   2187 O O   . LYS   A 1 346 ? 150.630 157.698 152.347 1.00 67.60  ? 338 LYS   A O   1 
ATOM   2188 C CB  . LYS   A 1 346 ? 152.103 154.999 151.104 1.00 61.50  ? 338 LYS   A CB  1 
ATOM   2189 C CG  . LYS   A 1 346 ? 153.209 156.002 150.852 1.00 61.37  ? 338 LYS   A CG  1 
ATOM   2190 C CD  . LYS   A 1 346 ? 153.723 155.884 149.429 1.00 68.55  ? 338 LYS   A CD  1 
ATOM   2191 C CE  . LYS   A 1 346 ? 154.262 154.491 149.154 1.00 76.79  ? 338 LYS   A CE  1 
ATOM   2192 N NZ  . LYS   A 1 346 ? 154.634 154.309 147.725 1.00 80.30  ? 338 LYS   A NZ  1 
ATOM   2193 N N   . ARG   A 1 347 ? 149.266 156.380 151.131 1.00 62.74  ? 339 ARG   A N   1 
ATOM   2194 C CA  . ARG   A 1 347 ? 148.388 157.488 150.774 1.00 64.49  ? 339 ARG   A CA  1 
ATOM   2195 C C   . ARG   A 1 347 ? 147.724 158.081 152.008 1.00 68.72  ? 339 ARG   A C   1 
ATOM   2196 O O   . ARG   A 1 347 ? 147.628 159.306 152.144 1.00 74.97  ? 339 ARG   A O   1 
ATOM   2197 C CB  . ARG   A 1 347 ? 147.331 157.017 149.777 1.00 71.94  ? 339 ARG   A CB  1 
ATOM   2198 C CG  . ARG   A 1 347 ? 147.601 157.416 148.338 1.00 82.07  ? 339 ARG   A CG  1 
ATOM   2199 C CD  . ARG   A 1 347 ? 146.501 156.914 147.417 1.00 85.57  ? 339 ARG   A CD  1 
ATOM   2200 N NE  . ARG   A 1 347 ? 146.520 155.462 147.282 1.00 88.09  ? 339 ARG   A NE  1 
ATOM   2201 C CZ  . ARG   A 1 347 ? 146.845 154.816 146.171 1.00 87.36  ? 339 ARG   A CZ  1 
ATOM   2202 N NH1 . ARG   A 1 347 ? 147.188 155.463 145.070 1.00 90.75  ? 339 ARG   A NH1 1 
ATOM   2203 N NH2 . ARG   A 1 347 ? 146.824 153.486 146.164 1.00 77.55  ? 339 ARG   A NH2 1 
ATOM   2204 N N   . CYS   A 1 348 ? 147.256 157.226 152.920 1.00 70.45  ? 340 CYS   A N   1 
ATOM   2205 C CA  . CYS   A 1 348 ? 146.614 157.718 154.134 1.00 65.96  ? 340 CYS   A CA  1 
ATOM   2206 C C   . CYS   A 1 348 ? 147.607 158.443 155.035 1.00 67.11  ? 340 CYS   A C   1 
ATOM   2207 O O   . CYS   A 1 348 ? 147.264 159.454 155.658 1.00 67.73  ? 340 CYS   A O   1 
ATOM   2208 C CB  . CYS   A 1 348 ? 145.951 156.563 154.878 1.00 60.16  ? 340 CYS   A CB  1 
ATOM   2209 S SG  . CYS   A 1 348 ? 144.464 155.926 154.075 1.00 77.04  ? 340 CYS   A SG  1 
ATOM   2210 N N   . PHE   A 1 349 ? 148.841 157.938 155.124 1.00 63.90  ? 341 PHE   A N   1 
ATOM   2211 C CA  . PHE   A 1 349 ? 149.865 158.625 155.904 1.00 60.99  ? 341 PHE   A CA  1 
ATOM   2212 C C   . PHE   A 1 349 ? 150.163 160.000 155.323 1.00 69.09  ? 341 PHE   A C   1 
ATOM   2213 O O   . PHE   A 1 349 ? 150.307 160.979 156.065 1.00 75.09  ? 341 PHE   A O   1 
ATOM   2214 C CB  . PHE   A 1 349 ? 151.140 157.784 155.964 1.00 59.15  ? 341 PHE   A CB  1 
ATOM   2215 C CG  . PHE   A 1 349 ? 151.000 156.515 156.757 1.00 60.71  ? 341 PHE   A CG  1 
ATOM   2216 C CD1 . PHE   A 1 349 ? 149.896 156.299 157.566 1.00 58.21  ? 341 PHE   A CD1 1 
ATOM   2217 C CD2 . PHE   A 1 349 ? 151.979 155.537 156.696 1.00 57.45  ? 341 PHE   A CD2 1 
ATOM   2218 C CE1 . PHE   A 1 349 ? 149.771 155.133 158.294 1.00 49.86  ? 341 PHE   A CE1 1 
ATOM   2219 C CE2 . PHE   A 1 349 ? 151.858 154.369 157.423 1.00 53.60  ? 341 PHE   A CE2 1 
ATOM   2220 C CZ  . PHE   A 1 349 ? 150.753 154.168 158.222 1.00 51.52  ? 341 PHE   A CZ  1 
ATOM   2221 N N   . ARG   A 1 350 ? 150.262 160.093 153.994 1.00 70.24  ? 342 ARG   A N   1 
ATOM   2222 C CA  . ARG   A 1 350 ? 150.475 161.390 153.361 1.00 74.27  ? 342 ARG   A CA  1 
ATOM   2223 C C   . ARG   A 1 350 ? 149.302 162.328 153.617 1.00 74.66  ? 342 ARG   A C   1 
ATOM   2224 O O   . ARG   A 1 350 ? 149.497 163.516 153.899 1.00 75.20  ? 342 ARG   A O   1 
ATOM   2225 C CB  . ARG   A 1 350 ? 150.698 161.212 151.860 1.00 77.24  ? 342 ARG   A CB  1 
ATOM   2226 C CG  . ARG   A 1 350 ? 152.112 161.520 151.401 1.00 85.63  ? 342 ARG   A CG  1 
ATOM   2227 C CD  . ARG   A 1 350 ? 152.178 161.831 149.909 1.00 90.06  ? 342 ARG   A CD  1 
ATOM   2228 N NE  . ARG   A 1 350 ? 151.551 160.804 149.084 1.00 95.83  ? 342 ARG   A NE  1 
ATOM   2229 C CZ  . ARG   A 1 350 ? 150.337 160.897 148.558 1.00 94.59  ? 342 ARG   A CZ  1 
ATOM   2230 N NH1 . ARG   A 1 350 ? 149.581 161.966 148.750 1.00 90.25  ? 342 ARG   A NH1 1 
ATOM   2231 N NH2 . ARG   A 1 350 ? 149.870 159.894 147.821 1.00 88.07  ? 342 ARG   A NH2 1 
ATOM   2232 N N   . ASP   A 1 351 ? 148.074 161.811 153.523 1.00 75.36  ? 343 ASP   A N   1 
ATOM   2233 C CA  . ASP   A 1 351 ? 146.896 162.641 153.753 1.00 74.77  ? 343 ASP   A CA  1 
ATOM   2234 C C   . ASP   A 1 351 ? 146.851 163.158 155.184 1.00 76.11  ? 343 ASP   A C   1 
ATOM   2235 O O   . ASP   A 1 351 ? 146.465 164.308 155.424 1.00 77.79  ? 343 ASP   A O   1 
ATOM   2236 C CB  . ASP   A 1 351 ? 145.627 161.853 153.429 1.00 75.35  ? 343 ASP   A CB  1 
ATOM   2237 C CG  . ASP   A 1 351 ? 145.006 162.265 152.111 1.00 84.47  ? 343 ASP   A CG  1 
ATOM   2238 O OD1 . ASP   A 1 351 ? 145.760 162.618 151.180 1.00 85.30  ? 343 ASP   A OD1 1 
ATOM   2239 O OD2 . ASP   A 1 351 ? 143.762 162.238 152.006 1.00 92.75  ? 343 ASP   A OD2 1 
ATOM   2240 N N   . PHE   A 1 352 ? 147.225 162.320 156.152 1.00 75.56  ? 344 PHE   A N   1 
ATOM   2241 C CA  . PHE   A 1 352 ? 147.236 162.763 157.542 1.00 72.18  ? 344 PHE   A CA  1 
ATOM   2242 C C   . PHE   A 1 352 ? 148.342 163.782 157.787 1.00 75.04  ? 344 PHE   A C   1 
ATOM   2243 O O   . PHE   A 1 352 ? 148.119 164.810 158.436 1.00 78.11  ? 344 PHE   A O   1 
ATOM   2244 C CB  . PHE   A 1 352 ? 147.394 161.566 158.479 1.00 66.76  ? 344 PHE   A CB  1 
ATOM   2245 C CG  . PHE   A 1 352 ? 147.297 161.923 159.934 1.00 63.16  ? 344 PHE   A CG  1 
ATOM   2246 C CD1 . PHE   A 1 352 ? 146.067 162.019 160.557 1.00 61.78  ? 344 PHE   A CD1 1 
ATOM   2247 C CD2 . PHE   A 1 352 ? 148.438 162.169 160.678 1.00 64.09  ? 344 PHE   A CD2 1 
ATOM   2248 C CE1 . PHE   A 1 352 ? 145.976 162.350 161.894 1.00 56.34  ? 344 PHE   A CE1 1 
ATOM   2249 C CE2 . PHE   A 1 352 ? 148.353 162.499 162.015 1.00 64.02  ? 344 PHE   A CE2 1 
ATOM   2250 C CZ  . PHE   A 1 352 ? 147.120 162.590 162.622 1.00 63.07  ? 344 PHE   A CZ  1 
ATOM   2251 N N   . CYS   A 1 353 ? 149.547 163.512 157.278 1.00 75.16  ? 345 CYS   A N   1 
ATOM   2252 C CA  . CYS   A 1 353 ? 150.661 164.426 157.510 1.00 75.15  ? 345 CYS   A CA  1 
ATOM   2253 C C   . CYS   A 1 353 ? 150.484 165.729 156.741 1.00 80.91  ? 345 CYS   A C   1 
ATOM   2254 O O   . CYS   A 1 353 ? 150.733 166.813 157.281 1.00 82.85  ? 345 CYS   A O   1 
ATOM   2255 C CB  . CYS   A 1 353 ? 151.980 163.754 157.132 1.00 76.66  ? 345 CYS   A CB  1 
ATOM   2256 S SG  . CYS   A 1 353 ? 152.489 162.423 158.242 1.00 81.17  ? 345 CYS   A SG  1 
ATOM   2257 N N   . PHE   A 1 354 ? 150.054 165.648 155.482 1.00 82.23  ? 346 PHE   A N   1 
ATOM   2258 C CA  . PHE   A 1 354 ? 149.912 166.815 154.610 1.00 83.16  ? 346 PHE   A CA  1 
ATOM   2259 C C   . PHE   A 1 354 ? 148.532 166.795 153.967 1.00 80.32  ? 346 PHE   A C   1 
ATOM   2260 O O   . PHE   A 1 354 ? 148.375 166.368 152.815 1.00 76.73  ? 346 PHE   A O   1 
ATOM   2261 C CB  . PHE   A 1 354 ? 151.012 166.847 153.549 1.00 83.32  ? 346 PHE   A CB  1 
ATOM   2262 C CG  . PHE   A 1 354 ? 152.361 166.435 154.063 1.00 84.94  ? 346 PHE   A CG  1 
ATOM   2263 C CD1 . PHE   A 1 354 ? 153.127 167.309 154.812 1.00 84.02  ? 346 PHE   A CD1 1 
ATOM   2264 C CD2 . PHE   A 1 354 ? 152.861 165.171 153.799 1.00 83.47  ? 346 PHE   A CD2 1 
ATOM   2265 C CE1 . PHE   A 1 354 ? 154.369 166.933 155.287 1.00 84.66  ? 346 PHE   A CE1 1 
ATOM   2266 C CE2 . PHE   A 1 354 ? 154.100 164.788 154.272 1.00 83.44  ? 346 PHE   A CE2 1 
ATOM   2267 C CZ  . PHE   A 1 354 ? 154.855 165.670 155.016 1.00 85.93  ? 346 PHE   A CZ  1 
ATOM   2268 N N   . PRO   A 1 355 ? 147.498 167.254 154.686 1.00 83.25  ? 347 PRO   A N   1 
ATOM   2269 C CA  . PRO   A 1 355 ? 146.137 167.296 154.142 1.00 86.00  ? 347 PRO   A CA  1 
ATOM   2270 C C   . PRO   A 1 355 ? 145.972 168.359 153.060 1.00 85.51  ? 347 PRO   A C   1 
ATOM   2271 O O   . PRO   A 1 355 ? 145.290 168.102 152.068 1.00 84.05  ? 347 PRO   A O   1 
ATOM   2272 C CB  . PRO   A 1 355 ? 145.281 167.629 155.366 1.00 85.54  ? 347 PRO   A CB  1 
ATOM   2273 C CG  . PRO   A 1 355 ? 146.197 168.363 156.275 1.00 86.56  ? 347 PRO   A CG  1 
ATOM   2274 C CD  . PRO   A 1 355 ? 147.566 167.786 156.058 1.00 82.96  ? 347 PRO   A CD  1 
HETATM 2275 C C01 . A1BNM B 2 .   ? 160.270 139.331 181.130 1.00 61.55  ? 401 A1BNM A C01 1 
HETATM 2276 C C02 . A1BNM B 2 .   ? 160.265 139.964 179.726 1.00 66.58  ? 401 A1BNM A C02 1 
HETATM 2277 C C04 . A1BNM B 2 .   ? 162.180 140.365 178.081 1.00 60.96  ? 401 A1BNM A C04 1 
HETATM 2278 C C05 . A1BNM B 2 .   ? 162.269 138.854 177.969 1.00 57.41  ? 401 A1BNM A C05 1 
HETATM 2279 C C06 . A1BNM B 2 .   ? 161.255 138.056 178.097 1.00 56.57  ? 401 A1BNM A C06 1 
HETATM 2280 C C07 . A1BNM B 2 .   ? 160.023 138.858 178.580 1.00 55.17  ? 401 A1BNM A C07 1 
HETATM 2281 C C08 . A1BNM B 2 .   ? 159.831 139.743 177.289 1.00 50.47  ? 401 A1BNM A C08 1 
HETATM 2282 C C09 . A1BNM B 2 .   ? 161.063 140.744 177.056 1.00 54.96  ? 401 A1BNM A C09 1 
HETATM 2283 C C10 . A1BNM B 2 .   ? 161.608 140.677 175.576 1.00 50.94  ? 401 A1BNM A C10 1 
HETATM 2284 C C12 . A1BNM B 2 .   ? 161.785 141.798 173.504 1.00 46.18  ? 401 A1BNM A C12 1 
HETATM 2285 C C14 . A1BNM B 2 .   ? 158.853 137.881 178.885 1.00 50.79  ? 401 A1BNM A C14 1 
HETATM 2286 C C15 . A1BNM B 2 .   ? 161.108 136.692 177.359 1.00 55.00  ? 401 A1BNM A C15 1 
HETATM 2287 C C16 . A1BNM B 2 .   ? 161.105 136.714 175.942 1.00 46.29  ? 401 A1BNM A C16 1 
HETATM 2288 C C17 . A1BNM B 2 .   ? 160.985 135.531 175.196 1.00 40.41  ? 401 A1BNM A C17 1 
HETATM 2289 C C18 . A1BNM B 2 .   ? 160.870 134.294 175.824 1.00 47.80  ? 401 A1BNM A C18 1 
HETATM 2290 C C19 . A1BNM B 2 .   ? 160.872 134.206 177.236 1.00 50.67  ? 401 A1BNM A C19 1 
HETATM 2291 C C21 . A1BNM B 2 .   ? 160.998 135.426 177.975 1.00 54.46  ? 401 A1BNM A C21 1 
HETATM 2292 C C22 . A1BNM B 2 .   ? 162.629 140.695 180.626 1.00 63.75  ? 401 A1BNM A C22 1 
HETATM 2293 C C23 . A1BNM B 2 .   ? 163.726 141.704 180.674 1.00 67.21  ? 401 A1BNM A C23 1 
HETATM 2294 C C24 . A1BNM B 2 .   ? 164.106 142.682 179.716 1.00 67.11  ? 401 A1BNM A C24 1 
HETATM 2295 C C27 . A1BNM B 2 .   ? 164.678 141.915 181.711 1.00 73.60  ? 401 A1BNM A C27 1 
HETATM 2296 C C28 . A1BNM B 2 .   ? 165.932 144.559 179.472 1.00 78.08  ? 401 A1BNM A C28 1 
HETATM 2297 C C29 . A1BNM B 2 .   ? 165.245 145.915 179.627 1.00 72.10  ? 401 A1BNM A C29 1 
HETATM 2298 N N03 . A1BNM B 2 .   ? 161.599 140.822 179.454 1.00 65.14  ? 401 A1BNM A N03 1 
HETATM 2299 N N25 . A1BNM B 2 .   ? 165.195 143.401 180.195 1.00 80.23  ? 401 A1BNM A N25 1 
HETATM 2300 N N26 . A1BNM B 2 .   ? 165.538 142.908 181.432 1.00 79.67  ? 401 A1BNM A N26 1 
HETATM 2301 O O11 . A1BNM B 2 .   ? 160.949 141.360 174.589 1.00 49.09  ? 401 A1BNM A O11 1 
HETATM 2302 O O13 . A1BNM B 2 .   ? 162.581 140.062 175.326 1.00 50.35  ? 401 A1BNM A O13 1 
HETATM 2303 O O20 . A1BNM B 2 .   ? 160.764 133.034 177.904 1.00 46.79  ? 401 A1BNM A O20 1 
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