data_8Y6Y
# 
_entry.id   8Y6Y 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   8Y6Y         pdb_00008y6y 10.2210/pdb8y6y/pdb 
WWPDB D_1300045125 ?            ?                   
EMDB  EMD-39004    ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-04-02 ? 
2 'EM metadata'     1 0 2025-04-02 ? 
3 FSC               1 0 2025-04-02 ? 
4 'Half map'        1 0 2025-04-02 1 
5 'Half map'        1 0 2025-04-02 2 
6 Image             1 0 2025-04-02 ? 
7 'Primary map'     1 0 2025-04-02 ? 
8 'Structure model' 1 1 2025-04-09 ? 
# 
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 FSC               repository 'Initial release' ? ? 
4 4 'Half map'        repository 'Initial release' ? ? 
5 5 'Half map'        repository 'Initial release' ? ? 
6 6 Image             repository 'Initial release' ? ? 
7 7 '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 8 'Structure model' 'Data collection'     
2 8 'Structure model' 'Database references' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 8 'Structure model' citation        
2 8 'Structure model' citation_author 
3 8 'Structure model' em_admin        
# 
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  8 'Structure model' '_citation.country'                 
2  8 'Structure model' '_citation.journal_abbrev'          
3  8 'Structure model' '_citation.journal_id_CSD'          
4  8 'Structure model' '_citation.journal_id_ISSN'         
5  8 'Structure model' '_citation.journal_volume'          
6  8 'Structure model' '_citation.page_first'              
7  8 'Structure model' '_citation.page_last'               
8  8 'Structure model' '_citation.pdbx_database_id_DOI'    
9  8 'Structure model' '_citation.pdbx_database_id_PubMed' 
10 8 'Structure model' '_citation.title'                   
11 8 'Structure model' '_citation.year'                    
12 8 'Structure model' '_em_admin.last_update'             
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  ? 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8Y6Y 
_pdbx_database_status.recvd_initial_deposition_date   2024-02-03 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBJ 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
_pdbx_database_related.db_name        EMDB 
_pdbx_database_related.details        'GLPG0974-bound human FFA2-BRIL' 
_pdbx_database_related.db_id          EMD-39004 
_pdbx_database_related.content_type   'associated EM volume' 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              c-hekato@g.ecc.u-tokyo.ac.jp 
_pdbx_contact_author.name_first         Hideaki 
_pdbx_contact_author.name_last          Kato 
_pdbx_contact_author.name_mi            E. 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-1941-5535 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Kugawa, M.'    1 0009-0000-9339-9820 
'Kawakami, K.'  2 0000-0002-2507-8619 
'Kise, R.'      3 0009-0000-6583-1719 
'Kobayashi, K.' 4 0000-0002-3366-3586 
'Kojima, A.'    5 ?                   
'Inoue, W.'     6 ?                   
'Fukuda, M.'    7 0000-0002-8824-846X 
'Inoue, A.'     8 ?                   
'Kato, H.E.'    9 0000-0002-1941-5535 
# 
_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                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Nat Commun' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2041-1723 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            16 
_citation.language                  ? 
_citation.page_first                2809 
_citation.page_last                 2809 
_citation.title                     'Structural insights into lipid chain-length selectivity and allosteric regulation of FFA2.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1038/s41467-025-57983-4 
_citation.pdbx_database_id_PubMed   40140663 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Kugawa, M.'       1  ?                   
primary 'Kawakami, K.'     2  0000-0002-2507-8619 
primary 'Kise, R.'         3  ?                   
primary 'Suomivuori, C.M.' 4  0000-0002-2445-8791 
primary 'Tsujimura, M.'    5  0000-0002-7554-7372 
primary 'Kobayashi, K.'    6  0000-0002-3366-3586 
primary 'Kojima, A.'       7  ?                   
primary 'Inoue, W.J.'      8  ?                   
primary 'Fukuda, M.'       9  0000-0002-8824-846X 
primary 'Matsui, T.E.'     10 ?                   
primary 'Fukunaga, A.'     11 ?                   
primary 'Koyanagi, J.'     12 ?                   
primary 'Kim, S.'          13 ?                   
primary 'Ikeda, H.'        14 ?                   
primary 'Yamashita, K.'    15 0000-0002-5442-7582 
primary 'Saito, K.'        16 0000-0002-2293-9743 
primary 'Ishikita, H.'     17 0000-0002-5849-8150 
primary 'Dror, R.O.'       18 0000-0002-6418-2793 
primary 'Inoue, A.'        19 0000-0003-0805-4049 
primary 'Kato, H.E.'       20 0000-0002-1941-5535 
# 
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 'Free fatty acid receptor 2,Soluble cytochrome b562' 48943.805 1 ? ? ? ? 
2 non-polymer syn 
'4-[[(2~{R})-1-(1-benzothiophen-3-ylcarbonyl)-2-methyl-azetidin-2-yl]carbonyl-[(3-chlorophenyl)methyl]amino]butanoic acid' 484.995 
1 ? ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'G-protein coupled receptor 43,Cytochrome b-562' 
# 
_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       
;MLPDWKSSLILMAYIIIFLTGLPANLLALRAFVGRIRQPQPAPVHILLLSLTLADLLLLLLLPFKIIEAASNFRWYLPKV
VCALTSFGFYSSIYCSTWLLAGISIERYLGVAFPVQYKLSRRPLYGVIAALVAWVMSFGHCTIVIIVQYLNTTEQVRSGN
EITCYENFTDNQLDVVLPVRLELCLVLFFIPMAVTIFCYWRFVWIMLSQPADLEDNWETLNDNLKVIEKADNAAQVKDAL
TKMRAAALDAQKATPPKLEDKSPDSPEMKDFRHGFDILVGQIDDALKLANEGKVKEAQAAAEQLKTTRNAYIQKYLLVGA
QRRRRAVGLAVVTLLNFLVCFGPYNVSHLVGYHQRKSPWWRSIAVVFSSLNASLDPLLFYFSSSVVRRAFGRGLQVLRNQ
GSSLLGRRGKDTAEGTNEDRGVGQGEGMPSSDFTTE
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MLPDWKSSLILMAYIIIFLTGLPANLLALRAFVGRIRQPQPAPVHILLLSLTLADLLLLLLLPFKIIEAASNFRWYLPKV
VCALTSFGFYSSIYCSTWLLAGISIERYLGVAFPVQYKLSRRPLYGVIAALVAWVMSFGHCTIVIIVQYLNTTEQVRSGN
EITCYENFTDNQLDVVLPVRLELCLVLFFIPMAVTIFCYWRFVWIMLSQPADLEDNWETLNDNLKVIEKADNAAQVKDAL
TKMRAAALDAQKATPPKLEDKSPDSPEMKDFRHGFDILVGQIDDALKLANEGKVKEAQAAAEQLKTTRNAYIQKYLLVGA
QRRRRAVGLAVVTLLNFLVCFGPYNVSHLVGYHQRKSPWWRSIAVVFSSLNASLDPLLFYFSSSVVRRAFGRGLQVLRNQ
GSSLLGRRGKDTAEGTNEDRGVGQGEGMPSSDFTTE
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
_pdbx_entity_nonpoly.entity_id   2 
_pdbx_entity_nonpoly.name        
'4-[[(2~{R})-1-(1-benzothiophen-3-ylcarbonyl)-2-methyl-azetidin-2-yl]carbonyl-[(3-chlorophenyl)methyl]amino]butanoic acid' 
_pdbx_entity_nonpoly.comp_id     A1LYD 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   LEU n 
1 3   PRO n 
1 4   ASP n 
1 5   TRP n 
1 6   LYS n 
1 7   SER n 
1 8   SER n 
1 9   LEU n 
1 10  ILE n 
1 11  LEU n 
1 12  MET n 
1 13  ALA n 
1 14  TYR n 
1 15  ILE n 
1 16  ILE n 
1 17  ILE n 
1 18  PHE n 
1 19  LEU n 
1 20  THR n 
1 21  GLY n 
1 22  LEU n 
1 23  PRO n 
1 24  ALA n 
1 25  ASN n 
1 26  LEU n 
1 27  LEU n 
1 28  ALA n 
1 29  LEU n 
1 30  ARG n 
1 31  ALA n 
1 32  PHE n 
1 33  VAL n 
1 34  GLY n 
1 35  ARG n 
1 36  ILE n 
1 37  ARG n 
1 38  GLN n 
1 39  PRO n 
1 40  GLN n 
1 41  PRO n 
1 42  ALA n 
1 43  PRO n 
1 44  VAL n 
1 45  HIS n 
1 46  ILE n 
1 47  LEU n 
1 48  LEU n 
1 49  LEU n 
1 50  SER n 
1 51  LEU n 
1 52  THR n 
1 53  LEU n 
1 54  ALA n 
1 55  ASP n 
1 56  LEU n 
1 57  LEU n 
1 58  LEU n 
1 59  LEU n 
1 60  LEU n 
1 61  LEU n 
1 62  LEU n 
1 63  PRO n 
1 64  PHE n 
1 65  LYS n 
1 66  ILE n 
1 67  ILE n 
1 68  GLU n 
1 69  ALA n 
1 70  ALA n 
1 71  SER n 
1 72  ASN n 
1 73  PHE n 
1 74  ARG n 
1 75  TRP n 
1 76  TYR n 
1 77  LEU n 
1 78  PRO n 
1 79  LYS n 
1 80  VAL n 
1 81  VAL n 
1 82  CYS n 
1 83  ALA n 
1 84  LEU n 
1 85  THR n 
1 86  SER n 
1 87  PHE n 
1 88  GLY n 
1 89  PHE n 
1 90  TYR n 
1 91  SER n 
1 92  SER n 
1 93  ILE n 
1 94  TYR n 
1 95  CYS n 
1 96  SER n 
1 97  THR n 
1 98  TRP n 
1 99  LEU n 
1 100 LEU n 
1 101 ALA n 
1 102 GLY n 
1 103 ILE n 
1 104 SER n 
1 105 ILE n 
1 106 GLU n 
1 107 ARG n 
1 108 TYR n 
1 109 LEU n 
1 110 GLY n 
1 111 VAL n 
1 112 ALA n 
1 113 PHE n 
1 114 PRO n 
1 115 VAL n 
1 116 GLN n 
1 117 TYR n 
1 118 LYS n 
1 119 LEU n 
1 120 SER n 
1 121 ARG n 
1 122 ARG n 
1 123 PRO n 
1 124 LEU n 
1 125 TYR n 
1 126 GLY n 
1 127 VAL n 
1 128 ILE n 
1 129 ALA n 
1 130 ALA n 
1 131 LEU n 
1 132 VAL n 
1 133 ALA n 
1 134 TRP n 
1 135 VAL n 
1 136 MET n 
1 137 SER n 
1 138 PHE n 
1 139 GLY n 
1 140 HIS n 
1 141 CYS n 
1 142 THR n 
1 143 ILE n 
1 144 VAL n 
1 145 ILE n 
1 146 ILE n 
1 147 VAL n 
1 148 GLN n 
1 149 TYR n 
1 150 LEU n 
1 151 ASN n 
1 152 THR n 
1 153 THR n 
1 154 GLU n 
1 155 GLN n 
1 156 VAL n 
1 157 ARG n 
1 158 SER n 
1 159 GLY n 
1 160 ASN n 
1 161 GLU n 
1 162 ILE n 
1 163 THR n 
1 164 CYS n 
1 165 TYR n 
1 166 GLU n 
1 167 ASN n 
1 168 PHE n 
1 169 THR n 
1 170 ASP n 
1 171 ASN n 
1 172 GLN n 
1 173 LEU n 
1 174 ASP n 
1 175 VAL n 
1 176 VAL n 
1 177 LEU n 
1 178 PRO n 
1 179 VAL n 
1 180 ARG n 
1 181 LEU n 
1 182 GLU n 
1 183 LEU n 
1 184 CYS n 
1 185 LEU n 
1 186 VAL n 
1 187 LEU n 
1 188 PHE n 
1 189 PHE n 
1 190 ILE n 
1 191 PRO n 
1 192 MET n 
1 193 ALA n 
1 194 VAL n 
1 195 THR n 
1 196 ILE n 
1 197 PHE n 
1 198 CYS n 
1 199 TYR n 
1 200 TRP n 
1 201 ARG n 
1 202 PHE n 
1 203 VAL n 
1 204 TRP n 
1 205 ILE n 
1 206 MET n 
1 207 LEU n 
1 208 SER n 
1 209 GLN n 
1 210 PRO n 
1 211 ALA n 
1 212 ASP n 
1 213 LEU n 
1 214 GLU n 
1 215 ASP n 
1 216 ASN n 
1 217 TRP n 
1 218 GLU n 
1 219 THR n 
1 220 LEU n 
1 221 ASN n 
1 222 ASP n 
1 223 ASN n 
1 224 LEU n 
1 225 LYS n 
1 226 VAL n 
1 227 ILE n 
1 228 GLU n 
1 229 LYS n 
1 230 ALA n 
1 231 ASP n 
1 232 ASN n 
1 233 ALA n 
1 234 ALA n 
1 235 GLN n 
1 236 VAL n 
1 237 LYS n 
1 238 ASP n 
1 239 ALA n 
1 240 LEU n 
1 241 THR n 
1 242 LYS n 
1 243 MET n 
1 244 ARG n 
1 245 ALA n 
1 246 ALA n 
1 247 ALA n 
1 248 LEU n 
1 249 ASP n 
1 250 ALA n 
1 251 GLN n 
1 252 LYS n 
1 253 ALA n 
1 254 THR n 
1 255 PRO n 
1 256 PRO n 
1 257 LYS n 
1 258 LEU n 
1 259 GLU n 
1 260 ASP n 
1 261 LYS n 
1 262 SER n 
1 263 PRO n 
1 264 ASP n 
1 265 SER n 
1 266 PRO n 
1 267 GLU n 
1 268 MET n 
1 269 LYS n 
1 270 ASP n 
1 271 PHE n 
1 272 ARG n 
1 273 HIS n 
1 274 GLY n 
1 275 PHE n 
1 276 ASP n 
1 277 ILE n 
1 278 LEU n 
1 279 VAL n 
1 280 GLY n 
1 281 GLN n 
1 282 ILE n 
1 283 ASP n 
1 284 ASP n 
1 285 ALA n 
1 286 LEU n 
1 287 LYS n 
1 288 LEU n 
1 289 ALA n 
1 290 ASN n 
1 291 GLU n 
1 292 GLY n 
1 293 LYS n 
1 294 VAL n 
1 295 LYS n 
1 296 GLU n 
1 297 ALA n 
1 298 GLN n 
1 299 ALA n 
1 300 ALA n 
1 301 ALA n 
1 302 GLU n 
1 303 GLN n 
1 304 LEU n 
1 305 LYS n 
1 306 THR n 
1 307 THR n 
1 308 ARG n 
1 309 ASN n 
1 310 ALA n 
1 311 TYR n 
1 312 ILE n 
1 313 GLN n 
1 314 LYS n 
1 315 TYR n 
1 316 LEU n 
1 317 LEU n 
1 318 VAL n 
1 319 GLY n 
1 320 ALA n 
1 321 GLN n 
1 322 ARG n 
1 323 ARG n 
1 324 ARG n 
1 325 ARG n 
1 326 ALA n 
1 327 VAL n 
1 328 GLY n 
1 329 LEU n 
1 330 ALA n 
1 331 VAL n 
1 332 VAL n 
1 333 THR n 
1 334 LEU n 
1 335 LEU n 
1 336 ASN n 
1 337 PHE n 
1 338 LEU n 
1 339 VAL n 
1 340 CYS n 
1 341 PHE n 
1 342 GLY n 
1 343 PRO n 
1 344 TYR n 
1 345 ASN n 
1 346 VAL n 
1 347 SER n 
1 348 HIS n 
1 349 LEU n 
1 350 VAL n 
1 351 GLY n 
1 352 TYR n 
1 353 HIS n 
1 354 GLN n 
1 355 ARG n 
1 356 LYS n 
1 357 SER n 
1 358 PRO n 
1 359 TRP n 
1 360 TRP n 
1 361 ARG n 
1 362 SER n 
1 363 ILE n 
1 364 ALA n 
1 365 VAL n 
1 366 VAL n 
1 367 PHE n 
1 368 SER n 
1 369 SER n 
1 370 LEU n 
1 371 ASN n 
1 372 ALA n 
1 373 SER n 
1 374 LEU n 
1 375 ASP n 
1 376 PRO n 
1 377 LEU n 
1 378 LEU n 
1 379 PHE n 
1 380 TYR n 
1 381 PHE n 
1 382 SER n 
1 383 SER n 
1 384 SER n 
1 385 VAL n 
1 386 VAL n 
1 387 ARG n 
1 388 ARG n 
1 389 ALA n 
1 390 PHE n 
1 391 GLY n 
1 392 ARG n 
1 393 GLY n 
1 394 LEU n 
1 395 GLN n 
1 396 VAL n 
1 397 LEU n 
1 398 ARG n 
1 399 ASN n 
1 400 GLN n 
1 401 GLY n 
1 402 SER n 
1 403 SER n 
1 404 LEU n 
1 405 LEU n 
1 406 GLY n 
1 407 ARG n 
1 408 ARG n 
1 409 GLY n 
1 410 LYS n 
1 411 ASP n 
1 412 THR n 
1 413 ALA n 
1 414 GLU n 
1 415 GLY n 
1 416 THR n 
1 417 ASN n 
1 418 GLU n 
1 419 ASP n 
1 420 ARG n 
1 421 GLY n 
1 422 VAL n 
1 423 GLY n 
1 424 GLN n 
1 425 GLY n 
1 426 GLU n 
1 427 GLY n 
1 428 MET n 
1 429 PRO n 
1 430 SER n 
1 431 SER n 
1 432 ASP n 
1 433 PHE n 
1 434 THR n 
1 435 THR n 
1 436 GLU n 
# 
loop_
_entity_src_gen.entity_id 
_entity_src_gen.pdbx_src_id 
_entity_src_gen.pdbx_alt_source_flag 
_entity_src_gen.pdbx_seq_type 
_entity_src_gen.pdbx_beg_seq_num 
_entity_src_gen.pdbx_end_seq_num 
_entity_src_gen.gene_src_common_name 
_entity_src_gen.gene_src_genus 
_entity_src_gen.pdbx_gene_src_gene 
_entity_src_gen.gene_src_species 
_entity_src_gen.gene_src_strain 
_entity_src_gen.gene_src_tissue 
_entity_src_gen.gene_src_tissue_fraction 
_entity_src_gen.gene_src_details 
_entity_src_gen.pdbx_gene_src_fragment 
_entity_src_gen.pdbx_gene_src_scientific_name 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 
_entity_src_gen.pdbx_gene_src_variant 
_entity_src_gen.pdbx_gene_src_cell_line 
_entity_src_gen.pdbx_gene_src_atcc 
_entity_src_gen.pdbx_gene_src_organ 
_entity_src_gen.pdbx_gene_src_organelle 
_entity_src_gen.pdbx_gene_src_cell 
_entity_src_gen.pdbx_gene_src_cellular_location 
_entity_src_gen.host_org_common_name 
_entity_src_gen.pdbx_host_org_scientific_name 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 
_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 
1 1 sample 'Biological sequence' 1   210 human ? 'FFAR2, FFA2, GPCR43, GPR43' ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? 
'Homo sapiens' 9606 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
1 2 sample 'Biological sequence' 211 316 human ? cybC                         ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? 
'Homo sapiens' 9606 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
1 3 sample 'Biological sequence' 317 436 human ? 'FFAR2, FFA2, GPCR43, GPR43' ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? 
'Homo sapiens' 9606 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
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 
A1LYD non-polymer         . 
'4-[[(2~{R})-1-(1-benzothiophen-3-ylcarbonyl)-2-methyl-azetidin-2-yl]carbonyl-[(3-chlorophenyl)methyl]amino]butanoic acid' ? 
'C25 H25 Cl N2 O4 S' 484.995 
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   MET 1   1   ?   ?   ?   A . n 
A 1 2   LEU 2   2   ?   ?   ?   A . n 
A 1 3   PRO 3   3   ?   ?   ?   A . n 
A 1 4   ASP 4   4   4   ASP ASP A . n 
A 1 5   TRP 5   5   5   TRP TRP A . n 
A 1 6   LYS 6   6   6   LYS LYS A . n 
A 1 7   SER 7   7   7   SER SER A . n 
A 1 8   SER 8   8   8   SER SER A . n 
A 1 9   LEU 9   9   9   LEU LEU A . n 
A 1 10  ILE 10  10  10  ILE ILE A . n 
A 1 11  LEU 11  11  11  LEU LEU A . n 
A 1 12  MET 12  12  12  MET MET A . n 
A 1 13  ALA 13  13  13  ALA ALA A . n 
A 1 14  TYR 14  14  14  TYR TYR A . n 
A 1 15  ILE 15  15  15  ILE ILE A . n 
A 1 16  ILE 16  16  16  ILE ILE A . n 
A 1 17  ILE 17  17  17  ILE ILE A . n 
A 1 18  PHE 18  18  18  PHE PHE A . n 
A 1 19  LEU 19  19  19  LEU LEU A . n 
A 1 20  THR 20  20  20  THR THR A . n 
A 1 21  GLY 21  21  21  GLY GLY A . n 
A 1 22  LEU 22  22  22  LEU LEU A . n 
A 1 23  PRO 23  23  23  PRO PRO A . n 
A 1 24  ALA 24  24  24  ALA ALA A . n 
A 1 25  ASN 25  25  25  ASN ASN A . n 
A 1 26  LEU 26  26  26  LEU LEU A . n 
A 1 27  LEU 27  27  27  LEU LEU A . n 
A 1 28  ALA 28  28  28  ALA ALA A . n 
A 1 29  LEU 29  29  29  LEU LEU A . n 
A 1 30  ARG 30  30  30  ARG ARG A . n 
A 1 31  ALA 31  31  31  ALA ALA A . n 
A 1 32  PHE 32  32  32  PHE PHE A . n 
A 1 33  VAL 33  33  33  VAL VAL A . n 
A 1 34  GLY 34  34  34  GLY GLY A . n 
A 1 35  ARG 35  35  35  ARG ARG A . n 
A 1 36  ILE 36  36  36  ILE ILE A . n 
A 1 37  ARG 37  37  37  ARG ARG A . n 
A 1 38  GLN 38  38  38  GLN GLN A . n 
A 1 39  PRO 39  39  39  PRO PRO A . n 
A 1 40  GLN 40  40  40  GLN GLN A . n 
A 1 41  PRO 41  41  41  PRO PRO A . n 
A 1 42  ALA 42  42  42  ALA ALA A . n 
A 1 43  PRO 43  43  43  PRO PRO A . n 
A 1 44  VAL 44  44  44  VAL VAL A . n 
A 1 45  HIS 45  45  45  HIS HIS A . n 
A 1 46  ILE 46  46  46  ILE ILE A . n 
A 1 47  LEU 47  47  47  LEU LEU A . n 
A 1 48  LEU 48  48  48  LEU LEU A . n 
A 1 49  LEU 49  49  49  LEU LEU A . n 
A 1 50  SER 50  50  50  SER SER A . n 
A 1 51  LEU 51  51  51  LEU LEU A . n 
A 1 52  THR 52  52  52  THR THR A . n 
A 1 53  LEU 53  53  53  LEU LEU A . n 
A 1 54  ALA 54  54  54  ALA ALA A . n 
A 1 55  ASP 55  55  55  ASP ASP A . n 
A 1 56  LEU 56  56  56  LEU LEU A . n 
A 1 57  LEU 57  57  57  LEU LEU A . n 
A 1 58  LEU 58  58  58  LEU LEU A . n 
A 1 59  LEU 59  59  59  LEU LEU A . n 
A 1 60  LEU 60  60  60  LEU LEU A . n 
A 1 61  LEU 61  61  61  LEU LEU A . n 
A 1 62  LEU 62  62  62  LEU LEU A . n 
A 1 63  PRO 63  63  63  PRO PRO A . n 
A 1 64  PHE 64  64  64  PHE PHE A . n 
A 1 65  LYS 65  65  65  LYS LYS A . n 
A 1 66  ILE 66  66  66  ILE ILE A . n 
A 1 67  ILE 67  67  67  ILE ILE A . n 
A 1 68  GLU 68  68  68  GLU GLU A . n 
A 1 69  ALA 69  69  69  ALA ALA A . n 
A 1 70  ALA 70  70  70  ALA ALA A . n 
A 1 71  SER 71  71  71  SER SER A . n 
A 1 72  ASN 72  72  72  ASN ASN A . n 
A 1 73  PHE 73  73  73  PHE PHE A . n 
A 1 74  ARG 74  74  74  ARG ARG A . n 
A 1 75  TRP 75  75  75  TRP TRP A . n 
A 1 76  TYR 76  76  76  TYR TYR A . n 
A 1 77  LEU 77  77  77  LEU LEU A . n 
A 1 78  PRO 78  78  78  PRO PRO A . n 
A 1 79  LYS 79  79  79  LYS LYS A . n 
A 1 80  VAL 80  80  80  VAL VAL A . n 
A 1 81  VAL 81  81  81  VAL VAL A . n 
A 1 82  CYS 82  82  82  CYS CYS A . n 
A 1 83  ALA 83  83  83  ALA ALA A . n 
A 1 84  LEU 84  84  84  LEU LEU A . n 
A 1 85  THR 85  85  85  THR THR A . n 
A 1 86  SER 86  86  86  SER SER A . n 
A 1 87  PHE 87  87  87  PHE PHE A . n 
A 1 88  GLY 88  88  88  GLY GLY A . n 
A 1 89  PHE 89  89  89  PHE PHE A . n 
A 1 90  TYR 90  90  90  TYR TYR A . n 
A 1 91  SER 91  91  91  SER SER A . n 
A 1 92  SER 92  92  92  SER SER A . n 
A 1 93  ILE 93  93  93  ILE ILE A . n 
A 1 94  TYR 94  94  94  TYR TYR A . n 
A 1 95  CYS 95  95  95  CYS CYS A . n 
A 1 96  SER 96  96  96  SER SER A . n 
A 1 97  THR 97  97  97  THR THR A . n 
A 1 98  TRP 98  98  98  TRP TRP A . n 
A 1 99  LEU 99  99  99  LEU LEU A . n 
A 1 100 LEU 100 100 100 LEU LEU A . n 
A 1 101 ALA 101 101 101 ALA ALA A . n 
A 1 102 GLY 102 102 102 GLY GLY A . n 
A 1 103 ILE 103 103 103 ILE ILE A . n 
A 1 104 SER 104 104 104 SER SER A . n 
A 1 105 ILE 105 105 105 ILE ILE A . n 
A 1 106 GLU 106 106 106 GLU GLU A . n 
A 1 107 ARG 107 107 107 ARG ARG A . n 
A 1 108 TYR 108 108 108 TYR TYR A . n 
A 1 109 LEU 109 109 109 LEU LEU A . n 
A 1 110 GLY 110 110 110 GLY GLY A . n 
A 1 111 VAL 111 111 111 VAL VAL A . n 
A 1 112 ALA 112 112 112 ALA ALA A . n 
A 1 113 PHE 113 113 113 PHE PHE A . n 
A 1 114 PRO 114 114 114 PRO PRO A . n 
A 1 115 VAL 115 115 115 VAL VAL A . n 
A 1 116 GLN 116 116 116 GLN GLN A . n 
A 1 117 TYR 117 117 117 TYR TYR A . n 
A 1 118 LYS 118 118 118 LYS LYS A . n 
A 1 119 LEU 119 119 119 LEU LEU A . n 
A 1 120 SER 120 120 120 SER SER A . n 
A 1 121 ARG 121 121 121 ARG ARG A . n 
A 1 122 ARG 122 122 122 ARG ARG A . n 
A 1 123 PRO 123 123 123 PRO PRO A . n 
A 1 124 LEU 124 124 124 LEU LEU A . n 
A 1 125 TYR 125 125 125 TYR TYR A . n 
A 1 126 GLY 126 126 126 GLY GLY A . n 
A 1 127 VAL 127 127 127 VAL VAL A . n 
A 1 128 ILE 128 128 128 ILE ILE A . n 
A 1 129 ALA 129 129 129 ALA ALA A . n 
A 1 130 ALA 130 130 130 ALA ALA A . n 
A 1 131 LEU 131 131 131 LEU LEU A . n 
A 1 132 VAL 132 132 132 VAL VAL A . n 
A 1 133 ALA 133 133 133 ALA ALA A . n 
A 1 134 TRP 134 134 134 TRP TRP A . n 
A 1 135 VAL 135 135 135 VAL VAL A . n 
A 1 136 MET 136 136 136 MET MET A . n 
A 1 137 SER 137 137 137 SER SER A . n 
A 1 138 PHE 138 138 138 PHE PHE A . n 
A 1 139 GLY 139 139 139 GLY GLY A . n 
A 1 140 HIS 140 140 140 HIS HIS A . n 
A 1 141 CYS 141 141 141 CYS CYS A . n 
A 1 142 THR 142 142 142 THR THR A . n 
A 1 143 ILE 143 143 143 ILE ILE A . n 
A 1 144 VAL 144 144 144 VAL VAL A . n 
A 1 145 ILE 145 145 145 ILE ILE A . n 
A 1 146 ILE 146 146 146 ILE ILE A . n 
A 1 147 VAL 147 147 147 VAL VAL A . n 
A 1 148 GLN 148 148 148 GLN GLN A . n 
A 1 149 TYR 149 149 149 TYR TYR A . n 
A 1 150 LEU 150 150 150 LEU LEU A . n 
A 1 151 ASN 151 151 ?   ?   ?   A . n 
A 1 152 THR 152 152 ?   ?   ?   A . n 
A 1 153 THR 153 153 ?   ?   ?   A . n 
A 1 154 GLU 154 154 ?   ?   ?   A . n 
A 1 155 GLN 155 155 ?   ?   ?   A . n 
A 1 156 VAL 156 156 ?   ?   ?   A . n 
A 1 157 ARG 157 157 ?   ?   ?   A . n 
A 1 158 SER 158 158 158 SER SER A . n 
A 1 159 GLY 159 159 159 GLY GLY A . n 
A 1 160 ASN 160 160 160 ASN ASN A . n 
A 1 161 GLU 161 161 161 GLU GLU A . n 
A 1 162 ILE 162 162 162 ILE ILE A . n 
A 1 163 THR 163 163 163 THR THR A . n 
A 1 164 CYS 164 164 164 CYS CYS A . n 
A 1 165 TYR 165 165 165 TYR TYR A . n 
A 1 166 GLU 166 166 166 GLU GLU A . n 
A 1 167 ASN 167 167 167 ASN ASN A . n 
A 1 168 PHE 168 168 168 PHE PHE A . n 
A 1 169 THR 169 169 169 THR THR A . n 
A 1 170 ASP 170 170 170 ASP ASP A . n 
A 1 171 ASN 171 171 171 ASN ASN A . n 
A 1 172 GLN 172 172 172 GLN GLN A . n 
A 1 173 LEU 173 173 173 LEU LEU A . n 
A 1 174 ASP 174 174 174 ASP ASP A . n 
A 1 175 VAL 175 175 175 VAL VAL A . n 
A 1 176 VAL 176 176 176 VAL VAL A . n 
A 1 177 LEU 177 177 177 LEU LEU A . n 
A 1 178 PRO 178 178 178 PRO PRO A . n 
A 1 179 VAL 179 179 179 VAL VAL A . n 
A 1 180 ARG 180 180 180 ARG ARG A . n 
A 1 181 LEU 181 181 181 LEU LEU A . n 
A 1 182 GLU 182 182 182 GLU GLU A . n 
A 1 183 LEU 183 183 183 LEU LEU A . n 
A 1 184 CYS 184 184 184 CYS CYS A . n 
A 1 185 LEU 185 185 185 LEU LEU A . n 
A 1 186 VAL 186 186 186 VAL VAL A . n 
A 1 187 LEU 187 187 187 LEU LEU A . n 
A 1 188 PHE 188 188 188 PHE PHE A . n 
A 1 189 PHE 189 189 189 PHE PHE A . n 
A 1 190 ILE 190 190 190 ILE ILE A . n 
A 1 191 PRO 191 191 191 PRO PRO A . n 
A 1 192 MET 192 192 192 MET MET A . n 
A 1 193 ALA 193 193 193 ALA ALA A . n 
A 1 194 VAL 194 194 194 VAL VAL A . n 
A 1 195 THR 195 195 195 THR THR A . n 
A 1 196 ILE 196 196 196 ILE ILE A . n 
A 1 197 PHE 197 197 197 PHE PHE A . n 
A 1 198 CYS 198 198 198 CYS CYS A . n 
A 1 199 TYR 199 199 199 TYR TYR A . n 
A 1 200 TRP 200 200 200 TRP TRP A . n 
A 1 201 ARG 201 201 201 ARG ARG A . n 
A 1 202 PHE 202 202 202 PHE PHE A . n 
A 1 203 VAL 203 203 203 VAL VAL A . n 
A 1 204 TRP 204 204 204 TRP TRP A . n 
A 1 205 ILE 205 205 205 ILE ILE A . n 
A 1 206 MET 206 206 206 MET MET A . n 
A 1 207 LEU 207 207 207 LEU LEU A . n 
A 1 208 SER 208 208 208 SER SER A . n 
A 1 209 GLN 209 209 ?   ?   ?   A . n 
A 1 210 PRO 210 210 ?   ?   ?   A . n 
A 1 211 ALA 211 211 ?   ?   ?   A . n 
A 1 212 ASP 212 212 ?   ?   ?   A . n 
A 1 213 LEU 213 213 ?   ?   ?   A . n 
A 1 214 GLU 214 214 ?   ?   ?   A . n 
A 1 215 ASP 215 215 ?   ?   ?   A . n 
A 1 216 ASN 216 216 ?   ?   ?   A . n 
A 1 217 TRP 217 217 ?   ?   ?   A . n 
A 1 218 GLU 218 218 ?   ?   ?   A . n 
A 1 219 THR 219 219 ?   ?   ?   A . n 
A 1 220 LEU 220 220 ?   ?   ?   A . n 
A 1 221 ASN 221 221 ?   ?   ?   A . n 
A 1 222 ASP 222 222 ?   ?   ?   A . n 
A 1 223 ASN 223 223 ?   ?   ?   A . n 
A 1 224 LEU 224 224 ?   ?   ?   A . n 
A 1 225 LYS 225 225 ?   ?   ?   A . n 
A 1 226 VAL 226 226 ?   ?   ?   A . n 
A 1 227 ILE 227 227 ?   ?   ?   A . n 
A 1 228 GLU 228 228 ?   ?   ?   A . n 
A 1 229 LYS 229 229 ?   ?   ?   A . n 
A 1 230 ALA 230 230 ?   ?   ?   A . n 
A 1 231 ASP 231 231 ?   ?   ?   A . n 
A 1 232 ASN 232 232 ?   ?   ?   A . n 
A 1 233 ALA 233 233 ?   ?   ?   A . n 
A 1 234 ALA 234 234 ?   ?   ?   A . n 
A 1 235 GLN 235 235 ?   ?   ?   A . n 
A 1 236 VAL 236 236 ?   ?   ?   A . n 
A 1 237 LYS 237 237 ?   ?   ?   A . n 
A 1 238 ASP 238 238 ?   ?   ?   A . n 
A 1 239 ALA 239 239 ?   ?   ?   A . n 
A 1 240 LEU 240 240 ?   ?   ?   A . n 
A 1 241 THR 241 241 ?   ?   ?   A . n 
A 1 242 LYS 242 242 ?   ?   ?   A . n 
A 1 243 MET 243 243 ?   ?   ?   A . n 
A 1 244 ARG 244 244 ?   ?   ?   A . n 
A 1 245 ALA 245 245 ?   ?   ?   A . n 
A 1 246 ALA 246 246 ?   ?   ?   A . n 
A 1 247 ALA 247 247 ?   ?   ?   A . n 
A 1 248 LEU 248 248 ?   ?   ?   A . n 
A 1 249 ASP 249 249 ?   ?   ?   A . n 
A 1 250 ALA 250 250 ?   ?   ?   A . n 
A 1 251 GLN 251 251 ?   ?   ?   A . n 
A 1 252 LYS 252 252 ?   ?   ?   A . n 
A 1 253 ALA 253 253 ?   ?   ?   A . n 
A 1 254 THR 254 254 ?   ?   ?   A . n 
A 1 255 PRO 255 255 ?   ?   ?   A . n 
A 1 256 PRO 256 256 ?   ?   ?   A . n 
A 1 257 LYS 257 257 ?   ?   ?   A . n 
A 1 258 LEU 258 258 ?   ?   ?   A . n 
A 1 259 GLU 259 259 ?   ?   ?   A . n 
A 1 260 ASP 260 260 ?   ?   ?   A . n 
A 1 261 LYS 261 261 ?   ?   ?   A . n 
A 1 262 SER 262 262 ?   ?   ?   A . n 
A 1 263 PRO 263 263 ?   ?   ?   A . n 
A 1 264 ASP 264 264 ?   ?   ?   A . n 
A 1 265 SER 265 265 ?   ?   ?   A . n 
A 1 266 PRO 266 266 ?   ?   ?   A . n 
A 1 267 GLU 267 267 ?   ?   ?   A . n 
A 1 268 MET 268 268 ?   ?   ?   A . n 
A 1 269 LYS 269 269 ?   ?   ?   A . n 
A 1 270 ASP 270 270 ?   ?   ?   A . n 
A 1 271 PHE 271 271 ?   ?   ?   A . n 
A 1 272 ARG 272 272 ?   ?   ?   A . n 
A 1 273 HIS 273 273 ?   ?   ?   A . n 
A 1 274 GLY 274 274 ?   ?   ?   A . n 
A 1 275 PHE 275 275 ?   ?   ?   A . n 
A 1 276 ASP 276 276 ?   ?   ?   A . n 
A 1 277 ILE 277 277 ?   ?   ?   A . n 
A 1 278 LEU 278 278 ?   ?   ?   A . n 
A 1 279 VAL 279 279 ?   ?   ?   A . n 
A 1 280 GLY 280 280 ?   ?   ?   A . n 
A 1 281 GLN 281 281 ?   ?   ?   A . n 
A 1 282 ILE 282 282 ?   ?   ?   A . n 
A 1 283 ASP 283 283 ?   ?   ?   A . n 
A 1 284 ASP 284 284 ?   ?   ?   A . n 
A 1 285 ALA 285 285 ?   ?   ?   A . n 
A 1 286 LEU 286 286 ?   ?   ?   A . n 
A 1 287 LYS 287 287 ?   ?   ?   A . n 
A 1 288 LEU 288 288 ?   ?   ?   A . n 
A 1 289 ALA 289 289 ?   ?   ?   A . n 
A 1 290 ASN 290 290 ?   ?   ?   A . n 
A 1 291 GLU 291 291 ?   ?   ?   A . n 
A 1 292 GLY 292 292 ?   ?   ?   A . n 
A 1 293 LYS 293 293 ?   ?   ?   A . n 
A 1 294 VAL 294 294 ?   ?   ?   A . n 
A 1 295 LYS 295 295 ?   ?   ?   A . n 
A 1 296 GLU 296 296 ?   ?   ?   A . n 
A 1 297 ALA 297 297 ?   ?   ?   A . n 
A 1 298 GLN 298 298 ?   ?   ?   A . n 
A 1 299 ALA 299 299 ?   ?   ?   A . n 
A 1 300 ALA 300 300 ?   ?   ?   A . n 
A 1 301 ALA 301 301 ?   ?   ?   A . n 
A 1 302 GLU 302 302 ?   ?   ?   A . n 
A 1 303 GLN 303 303 ?   ?   ?   A . n 
A 1 304 LEU 304 304 ?   ?   ?   A . n 
A 1 305 LYS 305 305 ?   ?   ?   A . n 
A 1 306 THR 306 306 ?   ?   ?   A . n 
A 1 307 THR 307 307 ?   ?   ?   A . n 
A 1 308 ARG 308 308 ?   ?   ?   A . n 
A 1 309 ASN 309 309 ?   ?   ?   A . n 
A 1 310 ALA 310 310 ?   ?   ?   A . n 
A 1 311 TYR 311 311 ?   ?   ?   A . n 
A 1 312 ILE 312 312 ?   ?   ?   A . n 
A 1 313 GLN 313 313 ?   ?   ?   A . n 
A 1 314 LYS 314 314 ?   ?   ?   A . n 
A 1 315 TYR 315 315 ?   ?   ?   A . n 
A 1 316 LEU 316 316 ?   ?   ?   A . n 
A 1 317 LEU 317 317 ?   ?   ?   A . n 
A 1 318 VAL 318 318 212 VAL VAL A . n 
A 1 319 GLY 319 319 213 GLY GLY A . n 
A 1 320 ALA 320 320 214 ALA ALA A . n 
A 1 321 GLN 321 321 215 GLN GLN A . n 
A 1 322 ARG 322 322 216 ARG ARG A . n 
A 1 323 ARG 323 323 217 ARG ARG A . n 
A 1 324 ARG 324 324 218 ARG ARG A . n 
A 1 325 ARG 325 325 219 ARG ARG A . n 
A 1 326 ALA 326 326 220 ALA ALA A . n 
A 1 327 VAL 327 327 221 VAL VAL A . n 
A 1 328 GLY 328 328 222 GLY GLY A . n 
A 1 329 LEU 329 329 223 LEU LEU A . n 
A 1 330 ALA 330 330 224 ALA ALA A . n 
A 1 331 VAL 331 331 225 VAL VAL A . n 
A 1 332 VAL 332 332 226 VAL VAL A . n 
A 1 333 THR 333 333 227 THR THR A . n 
A 1 334 LEU 334 334 228 LEU LEU A . n 
A 1 335 LEU 335 335 229 LEU LEU A . n 
A 1 336 ASN 336 336 230 ASN ASN A . n 
A 1 337 PHE 337 337 231 PHE PHE A . n 
A 1 338 LEU 338 338 232 LEU LEU A . n 
A 1 339 VAL 339 339 233 VAL VAL A . n 
A 1 340 CYS 340 340 234 CYS CYS A . n 
A 1 341 PHE 341 341 235 PHE PHE A . n 
A 1 342 GLY 342 342 236 GLY GLY A . n 
A 1 343 PRO 343 343 237 PRO PRO A . n 
A 1 344 TYR 344 344 238 TYR TYR A . n 
A 1 345 ASN 345 345 239 ASN ASN A . n 
A 1 346 VAL 346 346 240 VAL VAL A . n 
A 1 347 SER 347 347 241 SER SER A . n 
A 1 348 HIS 348 348 242 HIS HIS A . n 
A 1 349 LEU 349 349 243 LEU LEU A . n 
A 1 350 VAL 350 350 244 VAL VAL A . n 
A 1 351 GLY 351 351 245 GLY GLY A . n 
A 1 352 TYR 352 352 246 TYR TYR A . n 
A 1 353 HIS 353 353 247 HIS HIS A . n 
A 1 354 GLN 354 354 248 GLN GLN A . n 
A 1 355 ARG 355 355 249 ARG ARG A . n 
A 1 356 LYS 356 356 250 LYS LYS A . n 
A 1 357 SER 357 357 251 SER SER A . n 
A 1 358 PRO 358 358 252 PRO PRO A . n 
A 1 359 TRP 359 359 253 TRP TRP A . n 
A 1 360 TRP 360 360 254 TRP TRP A . n 
A 1 361 ARG 361 361 255 ARG ARG A . n 
A 1 362 SER 362 362 256 SER SER A . n 
A 1 363 ILE 363 363 257 ILE ILE A . n 
A 1 364 ALA 364 364 258 ALA ALA A . n 
A 1 365 VAL 365 365 259 VAL VAL A . n 
A 1 366 VAL 366 366 260 VAL VAL A . n 
A 1 367 PHE 367 367 261 PHE PHE A . n 
A 1 368 SER 368 368 262 SER SER A . n 
A 1 369 SER 369 369 263 SER SER A . n 
A 1 370 LEU 370 370 264 LEU LEU A . n 
A 1 371 ASN 371 371 265 ASN ASN A . n 
A 1 372 ALA 372 372 266 ALA ALA A . n 
A 1 373 SER 373 373 267 SER SER A . n 
A 1 374 LEU 374 374 268 LEU LEU A . n 
A 1 375 ASP 375 375 269 ASP ASP A . n 
A 1 376 PRO 376 376 270 PRO PRO A . n 
A 1 377 LEU 377 377 271 LEU LEU A . n 
A 1 378 LEU 378 378 272 LEU LEU A . n 
A 1 379 PHE 379 379 273 PHE PHE A . n 
A 1 380 TYR 380 380 274 TYR TYR A . n 
A 1 381 PHE 381 381 275 PHE PHE A . n 
A 1 382 SER 382 382 276 SER SER A . n 
A 1 383 SER 383 383 277 SER SER A . n 
A 1 384 SER 384 384 278 SER SER A . n 
A 1 385 VAL 385 385 279 VAL VAL A . n 
A 1 386 VAL 386 386 280 VAL VAL A . n 
A 1 387 ARG 387 387 281 ARG ARG A . n 
A 1 388 ARG 388 388 282 ARG ARG A . n 
A 1 389 ALA 389 389 283 ALA ALA A . n 
A 1 390 PHE 390 390 284 PHE PHE A . n 
A 1 391 GLY 391 391 285 GLY GLY A . n 
A 1 392 ARG 392 392 286 ARG ARG A . n 
A 1 393 GLY 393 393 287 GLY GLY A . n 
A 1 394 LEU 394 394 288 LEU LEU A . n 
A 1 395 GLN 395 395 289 GLN GLN A . n 
A 1 396 VAL 396 396 290 VAL VAL A . n 
A 1 397 LEU 397 397 291 LEU LEU A . n 
A 1 398 ARG 398 398 ?   ?   ?   A . n 
A 1 399 ASN 399 399 ?   ?   ?   A . n 
A 1 400 GLN 400 400 ?   ?   ?   A . n 
A 1 401 GLY 401 401 ?   ?   ?   A . n 
A 1 402 SER 402 402 ?   ?   ?   A . n 
A 1 403 SER 403 403 ?   ?   ?   A . n 
A 1 404 LEU 404 404 ?   ?   ?   A . n 
A 1 405 LEU 405 405 ?   ?   ?   A . n 
A 1 406 GLY 406 406 ?   ?   ?   A . n 
A 1 407 ARG 407 407 ?   ?   ?   A . n 
A 1 408 ARG 408 408 ?   ?   ?   A . n 
A 1 409 GLY 409 409 ?   ?   ?   A . n 
A 1 410 LYS 410 410 ?   ?   ?   A . n 
A 1 411 ASP 411 411 ?   ?   ?   A . n 
A 1 412 THR 412 412 ?   ?   ?   A . n 
A 1 413 ALA 413 413 ?   ?   ?   A . n 
A 1 414 GLU 414 414 ?   ?   ?   A . n 
A 1 415 GLY 415 415 ?   ?   ?   A . n 
A 1 416 THR 416 416 ?   ?   ?   A . n 
A 1 417 ASN 417 417 ?   ?   ?   A . n 
A 1 418 GLU 418 418 ?   ?   ?   A . n 
A 1 419 ASP 419 419 ?   ?   ?   A . n 
A 1 420 ARG 420 420 ?   ?   ?   A . n 
A 1 421 GLY 421 421 ?   ?   ?   A . n 
A 1 422 VAL 422 422 ?   ?   ?   A . n 
A 1 423 GLY 423 423 ?   ?   ?   A . n 
A 1 424 GLN 424 424 ?   ?   ?   A . n 
A 1 425 GLY 425 425 ?   ?   ?   A . n 
A 1 426 GLU 426 426 ?   ?   ?   A . n 
A 1 427 GLY 427 427 ?   ?   ?   A . n 
A 1 428 MET 428 428 ?   ?   ?   A . n 
A 1 429 PRO 429 429 ?   ?   ?   A . n 
A 1 430 SER 430 430 ?   ?   ?   A . n 
A 1 431 SER 431 431 ?   ?   ?   A . n 
A 1 432 ASP 432 432 ?   ?   ?   A . n 
A 1 433 PHE 433 433 ?   ?   ?   A . n 
A 1 434 THR 434 434 ?   ?   ?   A . n 
A 1 435 THR 435 435 ?   ?   ?   A . n 
A 1 436 GLU 436 436 ?   ?   ?   A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1LYD 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1LYD 
_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          A1LYD 
_pdbx_nonpoly_scheme.ndb_seq_num     1 
_pdbx_nonpoly_scheme.pdb_seq_num     501 
_pdbx_nonpoly_scheme.auth_seq_num    502 
_pdbx_nonpoly_scheme.pdb_mon_id      A1LYD 
_pdbx_nonpoly_scheme.auth_mon_id     GLP 
_pdbx_nonpoly_scheme.pdb_strand_id   A 
_pdbx_nonpoly_scheme.pdb_ins_code    . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A ARG 35  ? CG  ? A ARG 35  CG  
2  1 Y 1 A ARG 35  ? CD  ? A ARG 35  CD  
3  1 Y 1 A ARG 35  ? NE  ? A ARG 35  NE  
4  1 Y 1 A ARG 35  ? CZ  ? A ARG 35  CZ  
5  1 Y 1 A ARG 35  ? NH1 ? A ARG 35  NH1 
6  1 Y 1 A ARG 35  ? NH2 ? A ARG 35  NH2 
7  1 Y 1 A PHE 73  ? CG  ? A PHE 73  CG  
8  1 Y 1 A PHE 73  ? CD1 ? A PHE 73  CD1 
9  1 Y 1 A PHE 73  ? CD2 ? A PHE 73  CD2 
10 1 Y 1 A PHE 73  ? CE1 ? A PHE 73  CE1 
11 1 Y 1 A PHE 73  ? CE2 ? A PHE 73  CE2 
12 1 Y 1 A PHE 73  ? CZ  ? A PHE 73  CZ  
13 1 Y 1 A ARG 74  ? CG  ? A ARG 74  CG  
14 1 Y 1 A ARG 74  ? CD  ? A ARG 74  CD  
15 1 Y 1 A ARG 74  ? NE  ? A ARG 74  NE  
16 1 Y 1 A ARG 74  ? CZ  ? A ARG 74  CZ  
17 1 Y 1 A ARG 74  ? NH1 ? A ARG 74  NH1 
18 1 Y 1 A ARG 74  ? NH2 ? A ARG 74  NH2 
19 1 Y 1 A TYR 76  ? CG  ? A TYR 76  CG  
20 1 Y 1 A TYR 76  ? CD1 ? A TYR 76  CD1 
21 1 Y 1 A TYR 76  ? CD2 ? A TYR 76  CD2 
22 1 Y 1 A TYR 76  ? CE1 ? A TYR 76  CE1 
23 1 Y 1 A TYR 76  ? CE2 ? A TYR 76  CE2 
24 1 Y 1 A TYR 76  ? CZ  ? A TYR 76  CZ  
25 1 Y 1 A TYR 76  ? OH  ? A TYR 76  OH  
26 1 Y 1 A LYS 79  ? CG  ? A LYS 79  CG  
27 1 Y 1 A LYS 79  ? CD  ? A LYS 79  CD  
28 1 Y 1 A LYS 79  ? CE  ? A LYS 79  CE  
29 1 Y 1 A LYS 79  ? NZ  ? A LYS 79  NZ  
30 1 Y 1 A LYS 118 ? CG  ? A LYS 118 CG  
31 1 Y 1 A LYS 118 ? CD  ? A LYS 118 CD  
32 1 Y 1 A LYS 118 ? CE  ? A LYS 118 CE  
33 1 Y 1 A LYS 118 ? NZ  ? A LYS 118 NZ  
34 1 Y 1 A ARG 121 ? CG  ? A ARG 121 CG  
35 1 Y 1 A ARG 121 ? CD  ? A ARG 121 CD  
36 1 Y 1 A ARG 121 ? NE  ? A ARG 121 NE  
37 1 Y 1 A ARG 121 ? CZ  ? A ARG 121 CZ  
38 1 Y 1 A ARG 121 ? NH1 ? A ARG 121 NH1 
39 1 Y 1 A ARG 121 ? NH2 ? A ARG 121 NH2 
40 1 Y 1 A ARG 122 ? CG  ? A ARG 122 CG  
41 1 Y 1 A ARG 122 ? CD  ? A ARG 122 CD  
42 1 Y 1 A ARG 122 ? NE  ? A ARG 122 NE  
43 1 Y 1 A ARG 122 ? CZ  ? A ARG 122 CZ  
44 1 Y 1 A ARG 122 ? NH1 ? A ARG 122 NH1 
45 1 Y 1 A ARG 122 ? NH2 ? A ARG 122 NH2 
46 1 Y 1 A ASN 160 ? CG  ? A ASN 160 CG  
47 1 Y 1 A ASN 160 ? OD1 ? A ASN 160 OD1 
48 1 Y 1 A ASN 160 ? ND2 ? A ASN 160 ND2 
49 1 Y 1 A GLU 161 ? CG  ? A GLU 161 CG  
50 1 Y 1 A GLU 161 ? CD  ? A GLU 161 CD  
51 1 Y 1 A GLU 161 ? OE1 ? A GLU 161 OE1 
52 1 Y 1 A GLU 161 ? OE2 ? A GLU 161 OE2 
53 1 Y 1 A ILE 162 ? CG1 ? A ILE 162 CG1 
54 1 Y 1 A ILE 162 ? CG2 ? A ILE 162 CG2 
55 1 Y 1 A ILE 162 ? CD1 ? A ILE 162 CD1 
56 1 Y 1 A ARG 387 ? CG  ? A ARG 387 CG  
57 1 Y 1 A ARG 387 ? CD  ? A ARG 387 CD  
58 1 Y 1 A ARG 387 ? NE  ? A ARG 387 NE  
59 1 Y 1 A ARG 387 ? CZ  ? A ARG 387 CZ  
60 1 Y 1 A ARG 387 ? NH1 ? A ARG 387 NH1 
61 1 Y 1 A ARG 387 ? NH2 ? A ARG 387 NH2 
62 1 Y 1 A ARG 388 ? CG  ? A ARG 388 CG  
63 1 Y 1 A ARG 388 ? CD  ? A ARG 388 CD  
64 1 Y 1 A ARG 388 ? NE  ? A ARG 388 NE  
65 1 Y 1 A ARG 388 ? CZ  ? A ARG 388 CZ  
66 1 Y 1 A ARG 388 ? NH1 ? A ARG 388 NH1 
67 1 Y 1 A ARG 388 ? NH2 ? A ARG 388 NH2 
68 1 Y 1 A ARG 392 ? CG  ? A ARG 392 CG  
69 1 Y 1 A ARG 392 ? CD  ? A ARG 392 CD  
70 1 Y 1 A ARG 392 ? NE  ? A ARG 392 NE  
71 1 Y 1 A ARG 392 ? CZ  ? A ARG 392 CZ  
72 1 Y 1 A ARG 392 ? NH1 ? A ARG 392 NH1 
73 1 Y 1 A ARG 392 ? NH2 ? A ARG 392 NH2 
74 1 Y 1 A GLN 395 ? CG  ? A GLN 395 CG  
75 1 Y 1 A GLN 395 ? CD  ? A GLN 395 CD  
76 1 Y 1 A GLN 395 ? OE1 ? A GLN 395 OE1 
77 1 Y 1 A GLN 395 ? NE2 ? A GLN 395 NE2 
78 1 Y 1 A LEU 397 ? CG  ? A LEU 397 CG  
79 1 Y 1 A LEU 397 ? CD1 ? A LEU 397 CD1 
80 1 Y 1 A LEU 397 ? CD2 ? A LEU 397 CD2 
# 
_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                     8Y6Y 
_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                         8Y6Y 
_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                   8Y6Y 
_exptl.crystals_number            ? 
_exptl.details                    ? 
_exptl.method                     'ELECTRON MICROSCOPY' 
_exptl.method_details             ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 8Y6Y 
_refine.pdbx_refine_id                           'ELECTRON MICROSCOPY' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            3.36 
_refine.ls_d_res_low                             ? 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     ? 
_refine.ls_number_reflns_R_free                  ? 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    ? 
_refine.ls_percent_reflns_R_free                 ? 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          ? 
_refine.ls_R_factor_R_free                       ? 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       ? 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    ? 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               ? 
_refine.pdbx_method_to_determine_struct          ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           ? 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_struct.entry_id                     8Y6Y 
_struct.title                        'GLPG0974-bound human FFA2' 
_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        8Y6Y 
_struct_keywords.text            'GPCR, 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 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP FFAR2_HUMAN O15552 ? 1 
;MLPDWKSSLILMAYIIIFLTGLPANLLALRAFVGRIRQPQPAPVHILLLSLTLADLLLLLLLPFKIIEAASNFRWYLPKV
VCALTSFGFYSSIYCSTWLLAGISIERYLGVAFPVQYKLSRRPLYGVIAALVAWVMSFGHCTIVIIVQYLNTTEQVRSGN
EITCYENFTDNQLDVVLPVRLELCLVLFFIPMAVTIFCYWRFVWIMLSQP
;
1   
2 UNP C562_ECOLX  P0ABE7 ? 1 
;ADLEDNMETLNDNLKVIEKADNAAQVKDALTKMRAAALDAQKATPPKLEDKSPDSPEMKDFRHGFDILVGQIDDALKLAN
EGKVKEAQAAAEQLKTTRNAYHQKY
;
23  
3 UNP FFAR2_HUMAN O15552 ? 1 
;LVGAQRRRRAVGLAVVTLLNFLVCFGPYNVSHLVGYHQRKSPWWRSIAVVFSSLNASLDPLLFYFSSSVVRRAFGRGLQV
LRNQGSSLLGRRGKDTAEGTNEDRGVGQGEGMPSSDFTTE
;
211 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 8Y6Y A 1   ? 210 ? O15552 1   ? 210 ? 1 ?   
2 2 8Y6Y A 211 ? 315 ? P0ABE7 23  ? 127 ? ? ?   
3 3 8Y6Y A 317 ? 436 ? O15552 211 ? 330 ? ? 436 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
2 8Y6Y TRP A 217 ? UNP P0ABE7 MET 29  conflict ? 1 
2 8Y6Y ILE A 312 ? UNP P0ABE7 HIS 124 conflict ? 2 
2 8Y6Y LEU A 316 ? UNP P0ABE7 ?   ?   linker   ? 3 
# 
_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 ASP A 4   ? ARG A 37  ? ASP A 4   ARG A 37  1 ? 34 
HELX_P HELX_P2  AA2 ALA A 42  ? LEU A 62  ? ALA A 42  LEU A 62  1 ? 21 
HELX_P HELX_P3  AA3 LEU A 62  ? SER A 71  ? LEU A 62  SER A 71  1 ? 10 
HELX_P HELX_P4  AA4 PRO A 78  ? ALA A 112 ? PRO A 78  ALA A 112 1 ? 35 
HELX_P HELX_P5  AA5 PHE A 113 ? SER A 120 ? PHE A 113 SER A 120 1 ? 8  
HELX_P HELX_P6  AA6 PRO A 123 ? TYR A 149 ? PRO A 123 TYR A 149 1 ? 27 
HELX_P HELX_P7  AA7 THR A 169 ? LEU A 187 ? THR A 169 LEU A 187 1 ? 19 
HELX_P HELX_P8  AA8 PHE A 188 ? SER A 208 ? PHE A 188 SER A 208 1 ? 21 
HELX_P HELX_P9  AA9 GLY A 319 ? CYS A 340 ? GLY A 319 CYS A 340 1 ? 22 
HELX_P HELX_P10 AB1 PHE A 341 ? ARG A 355 ? PHE A 341 ARG A 355 1 ? 15 
HELX_P HELX_P11 AB2 TRP A 360 ? SER A 383 ? TRP A 360 SER A 383 1 ? 24 
HELX_P HELX_P12 AB3 SER A 383 ? LEU A 397 ? SER A 383 LEU A 397 1 ? 15 
# 
_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            82 
_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            164 
_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             82 
_struct_conn.ptnr2_auth_asym_id            A 
_struct_conn.ptnr2_auth_comp_id            CYS 
_struct_conn.ptnr2_auth_seq_id             164 
_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               2.036 
_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                       82 
_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      164 
_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                        82 
_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       164 
_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' 
# 
_pdbx_entry_details.entry_id                   8Y6Y 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ARG A 37  ? ? 49.74   -103.86 
2 1 PRO A 39  ? ? -34.58  118.85  
3 1 GLU A 166 ? ? -117.05 66.66   
4 1 PHE A 168 ? ? 51.73   -134.06 
5 1 PHE A 188 ? ? -138.35 -61.27  
# 
_em_3d_fitting.id                1 
_em_3d_fitting.entry_id          8Y6Y 
_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                    8Y6Y 
_em_3d_reconstruction.id                          1 
_em_3d_reconstruction.method                      ? 
_em_3d_reconstruction.algorithm                   ? 
_em_3d_reconstruction.citation_id                 ? 
_em_3d_reconstruction.details                     ? 
_em_3d_reconstruction.resolution                  3.36 
_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               76538 
_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                 'GLPG0974-bound human FFA2' 
_em_entity_assembly.details              ? 
_em_entity_assembly.synonym              ? 
_em_entity_assembly.oligomeric_details   ? 
_em_entity_assembly.entity_id_list       1 
# 
_em_imaging.entry_id                        8Y6Y 
_em_imaging.id                              1 
_em_imaging.astigmatism                     ? 
_em_imaging.electron_beam_tilt_params       ? 
_em_imaging.residual_tilt                   ? 
_em_imaging.microscope_model                'TFS KRIOS' 
_em_imaging.specimen_holder_type            ? 
_em_imaging.specimen_holder_model           ? 
_em_imaging.details                         ? 
_em_imaging.date                            ? 
_em_imaging.accelerating_voltage            300 
_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             1600 
_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             ? 
_em_imaging.c2_aperture_diameter            ? 
_em_imaging.specimen_id                     1 
_em_imaging.cryogen                         ? 
# 
_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   300 
_em_sample_support.grid_type        'Quantifoil R1.2/1.3' 
_em_sample_support.details          ? 
_em_sample_support.specimen_id      1 
_em_sample_support.citation_id      ? 
# 
_em_vitrification.entry_id              8Y6Y 
_em_vitrification.id                    1 
_em_vitrification.specimen_id           1 
_em_vitrification.cryogen_name          ETHANE 
_em_vitrification.humidity              100 
_em_vitrification.temp                  ? 
_em_vitrification.chamber_temperature   277 
_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                8Y6Y 
_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 MET 1   ? A MET 1   
2   1 Y 1 A LEU 2   ? A LEU 2   
3   1 Y 1 A PRO 3   ? A PRO 3   
4   1 Y 1 A ASN 151 ? A ASN 151 
5   1 Y 1 A THR 152 ? A THR 152 
6   1 Y 1 A THR 153 ? A THR 153 
7   1 Y 1 A GLU 154 ? A GLU 154 
8   1 Y 1 A GLN 155 ? A GLN 155 
9   1 Y 1 A VAL 156 ? A VAL 156 
10  1 Y 1 A ARG 157 ? A ARG 157 
11  1 Y 1 A GLN 209 ? A GLN 209 
12  1 Y 1 A PRO 210 ? A PRO 210 
13  1 Y 1 A ALA 211 ? A ALA 211 
14  1 Y 1 A ASP 212 ? A ASP 212 
15  1 Y 1 A LEU 213 ? A LEU 213 
16  1 Y 1 A GLU 214 ? A GLU 214 
17  1 Y 1 A ASP 215 ? A ASP 215 
18  1 Y 1 A ASN 216 ? A ASN 216 
19  1 Y 1 A TRP 217 ? A TRP 217 
20  1 Y 1 A GLU 218 ? A GLU 218 
21  1 Y 1 A THR 219 ? A THR 219 
22  1 Y 1 A LEU 220 ? A LEU 220 
23  1 Y 1 A ASN 221 ? A ASN 221 
24  1 Y 1 A ASP 222 ? A ASP 222 
25  1 Y 1 A ASN 223 ? A ASN 223 
26  1 Y 1 A LEU 224 ? A LEU 224 
27  1 Y 1 A LYS 225 ? A LYS 225 
28  1 Y 1 A VAL 226 ? A VAL 226 
29  1 Y 1 A ILE 227 ? A ILE 227 
30  1 Y 1 A GLU 228 ? A GLU 228 
31  1 Y 1 A LYS 229 ? A LYS 229 
32  1 Y 1 A ALA 230 ? A ALA 230 
33  1 Y 1 A ASP 231 ? A ASP 231 
34  1 Y 1 A ASN 232 ? A ASN 232 
35  1 Y 1 A ALA 233 ? A ALA 233 
36  1 Y 1 A ALA 234 ? A ALA 234 
37  1 Y 1 A GLN 235 ? A GLN 235 
38  1 Y 1 A VAL 236 ? A VAL 236 
39  1 Y 1 A LYS 237 ? A LYS 237 
40  1 Y 1 A ASP 238 ? A ASP 238 
41  1 Y 1 A ALA 239 ? A ALA 239 
42  1 Y 1 A LEU 240 ? A LEU 240 
43  1 Y 1 A THR 241 ? A THR 241 
44  1 Y 1 A LYS 242 ? A LYS 242 
45  1 Y 1 A MET 243 ? A MET 243 
46  1 Y 1 A ARG 244 ? A ARG 244 
47  1 Y 1 A ALA 245 ? A ALA 245 
48  1 Y 1 A ALA 246 ? A ALA 246 
49  1 Y 1 A ALA 247 ? A ALA 247 
50  1 Y 1 A LEU 248 ? A LEU 248 
51  1 Y 1 A ASP 249 ? A ASP 249 
52  1 Y 1 A ALA 250 ? A ALA 250 
53  1 Y 1 A GLN 251 ? A GLN 251 
54  1 Y 1 A LYS 252 ? A LYS 252 
55  1 Y 1 A ALA 253 ? A ALA 253 
56  1 Y 1 A THR 254 ? A THR 254 
57  1 Y 1 A PRO 255 ? A PRO 255 
58  1 Y 1 A PRO 256 ? A PRO 256 
59  1 Y 1 A LYS 257 ? A LYS 257 
60  1 Y 1 A LEU 258 ? A LEU 258 
61  1 Y 1 A GLU 259 ? A GLU 259 
62  1 Y 1 A ASP 260 ? A ASP 260 
63  1 Y 1 A LYS 261 ? A LYS 261 
64  1 Y 1 A SER 262 ? A SER 262 
65  1 Y 1 A PRO 263 ? A PRO 263 
66  1 Y 1 A ASP 264 ? A ASP 264 
67  1 Y 1 A SER 265 ? A SER 265 
68  1 Y 1 A PRO 266 ? A PRO 266 
69  1 Y 1 A GLU 267 ? A GLU 267 
70  1 Y 1 A MET 268 ? A MET 268 
71  1 Y 1 A LYS 269 ? A LYS 269 
72  1 Y 1 A ASP 270 ? A ASP 270 
73  1 Y 1 A PHE 271 ? A PHE 271 
74  1 Y 1 A ARG 272 ? A ARG 272 
75  1 Y 1 A HIS 273 ? A HIS 273 
76  1 Y 1 A GLY 274 ? A GLY 274 
77  1 Y 1 A PHE 275 ? A PHE 275 
78  1 Y 1 A ASP 276 ? A ASP 276 
79  1 Y 1 A ILE 277 ? A ILE 277 
80  1 Y 1 A LEU 278 ? A LEU 278 
81  1 Y 1 A VAL 279 ? A VAL 279 
82  1 Y 1 A GLY 280 ? A GLY 280 
83  1 Y 1 A GLN 281 ? A GLN 281 
84  1 Y 1 A ILE 282 ? A ILE 282 
85  1 Y 1 A ASP 283 ? A ASP 283 
86  1 Y 1 A ASP 284 ? A ASP 284 
87  1 Y 1 A ALA 285 ? A ALA 285 
88  1 Y 1 A LEU 286 ? A LEU 286 
89  1 Y 1 A LYS 287 ? A LYS 287 
90  1 Y 1 A LEU 288 ? A LEU 288 
91  1 Y 1 A ALA 289 ? A ALA 289 
92  1 Y 1 A ASN 290 ? A ASN 290 
93  1 Y 1 A GLU 291 ? A GLU 291 
94  1 Y 1 A GLY 292 ? A GLY 292 
95  1 Y 1 A LYS 293 ? A LYS 293 
96  1 Y 1 A VAL 294 ? A VAL 294 
97  1 Y 1 A LYS 295 ? A LYS 295 
98  1 Y 1 A GLU 296 ? A GLU 296 
99  1 Y 1 A ALA 297 ? A ALA 297 
100 1 Y 1 A GLN 298 ? A GLN 298 
101 1 Y 1 A ALA 299 ? A ALA 299 
102 1 Y 1 A ALA 300 ? A ALA 300 
103 1 Y 1 A ALA 301 ? A ALA 301 
104 1 Y 1 A GLU 302 ? A GLU 302 
105 1 Y 1 A GLN 303 ? A GLN 303 
106 1 Y 1 A LEU 304 ? A LEU 304 
107 1 Y 1 A LYS 305 ? A LYS 305 
108 1 Y 1 A THR 306 ? A THR 306 
109 1 Y 1 A THR 307 ? A THR 307 
110 1 Y 1 A ARG 308 ? A ARG 308 
111 1 Y 1 A ASN 309 ? A ASN 309 
112 1 Y 1 A ALA 310 ? A ALA 310 
113 1 Y 1 A TYR 311 ? A TYR 311 
114 1 Y 1 A ILE 312 ? A ILE 312 
115 1 Y 1 A GLN 313 ? A GLN 313 
116 1 Y 1 A LYS 314 ? A LYS 314 
117 1 Y 1 A TYR 315 ? A TYR 315 
118 1 Y 1 A LEU 316 ? A LEU 316 
119 1 Y 1 A LEU 317 ? A LEU 317 
120 1 Y 1 A ARG 398 ? A ARG 398 
121 1 Y 1 A ASN 399 ? A ASN 399 
122 1 Y 1 A GLN 400 ? A GLN 400 
123 1 Y 1 A GLY 401 ? A GLY 401 
124 1 Y 1 A SER 402 ? A SER 402 
125 1 Y 1 A SER 403 ? A SER 403 
126 1 Y 1 A LEU 404 ? A LEU 404 
127 1 Y 1 A LEU 405 ? A LEU 405 
128 1 Y 1 A GLY 406 ? A GLY 406 
129 1 Y 1 A ARG 407 ? A ARG 407 
130 1 Y 1 A ARG 408 ? A ARG 408 
131 1 Y 1 A GLY 409 ? A GLY 409 
132 1 Y 1 A LYS 410 ? A LYS 410 
133 1 Y 1 A ASP 411 ? A ASP 411 
134 1 Y 1 A THR 412 ? A THR 412 
135 1 Y 1 A ALA 413 ? A ALA 413 
136 1 Y 1 A GLU 414 ? A GLU 414 
137 1 Y 1 A GLY 415 ? A GLY 415 
138 1 Y 1 A THR 416 ? A THR 416 
139 1 Y 1 A ASN 417 ? A ASN 417 
140 1 Y 1 A GLU 418 ? A GLU 418 
141 1 Y 1 A ASP 419 ? A ASP 419 
142 1 Y 1 A ARG 420 ? A ARG 420 
143 1 Y 1 A GLY 421 ? A GLY 421 
144 1 Y 1 A VAL 422 ? A VAL 422 
145 1 Y 1 A GLY 423 ? A GLY 423 
146 1 Y 1 A GLN 424 ? A GLN 424 
147 1 Y 1 A GLY 425 ? A GLY 425 
148 1 Y 1 A GLU 426 ? A GLU 426 
149 1 Y 1 A GLY 427 ? A GLY 427 
150 1 Y 1 A MET 428 ? A MET 428 
151 1 Y 1 A PRO 429 ? A PRO 429 
152 1 Y 1 A SER 430 ? A SER 430 
153 1 Y 1 A SER 431 ? A SER 431 
154 1 Y 1 A ASP 432 ? A ASP 432 
155 1 Y 1 A PHE 433 ? A PHE 433 
156 1 Y 1 A THR 434 ? A THR 434 
157 1 Y 1 A THR 435 ? A THR 435 
158 1 Y 1 A GLU 436 ? A GLU 436 
# 
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 
A1LYD C1   C  N R 1   
A1LYD C2   C  N N 2   
A1LYD C3   C  N N 3   
A1LYD C4   C  N N 4   
A1LYD C5   C  N N 5   
A1LYD C6   C  N N 6   
A1LYD O1   O  N N 7   
A1LYD N2   N  N N 8   
A1LYD O3   O  N N 9   
A1LYD O4   O  N N 10  
A1LYD CL1  CL N N 11  
A1LYD S1   S  Y N 12  
A1LYD O2   O  N N 13  
A1LYD N1   N  N N 14  
A1LYD C7   C  N N 15  
A1LYD C8   C  N N 16  
A1LYD C9   C  Y N 17  
A1LYD C10  C  N N 18  
A1LYD C11  C  Y N 19  
A1LYD C12  C  Y N 20  
A1LYD C13  C  Y N 21  
A1LYD C14  C  N N 22  
A1LYD C15  C  Y N 23  
A1LYD C16  C  Y N 24  
A1LYD C17  C  Y N 25  
A1LYD C18  C  Y N 26  
A1LYD C19  C  Y N 27  
A1LYD C20  C  N N 28  
A1LYD C21  C  Y N 29  
A1LYD C22  C  Y N 30  
A1LYD C23  C  Y N 31  
A1LYD C24  C  Y N 32  
A1LYD C25  C  Y N 33  
A1LYD H1   H  N N 34  
A1LYD H2   H  N N 35  
A1LYD H3   H  N N 36  
A1LYD H4   H  N N 37  
A1LYD H5   H  N N 38  
A1LYD H6   H  N N 39  
A1LYD H7   H  N N 40  
A1LYD H8   H  N N 41  
A1LYD H9   H  N N 42  
A1LYD H10  H  N N 43  
A1LYD H11  H  N N 44  
A1LYD H12  H  N N 45  
A1LYD H13  H  N N 46  
A1LYD H14  H  N N 47  
A1LYD H15  H  N N 48  
A1LYD H16  H  N N 49  
A1LYD H17  H  N N 50  
A1LYD H18  H  N N 51  
A1LYD H19  H  N N 52  
A1LYD H20  H  N N 53  
A1LYD H21  H  N N 54  
A1LYD H22  H  N N 55  
A1LYD H23  H  N N 56  
A1LYD H24  H  N N 57  
A1LYD H25  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 
A1LYD CL1 C23  sing N N 1   
A1LYD C23 C17  doub Y N 2   
A1LYD C23 C25  sing Y N 3   
A1LYD C17 C12  sing Y N 4   
A1LYD C25 C24  doub Y N 5   
A1LYD C12 C8   sing N N 6   
A1LYD C12 C18  doub Y N 7   
A1LYD C8  N2   sing N N 8   
A1LYD C24 C18  sing Y N 9   
A1LYD C14 C10  sing N N 10  
A1LYD C14 C20  sing N N 11  
A1LYD C10 C7   sing N N 12  
A1LYD C7  N2   sing N N 13  
A1LYD N2  C4   sing N N 14  
A1LYD C20 O4   doub N N 15  
A1LYD C20 O3   sing N N 16  
A1LYD C4  O1   doub N N 17  
A1LYD C4  C1   sing N N 18  
A1LYD S1  C13  sing Y N 19  
A1LYD S1  C15  sing Y N 20  
A1LYD C1  C5   sing N N 21  
A1LYD C1  C2   sing N N 22  
A1LYD C1  N1   sing N N 23  
A1LYD C13 C9   doub Y N 24  
A1LYD C2  C3   sing N N 25  
A1LYD N1  C3   sing N N 26  
A1LYD N1  C6   sing N N 27  
A1LYD C15 C19  doub Y N 28  
A1LYD C15 C11  sing Y N 29  
A1LYD C9  C6   sing N N 30  
A1LYD C9  C11  sing Y N 31  
A1LYD C19 C22  sing Y N 32  
A1LYD C6  O2   doub N N 33  
A1LYD C11 C16  doub Y N 34  
A1LYD C22 C21  doub Y N 35  
A1LYD C16 C21  sing Y N 36  
A1LYD C2  H1   sing N N 37  
A1LYD C2  H2   sing N N 38  
A1LYD C3  H3   sing N N 39  
A1LYD C3  H4   sing N N 40  
A1LYD C5  H5   sing N N 41  
A1LYD C5  H6   sing N N 42  
A1LYD C5  H7   sing N N 43  
A1LYD O3  H8   sing N N 44  
A1LYD C7  H9   sing N N 45  
A1LYD C7  H10  sing N N 46  
A1LYD C8  H11  sing N N 47  
A1LYD C8  H12  sing N N 48  
A1LYD C10 H13  sing N N 49  
A1LYD C10 H14  sing N N 50  
A1LYD C13 H15  sing N N 51  
A1LYD C14 H16  sing N N 52  
A1LYD C14 H17  sing N N 53  
A1LYD C16 H18  sing N N 54  
A1LYD C17 H19  sing N N 55  
A1LYD C18 H20  sing N N 56  
A1LYD C19 H21  sing N N 57  
A1LYD C21 H22  sing N N 58  
A1LYD C22 H23  sing N N 59  
A1LYD C24 H24  sing N N 60  
A1LYD C25 H25  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    2024-02-03 
_em_admin.deposition_site    PDBJ 
_em_admin.entry_id           8Y6Y 
_em_admin.last_update        2025-04-09 
_em_admin.map_release_date   2025-04-02 
_em_admin.title              'GLPG0974-bound human FFA2' 
# 
_em_ctf_correction.details                  ? 
_em_ctf_correction.em_image_processing_id   1 
_em_ctf_correction.id                       1 
_em_ctf_correction.type                     'PHASE FLIPPING AND AMPLITUDE CORRECTION' 
# 
_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                ? 
_em_entity_assembly_molwt.value                ? 
# 
_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          9606 
_em_entity_assembly_naturalsource.organism             'Homo sapiens' 
_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          9606 
_em_entity_assembly_recombinant.organism             'Homo sapiens' 
_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         45.589 
_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                     ? 
# 
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 ? ? ? ? 
'IMAGE ACQUISITION'             ? 2  ? ? 1 ? ? 
MASKING                         ? 3  ? ? ? ? ? 
'CTF CORRECTION'                ? 4  1 ? ? ? ? 
'LAYERLINE INDEXING'            ? 5  ? ? ? ? ? 
'DIFFRACTION INDEXING'          ? 6  ? ? ? ? ? 
'MODEL FITTING'                 ? 7  ? ? ? ? ? 
'MODEL REFINEMENT'              ? 8  ? ? ? ? ? 
OTHER                           ? 9  ? ? ? ? ? 
'INITIAL EULER ASSIGNMENT'      ? 10 1 ? ? ? ? 
'FINAL EULER ASSIGNMENT'        ? 11 1 ? ? ? ? 
CLASSIFICATION                  ? 12 1 ? ? ? ? 
RECONSTRUCTION                  ? 13 1 ? ? ? ? 
'VOLUME SELECTION'              ? 14 1 1 1 ? ? 
'SERIES ALIGNMENT'              ? 15 1 1 1 ? ? 
'MOLECULAR REPLACEMENT'         ? 16 1 1 1 ? ? 
'LATTICE DISTORTION CORRECTION' ? 17 1 1 1 ? ? 
'SYMMETRY DETERMINATION'        ? 18 1 1 1 ? ? 
'CRYSTALLOGRAPHY MERGING'       ? 19 1 1 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 
'Japan Society for the Promotion of Science (JSPS)' Japan 21H05142 1 
'Japan Society for the Promotion of Science (JSPS)' Japan 21H04791 2 
# 
_atom_sites.entry_id                    8Y6Y 
_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  
CL 
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   . ASP   A 1 4   ? 103.912 138.173 98.073  1.00 41.01 ? 4   ASP   A N   1 
ATOM   2    C  CA  . ASP   A 1 4   ? 104.767 139.376 97.854  1.00 41.02 ? 4   ASP   A CA  1 
ATOM   3    C  C   . ASP   A 1 4   ? 105.338 139.821 99.200  1.00 41.03 ? 4   ASP   A C   1 
ATOM   4    O  O   . ASP   A 1 4   ? 106.505 139.556 99.490  1.00 40.99 ? 4   ASP   A O   1 
ATOM   5    C  CB  . ASP   A 1 4   ? 104.008 140.457 97.096  1.00 41.04 ? 4   ASP   A CB  1 
ATOM   6    C  CG  . ASP   A 1 4   ? 104.738 141.783 96.924  1.00 41.04 ? 4   ASP   A CG  1 
ATOM   7    O  OD1 . ASP   A 1 4   ? 105.797 141.789 96.261  1.00 41.03 ? 4   ASP   A OD1 1 
ATOM   8    O  OD2 . ASP   A 1 4   ? 104.241 142.798 97.456  1.00 41.04 ? 4   ASP   A OD2 1 
ATOM   9    N  N   . TRP   A 1 5   ? 104.502 140.470 100.025 1.00 41.04 ? 5   TRP   A N   1 
ATOM   10   C  CA  . TRP   A 1 5   ? 104.898 140.898 101.359 1.00 41.05 ? 5   TRP   A CA  1 
ATOM   11   C  C   . TRP   A 1 5   ? 105.163 139.675 102.235 1.00 41.00 ? 5   TRP   A C   1 
ATOM   12   O  O   . TRP   A 1 5   ? 106.038 139.711 103.100 1.00 40.97 ? 5   TRP   A O   1 
ATOM   13   C  CB  . TRP   A 1 5   ? 103.821 141.805 101.973 1.00 41.08 ? 5   TRP   A CB  1 
ATOM   14   C  CG  . TRP   A 1 5   ? 104.144 142.294 103.361 1.00 41.12 ? 5   TRP   A CG  1 
ATOM   15   C  CD1 . TRP   A 1 5   ? 103.648 141.812 104.536 1.00 41.13 ? 5   TRP   A CD1 1 
ATOM   16   C  CD2 . TRP   A 1 5   ? 105.051 143.362 103.716 1.00 41.14 ? 5   TRP   A CD2 1 
ATOM   17   N  NE1 . TRP   A 1 5   ? 104.172 142.504 105.595 1.00 41.13 ? 5   TRP   A NE1 1 
ATOM   18   C  CE2 . TRP   A 1 5   ? 105.036 143.459 105.126 1.00 41.14 ? 5   TRP   A CE2 1 
ATOM   19   C  CE3 . TRP   A 1 5   ? 105.866 144.238 102.989 1.00 41.14 ? 5   TRP   A CE3 1 
ATOM   20   C  CZ2 . TRP   A 1 5   ? 105.804 144.396 105.815 1.00 41.15 ? 5   TRP   A CZ2 1 
ATOM   21   C  CZ3 . TRP   A 1 5   ? 106.625 145.164 103.672 1.00 41.15 ? 5   TRP   A CZ3 1 
ATOM   22   C  CH2 . TRP   A 1 5   ? 106.593 145.240 105.066 1.00 41.15 ? 5   TRP   A CH2 1 
ATOM   23   N  N   . LYS   A 1 6   ? 104.405 138.597 101.984 1.00 40.97 ? 6   LYS   A N   1 
ATOM   24   C  CA  . LYS   A 1 6   ? 104.583 137.327 102.674 1.00 40.95 ? 6   LYS   A CA  1 
ATOM   25   C  C   . LYS   A 1 6   ? 106.018 136.840 102.468 1.00 40.95 ? 6   LYS   A C   1 
ATOM   26   O  O   . LYS   A 1 6   ? 106.641 136.343 103.405 1.00 40.94 ? 6   LYS   A O   1 
ATOM   27   C  CB  . LYS   A 1 6   ? 103.609 136.238 102.196 1.00 40.95 ? 6   LYS   A CB  1 
ATOM   28   C  CG  . LYS   A 1 6   ? 102.152 136.633 101.925 1.00 40.95 ? 6   LYS   A CG  1 
ATOM   29   C  CD  . LYS   A 1 6   ? 101.402 137.326 103.060 1.00 40.95 ? 6   LYS   A CD  1 
ATOM   30   C  CE  . LYS   A 1 6   ? 100.003 137.722 102.680 1.00 40.94 ? 6   LYS   A CE  1 
ATOM   31   N  NZ  . LYS   A 1 6   ? 99.319  138.475 103.737 1.00 40.94 ? 6   LYS   A NZ  1 
ATOM   32   N  N   . SER   A 1 7   ? 106.526 136.989 101.236 1.00 40.96 ? 7   SER   A N   1 
ATOM   33   C  CA  . SER   A 1 7   ? 107.886 136.596 100.896 1.00 40.97 ? 7   SER   A CA  1 
ATOM   34   C  C   . SER   A 1 7   ? 108.887 137.606 101.456 1.00 40.95 ? 7   SER   A C   1 
ATOM   35   O  O   . SER   A 1 7   ? 109.891 137.215 102.047 1.00 40.91 ? 7   SER   A O   1 
ATOM   36   C  CB  . SER   A 1 7   ? 108.052 136.435 99.402  1.00 40.99 ? 7   SER   A CB  1 
ATOM   37   O  OG  . SER   A 1 7   ? 107.172 135.440 98.894  1.00 41.00 ? 7   SER   A OG  1 
ATOM   38   N  N   . SER   A 1 8   ? 108.602 138.903 101.276 1.00 40.95 ? 8   SER   A N   1 
ATOM   39   C  CA  . SER   A 1 8   ? 109.496 139.969 101.706 1.00 40.94 ? 8   SER   A CA  1 
ATOM   40   C  C   . SER   A 1 8   ? 109.857 139.823 103.186 1.00 40.90 ? 8   SER   A C   1 
ATOM   41   O  O   . SER   A 1 8   ? 110.995 140.089 103.571 1.00 40.82 ? 8   SER   A O   1 
ATOM   42   C  CB  . SER   A 1 8   ? 108.897 141.328 101.429 1.00 40.95 ? 8   SER   A CB  1 
ATOM   43   O  OG  . SER   A 1 8   ? 108.665 141.511 100.039 1.00 40.95 ? 8   SER   A OG  1 
ATOM   44   N  N   . LEU   A 1 9   ? 108.886 139.399 104.008 1.00 40.91 ? 9   LEU   A N   1 
ATOM   45   C  CA  . LEU   A 1 9   ? 109.099 139.256 105.442 1.00 40.90 ? 9   LEU   A CA  1 
ATOM   46   C  C   . LEU   A 1 9   ? 110.199 138.230 105.722 1.00 40.87 ? 9   LEU   A C   1 
ATOM   47   O  O   . LEU   A 1 9   ? 111.030 138.466 106.598 1.00 40.82 ? 9   LEU   A O   1 
ATOM   48   C  CB  . LEU   A 1 9   ? 107.799 138.887 106.162 1.00 40.92 ? 9   LEU   A CB  1 
ATOM   49   C  CG  . LEU   A 1 9   ? 106.782 140.017 106.382 1.00 40.93 ? 9   LEU   A CG  1 
ATOM   50   C  CD1 . LEU   A 1 9   ? 105.431 139.441 106.800 1.00 40.94 ? 9   LEU   A CD1 1 
ATOM   51   C  CD2 . LEU   A 1 9   ? 107.253 141.057 107.403 1.00 40.94 ? 9   LEU   A CD2 1 
ATOM   52   N  N   . ILE   A 1 10  ? 110.214 137.110 104.982 1.00 40.84 ? 10  ILE   A N   1 
ATOM   53   C  CA  . ILE   A 1 10  ? 111.194 136.059 105.239 1.00 40.79 ? 10  ILE   A CA  1 
ATOM   54   C  C   . ILE   A 1 10  ? 112.563 136.573 104.787 1.00 40.76 ? 10  ILE   A C   1 
ATOM   55   O  O   . ILE   A 1 10  ? 113.564 136.308 105.449 1.00 40.72 ? 10  ILE   A O   1 
ATOM   56   C  CB  . ILE   A 1 10  ? 110.816 134.695 104.605 1.00 40.78 ? 10  ILE   A CB  1 
ATOM   57   C  CG1 . ILE   A 1 10  ? 111.215 134.574 103.111 1.00 40.77 ? 10  ILE   A CG1 1 
ATOM   58   C  CG2 . ILE   A 1 10  ? 109.333 134.372 104.836 1.00 40.78 ? 10  ILE   A CG2 1 
ATOM   59   C  CD1 . ILE   A 1 10  ? 111.058 133.184 102.512 1.00 40.77 ? 10  ILE   A CD1 1 
ATOM   60   N  N   . LEU   A 1 11  ? 112.583 137.345 103.688 1.00 40.76 ? 11  LEU   A N   1 
ATOM   61   C  CA  . LEU   A 1 11  ? 113.799 137.958 103.173 1.00 40.76 ? 11  LEU   A CA  1 
ATOM   62   C  C   . LEU   A 1 11  ? 114.440 138.811 104.266 1.00 40.75 ? 11  LEU   A C   1 
ATOM   63   O  O   . LEU   A 1 11  ? 115.627 138.657 104.555 1.00 40.72 ? 11  LEU   A O   1 
ATOM   64   C  CB  . LEU   A 1 11  ? 113.457 138.776 101.925 1.00 40.75 ? 11  LEU   A CB  1 
ATOM   65   C  CG  . LEU   A 1 11  ? 114.595 139.551 101.242 1.00 40.75 ? 11  LEU   A CG  1 
ATOM   66   C  CD1 . LEU   A 1 11  ? 114.249 139.787 99.779  1.00 40.74 ? 11  LEU   A CD1 1 
ATOM   67   C  CD2 . LEU   A 1 11  ? 114.908 140.889 101.907 1.00 40.75 ? 11  LEU   A CD2 1 
ATOM   68   N  N   . MET   A 1 12  ? 113.640 139.705 104.865 1.00 40.76 ? 12  MET   A N   1 
ATOM   69   C  CA  . MET   A 1 12  ? 114.143 140.662 105.837 1.00 40.75 ? 12  MET   A CA  1 
ATOM   70   C  C   . MET   A 1 12  ? 114.543 139.930 107.118 1.00 40.72 ? 12  MET   A C   1 
ATOM   71   O  O   . MET   A 1 12  ? 115.552 140.276 107.730 1.00 40.69 ? 12  MET   A O   1 
ATOM   72   C  CB  . MET   A 1 12  ? 113.094 141.741 106.140 1.00 40.77 ? 12  MET   A CB  1 
ATOM   73   C  CG  . MET   A 1 12  ? 113.637 142.983 106.838 1.00 40.77 ? 12  MET   A CG  1 
ATOM   74   S  SD  . MET   A 1 12  ? 114.969 143.828 105.958 1.00 40.76 ? 12  MET   A SD  1 
ATOM   75   C  CE  . MET   A 1 12  ? 114.197 144.396 104.436 1.00 40.75 ? 12  MET   A CE  1 
ATOM   76   N  N   . ALA   A 1 13  ? 113.753 138.919 107.508 1.00 40.72 ? 13  ALA   A N   1 
ATOM   77   C  CA  . ALA   A 1 13  ? 114.073 138.080 108.655 1.00 40.68 ? 13  ALA   A CA  1 
ATOM   78   C  C   . ALA   A 1 13  ? 115.432 137.408 108.457 1.00 40.64 ? 13  ALA   A C   1 
ATOM   79   O  O   . ALA   A 1 13  ? 116.233 137.353 109.388 1.00 40.59 ? 13  ALA   A O   1 
ATOM   80   C  CB  . ALA   A 1 13  ? 112.980 137.055 108.879 1.00 40.69 ? 13  ALA   A CB  1 
ATOM   81   N  N   . TYR   A 1 14  ? 115.680 136.904 107.240 1.00 40.63 ? 14  TYR   A N   1 
ATOM   82   C  CA  . TYR   A 1 14  ? 116.930 136.234 106.915 1.00 40.62 ? 14  TYR   A CA  1 
ATOM   83   C  C   . TYR   A 1 14  ? 118.083 137.239 106.917 1.00 40.63 ? 14  TYR   A C   1 
ATOM   84   O  O   . TYR   A 1 14  ? 119.178 136.906 107.369 1.00 40.58 ? 14  TYR   A O   1 
ATOM   85   C  CB  . TYR   A 1 14  ? 116.822 135.503 105.571 1.00 40.62 ? 14  TYR   A CB  1 
ATOM   86   C  CG  . TYR   A 1 14  ? 116.059 134.181 105.572 1.00 40.64 ? 14  TYR   A CG  1 
ATOM   87   C  CD1 . TYR   A 1 14  ? 116.361 133.164 106.476 1.00 40.65 ? 14  TYR   A CD1 1 
ATOM   88   C  CD2 . TYR   A 1 14  ? 115.038 133.945 104.655 1.00 40.67 ? 14  TYR   A CD2 1 
ATOM   89   C  CE1 . TYR   A 1 14  ? 115.671 131.962 106.468 1.00 40.67 ? 14  TYR   A CE1 1 
ATOM   90   C  CE2 . TYR   A 1 14  ? 114.334 132.752 104.646 1.00 40.69 ? 14  TYR   A CE2 1 
ATOM   91   C  CZ  . TYR   A 1 14  ? 114.655 131.756 105.552 1.00 40.68 ? 14  TYR   A CZ  1 
ATOM   92   O  OH  . TYR   A 1 14  ? 113.973 130.574 105.537 1.00 40.67 ? 14  TYR   A OH  1 
ATOM   93   N  N   . ILE   A 1 15  ? 117.840 138.457 106.405 1.00 40.66 ? 15  ILE   A N   1 
ATOM   94   C  CA  . ILE   A 1 15  ? 118.832 139.525 106.457 1.00 40.65 ? 15  ILE   A CA  1 
ATOM   95   C  C   . ILE   A 1 15  ? 119.175 139.814 107.920 1.00 40.63 ? 15  ILE   A C   1 
ATOM   96   O  O   . ILE   A 1 15  ? 120.351 139.934 108.258 1.00 40.62 ? 15  ILE   A O   1 
ATOM   97   C  CB  . ILE   A 1 15  ? 118.359 140.790 105.704 1.00 40.67 ? 15  ILE   A CB  1 
ATOM   98   C  CG1 . ILE   A 1 15  ? 118.512 140.622 104.176 1.00 40.70 ? 15  ILE   A CG1 1 
ATOM   99   C  CG2 . ILE   A 1 15  ? 119.075 142.048 106.215 1.00 40.66 ? 15  ILE   A CG2 1 
ATOM   100  C  CD1 . ILE   A 1 15  ? 118.023 141.797 103.342 1.00 40.71 ? 15  ILE   A CD1 1 
ATOM   101  N  N   . ILE   A 1 16  ? 118.149 139.920 108.776 1.00 40.61 ? 16  ILE   A N   1 
ATOM   102  C  CA  . ILE   A 1 16  ? 118.356 140.159 110.198 1.00 40.57 ? 16  ILE   A CA  1 
ATOM   103  C  C   . ILE   A 1 16  ? 119.239 139.041 110.756 1.00 40.52 ? 16  ILE   A C   1 
ATOM   104  O  O   . ILE   A 1 16  ? 120.271 139.326 111.357 1.00 40.49 ? 16  ILE   A O   1 
ATOM   105  C  CB  . ILE   A 1 16  ? 117.014 140.297 110.954 1.00 40.60 ? 16  ILE   A CB  1 
ATOM   106  C  CG1 . ILE   A 1 16  ? 116.284 141.607 110.582 1.00 40.62 ? 16  ILE   A CG1 1 
ATOM   107  C  CG2 . ILE   A 1 16  ? 117.211 140.170 112.469 1.00 40.61 ? 16  ILE   A CG2 1 
ATOM   108  C  CD1 . ILE   A 1 16  ? 114.787 141.604 110.850 1.00 40.62 ? 16  ILE   A CD1 1 
ATOM   109  N  N   . ILE   A 1 17  ? 118.847 137.779 110.520 1.00 40.48 ? 17  ILE   A N   1 
ATOM   110  C  CA  . ILE   A 1 17  ? 119.588 136.625 111.017 1.00 40.42 ? 17  ILE   A CA  1 
ATOM   111  C  C   . ILE   A 1 17  ? 121.043 136.716 110.549 1.00 40.42 ? 17  ILE   A C   1 
ATOM   112  O  O   . ILE   A 1 17  ? 121.954 136.443 111.329 1.00 40.46 ? 17  ILE   A O   1 
ATOM   113  C  CB  . ILE   A 1 17  ? 118.914 135.301 110.591 1.00 40.39 ? 17  ILE   A CB  1 
ATOM   114  C  CG1 . ILE   A 1 17  ? 117.580 135.077 111.341 1.00 40.39 ? 17  ILE   A CG1 1 
ATOM   115  C  CG2 . ILE   A 1 17  ? 119.863 134.108 110.758 1.00 40.37 ? 17  ILE   A CG2 1 
ATOM   116  C  CD1 . ILE   A 1 17  ? 116.641 134.070 110.697 1.00 40.39 ? 17  ILE   A CD1 1 
ATOM   117  N  N   . PHE   A 1 18  ? 121.250 137.106 109.283 1.00 40.44 ? 18  PHE   A N   1 
ATOM   118  C  CA  . PHE   A 1 18  ? 122.585 137.224 108.714 1.00 40.42 ? 18  PHE   A CA  1 
ATOM   119  C  C   . PHE   A 1 18  ? 123.368 138.321 109.438 1.00 40.44 ? 18  PHE   A C   1 
ATOM   120  O  O   . PHE   A 1 18  ? 124.478 138.072 109.909 1.00 40.45 ? 18  PHE   A O   1 
ATOM   121  C  CB  . PHE   A 1 18  ? 122.494 137.486 107.205 1.00 40.40 ? 18  PHE   A CB  1 
ATOM   122  C  CG  . PHE   A 1 18  ? 123.829 137.668 106.492 1.00 40.36 ? 18  PHE   A CG  1 
ATOM   123  C  CD1 . PHE   A 1 18  ? 124.552 136.568 106.037 1.00 40.34 ? 18  PHE   A CD1 1 
ATOM   124  C  CD2 . PHE   A 1 18  ? 124.353 138.939 106.262 1.00 40.36 ? 18  PHE   A CD2 1 
ATOM   125  C  CE1 . PHE   A 1 18  ? 125.765 136.735 105.384 1.00 40.33 ? 18  PHE   A CE1 1 
ATOM   126  C  CE2 . PHE   A 1 18  ? 125.567 139.100 105.607 1.00 40.35 ? 18  PHE   A CE2 1 
ATOM   127  C  CZ  . PHE   A 1 18  ? 126.268 137.999 105.168 1.00 40.34 ? 18  PHE   A CZ  1 
ATOM   128  N  N   . LEU   A 1 19  ? 122.776 139.520 109.541 1.00 40.45 ? 19  LEU   A N   1 
ATOM   129  C  CA  . LEU   A 1 19  ? 123.502 140.711 109.961 1.00 40.45 ? 19  LEU   A CA  1 
ATOM   130  C  C   . LEU   A 1 19  ? 123.631 140.733 111.486 1.00 40.47 ? 19  LEU   A C   1 
ATOM   131  O  O   . LEU   A 1 19  ? 124.491 141.431 112.018 1.00 40.47 ? 19  LEU   A O   1 
ATOM   132  C  CB  . LEU   A 1 19  ? 122.800 141.967 109.430 1.00 40.45 ? 19  LEU   A CB  1 
ATOM   133  C  CG  . LEU   A 1 19  ? 123.672 143.111 108.883 1.00 40.45 ? 19  LEU   A CG  1 
ATOM   134  C  CD1 . LEU   A 1 19  ? 124.679 143.669 109.891 1.00 40.46 ? 19  LEU   A CD1 1 
ATOM   135  C  CD2 . LEU   A 1 19  ? 124.384 142.714 107.584 1.00 40.44 ? 19  LEU   A CD2 1 
ATOM   136  N  N   . THR   A 1 20  ? 122.768 139.981 112.183 1.00 40.49 ? 20  THR   A N   1 
ATOM   137  C  CA  . THR   A 1 20  ? 122.866 139.818 113.626 1.00 40.51 ? 20  THR   A CA  1 
ATOM   138  C  C   . THR   A 1 20  ? 123.838 138.679 113.935 1.00 40.48 ? 20  THR   A C   1 
ATOM   139  O  O   . THR   A 1 20  ? 124.661 138.798 114.841 1.00 40.49 ? 20  THR   A O   1 
ATOM   140  C  CB  . THR   A 1 20  ? 121.479 139.558 114.221 1.00 40.52 ? 20  THR   A CB  1 
ATOM   141  O  OG1 . THR   A 1 20  ? 120.660 140.636 113.777 1.00 40.52 ? 20  THR   A OG1 1 
ATOM   142  C  CG2 . THR   A 1 20  ? 121.470 139.512 115.740 1.00 40.54 ? 20  THR   A CG2 1 
ATOM   143  N  N   . GLY   A 1 21  ? 123.734 137.583 113.171 1.00 40.47 ? 21  GLY   A N   1 
ATOM   144  C  CA  . GLY   A 1 21  ? 124.493 136.371 113.432 1.00 40.46 ? 21  GLY   A CA  1 
ATOM   145  C  C   . GLY   A 1 21  ? 125.970 136.522 113.076 1.00 40.45 ? 21  GLY   A C   1 
ATOM   146  O  O   . GLY   A 1 21  ? 126.826 136.380 113.947 1.00 40.47 ? 21  GLY   A O   1 
ATOM   147  N  N   . LEU   A 1 22  ? 126.251 136.824 111.799 1.00 40.44 ? 22  LEU   A N   1 
ATOM   148  C  CA  . LEU   A 1 22  ? 127.597 136.708 111.249 1.00 40.46 ? 22  LEU   A CA  1 
ATOM   149  C  C   . LEU   A 1 22  ? 128.598 137.491 112.106 1.00 40.48 ? 22  LEU   A C   1 
ATOM   150  O  O   . LEU   A 1 22  ? 129.639 136.934 112.448 1.00 40.49 ? 22  LEU   A O   1 
ATOM   151  C  CB  . LEU   A 1 22  ? 127.642 137.131 109.776 1.00 40.47 ? 22  LEU   A CB  1 
ATOM   152  C  CG  . LEU   A 1 22  ? 128.980 136.954 109.041 1.00 40.47 ? 22  LEU   A CG  1 
ATOM   153  C  CD1 . LEU   A 1 22  ? 129.307 135.488 108.750 1.00 40.46 ? 22  LEU   A CD1 1 
ATOM   154  C  CD2 . LEU   A 1 22  ? 129.007 137.773 107.753 1.00 40.47 ? 22  LEU   A CD2 1 
ATOM   155  N  N   . PRO   A 1 23  ? 128.360 138.773 112.492 1.00 40.49 ? 23  PRO   A N   1 
ATOM   156  C  CA  . PRO   A 1 23  ? 129.310 139.489 113.349 1.00 40.50 ? 23  PRO   A CA  1 
ATOM   157  C  C   . PRO   A 1 23  ? 129.554 138.786 114.685 1.00 40.51 ? 23  PRO   A C   1 
ATOM   158  O  O   . PRO   A 1 23  ? 130.700 138.662 115.110 1.00 40.52 ? 23  PRO   A O   1 
ATOM   159  C  CB  . PRO   A 1 23  ? 128.661 140.864 113.578 1.00 40.50 ? 23  PRO   A CB  1 
ATOM   160  C  CG  . PRO   A 1 23  ? 127.709 141.023 112.417 1.00 40.50 ? 23  PRO   A CG  1 
ATOM   161  C  CD  . PRO   A 1 23  ? 127.209 139.621 112.135 1.00 40.49 ? 23  PRO   A CD  1 
ATOM   162  N  N   . ALA   A 1 24  ? 128.472 138.318 115.325 1.00 40.49 ? 24  ALA   A N   1 
ATOM   163  C  CA  . ALA   A 1 24  ? 128.556 137.662 116.622 1.00 40.48 ? 24  ALA   A CA  1 
ATOM   164  C  C   . ALA   A 1 24  ? 129.275 136.320 116.495 1.00 40.47 ? 24  ALA   A C   1 
ATOM   165  O  O   . ALA   A 1 24  ? 130.010 135.929 117.399 1.00 40.49 ? 24  ALA   A O   1 
ATOM   166  C  CB  . ALA   A 1 24  ? 127.170 137.491 117.210 1.00 40.49 ? 24  ALA   A CB  1 
ATOM   167  N  N   . ASN   A 1 25  ? 129.052 135.627 115.369 1.00 40.46 ? 25  ASN   A N   1 
ATOM   168  C  CA  . ASN   A 1 25  ? 129.641 134.320 115.119 1.00 40.46 ? 25  ASN   A CA  1 
ATOM   169  C  C   . ASN   A 1 25  ? 131.128 134.474 114.797 1.00 40.48 ? 25  ASN   A C   1 
ATOM   170  O  O   . ASN   A 1 25  ? 131.932 133.637 115.204 1.00 40.48 ? 25  ASN   A O   1 
ATOM   171  C  CB  . ASN   A 1 25  ? 128.897 133.578 114.013 1.00 40.45 ? 25  ASN   A CB  1 
ATOM   172  C  CG  . ASN   A 1 25  ? 129.206 132.099 113.999 1.00 40.44 ? 25  ASN   A CG  1 
ATOM   173  O  OD1 . ASN   A 1 25  ? 129.873 131.614 113.078 1.00 40.43 ? 25  ASN   A OD1 1 
ATOM   174  N  ND2 . ASN   A 1 25  ? 128.736 131.367 114.999 1.00 40.43 ? 25  ASN   A ND2 1 
ATOM   175  N  N   . LEU   A 1 26  ? 131.480 135.536 114.058 1.00 40.49 ? 26  LEU   A N   1 
ATOM   176  C  CA  . LEU   A 1 26  ? 132.873 135.860 113.779 1.00 40.52 ? 26  LEU   A CA  1 
ATOM   177  C  C   . LEU   A 1 26  ? 133.570 136.272 115.075 1.00 40.54 ? 26  LEU   A C   1 
ATOM   178  O  O   . LEU   A 1 26  ? 134.708 135.871 115.313 1.00 40.57 ? 26  LEU   A O   1 
ATOM   179  C  CB  . LEU   A 1 26  ? 132.997 136.955 112.716 1.00 40.53 ? 26  LEU   A CB  1 
ATOM   180  C  CG  . LEU   A 1 26  ? 132.707 136.557 111.261 1.00 40.55 ? 26  LEU   A CG  1 
ATOM   181  C  CD1 . LEU   A 1 26  ? 132.555 137.806 110.395 1.00 40.55 ? 26  LEU   A CD1 1 
ATOM   182  C  CD2 . LEU   A 1 26  ? 133.769 135.630 110.667 1.00 40.56 ? 26  LEU   A CD2 1 
ATOM   183  N  N   . LEU   A 1 27  ? 132.882 137.079 115.898 1.00 40.55 ? 27  LEU   A N   1 
ATOM   184  C  CA  . LEU   A 1 27  ? 133.396 137.477 117.202 1.00 40.55 ? 27  LEU   A CA  1 
ATOM   185  C  C   . LEU   A 1 27  ? 133.591 136.241 118.079 1.00 40.54 ? 27  LEU   A C   1 
ATOM   186  O  O   . LEU   A 1 27  ? 134.555 136.184 118.836 1.00 40.56 ? 27  LEU   A O   1 
ATOM   187  C  CB  . LEU   A 1 27  ? 132.477 138.494 117.885 1.00 40.56 ? 27  LEU   A CB  1 
ATOM   188  C  CG  . LEU   A 1 27  ? 132.587 139.955 117.424 1.00 40.58 ? 27  LEU   A CG  1 
ATOM   189  C  CD1 . LEU   A 1 27  ? 131.370 140.753 117.887 1.00 40.58 ? 27  LEU   A CD1 1 
ATOM   190  C  CD2 . LEU   A 1 27  ? 133.875 140.631 117.899 1.00 40.58 ? 27  LEU   A CD2 1 
ATOM   191  N  N   . ALA   A 1 28  ? 132.671 135.270 117.978 1.00 40.52 ? 28  ALA   A N   1 
ATOM   192  C  CA  . ALA   A 1 28  ? 132.779 134.018 118.714 1.00 40.51 ? 28  ALA   A CA  1 
ATOM   193  C  C   . ALA   A 1 28  ? 133.981 133.216 118.215 1.00 40.50 ? 28  ALA   A C   1 
ATOM   194  O  O   . ALA   A 1 28  ? 134.761 132.716 119.022 1.00 40.53 ? 28  ALA   A O   1 
ATOM   195  C  CB  . ALA   A 1 28  ? 131.495 133.223 118.595 1.00 40.50 ? 28  ALA   A CB  1 
ATOM   196  N  N   . LEU   A 1 29  ? 134.128 133.109 116.886 1.00 40.51 ? 29  LEU   A N   1 
ATOM   197  C  CA  . LEU   A 1 29  ? 135.246 132.394 116.287 1.00 40.54 ? 29  LEU   A CA  1 
ATOM   198  C  C   . LEU   A 1 29  ? 136.555 133.020 116.770 1.00 40.58 ? 29  LEU   A C   1 
ATOM   199  O  O   . LEU   A 1 29  ? 137.445 132.306 117.230 1.00 40.61 ? 29  LEU   A O   1 
ATOM   200  C  CB  . LEU   A 1 29  ? 135.119 132.402 114.761 1.00 40.54 ? 29  LEU   A CB  1 
ATOM   201  C  CG  . LEU   A 1 29  ? 136.022 131.434 113.979 1.00 40.55 ? 29  LEU   A CG  1 
ATOM   202  C  CD1 . LEU   A 1 29  ? 135.365 131.040 112.659 1.00 40.55 ? 29  LEU   A CD1 1 
ATOM   203  C  CD2 . LEU   A 1 29  ? 137.419 131.997 113.716 1.00 40.56 ? 29  LEU   A CD2 1 
ATOM   204  N  N   . ARG   A 1 30  ? 136.650 134.355 116.679 1.00 40.61 ? 30  ARG   A N   1 
ATOM   205  C  CA  . ARG   A 1 30  ? 137.813 135.092 117.155 1.00 40.65 ? 30  ARG   A CA  1 
ATOM   206  C  C   . ARG   A 1 30  ? 137.982 134.915 118.664 1.00 40.65 ? 30  ARG   A C   1 
ATOM   207  O  O   . ARG   A 1 30  ? 139.112 134.844 119.144 1.00 40.65 ? 30  ARG   A O   1 
ATOM   208  C  CB  . ARG   A 1 30  ? 137.726 136.586 116.809 1.00 40.66 ? 30  ARG   A CB  1 
ATOM   209  C  CG  . ARG   A 1 30  ? 138.459 137.023 115.545 1.00 40.67 ? 30  ARG   A CG  1 
ATOM   210  C  CD  . ARG   A 1 30  ? 139.971 137.170 115.733 1.00 40.67 ? 30  ARG   A CD  1 
ATOM   211  N  NE  . ARG   A 1 30  ? 140.316 138.226 116.694 1.00 40.68 ? 30  ARG   A NE  1 
ATOM   212  C  CZ  . ARG   A 1 30  ? 140.822 138.073 117.921 1.00 40.68 ? 30  ARG   A CZ  1 
ATOM   213  N  NH1 . ARG   A 1 30  ? 141.086 139.141 118.657 1.00 40.68 ? 30  ARG   A NH1 1 
ATOM   214  N  NH2 . ARG   A 1 30  ? 141.065 136.873 118.424 1.00 40.69 ? 30  ARG   A NH2 1 
ATOM   215  N  N   . ALA   A 1 31  ? 136.865 134.863 119.404 1.00 40.64 ? 31  ALA   A N   1 
ATOM   216  C  CA  . ALA   A 1 31  ? 136.904 134.682 120.849 1.00 40.67 ? 31  ALA   A CA  1 
ATOM   217  C  C   . ALA   A 1 31  ? 137.567 133.349 121.192 1.00 40.66 ? 31  ALA   A C   1 
ATOM   218  O  O   . ALA   A 1 31  ? 138.440 133.311 122.056 1.00 40.70 ? 31  ALA   A O   1 
ATOM   219  C  CB  . ALA   A 1 31  ? 135.513 134.773 121.447 1.00 40.67 ? 31  ALA   A CB  1 
ATOM   220  N  N   . PHE   A 1 32  ? 137.161 132.269 120.507 1.00 40.62 ? 32  PHE   A N   1 
ATOM   221  C  CA  . PHE   A 1 32  ? 137.737 130.954 120.749 1.00 40.63 ? 32  PHE   A CA  1 
ATOM   222  C  C   . PHE   A 1 32  ? 139.202 130.961 120.318 1.00 40.66 ? 32  PHE   A C   1 
ATOM   223  O  O   . PHE   A 1 32  ? 140.057 130.515 121.079 1.00 40.77 ? 32  PHE   A O   1 
ATOM   224  C  CB  . PHE   A 1 32  ? 136.937 129.829 120.081 1.00 40.60 ? 32  PHE   A CB  1 
ATOM   225  C  CG  . PHE   A 1 32  ? 135.592 129.556 120.744 1.00 40.57 ? 32  PHE   A CG  1 
ATOM   226  C  CD1 . PHE   A 1 32  ? 135.524 128.948 121.996 1.00 40.54 ? 32  PHE   A CD1 1 
ATOM   227  C  CD2 . PHE   A 1 32  ? 134.398 129.898 120.114 1.00 40.55 ? 32  PHE   A CD2 1 
ATOM   228  C  CE1 . PHE   A 1 32  ? 134.300 128.706 122.603 1.00 40.53 ? 32  PHE   A CE1 1 
ATOM   229  C  CE2 . PHE   A 1 32  ? 133.177 129.650 120.723 1.00 40.54 ? 32  PHE   A CE2 1 
ATOM   230  C  CZ  . PHE   A 1 32  ? 133.131 129.058 121.965 1.00 40.53 ? 32  PHE   A CZ  1 
ATOM   231  N  N   . VAL   A 1 33  ? 139.488 131.495 119.121 1.00 40.68 ? 33  VAL   A N   1 
ATOM   232  C  CA  . VAL   A 1 33  ? 140.860 131.651 118.652 1.00 40.72 ? 33  VAL   A CA  1 
ATOM   233  C  C   . VAL   A 1 33  ? 141.661 132.414 119.711 1.00 40.76 ? 33  VAL   A C   1 
ATOM   234  O  O   . VAL   A 1 33  ? 142.842 132.135 119.909 1.00 40.77 ? 33  VAL   A O   1 
ATOM   235  C  CB  . VAL   A 1 33  ? 140.938 132.332 117.265 1.00 40.73 ? 33  VAL   A CB  1 
ATOM   236  C  CG1 . VAL   A 1 33  ? 142.339 132.843 116.929 1.00 40.73 ? 33  VAL   A CG1 1 
ATOM   237  C  CG2 . VAL   A 1 33  ? 140.430 131.418 116.151 1.00 40.73 ? 33  VAL   A CG2 1 
ATOM   238  N  N   . GLY   A 1 34  ? 141.013 133.375 120.385 1.00 40.78 ? 34  GLY   A N   1 
ATOM   239  C  CA  . GLY   A 1 34  ? 141.603 134.057 121.526 1.00 40.82 ? 34  GLY   A CA  1 
ATOM   240  C  C   . GLY   A 1 34  ? 141.706 133.138 122.743 1.00 40.85 ? 34  GLY   A C   1 
ATOM   241  O  O   . GLY   A 1 34  ? 142.778 133.013 123.332 1.00 40.92 ? 34  GLY   A O   1 
ATOM   242  N  N   . ARG   A 1 35  ? 140.585 132.490 123.094 1.00 40.86 ? 35  ARG   A N   1 
ATOM   243  C  CA  . ARG   A 1 35  ? 140.489 131.636 124.270 1.00 40.88 ? 35  ARG   A CA  1 
ATOM   244  C  C   . ARG   A 1 35  ? 141.525 130.514 124.212 1.00 40.90 ? 35  ARG   A C   1 
ATOM   245  O  O   . ARG   A 1 35  ? 141.971 130.040 125.256 1.00 40.90 ? 35  ARG   A O   1 
ATOM   246  C  CB  . ARG   A 1 35  ? 139.085 131.035 124.407 1.00 40.87 ? 35  ARG   A CB  1 
ATOM   247  N  N   . ILE   A 1 36  ? 141.875 130.081 122.991 1.00 40.91 ? 36  ILE   A N   1 
ATOM   248  C  CA  . ILE   A 1 36  ? 142.971 129.147 122.771 1.00 40.96 ? 36  ILE   A CA  1 
ATOM   249  C  C   . ILE   A 1 36  ? 144.159 129.557 123.647 1.00 41.00 ? 36  ILE   A C   1 
ATOM   250  O  O   . ILE   A 1 36  ? 144.593 128.762 124.476 1.00 41.01 ? 36  ILE   A O   1 
ATOM   251  C  CB  . ILE   A 1 36  ? 143.315 129.036 121.262 1.00 40.96 ? 36  ILE   A CB  1 
ATOM   252  C  CG1 . ILE   A 1 36  ? 142.723 127.756 120.622 1.00 40.96 ? 36  ILE   A CG1 1 
ATOM   253  C  CG2 . ILE   A 1 36  ? 144.820 129.127 120.985 1.00 40.96 ? 36  ILE   A CG2 1 
ATOM   254  C  CD1 . ILE   A 1 36  ? 141.255 127.843 120.240 1.00 40.95 ? 36  ILE   A CD1 1 
ATOM   255  N  N   . ARG   A 1 37  ? 144.637 130.805 123.505 1.00 41.03 ? 37  ARG   A N   1 
ATOM   256  C  CA  . ARG   A 1 37  ? 145.893 131.241 124.104 1.00 41.10 ? 37  ARG   A CA  1 
ATOM   257  C  C   . ARG   A 1 37  ? 146.975 130.214 123.752 1.00 41.13 ? 37  ARG   A C   1 
ATOM   258  O  O   . ARG   A 1 37  ? 147.470 130.212 122.627 1.00 41.13 ? 37  ARG   A O   1 
ATOM   259  C  CB  . ARG   A 1 37  ? 145.731 131.501 125.611 1.00 41.13 ? 37  ARG   A CB  1 
ATOM   260  C  CG  . ARG   A 1 37  ? 144.767 132.595 126.057 1.00 41.16 ? 37  ARG   A CG  1 
ATOM   261  C  CD  . ARG   A 1 37  ? 145.205 134.026 125.745 1.00 41.20 ? 37  ARG   A CD  1 
ATOM   262  N  NE  . ARG   A 1 37  ? 144.822 134.457 124.394 1.00 41.22 ? 37  ARG   A NE  1 
ATOM   263  C  CZ  . ARG   A 1 37  ? 145.622 134.836 123.395 1.00 41.23 ? 37  ARG   A CZ  1 
ATOM   264  N  NH1 . ARG   A 1 37  ? 145.086 135.221 122.249 1.00 41.23 ? 37  ARG   A NH1 1 
ATOM   265  N  NH2 . ARG   A 1 37  ? 146.940 134.839 123.521 1.00 41.24 ? 37  ARG   A NH2 1 
ATOM   266  N  N   . GLN   A 1 38  ? 147.348 129.361 124.720 1.00 41.17 ? 38  GLN   A N   1 
ATOM   267  C  CA  . GLN   A 1 38  ? 148.036 128.107 124.446 1.00 41.21 ? 38  GLN   A CA  1 
ATOM   268  C  C   . GLN   A 1 38  ? 146.961 127.068 124.126 1.00 41.22 ? 38  GLN   A C   1 
ATOM   269  O  O   . GLN   A 1 38  ? 146.111 126.802 124.975 1.00 41.22 ? 38  GLN   A O   1 
ATOM   270  C  CB  . GLN   A 1 38  ? 148.967 127.768 125.618 1.00 41.22 ? 38  GLN   A CB  1 
ATOM   271  C  CG  . GLN   A 1 38  ? 149.138 126.282 125.930 1.00 41.23 ? 38  GLN   A CG  1 
ATOM   272  C  CD  . GLN   A 1 38  ? 148.122 125.760 126.927 1.00 41.24 ? 38  GLN   A CD  1 
ATOM   273  O  OE1 . GLN   A 1 38  ? 148.087 126.187 128.087 1.00 41.25 ? 38  GLN   A OE1 1 
ATOM   274  N  NE2 . GLN   A 1 38  ? 147.285 124.826 126.497 1.00 41.24 ? 38  GLN   A NE2 1 
ATOM   275  N  N   . PRO   A 1 39  ? 146.941 126.459 122.911 1.00 41.22 ? 39  PRO   A N   1 
ATOM   276  C  CA  . PRO   A 1 39  ? 145.787 125.674 122.461 1.00 41.22 ? 39  PRO   A CA  1 
ATOM   277  C  C   . PRO   A 1 39  ? 145.099 124.928 123.604 1.00 41.21 ? 39  PRO   A C   1 
ATOM   278  O  O   . PRO   A 1 39  ? 145.715 124.092 124.265 1.00 41.23 ? 39  PRO   A O   1 
ATOM   279  C  CB  . PRO   A 1 39  ? 146.417 124.731 121.426 1.00 41.23 ? 39  PRO   A CB  1 
ATOM   280  C  CG  . PRO   A 1 39  ? 147.499 125.578 120.791 1.00 41.23 ? 39  PRO   A CG  1 
ATOM   281  C  CD  . PRO   A 1 39  ? 148.030 126.444 121.918 1.00 41.23 ? 39  PRO   A CD  1 
ATOM   282  N  N   . GLN   A 1 40  ? 143.819 125.268 123.816 1.00 41.17 ? 40  GLN   A N   1 
ATOM   283  C  CA  . GLN   A 1 40  ? 143.039 124.865 124.978 1.00 41.13 ? 40  GLN   A CA  1 
ATOM   284  C  C   . GLN   A 1 40  ? 143.316 123.411 125.367 1.00 41.10 ? 40  GLN   A C   1 
ATOM   285  O  O   . GLN   A 1 40  ? 143.443 122.548 124.498 1.00 41.10 ? 40  GLN   A O   1 
ATOM   286  C  CB  . GLN   A 1 40  ? 141.544 125.089 124.726 1.00 41.12 ? 40  GLN   A CB  1 
ATOM   287  C  CG  . GLN   A 1 40  ? 140.872 124.119 123.754 1.00 41.12 ? 40  GLN   A CG  1 
ATOM   288  C  CD  . GLN   A 1 40  ? 141.327 124.246 122.314 1.00 41.12 ? 40  GLN   A CD  1 
ATOM   289  O  OE1 . GLN   A 1 40  ? 140.673 124.900 121.495 1.00 41.11 ? 40  GLN   A OE1 1 
ATOM   290  N  NE2 . GLN   A 1 40  ? 142.443 123.613 121.980 1.00 41.12 ? 40  GLN   A NE2 1 
ATOM   291  N  N   . PRO   A 1 41  ? 143.418 123.091 126.682 1.00 41.04 ? 41  PRO   A N   1 
ATOM   292  C  CA  . PRO   A 1 41  ? 143.424 121.699 127.140 1.00 41.01 ? 41  PRO   A CA  1 
ATOM   293  C  C   . PRO   A 1 41  ? 142.031 121.119 127.393 1.00 40.96 ? 41  PRO   A C   1 
ATOM   294  O  O   . PRO   A 1 41  ? 141.911 119.948 127.752 1.00 40.96 ? 41  PRO   A O   1 
ATOM   295  C  CB  . PRO   A 1 41  ? 144.213 121.805 128.454 1.00 41.02 ? 41  PRO   A CB  1 
ATOM   296  C  CG  . PRO   A 1 41  ? 143.812 123.155 129.014 1.00 41.02 ? 41  PRO   A CG  1 
ATOM   297  C  CD  . PRO   A 1 41  ? 143.586 124.037 127.801 1.00 41.02 ? 41  PRO   A CD  1 
ATOM   298  N  N   . ALA   A 1 42  ? 140.986 121.935 127.183 1.00 40.88 ? 42  ALA   A N   1 
ATOM   299  C  CA  . ALA   A 1 42  ? 139.631 121.590 127.584 1.00 40.80 ? 42  ALA   A CA  1 
ATOM   300  C  C   . ALA   A 1 42  ? 138.851 121.036 126.391 1.00 40.73 ? 42  ALA   A C   1 
ATOM   301  O  O   . ALA   A 1 42  ? 138.751 121.700 125.358 1.00 40.65 ? 42  ALA   A O   1 
ATOM   302  C  CB  . ALA   A 1 42  ? 138.945 122.805 128.174 1.00 40.81 ? 42  ALA   A CB  1 
ATOM   303  N  N   . PRO   A 1 43  ? 138.250 119.823 126.496 1.00 40.67 ? 43  PRO   A N   1 
ATOM   304  C  CA  . PRO   A 1 43  ? 137.517 119.231 125.373 1.00 40.63 ? 43  PRO   A CA  1 
ATOM   305  C  C   . PRO   A 1 43  ? 136.267 120.021 124.981 1.00 40.59 ? 43  PRO   A C   1 
ATOM   306  O  O   . PRO   A 1 43  ? 135.867 119.997 123.819 1.00 40.58 ? 43  PRO   A O   1 
ATOM   307  C  CB  . PRO   A 1 43  ? 137.136 117.827 125.873 1.00 40.64 ? 43  PRO   A CB  1 
ATOM   308  C  CG  . PRO   A 1 43  ? 137.154 117.937 127.382 1.00 40.66 ? 43  PRO   A CG  1 
ATOM   309  C  CD  . PRO   A 1 43  ? 138.226 118.960 127.690 1.00 40.67 ? 43  PRO   A CD  1 
ATOM   310  N  N   . VAL   A 1 44  ? 135.665 120.720 125.955 1.00 40.55 ? 44  VAL   A N   1 
ATOM   311  C  CA  . VAL   A 1 44  ? 134.475 121.526 125.721 1.00 40.53 ? 44  VAL   A CA  1 
ATOM   312  C  C   . VAL   A 1 44  ? 134.789 122.595 124.670 1.00 40.53 ? 44  VAL   A C   1 
ATOM   313  O  O   . VAL   A 1 44  ? 134.055 122.725 123.690 1.00 40.44 ? 44  VAL   A O   1 
ATOM   314  C  CB  . VAL   A 1 44  ? 133.899 122.129 127.027 1.00 40.55 ? 44  VAL   A CB  1 
ATOM   315  C  CG1 . VAL   A 1 44  ? 134.862 123.077 127.746 1.00 40.55 ? 44  VAL   A CG1 1 
ATOM   316  C  CG2 . VAL   A 1 44  ? 132.549 122.810 126.805 1.00 40.54 ? 44  VAL   A CG2 1 
ATOM   317  N  N   . HIS   A 1 45  ? 135.913 123.307 124.842 1.00 40.57 ? 45  HIS   A N   1 
ATOM   318  C  CA  . HIS   A 1 45  ? 136.208 124.496 124.054 1.00 40.59 ? 45  HIS   A CA  1 
ATOM   319  C  C   . HIS   A 1 45  ? 136.457 124.134 122.589 1.00 40.58 ? 45  HIS   A C   1 
ATOM   320  O  O   . HIS   A 1 45  ? 136.247 124.969 121.711 1.00 40.59 ? 45  HIS   A O   1 
ATOM   321  C  CB  . HIS   A 1 45  ? 137.383 125.276 124.659 1.00 40.63 ? 45  HIS   A CB  1 
ATOM   322  C  CG  . HIS   A 1 45  ? 137.028 126.088 125.861 1.00 40.67 ? 45  HIS   A CG  1 
ATOM   323  N  ND1 . HIS   A 1 45  ? 137.147 125.617 127.151 1.00 40.69 ? 45  HIS   A ND1 1 
ATOM   324  C  CD2 . HIS   A 1 45  ? 136.571 127.342 125.966 1.00 40.70 ? 45  HIS   A CD2 1 
ATOM   325  C  CE1 . HIS   A 1 45  ? 136.764 126.562 127.998 1.00 40.71 ? 45  HIS   A CE1 1 
ATOM   326  N  NE2 . HIS   A 1 45  ? 136.410 127.618 127.299 1.00 40.71 ? 45  HIS   A NE2 1 
ATOM   327  N  N   . ILE   A 1 46  ? 136.904 122.895 122.332 1.00 40.56 ? 46  ILE   A N   1 
ATOM   328  C  CA  . ILE   A 1 46  ? 137.129 122.422 120.972 1.00 40.50 ? 46  ILE   A CA  1 
ATOM   329  C  C   . ILE   A 1 46  ? 135.777 122.163 120.304 1.00 40.43 ? 46  ILE   A C   1 
ATOM   330  O  O   . ILE   A 1 46  ? 135.540 122.640 119.196 1.00 40.38 ? 46  ILE   A O   1 
ATOM   331  C  CB  . ILE   A 1 46  ? 138.043 121.177 120.952 1.00 40.53 ? 46  ILE   A CB  1 
ATOM   332  C  CG1 . ILE   A 1 46  ? 139.448 121.504 121.499 1.00 40.56 ? 46  ILE   A CG1 1 
ATOM   333  C  CG2 . ILE   A 1 46  ? 138.105 120.555 119.552 1.00 40.55 ? 46  ILE   A CG2 1 
ATOM   334  C  CD1 . ILE   A 1 46  ? 140.290 120.300 121.883 1.00 40.58 ? 46  ILE   A CD1 1 
ATOM   335  N  N   . LEU   A 1 47  ? 134.894 121.416 120.983 1.00 40.39 ? 47  LEU   A N   1 
ATOM   336  C  CA  . LEU   A 1 47  ? 133.603 121.045 120.416 1.00 40.34 ? 47  LEU   A CA  1 
ATOM   337  C  C   . LEU   A 1 47  ? 132.816 122.303 120.045 1.00 40.31 ? 47  LEU   A C   1 
ATOM   338  O  O   . LEU   A 1 47  ? 132.208 122.351 118.977 1.00 40.30 ? 47  LEU   A O   1 
ATOM   339  C  CB  . LEU   A 1 47  ? 132.804 120.144 121.362 1.00 40.34 ? 47  LEU   A CB  1 
ATOM   340  C  CG  . LEU   A 1 47  ? 132.968 118.628 121.177 1.00 40.35 ? 47  LEU   A CG  1 
ATOM   341  C  CD1 . LEU   A 1 47  ? 134.361 118.107 121.533 1.00 40.37 ? 47  LEU   A CD1 1 
ATOM   342  C  CD2 . LEU   A 1 47  ? 131.900 117.878 121.974 1.00 40.34 ? 47  LEU   A CD2 1 
ATOM   343  N  N   . LEU   A 1 48  ? 132.840 123.315 120.924 1.00 40.31 ? 48  LEU   A N   1 
ATOM   344  C  CA  . LEU   A 1 48  ? 132.135 124.567 120.678 1.00 40.28 ? 48  LEU   A CA  1 
ATOM   345  C  C   . LEU   A 1 48  ? 132.667 125.235 119.409 1.00 40.28 ? 48  LEU   A C   1 
ATOM   346  O  O   . LEU   A 1 48  ? 131.882 125.775 118.631 1.00 40.24 ? 48  LEU   A O   1 
ATOM   347  C  CB  . LEU   A 1 48  ? 132.228 125.507 121.884 1.00 40.28 ? 48  LEU   A CB  1 
ATOM   348  C  CG  . LEU   A 1 48  ? 131.119 125.393 122.940 1.00 40.28 ? 48  LEU   A CG  1 
ATOM   349  C  CD1 . LEU   A 1 48  ? 131.061 124.033 123.627 1.00 40.28 ? 48  LEU   A CD1 1 
ATOM   350  C  CD2 . LEU   A 1 48  ? 131.260 126.497 123.984 1.00 40.28 ? 48  LEU   A CD2 1 
ATOM   351  N  N   . LEU   A 1 49  ? 133.992 125.193 119.201 1.00 40.29 ? 49  LEU   A N   1 
ATOM   352  C  CA  . LEU   A 1 49  ? 134.605 125.798 118.026 1.00 40.26 ? 49  LEU   A CA  1 
ATOM   353  C  C   . LEU   A 1 49  ? 133.988 125.196 116.762 1.00 40.25 ? 49  LEU   A C   1 
ATOM   354  O  O   . LEU   A 1 49  ? 133.681 125.928 115.823 1.00 40.24 ? 49  LEU   A O   1 
ATOM   355  C  CB  . LEU   A 1 49  ? 136.127 125.627 118.050 1.00 40.27 ? 49  LEU   A CB  1 
ATOM   356  C  CG  . LEU   A 1 49  ? 136.919 126.209 116.869 1.00 40.29 ? 49  LEU   A CG  1 
ATOM   357  C  CD1 . LEU   A 1 49  ? 136.891 127.737 116.813 1.00 40.31 ? 49  LEU   A CD1 1 
ATOM   358  C  CD2 . LEU   A 1 49  ? 138.360 125.702 116.895 1.00 40.31 ? 49  LEU   A CD2 1 
ATOM   359  N  N   . SER   A 1 50  ? 133.799 123.868 116.753 1.00 40.25 ? 50  SER   A N   1 
ATOM   360  C  CA  . SER   A 1 50  ? 133.214 123.180 115.611 1.00 40.21 ? 50  SER   A CA  1 
ATOM   361  C  C   . SER   A 1 50  ? 131.823 123.738 115.312 1.00 40.18 ? 50  SER   A C   1 
ATOM   362  O  O   . SER   A 1 50  ? 131.490 123.964 114.149 1.00 40.19 ? 50  SER   A O   1 
ATOM   363  C  CB  . SER   A 1 50  ? 133.171 121.685 115.829 1.00 40.21 ? 50  SER   A CB  1 
ATOM   364  O  OG  . SER   A 1 50  ? 132.733 121.010 114.657 1.00 40.21 ? 50  SER   A OG  1 
ATOM   365  N  N   . LEU   A 1 51  ? 131.028 123.973 116.367 1.00 40.16 ? 51  LEU   A N   1 
ATOM   366  C  CA  . LEU   A 1 51  ? 129.683 124.512 116.220 1.00 40.12 ? 51  LEU   A CA  1 
ATOM   367  C  C   . LEU   A 1 51  ? 129.753 125.882 115.546 1.00 40.15 ? 51  LEU   A C   1 
ATOM   368  O  O   . LEU   A 1 51  ? 128.923 126.187 114.691 1.00 40.18 ? 51  LEU   A O   1 
ATOM   369  C  CB  . LEU   A 1 51  ? 128.976 124.597 117.576 1.00 40.08 ? 51  LEU   A CB  1 
ATOM   370  C  CG  . LEU   A 1 51  ? 127.459 124.841 117.550 1.00 40.06 ? 51  LEU   A CG  1 
ATOM   371  C  CD1 . LEU   A 1 51  ? 126.675 123.565 117.250 1.00 40.06 ? 51  LEU   A CD1 1 
ATOM   372  C  CD2 . LEU   A 1 51  ? 126.976 125.473 118.851 1.00 40.05 ? 51  LEU   A CD2 1 
ATOM   373  N  N   . THR   A 1 52  ? 130.748 126.694 115.934 1.00 40.20 ? 52  THR   A N   1 
ATOM   374  C  CA  . THR   A 1 52  ? 130.921 128.030 115.384 1.00 40.24 ? 52  THR   A CA  1 
ATOM   375  C  C   . THR   A 1 52  ? 131.225 127.928 113.889 1.00 40.24 ? 52  THR   A C   1 
ATOM   376  O  O   . THR   A 1 52  ? 130.723 128.731 113.103 1.00 40.26 ? 52  THR   A O   1 
ATOM   377  C  CB  . THR   A 1 52  ? 132.029 128.772 116.136 1.00 40.27 ? 52  THR   A CB  1 
ATOM   378  O  OG1 . THR   A 1 52  ? 131.814 128.522 117.522 1.00 40.28 ? 52  THR   A OG1 1 
ATOM   379  C  CG2 . THR   A 1 52  ? 132.022 130.271 115.885 1.00 40.29 ? 52  THR   A CG2 1 
ATOM   380  N  N   . LEU   A 1 53  ? 132.042 126.933 113.509 1.00 40.23 ? 53  LEU   A N   1 
ATOM   381  C  CA  . LEU   A 1 53  ? 132.409 126.714 112.117 1.00 40.23 ? 53  LEU   A CA  1 
ATOM   382  C  C   . LEU   A 1 53  ? 131.186 126.235 111.335 1.00 40.21 ? 53  LEU   A C   1 
ATOM   383  O  O   . LEU   A 1 53  ? 130.969 126.671 110.205 1.00 40.22 ? 53  LEU   A O   1 
ATOM   384  C  CB  . LEU   A 1 53  ? 133.565 125.716 112.008 1.00 40.25 ? 53  LEU   A CB  1 
ATOM   385  C  CG  . LEU   A 1 53  ? 134.924 126.159 112.571 1.00 40.26 ? 53  LEU   A CG  1 
ATOM   386  C  CD1 . LEU   A 1 53  ? 135.850 124.956 112.742 1.00 40.27 ? 53  LEU   A CD1 1 
ATOM   387  C  CD2 . LEU   A 1 53  ? 135.601 127.231 111.715 1.00 40.28 ? 53  LEU   A CD2 1 
ATOM   388  N  N   . ALA   A 1 54  ? 130.397 125.341 111.948 1.00 40.18 ? 54  ALA   A N   1 
ATOM   389  C  CA  . ALA   A 1 54  ? 129.173 124.831 111.345 1.00 40.17 ? 54  ALA   A CA  1 
ATOM   390  C  C   . ALA   A 1 54  ? 128.171 125.966 111.131 1.00 40.18 ? 54  ALA   A C   1 
ATOM   391  O  O   . ALA   A 1 54  ? 127.476 125.987 110.117 1.00 40.19 ? 54  ALA   A O   1 
ATOM   392  C  CB  . ALA   A 1 54  ? 128.586 123.732 112.206 1.00 40.17 ? 54  ALA   A CB  1 
ATOM   393  N  N   . ASP   A 1 55  ? 128.102 126.897 112.094 1.00 40.20 ? 55  ASP   A N   1 
ATOM   394  C  CA  . ASP   A 1 55  ? 127.240 128.064 111.989 1.00 40.25 ? 55  ASP   A CA  1 
ATOM   395  C  C   . ASP   A 1 55  ? 127.736 128.972 110.864 1.00 40.25 ? 55  ASP   A C   1 
ATOM   396  O  O   . ASP   A 1 55  ? 126.950 129.370 110.007 1.00 40.22 ? 55  ASP   A O   1 
ATOM   397  C  CB  . ASP   A 1 55  ? 127.139 128.811 113.312 1.00 40.27 ? 55  ASP   A CB  1 
ATOM   398  C  CG  . ASP   A 1 55  ? 126.501 128.049 114.465 1.00 40.29 ? 55  ASP   A CG  1 
ATOM   399  O  OD1 . ASP   A 1 55  ? 126.015 126.920 114.235 1.00 40.30 ? 55  ASP   A OD1 1 
ATOM   400  O  OD2 . ASP   A 1 55  ? 126.505 128.588 115.590 1.00 40.31 ? 55  ASP   A OD2 1 
ATOM   401  N  N   . LEU   A 1 56  ? 129.041 129.285 110.876 1.00 40.27 ? 56  LEU   A N   1 
ATOM   402  C  CA  . LEU   A 1 56  ? 129.657 130.122 109.855 1.00 40.29 ? 56  LEU   A CA  1 
ATOM   403  C  C   . LEU   A 1 56  ? 129.340 129.562 108.468 1.00 40.28 ? 56  LEU   A C   1 
ATOM   404  O  O   . LEU   A 1 56  ? 128.970 130.318 107.570 1.00 40.27 ? 56  LEU   A O   1 
ATOM   405  C  CB  . LEU   A 1 56  ? 131.166 130.218 110.091 1.00 40.33 ? 56  LEU   A CB  1 
ATOM   406  C  CG  . LEU   A 1 56  ? 131.979 131.058 109.094 1.00 40.37 ? 56  LEU   A CG  1 
ATOM   407  C  CD1 . LEU   A 1 56  ? 131.723 132.559 109.231 1.00 40.39 ? 56  LEU   A CD1 1 
ATOM   408  C  CD2 . LEU   A 1 56  ? 133.470 130.755 109.222 1.00 40.38 ? 56  LEU   A CD2 1 
ATOM   409  N  N   . LEU   A 1 57  ? 129.487 128.237 108.311 1.00 40.24 ? 57  LEU   A N   1 
ATOM   410  C  CA  . LEU   A 1 57  ? 129.232 127.557 107.049 1.00 40.21 ? 57  LEU   A CA  1 
ATOM   411  C  C   . LEU   A 1 57  ? 127.818 127.881 106.564 1.00 40.18 ? 57  LEU   A C   1 
ATOM   412  O  O   . LEU   A 1 57  ? 127.620 128.143 105.379 1.00 40.17 ? 57  LEU   A O   1 
ATOM   413  C  CB  . LEU   A 1 57  ? 129.453 126.051 107.223 1.00 40.21 ? 57  LEU   A CB  1 
ATOM   414  C  CG  . LEU   A 1 57  ? 129.591 125.209 105.946 1.00 40.22 ? 57  LEU   A CG  1 
ATOM   415  C  CD1 . LEU   A 1 57  ? 130.430 123.962 106.222 1.00 40.23 ? 57  LEU   A CD1 1 
ATOM   416  C  CD2 . LEU   A 1 57  ? 128.247 124.804 105.340 1.00 40.22 ? 57  LEU   A CD2 1 
ATOM   417  N  N   . LEU   A 1 58  ? 126.847 127.868 107.488 1.00 40.16 ? 58  LEU   A N   1 
ATOM   418  C  CA  . LEU   A 1 58  ? 125.452 128.115 107.156 1.00 40.14 ? 58  LEU   A CA  1 
ATOM   419  C  C   . LEU   A 1 58  ? 125.240 129.605 106.880 1.00 40.19 ? 58  LEU   A C   1 
ATOM   420  O  O   . LEU   A 1 58  ? 124.632 129.961 105.871 1.00 40.24 ? 58  LEU   A O   1 
ATOM   421  C  CB  . LEU   A 1 58  ? 124.574 127.591 108.295 1.00 40.11 ? 58  LEU   A CB  1 
ATOM   422  C  CG  . LEU   A 1 58  ? 123.055 127.586 108.066 1.00 40.09 ? 58  LEU   A CG  1 
ATOM   423  C  CD1 . LEU   A 1 58  ? 122.415 126.349 108.693 1.00 40.09 ? 58  LEU   A CD1 1 
ATOM   424  C  CD2 . LEU   A 1 58  ? 122.385 128.849 108.607 1.00 40.09 ? 58  LEU   A CD2 1 
ATOM   425  N  N   . LEU   A 1 59  ? 125.767 130.465 107.766 1.00 40.21 ? 59  LEU   A N   1 
ATOM   426  C  CA  . LEU   A 1 59  ? 125.516 131.899 107.708 1.00 40.22 ? 59  LEU   A CA  1 
ATOM   427  C  C   . LEU   A 1 59  ? 126.131 132.516 106.450 1.00 40.23 ? 59  LEU   A C   1 
ATOM   428  O  O   . LEU   A 1 59  ? 125.583 133.483 105.926 1.00 40.22 ? 59  LEU   A O   1 
ATOM   429  C  CB  . LEU   A 1 59  ? 126.025 132.602 108.970 1.00 40.21 ? 59  LEU   A CB  1 
ATOM   430  C  CG  . LEU   A 1 59  ? 125.131 132.527 110.218 1.00 40.19 ? 59  LEU   A CG  1 
ATOM   431  C  CD1 . LEU   A 1 59  ? 125.900 132.979 111.457 1.00 40.18 ? 59  LEU   A CD1 1 
ATOM   432  C  CD2 . LEU   A 1 59  ? 123.841 133.340 110.076 1.00 40.18 ? 59  LEU   A CD2 1 
ATOM   433  N  N   . LEU   A 1 60  ? 127.256 131.968 105.967 1.00 40.24 ? 60  LEU   A N   1 
ATOM   434  C  CA  . LEU   A 1 60  ? 127.917 132.518 104.789 1.00 40.26 ? 60  LEU   A CA  1 
ATOM   435  C  C   . LEU   A 1 60  ? 127.129 132.144 103.531 1.00 40.27 ? 60  LEU   A C   1 
ATOM   436  O  O   . LEU   A 1 60  ? 127.199 132.860 102.533 1.00 40.29 ? 60  LEU   A O   1 
ATOM   437  C  CB  . LEU   A 1 60  ? 129.385 132.080 104.711 1.00 40.28 ? 60  LEU   A CB  1 
ATOM   438  C  CG  . LEU   A 1 60  ? 129.704 130.700 104.114 1.00 40.30 ? 60  LEU   A CG  1 
ATOM   439  C  CD1 . LEU   A 1 60  ? 129.856 130.723 102.590 1.00 40.29 ? 60  LEU   A CD1 1 
ATOM   440  C  CD2 . LEU   A 1 60  ? 130.962 130.115 104.753 1.00 40.31 ? 60  LEU   A CD2 1 
ATOM   441  N  N   . LEU   A 1 61  ? 126.386 131.026 103.586 1.00 40.25 ? 61  LEU   A N   1 
ATOM   442  C  CA  . LEU   A 1 61  ? 125.613 130.537 102.453 1.00 40.24 ? 61  LEU   A CA  1 
ATOM   443  C  C   . LEU   A 1 61  ? 124.160 131.009 102.563 1.00 40.23 ? 61  LEU   A C   1 
ATOM   444  O  O   . LEU   A 1 61  ? 123.399 130.905 101.603 1.00 40.26 ? 61  LEU   A O   1 
ATOM   445  C  CB  . LEU   A 1 61  ? 125.764 129.012 102.431 1.00 40.23 ? 61  LEU   A CB  1 
ATOM   446  C  CG  . LEU   A 1 61  ? 125.371 128.238 101.160 1.00 40.23 ? 61  LEU   A CG  1 
ATOM   447  C  CD1 . LEU   A 1 61  ? 123.924 127.748 101.222 1.00 40.22 ? 61  LEU   A CD1 1 
ATOM   448  C  CD2 . LEU   A 1 61  ? 125.615 128.995 99.849  1.00 40.24 ? 61  LEU   A CD2 1 
ATOM   449  N  N   . LEU   A 1 62  ? 123.807 131.588 103.722 1.00 40.23 ? 62  LEU   A N   1 
ATOM   450  C  CA  . LEU   A 1 62  ? 122.463 132.078 104.002 1.00 40.25 ? 62  LEU   A CA  1 
ATOM   451  C  C   . LEU   A 1 62  ? 122.005 133.086 102.940 1.00 40.27 ? 62  LEU   A C   1 
ATOM   452  O  O   . LEU   A 1 62  ? 120.887 132.950 102.448 1.00 40.30 ? 62  LEU   A O   1 
ATOM   453  C  CB  . LEU   A 1 62  ? 122.428 132.672 105.416 1.00 40.25 ? 62  LEU   A CB  1 
ATOM   454  C  CG  . LEU   A 1 62  ? 121.088 132.709 106.170 1.00 40.26 ? 62  LEU   A CG  1 
ATOM   455  C  CD1 . LEU   A 1 62  ? 120.080 133.692 105.578 1.00 40.27 ? 62  LEU   A CD1 1 
ATOM   456  C  CD2 . LEU   A 1 62  ? 120.454 131.325 106.317 1.00 40.26 ? 62  LEU   A CD2 1 
ATOM   457  N  N   . PRO   A 1 63  ? 122.804 134.109 102.530 1.00 40.27 ? 63  PRO   A N   1 
ATOM   458  C  CA  . PRO   A 1 63  ? 122.304 135.165 101.640 1.00 40.28 ? 63  PRO   A CA  1 
ATOM   459  C  C   . PRO   A 1 63  ? 121.599 134.667 100.376 1.00 40.30 ? 63  PRO   A C   1 
ATOM   460  O  O   . PRO   A 1 63  ? 120.695 135.336 99.876  1.00 40.39 ? 63  PRO   A O   1 
ATOM   461  C  CB  . PRO   A 1 63  ? 123.558 135.965 101.240 1.00 40.27 ? 63  PRO   A CB  1 
ATOM   462  C  CG  . PRO   A 1 63  ? 124.723 135.092 101.652 1.00 40.27 ? 63  PRO   A CG  1 
ATOM   463  C  CD  . PRO   A 1 63  ? 124.222 134.331 102.860 1.00 40.27 ? 63  PRO   A CD  1 
ATOM   464  N  N   . PHE   A 1 64  ? 122.010 133.494 99.873  1.00 40.29 ? 64  PHE   A N   1 
ATOM   465  C  CA  . PHE   A 1 64  ? 121.357 132.874 98.728  1.00 40.28 ? 64  PHE   A CA  1 
ATOM   466  C  C   . PHE   A 1 64  ? 119.841 132.926 98.915  1.00 40.29 ? 64  PHE   A C   1 
ATOM   467  O  O   . PHE   A 1 64  ? 119.120 133.256 97.977  1.00 40.30 ? 64  PHE   A O   1 
ATOM   468  C  CB  . PHE   A 1 64  ? 121.830 131.430 98.514  1.00 40.26 ? 64  PHE   A CB  1 
ATOM   469  C  CG  . PHE   A 1 64  ? 123.119 131.250 97.716  1.00 40.26 ? 64  PHE   A CG  1 
ATOM   470  C  CD1 . PHE   A 1 64  ? 123.247 130.194 96.815  1.00 40.27 ? 64  PHE   A CD1 1 
ATOM   471  C  CD2 . PHE   A 1 64  ? 124.204 132.114 97.869  1.00 40.27 ? 64  PHE   A CD2 1 
ATOM   472  C  CE1 . PHE   A 1 64  ? 124.413 130.018 96.084  1.00 40.29 ? 64  PHE   A CE1 1 
ATOM   473  C  CE2 . PHE   A 1 64  ? 125.368 131.931 97.135  1.00 40.28 ? 64  PHE   A CE2 1 
ATOM   474  C  CZ  . PHE   A 1 64  ? 125.471 130.884 96.246  1.00 40.29 ? 64  PHE   A CZ  1 
ATOM   475  N  N   . LYS   A 1 65  ? 119.378 132.624 100.137 1.00 40.32 ? 65  LYS   A N   1 
ATOM   476  C  CA  . LYS   A 1 65  ? 117.957 132.530 100.437 1.00 40.39 ? 65  LYS   A CA  1 
ATOM   477  C  C   . LYS   A 1 65  ? 117.282 133.896 100.312 1.00 40.45 ? 65  LYS   A C   1 
ATOM   478  O  O   . LYS   A 1 65  ? 116.162 133.971 99.808  1.00 40.50 ? 65  LYS   A O   1 
ATOM   479  C  CB  . LYS   A 1 65  ? 117.744 131.915 101.826 1.00 40.38 ? 65  LYS   A CB  1 
ATOM   480  C  CG  . LYS   A 1 65  ? 116.332 131.397 102.098 1.00 40.37 ? 65  LYS   A CG  1 
ATOM   481  C  CD  . LYS   A 1 65  ? 116.262 130.102 102.903 1.00 40.36 ? 65  LYS   A CD  1 
ATOM   482  C  CE  . LYS   A 1 65  ? 116.276 128.852 102.068 1.00 40.35 ? 65  LYS   A CE  1 
ATOM   483  N  NZ  . LYS   A 1 65  ? 117.324 128.786 101.044 1.00 40.36 ? 65  LYS   A NZ  1 
ATOM   484  N  N   . ILE   A 1 66  ? 117.961 134.970 100.748 1.00 40.48 ? 66  ILE   A N   1 
ATOM   485  C  CA  . ILE   A 1 66  ? 117.363 136.301 100.717 1.00 40.52 ? 66  ILE   A CA  1 
ATOM   486  C  C   . ILE   A 1 66  ? 117.156 136.680 99.249  1.00 40.52 ? 66  ILE   A C   1 
ATOM   487  O  O   . ILE   A 1 66  ? 116.139 137.279 98.905  1.00 40.55 ? 66  ILE   A O   1 
ATOM   488  C  CB  . ILE   A 1 66  ? 118.172 137.365 101.508 1.00 40.53 ? 66  ILE   A CB  1 
ATOM   489  C  CG1 . ILE   A 1 66  ? 119.238 138.124 100.671 1.00 40.55 ? 66  ILE   A CG1 1 
ATOM   490  C  CG2 . ILE   A 1 66  ? 118.785 136.775 102.783 1.00 40.54 ? 66  ILE   A CG2 1 
ATOM   491  C  CD1 . ILE   A 1 66  ? 118.728 139.377 99.975  1.00 40.57 ? 66  ILE   A CD1 1 
ATOM   492  N  N   . ILE   A 1 67  ? 118.110 136.287 98.393  1.00 40.51 ? 67  ILE   A N   1 
ATOM   493  C  CA  . ILE   A 1 67  ? 118.046 136.576 96.967  1.00 40.55 ? 67  ILE   A CA  1 
ATOM   494  C  C   . ILE   A 1 67  ? 116.852 135.823 96.376  1.00 40.57 ? 67  ILE   A C   1 
ATOM   495  O  O   . ILE   A 1 67  ? 116.117 136.382 95.562  1.00 40.60 ? 67  ILE   A O   1 
ATOM   496  C  CB  . ILE   A 1 67  ? 119.383 136.233 96.271  1.00 40.58 ? 67  ILE   A CB  1 
ATOM   497  C  CG1 . ILE   A 1 67  ? 120.542 137.112 96.802  1.00 40.60 ? 67  ILE   A CG1 1 
ATOM   498  C  CG2 . ILE   A 1 67  ? 119.257 136.318 94.745  1.00 40.59 ? 67  ILE   A CG2 1 
ATOM   499  C  CD1 . ILE   A 1 67  ? 121.939 136.586 96.506  1.00 40.61 ? 67  ILE   A CD1 1 
ATOM   500  N  N   . GLU   A 1 68  ? 116.646 134.573 96.816  1.00 40.57 ? 68  GLU   A N   1 
ATOM   501  C  CA  . GLU   A 1 68  ? 115.534 133.760 96.341  1.00 40.60 ? 68  GLU   A CA  1 
ATOM   502  C  C   . GLU   A 1 68  ? 114.211 134.425 96.713  1.00 40.60 ? 68  GLU   A C   1 
ATOM   503  O  O   . GLU   A 1 68  ? 113.330 134.573 95.865  1.00 40.66 ? 68  GLU   A O   1 
ATOM   504  C  CB  . GLU   A 1 68  ? 115.480 132.345 96.921  1.00 40.61 ? 68  GLU   A CB  1 
ATOM   505  C  CG  . GLU   A 1 68  ? 116.784 131.559 96.828  1.00 40.62 ? 68  GLU   A CG  1 
ATOM   506  C  CD  . GLU   A 1 68  ? 116.568 130.073 96.643  1.00 40.64 ? 68  GLU   A CD  1 
ATOM   507  O  OE1 . GLU   A 1 68  ? 117.127 129.515 95.677  1.00 40.65 ? 68  GLU   A OE1 1 
ATOM   508  O  OE2 . GLU   A 1 68  ? 115.829 129.482 97.460  1.00 40.64 ? 68  GLU   A OE2 1 
ATOM   509  N  N   . ALA   A 1 69  ? 114.095 134.828 97.987  1.00 40.60 ? 69  ALA   A N   1 
ATOM   510  C  CA  . ALA   A 1 69  ? 112.843 135.315 98.545  1.00 40.62 ? 69  ALA   A CA  1 
ATOM   511  C  C   . ALA   A 1 69  ? 112.376 136.572 97.811  1.00 40.63 ? 69  ALA   A C   1 
ATOM   512  O  O   . ALA   A 1 69  ? 111.177 136.841 97.758  1.00 40.63 ? 69  ALA   A O   1 
ATOM   513  C  CB  . ALA   A 1 69  ? 113.009 135.565 100.028 1.00 40.65 ? 69  ALA   A CB  1 
ATOM   514  N  N   . ALA   A 1 70  ? 113.329 137.335 97.255  1.00 40.64 ? 70  ALA   A N   1 
ATOM   515  C  CA  . ALA   A 1 70  ? 113.015 138.493 96.432  1.00 40.67 ? 70  ALA   A CA  1 
ATOM   516  C  C   . ALA   A 1 70  ? 112.353 138.056 95.126  1.00 40.68 ? 70  ALA   A C   1 
ATOM   517  O  O   . ALA   A 1 70  ? 111.337 138.624 94.730  1.00 40.67 ? 70  ALA   A O   1 
ATOM   518  C  CB  . ALA   A 1 70  ? 114.269 139.297 96.155  1.00 40.67 ? 70  ALA   A CB  1 
ATOM   519  N  N   . SER   A 1 71  ? 112.933 137.034 94.479  1.00 40.70 ? 71  SER   A N   1 
ATOM   520  C  CA  . SER   A 1 71  ? 112.596 136.689 93.106  1.00 40.73 ? 71  SER   A CA  1 
ATOM   521  C  C   . SER   A 1 71  ? 111.587 135.541 93.048  1.00 40.75 ? 71  SER   A C   1 
ATOM   522  O  O   . SER   A 1 71  ? 111.533 134.828 92.047  1.00 40.75 ? 71  SER   A O   1 
ATOM   523  C  CB  . SER   A 1 71  ? 113.847 136.356 92.322  1.00 40.74 ? 71  SER   A CB  1 
ATOM   524  O  OG  . SER   A 1 71  ? 114.772 137.435 92.351  1.00 40.73 ? 71  SER   A OG  1 
ATOM   525  N  N   . ASN   A 1 72  ? 110.788 135.363 94.113  1.00 40.75 ? 72  ASN   A N   1 
ATOM   526  C  CA  . ASN   A 1 72  ? 109.688 134.407 94.113  1.00 40.78 ? 72  ASN   A CA  1 
ATOM   527  C  C   . ASN   A 1 72  ? 110.224 133.026 93.717  1.00 40.77 ? 72  ASN   A C   1 
ATOM   528  O  O   . ASN   A 1 72  ? 109.523 132.239 93.083  1.00 40.77 ? 72  ASN   A O   1 
ATOM   529  C  CB  . ASN   A 1 72  ? 108.522 134.965 93.292  1.00 40.81 ? 72  ASN   A CB  1 
ATOM   530  C  CG  . ASN   A 1 72  ? 107.655 133.907 92.649  1.00 40.83 ? 72  ASN   A CG  1 
ATOM   531  O  OD1 . ASN   A 1 72  ? 106.671 133.460 93.248  1.00 40.84 ? 72  ASN   A OD1 1 
ATOM   532  N  ND2 . ASN   A 1 72  ? 107.998 133.495 91.436  1.00 40.83 ? 72  ASN   A ND2 1 
ATOM   533  N  N   . PHE   A 1 73  ? 111.464 132.732 94.140  1.00 40.75 ? 73  PHE   A N   1 
ATOM   534  C  CA  . PHE   A 1 73  ? 112.171 131.514 93.769  1.00 40.73 ? 73  PHE   A CA  1 
ATOM   535  C  C   . PHE   A 1 73  ? 112.031 131.272 92.266  1.00 40.73 ? 73  PHE   A C   1 
ATOM   536  O  O   . PHE   A 1 73  ? 111.492 130.247 91.850  1.00 40.78 ? 73  PHE   A O   1 
ATOM   537  C  CB  . PHE   A 1 73  ? 111.645 130.357 94.627  1.00 40.72 ? 73  PHE   A CB  1 
ATOM   538  N  N   . ARG   A 1 74  ? 112.530 132.224 91.462  1.00 40.74 ? 74  ARG   A N   1 
ATOM   539  C  CA  . ARG   A 1 74  ? 112.413 132.166 90.011  1.00 40.75 ? 74  ARG   A CA  1 
ATOM   540  C  C   . ARG   A 1 74  ? 113.748 131.758 89.389  1.00 40.77 ? 74  ARG   A C   1 
ATOM   541  O  O   . ARG   A 1 74  ? 113.789 130.811 88.605  1.00 40.79 ? 74  ARG   A O   1 
ATOM   542  C  CB  . ARG   A 1 74  ? 111.938 133.502 89.427  1.00 40.75 ? 74  ARG   A CB  1 
ATOM   543  N  N   . TRP   A 1 75  ? 114.825 132.485 89.729  1.00 40.76 ? 75  TRP   A N   1 
ATOM   544  C  CA  . TRP   A 1 75  ? 116.141 132.249 89.150  1.00 40.75 ? 75  TRP   A CA  1 
ATOM   545  C  C   . TRP   A 1 75  ? 116.467 130.754 89.187  1.00 40.72 ? 75  TRP   A C   1 
ATOM   546  O  O   . TRP   A 1 75  ? 116.408 130.126 90.243  1.00 40.71 ? 75  TRP   A O   1 
ATOM   547  C  CB  . TRP   A 1 75  ? 117.218 133.091 89.860  1.00 40.76 ? 75  TRP   A CB  1 
ATOM   548  C  CG  . TRP   A 1 75  ? 117.497 132.737 91.300  1.00 40.77 ? 75  TRP   A CG  1 
ATOM   549  C  CD1 . TRP   A 1 75  ? 116.630 132.225 92.221  1.00 40.77 ? 75  TRP   A CD1 1 
ATOM   550  C  CD2 . TRP   A 1 75  ? 118.759 132.895 91.989  1.00 40.77 ? 75  TRP   A CD2 1 
ATOM   551  N  NE1 . TRP   A 1 75  ? 117.260 132.042 93.421  1.00 40.77 ? 75  TRP   A NE1 1 
ATOM   552  C  CE2 . TRP   A 1 75  ? 118.564 132.446 93.315  1.00 40.76 ? 75  TRP   A CE2 1 
ATOM   553  C  CE3 . TRP   A 1 75  ? 120.026 133.366 91.619  1.00 40.77 ? 75  TRP   A CE3 1 
ATOM   554  C  CZ2 . TRP   A 1 75  ? 119.587 132.455 94.262  1.00 40.75 ? 75  TRP   A CZ2 1 
ATOM   555  C  CZ3 . TRP   A 1 75  ? 121.035 133.375 92.558  1.00 40.76 ? 75  TRP   A CZ3 1 
ATOM   556  C  CH2 . TRP   A 1 75  ? 120.817 132.926 93.861  1.00 40.75 ? 75  TRP   A CH2 1 
ATOM   557  N  N   . TYR   A 1 76  ? 116.780 130.192 88.011  1.00 40.71 ? 76  TYR   A N   1 
ATOM   558  C  CA  . TYR   A 1 76  ? 116.998 128.762 87.860  1.00 40.71 ? 76  TYR   A CA  1 
ATOM   559  C  C   . TYR   A 1 76  ? 118.488 128.465 88.019  1.00 40.71 ? 76  TYR   A C   1 
ATOM   560  O  O   . TYR   A 1 76  ? 119.311 129.031 87.301  1.00 40.72 ? 76  TYR   A O   1 
ATOM   561  C  CB  . TYR   A 1 76  ? 116.466 128.286 86.504  1.00 40.70 ? 76  TYR   A CB  1 
ATOM   562  N  N   . LEU   A 1 77  ? 118.816 127.575 88.966  1.00 40.71 ? 77  LEU   A N   1 
ATOM   563  C  CA  . LEU   A 1 77  ? 120.191 127.178 89.226  1.00 40.70 ? 77  LEU   A CA  1 
ATOM   564  C  C   . LEU   A 1 77  ? 120.425 125.789 88.633  1.00 40.68 ? 77  LEU   A C   1 
ATOM   565  O  O   . LEU   A 1 77  ? 119.512 124.965 88.631  1.00 40.68 ? 77  LEU   A O   1 
ATOM   566  C  CB  . LEU   A 1 77  ? 120.501 127.190 90.727  1.00 40.70 ? 77  LEU   A CB  1 
ATOM   567  C  CG  . LEU   A 1 77  ? 120.687 128.548 91.423  1.00 40.71 ? 77  LEU   A CG  1 
ATOM   568  C  CD1 . LEU   A 1 77  ? 121.791 129.403 90.791  1.00 40.71 ? 77  LEU   A CD1 1 
ATOM   569  C  CD2 . LEU   A 1 77  ? 119.386 129.345 91.527  1.00 40.70 ? 77  LEU   A CD2 1 
ATOM   570  N  N   . PRO   A 1 78  ? 121.636 125.484 88.101  1.00 40.67 ? 78  PRO   A N   1 
ATOM   571  C  CA  . PRO   A 1 78  ? 121.978 124.117 87.698  1.00 40.66 ? 78  PRO   A CA  1 
ATOM   572  C  C   . PRO   A 1 78  ? 121.811 123.097 88.823  1.00 40.63 ? 78  PRO   A C   1 
ATOM   573  O  O   . PRO   A 1 78  ? 121.972 123.431 89.998  1.00 40.56 ? 78  PRO   A O   1 
ATOM   574  C  CB  . PRO   A 1 78  ? 123.459 124.208 87.296  1.00 40.67 ? 78  PRO   A CB  1 
ATOM   575  C  CG  . PRO   A 1 78  ? 123.651 125.655 86.898  1.00 40.67 ? 78  PRO   A CG  1 
ATOM   576  C  CD  . PRO   A 1 78  ? 122.721 126.436 87.802  1.00 40.67 ? 78  PRO   A CD  1 
ATOM   577  N  N   . LYS   A 1 79  ? 121.514 121.847 88.437  1.00 40.61 ? 79  LYS   A N   1 
ATOM   578  C  CA  . LYS   A 1 79  ? 121.261 120.763 89.376  1.00 40.60 ? 79  LYS   A CA  1 
ATOM   579  C  C   . LYS   A 1 79  ? 122.458 120.565 90.305  1.00 40.59 ? 79  LYS   A C   1 
ATOM   580  O  O   . LYS   A 1 79  ? 122.279 120.187 91.461  1.00 40.59 ? 79  LYS   A O   1 
ATOM   581  C  CB  . LYS   A 1 79  ? 120.951 119.459 88.630  1.00 40.60 ? 79  LYS   A CB  1 
ATOM   582  N  N   . VAL   A 1 80  ? 123.670 120.814 89.788  1.00 40.57 ? 80  VAL   A N   1 
ATOM   583  C  CA  . VAL   A 1 80  ? 124.892 120.725 90.576  1.00 40.54 ? 80  VAL   A CA  1 
ATOM   584  C  C   . VAL   A 1 80  ? 124.844 121.793 91.671  1.00 40.51 ? 80  VAL   A C   1 
ATOM   585  O  O   . VAL   A 1 80  ? 125.024 121.476 92.847  1.00 40.45 ? 80  VAL   A O   1 
ATOM   586  C  CB  . VAL   A 1 80  ? 126.165 120.853 89.708  1.00 40.56 ? 80  VAL   A CB  1 
ATOM   587  C  CG1 . VAL   A 1 80  ? 127.440 120.936 90.546  1.00 40.56 ? 80  VAL   A CG1 1 
ATOM   588  C  CG2 . VAL   A 1 80  ? 126.277 119.728 88.679  1.00 40.56 ? 80  VAL   A CG2 1 
ATOM   589  N  N   . VAL   A 1 81  ? 124.574 123.047 91.278  1.00 40.50 ? 81  VAL   A N   1 
ATOM   590  C  CA  . VAL   A 1 81  ? 124.565 124.172 92.205  1.00 40.49 ? 81  VAL   A CA  1 
ATOM   591  C  C   . VAL   A 1 81  ? 123.496 123.915 93.269  1.00 40.47 ? 81  VAL   A C   1 
ATOM   592  O  O   . VAL   A 1 81  ? 123.749 124.103 94.459  1.00 40.40 ? 81  VAL   A O   1 
ATOM   593  C  CB  . VAL   A 1 81  ? 124.346 125.528 91.494  1.00 40.52 ? 81  VAL   A CB  1 
ATOM   594  C  CG1 . VAL   A 1 81  ? 124.175 126.686 92.477  1.00 40.52 ? 81  VAL   A CG1 1 
ATOM   595  C  CG2 . VAL   A 1 81  ? 125.458 125.842 90.493  1.00 40.53 ? 81  VAL   A CG2 1 
ATOM   596  N  N   . CYS   A 1 82  ? 122.313 123.469 92.822  1.00 40.48 ? 82  CYS   A N   1 
ATOM   597  C  CA  . CYS   A 1 82  ? 121.201 123.143 93.704  1.00 40.46 ? 82  CYS   A CA  1 
ATOM   598  C  C   . CYS   A 1 82  ? 121.630 122.091 94.730  1.00 40.41 ? 82  CYS   A C   1 
ATOM   599  O  O   . CYS   A 1 82  ? 121.272 122.194 95.903  1.00 40.33 ? 82  CYS   A O   1 
ATOM   600  C  CB  . CYS   A 1 82  ? 119.994 122.682 92.891  1.00 40.50 ? 82  CYS   A CB  1 
ATOM   601  S  SG  . CYS   A 1 82  ? 118.453 122.598 93.839  1.00 40.55 ? 82  CYS   A SG  1 
ATOM   602  N  N   . ALA   A 1 83  ? 122.411 121.096 94.282  1.00 40.40 ? 83  ALA   A N   1 
ATOM   603  C  CA  . ALA   A 1 83  ? 122.852 120.000 95.136  1.00 40.37 ? 83  ALA   A CA  1 
ATOM   604  C  C   . ALA   A 1 83  ? 123.899 120.481 96.141  1.00 40.35 ? 83  ALA   A C   1 
ATOM   605  O  O   . ALA   A 1 83  ? 123.829 120.123 97.316  1.00 40.30 ? 83  ALA   A O   1 
ATOM   606  C  CB  . ALA   A 1 83  ? 123.386 118.861 94.290  1.00 40.37 ? 83  ALA   A CB  1 
ATOM   607  N  N   . LEU   A 1 84  ? 124.867 121.281 95.670  1.00 40.35 ? 84  LEU   A N   1 
ATOM   608  C  CA  . LEU   A 1 84  ? 125.951 121.774 96.511  1.00 40.32 ? 84  LEU   A CA  1 
ATOM   609  C  C   . LEU   A 1 84  ? 125.380 122.592 97.669  1.00 40.29 ? 84  LEU   A C   1 
ATOM   610  O  O   . LEU   A 1 84  ? 125.798 122.417 98.813  1.00 40.24 ? 84  LEU   A O   1 
ATOM   611  C  CB  . LEU   A 1 84  ? 126.947 122.604 95.695  1.00 40.33 ? 84  LEU   A CB  1 
ATOM   612  C  CG  . LEU   A 1 84  ? 127.866 121.844 94.727  1.00 40.35 ? 84  LEU   A CG  1 
ATOM   613  C  CD1 . LEU   A 1 84  ? 128.525 122.815 93.750  1.00 40.35 ? 84  LEU   A CD1 1 
ATOM   614  C  CD2 . LEU   A 1 84  ? 128.932 121.014 95.446  1.00 40.35 ? 84  LEU   A CD2 1 
ATOM   615  N  N   . THR   A 1 85  ? 124.424 123.478 97.357  1.00 40.27 ? 85  THR   A N   1 
ATOM   616  C  CA  . THR   A 1 85  ? 123.829 124.364 98.348  1.00 40.23 ? 85  THR   A CA  1 
ATOM   617  C  C   . THR   A 1 85  ? 123.005 123.550 99.346  1.00 40.20 ? 85  THR   A C   1 
ATOM   618  O  O   . THR   A 1 85  ? 123.060 123.818 100.547 1.00 40.14 ? 85  THR   A O   1 
ATOM   619  C  CB  . THR   A 1 85  ? 122.983 125.432 97.652  1.00 40.22 ? 85  THR   A CB  1 
ATOM   620  O  OG1 . THR   A 1 85  ? 122.159 124.719 96.735  1.00 40.22 ? 85  THR   A OG1 1 
ATOM   621  C  CG2 . THR   A 1 85  ? 123.815 126.468 96.915  1.00 40.23 ? 85  THR   A CG2 1 
ATOM   622  N  N   . SER   A 1 86  ? 122.249 122.560 98.846  1.00 40.21 ? 86  SER   A N   1 
ATOM   623  C  CA  . SER   A 1 86  ? 121.443 121.701 99.702  1.00 40.18 ? 86  SER   A CA  1 
ATOM   624  C  C   . SER   A 1 86  ? 122.340 120.942 100.680 1.00 40.15 ? 86  SER   A C   1 
ATOM   625  O  O   . SER   A 1 86  ? 122.058 120.911 101.878 1.00 40.09 ? 86  SER   A O   1 
ATOM   626  C  CB  . SER   A 1 86  ? 120.583 120.753 98.895  1.00 40.18 ? 86  SER   A CB  1 
ATOM   627  O  OG  . SER   A 1 86  ? 121.377 119.810 98.188  1.00 40.19 ? 86  SER   A OG  1 
ATOM   628  N  N   . PHE   A 1 87  ? 123.423 120.346 100.157 1.00 40.16 ? 87  PHE   A N   1 
ATOM   629  C  CA  . PHE   A 1 87  ? 124.393 119.629 100.972 1.00 40.14 ? 87  PHE   A CA  1 
ATOM   630  C  C   . PHE   A 1 87  ? 124.992 120.577 102.012 1.00 40.11 ? 87  PHE   A C   1 
ATOM   631  O  O   . PHE   A 1 87  ? 125.151 120.196 103.172 1.00 40.07 ? 87  PHE   A O   1 
ATOM   632  C  CB  . PHE   A 1 87  ? 125.475 119.003 100.085 1.00 40.17 ? 87  PHE   A CB  1 
ATOM   633  C  CG  . PHE   A 1 87  ? 126.566 118.251 100.838 1.00 40.18 ? 87  PHE   A CG  1 
ATOM   634  C  CD1 . PHE   A 1 87  ? 127.787 118.857 101.126 1.00 40.19 ? 87  PHE   A CD1 1 
ATOM   635  C  CD2 . PHE   A 1 87  ? 126.365 116.939 101.264 1.00 40.20 ? 87  PHE   A CD2 1 
ATOM   636  C  CE1 . PHE   A 1 87  ? 128.776 118.169 101.815 1.00 40.21 ? 87  PHE   A CE1 1 
ATOM   637  C  CE2 . PHE   A 1 87  ? 127.358 116.257 101.952 1.00 40.21 ? 87  PHE   A CE2 1 
ATOM   638  C  CZ  . PHE   A 1 87  ? 128.560 116.872 102.226 1.00 40.21 ? 87  PHE   A CZ  1 
ATOM   639  N  N   . GLY   A 1 88  ? 125.323 121.803 101.580 1.00 40.11 ? 88  GLY   A N   1 
ATOM   640  C  CA  . GLY   A 1 88  ? 125.856 122.831 102.460 1.00 40.06 ? 88  GLY   A CA  1 
ATOM   641  C  C   . GLY   A 1 88  ? 125.002 123.014 103.713 1.00 40.02 ? 88  GLY   A C   1 
ATOM   642  O  O   . GLY   A 1 88  ? 125.536 123.074 104.819 1.00 40.02 ? 88  GLY   A O   1 
ATOM   643  N  N   . PHE   A 1 89  ? 123.677 123.097 103.527 1.00 40.00 ? 89  PHE   A N   1 
ATOM   644  C  CA  . PHE   A 1 89  ? 122.749 123.287 104.633 1.00 39.95 ? 89  PHE   A CA  1 
ATOM   645  C  C   . PHE   A 1 89  ? 122.699 122.024 105.492 1.00 39.95 ? 89  PHE   A C   1 
ATOM   646  O  O   . PHE   A 1 89  ? 122.999 122.087 106.684 1.00 39.95 ? 89  PHE   A O   1 
ATOM   647  C  CB  . PHE   A 1 89  ? 121.368 123.690 104.103 1.00 39.93 ? 89  PHE   A CB  1 
ATOM   648  C  CG  . PHE   A 1 89  ? 120.225 123.595 105.108 1.00 39.90 ? 89  PHE   A CG  1 
ATOM   649  C  CD1 . PHE   A 1 89  ? 120.034 124.581 106.073 1.00 39.89 ? 89  PHE   A CD1 1 
ATOM   650  C  CD2 . PHE   A 1 89  ? 119.329 122.529 105.071 1.00 39.89 ? 89  PHE   A CD2 1 
ATOM   651  C  CE1 . PHE   A 1 89  ? 118.984 124.496 106.977 1.00 39.89 ? 89  PHE   A CE1 1 
ATOM   652  C  CE2 . PHE   A 1 89  ? 118.283 122.448 105.978 1.00 39.89 ? 89  PHE   A CE2 1 
ATOM   653  C  CZ  . PHE   A 1 89  ? 118.111 123.431 106.927 1.00 39.89 ? 89  PHE   A CZ  1 
ATOM   654  N  N   . TYR   A 1 90  ? 122.326 120.888 104.880 1.00 39.96 ? 90  TYR   A N   1 
ATOM   655  C  CA  . TYR   A 1 90  ? 122.125 119.639 105.604 1.00 39.93 ? 90  TYR   A CA  1 
ATOM   656  C  C   . TYR   A 1 90  ? 123.273 119.419 106.589 1.00 39.95 ? 90  TYR   A C   1 
ATOM   657  O  O   . TYR   A 1 90  ? 123.032 119.199 107.777 1.00 39.96 ? 90  TYR   A O   1 
ATOM   658  C  CB  . TYR   A 1 90  ? 122.005 118.438 104.656 1.00 39.89 ? 90  TYR   A CB  1 
ATOM   659  C  CG  . TYR   A 1 90  ? 120.749 118.363 103.792 1.00 39.86 ? 90  TYR   A CG  1 
ATOM   660  C  CD1 . TYR   A 1 90  ? 119.477 118.556 104.329 1.00 39.84 ? 90  TYR   A CD1 1 
ATOM   661  C  CD2 . TYR   A 1 90  ? 120.837 118.082 102.431 1.00 39.87 ? 90  TYR   A CD2 1 
ATOM   662  C  CE1 . TYR   A 1 90  ? 118.340 118.479 103.540 1.00 39.84 ? 90  TYR   A CE1 1 
ATOM   663  C  CE2 . TYR   A 1 90  ? 119.707 118.007 101.631 1.00 39.86 ? 90  TYR   A CE2 1 
ATOM   664  C  CZ  . TYR   A 1 90  ? 118.456 118.205 102.188 1.00 39.84 ? 90  TYR   A CZ  1 
ATOM   665  O  OH  . TYR   A 1 90  ? 117.339 118.130 101.406 1.00 39.84 ? 90  TYR   A OH  1 
ATOM   666  N  N   . SER   A 1 91  ? 124.514 119.499 106.083 1.00 39.96 ? 91  SER   A N   1 
ATOM   667  C  CA  . SER   A 1 91  ? 125.707 119.242 106.876 1.00 39.94 ? 91  SER   A CA  1 
ATOM   668  C  C   . SER   A 1 91  ? 125.655 120.002 108.202 1.00 39.92 ? 91  SER   A C   1 
ATOM   669  O  O   . SER   A 1 91  ? 125.834 119.402 109.260 1.00 39.92 ? 91  SER   A O   1 
ATOM   670  C  CB  . SER   A 1 91  ? 126.961 119.583 106.103 1.00 39.94 ? 91  SER   A CB  1 
ATOM   671  O  OG  . SER   A 1 91  ? 126.979 120.956 105.735 1.00 39.94 ? 91  SER   A OG  1 
ATOM   672  N  N   . SER   A 1 92  ? 125.386 121.314 108.130 1.00 39.92 ? 92  SER   A N   1 
ATOM   673  C  CA  . SER   A 1 92  ? 125.460 122.196 109.286 1.00 39.94 ? 92  SER   A CA  1 
ATOM   674  C  C   . SER   A 1 92  ? 124.507 121.738 110.390 1.00 39.94 ? 92  SER   A C   1 
ATOM   675  O  O   . SER   A 1 92  ? 124.910 121.643 111.549 1.00 39.94 ? 92  SER   A O   1 
ATOM   676  C  CB  . SER   A 1 92  ? 125.183 123.630 108.894 1.00 39.95 ? 92  SER   A CB  1 
ATOM   677  O  OG  . SER   A 1 92  ? 125.247 124.492 110.022 1.00 39.96 ? 92  SER   A OG  1 
ATOM   678  N  N   . ILE   A 1 93  ? 123.252 121.445 110.018 1.00 39.93 ? 93  ILE   A N   1 
ATOM   679  C  CA  . ILE   A 1 93  ? 122.192 121.190 110.985 1.00 39.93 ? 93  ILE   A CA  1 
ATOM   680  C  C   . ILE   A 1 93  ? 122.508 119.904 111.748 1.00 39.95 ? 93  ILE   A C   1 
ATOM   681  O  O   . ILE   A 1 93  ? 122.522 119.902 112.979 1.00 39.94 ? 93  ILE   A O   1 
ATOM   682  C  CB  . ILE   A 1 93  ? 120.807 121.125 110.300 1.00 39.91 ? 93  ILE   A CB  1 
ATOM   683  C  CG1 . ILE   A 1 93  ? 120.437 122.440 109.564 1.00 39.91 ? 93  ILE   A CG1 1 
ATOM   684  C  CG2 . ILE   A 1 93  ? 119.712 120.694 111.284 1.00 39.91 ? 93  ILE   A CG2 1 
ATOM   685  C  CD1 . ILE   A 1 93  ? 120.291 123.677 110.441 1.00 39.92 ? 93  ILE   A CD1 1 
ATOM   686  N  N   . TYR   A 1 94  ? 122.772 118.820 111.008 1.00 39.94 ? 94  TYR   A N   1 
ATOM   687  C  CA  . TYR   A 1 94  ? 122.881 117.494 111.597 1.00 39.92 ? 94  TYR   A CA  1 
ATOM   688  C  C   . TYR   A 1 94  ? 124.240 117.331 112.281 1.00 39.91 ? 94  TYR   A C   1 
ATOM   689  O  O   . TYR   A 1 94  ? 124.380 116.487 113.165 1.00 39.93 ? 94  TYR   A O   1 
ATOM   690  C  CB  . TYR   A 1 94  ? 122.562 116.470 110.501 1.00 39.91 ? 94  TYR   A CB  1 
ATOM   691  C  CG  . TYR   A 1 94  ? 121.128 116.546 109.984 1.00 39.89 ? 94  TYR   A CG  1 
ATOM   692  C  CD1 . TYR   A 1 94  ? 120.041 116.523 110.855 1.00 39.88 ? 94  TYR   A CD1 1 
ATOM   693  C  CD2 . TYR   A 1 94  ? 120.859 116.674 108.623 1.00 39.89 ? 94  TYR   A CD2 1 
ATOM   694  C  CE1 . TYR   A 1 94  ? 118.738 116.601 110.391 1.00 39.88 ? 94  TYR   A CE1 1 
ATOM   695  C  CE2 . TYR   A 1 94  ? 119.560 116.756 108.147 1.00 39.89 ? 94  TYR   A CE2 1 
ATOM   696  C  CZ  . TYR   A 1 94  ? 118.497 116.719 109.033 1.00 39.88 ? 94  TYR   A CZ  1 
ATOM   697  O  OH  . TYR   A 1 94  ? 117.215 116.799 108.570 1.00 39.89 ? 94  TYR   A OH  1 
ATOM   698  N  N   . CYS   A 1 95  ? 125.227 118.148 111.884 1.00 39.90 ? 95  CYS   A N   1 
ATOM   699  C  CA  . CYS   A 1 95  ? 126.470 118.261 112.634 1.00 39.90 ? 95  CYS   A CA  1 
ATOM   700  C  C   . CYS   A 1 95  ? 126.200 118.949 113.972 1.00 39.90 ? 95  CYS   A C   1 
ATOM   701  O  O   . CYS   A 1 95  ? 126.679 118.489 115.009 1.00 39.94 ? 95  CYS   A O   1 
ATOM   702  C  CB  . CYS   A 1 95  ? 127.537 119.019 111.852 1.00 39.89 ? 95  CYS   A CB  1 
ATOM   703  S  SG  . CYS   A 1 95  ? 129.149 119.049 112.678 1.00 39.87 ? 95  CYS   A SG  1 
ATOM   704  N  N   . SER   A 1 96  ? 125.422 120.042 113.936 1.00 39.89 ? 96  SER   A N   1 
ATOM   705  C  CA  . SER   A 1 96  ? 125.128 120.831 115.124 1.00 39.89 ? 96  SER   A CA  1 
ATOM   706  C  C   . SER   A 1 96  ? 124.420 119.983 116.181 1.00 39.90 ? 96  SER   A C   1 
ATOM   707  O  O   . SER   A 1 96  ? 124.749 120.083 117.361 1.00 39.94 ? 96  SER   A O   1 
ATOM   708  C  CB  . SER   A 1 96  ? 124.316 122.062 114.787 1.00 39.88 ? 96  SER   A CB  1 
ATOM   709  O  OG  . SER   A 1 96  ? 125.027 122.918 113.903 1.00 39.89 ? 96  SER   A OG  1 
ATOM   710  N  N   . THR   A 1 97  ? 123.459 119.151 115.752 1.00 39.89 ? 97  THR   A N   1 
ATOM   711  C  CA  . THR   A 1 97  ? 122.671 118.340 116.674 1.00 39.86 ? 97  THR   A CA  1 
ATOM   712  C  C   . THR   A 1 97  ? 123.597 117.430 117.484 1.00 39.89 ? 97  THR   A C   1 
ATOM   713  O  O   . THR   A 1 97  ? 123.498 117.394 118.710 1.00 39.94 ? 97  THR   A O   1 
ATOM   714  C  CB  . THR   A 1 97  ? 121.609 117.528 115.926 1.00 39.84 ? 97  THR   A CB  1 
ATOM   715  O  OG1 . THR   A 1 97  ? 122.298 116.858 114.874 1.00 39.84 ? 97  THR   A OG1 1 
ATOM   716  C  CG2 . THR   A 1 97  ? 120.489 118.383 115.357 1.00 39.83 ? 97  THR   A CG2 1 
ATOM   717  N  N   . TRP   A 1 98  ? 124.495 116.708 116.796 1.00 39.93 ? 98  TRP   A N   1 
ATOM   718  C  CA  . TRP   A 1 98  ? 125.395 115.772 117.458 1.00 39.96 ? 98  TRP   A CA  1 
ATOM   719  C  C   . TRP   A 1 98  ? 126.440 116.511 118.295 1.00 39.96 ? 98  TRP   A C   1 
ATOM   720  O  O   . TRP   A 1 98  ? 126.886 115.982 119.312 1.00 40.00 ? 98  TRP   A O   1 
ATOM   721  C  CB  . TRP   A 1 98  ? 126.071 114.834 116.444 1.00 39.99 ? 98  TRP   A CB  1 
ATOM   722  C  CG  . TRP   A 1 98  ? 125.347 113.532 116.210 1.00 40.02 ? 98  TRP   A CG  1 
ATOM   723  C  CD1 . TRP   A 1 98  ? 124.998 113.007 115.001 1.00 40.04 ? 98  TRP   A CD1 1 
ATOM   724  C  CD2 . TRP   A 1 98  ? 124.922 112.567 117.202 1.00 40.02 ? 98  TRP   A CD2 1 
ATOM   725  N  NE1 . TRP   A 1 98  ? 124.366 111.804 115.166 1.00 40.04 ? 98  TRP   A NE1 1 
ATOM   726  C  CE2 . TRP   A 1 98  ? 124.308 111.504 116.501 1.00 40.03 ? 98  TRP   A CE2 1 
ATOM   727  C  CE3 . TRP   A 1 98  ? 124.990 112.496 118.600 1.00 40.03 ? 98  TRP   A CE3 1 
ATOM   728  C  CZ2 . TRP   A 1 98  ? 123.772 110.393 117.150 1.00 40.03 ? 98  TRP   A CZ2 1 
ATOM   729  C  CZ3 . TRP   A 1 98  ? 124.460 111.396 119.240 1.00 40.03 ? 98  TRP   A CZ3 1 
ATOM   730  C  CH2 . TRP   A 1 98  ? 123.861 110.360 118.524 1.00 40.04 ? 98  TRP   A CH2 1 
ATOM   731  N  N   . LEU   A 1 99  ? 126.836 117.718 117.864 1.00 39.94 ? 99  LEU   A N   1 
ATOM   732  C  CA  . LEU   A 1 99  ? 127.758 118.538 118.639 1.00 39.94 ? 99  LEU   A CA  1 
ATOM   733  C  C   . LEU   A 1 99  ? 127.087 118.965 119.945 1.00 39.96 ? 99  LEU   A C   1 
ATOM   734  O  O   . LEU   A 1 99  ? 127.706 118.880 121.003 1.00 40.02 ? 99  LEU   A O   1 
ATOM   735  C  CB  . LEU   A 1 99  ? 128.248 119.752 117.845 1.00 39.92 ? 99  LEU   A CB  1 
ATOM   736  C  CG  . LEU   A 1 99  ? 129.323 119.499 116.779 1.00 39.92 ? 99  LEU   A CG  1 
ATOM   737  C  CD1 . LEU   A 1 99  ? 129.480 120.734 115.897 1.00 39.93 ? 99  LEU   A CD1 1 
ATOM   738  C  CD2 . LEU   A 1 99  ? 130.678 119.097 117.366 1.00 39.94 ? 99  LEU   A CD2 1 
ATOM   739  N  N   . LEU   A 1 100 ? 125.825 119.410 119.862 1.00 39.96 ? 100 LEU   A N   1 
ATOM   740  C  CA  . LEU   A 1 100 ? 125.069 119.831 121.035 1.00 39.97 ? 100 LEU   A CA  1 
ATOM   741  C  C   . LEU   A 1 100 ? 124.875 118.645 121.980 1.00 39.98 ? 100 LEU   A C   1 
ATOM   742  O  O   . LEU   A 1 100 ? 124.930 118.814 123.198 1.00 40.04 ? 100 LEU   A O   1 
ATOM   743  C  CB  . LEU   A 1 100 ? 123.731 120.452 120.626 1.00 39.96 ? 100 LEU   A CB  1 
ATOM   744  C  CG  . LEU   A 1 100 ? 123.783 121.842 119.973 1.00 39.97 ? 100 LEU   A CG  1 
ATOM   745  C  CD1 . LEU   A 1 100 ? 122.477 122.148 119.244 1.00 39.97 ? 100 LEU   A CD1 1 
ATOM   746  C  CD2 . LEU   A 1 100 ? 124.101 122.956 120.970 1.00 39.98 ? 100 LEU   A CD2 1 
ATOM   747  N  N   . ALA   A 1 101 ? 124.651 117.451 121.411 1.00 39.99 ? 101 ALA   A N   1 
ATOM   748  C  CA  . ALA   A 1 101 ? 124.587 116.222 122.189 1.00 40.02 ? 101 ALA   A CA  1 
ATOM   749  C  C   . ALA   A 1 101 ? 125.938 115.947 122.851 1.00 40.05 ? 101 ALA   A C   1 
ATOM   750  O  O   . ALA   A 1 101 ? 125.986 115.559 124.017 1.00 40.11 ? 101 ALA   A O   1 
ATOM   751  C  CB  . ALA   A 1 101 ? 124.154 115.066 121.309 1.00 40.02 ? 101 ALA   A CB  1 
ATOM   752  N  N   . GLY   A 1 102 ? 127.029 116.151 122.098 1.00 40.06 ? 102 GLY   A N   1 
ATOM   753  C  CA  . GLY   A 1 102 ? 128.380 115.998 122.616 1.00 40.09 ? 102 GLY   A CA  1 
ATOM   754  C  C   . GLY   A 1 102 ? 128.662 116.953 123.775 1.00 40.10 ? 102 GLY   A C   1 
ATOM   755  O  O   . GLY   A 1 102 ? 129.353 116.584 124.723 1.00 40.17 ? 102 GLY   A O   1 
ATOM   756  N  N   . ILE   A 1 103 ? 128.127 118.179 123.683 1.00 40.08 ? 103 ILE   A N   1 
ATOM   757  C  CA  . ILE   A 1 103 ? 128.267 119.174 124.738 1.00 40.08 ? 103 ILE   A CA  1 
ATOM   758  C  C   . ILE   A 1 103 ? 127.491 118.695 125.966 1.00 40.11 ? 103 ILE   A C   1 
ATOM   759  O  O   . ILE   A 1 103 ? 128.017 118.739 127.077 1.00 40.17 ? 103 ILE   A O   1 
ATOM   760  C  CB  . ILE   A 1 103 ? 127.815 120.571 124.256 1.00 40.06 ? 103 ILE   A CB  1 
ATOM   761  C  CG1 . ILE   A 1 103 ? 128.738 121.111 123.141 1.00 40.06 ? 103 ILE   A CG1 1 
ATOM   762  C  CG2 . ILE   A 1 103 ? 127.703 121.557 125.426 1.00 40.06 ? 103 ILE   A CG2 1 
ATOM   763  C  CD1 . ILE   A 1 103 ? 128.137 122.219 122.289 1.00 40.06 ? 103 ILE   A CD1 1 
ATOM   764  N  N   . SER   A 1 104 ? 126.252 118.223 125.755 1.00 40.14 ? 104 SER   A N   1 
ATOM   765  C  CA  . SER   A 1 104 ? 125.429 117.699 126.836 1.00 40.20 ? 104 SER   A CA  1 
ATOM   766  C  C   . SER   A 1 104 ? 126.172 116.582 127.571 1.00 40.22 ? 104 SER   A C   1 
ATOM   767  O  O   . SER   A 1 104 ? 126.175 116.548 128.802 1.00 40.27 ? 104 SER   A O   1 
ATOM   768  C  CB  . SER   A 1 104 ? 124.084 117.225 126.331 1.00 40.23 ? 104 SER   A CB  1 
ATOM   769  O  OG  . SER   A 1 104 ? 124.196 116.007 125.609 1.00 40.25 ? 104 SER   A OG  1 
ATOM   770  N  N   . ILE   A 1 105 ? 126.799 115.678 126.802 1.00 40.20 ? 105 ILE   A N   1 
ATOM   771  C  CA  . ILE   A 1 105 ? 127.648 114.631 127.355 1.00 40.24 ? 105 ILE   A CA  1 
ATOM   772  C  C   . ILE   A 1 105 ? 128.770 115.279 128.168 1.00 40.27 ? 105 ILE   A C   1 
ATOM   773  O  O   . ILE   A 1 105 ? 128.984 114.908 129.321 1.00 40.32 ? 105 ILE   A O   1 
ATOM   774  C  CB  . ILE   A 1 105 ? 128.196 113.706 126.242 1.00 40.25 ? 105 ILE   A CB  1 
ATOM   775  C  CG1 . ILE   A 1 105 ? 127.094 112.820 125.600 1.00 40.25 ? 105 ILE   A CG1 1 
ATOM   776  C  CG2 . ILE   A 1 105 ? 129.385 112.870 126.734 1.00 40.26 ? 105 ILE   A CG2 1 
ATOM   777  C  CD1 . ILE   A 1 105 ? 126.579 111.672 126.457 1.00 40.26 ? 105 ILE   A CD1 1 
ATOM   778  N  N   . GLU   A 1 106 ? 129.466 116.254 127.563 1.00 40.27 ? 106 GLU   A N   1 
ATOM   779  C  CA  . GLU   A 1 106 ? 130.669 116.834 128.146 1.00 40.30 ? 106 GLU   A CA  1 
ATOM   780  C  C   . GLU   A 1 106 ? 130.352 117.465 129.502 1.00 40.29 ? 106 GLU   A C   1 
ATOM   781  O  O   . GLU   A 1 106 ? 131.088 117.243 130.460 1.00 40.35 ? 106 GLU   A O   1 
ATOM   782  C  CB  . GLU   A 1 106 ? 131.310 117.854 127.200 1.00 40.31 ? 106 GLU   A CB  1 
ATOM   783  C  CG  . GLU   A 1 106 ? 132.769 118.177 127.522 1.00 40.32 ? 106 GLU   A CG  1 
ATOM   784  C  CD  . GLU   A 1 106 ? 133.037 119.059 128.732 1.00 40.32 ? 106 GLU   A CD  1 
ATOM   785  O  OE1 . GLU   A 1 106 ? 134.196 119.051 129.198 1.00 40.33 ? 106 GLU   A OE1 1 
ATOM   786  O  OE2 . GLU   A 1 106 ? 132.123 119.777 129.192 1.00 40.32 ? 106 GLU   A OE2 1 
ATOM   787  N  N   . ARG   A 1 107 ? 129.271 118.256 129.575 1.00 40.28 ? 107 ARG   A N   1 
ATOM   788  C  CA  . ARG   A 1 107 ? 128.941 118.992 130.788 1.00 40.31 ? 107 ARG   A CA  1 
ATOM   789  C  C   . ARG   A 1 107 ? 128.592 118.011 131.908 1.00 40.35 ? 107 ARG   A C   1 
ATOM   790  O  O   . ARG   A 1 107 ? 129.090 118.151 133.024 1.00 40.42 ? 107 ARG   A O   1 
ATOM   791  C  CB  . ARG   A 1 107 ? 127.790 119.991 130.597 1.00 40.31 ? 107 ARG   A CB  1 
ATOM   792  C  CG  . ARG   A 1 107 ? 127.959 121.063 129.526 1.00 40.32 ? 107 ARG   A CG  1 
ATOM   793  C  CD  . ARG   A 1 107 ? 129.153 122.002 129.699 1.00 40.32 ? 107 ARG   A CD  1 
ATOM   794  N  NE  . ARG   A 1 107 ? 129.167 122.719 130.981 1.00 40.33 ? 107 ARG   A NE  1 
ATOM   795  C  CZ  . ARG   A 1 107 ? 130.192 122.808 131.833 1.00 40.34 ? 107 ARG   A CZ  1 
ATOM   796  N  NH1 . ARG   A 1 107 ? 131.358 122.246 131.561 1.00 40.34 ? 107 ARG   A NH1 1 
ATOM   797  N  NH2 . ARG   A 1 107 ? 130.049 123.478 132.964 1.00 40.36 ? 107 ARG   A NH2 1 
ATOM   798  N  N   . TYR   A 1 108 ? 127.742 117.020 131.595 1.00 40.36 ? 108 TYR   A N   1 
ATOM   799  C  CA  . TYR   A 1 108 ? 127.315 116.026 132.569 1.00 40.39 ? 108 TYR   A CA  1 
ATOM   800  C  C   . TYR   A 1 108 ? 128.525 115.224 133.050 1.00 40.41 ? 108 TYR   A C   1 
ATOM   801  O  O   . TYR   A 1 108 ? 128.815 115.209 134.244 1.00 40.51 ? 108 TYR   A O   1 
ATOM   802  C  CB  . TYR   A 1 108 ? 126.216 115.131 131.981 1.00 40.40 ? 108 TYR   A CB  1 
ATOM   803  C  CG  . TYR   A 1 108 ? 125.935 113.854 132.765 1.00 40.38 ? 108 TYR   A CG  1 
ATOM   804  C  CD1 . TYR   A 1 108 ? 126.446 112.628 132.347 1.00 40.37 ? 108 TYR   A CD1 1 
ATOM   805  C  CD2 . TYR   A 1 108 ? 125.170 113.874 133.928 1.00 40.37 ? 108 TYR   A CD2 1 
ATOM   806  C  CE1 . TYR   A 1 108 ? 126.199 111.462 133.056 1.00 40.37 ? 108 TYR   A CE1 1 
ATOM   807  C  CE2 . TYR   A 1 108 ? 124.918 112.715 134.646 1.00 40.37 ? 108 TYR   A CE2 1 
ATOM   808  C  CZ  . TYR   A 1 108 ? 125.433 111.507 134.208 1.00 40.37 ? 108 TYR   A CZ  1 
ATOM   809  O  OH  . TYR   A 1 108 ? 125.186 110.362 134.910 1.00 40.37 ? 108 TYR   A OH  1 
ATOM   810  N  N   . LEU   A 1 109 ? 129.233 114.582 132.110 1.00 40.41 ? 109 LEU   A N   1 
ATOM   811  C  CA  . LEU   A 1 109 ? 130.321 113.669 132.434 1.00 40.44 ? 109 LEU   A CA  1 
ATOM   812  C  C   . LEU   A 1 109 ? 131.475 114.440 133.077 1.00 40.45 ? 109 LEU   A C   1 
ATOM   813  O  O   . LEU   A 1 109 ? 132.176 113.901 133.931 1.00 40.45 ? 109 LEU   A O   1 
ATOM   814  C  CB  . LEU   A 1 109 ? 130.754 112.927 131.166 1.00 40.47 ? 109 LEU   A CB  1 
ATOM   815  C  CG  . LEU   A 1 109 ? 131.522 111.608 131.347 1.00 40.50 ? 109 LEU   A CG  1 
ATOM   816  C  CD1 . LEU   A 1 109 ? 131.224 110.654 130.191 1.00 40.50 ? 109 LEU   A CD1 1 
ATOM   817  C  CD2 . LEU   A 1 109 ? 133.031 111.798 131.504 1.00 40.53 ? 109 LEU   A CD2 1 
ATOM   818  N  N   . GLY   A 1 110 ? 131.658 115.703 132.667 1.00 40.45 ? 110 GLY   A N   1 
ATOM   819  C  CA  . GLY   A 1 110 ? 132.719 116.549 133.188 1.00 40.49 ? 110 GLY   A CA  1 
ATOM   820  C  C   . GLY   A 1 110 ? 132.464 116.967 134.635 1.00 40.52 ? 110 GLY   A C   1 
ATOM   821  O  O   . GLY   A 1 110 ? 133.283 116.689 135.509 1.00 40.54 ? 110 GLY   A O   1 
ATOM   822  N  N   . VAL   A 1 111 ? 131.323 117.631 134.875 1.00 40.55 ? 111 VAL   A N   1 
ATOM   823  C  CA  . VAL   A 1 111 ? 131.036 118.230 136.172 1.00 40.61 ? 111 VAL   A CA  1 
ATOM   824  C  C   . VAL   A 1 111 ? 130.621 117.124 137.143 1.00 40.65 ? 111 VAL   A C   1 
ATOM   825  O  O   . VAL   A 1 111 ? 131.264 116.950 138.178 1.00 40.65 ? 111 VAL   A O   1 
ATOM   826  C  CB  . VAL   A 1 111 ? 129.982 119.358 136.089 1.00 40.60 ? 111 VAL   A CB  1 
ATOM   827  C  CG1 . VAL   A 1 111 ? 129.593 119.894 137.466 1.00 40.61 ? 111 VAL   A CG1 1 
ATOM   828  C  CG2 . VAL   A 1 111 ? 130.439 120.499 135.181 1.00 40.60 ? 111 VAL   A CG2 1 
ATOM   829  N  N   . ALA   A 1 112 ? 129.552 116.385 136.810 1.00 40.70 ? 112 ALA   A N   1 
ATOM   830  C  CA  . ALA   A 1 112 ? 129.128 115.247 137.612 1.00 40.82 ? 112 ALA   A CA  1 
ATOM   831  C  C   . ALA   A 1 112 ? 130.060 114.071 137.334 1.00 40.90 ? 112 ALA   A C   1 
ATOM   832  O  O   . ALA   A 1 112 ? 130.535 113.919 136.210 1.00 40.90 ? 112 ALA   A O   1 
ATOM   833  C  CB  . ALA   A 1 112 ? 127.684 114.898 137.323 1.00 40.82 ? 112 ALA   A CB  1 
ATOM   834  N  N   . PHE   A 1 113 ? 130.305 113.246 138.364 1.00 41.00 ? 113 PHE   A N   1 
ATOM   835  C  CA  . PHE   A 1 113 ? 131.330 112.212 138.322 1.00 41.08 ? 113 PHE   A CA  1 
ATOM   836  C  C   . PHE   A 1 113 ? 132.646 112.856 137.879 1.00 41.13 ? 113 PHE   A C   1 
ATOM   837  O  O   . PHE   A 1 113 ? 133.169 112.527 136.815 1.00 41.14 ? 113 PHE   A O   1 
ATOM   838  C  CB  . PHE   A 1 113 ? 130.832 111.060 137.436 1.00 41.12 ? 113 PHE   A CB  1 
ATOM   839  C  CG  . PHE   A 1 113 ? 131.789 109.893 137.210 1.00 41.18 ? 113 PHE   A CG  1 
ATOM   840  C  CD1 . PHE   A 1 113 ? 132.540 109.352 138.253 1.00 41.20 ? 113 PHE   A CD1 1 
ATOM   841  C  CD2 . PHE   A 1 113 ? 131.932 109.334 135.942 1.00 41.20 ? 113 PHE   A CD2 1 
ATOM   842  C  CE1 . PHE   A 1 113 ? 133.404 108.288 138.029 1.00 41.21 ? 113 PHE   A CE1 1 
ATOM   843  C  CE2 . PHE   A 1 113 ? 132.797 108.271 135.725 1.00 41.21 ? 113 PHE   A CE2 1 
ATOM   844  C  CZ  . PHE   A 1 113 ? 133.531 107.750 136.767 1.00 41.22 ? 113 PHE   A CZ  1 
ATOM   845  N  N   . PRO   A 1 114 ? 133.223 113.800 138.668 1.00 41.18 ? 114 PRO   A N   1 
ATOM   846  C  CA  . PRO   A 1 114 ? 134.394 114.564 138.224 1.00 41.22 ? 114 PRO   A CA  1 
ATOM   847  C  C   . PRO   A 1 114 ? 135.730 113.822 138.293 1.00 41.28 ? 114 PRO   A C   1 
ATOM   848  O  O   . PRO   A 1 114 ? 136.715 114.288 137.722 1.00 41.33 ? 114 PRO   A O   1 
ATOM   849  C  CB  . PRO   A 1 114 ? 134.409 115.754 139.199 1.00 41.20 ? 114 PRO   A CB  1 
ATOM   850  C  CG  . PRO   A 1 114 ? 133.830 115.190 140.478 1.00 41.19 ? 114 PRO   A CG  1 
ATOM   851  C  CD  . PRO   A 1 114 ? 132.788 114.190 140.023 1.00 41.18 ? 114 PRO   A CD  1 
ATOM   852  N  N   . VAL   A 1 115 ? 135.755 112.671 138.981 1.00 41.33 ? 115 VAL   A N   1 
ATOM   853  C  CA  . VAL   A 1 115 ? 136.969 111.882 139.146 1.00 41.38 ? 115 VAL   A CA  1 
ATOM   854  C  C   . VAL   A 1 115 ? 137.531 111.559 137.760 1.00 41.40 ? 115 VAL   A C   1 
ATOM   855  O  O   . VAL   A 1 115 ? 138.725 111.737 137.519 1.00 41.42 ? 115 VAL   A O   1 
ATOM   856  C  CB  . VAL   A 1 115 ? 136.734 110.601 139.980 1.00 41.39 ? 115 VAL   A CB  1 
ATOM   857  C  CG1 . VAL   A 1 115 ? 137.953 109.680 139.998 1.00 41.40 ? 115 VAL   A CG1 1 
ATOM   858  C  CG2 . VAL   A 1 115 ? 136.284 110.914 141.408 1.00 41.39 ? 115 VAL   A CG2 1 
ATOM   859  N  N   . GLN   A 1 116 ? 136.654 111.102 136.854 1.00 41.42 ? 116 GLN   A N   1 
ATOM   860  C  CA  . GLN   A 1 116 ? 137.040 110.758 135.493 1.00 41.44 ? 116 GLN   A CA  1 
ATOM   861  C  C   . GLN   A 1 116 ? 137.556 111.998 134.763 1.00 41.43 ? 116 GLN   A C   1 
ATOM   862  O  O   . GLN   A 1 116 ? 138.514 111.898 134.000 1.00 41.43 ? 116 GLN   A O   1 
ATOM   863  C  CB  . GLN   A 1 116 ? 135.862 110.115 134.754 1.00 41.45 ? 116 GLN   A CB  1 
ATOM   864  C  CG  . GLN   A 1 116 ? 136.164 109.666 133.326 1.00 41.47 ? 116 GLN   A CG  1 
ATOM   865  C  CD  . GLN   A 1 116 ? 137.275 108.642 133.228 1.00 41.49 ? 116 GLN   A CD  1 
ATOM   866  O  OE1 . GLN   A 1 116 ? 138.344 108.906 132.666 1.00 41.49 ? 116 GLN   A OE1 1 
ATOM   867  N  NE2 . GLN   A 1 116 ? 137.039 107.459 133.778 1.00 41.48 ? 116 GLN   A NE2 1 
ATOM   868  N  N   . TYR   A 1 117 ? 136.920 113.155 134.996 1.00 41.41 ? 117 TYR   A N   1 
ATOM   869  C  CA  . TYR   A 1 117 ? 137.296 114.395 134.331 1.00 41.42 ? 117 TYR   A CA  1 
ATOM   870  C  C   . TYR   A 1 117 ? 138.671 114.853 134.820 1.00 41.42 ? 117 TYR   A C   1 
ATOM   871  O  O   . TYR   A 1 117 ? 139.446 115.406 134.041 1.00 41.40 ? 117 TYR   A O   1 
ATOM   872  C  CB  . TYR   A 1 117 ? 136.239 115.481 134.563 1.00 41.44 ? 117 TYR   A CB  1 
ATOM   873  C  CG  . TYR   A 1 117 ? 136.423 116.773 133.772 1.00 41.46 ? 117 TYR   A CG  1 
ATOM   874  C  CD1 . TYR   A 1 117 ? 136.652 116.761 132.397 1.00 41.47 ? 117 TYR   A CD1 1 
ATOM   875  C  CD2 . TYR   A 1 117 ? 136.370 118.013 134.405 1.00 41.48 ? 117 TYR   A CD2 1 
ATOM   876  C  CE1 . TYR   A 1 117 ? 136.818 117.937 131.681 1.00 41.48 ? 117 TYR   A CE1 1 
ATOM   877  C  CE2 . TYR   A 1 117 ? 136.537 119.194 133.699 1.00 41.49 ? 117 TYR   A CE2 1 
ATOM   878  C  CZ  . TYR   A 1 117 ? 136.761 119.156 132.334 1.00 41.49 ? 117 TYR   A CZ  1 
ATOM   879  O  OH  . TYR   A 1 117 ? 136.926 120.316 131.634 1.00 41.48 ? 117 TYR   A OH  1 
ATOM   880  N  N   . LYS   A 1 118 ? 138.957 114.623 136.110 1.00 41.41 ? 118 LYS   A N   1 
ATOM   881  C  CA  . LYS   A 1 118 ? 140.239 114.974 136.704 1.00 41.44 ? 118 LYS   A CA  1 
ATOM   882  C  C   . LYS   A 1 118 ? 141.363 114.201 136.013 1.00 41.45 ? 118 LYS   A C   1 
ATOM   883  O  O   . LYS   A 1 118 ? 142.407 114.777 135.711 1.00 41.45 ? 118 LYS   A O   1 
ATOM   884  C  CB  . LYS   A 1 118 ? 140.239 114.701 138.213 1.00 41.44 ? 118 LYS   A CB  1 
ATOM   885  N  N   . LEU   A 1 119 ? 141.140 112.900 135.773 1.00 41.45 ? 119 LEU   A N   1 
ATOM   886  C  CA  . LEU   A 1 119 ? 142.104 112.066 135.067 1.00 41.47 ? 119 LEU   A CA  1 
ATOM   887  C  C   . LEU   A 1 119 ? 142.116 112.442 133.585 1.00 41.46 ? 119 LEU   A C   1 
ATOM   888  O  O   . LEU   A 1 119 ? 143.182 112.685 133.023 1.00 41.46 ? 119 LEU   A O   1 
ATOM   889  C  CB  . LEU   A 1 119 ? 141.807 110.574 135.263 1.00 41.47 ? 119 LEU   A CB  1 
ATOM   890  C  CG  . LEU   A 1 119 ? 142.381 109.881 136.510 1.00 41.48 ? 119 LEU   A CG  1 
ATOM   891  C  CD1 . LEU   A 1 119 ? 143.900 109.709 136.420 1.00 41.48 ? 119 LEU   A CD1 1 
ATOM   892  C  CD2 . LEU   A 1 119 ? 141.996 110.561 137.826 1.00 41.48 ? 119 LEU   A CD2 1 
ATOM   893  N  N   . SER   A 1 120 ? 140.926 112.492 132.968 1.00 41.45 ? 120 SER   A N   1 
ATOM   894  C  CA  . SER   A 1 120 ? 140.785 112.809 131.555 1.00 41.45 ? 120 SER   A CA  1 
ATOM   895  C  C   . SER   A 1 120 ? 140.461 114.293 131.387 1.00 41.42 ? 120 SER   A C   1 
ATOM   896  O  O   . SER   A 1 120 ? 139.349 114.652 131.001 1.00 41.41 ? 120 SER   A O   1 
ATOM   897  C  CB  . SER   A 1 120 ? 139.743 111.931 130.900 1.00 41.46 ? 120 SER   A CB  1 
ATOM   898  O  OG  . SER   A 1 120 ? 139.624 112.224 129.514 1.00 41.47 ? 120 SER   A OG  1 
ATOM   899  N  N   . ARG   A 1 121 ? 141.452 115.143 131.691 1.00 41.39 ? 121 ARG   A N   1 
ATOM   900  C  CA  . ARG   A 1 121 ? 141.368 116.576 131.452 1.00 41.36 ? 121 ARG   A CA  1 
ATOM   901  C  C   . ARG   A 1 121 ? 142.202 116.946 130.224 1.00 41.33 ? 121 ARG   A C   1 
ATOM   902  O  O   . ARG   A 1 121 ? 142.507 118.120 130.017 1.00 41.32 ? 121 ARG   A O   1 
ATOM   903  C  CB  . ARG   A 1 121 ? 141.836 117.345 132.693 1.00 41.37 ? 121 ARG   A CB  1 
ATOM   904  N  N   . ARG   A 1 122 ? 142.557 115.939 129.411 1.00 41.27 ? 122 ARG   A N   1 
ATOM   905  C  CA  . ARG   A 1 122 ? 143.355 116.142 128.211 1.00 41.22 ? 122 ARG   A CA  1 
ATOM   906  C  C   . ARG   A 1 122 ? 142.430 116.499 127.048 1.00 41.16 ? 122 ARG   A C   1 
ATOM   907  O  O   . ARG   A 1 122 ? 141.314 115.986 126.974 1.00 41.15 ? 122 ARG   A O   1 
ATOM   908  C  CB  . ARG   A 1 122 ? 144.175 114.886 127.893 1.00 41.23 ? 122 ARG   A CB  1 
ATOM   909  N  N   . PRO   A 1 123 ? 142.851 117.376 126.102 1.00 41.10 ? 123 PRO   A N   1 
ATOM   910  C  CA  . PRO   A 1 123 ? 141.978 117.797 125.002 1.00 41.07 ? 123 PRO   A CA  1 
ATOM   911  C  C   . PRO   A 1 123 ? 141.759 116.754 123.904 1.00 41.04 ? 123 PRO   A C   1 
ATOM   912  O  O   . PRO   A 1 123 ? 140.722 116.770 123.243 1.00 40.99 ? 123 PRO   A O   1 
ATOM   913  C  CB  . PRO   A 1 123 ? 142.716 119.013 124.416 1.00 41.06 ? 123 PRO   A CB  1 
ATOM   914  C  CG  . PRO   A 1 123 ? 144.175 118.747 124.712 1.00 41.07 ? 123 PRO   A CG  1 
ATOM   915  C  CD  . PRO   A 1 123 ? 144.176 118.021 126.041 1.00 41.09 ? 123 PRO   A CD  1 
ATOM   916  N  N   . LEU   A 1 124 ? 142.729 115.843 123.729 1.00 41.01 ? 124 LEU   A N   1 
ATOM   917  C  CA  . LEU   A 1 124 ? 142.767 114.956 122.575 1.00 40.99 ? 124 LEU   A CA  1 
ATOM   918  C  C   . LEU   A 1 124 ? 141.620 113.946 122.639 1.00 40.98 ? 124 LEU   A C   1 
ATOM   919  O  O   . LEU   A 1 124 ? 141.113 113.529 121.600 1.00 40.93 ? 124 LEU   A O   1 
ATOM   920  C  CB  . LEU   A 1 124 ? 144.130 114.261 122.501 1.00 41.00 ? 124 LEU   A CB  1 
ATOM   921  C  CG  . LEU   A 1 124 ? 144.477 113.540 121.190 1.00 40.99 ? 124 LEU   A CG  1 
ATOM   922  C  CD1 . LEU   A 1 124 ? 144.712 114.503 120.023 1.00 40.98 ? 124 LEU   A CD1 1 
ATOM   923  C  CD2 . LEU   A 1 124 ? 145.695 112.640 121.382 1.00 41.00 ? 124 LEU   A CD2 1 
ATOM   924  N  N   . TYR   A 1 125 ? 141.209 113.563 123.856 1.00 40.98 ? 125 TYR   A N   1 
ATOM   925  C  CA  . TYR   A 1 125 ? 140.083 112.658 124.038 1.00 40.98 ? 125 TYR   A CA  1 
ATOM   926  C  C   . TYR   A 1 125 ? 138.802 113.308 123.511 1.00 40.94 ? 125 TYR   A C   1 
ATOM   927  O  O   . TYR   A 1 125 ? 137.869 112.605 123.130 1.00 40.93 ? 125 TYR   A O   1 
ATOM   928  C  CB  . TYR   A 1 125 ? 139.936 112.261 125.512 1.00 41.02 ? 125 TYR   A CB  1 
ATOM   929  C  CG  . TYR   A 1 125 ? 138.891 111.189 125.810 1.00 41.06 ? 125 TYR   A CG  1 
ATOM   930  C  CD1 . TYR   A 1 125 ? 137.940 111.375 126.810 1.00 41.08 ? 125 TYR   A CD1 1 
ATOM   931  C  CD2 . TYR   A 1 125 ? 138.871 109.979 125.119 1.00 41.08 ? 125 TYR   A CD2 1 
ATOM   932  C  CE1 . TYR   A 1 125 ? 136.990 110.406 127.095 1.00 41.09 ? 125 TYR   A CE1 1 
ATOM   933  C  CE2 . TYR   A 1 125 ? 137.927 109.002 125.396 1.00 41.09 ? 125 TYR   A CE2 1 
ATOM   934  C  CZ  . TYR   A 1 125 ? 136.985 109.216 126.387 1.00 41.09 ? 125 TYR   A CZ  1 
ATOM   935  O  OH  . TYR   A 1 125 ? 136.054 108.258 126.665 1.00 41.09 ? 125 TYR   A OH  1 
ATOM   936  N  N   . GLY   A 1 126 ? 138.766 114.649 123.497 1.00 40.91 ? 126 GLY   A N   1 
ATOM   937  C  CA  . GLY   A 1 126 ? 137.612 115.397 123.024 1.00 40.85 ? 126 GLY   A CA  1 
ATOM   938  C  C   . GLY   A 1 126 ? 137.522 115.452 121.500 1.00 40.81 ? 126 GLY   A C   1 
ATOM   939  O  O   . GLY   A 1 126 ? 136.430 115.309 120.951 1.00 40.75 ? 126 GLY   A O   1 
ATOM   940  N  N   . VAL   A 1 127 ? 138.666 115.649 120.824 1.00 40.80 ? 127 VAL   A N   1 
ATOM   941  C  CA  . VAL   A 1 127 ? 138.672 116.033 119.415 1.00 40.74 ? 127 VAL   A CA  1 
ATOM   942  C  C   . VAL   A 1 127 ? 137.869 115.011 118.607 1.00 40.70 ? 127 VAL   A C   1 
ATOM   943  O  O   . VAL   A 1 127 ? 137.129 115.396 117.703 1.00 40.65 ? 127 VAL   A O   1 
ATOM   944  C  CB  . VAL   A 1 127 ? 140.070 116.251 118.783 1.00 40.74 ? 127 VAL   A CB  1 
ATOM   945  C  CG1 . VAL   A 1 127 ? 140.861 117.348 119.493 1.00 40.73 ? 127 VAL   A CG1 1 
ATOM   946  C  CG2 . VAL   A 1 127 ? 140.900 114.971 118.681 1.00 40.75 ? 127 VAL   A CG2 1 
ATOM   947  N  N   . ILE   A 1 128 ? 137.999 113.720 118.952 1.00 40.67 ? 128 ILE   A N   1 
ATOM   948  C  CA  . ILE   A 1 128 ? 137.382 112.643 118.187 1.00 40.66 ? 128 ILE   A CA  1 
ATOM   949  C  C   . ILE   A 1 128 ? 135.877 112.896 118.056 1.00 40.65 ? 128 ILE   A C   1 
ATOM   950  O  O   . ILE   A 1 128 ? 135.319 112.665 116.986 1.00 40.63 ? 128 ILE   A O   1 
ATOM   951  C  CB  . ILE   A 1 128 ? 137.703 111.256 118.796 1.00 40.67 ? 128 ILE   A CB  1 
ATOM   952  C  CG1 . ILE   A 1 128 ? 137.338 110.112 117.821 1.00 40.68 ? 128 ILE   A CG1 1 
ATOM   953  C  CG2 . ILE   A 1 128 ? 137.058 111.065 120.175 1.00 40.67 ? 128 ILE   A CG2 1 
ATOM   954  C  CD1 . ILE   A 1 128 ? 137.963 108.765 118.149 1.00 40.68 ? 128 ILE   A CD1 1 
ATOM   955  N  N   . ALA   A 1 129 ? 135.237 113.403 119.121 1.00 40.64 ? 129 ALA   A N   1 
ATOM   956  C  CA  . ALA   A 1 129 ? 133.796 113.616 119.130 1.00 40.61 ? 129 ALA   A CA  1 
ATOM   957  C  C   . ALA   A 1 129 ? 133.387 114.566 118.003 1.00 40.60 ? 129 ALA   A C   1 
ATOM   958  O  O   . ALA   A 1 129 ? 132.374 114.334 117.342 1.00 40.58 ? 129 ALA   A O   1 
ATOM   959  C  CB  . ALA   A 1 129 ? 133.350 114.139 120.480 1.00 40.60 ? 129 ALA   A CB  1 
ATOM   960  N  N   . ALA   A 1 130 ? 134.181 115.626 117.790 1.00 40.60 ? 130 ALA   A N   1 
ATOM   961  C  CA  . ALA   A 1 130 ? 133.924 116.588 116.728 1.00 40.58 ? 130 ALA   A CA  1 
ATOM   962  C  C   . ALA   A 1 130 ? 134.079 115.921 115.361 1.00 40.58 ? 130 ALA   A C   1 
ATOM   963  O  O   . ALA   A 1 130 ? 133.276 116.168 114.462 1.00 40.56 ? 130 ALA   A O   1 
ATOM   964  C  CB  . ALA   A 1 130 ? 134.845 117.783 116.868 1.00 40.57 ? 130 ALA   A CB  1 
ATOM   965  N  N   . LEU   A 1 131 ? 135.109 115.072 115.221 1.00 40.60 ? 131 LEU   A N   1 
ATOM   966  C  CA  . LEU   A 1 131 ? 135.363 114.361 113.976 1.00 40.60 ? 131 LEU   A CA  1 
ATOM   967  C  C   . LEU   A 1 131 ? 134.225 113.374 113.711 1.00 40.59 ? 131 LEU   A C   1 
ATOM   968  O  O   . LEU   A 1 131 ? 133.763 113.266 112.578 1.00 40.60 ? 131 LEU   A O   1 
ATOM   969  C  CB  . LEU   A 1 131 ? 136.722 113.655 113.994 1.00 40.61 ? 131 LEU   A CB  1 
ATOM   970  C  CG  . LEU   A 1 131 ? 137.945 114.488 113.582 1.00 40.62 ? 131 LEU   A CG  1 
ATOM   971  C  CD1 . LEU   A 1 131 ? 138.328 115.570 114.593 1.00 40.62 ? 131 LEU   A CD1 1 
ATOM   972  C  CD2 . LEU   A 1 131 ? 139.139 113.574 113.306 1.00 40.63 ? 131 LEU   A CD2 1 
ATOM   973  N  N   . VAL   A 1 132 ? 133.780 112.669 114.761 1.00 40.59 ? 132 VAL   A N   1 
ATOM   974  C  CA  . VAL   A 1 132 ? 132.665 111.736 114.663 1.00 40.57 ? 132 VAL   A CA  1 
ATOM   975  C  C   . VAL   A 1 132 ? 131.426 112.498 114.190 1.00 40.56 ? 132 VAL   A C   1 
ATOM   976  O  O   . VAL   A 1 132 ? 130.729 112.031 113.291 1.00 40.58 ? 132 VAL   A O   1 
ATOM   977  C  CB  . VAL   A 1 132 ? 132.407 110.983 115.989 1.00 40.56 ? 132 VAL   A CB  1 
ATOM   978  C  CG1 . VAL   A 1 132 ? 131.032 110.316 116.035 1.00 40.57 ? 132 VAL   A CG1 1 
ATOM   979  C  CG2 . VAL   A 1 132 ? 133.503 109.961 116.289 1.00 40.57 ? 132 VAL   A CG2 1 
ATOM   980  N  N   . ALA   A 1 133 ? 131.169 113.670 114.790 1.00 40.55 ? 133 ALA   A N   1 
ATOM   981  C  CA  . ALA   A 1 133 ? 130.031 114.499 114.419 1.00 40.52 ? 133 ALA   A CA  1 
ATOM   982  C  C   . ALA   A 1 133 ? 130.108 114.883 112.940 1.00 40.53 ? 133 ALA   A C   1 
ATOM   983  O  O   . ALA   A 1 133 ? 129.114 114.765 112.224 1.00 40.53 ? 133 ALA   A O   1 
ATOM   984  C  CB  . ALA   A 1 133 ? 129.961 115.725 115.309 1.00 40.50 ? 133 ALA   A CB  1 
ATOM   985  N  N   . TRP   A 1 134 ? 131.291 115.332 112.493 1.00 40.56 ? 134 TRP   A N   1 
ATOM   986  C  CA  . TRP   A 1 134 ? 131.500 115.739 111.109 1.00 40.59 ? 134 TRP   A CA  1 
ATOM   987  C  C   . TRP   A 1 134 ? 131.317 114.553 110.159 1.00 40.59 ? 134 TRP   A C   1 
ATOM   988  O  O   . TRP   A 1 134 ? 130.621 114.678 109.153 1.00 40.58 ? 134 TRP   A O   1 
ATOM   989  C  CB  . TRP   A 1 134 ? 132.888 116.376 110.931 1.00 40.61 ? 134 TRP   A CB  1 
ATOM   990  C  CG  . TRP   A 1 134 ? 132.971 117.830 111.321 1.00 40.63 ? 134 TRP   A CG  1 
ATOM   991  C  CD1 . TRP   A 1 134 ? 133.818 118.377 112.240 1.00 40.65 ? 134 TRP   A CD1 1 
ATOM   992  C  CD2 . TRP   A 1 134 ? 132.215 118.932 110.770 1.00 40.62 ? 134 TRP   A CD2 1 
ATOM   993  N  NE1 . TRP   A 1 134 ? 133.624 119.729 112.324 1.00 40.63 ? 134 TRP   A NE1 1 
ATOM   994  C  CE2 . TRP   A 1 134 ? 132.654 120.102 111.432 1.00 40.62 ? 134 TRP   A CE2 1 
ATOM   995  C  CE3 . TRP   A 1 134 ? 131.213 119.047 109.797 1.00 40.62 ? 134 TRP   A CE3 1 
ATOM   996  C  CZ2 . TRP   A 1 134 ? 132.125 121.360 111.149 1.00 40.62 ? 134 TRP   A CZ2 1 
ATOM   997  C  CZ3 . TRP   A 1 134 ? 130.693 120.293 109.518 1.00 40.62 ? 134 TRP   A CZ3 1 
ATOM   998  C  CH2 . TRP   A 1 134 ? 131.145 121.433 110.184 1.00 40.61 ? 134 TRP   A CH2 1 
ATOM   999  N  N   . VAL   A 1 135 ? 131.944 113.413 110.486 1.00 40.59 ? 135 VAL   A N   1 
ATOM   1000 C  CA  . VAL   A 1 135 ? 131.913 112.230 109.634 1.00 40.59 ? 135 VAL   A CA  1 
ATOM   1001 C  C   . VAL   A 1 135 ? 130.475 111.717 109.540 1.00 40.57 ? 135 VAL   A C   1 
ATOM   1002 O  O   . VAL   A 1 135 ? 130.011 111.399 108.447 1.00 40.58 ? 135 VAL   A O   1 
ATOM   1003 C  CB  . VAL   A 1 135 ? 132.884 111.128 110.119 1.00 40.60 ? 135 VAL   A CB  1 
ATOM   1004 C  CG1 . VAL   A 1 135 ? 132.581 109.760 109.507 1.00 40.60 ? 135 VAL   A CG1 1 
ATOM   1005 C  CG2 . VAL   A 1 135 ? 134.345 111.507 109.878 1.00 40.61 ? 135 VAL   A CG2 1 
ATOM   1006 N  N   . MET   A 1 136 ? 129.781 111.640 110.685 1.00 40.56 ? 136 MET   A N   1 
ATOM   1007 C  CA  . MET   A 1 136 ? 128.400 111.182 110.722 1.00 40.56 ? 136 MET   A CA  1 
ATOM   1008 C  C   . MET   A 1 136 ? 127.533 112.103 109.864 1.00 40.55 ? 136 MET   A C   1 
ATOM   1009 O  O   . MET   A 1 136 ? 126.734 111.622 109.062 1.00 40.55 ? 136 MET   A O   1 
ATOM   1010 C  CB  . MET   A 1 136 ? 127.863 111.142 112.160 1.00 40.57 ? 136 MET   A CB  1 
ATOM   1011 C  CG  . MET   A 1 136 ? 126.487 110.506 112.313 1.00 40.58 ? 136 MET   A CG  1 
ATOM   1012 S  SD  . MET   A 1 136 ? 126.455 108.748 111.908 1.00 40.60 ? 136 MET   A SD  1 
ATOM   1013 C  CE  . MET   A 1 136 ? 124.704 108.392 112.111 1.00 40.59 ? 136 MET   A CE  1 
ATOM   1014 N  N   . SER   A 1 137 ? 127.708 113.423 110.033 1.00 40.53 ? 137 SER   A N   1 
ATOM   1015 C  CA  . SER   A 1 137 ? 126.921 114.406 109.303 1.00 40.53 ? 137 SER   A CA  1 
ATOM   1016 C  C   . SER   A 1 137 ? 127.177 114.273 107.801 1.00 40.55 ? 137 SER   A C   1 
ATOM   1017 O  O   . SER   A 1 137 ? 126.252 113.967 107.051 1.00 40.54 ? 137 SER   A O   1 
ATOM   1018 C  CB  . SER   A 1 137 ? 127.194 115.810 109.794 1.00 40.52 ? 137 SER   A CB  1 
ATOM   1019 O  OG  . SER   A 1 137 ? 126.353 116.752 109.144 1.00 40.49 ? 137 SER   A OG  1 
ATOM   1020 N  N   . PHE   A 1 138 ? 128.434 114.475 107.378 1.00 40.57 ? 138 PHE   A N   1 
ATOM   1021 C  CA  . PHE   A 1 138 ? 128.796 114.429 105.968 1.00 40.58 ? 138 PHE   A CA  1 
ATOM   1022 C  C   . PHE   A 1 138 ? 128.368 113.088 105.373 1.00 40.58 ? 138 PHE   A C   1 
ATOM   1023 O  O   . PHE   A 1 138 ? 127.632 113.059 104.389 1.00 40.56 ? 138 PHE   A O   1 
ATOM   1024 C  CB  . PHE   A 1 138 ? 130.299 114.639 105.739 1.00 40.59 ? 138 PHE   A CB  1 
ATOM   1025 C  CG  . PHE   A 1 138 ? 130.858 116.038 105.986 1.00 40.59 ? 138 PHE   A CG  1 
ATOM   1026 C  CD1 . PHE   A 1 138 ? 130.193 117.180 105.540 1.00 40.60 ? 138 PHE   A CD1 1 
ATOM   1027 C  CD2 . PHE   A 1 138 ? 132.071 116.205 106.651 1.00 40.60 ? 138 PHE   A CD2 1 
ATOM   1028 C  CE1 . PHE   A 1 138 ? 130.722 118.444 105.765 1.00 40.60 ? 138 PHE   A CE1 1 
ATOM   1029 C  CE2 . PHE   A 1 138 ? 132.594 117.472 106.873 1.00 40.61 ? 138 PHE   A CE2 1 
ATOM   1030 C  CZ  . PHE   A 1 138 ? 131.919 118.587 106.429 1.00 40.61 ? 138 PHE   A CZ  1 
ATOM   1031 N  N   . GLY   A 1 139 ? 128.823 111.990 105.995 1.00 40.59 ? 139 GLY   A N   1 
ATOM   1032 C  CA  . GLY   A 1 139 ? 128.626 110.645 105.477 1.00 40.59 ? 139 GLY   A CA  1 
ATOM   1033 C  C   . GLY   A 1 139 ? 127.159 110.345 105.176 1.00 40.59 ? 139 GLY   A C   1 
ATOM   1034 O  O   . GLY   A 1 139 ? 126.844 109.849 104.096 1.00 40.59 ? 139 GLY   A O   1 
ATOM   1035 N  N   . HIS   A 1 140 ? 126.273 110.653 106.134 1.00 40.57 ? 140 HIS   A N   1 
ATOM   1036 C  CA  . HIS   A 1 140 ? 124.863 110.310 106.013 1.00 40.56 ? 140 HIS   A CA  1 
ATOM   1037 C  C   . HIS   A 1 140 ? 124.164 111.303 105.084 1.00 40.54 ? 140 HIS   A C   1 
ATOM   1038 O  O   . HIS   A 1 140 ? 123.338 110.899 104.268 1.00 40.54 ? 140 HIS   A O   1 
ATOM   1039 C  CB  . HIS   A 1 140 ? 124.198 110.225 107.394 1.00 40.58 ? 140 HIS   A CB  1 
ATOM   1040 C  CG  . HIS   A 1 140 ? 123.072 109.244 107.473 1.00 40.60 ? 140 HIS   A CG  1 
ATOM   1041 N  ND1 . HIS   A 1 140 ? 122.256 108.920 106.410 1.00 40.61 ? 140 HIS   A ND1 1 
ATOM   1042 C  CD2 . HIS   A 1 140 ? 122.644 108.503 108.504 1.00 40.61 ? 140 HIS   A CD2 1 
ATOM   1043 C  CE1 . HIS   A 1 140 ? 121.366 108.018 106.800 1.00 40.60 ? 140 HIS   A CE1 1 
ATOM   1044 N  NE2 . HIS   A 1 140 ? 121.583 107.752 108.069 1.00 40.61 ? 140 HIS   A NE2 1 
ATOM   1045 N  N   . CYS   A 1 141 ? 124.502 112.596 105.207 1.00 40.52 ? 141 CYS   A N   1 
ATOM   1046 C  CA  . CYS   A 1 141 ? 123.894 113.638 104.389 1.00 40.51 ? 141 CYS   A CA  1 
ATOM   1047 C  C   . CYS   A 1 141 ? 124.168 113.397 102.903 1.00 40.52 ? 141 CYS   A C   1 
ATOM   1048 O  O   . CYS   A 1 141 ? 123.301 113.658 102.072 1.00 40.52 ? 141 CYS   A O   1 
ATOM   1049 C  CB  . CYS   A 1 141 ? 124.388 115.026 104.782 1.00 40.51 ? 141 CYS   A CB  1 
ATOM   1050 S  SG  . CYS   A 1 141 ? 123.879 115.531 106.445 1.00 40.52 ? 141 CYS   A SG  1 
ATOM   1051 N  N   . THR   A 1 142 ? 125.371 112.899 102.580 1.00 40.54 ? 142 THR   A N   1 
ATOM   1052 C  CA  . THR   A 1 142 ? 125.762 112.637 101.201 1.00 40.55 ? 142 THR   A CA  1 
ATOM   1053 C  C   . THR   A 1 142 ? 124.732 111.722 100.533 1.00 40.54 ? 142 THR   A C   1 
ATOM   1054 O  O   . THR   A 1 142 ? 124.383 111.935 99.372  1.00 40.54 ? 142 THR   A O   1 
ATOM   1055 C  CB  . THR   A 1 142 ? 127.169 112.033 101.161 1.00 40.58 ? 142 THR   A CB  1 
ATOM   1056 O  OG1 . THR   A 1 142 ? 127.993 112.877 101.958 1.00 40.58 ? 142 THR   A OG1 1 
ATOM   1057 C  CG2 . THR   A 1 142 ? 127.759 111.971 99.762  1.00 40.60 ? 142 THR   A CG2 1 
ATOM   1058 N  N   . ILE   A 1 143 ? 124.235 110.721 101.276 1.00 40.54 ? 143 ILE   A N   1 
ATOM   1059 C  CA  . ILE   A 1 143 ? 123.288 109.752 100.739 1.00 40.54 ? 143 ILE   A CA  1 
ATOM   1060 C  C   . ILE   A 1 143 ? 122.082 110.497 100.161 1.00 40.53 ? 143 ILE   A C   1 
ATOM   1061 O  O   . ILE   A 1 143 ? 121.600 110.140 99.087  1.00 40.56 ? 143 ILE   A O   1 
ATOM   1062 C  CB  . ILE   A 1 143 ? 122.874 108.711 101.805 1.00 40.57 ? 143 ILE   A CB  1 
ATOM   1063 C  CG1 . ILE   A 1 143 ? 124.076 107.856 102.274 1.00 40.57 ? 143 ILE   A CG1 1 
ATOM   1064 C  CG2 . ILE   A 1 143 ? 121.717 107.835 101.308 1.00 40.58 ? 143 ILE   A CG2 1 
ATOM   1065 C  CD1 . ILE   A 1 143 ? 123.867 107.121 103.590 1.00 40.57 ? 143 ILE   A CD1 1 
ATOM   1066 N  N   . VAL   A 1 144 ? 121.619 111.542 100.864 1.00 40.51 ? 144 VAL   A N   1 
ATOM   1067 C  CA  . VAL   A 1 144 ? 120.432 112.283 100.457 1.00 40.50 ? 144 VAL   A CA  1 
ATOM   1068 C  C   . VAL   A 1 144 ? 120.637 112.792 99.029  1.00 40.51 ? 144 VAL   A C   1 
ATOM   1069 O  O   . VAL   A 1 144 ? 119.810 112.518 98.159  1.00 40.54 ? 144 VAL   A O   1 
ATOM   1070 C  CB  . VAL   A 1 144 ? 120.064 113.438 101.418 1.00 40.47 ? 144 VAL   A CB  1 
ATOM   1071 C  CG1 . VAL   A 1 144 ? 118.898 114.280 100.901 1.00 40.46 ? 144 VAL   A CG1 1 
ATOM   1072 C  CG2 . VAL   A 1 144 ? 119.772 112.945 102.834 1.00 40.46 ? 144 VAL   A CG2 1 
ATOM   1073 N  N   . ILE   A 1 145 ? 121.750 113.505 98.790  1.00 40.52 ? 145 ILE   A N   1 
ATOM   1074 C  CA  . ILE   A 1 145 ? 121.974 114.173 97.512  1.00 40.51 ? 145 ILE   A CA  1 
ATOM   1075 C  C   . ILE   A 1 145 ? 122.276 113.131 96.431  1.00 40.55 ? 145 ILE   A C   1 
ATOM   1076 O  O   . ILE   A 1 145 ? 121.981 113.371 95.261  1.00 40.59 ? 145 ILE   A O   1 
ATOM   1077 C  CB  . ILE   A 1 145 ? 123.070 115.263 97.595  1.00 40.49 ? 145 ILE   A CB  1 
ATOM   1078 C  CG1 . ILE   A 1 145 ? 124.458 114.706 97.998  1.00 40.51 ? 145 ILE   A CG1 1 
ATOM   1079 C  CG2 . ILE   A 1 145 ? 122.622 116.408 98.513  1.00 40.47 ? 145 ILE   A CG2 1 
ATOM   1080 C  CD1 . ILE   A 1 145 ? 125.630 115.622 97.683  1.00 40.51 ? 145 ILE   A CD1 1 
ATOM   1081 N  N   . ILE   A 1 146 ? 122.849 111.981 96.823  1.00 40.57 ? 146 ILE   A N   1 
ATOM   1082 C  CA  . ILE   A 1 146 ? 123.064 110.874 95.898  1.00 40.61 ? 146 ILE   A CA  1 
ATOM   1083 C  C   . ILE   A 1 146 ? 121.708 110.389 95.383  1.00 40.61 ? 146 ILE   A C   1 
ATOM   1084 O  O   . ILE   A 1 146 ? 121.536 110.221 94.177  1.00 40.63 ? 146 ILE   A O   1 
ATOM   1085 C  CB  . ILE   A 1 146 ? 123.879 109.733 96.548  1.00 40.63 ? 146 ILE   A CB  1 
ATOM   1086 C  CG1 . ILE   A 1 146 ? 125.360 110.127 96.745  1.00 40.64 ? 146 ILE   A CG1 1 
ATOM   1087 C  CG2 . ILE   A 1 146 ? 123.740 108.428 95.752  1.00 40.63 ? 146 ILE   A CG2 1 
ATOM   1088 C  CD1 . ILE   A 1 146 ? 126.157 109.199 97.649  1.00 40.65 ? 146 ILE   A CD1 1 
ATOM   1089 N  N   . VAL   A 1 147 ? 120.753 110.177 96.300  1.00 40.60 ? 147 VAL   A N   1 
ATOM   1090 C  CA  . VAL   A 1 147 ? 119.466 109.590 95.953  1.00 40.61 ? 147 VAL   A CA  1 
ATOM   1091 C  C   . VAL   A 1 147 ? 118.669 110.587 95.110  1.00 40.60 ? 147 VAL   A C   1 
ATOM   1092 O  O   . VAL   A 1 147 ? 118.213 110.235 94.023  1.00 40.59 ? 147 VAL   A O   1 
ATOM   1093 C  CB  . VAL   A 1 147 ? 118.668 109.123 97.192  1.00 40.61 ? 147 VAL   A CB  1 
ATOM   1094 C  CG1 . VAL   A 1 147 ? 117.225 108.751 96.854  1.00 40.61 ? 147 VAL   A CG1 1 
ATOM   1095 C  CG2 . VAL   A 1 147 ? 119.354 107.965 97.916  1.00 40.61 ? 147 VAL   A CG2 1 
ATOM   1096 N  N   . GLN   A 1 148 ? 118.515 111.826 95.604  1.00 40.60 ? 148 GLN   A N   1 
ATOM   1097 C  CA  . GLN   A 1 148 ? 117.592 112.776 94.993  1.00 40.64 ? 148 GLN   A CA  1 
ATOM   1098 C  C   . GLN   A 1 148 ? 118.175 113.331 93.690  1.00 40.64 ? 148 GLN   A C   1 
ATOM   1099 O  O   . GLN   A 1 148 ? 117.417 113.592 92.757  1.00 40.64 ? 148 GLN   A O   1 
ATOM   1100 C  CB  . GLN   A 1 148 ? 117.148 113.878 95.963  1.00 40.66 ? 148 GLN   A CB  1 
ATOM   1101 C  CG  . GLN   A 1 148 ? 118.218 114.898 96.342  1.00 40.69 ? 148 GLN   A CG  1 
ATOM   1102 C  CD  . GLN   A 1 148 ? 117.677 116.071 97.133  1.00 40.72 ? 148 GLN   A CD  1 
ATOM   1103 O  OE1 . GLN   A 1 148 ? 118.006 116.258 98.310  1.00 40.74 ? 148 GLN   A OE1 1 
ATOM   1104 N  NE2 . GLN   A 1 148 ? 116.841 116.880 96.498  1.00 40.73 ? 148 GLN   A NE2 1 
ATOM   1105 N  N   . TYR   A 1 149 ? 119.505 113.512 93.624  1.00 40.65 ? 149 TYR   A N   1 
ATOM   1106 C  CA  . TYR   A 1 149 ? 120.155 113.982 92.408  1.00 40.69 ? 149 TYR   A CA  1 
ATOM   1107 C  C   . TYR   A 1 149 ? 121.080 112.889 91.873  1.00 40.73 ? 149 TYR   A C   1 
ATOM   1108 O  O   . TYR   A 1 149 ? 122.123 112.616 92.465  1.00 40.73 ? 149 TYR   A O   1 
ATOM   1109 C  CB  . TYR   A 1 149 ? 120.929 115.288 92.626  1.00 40.69 ? 149 TYR   A CB  1 
ATOM   1110 C  CG  . TYR   A 1 149 ? 120.077 116.486 93.028  1.00 40.68 ? 149 TYR   A CG  1 
ATOM   1111 C  CD1 . TYR   A 1 149 ? 119.201 117.082 92.124  1.00 40.68 ? 149 TYR   A CD1 1 
ATOM   1112 C  CD2 . TYR   A 1 149 ? 120.171 117.044 94.300  1.00 40.68 ? 149 TYR   A CD2 1 
ATOM   1113 C  CE1 . TYR   A 1 149 ? 118.425 118.173 92.482  1.00 40.68 ? 149 TYR   A CE1 1 
ATOM   1114 C  CE2 . TYR   A 1 149 ? 119.401 118.135 94.670  1.00 40.68 ? 149 TYR   A CE2 1 
ATOM   1115 C  CZ  . TYR   A 1 149 ? 118.528 118.702 93.758  1.00 40.68 ? 149 TYR   A CZ  1 
ATOM   1116 O  OH  . TYR   A 1 149 ? 117.769 119.777 94.116  1.00 40.67 ? 149 TYR   A OH  1 
ATOM   1117 N  N   . LEU   A 1 150 ? 120.675 112.279 90.748  1.00 40.77 ? 150 LEU   A N   1 
ATOM   1118 C  CA  . LEU   A 1 150 ? 121.454 111.270 90.041  1.00 40.80 ? 150 LEU   A CA  1 
ATOM   1119 C  C   . LEU   A 1 150 ? 121.844 110.146 91.022  1.00 40.81 ? 150 LEU   A C   1 
ATOM   1120 O  O   . LEU   A 1 150 ? 123.030 110.100 91.423  1.00 40.80 ? 150 LEU   A O   1 
ATOM   1121 C  CB  . LEU   A 1 150 ? 122.682 111.878 89.352  1.00 40.81 ? 150 LEU   A CB  1 
ATOM   1122 C  CG  . LEU   A 1 150 ? 122.461 112.760 88.110  1.00 40.81 ? 150 LEU   A CG  1 
ATOM   1123 C  CD1 . LEU   A 1 150 ? 121.823 111.990 86.949  1.00 40.80 ? 150 LEU   A CD1 1 
ATOM   1124 C  CD2 . LEU   A 1 150 ? 121.671 114.040 88.398  1.00 40.81 ? 150 LEU   A CD2 1 
ATOM   1125 N  N   . SER   A 1 158 ? 110.340 124.631 80.955  1.00 41.23 ? 158 SER   A N   1 
ATOM   1126 C  CA  . SER   A 1 158 ? 109.694 124.790 82.286  1.00 41.23 ? 158 SER   A CA  1 
ATOM   1127 C  C   . SER   A 1 158 ? 109.982 126.187 82.835  1.00 41.23 ? 158 SER   A C   1 
ATOM   1128 O  O   . SER   A 1 158 ? 111.142 126.583 82.941  1.00 41.23 ? 158 SER   A O   1 
ATOM   1129 C  CB  . SER   A 1 158 ? 110.147 123.717 83.249  1.00 41.23 ? 158 SER   A CB  1 
ATOM   1130 O  OG  . SER   A 1 158 ? 111.557 123.749 83.427  1.00 41.24 ? 158 SER   A OG  1 
ATOM   1131 N  N   . GLY   A 1 159 ? 108.912 126.922 83.170  1.00 41.21 ? 159 GLY   A N   1 
ATOM   1132 C  CA  . GLY   A 1 159 ? 109.020 128.250 83.753  1.00 41.19 ? 159 GLY   A CA  1 
ATOM   1133 C  C   . GLY   A 1 159 ? 108.118 128.388 84.978  1.00 41.16 ? 159 GLY   A C   1 
ATOM   1134 O  O   . GLY   A 1 159 ? 107.308 129.310 85.049  1.00 41.16 ? 159 GLY   A O   1 
ATOM   1135 N  N   . ASN   A 1 160 ? 108.281 127.462 85.933  1.00 41.14 ? 160 ASN   A N   1 
ATOM   1136 C  CA  . ASN   A 1 160 ? 107.473 127.428 87.142  1.00 41.10 ? 160 ASN   A CA  1 
ATOM   1137 C  C   . ASN   A 1 160 ? 108.151 128.262 88.227  1.00 41.06 ? 160 ASN   A C   1 
ATOM   1138 O  O   . ASN   A 1 160 ? 109.365 128.460 88.192  1.00 41.05 ? 160 ASN   A O   1 
ATOM   1139 C  CB  . ASN   A 1 160 ? 107.228 125.996 87.610  1.00 41.12 ? 160 ASN   A CB  1 
ATOM   1140 N  N   . GLU   A 1 161 ? 107.349 128.738 89.190  1.00 41.01 ? 161 GLU   A N   1 
ATOM   1141 C  CA  . GLU   A 1 161 ? 107.840 129.555 90.289  1.00 40.97 ? 161 GLU   A CA  1 
ATOM   1142 C  C   . GLU   A 1 161 ? 108.438 128.647 91.362  1.00 40.92 ? 161 GLU   A C   1 
ATOM   1143 O  O   . GLU   A 1 161 ? 107.812 128.404 92.394  1.00 40.91 ? 161 GLU   A O   1 
ATOM   1144 C  CB  . GLU   A 1 161 ? 106.712 130.426 90.845  1.00 40.98 ? 161 GLU   A CB  1 
ATOM   1145 N  N   . ILE   A 1 162 ? 109.656 128.152 91.100  1.00 40.86 ? 162 ILE   A N   1 
ATOM   1146 C  CA  . ILE   A 1 162 ? 110.350 127.247 92.003  1.00 40.84 ? 162 ILE   A CA  1 
ATOM   1147 C  C   . ILE   A 1 162 ? 111.842 127.278 91.674  1.00 40.80 ? 162 ILE   A C   1 
ATOM   1148 O  O   . ILE   A 1 162 ? 112.230 127.044 90.530  1.00 40.80 ? 162 ILE   A O   1 
ATOM   1149 C  CB  . ILE   A 1 162 ? 109.776 125.821 91.911  1.00 40.83 ? 162 ILE   A CB  1 
ATOM   1150 N  N   . THR   A 1 163 ? 112.663 127.581 92.689  1.00 40.76 ? 163 THR   A N   1 
ATOM   1151 C  CA  . THR   A 1 163 ? 114.111 127.651 92.534  1.00 40.73 ? 163 THR   A CA  1 
ATOM   1152 C  C   . THR   A 1 163 ? 114.659 126.258 92.216  1.00 40.74 ? 163 THR   A C   1 
ATOM   1153 O  O   . THR   A 1 163 ? 115.574 126.129 91.404  1.00 40.76 ? 163 THR   A O   1 
ATOM   1154 C  CB  . THR   A 1 163 ? 114.758 128.264 93.783  1.00 40.71 ? 163 THR   A CB  1 
ATOM   1155 O  OG1 . THR   A 1 163 ? 116.146 128.348 93.476  1.00 40.71 ? 163 THR   A OG1 1 
ATOM   1156 C  CG2 . THR   A 1 163 ? 114.566 127.452 95.055  1.00 40.70 ? 163 THR   A CG2 1 
ATOM   1157 N  N   . CYS   A 1 164 ? 114.095 125.229 92.865  1.00 40.73 ? 164 CYS   A N   1 
ATOM   1158 C  CA  . CYS   A 1 164 ? 114.386 123.837 92.562  1.00 40.73 ? 164 CYS   A CA  1 
ATOM   1159 C  C   . CYS   A 1 164 ? 113.129 123.009 92.822  1.00 40.77 ? 164 CYS   A C   1 
ATOM   1160 O  O   . CYS   A 1 164 ? 112.917 122.538 93.939  1.00 40.76 ? 164 CYS   A O   1 
ATOM   1161 C  CB  . CYS   A 1 164 ? 115.544 123.297 93.397  1.00 40.69 ? 164 CYS   A CB  1 
ATOM   1162 S  SG  . CYS   A 1 164 ? 117.184 123.855 92.862  1.00 40.63 ? 164 CYS   A SG  1 
ATOM   1163 N  N   . TYR   A 1 165 ? 112.291 122.861 91.787  1.00 40.84 ? 165 TYR   A N   1 
ATOM   1164 C  CA  . TYR   A 1 165 ? 111.070 122.078 91.894  1.00 40.90 ? 165 TYR   A CA  1 
ATOM   1165 C  C   . TYR   A 1 165 ? 111.452 120.618 92.127  1.00 40.92 ? 165 TYR   A C   1 
ATOM   1166 O  O   . TYR   A 1 165 ? 112.313 120.084 91.430  1.00 40.93 ? 165 TYR   A O   1 
ATOM   1167 C  CB  . TYR   A 1 165 ? 110.188 122.242 90.649  1.00 40.93 ? 165 TYR   A CB  1 
ATOM   1168 C  CG  . TYR   A 1 165 ? 108.841 121.525 90.684  1.00 40.97 ? 165 TYR   A CG  1 
ATOM   1169 C  CD1 . TYR   A 1 165 ? 108.372 120.839 89.567  1.00 40.99 ? 165 TYR   A CD1 1 
ATOM   1170 C  CD2 . TYR   A 1 165 ? 108.024 121.553 91.813  1.00 40.99 ? 165 TYR   A CD2 1 
ATOM   1171 C  CE1 . TYR   A 1 165 ? 107.148 120.188 89.578  1.00 41.01 ? 165 TYR   A CE1 1 
ATOM   1172 C  CE2 . TYR   A 1 165 ? 106.799 120.904 91.837  1.00 41.01 ? 165 TYR   A CE2 1 
ATOM   1173 C  CZ  . TYR   A 1 165 ? 106.360 120.220 90.716  1.00 41.02 ? 165 TYR   A CZ  1 
ATOM   1174 O  OH  . TYR   A 1 165 ? 105.154 119.582 90.731  1.00 41.03 ? 165 TYR   A OH  1 
ATOM   1175 N  N   . GLU   A 1 166 ? 110.795 119.989 93.111  1.00 40.94 ? 166 GLU   A N   1 
ATOM   1176 C  CA  . GLU   A 1 166 ? 111.164 118.659 93.574  1.00 40.94 ? 166 GLU   A CA  1 
ATOM   1177 C  C   . GLU   A 1 166 ? 110.008 117.695 93.308  1.00 40.96 ? 166 GLU   A C   1 
ATOM   1178 O  O   . GLU   A 1 166 ? 109.385 117.181 94.237  1.00 40.96 ? 166 GLU   A O   1 
ATOM   1179 C  CB  . GLU   A 1 166 ? 111.622 118.696 95.037  1.00 40.95 ? 166 GLU   A CB  1 
ATOM   1180 C  CG  . GLU   A 1 166 ? 110.695 119.443 95.995  1.00 40.95 ? 166 GLU   A CG  1 
ATOM   1181 C  CD  . GLU   A 1 166 ? 111.120 119.374 97.451  1.00 40.95 ? 166 GLU   A CD  1 
ATOM   1182 O  OE1 . GLU   A 1 166 ? 112.215 119.881 97.776  1.00 40.96 ? 166 GLU   A OE1 1 
ATOM   1183 O  OE2 . GLU   A 1 166 ? 110.355 118.811 98.262  1.00 40.95 ? 166 GLU   A OE2 1 
ATOM   1184 N  N   . ASN   A 1 167 ? 109.738 117.457 92.017  1.00 40.99 ? 167 ASN   A N   1 
ATOM   1185 C  CA  . ASN   A 1 167 ? 108.761 116.466 91.594  1.00 41.01 ? 167 ASN   A CA  1 
ATOM   1186 C  C   . ASN   A 1 167 ? 109.314 115.063 91.843  1.00 41.04 ? 167 ASN   A C   1 
ATOM   1187 O  O   . ASN   A 1 167 ? 108.554 114.160 92.191  1.00 41.03 ? 167 ASN   A O   1 
ATOM   1188 C  CB  . ASN   A 1 167 ? 108.348 116.650 90.135  1.00 41.01 ? 167 ASN   A CB  1 
ATOM   1189 C  CG  . ASN   A 1 167 ? 109.506 116.509 89.172  1.00 41.00 ? 167 ASN   A CG  1 
ATOM   1190 O  OD1 . ASN   A 1 167 ? 110.449 117.307 89.216  1.00 41.00 ? 167 ASN   A OD1 1 
ATOM   1191 N  ND2 . ASN   A 1 167 ? 109.457 115.517 88.294  1.00 41.00 ? 167 ASN   A ND2 1 
ATOM   1192 N  N   . PHE   A 1 168 ? 110.636 114.903 91.669  1.00 41.07 ? 168 PHE   A N   1 
ATOM   1193 C  CA  . PHE   A 1 168 ? 111.303 113.610 91.736  1.00 41.10 ? 168 PHE   A CA  1 
ATOM   1194 C  C   . PHE   A 1 168 ? 110.564 112.646 90.803  1.00 41.12 ? 168 PHE   A C   1 
ATOM   1195 O  O   . PHE   A 1 168 ? 110.271 113.005 89.664  1.00 41.13 ? 168 PHE   A O   1 
ATOM   1196 C  CB  . PHE   A 1 168 ? 111.421 113.163 93.203  1.00 41.11 ? 168 PHE   A CB  1 
ATOM   1197 C  CG  . PHE   A 1 168 ? 112.174 114.086 94.157  1.00 41.13 ? 168 PHE   A CG  1 
ATOM   1198 C  CD1 . PHE   A 1 168 ? 111.742 114.243 95.473  1.00 41.14 ? 168 PHE   A CD1 1 
ATOM   1199 C  CD2 . PHE   A 1 168 ? 113.330 114.761 93.763  1.00 41.14 ? 168 PHE   A CD2 1 
ATOM   1200 C  CE1 . PHE   A 1 168 ? 112.427 115.068 96.355  1.00 41.14 ? 168 PHE   A CE1 1 
ATOM   1201 C  CE2 . PHE   A 1 168 ? 114.009 115.586 94.650  1.00 41.15 ? 168 PHE   A CE2 1 
ATOM   1202 C  CZ  . PHE   A 1 168 ? 113.560 115.733 95.944  1.00 41.15 ? 168 PHE   A CZ  1 
ATOM   1203 N  N   . THR   A 1 169 ? 110.284 111.423 91.280  1.00 41.12 ? 169 THR   A N   1 
ATOM   1204 C  CA  . THR   A 1 169 ? 109.524 110.436 90.529  1.00 41.12 ? 169 THR   A CA  1 
ATOM   1205 C  C   . THR   A 1 169 ? 108.728 109.599 91.529  1.00 41.10 ? 169 THR   A C   1 
ATOM   1206 O  O   . THR   A 1 169 ? 109.167 109.419 92.663  1.00 41.02 ? 169 THR   A O   1 
ATOM   1207 C  CB  . THR   A 1 169 ? 110.470 109.578 89.683  1.00 41.13 ? 169 THR   A CB  1 
ATOM   1208 O  OG1 . THR   A 1 169 ? 111.385 110.464 89.044  1.00 41.13 ? 169 THR   A OG1 1 
ATOM   1209 C  CG2 . THR   A 1 169 ? 109.757 108.771 88.612  1.00 41.13 ? 169 THR   A CG2 1 
ATOM   1210 N  N   . ASP   A 1 170 ? 107.562 109.095 91.103  1.00 41.12 ? 170 ASP   A N   1 
ATOM   1211 C  CA  . ASP   A 1 170 ? 106.677 108.328 91.969  1.00 41.13 ? 170 ASP   A CA  1 
ATOM   1212 C  C   . ASP   A 1 170 ? 107.418 107.131 92.566  1.00 41.11 ? 170 ASP   A C   1 
ATOM   1213 O  O   . ASP   A 1 170 ? 107.185 106.784 93.722  1.00 41.11 ? 170 ASP   A O   1 
ATOM   1214 C  CB  . ASP   A 1 170 ? 105.409 107.905 91.241  1.00 41.15 ? 170 ASP   A CB  1 
ATOM   1215 C  CG  . ASP   A 1 170 ? 104.499 109.035 90.776  1.00 41.17 ? 170 ASP   A CG  1 
ATOM   1216 O  OD1 . ASP   A 1 170 ? 104.858 110.213 90.989  1.00 41.17 ? 170 ASP   A OD1 1 
ATOM   1217 O  OD2 . ASP   A 1 170 ? 103.433 108.726 90.203  1.00 41.18 ? 170 ASP   A OD2 1 
ATOM   1218 N  N   . ASN   A 1 171 ? 108.299 106.503 91.772  1.00 41.08 ? 171 ASN   A N   1 
ATOM   1219 C  CA  . ASN   A 1 171 ? 109.132 105.410 92.255  1.00 41.05 ? 171 ASN   A CA  1 
ATOM   1220 C  C   . ASN   A 1 171 ? 110.196 105.955 93.211  1.00 41.02 ? 171 ASN   A C   1 
ATOM   1221 O  O   . ASN   A 1 171 ? 110.412 105.381 94.277  1.00 40.97 ? 171 ASN   A O   1 
ATOM   1222 C  CB  . ASN   A 1 171 ? 109.727 104.581 91.116  1.00 41.05 ? 171 ASN   A CB  1 
ATOM   1223 C  CG  . ASN   A 1 171 ? 110.461 105.407 90.083  1.00 41.03 ? 171 ASN   A CG  1 
ATOM   1224 O  OD1 . ASN   A 1 171 ? 111.471 106.046 90.398  1.00 41.02 ? 171 ASN   A OD1 1 
ATOM   1225 N  ND2 . ASN   A 1 171 ? 109.990 105.393 88.843  1.00 41.02 ? 171 ASN   A ND2 1 
ATOM   1226 N  N   . GLN   A 1 172 ? 110.838 107.071 92.832  1.00 41.00 ? 172 GLN   A N   1 
ATOM   1227 C  CA  . GLN   A 1 172 ? 111.889 107.678 93.639  1.00 40.98 ? 172 GLN   A CA  1 
ATOM   1228 C  C   . GLN   A 1 172 ? 111.329 108.113 94.993  1.00 40.94 ? 172 GLN   A C   1 
ATOM   1229 O  O   . GLN   A 1 172 ? 112.016 107.989 96.002  1.00 40.85 ? 172 GLN   A O   1 
ATOM   1230 C  CB  . GLN   A 1 172 ? 112.543 108.871 92.936  1.00 41.02 ? 172 GLN   A CB  1 
ATOM   1231 C  CG  . GLN   A 1 172 ? 113.529 108.503 91.830  1.00 41.05 ? 172 GLN   A CG  1 
ATOM   1232 C  CD  . GLN   A 1 172 ? 114.812 107.887 92.347  1.00 41.07 ? 172 GLN   A CD  1 
ATOM   1233 O  OE1 . GLN   A 1 172 ? 115.584 108.526 93.071  1.00 41.08 ? 172 GLN   A OE1 1 
ATOM   1234 N  NE2 . GLN   A 1 172 ? 115.063 106.637 91.980  1.00 41.08 ? 172 GLN   A NE2 1 
ATOM   1235 N  N   . LEU   A 1 173 ? 110.083 108.610 95.004  1.00 40.91 ? 173 LEU   A N   1 
ATOM   1236 C  CA  . LEU   A 1 173 ? 109.405 109.029 96.223  1.00 40.87 ? 173 LEU   A CA  1 
ATOM   1237 C  C   . LEU   A 1 173 ? 109.485 107.917 97.271  1.00 40.86 ? 173 LEU   A C   1 
ATOM   1238 O  O   . LEU   A 1 173 ? 109.770 108.190 98.437  1.00 40.77 ? 173 LEU   A O   1 
ATOM   1239 C  CB  . LEU   A 1 173 ? 107.959 109.407 95.887  1.00 40.86 ? 173 LEU   A CB  1 
ATOM   1240 C  CG  . LEU   A 1 173 ? 107.156 110.159 96.960  1.00 40.86 ? 173 LEU   A CG  1 
ATOM   1241 C  CD1 . LEU   A 1 173 ? 106.078 111.022 96.307  1.00 40.87 ? 173 LEU   A CD1 1 
ATOM   1242 C  CD2 . LEU   A 1 173 ? 106.519 109.235 98.000  1.00 40.86 ? 173 LEU   A CD2 1 
ATOM   1243 N  N   . ASP   A 1 174 ? 109.258 106.668 96.838  1.00 40.88 ? 174 ASP   A N   1 
ATOM   1244 C  CA  . ASP   A 1 174 ? 109.229 105.518 97.731  1.00 40.87 ? 174 ASP   A CA  1 
ATOM   1245 C  C   . ASP   A 1 174 ? 110.623 105.216 98.283  1.00 40.84 ? 174 ASP   A C   1 
ATOM   1246 O  O   . ASP   A 1 174 ? 110.740 104.518 99.289  1.00 40.83 ? 174 ASP   A O   1 
ATOM   1247 C  CB  . ASP   A 1 174 ? 108.630 104.298 97.045  1.00 40.90 ? 174 ASP   A CB  1 
ATOM   1248 C  CG  . ASP   A 1 174 ? 107.192 104.441 96.563  1.00 40.91 ? 174 ASP   A CG  1 
ATOM   1249 O  OD1 . ASP   A 1 174 ? 106.608 105.530 96.751  1.00 40.91 ? 174 ASP   A OD1 1 
ATOM   1250 O  OD2 . ASP   A 1 174 ? 106.665 103.458 96.000  1.00 40.92 ? 174 ASP   A OD2 1 
ATOM   1251 N  N   . VAL   A 1 175 ? 111.670 105.722 97.614  1.00 40.81 ? 175 VAL   A N   1 
ATOM   1252 C  CA  . VAL   A 1 175 ? 113.049 105.550 98.055  1.00 40.78 ? 175 VAL   A CA  1 
ATOM   1253 C  C   . VAL   A 1 175 ? 113.477 106.769 98.876  1.00 40.74 ? 175 VAL   A C   1 
ATOM   1254 O  O   . VAL   A 1 175 ? 114.164 106.616 99.884  1.00 40.74 ? 175 VAL   A O   1 
ATOM   1255 C  CB  . VAL   A 1 175 ? 113.998 105.310 96.859  1.00 40.79 ? 175 VAL   A CB  1 
ATOM   1256 C  CG1 . VAL   A 1 175 ? 115.455 105.139 97.292  1.00 40.78 ? 175 VAL   A CG1 1 
ATOM   1257 C  CG2 . VAL   A 1 175 ? 113.558 104.123 96.002  1.00 40.79 ? 175 VAL   A CG2 1 
ATOM   1258 N  N   . VAL   A 1 176 ? 113.060 107.971 98.446  1.00 40.71 ? 176 VAL   A N   1 
ATOM   1259 C  CA  . VAL   A 1 176 ? 113.522 109.225 99.029  1.00 40.65 ? 176 VAL   A CA  1 
ATOM   1260 C  C   . VAL   A 1 176 ? 113.029 109.334 100.473 1.00 40.62 ? 176 VAL   A C   1 
ATOM   1261 O  O   . VAL   A 1 176 ? 113.838 109.515 101.381 1.00 40.56 ? 176 VAL   A O   1 
ATOM   1262 C  CB  . VAL   A 1 176 ? 113.096 110.452 98.189  1.00 40.66 ? 176 VAL   A CB  1 
ATOM   1263 C  CG1 . VAL   A 1 176 ? 113.218 111.768 98.958  1.00 40.64 ? 176 VAL   A CG1 1 
ATOM   1264 C  CG2 . VAL   A 1 176 ? 113.858 110.543 96.868  1.00 40.67 ? 176 VAL   A CG2 1 
ATOM   1265 N  N   . LEU   A 1 177 ? 111.708 109.219 100.679 1.00 40.61 ? 177 LEU   A N   1 
ATOM   1266 C  CA  . LEU   A 1 177 ? 111.099 109.536 101.966 1.00 40.55 ? 177 LEU   A CA  1 
ATOM   1267 C  C   . LEU   A 1 177 ? 111.746 108.711 103.085 1.00 40.51 ? 177 LEU   A C   1 
ATOM   1268 O  O   . LEU   A 1 177 ? 112.143 109.292 104.096 1.00 40.44 ? 177 LEU   A O   1 
ATOM   1269 C  CB  . LEU   A 1 177 ? 109.574 109.370 101.932 1.00 40.54 ? 177 LEU   A CB  1 
ATOM   1270 C  CG  . LEU   A 1 177 ? 108.729 110.589 101.528 1.00 40.53 ? 177 LEU   A CG  1 
ATOM   1271 C  CD1 . LEU   A 1 177 ? 108.772 111.692 102.588 1.00 40.53 ? 177 LEU   A CD1 1 
ATOM   1272 C  CD2 . LEU   A 1 177 ? 109.091 111.159 100.154 1.00 40.54 ? 177 LEU   A CD2 1 
ATOM   1273 N  N   . PRO   A 1 178 ? 111.890 107.363 102.972 1.00 40.50 ? 178 PRO   A N   1 
ATOM   1274 C  CA  . PRO   A 1 178 ? 112.610 106.584 103.985 1.00 40.48 ? 178 PRO   A CA  1 
ATOM   1275 C  C   . PRO   A 1 178 ? 113.952 107.170 104.428 1.00 40.45 ? 178 PRO   A C   1 
ATOM   1276 O  O   . PRO   A 1 178 ? 114.289 107.091 105.607 1.00 40.41 ? 178 PRO   A O   1 
ATOM   1277 C  CB  . PRO   A 1 178 ? 112.847 105.237 103.284 1.00 40.49 ? 178 PRO   A CB  1 
ATOM   1278 C  CG  . PRO   A 1 178 ? 111.651 105.087 102.378 1.00 40.50 ? 178 PRO   A CG  1 
ATOM   1279 C  CD  . PRO   A 1 178 ? 111.334 106.496 101.916 1.00 40.50 ? 178 PRO   A CD  1 
ATOM   1280 N  N   . VAL   A 1 179 ? 114.705 107.753 103.483 1.00 40.43 ? 179 VAL   A N   1 
ATOM   1281 C  CA  . VAL   A 1 179 ? 116.013 108.324 103.777 1.00 40.39 ? 179 VAL   A CA  1 
ATOM   1282 C  C   . VAL   A 1 179 ? 115.814 109.564 104.651 1.00 40.36 ? 179 VAL   A C   1 
ATOM   1283 O  O   . VAL   A 1 179 ? 116.512 109.727 105.651 1.00 40.33 ? 179 VAL   A O   1 
ATOM   1284 C  CB  . VAL   A 1 179 ? 116.837 108.646 102.508 1.00 40.38 ? 179 VAL   A CB  1 
ATOM   1285 C  CG1 . VAL   A 1 179 ? 118.154 109.352 102.826 1.00 40.37 ? 179 VAL   A CG1 1 
ATOM   1286 C  CG2 . VAL   A 1 179 ? 117.096 107.403 101.658 1.00 40.37 ? 179 VAL   A CG2 1 
ATOM   1287 N  N   . ARG   A 1 180 ? 114.852 110.422 104.279 1.00 40.36 ? 180 ARG   A N   1 
ATOM   1288 C  CA  . ARG   A 1 180 ? 114.558 111.626 105.044 1.00 40.33 ? 180 ARG   A CA  1 
ATOM   1289 C  C   . ARG   A 1 180 ? 114.113 111.253 106.459 1.00 40.35 ? 180 ARG   A C   1 
ATOM   1290 O  O   . ARG   A 1 180 ? 114.487 111.933 107.414 1.00 40.33 ? 180 ARG   A O   1 
ATOM   1291 C  CB  . ARG   A 1 180 ? 113.510 112.527 104.372 1.00 40.32 ? 180 ARG   A CB  1 
ATOM   1292 C  CG  . ARG   A 1 180 ? 114.043 113.740 103.618 1.00 40.31 ? 180 ARG   A CG  1 
ATOM   1293 C  CD  . ARG   A 1 180 ? 114.597 113.469 102.223 1.00 40.31 ? 180 ARG   A CD  1 
ATOM   1294 N  NE  . ARG   A 1 180 ? 114.953 114.713 101.527 1.00 40.31 ? 180 ARG   A NE  1 
ATOM   1295 C  CZ  . ARG   A 1 180 ? 114.103 115.630 101.059 1.00 40.30 ? 180 ARG   A CZ  1 
ATOM   1296 N  NH1 . ARG   A 1 180 ? 112.795 115.434 101.118 1.00 40.31 ? 180 ARG   A NH1 1 
ATOM   1297 N  NH2 . ARG   A 1 180 ? 114.563 116.744 100.514 1.00 40.30 ? 180 ARG   A NH2 1 
ATOM   1298 N  N   . LEU   A 1 181 ? 113.323 110.176 106.587 1.00 40.37 ? 181 LEU   A N   1 
ATOM   1299 C  CA  . LEU   A 1 181 ? 112.872 109.698 107.887 1.00 40.37 ? 181 LEU   A CA  1 
ATOM   1300 C  C   . LEU   A 1 181 ? 114.062 109.130 108.664 1.00 40.34 ? 181 LEU   A C   1 
ATOM   1301 O  O   . LEU   A 1 181 ? 114.152 109.329 109.874 1.00 40.31 ? 181 LEU   A O   1 
ATOM   1302 C  CB  . LEU   A 1 181 ? 111.750 108.669 107.722 1.00 40.40 ? 181 LEU   A CB  1 
ATOM   1303 C  CG  . LEU   A 1 181 ? 110.955 108.299 108.984 1.00 40.42 ? 181 LEU   A CG  1 
ATOM   1304 C  CD1 . LEU   A 1 181 ? 109.509 107.953 108.635 1.00 40.43 ? 181 LEU   A CD1 1 
ATOM   1305 C  CD2 . LEU   A 1 181 ? 111.581 107.146 109.773 1.00 40.43 ? 181 LEU   A CD2 1 
ATOM   1306 N  N   . GLU   A 1 182 ? 114.966 108.429 107.964 1.00 40.33 ? 182 GLU   A N   1 
ATOM   1307 C  CA  . GLU   A 1 182 ? 116.141 107.835 108.587 1.00 40.30 ? 182 GLU   A CA  1 
ATOM   1308 C  C   . GLU   A 1 182 ? 116.993 108.935 109.221 1.00 40.26 ? 182 GLU   A C   1 
ATOM   1309 O  O   . GLU   A 1 182 ? 117.388 108.812 110.380 1.00 40.23 ? 182 GLU   A O   1 
ATOM   1310 C  CB  . GLU   A 1 182 ? 116.949 107.007 107.583 1.00 40.32 ? 182 GLU   A CB  1 
ATOM   1311 C  CG  . GLU   A 1 182 ? 118.003 106.098 108.213 1.00 40.35 ? 182 GLU   A CG  1 
ATOM   1312 C  CD  . GLU   A 1 182 ? 117.485 104.881 108.966 1.00 40.38 ? 182 GLU   A CD  1 
ATOM   1313 O  OE1 . GLU   A 1 182 ? 118.327 104.193 109.580 1.00 40.39 ? 182 GLU   A OE1 1 
ATOM   1314 O  OE2 . GLU   A 1 182 ? 116.266 104.604 108.941 1.00 40.38 ? 182 GLU   A OE2 1 
ATOM   1315 N  N   . LEU   A 1 183 ? 117.268 110.006 108.460 1.00 40.26 ? 183 LEU   A N   1 
ATOM   1316 C  CA  . LEU   A 1 183 ? 118.006 111.148 108.984 1.00 40.24 ? 183 LEU   A CA  1 
ATOM   1317 C  C   . LEU   A 1 183 ? 117.210 111.783 110.125 1.00 40.24 ? 183 LEU   A C   1 
ATOM   1318 O  O   . LEU   A 1 183 ? 117.769 112.047 111.186 1.00 40.21 ? 183 LEU   A O   1 
ATOM   1319 C  CB  . LEU   A 1 183 ? 118.338 112.184 107.905 1.00 40.25 ? 183 LEU   A CB  1 
ATOM   1320 C  CG  . LEU   A 1 183 ? 119.632 111.964 107.107 1.00 40.26 ? 183 LEU   A CG  1 
ATOM   1321 C  CD1 . LEU   A 1 183 ? 119.485 110.906 106.016 1.00 40.28 ? 183 LEU   A CD1 1 
ATOM   1322 C  CD2 . LEU   A 1 183 ? 120.134 113.281 106.518 1.00 40.26 ? 183 LEU   A CD2 1 
ATOM   1323 N  N   . CYS   A 1 184 ? 115.909 112.013 109.901 1.00 40.25 ? 184 CYS   A N   1 
ATOM   1324 C  CA  . CYS   A 1 184 ? 115.045 112.617 110.907 1.00 40.22 ? 184 CYS   A CA  1 
ATOM   1325 C  C   . CYS   A 1 184 ? 115.177 111.880 112.241 1.00 40.21 ? 184 CYS   A C   1 
ATOM   1326 O  O   . CYS   A 1 184 ? 115.286 112.516 113.286 1.00 40.18 ? 184 CYS   A O   1 
ATOM   1327 C  CB  . CYS   A 1 184 ? 113.591 112.638 110.447 1.00 40.23 ? 184 CYS   A CB  1 
ATOM   1328 S  SG  . CYS   A 1 184 ? 112.450 113.334 111.669 1.00 40.25 ? 184 CYS   A SG  1 
ATOM   1329 N  N   . LEU   A 1 185 ? 115.179 110.541 112.193 1.00 40.23 ? 185 LEU   A N   1 
ATOM   1330 C  CA  . LEU   A 1 185 ? 115.201 109.723 113.397 1.00 40.21 ? 185 LEU   A CA  1 
ATOM   1331 C  C   . LEU   A 1 185 ? 116.598 109.748 114.018 1.00 40.19 ? 185 LEU   A C   1 
ATOM   1332 O  O   . LEU   A 1 185 ? 116.750 110.137 115.176 1.00 40.19 ? 185 LEU   A O   1 
ATOM   1333 C  CB  . LEU   A 1 185 ? 114.739 108.303 113.054 1.00 40.24 ? 185 LEU   A CB  1 
ATOM   1334 C  CG  . LEU   A 1 185 ? 114.285 107.410 114.219 1.00 40.27 ? 185 LEU   A CG  1 
ATOM   1335 C  CD1 . LEU   A 1 185 ? 113.388 106.287 113.700 1.00 40.28 ? 185 LEU   A CD1 1 
ATOM   1336 C  CD2 . LEU   A 1 185 ? 115.444 106.821 115.026 1.00 40.28 ? 185 LEU   A CD2 1 
ATOM   1337 N  N   . VAL   A 1 186 ? 117.613 109.359 113.233 1.00 40.18 ? 186 VAL   A N   1 
ATOM   1338 C  CA  . VAL   A 1 186 ? 118.927 109.031 113.770 1.00 40.16 ? 186 VAL   A CA  1 
ATOM   1339 C  C   . VAL   A 1 186 ? 119.691 110.318 114.093 1.00 40.15 ? 186 VAL   A C   1 
ATOM   1340 O  O   . VAL   A 1 186 ? 120.415 110.360 115.086 1.00 40.16 ? 186 VAL   A O   1 
ATOM   1341 C  CB  . VAL   A 1 186 ? 119.727 108.111 112.820 1.00 40.16 ? 186 VAL   A CB  1 
ATOM   1342 C  CG1 . VAL   A 1 186 ? 121.137 107.817 113.334 1.00 40.17 ? 186 VAL   A CG1 1 
ATOM   1343 C  CG2 . VAL   A 1 186 ? 118.993 106.801 112.532 1.00 40.17 ? 186 VAL   A CG2 1 
ATOM   1344 N  N   . LEU   A 1 187 ? 119.519 111.365 113.270 1.00 40.14 ? 187 LEU   A N   1 
ATOM   1345 C  CA  . LEU   A 1 187 ? 120.329 112.572 113.379 1.00 40.11 ? 187 LEU   A CA  1 
ATOM   1346 C  C   . LEU   A 1 187 ? 119.614 113.649 114.201 1.00 40.08 ? 187 LEU   A C   1 
ATOM   1347 O  O   . LEU   A 1 187 ? 120.159 114.741 114.362 1.00 40.06 ? 187 LEU   A O   1 
ATOM   1348 C  CB  . LEU   A 1 187 ? 120.706 113.100 111.989 1.00 40.13 ? 187 LEU   A CB  1 
ATOM   1349 C  CG  . LEU   A 1 187 ? 121.849 112.408 111.226 1.00 40.16 ? 187 LEU   A CG  1 
ATOM   1350 C  CD1 . LEU   A 1 187 ? 123.215 112.693 111.854 1.00 40.16 ? 187 LEU   A CD1 1 
ATOM   1351 C  CD2 . LEU   A 1 187 ? 121.652 110.904 111.045 1.00 40.18 ? 187 LEU   A CD2 1 
ATOM   1352 N  N   . PHE   A 1 188 ? 118.412 113.359 114.727 1.00 40.09 ? 188 PHE   A N   1 
ATOM   1353 C  CA  . PHE   A 1 188 ? 117.698 114.325 115.553 1.00 40.09 ? 188 PHE   A CA  1 
ATOM   1354 C  C   . PHE   A 1 188 ? 117.057 113.633 116.758 1.00 40.14 ? 188 PHE   A C   1 
ATOM   1355 O  O   . PHE   A 1 188 ? 117.402 113.955 117.895 1.00 40.13 ? 188 PHE   A O   1 
ATOM   1356 C  CB  . PHE   A 1 188 ? 116.692 115.109 114.700 1.00 40.05 ? 188 PHE   A CB  1 
ATOM   1357 C  CG  . PHE   A 1 188 ? 115.767 116.035 115.481 1.00 40.03 ? 188 PHE   A CG  1 
ATOM   1358 C  CD1 . PHE   A 1 188 ? 116.220 117.263 115.959 1.00 40.03 ? 188 PHE   A CD1 1 
ATOM   1359 C  CD2 . PHE   A 1 188 ? 114.441 115.683 115.724 1.00 40.02 ? 188 PHE   A CD2 1 
ATOM   1360 C  CE1 . PHE   A 1 188 ? 115.374 118.103 116.670 1.00 40.05 ? 188 PHE   A CE1 1 
ATOM   1361 C  CE2 . PHE   A 1 188 ? 113.600 116.529 116.433 1.00 40.03 ? 188 PHE   A CE2 1 
ATOM   1362 C  CZ  . PHE   A 1 188 ? 114.067 117.736 116.904 1.00 40.04 ? 188 PHE   A CZ  1 
ATOM   1363 N  N   . PHE   A 1 189 ? 116.139 112.685 116.514 1.00 40.18 ? 189 PHE   A N   1 
ATOM   1364 C  CA  . PHE   A 1 189 ? 115.323 112.120 117.582 1.00 40.20 ? 189 PHE   A CA  1 
ATOM   1365 C  C   . PHE   A 1 189 ? 116.195 111.351 118.577 1.00 40.18 ? 189 PHE   A C   1 
ATOM   1366 O  O   . PHE   A 1 189 ? 115.833 111.256 119.749 1.00 40.19 ? 189 PHE   A O   1 
ATOM   1367 C  CB  . PHE   A 1 189 ? 114.191 111.221 117.063 1.00 40.23 ? 189 PHE   A CB  1 
ATOM   1368 C  CG  . PHE   A 1 189 ? 112.954 111.917 116.500 1.00 40.26 ? 189 PHE   A CG  1 
ATOM   1369 C  CD1 . PHE   A 1 189 ? 112.416 113.056 117.102 1.00 40.27 ? 189 PHE   A CD1 1 
ATOM   1370 C  CD2 . PHE   A 1 189 ? 112.310 111.411 115.373 1.00 40.29 ? 189 PHE   A CD2 1 
ATOM   1371 C  CE1 . PHE   A 1 189 ? 111.285 113.670 116.581 1.00 40.28 ? 189 PHE   A CE1 1 
ATOM   1372 C  CE2 . PHE   A 1 189 ? 111.179 112.030 114.858 1.00 40.30 ? 189 PHE   A CE2 1 
ATOM   1373 C  CZ  . PHE   A 1 189 ? 110.670 113.158 115.462 1.00 40.29 ? 189 PHE   A CZ  1 
ATOM   1374 N  N   . ILE   A 1 190 ? 117.330 110.802 118.118 1.00 40.15 ? 190 ILE   A N   1 
ATOM   1375 C  CA  . ILE   A 1 190 ? 118.262 110.127 119.015 1.00 40.14 ? 190 ILE   A CA  1 
ATOM   1376 C  C   . ILE   A 1 190 ? 119.040 111.183 119.813 1.00 40.12 ? 190 ILE   A C   1 
ATOM   1377 O  O   . ILE   A 1 190 ? 119.009 111.135 121.043 1.00 40.14 ? 190 ILE   A O   1 
ATOM   1378 C  CB  . ILE   A 1 190 ? 119.171 109.130 118.254 1.00 40.16 ? 190 ILE   A CB  1 
ATOM   1379 C  CG1 . ILE   A 1 190 ? 118.368 107.997 117.558 1.00 40.19 ? 190 ILE   A CG1 1 
ATOM   1380 C  CG2 . ILE   A 1 190 ? 120.279 108.576 119.159 1.00 40.17 ? 190 ILE   A CG2 1 
ATOM   1381 C  CD1 . ILE   A 1 190 ? 117.605 107.054 118.479 1.00 40.20 ? 190 ILE   A CD1 1 
ATOM   1382 N  N   . PRO   A 1 191 ? 119.756 112.161 119.193 1.00 40.10 ? 191 PRO   A N   1 
ATOM   1383 C  CA  . PRO   A 1 191 ? 120.326 113.284 119.946 1.00 40.09 ? 191 PRO   A CA  1 
ATOM   1384 C  C   . PRO   A 1 191 ? 119.392 113.914 120.980 1.00 40.09 ? 191 PRO   A C   1 
ATOM   1385 O  O   . PRO   A 1 191 ? 119.839 114.266 122.069 1.00 40.13 ? 191 PRO   A O   1 
ATOM   1386 C  CB  . PRO   A 1 191 ? 120.647 114.307 118.845 1.00 40.09 ? 191 PRO   A CB  1 
ATOM   1387 C  CG  . PRO   A 1 191 ? 121.017 113.456 117.654 1.00 40.11 ? 191 PRO   A CG  1 
ATOM   1388 C  CD  . PRO   A 1 191 ? 120.162 112.209 117.776 1.00 40.11 ? 191 PRO   A CD  1 
ATOM   1389 N  N   . MET   A 1 192 ? 118.104 114.053 120.630 1.00 40.11 ? 192 MET   A N   1 
ATOM   1390 C  CA  . MET   A 1 192 ? 117.103 114.606 121.532 1.00 40.14 ? 192 MET   A CA  1 
ATOM   1391 C  C   . MET   A 1 192 ? 117.055 113.780 122.818 1.00 40.15 ? 192 MET   A C   1 
ATOM   1392 O  O   . MET   A 1 192 ? 117.066 114.345 123.912 1.00 40.17 ? 192 MET   A O   1 
ATOM   1393 C  CB  . MET   A 1 192 ? 115.721 114.635 120.861 1.00 40.16 ? 192 MET   A CB  1 
ATOM   1394 C  CG  . MET   A 1 192 ? 114.592 115.185 121.724 1.00 40.17 ? 192 MET   A CG  1 
ATOM   1395 S  SD  . MET   A 1 192 ? 114.806 116.910 122.210 1.00 40.19 ? 192 MET   A SD  1 
ATOM   1396 C  CE  . MET   A 1 192 ? 113.312 117.164 123.177 1.00 40.21 ? 192 MET   A CE  1 
ATOM   1397 N  N   . ALA   A 1 193 ? 117.020 112.446 122.674 1.00 40.16 ? 193 ALA   A N   1 
ATOM   1398 C  CA  . ALA   A 1 193 ? 116.900 111.539 123.806 1.00 40.17 ? 193 ALA   A CA  1 
ATOM   1399 C  C   . ALA   A 1 193 ? 118.126 111.639 124.715 1.00 40.16 ? 193 ALA   A C   1 
ATOM   1400 O  O   . ALA   A 1 193 ? 118.002 111.479 125.927 1.00 40.18 ? 193 ALA   A O   1 
ATOM   1401 C  CB  . ALA   A 1 193 ? 116.695 110.120 123.317 1.00 40.18 ? 193 ALA   A CB  1 
ATOM   1402 N  N   . VAL   A 1 194 ? 119.301 111.898 124.122 1.00 40.15 ? 194 VAL   A N   1 
ATOM   1403 C  CA  . VAL   A 1 194 ? 120.542 112.023 124.876 1.00 40.14 ? 194 VAL   A CA  1 
ATOM   1404 C  C   . VAL   A 1 194 ? 120.553 113.379 125.585 1.00 40.15 ? 194 VAL   A C   1 
ATOM   1405 O  O   . VAL   A 1 194 ? 120.762 113.439 126.797 1.00 40.22 ? 194 VAL   A O   1 
ATOM   1406 C  CB  . VAL   A 1 194 ? 121.790 111.838 123.982 1.00 40.14 ? 194 VAL   A CB  1 
ATOM   1407 C  CG1 . VAL   A 1 194 ? 123.094 112.077 124.743 1.00 40.15 ? 194 VAL   A CG1 1 
ATOM   1408 C  CG2 . VAL   A 1 194 ? 121.815 110.470 123.300 1.00 40.14 ? 194 VAL   A CG2 1 
ATOM   1409 N  N   . THR   A 1 195 ? 120.312 114.454 124.820 1.00 40.16 ? 195 THR   A N   1 
ATOM   1410 C  CA  . THR   A 1 195 ? 120.430 115.822 125.308 1.00 40.17 ? 195 THR   A CA  1 
ATOM   1411 C  C   . THR   A 1 195 ? 119.599 116.000 126.581 1.00 40.20 ? 195 THR   A C   1 
ATOM   1412 O  O   . THR   A 1 195 ? 120.100 116.538 127.568 1.00 40.24 ? 195 THR   A O   1 
ATOM   1413 C  CB  . THR   A 1 195 ? 120.005 116.797 124.206 1.00 40.18 ? 195 THR   A CB  1 
ATOM   1414 O  OG1 . THR   A 1 195 ? 120.829 116.495 123.085 1.00 40.19 ? 195 THR   A OG1 1 
ATOM   1415 C  CG2 . THR   A 1 195 ? 120.196 118.258 124.578 1.00 40.17 ? 195 THR   A CG2 1 
ATOM   1416 N  N   . ILE   A 1 196 ? 118.340 115.538 126.552 1.00 40.23 ? 196 ILE   A N   1 
ATOM   1417 C  CA  . ILE   A 1 196 ? 117.425 115.731 127.672 1.00 40.27 ? 196 ILE   A CA  1 
ATOM   1418 C  C   . ILE   A 1 196 ? 117.871 114.861 128.850 1.00 40.29 ? 196 ILE   A C   1 
ATOM   1419 O  O   . ILE   A 1 196 ? 117.736 115.279 129.999 1.00 40.31 ? 196 ILE   A O   1 
ATOM   1420 C  CB  . ILE   A 1 196 ? 115.949 115.477 127.275 1.00 40.29 ? 196 ILE   A CB  1 
ATOM   1421 C  CG1 . ILE   A 1 196 ? 115.648 114.005 126.885 1.00 40.31 ? 196 ILE   A CG1 1 
ATOM   1422 C  CG2 . ILE   A 1 196 ? 115.502 116.452 126.180 1.00 40.29 ? 196 ILE   A CG2 1 
ATOM   1423 C  CD1 . ILE   A 1 196 ? 115.107 113.142 128.014 1.00 40.32 ? 196 ILE   A CD1 1 
ATOM   1424 N  N   . PHE   A 1 197 ? 118.417 113.670 128.560 1.00 40.29 ? 197 PHE   A N   1 
ATOM   1425 C  CA  . PHE   A 1 197 ? 118.829 112.732 129.595 1.00 40.32 ? 197 PHE   A CA  1 
ATOM   1426 C  C   . PHE   A 1 197 ? 120.000 113.319 130.381 1.00 40.30 ? 197 PHE   A C   1 
ATOM   1427 O  O   . PHE   A 1 197 ? 120.043 113.196 131.604 1.00 40.30 ? 197 PHE   A O   1 
ATOM   1428 C  CB  . PHE   A 1 197 ? 119.182 111.369 128.986 1.00 40.35 ? 197 PHE   A CB  1 
ATOM   1429 C  CG  . PHE   A 1 197 ? 119.728 110.339 129.968 1.00 40.39 ? 197 PHE   A CG  1 
ATOM   1430 C  CD1 . PHE   A 1 197 ? 118.868 109.545 130.724 1.00 40.42 ? 197 PHE   A CD1 1 
ATOM   1431 C  CD2 . PHE   A 1 197 ? 121.100 110.156 130.124 1.00 40.40 ? 197 PHE   A CD2 1 
ATOM   1432 C  CE1 . PHE   A 1 197 ? 119.368 108.606 131.616 1.00 40.42 ? 197 PHE   A CE1 1 
ATOM   1433 C  CE2 . PHE   A 1 197 ? 121.595 109.215 131.017 1.00 40.41 ? 197 PHE   A CE2 1 
ATOM   1434 C  CZ  . PHE   A 1 197 ? 120.729 108.442 131.760 1.00 40.42 ? 197 PHE   A CZ  1 
ATOM   1435 N  N   . CYS   A 1 198 ? 120.942 113.951 129.667 1.00 40.28 ? 198 CYS   A N   1 
ATOM   1436 C  CA  . CYS   A 1 198 ? 122.122 114.535 130.286 1.00 40.29 ? 198 CYS   A CA  1 
ATOM   1437 C  C   . CYS   A 1 198 ? 121.739 115.771 131.100 1.00 40.30 ? 198 CYS   A C   1 
ATOM   1438 O  O   . CYS   A 1 198 ? 122.037 115.839 132.291 1.00 40.37 ? 198 CYS   A O   1 
ATOM   1439 C  CB  . CYS   A 1 198 ? 123.177 114.887 129.243 1.00 40.28 ? 198 CYS   A CB  1 
ATOM   1440 S  SG  . CYS   A 1 198 ? 123.768 113.457 128.300 1.00 40.28 ? 198 CYS   A SG  1 
ATOM   1441 N  N   . TYR   A 1 199 ? 121.062 116.732 130.454 1.00 40.30 ? 199 TYR   A N   1 
ATOM   1442 C  CA  . TYR   A 1 199 ? 120.832 118.044 131.044 1.00 40.32 ? 199 TYR   A CA  1 
ATOM   1443 C  C   . TYR   A 1 199 ? 119.882 117.940 132.237 1.00 40.35 ? 199 TYR   A C   1 
ATOM   1444 O  O   . TYR   A 1 199 ? 120.046 118.683 133.203 1.00 40.38 ? 199 TYR   A O   1 
ATOM   1445 C  CB  . TYR   A 1 199 ? 120.335 119.050 129.998 1.00 40.31 ? 199 TYR   A CB  1 
ATOM   1446 C  CG  . TYR   A 1 199 ? 121.436 119.696 129.164 1.00 40.29 ? 199 TYR   A CG  1 
ATOM   1447 C  CD1 . TYR   A 1 199 ? 122.513 120.346 129.764 1.00 40.29 ? 199 TYR   A CD1 1 
ATOM   1448 C  CD2 . TYR   A 1 199 ? 121.412 119.641 127.774 1.00 40.30 ? 199 TYR   A CD2 1 
ATOM   1449 C  CE1 . TYR   A 1 199 ? 123.519 120.929 129.011 1.00 40.28 ? 199 TYR   A CE1 1 
ATOM   1450 C  CE2 . TYR   A 1 199 ? 122.413 120.220 127.010 1.00 40.29 ? 199 TYR   A CE2 1 
ATOM   1451 C  CZ  . TYR   A 1 199 ? 123.470 120.865 127.630 1.00 40.28 ? 199 TYR   A CZ  1 
ATOM   1452 O  OH  . TYR   A 1 199 ? 124.462 121.437 126.888 1.00 40.27 ? 199 TYR   A OH  1 
ATOM   1453 N  N   . TRP   A 1 200 ? 118.904 117.025 132.177 1.00 40.38 ? 200 TRP   A N   1 
ATOM   1454 C  CA  . TRP   A 1 200 ? 118.014 116.795 133.307 1.00 40.43 ? 200 TRP   A CA  1 
ATOM   1455 C  C   . TRP   A 1 200 ? 118.826 116.448 134.556 1.00 40.45 ? 200 TRP   A C   1 
ATOM   1456 O  O   . TRP   A 1 200 ? 118.486 116.892 135.651 1.00 40.47 ? 200 TRP   A O   1 
ATOM   1457 C  CB  . TRP   A 1 200 ? 116.990 115.694 132.993 1.00 40.46 ? 200 TRP   A CB  1 
ATOM   1458 C  CG  . TRP   A 1 200 ? 116.074 115.372 134.145 1.00 40.49 ? 200 TRP   A CG  1 
ATOM   1459 C  CD1 . TRP   A 1 200 ? 116.155 114.298 134.982 1.00 40.50 ? 200 TRP   A CD1 1 
ATOM   1460 C  CD2 . TRP   A 1 200 ? 114.947 116.152 134.601 1.00 40.50 ? 200 TRP   A CD2 1 
ATOM   1461 N  NE1 . TRP   A 1 200 ? 115.155 114.345 135.916 1.00 40.51 ? 200 TRP   A NE1 1 
ATOM   1462 C  CE2 . TRP   A 1 200 ? 114.400 115.470 135.711 1.00 40.51 ? 200 TRP   A CE2 1 
ATOM   1463 C  CE3 . TRP   A 1 200 ? 114.349 117.348 134.183 1.00 40.48 ? 200 TRP   A CE3 1 
ATOM   1464 C  CZ2 . TRP   A 1 200 ? 113.287 115.947 136.402 1.00 40.50 ? 200 TRP   A CZ2 1 
ATOM   1465 C  CZ3 . TRP   A 1 200 ? 113.250 117.819 134.869 1.00 40.48 ? 200 TRP   A CZ3 1 
ATOM   1466 C  CH2 . TRP   A 1 200 ? 112.729 117.127 135.963 1.00 40.49 ? 200 TRP   A CH2 1 
ATOM   1467 N  N   . ARG   A 1 201 ? 119.896 115.660 134.378 1.00 40.45 ? 201 ARG   A N   1 
ATOM   1468 C  CA  . ARG   A 1 201 ? 120.765 115.272 135.480 1.00 40.48 ? 201 ARG   A CA  1 
ATOM   1469 C  C   . ARG   A 1 201 ? 121.703 116.429 135.828 1.00 40.47 ? 201 ARG   A C   1 
ATOM   1470 O  O   . ARG   A 1 201 ? 121.829 116.781 136.998 1.00 40.53 ? 201 ARG   A O   1 
ATOM   1471 C  CB  . ARG   A 1 201 ? 121.539 113.989 135.147 1.00 40.48 ? 201 ARG   A CB  1 
ATOM   1472 C  CG  . ARG   A 1 201 ? 120.677 112.737 135.040 1.00 40.49 ? 201 ARG   A CG  1 
ATOM   1473 C  CD  . ARG   A 1 201 ? 121.469 111.487 134.674 1.00 40.51 ? 201 ARG   A CD  1 
ATOM   1474 N  NE  . ARG   A 1 201 ? 120.618 110.291 134.610 1.00 40.53 ? 201 ARG   A NE  1 
ATOM   1475 C  CZ  . ARG   A 1 201 ? 120.737 109.159 135.312 1.00 40.55 ? 201 ARG   A CZ  1 
ATOM   1476 N  NH1 . ARG   A 1 201 ? 119.856 108.188 135.127 1.00 40.55 ? 201 ARG   A NH1 1 
ATOM   1477 N  NH2 . ARG   A 1 201 ? 121.712 108.980 136.192 1.00 40.56 ? 201 ARG   A NH2 1 
ATOM   1478 N  N   . PHE   A 1 202 ? 122.341 117.023 134.808 1.00 40.43 ? 202 PHE   A N   1 
ATOM   1479 C  CA  . PHE   A 1 202 ? 123.310 118.092 135.007 1.00 40.42 ? 202 PHE   A CA  1 
ATOM   1480 C  C   . PHE   A 1 202 ? 122.693 119.216 135.840 1.00 40.44 ? 202 PHE   A C   1 
ATOM   1481 O  O   . PHE   A 1 202 ? 123.315 119.684 136.793 1.00 40.50 ? 202 PHE   A O   1 
ATOM   1482 C  CB  . PHE   A 1 202 ? 123.825 118.625 133.663 1.00 40.38 ? 202 PHE   A CB  1 
ATOM   1483 C  CG  . PHE   A 1 202 ? 124.787 119.807 133.743 1.00 40.33 ? 202 PHE   A CG  1 
ATOM   1484 C  CD1 . PHE   A 1 202 ? 125.875 119.800 134.616 1.00 40.33 ? 202 PHE   A CD1 1 
ATOM   1485 C  CD2 . PHE   A 1 202 ? 124.594 120.936 132.948 1.00 40.31 ? 202 PHE   A CD2 1 
ATOM   1486 C  CE1 . PHE   A 1 202 ? 126.741 120.883 134.680 1.00 40.32 ? 202 PHE   A CE1 1 
ATOM   1487 C  CE2 . PHE   A 1 202 ? 125.463 122.016 133.020 1.00 40.29 ? 202 PHE   A CE2 1 
ATOM   1488 C  CZ  . PHE   A 1 202 ? 126.533 121.987 133.885 1.00 40.30 ? 202 PHE   A CZ  1 
ATOM   1489 N  N   . VAL   A 1 203 ? 121.474 119.639 135.474 1.00 40.43 ? 203 VAL   A N   1 
ATOM   1490 C  CA  . VAL   A 1 203 ? 120.784 120.719 136.168 1.00 40.47 ? 203 VAL   A CA  1 
ATOM   1491 C  C   . VAL   A 1 203 ? 120.510 120.288 137.611 1.00 40.53 ? 203 VAL   A C   1 
ATOM   1492 O  O   . VAL   A 1 203 ? 120.670 121.092 138.527 1.00 40.59 ? 203 VAL   A O   1 
ATOM   1493 C  CB  . VAL   A 1 203 ? 119.490 121.155 135.442 1.00 40.46 ? 203 VAL   A CB  1 
ATOM   1494 C  CG1 . VAL   A 1 203 ? 118.596 122.044 136.305 1.00 40.47 ? 203 VAL   A CG1 1 
ATOM   1495 C  CG2 . VAL   A 1 203 ? 119.787 121.839 134.108 1.00 40.46 ? 203 VAL   A CG2 1 
ATOM   1496 N  N   . TRP   A 1 204 ? 120.112 119.022 137.804 1.00 40.58 ? 204 TRP   A N   1 
ATOM   1497 C  CA  . TRP   A 1 204 ? 119.820 118.493 139.129 1.00 40.63 ? 204 TRP   A CA  1 
ATOM   1498 C  C   . TRP   A 1 204 ? 121.077 118.515 140.001 1.00 40.63 ? 204 TRP   A C   1 
ATOM   1499 O  O   . TRP   A 1 204 ? 121.002 118.866 141.178 1.00 40.67 ? 204 TRP   A O   1 
ATOM   1500 C  CB  . TRP   A 1 204 ? 119.243 117.072 139.027 1.00 40.68 ? 204 TRP   A CB  1 
ATOM   1501 C  CG  . TRP   A 1 204 ? 118.739 116.504 140.329 1.00 40.74 ? 204 TRP   A CG  1 
ATOM   1502 C  CD1 . TRP   A 1 204 ? 119.146 115.342 140.915 1.00 40.76 ? 204 TRP   A CD1 1 
ATOM   1503 C  CD2 . TRP   A 1 204 ? 117.709 117.047 141.186 1.00 40.78 ? 204 TRP   A CD2 1 
ATOM   1504 N  NE1 . TRP   A 1 204 ? 118.465 115.133 142.084 1.00 40.78 ? 204 TRP   A NE1 1 
ATOM   1505 C  CE2 . TRP   A 1 204 ? 117.574 116.156 142.275 1.00 40.80 ? 204 TRP   A CE2 1 
ATOM   1506 C  CE3 . TRP   A 1 204 ? 116.897 118.188 141.147 1.00 40.78 ? 204 TRP   A CE3 1 
ATOM   1507 C  CZ2 . TRP   A 1 204 ? 116.664 116.375 143.308 1.00 40.80 ? 204 TRP   A CZ2 1 
ATOM   1508 C  CZ3 . TRP   A 1 204 ? 115.996 118.401 142.168 1.00 40.79 ? 204 TRP   A CZ3 1 
ATOM   1509 C  CH2 . TRP   A 1 204 ? 115.882 117.506 143.232 1.00 40.80 ? 204 TRP   A CH2 1 
ATOM   1510 N  N   . ILE   A 1 205 ? 122.222 118.143 139.410 1.00 40.60 ? 205 ILE   A N   1 
ATOM   1511 C  CA  . ILE   A 1 205 ? 123.503 118.134 140.105 1.00 40.60 ? 205 ILE   A CA  1 
ATOM   1512 C  C   . ILE   A 1 205 ? 123.882 119.569 140.476 1.00 40.60 ? 205 ILE   A C   1 
ATOM   1513 O  O   . ILE   A 1 205 ? 124.328 119.814 141.595 1.00 40.59 ? 205 ILE   A O   1 
ATOM   1514 C  CB  . ILE   A 1 205 ? 124.593 117.442 139.253 1.00 40.61 ? 205 ILE   A CB  1 
ATOM   1515 C  CG1 . ILE   A 1 205 ? 124.323 115.924 139.057 1.00 40.61 ? 205 ILE   A CG1 1 
ATOM   1516 C  CG2 . ILE   A 1 205 ? 126.000 117.704 139.807 1.00 40.60 ? 205 ILE   A CG2 1 
ATOM   1517 C  CD1 . ILE   A 1 205 ? 124.460 115.056 140.300 1.00 40.62 ? 205 ILE   A CD1 1 
ATOM   1518 N  N   . MET   A 1 206 ? 123.697 120.507 139.535 1.00 40.60 ? 206 MET   A N   1 
ATOM   1519 C  CA  . MET   A 1 206 ? 124.032 121.908 139.759 1.00 40.63 ? 206 MET   A CA  1 
ATOM   1520 C  C   . MET   A 1 206 ? 123.115 122.516 140.821 1.00 40.66 ? 206 MET   A C   1 
ATOM   1521 O  O   . MET   A 1 206 ? 123.562 123.346 141.611 1.00 40.67 ? 206 MET   A O   1 
ATOM   1522 C  CB  . MET   A 1 206 ? 123.921 122.723 138.462 1.00 40.64 ? 206 MET   A CB  1 
ATOM   1523 C  CG  . MET   A 1 206 ? 125.052 122.503 137.464 1.00 40.63 ? 206 MET   A CG  1 
ATOM   1524 S  SD  . MET   A 1 206 ? 126.448 123.632 137.656 1.00 40.64 ? 206 MET   A SD  1 
ATOM   1525 C  CE  . MET   A 1 206 ? 127.434 122.950 138.996 1.00 40.65 ? 206 MET   A CE  1 
ATOM   1526 N  N   . LEU   A 1 207 ? 121.839 122.103 140.831 1.00 40.68 ? 207 LEU   A N   1 
ATOM   1527 C  CA  . LEU   A 1 207 ? 120.863 122.610 141.786 1.00 40.74 ? 207 LEU   A CA  1 
ATOM   1528 C  C   . LEU   A 1 207 ? 121.184 122.077 143.183 1.00 40.75 ? 207 LEU   A C   1 
ATOM   1529 O  O   . LEU   A 1 207 ? 121.155 122.837 144.150 1.00 40.75 ? 207 LEU   A O   1 
ATOM   1530 C  CB  . LEU   A 1 207 ? 119.445 122.231 141.350 1.00 40.77 ? 207 LEU   A CB  1 
ATOM   1531 C  CG  . LEU   A 1 207 ? 118.282 122.839 142.150 1.00 40.80 ? 207 LEU   A CG  1 
ATOM   1532 C  CD1 . LEU   A 1 207 ? 118.101 124.336 141.894 1.00 40.81 ? 207 LEU   A CD1 1 
ATOM   1533 C  CD2 . LEU   A 1 207 ? 116.984 122.086 141.866 1.00 40.81 ? 207 LEU   A CD2 1 
ATOM   1534 N  N   . SER   A 1 208 ? 121.481 120.772 143.277 1.00 40.75 ? 208 SER   A N   1 
ATOM   1535 C  CA  . SER   A 1 208 ? 121.776 120.134 144.552 1.00 40.78 ? 208 SER   A CA  1 
ATOM   1536 C  C   . SER   A 1 208 ? 123.107 120.659 145.114 1.00 40.77 ? 208 SER   A C   1 
ATOM   1537 O  O   . SER   A 1 208 ? 124.058 120.800 144.313 1.00 40.75 ? 208 SER   A O   1 
ATOM   1538 C  CB  . SER   A 1 208 ? 121.797 118.628 144.423 1.00 40.79 ? 208 SER   A CB  1 
ATOM   1539 O  OG  . SER   A 1 208 ? 122.785 118.206 143.493 1.00 40.79 ? 208 SER   A OG  1 
ATOM   1540 N  N   . VAL   A 1 318 ? 129.102 134.057 142.982 1.00 40.92 ? 318 VAL   A N   1 
ATOM   1541 C  CA  . VAL   A 1 318 ? 129.670 133.191 141.898 1.00 40.93 ? 318 VAL   A CA  1 
ATOM   1542 C  C   . VAL   A 1 318 ? 128.767 131.971 141.697 1.00 40.91 ? 318 VAL   A C   1 
ATOM   1543 O  O   . VAL   A 1 318 ? 128.520 131.579 140.558 1.00 40.86 ? 318 VAL   A O   1 
ATOM   1544 C  CB  . VAL   A 1 318 ? 131.144 132.772 142.119 1.00 40.95 ? 318 VAL   A CB  1 
ATOM   1545 C  CG1 . VAL   A 1 318 ? 132.110 133.929 141.864 1.00 40.95 ? 318 VAL   A CG1 1 
ATOM   1546 C  CG2 . VAL   A 1 318 ? 131.402 132.149 143.493 1.00 40.95 ? 318 VAL   A CG2 1 
ATOM   1547 N  N   . GLY   A 1 319 ? 128.270 131.384 142.797 1.00 40.90 ? 319 GLY   A N   1 
ATOM   1548 C  CA  . GLY   A 1 319 ? 127.395 130.223 142.736 1.00 40.89 ? 319 GLY   A CA  1 
ATOM   1549 C  C   . GLY   A 1 319 ? 126.129 130.506 141.928 1.00 40.88 ? 319 GLY   A C   1 
ATOM   1550 O  O   . GLY   A 1 319 ? 125.701 129.667 141.137 1.00 40.83 ? 319 GLY   A O   1 
ATOM   1551 N  N   . ALA   A 1 320 ? 125.542 131.692 142.142 1.00 40.87 ? 320 ALA   A N   1 
ATOM   1552 C  CA  . ALA   A 1 320 ? 124.364 132.128 141.406 1.00 40.85 ? 320 ALA   A CA  1 
ATOM   1553 C  C   . ALA   A 1 320 ? 124.693 132.294 139.923 1.00 40.83 ? 320 ALA   A C   1 
ATOM   1554 O  O   . ALA   A 1 320 ? 123.879 131.939 139.071 1.00 40.78 ? 320 ALA   A O   1 
ATOM   1555 C  CB  . ALA   A 1 320 ? 123.826 133.414 141.999 1.00 40.86 ? 320 ALA   A CB  1 
ATOM   1556 N  N   . GLN   A 1 321 ? 125.885 132.834 139.628 1.00 40.83 ? 321 GLN   A N   1 
ATOM   1557 C  CA  . GLN   A 1 321 ? 126.333 133.026 138.256 1.00 40.82 ? 321 GLN   A CA  1 
ATOM   1558 C  C   . GLN   A 1 321 ? 126.500 131.662 137.587 1.00 40.80 ? 321 GLN   A C   1 
ATOM   1559 O  O   . GLN   A 1 321 ? 126.037 131.466 136.465 1.00 40.73 ? 321 GLN   A O   1 
ATOM   1560 C  CB  . GLN   A 1 321 ? 127.626 133.846 138.220 1.00 40.83 ? 321 GLN   A CB  1 
ATOM   1561 C  CG  . GLN   A 1 321 ? 128.062 134.301 136.829 1.00 40.84 ? 321 GLN   A CG  1 
ATOM   1562 C  CD  . GLN   A 1 321 ? 127.137 135.332 136.214 1.00 40.84 ? 321 GLN   A CD  1 
ATOM   1563 O  OE1 . GLN   A 1 321 ? 126.978 136.442 136.735 1.00 40.84 ? 321 GLN   A OE1 1 
ATOM   1564 N  NE2 . GLN   A 1 321 ? 126.519 134.983 135.094 1.00 40.83 ? 321 GLN   A NE2 1 
ATOM   1565 N  N   . ARG   A 1 322 ? 127.155 130.728 138.294 1.00 40.80 ? 322 ARG   A N   1 
ATOM   1566 C  CA  . ARG   A 1 322 ? 127.349 129.366 137.817 1.00 40.78 ? 322 ARG   A CA  1 
ATOM   1567 C  C   . ARG   A 1 322 ? 125.993 128.714 137.548 1.00 40.75 ? 322 ARG   A C   1 
ATOM   1568 O  O   . ARG   A 1 322 ? 125.819 128.062 136.519 1.00 40.68 ? 322 ARG   A O   1 
ATOM   1569 C  CB  . ARG   A 1 322 ? 128.171 128.567 138.840 1.00 40.81 ? 322 ARG   A CB  1 
ATOM   1570 C  CG  . ARG   A 1 322 ? 128.542 127.130 138.491 1.00 40.84 ? 322 ARG   A CG  1 
ATOM   1571 C  CD  . ARG   A 1 322 ? 129.636 126.978 137.433 1.00 40.87 ? 322 ARG   A CD  1 
ATOM   1572 N  NE  . ARG   A 1 322 ? 129.167 127.146 136.052 1.00 40.90 ? 322 ARG   A NE  1 
ATOM   1573 C  CZ  . ARG   A 1 322 ? 129.928 127.108 134.957 1.00 40.92 ? 322 ARG   A CZ  1 
ATOM   1574 N  NH1 . ARG   A 1 322 ? 129.375 127.268 133.766 1.00 40.92 ? 322 ARG   A NH1 1 
ATOM   1575 N  NH2 . ARG   A 1 322 ? 131.234 126.912 135.043 1.00 40.93 ? 322 ARG   A NH2 1 
ATOM   1576 N  N   . ARG   A 1 323 ? 125.043 128.900 138.477 1.00 40.74 ? 323 ARG   A N   1 
ATOM   1577 C  CA  . ARG   A 1 323 ? 123.708 128.330 138.358 1.00 40.72 ? 323 ARG   A CA  1 
ATOM   1578 C  C   . ARG   A 1 323 ? 123.012 128.893 137.119 1.00 40.68 ? 323 ARG   A C   1 
ATOM   1579 O  O   . ARG   A 1 323 ? 122.469 128.130 136.321 1.00 40.61 ? 323 ARG   A O   1 
ATOM   1580 C  CB  . ARG   A 1 323 ? 122.891 128.605 139.628 1.00 40.76 ? 323 ARG   A CB  1 
ATOM   1581 C  CG  . ARG   A 1 323 ? 121.566 127.858 139.735 1.00 40.79 ? 323 ARG   A CG  1 
ATOM   1582 C  CD  . ARG   A 1 323 ? 120.768 128.218 140.985 1.00 40.81 ? 323 ARG   A CD  1 
ATOM   1583 N  NE  . ARG   A 1 323 ? 121.480 127.900 142.231 1.00 40.83 ? 323 ARG   A NE  1 
ATOM   1584 C  CZ  . ARG   A 1 323 ? 121.885 128.756 143.174 1.00 40.84 ? 323 ARG   A CZ  1 
ATOM   1585 N  NH1 . ARG   A 1 323 ? 122.521 128.297 144.240 1.00 40.85 ? 323 ARG   A NH1 1 
ATOM   1586 N  NH2 . ARG   A 1 323 ? 121.663 130.057 143.069 1.00 40.84 ? 323 ARG   A NH2 1 
ATOM   1587 N  N   . ARG   A 1 324 ? 123.043 130.225 136.964 1.00 40.67 ? 324 ARG   A N   1 
ATOM   1588 C  CA  . ARG   A 1 324 ? 122.359 130.900 135.869 1.00 40.64 ? 324 ARG   A CA  1 
ATOM   1589 C  C   . ARG   A 1 324 ? 122.976 130.481 134.534 1.00 40.58 ? 324 ARG   A C   1 
ATOM   1590 O  O   . ARG   A 1 324 ? 122.249 130.265 133.564 1.00 40.52 ? 324 ARG   A O   1 
ATOM   1591 C  CB  . ARG   A 1 324 ? 122.400 132.421 136.070 1.00 40.68 ? 324 ARG   A CB  1 
ATOM   1592 C  CG  . ARG   A 1 324 ? 121.533 133.231 135.114 1.00 40.71 ? 324 ARG   A CG  1 
ATOM   1593 C  CD  . ARG   A 1 324 ? 121.448 134.710 135.482 1.00 40.74 ? 324 ARG   A CD  1 
ATOM   1594 N  NE  . ARG   A 1 324 ? 120.716 134.932 136.737 1.00 40.75 ? 324 ARG   A NE  1 
ATOM   1595 C  CZ  . ARG   A 1 324 ? 121.210 135.380 137.894 1.00 40.76 ? 324 ARG   A CZ  1 
ATOM   1596 N  NH1 . ARG   A 1 324 ? 120.404 135.539 138.931 1.00 40.76 ? 324 ARG   A NH1 1 
ATOM   1597 N  NH2 . ARG   A 1 324 ? 122.494 135.672 138.029 1.00 40.76 ? 324 ARG   A NH2 1 
ATOM   1598 N  N   . ARG   A 1 325 ? 124.312 130.375 134.494 1.00 40.58 ? 325 ARG   A N   1 
ATOM   1599 C  CA  . ARG   A 1 325 ? 125.021 129.887 133.319 1.00 40.54 ? 325 ARG   A CA  1 
ATOM   1600 C  C   . ARG   A 1 325 ? 124.562 128.467 132.988 1.00 40.52 ? 325 ARG   A C   1 
ATOM   1601 O  O   . ARG   A 1 325 ? 124.200 128.191 131.846 1.00 40.46 ? 325 ARG   A O   1 
ATOM   1602 C  CB  . ARG   A 1 325 ? 126.543 129.915 133.519 1.00 40.55 ? 325 ARG   A CB  1 
ATOM   1603 C  CG  . ARG   A 1 325 ? 127.204 131.283 133.402 1.00 40.55 ? 325 ARG   A CG  1 
ATOM   1604 C  CD  . ARG   A 1 325 ? 128.681 131.253 133.789 1.00 40.56 ? 325 ARG   A CD  1 
ATOM   1605 N  NE  . ARG   A 1 325 ? 129.351 132.552 133.643 1.00 40.57 ? 325 ARG   A NE  1 
ATOM   1606 C  CZ  . ARG   A 1 325 ? 129.719 133.131 132.499 1.00 40.57 ? 325 ARG   A CZ  1 
ATOM   1607 N  NH1 . ARG   A 1 325 ? 130.301 134.319 132.520 1.00 40.57 ? 325 ARG   A NH1 1 
ATOM   1608 N  NH2 . ARG   A 1 325 ? 129.513 132.533 131.337 1.00 40.57 ? 325 ARG   A NH2 1 
ATOM   1609 N  N   . ALA   A 1 326 ? 124.569 127.582 133.998 1.00 40.53 ? 326 ALA   A N   1 
ATOM   1610 C  CA  . ALA   A 1 326 ? 124.287 126.167 133.801 1.00 40.50 ? 326 ALA   A CA  1 
ATOM   1611 C  C   . ALA   A 1 326 ? 122.849 125.958 133.328 1.00 40.46 ? 326 ALA   A C   1 
ATOM   1612 O  O   . ALA   A 1 326 ? 122.616 125.177 132.406 1.00 40.45 ? 326 ALA   A O   1 
ATOM   1613 C  CB  . ALA   A 1 326 ? 124.560 125.398 135.077 1.00 40.51 ? 326 ALA   A CB  1 
ATOM   1614 N  N   . VAL   A 1 327 ? 121.894 126.651 133.966 1.00 40.46 ? 327 VAL   A N   1 
ATOM   1615 C  CA  . VAL   A 1 327 ? 120.487 126.545 133.602 1.00 40.42 ? 327 VAL   A CA  1 
ATOM   1616 C  C   . VAL   A 1 327 ? 120.308 127.137 132.203 1.00 40.39 ? 327 VAL   A C   1 
ATOM   1617 O  O   . VAL   A 1 327 ? 119.779 126.468 131.317 1.00 40.33 ? 327 VAL   A O   1 
ATOM   1618 C  CB  . VAL   A 1 327 ? 119.547 127.210 134.634 1.00 40.43 ? 327 VAL   A CB  1 
ATOM   1619 C  CG1 . VAL   A 1 327 ? 118.114 127.349 134.119 1.00 40.43 ? 327 VAL   A CG1 1 
ATOM   1620 C  CG2 . VAL   A 1 327 ? 119.562 126.481 135.977 1.00 40.44 ? 327 VAL   A CG2 1 
ATOM   1621 N  N   . GLY   A 1 328 ? 120.772 128.382 132.014 1.00 40.39 ? 328 GLY   A N   1 
ATOM   1622 C  CA  . GLY   A 1 328 ? 120.684 129.065 130.732 1.00 40.33 ? 328 GLY   A CA  1 
ATOM   1623 C  C   . GLY   A 1 328 ? 121.167 128.185 129.580 1.00 40.30 ? 328 GLY   A C   1 
ATOM   1624 O  O   . GLY   A 1 328 ? 120.498 128.092 128.552 1.00 40.26 ? 328 GLY   A O   1 
ATOM   1625 N  N   . LEU   A 1 329 ? 122.326 127.539 129.775 1.00 40.30 ? 329 LEU   A N   1 
ATOM   1626 C  CA  . LEU   A 1 329 ? 122.910 126.648 128.783 1.00 40.26 ? 329 LEU   A CA  1 
ATOM   1627 C  C   . LEU   A 1 329 ? 121.899 125.564 128.402 1.00 40.25 ? 329 LEU   A C   1 
ATOM   1628 O  O   . LEU   A 1 329 ? 121.669 125.326 127.217 1.00 40.23 ? 329 LEU   A O   1 
ATOM   1629 C  CB  . LEU   A 1 329 ? 124.206 126.042 129.329 1.00 40.25 ? 329 LEU   A CB  1 
ATOM   1630 C  CG  . LEU   A 1 329 ? 125.149 125.378 128.315 1.00 40.23 ? 329 LEU   A CG  1 
ATOM   1631 C  CD1 . LEU   A 1 329 ? 125.953 126.408 127.521 1.00 40.24 ? 329 LEU   A CD1 1 
ATOM   1632 C  CD2 . LEU   A 1 329 ? 126.082 124.387 129.005 1.00 40.23 ? 329 LEU   A CD2 1 
ATOM   1633 N  N   . ALA   A 1 330 ? 121.295 124.926 129.415 1.00 40.26 ? 330 ALA   A N   1 
ATOM   1634 C  CA  . ALA   A 1 330 ? 120.354 123.835 129.201 1.00 40.25 ? 330 ALA   A CA  1 
ATOM   1635 C  C   . ALA   A 1 330 ? 119.095 124.345 128.499 1.00 40.24 ? 330 ALA   A C   1 
ATOM   1636 O  O   . ALA   A 1 330 ? 118.572 123.674 127.611 1.00 40.22 ? 330 ALA   A O   1 
ATOM   1637 C  CB  . ALA   A 1 330 ? 120.019 123.168 130.520 1.00 40.26 ? 330 ALA   A CB  1 
ATOM   1638 N  N   . VAL   A 1 331 ? 118.623 125.534 128.902 1.00 40.24 ? 331 VAL   A N   1 
ATOM   1639 C  CA  . VAL   A 1 331 ? 117.433 126.139 128.318 1.00 40.22 ? 331 VAL   A CA  1 
ATOM   1640 C  C   . VAL   A 1 331 ? 117.666 126.342 126.819 1.00 40.20 ? 331 VAL   A C   1 
ATOM   1641 O  O   . VAL   A 1 331 ? 116.810 125.978 126.015 1.00 40.18 ? 331 VAL   A O   1 
ATOM   1642 C  CB  . VAL   A 1 331 ? 117.035 127.459 129.019 1.00 40.24 ? 331 VAL   A CB  1 
ATOM   1643 C  CG1 . VAL   A 1 331 ? 115.984 128.248 128.237 1.00 40.25 ? 331 VAL   A CG1 1 
ATOM   1644 C  CG2 . VAL   A 1 331 ? 116.564 127.227 130.455 1.00 40.25 ? 331 VAL   A CG2 1 
ATOM   1645 N  N   . VAL   A 1 332 ? 118.829 126.904 126.456 1.00 40.19 ? 332 VAL   A N   1 
ATOM   1646 C  CA  . VAL   A 1 332 ? 119.153 127.197 125.066 1.00 40.16 ? 332 VAL   A CA  1 
ATOM   1647 C  C   . VAL   A 1 332 ? 119.123 125.898 124.257 1.00 40.15 ? 332 VAL   A C   1 
ATOM   1648 O  O   . VAL   A 1 332 ? 118.464 125.840 123.220 1.00 40.12 ? 332 VAL   A O   1 
ATOM   1649 C  CB  . VAL   A 1 332 ? 120.505 127.933 124.918 1.00 40.15 ? 332 VAL   A CB  1 
ATOM   1650 C  CG1 . VAL   A 1 332 ? 121.034 127.917 123.483 1.00 40.15 ? 332 VAL   A CG1 1 
ATOM   1651 C  CG2 . VAL   A 1 332 ? 120.436 129.367 125.442 1.00 40.15 ? 332 VAL   A CG2 1 
ATOM   1652 N  N   . THR   A 1 333 ? 119.824 124.861 124.743 1.00 40.16 ? 333 THR   A N   1 
ATOM   1653 C  CA  . THR   A 1 333 ? 119.952 123.606 124.012 1.00 40.16 ? 333 THR   A CA  1 
ATOM   1654 C  C   . THR   A 1 333 ? 118.572 122.979 123.809 1.00 40.17 ? 333 THR   A C   1 
ATOM   1655 O  O   . THR   A 1 333 ? 118.267 122.522 122.710 1.00 40.17 ? 333 THR   A O   1 
ATOM   1656 C  CB  . THR   A 1 333 ? 120.895 122.639 124.733 1.00 40.17 ? 333 THR   A CB  1 
ATOM   1657 O  OG1 . THR   A 1 333 ? 120.433 122.580 126.079 1.00 40.17 ? 333 THR   A OG1 1 
ATOM   1658 C  CG2 . THR   A 1 333 ? 122.347 123.083 124.697 1.00 40.17 ? 333 THR   A CG2 1 
ATOM   1659 N  N   . LEU   A 1 334 ? 117.755 122.951 124.872 1.00 40.19 ? 334 LEU   A N   1 
ATOM   1660 C  CA  . LEU   A 1 334 ? 116.386 122.461 124.778 1.00 40.18 ? 334 LEU   A CA  1 
ATOM   1661 C  C   . LEU   A 1 334 ? 115.633 123.262 123.716 1.00 40.14 ? 334 LEU   A C   1 
ATOM   1662 O  O   . LEU   A 1 334 ? 115.102 122.680 122.771 1.00 40.09 ? 334 LEU   A O   1 
ATOM   1663 C  CB  . LEU   A 1 334 ? 115.674 122.518 126.135 1.00 40.22 ? 334 LEU   A CB  1 
ATOM   1664 C  CG  . LEU   A 1 334 ? 115.674 121.250 127.005 1.00 40.24 ? 334 LEU   A CG  1 
ATOM   1665 C  CD1 . LEU   A 1 334 ? 114.694 120.207 126.459 1.00 40.25 ? 334 LEU   A CD1 1 
ATOM   1666 C  CD2 . LEU   A 1 334 ? 117.058 120.629 127.216 1.00 40.25 ? 334 LEU   A CD2 1 
ATOM   1667 N  N   . LEU   A 1 335 ? 115.623 124.595 123.867 1.00 40.12 ? 335 LEU   A N   1 
ATOM   1668 C  CA  . LEU   A 1 335 ? 114.870 125.482 122.990 1.00 40.10 ? 335 LEU   A CA  1 
ATOM   1669 C  C   . LEU   A 1 335 ? 115.215 125.184 121.530 1.00 40.07 ? 335 LEU   A C   1 
ATOM   1670 O  O   . LEU   A 1 335 ? 114.312 125.031 120.709 1.00 40.05 ? 335 LEU   A O   1 
ATOM   1671 C  CB  . LEU   A 1 335 ? 115.152 126.938 123.371 1.00 40.12 ? 335 LEU   A CB  1 
ATOM   1672 C  CG  . LEU   A 1 335 ? 114.244 128.015 122.758 1.00 40.14 ? 335 LEU   A CG  1 
ATOM   1673 C  CD1 . LEU   A 1 335 ? 114.164 129.232 123.678 1.00 40.15 ? 335 LEU   A CD1 1 
ATOM   1674 C  CD2 . LEU   A 1 335 ? 114.692 128.448 121.363 1.00 40.14 ? 335 LEU   A CD2 1 
ATOM   1675 N  N   . ASN   A 1 336 ? 116.518 125.086 121.224 1.00 40.05 ? 336 ASN   A N   1 
ATOM   1676 C  CA  . ASN   A 1 336 ? 116.989 124.857 119.864 1.00 40.02 ? 336 ASN   A CA  1 
ATOM   1677 C  C   . ASN   A 1 336 ? 116.256 123.673 119.232 1.00 40.00 ? 336 ASN   A C   1 
ATOM   1678 O  O   . ASN   A 1 336 ? 115.758 123.784 118.113 1.00 39.99 ? 336 ASN   A O   1 
ATOM   1679 C  CB  . ASN   A 1 336 ? 118.502 124.649 119.813 1.00 40.03 ? 336 ASN   A CB  1 
ATOM   1680 C  CG  . ASN   A 1 336 ? 119.283 125.899 120.150 1.00 40.05 ? 336 ASN   A CG  1 
ATOM   1681 O  OD1 . ASN   A 1 336 ? 118.697 126.948 120.441 1.00 40.06 ? 336 ASN   A OD1 1 
ATOM   1682 N  ND2 . ASN   A 1 336 ? 120.606 125.812 120.118 1.00 40.06 ? 336 ASN   A ND2 1 
ATOM   1683 N  N   . PHE   A 1 337 ? 116.184 122.547 119.957 1.00 39.98 ? 337 PHE   A N   1 
ATOM   1684 C  CA  . PHE   A 1 337 ? 115.639 121.313 119.409 1.00 39.93 ? 337 PHE   A CA  1 
ATOM   1685 C  C   . PHE   A 1 337 ? 114.146 121.477 119.120 1.00 39.95 ? 337 PHE   A C   1 
ATOM   1686 O  O   . PHE   A 1 337 ? 113.666 120.985 118.100 1.00 39.96 ? 337 PHE   A O   1 
ATOM   1687 C  CB  . PHE   A 1 337 ? 115.892 120.113 120.331 1.00 39.90 ? 337 PHE   A CB  1 
ATOM   1688 C  CG  . PHE   A 1 337 ? 117.274 119.475 120.223 1.00 39.86 ? 337 PHE   A CG  1 
ATOM   1689 C  CD1 . PHE   A 1 337 ? 118.439 120.234 120.338 1.00 39.84 ? 337 PHE   A CD1 1 
ATOM   1690 C  CD2 . PHE   A 1 337 ? 117.406 118.108 119.987 1.00 39.84 ? 337 PHE   A CD2 1 
ATOM   1691 C  CE1 . PHE   A 1 337 ? 119.689 119.639 120.234 1.00 39.83 ? 337 PHE   A CE1 1 
ATOM   1692 C  CE2 . PHE   A 1 337 ? 118.659 117.521 119.881 1.00 39.82 ? 337 PHE   A CE2 1 
ATOM   1693 C  CZ  . PHE   A 1 337 ? 119.797 118.286 120.006 1.00 39.82 ? 337 PHE   A CZ  1 
ATOM   1694 N  N   . LEU   A 1 338 ? 113.422 122.170 120.012 1.00 39.99 ? 338 LEU   A N   1 
ATOM   1695 C  CA  . LEU   A 1 338 ? 111.975 122.298 119.900 1.00 40.02 ? 338 LEU   A CA  1 
ATOM   1696 C  C   . LEU   A 1 338 ? 111.622 123.356 118.855 1.00 40.02 ? 338 LEU   A C   1 
ATOM   1697 O  O   . LEU   A 1 338 ? 110.827 123.090 117.955 1.00 40.04 ? 338 LEU   A O   1 
ATOM   1698 C  CB  . LEU   A 1 338 ? 111.333 122.624 121.252 1.00 40.05 ? 338 LEU   A CB  1 
ATOM   1699 C  CG  . LEU   A 1 338 ? 111.059 121.444 122.196 1.00 40.09 ? 338 LEU   A CG  1 
ATOM   1700 C  CD1 . LEU   A 1 338 ? 112.323 120.862 122.829 1.00 40.10 ? 338 LEU   A CD1 1 
ATOM   1701 C  CD2 . LEU   A 1 338 ? 110.071 121.859 123.286 1.00 40.11 ? 338 LEU   A CD2 1 
ATOM   1702 N  N   . VAL   A 1 339 ? 112.217 124.550 118.982 1.00 40.02 ? 339 VAL   A N   1 
ATOM   1703 C  CA  . VAL   A 1 339 ? 111.803 125.713 118.210 1.00 40.01 ? 339 VAL   A CA  1 
ATOM   1704 C  C   . VAL   A 1 339 ? 112.512 125.699 116.855 1.00 39.98 ? 339 VAL   A C   1 
ATOM   1705 O  O   . VAL   A 1 339 ? 111.856 125.814 115.822 1.00 39.97 ? 339 VAL   A O   1 
ATOM   1706 C  CB  . VAL   A 1 339 ? 112.059 127.035 118.969 1.00 40.05 ? 339 VAL   A CB  1 
ATOM   1707 C  CG1 . VAL   A 1 339 ? 111.719 128.267 118.131 1.00 40.07 ? 339 VAL   A CG1 1 
ATOM   1708 C  CG2 . VAL   A 1 339 ? 111.323 127.080 120.308 1.00 40.07 ? 339 VAL   A CG2 1 
ATOM   1709 N  N   . CYS   A 1 340 ? 113.845 125.560 116.868 1.00 39.96 ? 340 CYS   A N   1 
ATOM   1710 C  CA  . CYS   A 1 340 ? 114.652 125.787 115.677 1.00 39.95 ? 340 CYS   A CA  1 
ATOM   1711 C  C   . CYS   A 1 340 ? 114.634 124.554 114.772 1.00 39.94 ? 340 CYS   A C   1 
ATOM   1712 O  O   . CYS   A 1 340 ? 114.306 124.666 113.592 1.00 39.95 ? 340 CYS   A O   1 
ATOM   1713 C  CB  . CYS   A 1 340 ? 116.076 126.195 116.042 1.00 39.95 ? 340 CYS   A CB  1 
ATOM   1714 S  SG  . CYS   A 1 340 ? 116.154 127.674 117.087 1.00 39.93 ? 340 CYS   A SG  1 
ATOM   1715 N  N   . PHE   A 1 341 ? 114.979 123.384 115.329 1.00 39.94 ? 341 PHE   A N   1 
ATOM   1716 C  CA  . PHE   A 1 341 ? 115.165 122.175 114.539 1.00 39.92 ? 341 PHE   A CA  1 
ATOM   1717 C  C   . PHE   A 1 341 ? 113.867 121.371 114.447 1.00 39.94 ? 341 PHE   A C   1 
ATOM   1718 O  O   . PHE   A 1 341 ? 113.701 120.594 113.509 1.00 39.95 ? 341 PHE   A O   1 
ATOM   1719 C  CB  . PHE   A 1 341 ? 116.290 121.324 115.141 1.00 39.90 ? 341 PHE   A CB  1 
ATOM   1720 C  CG  . PHE   A 1 341 ? 117.658 121.993 115.232 1.00 39.89 ? 341 PHE   A CG  1 
ATOM   1721 C  CD1 . PHE   A 1 341 ? 118.194 122.703 114.157 1.00 39.89 ? 341 PHE   A CD1 1 
ATOM   1722 C  CD2 . PHE   A 1 341 ? 118.408 121.914 116.403 1.00 39.91 ? 341 PHE   A CD2 1 
ATOM   1723 C  CE1 . PHE   A 1 341 ? 119.440 123.307 114.254 1.00 39.90 ? 341 PHE   A CE1 1 
ATOM   1724 C  CE2 . PHE   A 1 341 ? 119.653 122.521 116.494 1.00 39.91 ? 341 PHE   A CE2 1 
ATOM   1725 C  CZ  . PHE   A 1 341 ? 120.166 123.215 115.421 1.00 39.91 ? 341 PHE   A CZ  1 
ATOM   1726 N  N   . GLY   A 1 342 ? 112.963 121.555 115.421 1.00 39.95 ? 342 GLY   A N   1 
ATOM   1727 C  CA  . GLY   A 1 342 ? 111.731 120.783 115.513 1.00 39.96 ? 342 GLY   A CA  1 
ATOM   1728 C  C   . GLY   A 1 342 ? 110.926 120.781 114.213 1.00 39.96 ? 342 GLY   A C   1 
ATOM   1729 O  O   . GLY   A 1 342 ? 110.847 119.747 113.550 1.00 40.02 ? 342 GLY   A O   1 
ATOM   1730 N  N   . PRO   A 1 343 ? 110.317 121.921 113.795 1.00 39.94 ? 343 PRO   A N   1 
ATOM   1731 C  CA  . PRO   A 1 343 ? 109.309 121.914 112.730 1.00 39.96 ? 343 PRO   A CA  1 
ATOM   1732 C  C   . PRO   A 1 343 ? 109.793 121.304 111.413 1.00 39.98 ? 343 PRO   A C   1 
ATOM   1733 O  O   . PRO   A 1 343 ? 109.009 120.673 110.707 1.00 40.06 ? 343 PRO   A O   1 
ATOM   1734 C  CB  . PRO   A 1 343 ? 108.953 123.399 112.528 1.00 39.95 ? 343 PRO   A CB  1 
ATOM   1735 C  CG  . PRO   A 1 343 ? 110.102 124.162 113.152 1.00 39.95 ? 343 PRO   A CG  1 
ATOM   1736 C  CD  . PRO   A 1 343 ? 110.585 123.283 114.286 1.00 39.94 ? 343 PRO   A CD  1 
ATOM   1737 N  N   . TYR   A 1 344 ? 111.082 121.492 111.099 1.00 39.96 ? 344 TYR   A N   1 
ATOM   1738 C  CA  . TYR   A 1 344 ? 111.676 120.949 109.886 1.00 39.94 ? 344 TYR   A CA  1 
ATOM   1739 C  C   . TYR   A 1 344 ? 111.658 119.421 109.942 1.00 39.99 ? 344 TYR   A C   1 
ATOM   1740 O  O   . TYR   A 1 344 ? 111.277 118.771 108.968 1.00 40.06 ? 344 TYR   A O   1 
ATOM   1741 C  CB  . TYR   A 1 344 ? 113.100 121.487 109.710 1.00 39.90 ? 344 TYR   A CB  1 
ATOM   1742 C  CG  . TYR   A 1 344 ? 113.785 121.113 108.400 1.00 39.86 ? 344 TYR   A CG  1 
ATOM   1743 C  CD1 . TYR   A 1 344 ? 113.188 121.374 107.169 1.00 39.85 ? 344 TYR   A CD1 1 
ATOM   1744 C  CD2 . TYR   A 1 344 ? 115.027 120.482 108.395 1.00 39.83 ? 344 TYR   A CD2 1 
ATOM   1745 C  CE1 . TYR   A 1 344 ? 113.809 121.033 105.978 1.00 39.84 ? 344 TYR   A CE1 1 
ATOM   1746 C  CE2 . TYR   A 1 344 ? 115.655 120.133 107.210 1.00 39.83 ? 344 TYR   A CE2 1 
ATOM   1747 C  CZ  . TYR   A 1 344 ? 115.044 120.410 105.999 1.00 39.83 ? 344 TYR   A CZ  1 
ATOM   1748 O  OH  . TYR   A 1 344 ? 115.652 120.072 104.825 1.00 39.84 ? 344 TYR   A OH  1 
ATOM   1749 N  N   . ASN   A 1 345 ? 112.065 118.861 111.090 1.00 40.01 ? 345 ASN   A N   1 
ATOM   1750 C  CA  . ASN   A 1 345 ? 112.169 117.419 111.258 1.00 40.04 ? 345 ASN   A CA  1 
ATOM   1751 C  C   . ASN   A 1 345 ? 110.778 116.802 111.408 1.00 40.06 ? 345 ASN   A C   1 
ATOM   1752 O  O   . ASN   A 1 345 ? 110.590 115.634 111.074 1.00 40.11 ? 345 ASN   A O   1 
ATOM   1753 C  CB  . ASN   A 1 345 ? 113.101 117.056 112.411 1.00 40.04 ? 345 ASN   A CB  1 
ATOM   1754 C  CG  . ASN   A 1 345 ? 114.558 117.144 112.019 1.00 40.04 ? 345 ASN   A CG  1 
ATOM   1755 O  OD1 . ASN   A 1 345 ? 115.260 118.067 112.446 1.00 40.04 ? 345 ASN   A OD1 1 
ATOM   1756 N  ND2 . ASN   A 1 345 ? 115.033 116.206 111.211 1.00 40.04 ? 345 ASN   A ND2 1 
ATOM   1757 N  N   . VAL   A 1 346 ? 109.812 117.586 111.909 1.00 40.08 ? 346 VAL   A N   1 
ATOM   1758 C  CA  . VAL   A 1 346 ? 108.418 117.163 111.939 1.00 40.14 ? 346 VAL   A CA  1 
ATOM   1759 C  C   . VAL   A 1 346 ? 107.902 117.111 110.499 1.00 40.16 ? 346 VAL   A C   1 
ATOM   1760 O  O   . VAL   A 1 346 ? 107.268 116.132 110.106 1.00 40.25 ? 346 VAL   A O   1 
ATOM   1761 C  CB  . VAL   A 1 346 ? 107.534 118.068 112.829 1.00 40.18 ? 346 VAL   A CB  1 
ATOM   1762 C  CG1 . VAL   A 1 346 ? 106.044 117.765 112.678 1.00 40.19 ? 346 VAL   A CG1 1 
ATOM   1763 C  CG2 . VAL   A 1 346 ? 107.943 118.002 114.300 1.00 40.19 ? 346 VAL   A CG2 1 
ATOM   1764 N  N   . SER   A 1 347 ? 108.202 118.161 109.719 1.00 40.17 ? 347 SER   A N   1 
ATOM   1765 C  CA  . SER   A 1 347 ? 107.737 118.282 108.344 1.00 40.22 ? 347 SER   A CA  1 
ATOM   1766 C  C   . SER   A 1 347 ? 108.156 117.068 107.515 1.00 40.21 ? 347 SER   A C   1 
ATOM   1767 O  O   . SER   A 1 347 ? 107.401 116.626 106.651 1.00 40.22 ? 347 SER   A O   1 
ATOM   1768 C  CB  . SER   A 1 347 ? 108.229 119.562 107.711 1.00 40.23 ? 347 SER   A CB  1 
ATOM   1769 O  OG  . SER   A 1 347 ? 107.601 119.786 106.457 1.00 40.26 ? 347 SER   A OG  1 
ATOM   1770 N  N   . HIS   A 1 348 ? 109.365 116.548 107.773 1.00 40.18 ? 348 HIS   A N   1 
ATOM   1771 C  CA  . HIS   A 1 348 ? 109.842 115.331 107.129 1.00 40.22 ? 348 HIS   A CA  1 
ATOM   1772 C  C   . HIS   A 1 348 ? 108.915 114.159 107.452 1.00 40.26 ? 348 HIS   A C   1 
ATOM   1773 O  O   . HIS   A 1 348 ? 108.507 113.433 106.548 1.00 40.31 ? 348 HIS   A O   1 
ATOM   1774 C  CB  . HIS   A 1 348 ? 111.294 115.031 107.527 1.00 40.25 ? 348 HIS   A CB  1 
ATOM   1775 C  CG  . HIS   A 1 348 ? 112.319 115.832 106.791 1.00 40.29 ? 348 HIS   A CG  1 
ATOM   1776 N  ND1 . HIS   A 1 348 ? 112.064 117.041 106.180 1.00 40.32 ? 348 HIS   A ND1 1 
ATOM   1777 C  CD2 . HIS   A 1 348 ? 113.614 115.571 106.564 1.00 40.31 ? 348 HIS   A CD2 1 
ATOM   1778 C  CE1 . HIS   A 1 348 ? 113.175 117.487 105.611 1.00 40.33 ? 348 HIS   A CE1 1 
ATOM   1779 N  NE2 . HIS   A 1 348 ? 114.129 116.610 105.833 1.00 40.32 ? 348 HIS   A NE2 1 
ATOM   1780 N  N   . LEU   A 1 349 ? 108.579 113.992 108.740 1.00 40.30 ? 349 LEU   A N   1 
ATOM   1781 C  CA  . LEU   A 1 349 ? 107.785 112.862 109.203 1.00 40.35 ? 349 LEU   A CA  1 
ATOM   1782 C  C   . LEU   A 1 349 ? 106.375 112.931 108.613 1.00 40.37 ? 349 LEU   A C   1 
ATOM   1783 O  O   . LEU   A 1 349 ? 105.813 111.900 108.246 1.00 40.41 ? 349 LEU   A O   1 
ATOM   1784 C  CB  . LEU   A 1 349 ? 107.767 112.838 110.733 1.00 40.36 ? 349 LEU   A CB  1 
ATOM   1785 C  CG  . LEU   A 1 349 ? 107.061 111.655 111.413 1.00 40.37 ? 349 LEU   A CG  1 
ATOM   1786 C  CD1 . LEU   A 1 349 ? 107.718 110.305 111.122 1.00 40.38 ? 349 LEU   A CD1 1 
ATOM   1787 C  CD2 . LEU   A 1 349 ? 106.979 111.889 112.920 1.00 40.37 ? 349 LEU   A CD2 1 
ATOM   1788 N  N   . VAL   A 1 350 ? 105.822 114.150 108.514 1.00 40.36 ? 350 VAL   A N   1 
ATOM   1789 C  CA  . VAL   A 1 350 ? 104.513 114.374 107.912 1.00 40.39 ? 350 VAL   A CA  1 
ATOM   1790 C  C   . VAL   A 1 350 ? 104.511 113.810 106.489 1.00 40.41 ? 350 VAL   A C   1 
ATOM   1791 O  O   . VAL   A 1 350 ? 103.469 113.374 105.998 1.00 40.50 ? 350 VAL   A O   1 
ATOM   1792 C  CB  . VAL   A 1 350 ? 104.114 115.869 107.938 1.00 40.40 ? 350 VAL   A CB  1 
ATOM   1793 C  CG1 . VAL   A 1 350 ? 102.889 116.173 107.075 1.00 40.40 ? 350 VAL   A CG1 1 
ATOM   1794 C  CG2 . VAL   A 1 350 ? 103.896 116.381 109.362 1.00 40.41 ? 350 VAL   A CG2 1 
ATOM   1795 N  N   . GLY   A 1 351 ? 105.684 113.818 105.839 1.00 40.40 ? 351 GLY   A N   1 
ATOM   1796 C  CA  . GLY   A 1 351 ? 105.872 113.234 104.519 1.00 40.43 ? 351 GLY   A CA  1 
ATOM   1797 C  C   . GLY   A 1 351 ? 105.195 111.872 104.360 1.00 40.46 ? 351 GLY   A C   1 
ATOM   1798 O  O   . GLY   A 1 351 ? 104.630 111.596 103.305 1.00 40.50 ? 351 GLY   A O   1 
ATOM   1799 N  N   . TYR   A 1 352 ? 105.266 111.021 105.395 1.00 40.48 ? 352 TYR   A N   1 
ATOM   1800 C  CA  . TYR   A 1 352 ? 104.660 109.696 105.344 1.00 40.52 ? 352 TYR   A CA  1 
ATOM   1801 C  C   . TYR   A 1 352 ? 103.135 109.809 105.319 1.00 40.54 ? 352 TYR   A C   1 
ATOM   1802 O  O   . TYR   A 1 352 ? 102.482 109.076 104.578 1.00 40.55 ? 352 TYR   A O   1 
ATOM   1803 C  CB  . TYR   A 1 352 ? 105.120 108.796 106.499 1.00 40.54 ? 352 TYR   A CB  1 
ATOM   1804 C  CG  . TYR   A 1 352 ? 106.287 107.866 106.178 1.00 40.57 ? 352 TYR   A CG  1 
ATOM   1805 C  CD1 . TYR   A 1 352 ? 106.251 106.525 106.554 1.00 40.59 ? 352 TYR   A CD1 1 
ATOM   1806 C  CD2 . TYR   A 1 352 ? 107.425 108.319 105.514 1.00 40.58 ? 352 TYR   A CD2 1 
ATOM   1807 C  CE1 . TYR   A 1 352 ? 107.300 105.665 106.270 1.00 40.60 ? 352 TYR   A CE1 1 
ATOM   1808 C  CE2 . TYR   A 1 352 ? 108.480 107.468 105.224 1.00 40.59 ? 352 TYR   A CE2 1 
ATOM   1809 C  CZ  . TYR   A 1 352 ? 108.418 106.138 105.605 1.00 40.60 ? 352 TYR   A CZ  1 
ATOM   1810 O  OH  . TYR   A 1 352 ? 109.455 105.296 105.326 1.00 40.60 ? 352 TYR   A OH  1 
ATOM   1811 N  N   . HIS   A 1 353 ? 102.576 110.716 106.133 1.00 40.57 ? 353 HIS   A N   1 
ATOM   1812 C  CA  . HIS   A 1 353 ? 101.133 110.892 106.221 1.00 40.62 ? 353 HIS   A CA  1 
ATOM   1813 C  C   . HIS   A 1 353 ? 100.573 111.399 104.892 1.00 40.61 ? 353 HIS   A C   1 
ATOM   1814 O  O   . HIS   A 1 353 ? 99.596  110.849 104.388 1.00 40.59 ? 353 HIS   A O   1 
ATOM   1815 C  CB  . HIS   A 1 353 ? 100.758 111.844 107.365 1.00 40.67 ? 353 HIS   A CB  1 
ATOM   1816 C  CG  . HIS   A 1 353 ? 101.064 111.333 108.736 1.00 40.72 ? 353 HIS   A CG  1 
ATOM   1817 N  ND1 . HIS   A 1 353 ? 101.459 112.173 109.755 1.00 40.73 ? 353 HIS   A ND1 1 
ATOM   1818 C  CD2 . HIS   A 1 353 ? 101.034 110.101 109.266 1.00 40.75 ? 353 HIS   A CD2 1 
ATOM   1819 C  CE1 . HIS   A 1 353 ? 101.660 111.463 110.856 1.00 40.74 ? 353 HIS   A CE1 1 
ATOM   1820 N  NE2 . HIS   A 1 353 ? 101.408 110.202 110.581 1.00 40.75 ? 353 HIS   A NE2 1 
ATOM   1821 N  N   . GLN   A 1 354 ? 101.206 112.440 104.331 1.00 40.60 ? 354 GLN   A N   1 
ATOM   1822 C  CA  . GLN   A 1 354 ? 100.641 113.181 103.212 1.00 40.63 ? 354 GLN   A CA  1 
ATOM   1823 C  C   . GLN   A 1 354 ? 101.091 112.586 101.876 1.00 40.61 ? 354 GLN   A C   1 
ATOM   1824 O  O   . GLN   A 1 354 ? 100.326 112.614 100.913 1.00 40.62 ? 354 GLN   A O   1 
ATOM   1825 C  CB  . GLN   A 1 354 ? 101.038 114.656 103.319 1.00 40.67 ? 354 GLN   A CB  1 
ATOM   1826 C  CG  . GLN   A 1 354 ? 100.168 115.613 102.507 1.00 40.70 ? 354 GLN   A CG  1 
ATOM   1827 C  CD  . GLN   A 1 354 ? 98.761  115.762 103.048 1.00 40.73 ? 354 GLN   A CD  1 
ATOM   1828 O  OE1 . GLN   A 1 354 ? 97.782  115.363 102.408 1.00 40.74 ? 354 GLN   A OE1 1 
ATOM   1829 N  NE2 . GLN   A 1 354 ? 98.641  116.338 104.236 1.00 40.73 ? 354 GLN   A NE2 1 
ATOM   1830 N  N   . ARG   A 1 355 ? 102.325 112.057 101.828 1.00 40.59 ? 355 ARG   A N   1 
ATOM   1831 C  CA  . ARG   A 1 355 ? 102.970 111.622 100.594 1.00 40.60 ? 355 ARG   A CA  1 
ATOM   1832 C  C   . ARG   A 1 355 ? 103.087 112.818 99.647  1.00 40.60 ? 355 ARG   A C   1 
ATOM   1833 O  O   . ARG   A 1 355 ? 102.814 112.705 98.452  1.00 40.58 ? 355 ARG   A O   1 
ATOM   1834 C  CB  . ARG   A 1 355 ? 102.259 110.417 99.958  1.00 40.61 ? 355 ARG   A CB  1 
ATOM   1835 C  CG  . ARG   A 1 355 ? 102.187 109.177 100.840 1.00 40.61 ? 355 ARG   A CG  1 
ATOM   1836 C  CD  . ARG   A 1 355 ? 101.473 108.005 100.173 1.00 40.62 ? 355 ARG   A CD  1 
ATOM   1837 N  NE  . ARG   A 1 355 ? 101.363 106.833 101.051 1.00 40.64 ? 355 ARG   A NE  1 
ATOM   1838 C  CZ  . ARG   A 1 355 ? 100.762 105.679 100.755 1.00 40.65 ? 355 ARG   A CZ  1 
ATOM   1839 N  NH1 . ARG   A 1 355 ? 100.736 104.707 101.653 1.00 40.66 ? 355 ARG   A NH1 1 
ATOM   1840 N  NH2 . ARG   A 1 355 ? 100.188 105.490 99.576  1.00 40.66 ? 355 ARG   A NH2 1 
ATOM   1841 N  N   . LYS   A 1 356 ? 103.516 113.958 100.209 1.00 40.61 ? 356 LYS   A N   1 
ATOM   1842 C  CA  . LYS   A 1 356 ? 103.631 115.221 99.495  1.00 40.64 ? 356 LYS   A CA  1 
ATOM   1843 C  C   . LYS   A 1 356 ? 104.430 116.187 100.368 1.00 40.61 ? 356 LYS   A C   1 
ATOM   1844 O  O   . LYS   A 1 356 ? 104.258 116.196 101.586 1.00 40.62 ? 356 LYS   A O   1 
ATOM   1845 C  CB  . LYS   A 1 356 ? 102.240 115.788 99.173  1.00 40.67 ? 356 LYS   A CB  1 
ATOM   1846 C  CG  . LYS   A 1 356 ? 102.174 117.117 98.415  1.00 40.70 ? 356 LYS   A CG  1 
ATOM   1847 C  CD  . LYS   A 1 356 ? 102.604 117.069 96.951  1.00 40.72 ? 356 LYS   A CD  1 
ATOM   1848 C  CE  . LYS   A 1 356 ? 102.440 118.384 96.243  1.00 40.72 ? 356 LYS   A CE  1 
ATOM   1849 N  NZ  . LYS   A 1 356 ? 102.842 118.322 94.835  1.00 40.72 ? 356 LYS   A NZ  1 
ATOM   1850 N  N   . SER   A 1 357 ? 105.297 116.992 99.738  1.00 40.57 ? 357 SER   A N   1 
ATOM   1851 C  CA  . SER   A 1 357 ? 106.112 117.964 100.450 1.00 40.54 ? 357 SER   A CA  1 
ATOM   1852 C  C   . SER   A 1 357 ? 105.216 119.063 101.023 1.00 40.50 ? 357 SER   A C   1 
ATOM   1853 O  O   . SER   A 1 357 ? 104.561 119.770 100.258 1.00 40.50 ? 357 SER   A O   1 
ATOM   1854 C  CB  . SER   A 1 357 ? 107.187 118.539 99.558  1.00 40.55 ? 357 SER   A CB  1 
ATOM   1855 O  OG  . SER   A 1 357 ? 108.022 119.439 100.274 1.00 40.55 ? 357 SER   A OG  1 
ATOM   1856 N  N   . PRO   A 1 358 ? 105.131 119.240 102.368 1.00 40.46 ? 358 PRO   A N   1 
ATOM   1857 C  CA  . PRO   A 1 358 ? 104.268 120.271 102.954 1.00 40.45 ? 358 PRO   A CA  1 
ATOM   1858 C  C   . PRO   A 1 358 ? 104.622 121.689 102.507 1.00 40.46 ? 358 PRO   A C   1 
ATOM   1859 O  O   . PRO   A 1 358 ? 105.791 121.999 102.280 1.00 40.41 ? 358 PRO   A O   1 
ATOM   1860 C  CB  . PRO   A 1 358 ? 104.491 120.130 104.469 1.00 40.44 ? 358 PRO   A CB  1 
ATOM   1861 C  CG  . PRO   A 1 358 ? 104.988 118.713 104.642 1.00 40.44 ? 358 PRO   A CG  1 
ATOM   1862 C  CD  . PRO   A 1 358 ? 105.820 118.451 103.405 1.00 40.44 ? 358 PRO   A CD  1 
ATOM   1863 N  N   . TRP   A 1 359 ? 103.595 122.546 102.418 1.00 40.47 ? 359 TRP   A N   1 
ATOM   1864 C  CA  . TRP   A 1 359 ? 103.739 123.907 101.920 1.00 40.48 ? 359 TRP   A CA  1 
ATOM   1865 C  C   . TRP   A 1 359 ? 104.557 124.759 102.892 1.00 40.44 ? 359 TRP   A C   1 
ATOM   1866 O  O   . TRP   A 1 359 ? 105.172 125.741 102.478 1.00 40.44 ? 359 TRP   A O   1 
ATOM   1867 C  CB  . TRP   A 1 359 ? 102.359 124.535 101.667 1.00 40.51 ? 359 TRP   A CB  1 
ATOM   1868 C  CG  . TRP   A 1 359 ? 101.624 124.957 102.914 1.00 40.54 ? 359 TRP   A CG  1 
ATOM   1869 C  CD1 . TRP   A 1 359 ? 101.732 126.156 103.556 1.00 40.55 ? 359 TRP   A CD1 1 
ATOM   1870 C  CD2 . TRP   A 1 359 ? 100.656 124.188 103.664 1.00 40.58 ? 359 TRP   A CD2 1 
ATOM   1871 N  NE1 . TRP   A 1 359 ? 100.913 126.187 104.652 1.00 40.57 ? 359 TRP   A NE1 1 
ATOM   1872 C  CE2 . TRP   A 1 359 ? 100.239 124.998 104.745 1.00 40.58 ? 359 TRP   A CE2 1 
ATOM   1873 C  CE3 . TRP   A 1 359 ? 100.106 122.907 103.533 1.00 40.60 ? 359 TRP   A CE3 1 
ATOM   1874 C  CZ2 . TRP   A 1 359 ? 99.302  124.566 105.681 1.00 40.59 ? 359 TRP   A CZ2 1 
ATOM   1875 C  CZ3 . TRP   A 1 359 ? 99.179  122.481 104.460 1.00 40.60 ? 359 TRP   A CZ3 1 
ATOM   1876 C  CH2 . TRP   A 1 359 ? 98.783  123.300 105.519 1.00 40.60 ? 359 TRP   A CH2 1 
ATOM   1877 N  N   . TRP   A 1 360 ? 104.562 124.370 104.175 1.00 40.40 ? 360 TRP   A N   1 
ATOM   1878 C  CA  . TRP   A 1 360 ? 105.200 125.144 105.231 1.00 40.38 ? 360 TRP   A CA  1 
ATOM   1879 C  C   . TRP   A 1 360 ? 106.639 124.673 105.468 1.00 40.32 ? 360 TRP   A C   1 
ATOM   1880 O  O   . TRP   A 1 360 ? 107.245 125.037 106.474 1.00 40.26 ? 360 TRP   A O   1 
ATOM   1881 C  CB  . TRP   A 1 360 ? 104.361 125.086 106.520 1.00 40.42 ? 360 TRP   A CB  1 
ATOM   1882 C  CG  . TRP   A 1 360 ? 104.004 123.699 106.993 1.00 40.43 ? 360 TRP   A CG  1 
ATOM   1883 C  CD1 . TRP   A 1 360 ? 102.950 122.940 106.577 1.00 40.44 ? 360 TRP   A CD1 1 
ATOM   1884 C  CD2 . TRP   A 1 360 ? 104.686 122.918 108.000 1.00 40.43 ? 360 TRP   A CD2 1 
ATOM   1885 N  NE1 . TRP   A 1 360 ? 102.936 121.739 107.233 1.00 40.44 ? 360 TRP   A NE1 1 
ATOM   1886 C  CE2 . TRP   A 1 360 ? 103.984 121.696 108.115 1.00 40.43 ? 360 TRP   A CE2 1 
ATOM   1887 C  CE3 . TRP   A 1 360 ? 105.812 123.125 108.805 1.00 40.42 ? 360 TRP   A CE3 1 
ATOM   1888 C  CZ2 . TRP   A 1 360 ? 104.374 120.694 109.001 1.00 40.42 ? 360 TRP   A CZ2 1 
ATOM   1889 C  CZ3 . TRP   A 1 360 ? 106.195 122.134 109.683 1.00 40.41 ? 360 TRP   A CZ3 1 
ATOM   1890 C  CH2 . TRP   A 1 360 ? 105.485 120.936 109.779 1.00 40.41 ? 360 TRP   A CH2 1 
ATOM   1891 N  N   . ARG   A 1 361 ? 107.189 123.888 104.527 1.00 40.28 ? 361 ARG   A N   1 
ATOM   1892 C  CA  . ARG   A 1 361 ? 108.603 123.535 104.539 1.00 40.23 ? 361 ARG   A CA  1 
ATOM   1893 C  C   . ARG   A 1 361 ? 109.457 124.804 104.526 1.00 40.21 ? 361 ARG   A C   1 
ATOM   1894 O  O   . ARG   A 1 361 ? 110.364 124.941 105.345 1.00 40.16 ? 361 ARG   A O   1 
ATOM   1895 C  CB  . ARG   A 1 361 ? 108.965 122.625 103.356 1.00 40.24 ? 361 ARG   A CB  1 
ATOM   1896 C  CG  . ARG   A 1 361 ? 108.849 121.127 103.611 1.00 40.25 ? 361 ARG   A CG  1 
ATOM   1897 C  CD  . ARG   A 1 361 ? 110.064 120.494 104.298 1.00 40.26 ? 361 ARG   A CD  1 
ATOM   1898 N  NE  . ARG   A 1 361 ? 111.062 119.957 103.363 1.00 40.29 ? 361 ARG   A NE  1 
ATOM   1899 C  CZ  . ARG   A 1 361 ? 111.962 120.636 102.648 1.00 40.32 ? 361 ARG   A CZ  1 
ATOM   1900 N  NH1 . ARG   A 1 361 ? 112.088 121.946 102.771 1.00 40.32 ? 361 ARG   A NH1 1 
ATOM   1901 N  NH2 . ARG   A 1 361 ? 112.758 119.990 101.812 1.00 40.34 ? 361 ARG   A NH2 1 
ATOM   1902 N  N   . SER   A 1 362 ? 109.150 125.725 103.601 1.00 40.22 ? 362 SER   A N   1 
ATOM   1903 C  CA  . SER   A 1 362 ? 109.880 126.978 103.468 1.00 40.23 ? 362 SER   A CA  1 
ATOM   1904 C  C   . SER   A 1 362 ? 109.821 127.779 104.769 1.00 40.22 ? 362 SER   A C   1 
ATOM   1905 O  O   . SER   A 1 362 ? 110.784 128.463 105.111 1.00 40.23 ? 362 SER   A O   1 
ATOM   1906 C  CB  . SER   A 1 362 ? 109.361 127.791 102.305 1.00 40.23 ? 362 SER   A CB  1 
ATOM   1907 O  OG  . SER   A 1 362 ? 110.117 128.982 102.133 1.00 40.23 ? 362 SER   A OG  1 
ATOM   1908 N  N   . ILE   A 1 363 ? 108.688 127.691 105.480 1.00 40.20 ? 363 ILE   A N   1 
ATOM   1909 C  CA  . ILE   A 1 363 ? 108.513 128.367 106.758 1.00 40.18 ? 363 ILE   A CA  1 
ATOM   1910 C  C   . ILE   A 1 363 ? 109.372 127.660 107.808 1.00 40.14 ? 363 ILE   A C   1 
ATOM   1911 O  O   . ILE   A 1 363 ? 110.063 128.319 108.583 1.00 40.11 ? 363 ILE   A O   1 
ATOM   1912 C  CB  . ILE   A 1 363 ? 107.022 128.432 107.158 1.00 40.21 ? 363 ILE   A CB  1 
ATOM   1913 C  CG1 . ILE   A 1 363 ? 106.197 129.264 106.148 1.00 40.22 ? 363 ILE   A CG1 1 
ATOM   1914 C  CG2 . ILE   A 1 363 ? 106.852 128.945 108.594 1.00 40.22 ? 363 ILE   A CG2 1 
ATOM   1915 C  CD1 . ILE   A 1 363 ? 104.691 129.060 106.222 1.00 40.22 ? 363 ILE   A CD1 1 
ATOM   1916 N  N   . ALA   A 1 364 ? 109.334 126.320 107.816 1.00 40.14 ? 364 ALA   A N   1 
ATOM   1917 C  CA  . ALA   A 1 364 ? 110.095 125.523 108.769 1.00 40.12 ? 364 ALA   A CA  1 
ATOM   1918 C  C   . ALA   A 1 364 ? 111.592 125.814 108.646 1.00 40.08 ? 364 ALA   A C   1 
ATOM   1919 O  O   . ALA   A 1 364 ? 112.295 125.849 109.655 1.00 40.04 ? 364 ALA   A O   1 
ATOM   1920 C  CB  . ALA   A 1 364 ? 109.802 124.051 108.568 1.00 40.15 ? 364 ALA   A CB  1 
ATOM   1921 N  N   . VAL   A 1 365 ? 112.065 126.032 107.409 1.00 40.05 ? 365 VAL   A N   1 
ATOM   1922 C  CA  . VAL   A 1 365 ? 113.471 126.310 107.144 1.00 40.01 ? 365 VAL   A CA  1 
ATOM   1923 C  C   . VAL   A 1 365 ? 113.902 127.568 107.902 1.00 40.00 ? 365 VAL   A C   1 
ATOM   1924 O  O   . VAL   A 1 365 ? 115.027 127.622 108.398 1.00 39.99 ? 365 VAL   A O   1 
ATOM   1925 C  CB  . VAL   A 1 365 ? 113.759 126.420 105.629 1.00 40.02 ? 365 VAL   A CB  1 
ATOM   1926 C  CG1 . VAL   A 1 365 ? 115.098 127.091 105.325 1.00 40.03 ? 365 VAL   A CG1 1 
ATOM   1927 C  CG2 . VAL   A 1 365 ? 113.678 125.062 104.932 1.00 40.02 ? 365 VAL   A CG2 1 
ATOM   1928 N  N   . VAL   A 1 366 ? 113.009 128.566 108.005 1.00 40.02 ? 366 VAL   A N   1 
ATOM   1929 C  CA  . VAL   A 1 366 ? 113.315 129.802 108.719 1.00 40.00 ? 366 VAL   A CA  1 
ATOM   1930 C  C   . VAL   A 1 366 ? 113.868 129.428 110.096 1.00 39.99 ? 366 VAL   A C   1 
ATOM   1931 O  O   . VAL   A 1 366 ? 114.926 129.915 110.493 1.00 39.98 ? 366 VAL   A O   1 
ATOM   1932 C  CB  . VAL   A 1 366 ? 112.125 130.783 108.861 1.00 40.02 ? 366 VAL   A CB  1 
ATOM   1933 C  CG1 . VAL   A 1 366 ? 112.504 132.043 109.640 1.00 40.02 ? 366 VAL   A CG1 1 
ATOM   1934 C  CG2 . VAL   A 1 366 ? 111.505 131.166 107.518 1.00 40.02 ? 366 VAL   A CG2 1 
ATOM   1935 N  N   . PHE   A 1 367 ? 113.153 128.539 110.801 1.00 39.99 ? 367 PHE   A N   1 
ATOM   1936 C  CA  . PHE   A 1 367 ? 113.501 128.157 112.161 1.00 39.96 ? 367 PHE   A CA  1 
ATOM   1937 C  C   . PHE   A 1 367 ? 114.870 127.476 112.178 1.00 39.97 ? 367 PHE   A C   1 
ATOM   1938 O  O   . PHE   A 1 367 ? 115.653 127.694 113.101 1.00 39.99 ? 367 PHE   A O   1 
ATOM   1939 C  CB  . PHE   A 1 367 ? 112.403 127.266 112.753 1.00 39.93 ? 367 PHE   A CB  1 
ATOM   1940 C  CG  . PHE   A 1 367 ? 111.066 127.960 112.982 1.00 39.91 ? 367 PHE   A CG  1 
ATOM   1941 C  CD1 . PHE   A 1 367 ? 110.076 127.953 112.001 1.00 39.91 ? 367 PHE   A CD1 1 
ATOM   1942 C  CD2 . PHE   A 1 367 ? 110.797 128.616 114.181 1.00 39.91 ? 367 PHE   A CD2 1 
ATOM   1943 C  CE1 . PHE   A 1 367 ? 108.860 128.586 112.213 1.00 39.91 ? 367 PHE   A CE1 1 
ATOM   1944 C  CE2 . PHE   A 1 367 ? 109.578 129.247 114.388 1.00 39.92 ? 367 PHE   A CE2 1 
ATOM   1945 C  CZ  . PHE   A 1 367 ? 108.613 129.231 113.405 1.00 39.92 ? 367 PHE   A CZ  1 
ATOM   1946 N  N   . SER   A 1 368 ? 115.156 126.666 111.148 1.00 39.96 ? 368 SER   A N   1 
ATOM   1947 C  CA  . SER   A 1 368 ? 116.425 125.959 111.044 1.00 39.95 ? 368 SER   A CA  1 
ATOM   1948 C  C   . SER   A 1 368 ? 117.589 126.944 110.938 1.00 39.93 ? 368 SER   A C   1 
ATOM   1949 O  O   . SER   A 1 368 ? 118.684 126.645 111.409 1.00 39.93 ? 368 SER   A O   1 
ATOM   1950 C  CB  . SER   A 1 368 ? 116.427 124.993 109.883 1.00 39.97 ? 368 SER   A CB  1 
ATOM   1951 O  OG  . SER   A 1 368 ? 115.390 124.030 110.017 1.00 39.99 ? 368 SER   A OG  1 
ATOM   1952 N  N   . SER   A 1 369 ? 117.352 128.106 110.310 1.00 39.96 ? 369 SER   A N   1 
ATOM   1953 C  CA  . SER   A 1 369 ? 118.356 129.156 110.217 1.00 39.98 ? 369 SER   A CA  1 
ATOM   1954 C  C   . SER   A 1 369 ? 118.430 129.938 111.528 1.00 39.98 ? 369 SER   A C   1 
ATOM   1955 O  O   . SER   A 1 369 ? 119.513 130.353 111.939 1.00 40.01 ? 369 SER   A O   1 
ATOM   1956 C  CB  . SER   A 1 369 ? 118.079 130.080 109.059 1.00 40.01 ? 369 SER   A CB  1 
ATOM   1957 O  OG  . SER   A 1 369 ? 116.911 130.854 109.290 1.00 40.04 ? 369 SER   A OG  1 
ATOM   1958 N  N   . LEU   A 1 370 ? 117.268 130.126 112.172 1.00 39.98 ? 370 LEU   A N   1 
ATOM   1959 C  CA  . LEU   A 1 370 ? 117.144 130.926 113.384 1.00 39.98 ? 370 LEU   A CA  1 
ATOM   1960 C  C   . LEU   A 1 370 ? 118.159 130.467 114.434 1.00 39.98 ? 370 LEU   A C   1 
ATOM   1961 O  O   . LEU   A 1 370 ? 118.676 131.296 115.181 1.00 40.00 ? 370 LEU   A O   1 
ATOM   1962 C  CB  . LEU   A 1 370 ? 115.703 130.842 113.899 1.00 39.98 ? 370 LEU   A CB  1 
ATOM   1963 C  CG  . LEU   A 1 370 ? 115.193 132.003 114.766 1.00 39.99 ? 370 LEU   A CG  1 
ATOM   1964 C  CD1 . LEU   A 1 370 ? 113.672 132.105 114.666 1.00 39.99 ? 370 LEU   A CD1 1 
ATOM   1965 C  CD2 . LEU   A 1 370 ? 115.606 131.898 116.233 1.00 40.00 ? 370 LEU   A CD2 1 
ATOM   1966 N  N   . ASN   A 1 371 ? 118.459 129.158 114.471 1.00 39.99 ? 371 ASN   A N   1 
ATOM   1967 C  CA  . ASN   A 1 371 ? 119.398 128.599 115.437 1.00 40.01 ? 371 ASN   A CA  1 
ATOM   1968 C  C   . ASN   A 1 371 ? 120.697 129.407 115.458 1.00 40.05 ? 371 ASN   A C   1 
ATOM   1969 O  O   . ASN   A 1 371 ? 121.255 129.636 116.530 1.00 40.10 ? 371 ASN   A O   1 
ATOM   1970 C  CB  . ASN   A 1 371 ? 119.669 127.115 115.190 1.00 39.99 ? 371 ASN   A CB  1 
ATOM   1971 C  CG  . ASN   A 1 371 ? 120.784 126.861 114.201 1.00 39.96 ? 371 ASN   A CG  1 
ATOM   1972 O  OD1 . ASN   A 1 371 ? 121.847 126.362 114.586 1.00 39.93 ? 371 ASN   A OD1 1 
ATOM   1973 N  ND2 . ASN   A 1 371 ? 120.577 127.190 112.933 1.00 39.97 ? 371 ASN   A ND2 1 
ATOM   1974 N  N   . ALA   A 1 372 ? 121.154 129.860 114.280 1.00 40.05 ? 372 ALA   A N   1 
ATOM   1975 C  CA  . ALA   A 1 372 ? 122.438 130.533 114.142 1.00 40.04 ? 372 ALA   A CA  1 
ATOM   1976 C  C   . ALA   A 1 372 ? 122.463 131.852 114.917 1.00 40.03 ? 372 ALA   A C   1 
ATOM   1977 O  O   . ALA   A 1 372 ? 123.541 132.348 115.238 1.00 40.03 ? 372 ALA   A O   1 
ATOM   1978 C  CB  . ALA   A 1 372 ? 122.747 130.756 112.675 1.00 40.04 ? 372 ALA   A CB  1 
ATOM   1979 N  N   . SER   A 1 373 ? 121.280 132.420 115.197 1.00 40.04 ? 373 SER   A N   1 
ATOM   1980 C  CA  . SER   A 1 373 ? 121.170 133.639 115.985 1.00 40.07 ? 373 SER   A CA  1 
ATOM   1981 C  C   . SER   A 1 373 ? 121.258 133.333 117.480 1.00 40.10 ? 373 SER   A C   1 
ATOM   1982 O  O   . SER   A 1 373 ? 121.766 134.155 118.241 1.00 40.11 ? 373 SER   A O   1 
ATOM   1983 C  CB  . SER   A 1 373 ? 119.897 134.384 115.660 1.00 40.09 ? 373 SER   A CB  1 
ATOM   1984 O  OG  . SER   A 1 373 ? 119.828 135.616 116.366 1.00 40.10 ? 373 SER   A OG  1 
ATOM   1985 N  N   . LEU   A 1 374 ? 120.765 132.155 117.894 1.00 40.12 ? 374 LEU   A N   1 
ATOM   1986 C  CA  . LEU   A 1 374 ? 120.652 131.811 119.306 1.00 40.15 ? 374 LEU   A CA  1 
ATOM   1987 C  C   . LEU   A 1 374 ? 121.865 131.007 119.781 1.00 40.15 ? 374 LEU   A C   1 
ATOM   1988 O  O   . LEU   A 1 374 ? 122.094 130.916 120.986 1.00 40.17 ? 374 LEU   A O   1 
ATOM   1989 C  CB  . LEU   A 1 374 ? 119.352 131.043 119.558 1.00 40.17 ? 374 LEU   A CB  1 
ATOM   1990 C  CG  . LEU   A 1 374 ? 118.040 131.828 119.412 1.00 40.20 ? 374 LEU   A CG  1 
ATOM   1991 C  CD1 . LEU   A 1 374 ? 116.853 130.871 119.459 1.00 40.20 ? 374 LEU   A CD1 1 
ATOM   1992 C  CD2 . LEU   A 1 374 ? 117.869 132.929 120.462 1.00 40.20 ? 374 LEU   A CD2 1 
ATOM   1993 N  N   . ASP   A 1 375 ? 122.627 130.421 118.847 1.00 40.15 ? 375 ASP   A N   1 
ATOM   1994 C  CA  . ASP   A 1 375 ? 123.819 129.658 119.191 1.00 40.16 ? 375 ASP   A CA  1 
ATOM   1995 C  C   . ASP   A 1 375 ? 124.845 130.547 119.901 1.00 40.15 ? 375 ASP   A C   1 
ATOM   1996 O  O   . ASP   A 1 375 ? 125.432 130.106 120.887 1.00 40.14 ? 375 ASP   A O   1 
ATOM   1997 C  CB  . ASP   A 1 375 ? 124.394 128.926 117.985 1.00 40.17 ? 375 ASP   A CB  1 
ATOM   1998 C  CG  . ASP   A 1 375 ? 123.595 127.730 117.483 1.00 40.18 ? 375 ASP   A CG  1 
ATOM   1999 O  OD1 . ASP   A 1 375 ? 122.533 127.434 118.071 1.00 40.18 ? 375 ASP   A OD1 1 
ATOM   2000 O  OD2 . ASP   A 1 375 ? 124.045 127.099 116.503 1.00 40.19 ? 375 ASP   A OD2 1 
ATOM   2001 N  N   . PRO   A 1 376 ? 125.125 131.798 119.449 1.00 40.13 ? 376 PRO   A N   1 
ATOM   2002 C  CA  . PRO   A 1 376 ? 125.987 132.716 120.203 1.00 40.13 ? 376 PRO   A CA  1 
ATOM   2003 C  C   . PRO   A 1 376 ? 125.808 132.697 121.723 1.00 40.12 ? 376 PRO   A C   1 
ATOM   2004 O  O   . PRO   A 1 376 ? 126.799 132.695 122.453 1.00 40.13 ? 376 PRO   A O   1 
ATOM   2005 C  CB  . PRO   A 1 376 ? 125.576 134.080 119.627 1.00 40.14 ? 376 PRO   A CB  1 
ATOM   2006 C  CG  . PRO   A 1 376 ? 125.301 133.783 118.170 1.00 40.14 ? 376 PRO   A CG  1 
ATOM   2007 C  CD  . PRO   A 1 376 ? 124.711 132.387 118.162 1.00 40.14 ? 376 PRO   A CD  1 
ATOM   2008 N  N   . LEU   A 1 377 ? 124.550 132.667 122.190 1.00 40.10 ? 377 LEU   A N   1 
ATOM   2009 C  CA  . LEU   A 1 377 ? 124.245 132.690 123.615 1.00 40.09 ? 377 LEU   A CA  1 
ATOM   2010 C  C   . LEU   A 1 377 ? 124.895 131.492 124.308 1.00 40.10 ? 377 LEU   A C   1 
ATOM   2011 O  O   . LEU   A 1 377 ? 125.443 131.640 125.400 1.00 40.13 ? 377 LEU   A O   1 
ATOM   2012 C  CB  . LEU   A 1 377 ? 122.733 132.712 123.857 1.00 40.07 ? 377 LEU   A CB  1 
ATOM   2013 C  CG  . LEU   A 1 377 ? 121.980 133.993 123.468 1.00 40.08 ? 377 LEU   A CG  1 
ATOM   2014 C  CD1 . LEU   A 1 377 ? 120.473 133.742 123.449 1.00 40.08 ? 377 LEU   A CD1 1 
ATOM   2015 C  CD2 . LEU   A 1 377 ? 122.306 135.177 124.382 1.00 40.08 ? 377 LEU   A CD2 1 
ATOM   2016 N  N   . LEU   A 1 378 ? 124.833 130.316 123.663 1.00 40.10 ? 378 LEU   A N   1 
ATOM   2017 C  CA  . LEU   A 1 378 ? 125.448 129.103 124.184 1.00 40.09 ? 378 LEU   A CA  1 
ATOM   2018 C  C   . LEU   A 1 378 ? 126.882 129.400 124.622 1.00 40.12 ? 378 LEU   A C   1 
ATOM   2019 O  O   . LEU   A 1 378 ? 127.286 129.005 125.714 1.00 40.14 ? 378 LEU   A O   1 
ATOM   2020 C  CB  . LEU   A 1 378 ? 125.417 127.990 123.133 1.00 40.07 ? 378 LEU   A CB  1 
ATOM   2021 C  CG  . LEU   A 1 378 ? 125.753 126.571 123.614 1.00 40.07 ? 378 LEU   A CG  1 
ATOM   2022 C  CD1 . LEU   A 1 378 ? 124.540 125.883 124.233 1.00 40.08 ? 378 LEU   A CD1 1 
ATOM   2023 C  CD2 . LEU   A 1 378 ? 126.337 125.726 122.487 1.00 40.08 ? 378 LEU   A CD2 1 
ATOM   2024 N  N   . PHE   A 1 379 ? 127.633 130.106 123.764 1.00 40.14 ? 379 PHE   A N   1 
ATOM   2025 C  CA  . PHE   A 1 379 ? 129.044 130.376 123.998 1.00 40.16 ? 379 PHE   A CA  1 
ATOM   2026 C  C   . PHE   A 1 379 ? 129.196 131.312 125.198 1.00 40.17 ? 379 PHE   A C   1 
ATOM   2027 O  O   . PHE   A 1 379 ? 130.111 131.135 126.002 1.00 40.23 ? 379 PHE   A O   1 
ATOM   2028 C  CB  . PHE   A 1 379 ? 129.707 130.971 122.749 1.00 40.16 ? 379 PHE   A CB  1 
ATOM   2029 C  CG  . PHE   A 1 379 ? 129.474 130.231 121.434 1.00 40.13 ? 379 PHE   A CG  1 
ATOM   2030 C  CD1 . PHE   A 1 379 ? 129.495 128.838 121.366 1.00 40.14 ? 379 PHE   A CD1 1 
ATOM   2031 C  CD2 . PHE   A 1 379 ? 129.230 130.939 120.260 1.00 40.12 ? 379 PHE   A CD2 1 
ATOM   2032 C  CE1 . PHE   A 1 379 ? 129.280 128.182 120.161 1.00 40.14 ? 379 PHE   A CE1 1 
ATOM   2033 C  CE2 . PHE   A 1 379 ? 129.014 130.278 119.059 1.00 40.11 ? 379 PHE   A CE2 1 
ATOM   2034 C  CZ  . PHE   A 1 379 ? 129.038 128.902 119.013 1.00 40.13 ? 379 PHE   A CZ  1 
ATOM   2035 N  N   . TYR   A 1 380 ? 128.295 132.300 125.306 1.00 40.16 ? 380 TYR   A N   1 
ATOM   2036 C  CA  . TYR   A 1 380 ? 128.327 133.273 126.390 1.00 40.16 ? 380 TYR   A CA  1 
ATOM   2037 C  C   . TYR   A 1 380 ? 128.099 132.563 127.724 1.00 40.16 ? 380 TYR   A C   1 
ATOM   2038 O  O   . TYR   A 1 380 ? 128.815 132.827 128.689 1.00 40.18 ? 380 TYR   A O   1 
ATOM   2039 C  CB  . TYR   A 1 380 ? 127.291 134.380 126.161 1.00 40.16 ? 380 TYR   A CB  1 
ATOM   2040 C  CG  . TYR   A 1 380 ? 127.292 135.491 127.205 1.00 40.17 ? 380 TYR   A CG  1 
ATOM   2041 C  CD1 . TYR   A 1 380 ? 128.085 136.624 127.049 1.00 40.18 ? 380 TYR   A CD1 1 
ATOM   2042 C  CD2 . TYR   A 1 380 ? 126.495 135.411 128.345 1.00 40.17 ? 380 TYR   A CD2 1 
ATOM   2043 C  CE1 . TYR   A 1 380 ? 128.089 137.639 127.993 1.00 40.18 ? 380 TYR   A CE1 1 
ATOM   2044 C  CE2 . TYR   A 1 380 ? 126.492 136.418 129.297 1.00 40.18 ? 380 TYR   A CE2 1 
ATOM   2045 C  CZ  . TYR   A 1 380 ? 127.291 137.535 129.120 1.00 40.18 ? 380 TYR   A CZ  1 
ATOM   2046 O  OH  . TYR   A 1 380 ? 127.291 138.532 130.053 1.00 40.20 ? 380 TYR   A OH  1 
ATOM   2047 N  N   . PHE   A 1 381 ? 127.099 131.670 127.767 1.00 40.14 ? 381 PHE   A N   1 
ATOM   2048 C  CA  . PHE   A 1 381 ? 126.761 130.941 128.981 1.00 40.14 ? 381 PHE   A CA  1 
ATOM   2049 C  C   . PHE   A 1 381 ? 127.864 129.937 129.319 1.00 40.17 ? 381 PHE   A C   1 
ATOM   2050 O  O   . PHE   A 1 381 ? 128.151 129.721 130.495 1.00 40.19 ? 381 PHE   A O   1 
ATOM   2051 C  CB  . PHE   A 1 381 ? 125.405 130.238 128.844 1.00 40.12 ? 381 PHE   A CB  1 
ATOM   2052 C  CG  . PHE   A 1 381 ? 124.176 131.144 128.835 1.00 40.11 ? 381 PHE   A CG  1 
ATOM   2053 C  CD1 . PHE   A 1 381 ? 123.992 132.127 129.808 1.00 40.12 ? 381 PHE   A CD1 1 
ATOM   2054 C  CD2 . PHE   A 1 381 ? 123.200 131.008 127.849 1.00 40.12 ? 381 PHE   A CD2 1 
ATOM   2055 C  CE1 . PHE   A 1 381 ? 122.869 132.943 129.792 1.00 40.13 ? 381 PHE   A CE1 1 
ATOM   2056 C  CE2 . PHE   A 1 381 ? 122.081 131.829 127.838 1.00 40.13 ? 381 PHE   A CE2 1 
ATOM   2057 C  CZ  . PHE   A 1 381 ? 121.917 132.793 128.808 1.00 40.13 ? 381 PHE   A CZ  1 
ATOM   2058 N  N   . SER   A 1 382 ? 128.476 129.333 128.290 1.00 40.19 ? 382 SER   A N   1 
ATOM   2059 C  CA  . SER   A 1 382 ? 129.467 128.286 128.490 1.00 40.24 ? 382 SER   A CA  1 
ATOM   2060 C  C   . SER   A 1 382 ? 130.787 128.879 128.984 1.00 40.30 ? 382 SER   A C   1 
ATOM   2061 O  O   . SER   A 1 382 ? 131.224 128.560 130.088 1.00 40.31 ? 382 SER   A O   1 
ATOM   2062 C  CB  . SER   A 1 382 ? 129.670 127.471 127.233 1.00 40.25 ? 382 SER   A CB  1 
ATOM   2063 O  OG  . SER   A 1 382 ? 130.602 126.419 127.448 1.00 40.26 ? 382 SER   A OG  1 
ATOM   2064 N  N   . SER   A 1 383 ? 131.406 129.745 128.167 1.00 40.35 ? 383 SER   A N   1 
ATOM   2065 C  CA  . SER   A 1 383 ? 132.773 130.190 128.400 1.00 40.44 ? 383 SER   A CA  1 
ATOM   2066 C  C   . SER   A 1 383 ? 132.797 131.663 128.807 1.00 40.50 ? 383 SER   A C   1 
ATOM   2067 O  O   . SER   A 1 383 ? 132.213 132.507 128.128 1.00 40.54 ? 383 SER   A O   1 
ATOM   2068 C  CB  . SER   A 1 383 ? 133.633 129.945 127.184 1.00 40.44 ? 383 SER   A CB  1 
ATOM   2069 O  OG  . SER   A 1 383 ? 133.721 128.557 126.893 1.00 40.44 ? 383 SER   A OG  1 
ATOM   2070 N  N   . SER   A 1 384 ? 133.501 131.954 129.910 1.00 40.57 ? 384 SER   A N   1 
ATOM   2071 C  CA  . SER   A 1 384 ? 133.621 133.305 130.439 1.00 40.61 ? 384 SER   A CA  1 
ATOM   2072 C  C   . SER   A 1 384 ? 134.495 134.167 129.529 1.00 40.63 ? 384 SER   A C   1 
ATOM   2073 O  O   . SER   A 1 384 ? 134.287 135.377 129.443 1.00 40.66 ? 384 SER   A O   1 
ATOM   2074 C  CB  . SER   A 1 384 ? 134.160 133.290 131.851 1.00 40.62 ? 384 SER   A CB  1 
ATOM   2075 O  OG  . SER   A 1 384 ? 135.442 132.681 131.905 1.00 40.62 ? 384 SER   A OG  1 
ATOM   2076 N  N   . VAL   A 1 385 ? 135.463 133.536 128.849 1.00 40.63 ? 385 VAL   A N   1 
ATOM   2077 C  CA  . VAL   A 1 385 ? 136.378 134.241 127.961 1.00 40.64 ? 385 VAL   A CA  1 
ATOM   2078 C  C   . VAL   A 1 385 ? 135.565 134.864 126.824 1.00 40.61 ? 385 VAL   A C   1 
ATOM   2079 O  O   . VAL   A 1 385 ? 135.878 135.966 126.378 1.00 40.65 ? 385 VAL   A O   1 
ATOM   2080 C  CB  . VAL   A 1 385 ? 137.514 133.349 127.409 1.00 40.66 ? 385 VAL   A CB  1 
ATOM   2081 C  CG1 . VAL   A 1 385 ? 138.456 134.121 126.485 1.00 40.67 ? 385 VAL   A CG1 1 
ATOM   2082 C  CG2 . VAL   A 1 385 ? 138.311 132.663 128.518 1.00 40.67 ? 385 VAL   A CG2 1 
ATOM   2083 N  N   . VAL   A 1 386 ? 134.521 134.154 126.372 1.00 40.58 ? 386 VAL   A N   1 
ATOM   2084 C  CA  . VAL   A 1 386 ? 133.637 134.651 125.326 1.00 40.58 ? 386 VAL   A CA  1 
ATOM   2085 C  C   . VAL   A 1 386 ? 132.903 135.886 125.851 1.00 40.61 ? 386 VAL   A C   1 
ATOM   2086 O  O   . VAL   A 1 386 ? 132.733 136.858 125.117 1.00 40.64 ? 386 VAL   A O   1 
ATOM   2087 C  CB  . VAL   A 1 386 ? 132.654 133.570 124.822 1.00 40.56 ? 386 VAL   A CB  1 
ATOM   2088 C  CG1 . VAL   A 1 386 ? 131.595 134.137 123.878 1.00 40.56 ? 386 VAL   A CG1 1 
ATOM   2089 C  CG2 . VAL   A 1 386 ? 133.377 132.396 124.164 1.00 40.56 ? 386 VAL   A CG2 1 
ATOM   2090 N  N   . ARG   A 1 387 ? 132.478 135.840 127.123 1.00 40.65 ? 387 ARG   A N   1 
ATOM   2091 C  CA  . ARG   A 1 387 ? 131.814 136.966 127.765 1.00 40.69 ? 387 ARG   A CA  1 
ATOM   2092 C  C   . ARG   A 1 387 ? 132.759 138.166 127.827 1.00 40.73 ? 387 ARG   A C   1 
ATOM   2093 O  O   . ARG   A 1 387 ? 132.324 139.300 127.629 1.00 40.76 ? 387 ARG   A O   1 
ATOM   2094 C  CB  . ARG   A 1 387 ? 131.327 136.591 129.171 1.00 40.68 ? 387 ARG   A CB  1 
ATOM   2095 N  N   . ARG   A 1 388 ? 134.044 137.905 128.106 1.00 40.73 ? 388 ARG   A N   1 
ATOM   2096 C  CA  . ARG   A 1 388 ? 135.062 138.946 128.149 1.00 40.75 ? 388 ARG   A CA  1 
ATOM   2097 C  C   . ARG   A 1 388 ? 135.292 139.519 126.750 1.00 40.75 ? 388 ARG   A C   1 
ATOM   2098 O  O   . ARG   A 1 388 ? 135.428 140.732 126.597 1.00 40.79 ? 388 ARG   A O   1 
ATOM   2099 C  CB  . ARG   A 1 388 ? 136.374 138.404 128.730 1.00 40.74 ? 388 ARG   A CB  1 
ATOM   2100 N  N   . ALA   A 1 389 ? 135.334 138.638 125.739 1.00 40.72 ? 389 ALA   A N   1 
ATOM   2101 C  CA  . ALA   A 1 389 ? 135.583 139.039 124.362 1.00 40.73 ? 389 ALA   A CA  1 
ATOM   2102 C  C   . ALA   A 1 389 ? 134.418 139.874 123.830 1.00 40.73 ? 389 ALA   A C   1 
ATOM   2103 O  O   . ALA   A 1 389 ? 134.641 140.914 123.211 1.00 40.78 ? 389 ALA   A O   1 
ATOM   2104 C  CB  . ALA   A 1 389 ? 135.829 137.819 123.499 1.00 40.73 ? 389 ALA   A CB  1 
ATOM   2105 N  N   . PHE   A 1 390 ? 133.182 139.411 124.074 1.00 40.72 ? 390 PHE   A N   1 
ATOM   2106 C  CA  . PHE   A 1 390 ? 131.989 140.162 123.708 1.00 40.75 ? 390 PHE   A CA  1 
ATOM   2107 C  C   . PHE   A 1 390 ? 131.929 141.451 124.527 1.00 40.80 ? 390 PHE   A C   1 
ATOM   2108 O  O   . PHE   A 1 390 ? 131.419 142.458 124.042 1.00 40.84 ? 390 PHE   A O   1 
ATOM   2109 C  CB  . PHE   A 1 390 ? 130.689 139.370 123.905 1.00 40.74 ? 390 PHE   A CB  1 
ATOM   2110 C  CG  . PHE   A 1 390 ? 130.419 138.193 122.970 1.00 40.72 ? 390 PHE   A CG  1 
ATOM   2111 C  CD1 . PHE   A 1 390 ? 131.138 138.000 121.789 1.00 40.71 ? 390 PHE   A CD1 1 
ATOM   2112 C  CD2 . PHE   A 1 390 ? 129.398 137.291 123.265 1.00 40.71 ? 390 PHE   A CD2 1 
ATOM   2113 C  CE1 . PHE   A 1 390 ? 130.859 136.927 120.953 1.00 40.70 ? 390 PHE   A CE1 1 
ATOM   2114 C  CE2 . PHE   A 1 390 ? 129.122 136.223 122.423 1.00 40.70 ? 390 PHE   A CE2 1 
ATOM   2115 C  CZ  . PHE   A 1 390 ? 129.853 136.043 121.270 1.00 40.70 ? 390 PHE   A CZ  1 
ATOM   2116 N  N   . GLY   A 1 391 ? 132.432 141.402 125.769 1.00 40.82 ? 391 GLY   A N   1 
ATOM   2117 C  CA  . GLY   A 1 391 ? 132.578 142.588 126.599 1.00 40.86 ? 391 GLY   A CA  1 
ATOM   2118 C  C   . GLY   A 1 391 ? 133.460 143.640 125.928 1.00 40.88 ? 391 GLY   A C   1 
ATOM   2119 O  O   . GLY   A 1 391 ? 133.109 144.819 125.909 1.00 40.93 ? 391 GLY   A O   1 
ATOM   2120 N  N   . ARG   A 1 392 ? 134.602 143.197 125.382 1.00 40.88 ? 392 ARG   A N   1 
ATOM   2121 C  CA  . ARG   A 1 392 ? 135.515 144.068 124.656 1.00 40.89 ? 392 ARG   A CA  1 
ATOM   2122 C  C   . ARG   A 1 392 ? 134.840 144.586 123.386 1.00 40.90 ? 392 ARG   A C   1 
ATOM   2123 O  O   . ARG   A 1 392 ? 134.953 145.769 123.067 1.00 40.94 ? 392 ARG   A O   1 
ATOM   2124 C  CB  . ARG   A 1 392 ? 136.821 143.338 124.319 1.00 40.89 ? 392 ARG   A CB  1 
ATOM   2125 N  N   . GLY   A 1 393 ? 134.144 143.691 122.669 1.00 40.88 ? 393 GLY   A N   1 
ATOM   2126 C  CA  . GLY   A 1 393 ? 133.407 144.055 121.468 1.00 40.91 ? 393 GLY   A CA  1 
ATOM   2127 C  C   . GLY   A 1 393 ? 132.340 145.112 121.750 1.00 40.93 ? 393 GLY   A C   1 
ATOM   2128 O  O   . GLY   A 1 393 ? 132.187 146.057 120.978 1.00 40.97 ? 393 GLY   A O   1 
ATOM   2129 N  N   . LEU   A 1 394 ? 131.610 144.937 122.862 1.00 40.93 ? 394 LEU   A N   1 
ATOM   2130 C  CA  . LEU   A 1 394 ? 130.575 145.870 123.282 1.00 40.97 ? 394 LEU   A CA  1 
ATOM   2131 C  C   . LEU   A 1 394 ? 131.213 147.182 123.737 1.00 40.99 ? 394 LEU   A C   1 
ATOM   2132 O  O   . LEU   A 1 394 ? 130.629 148.247 123.545 1.00 40.99 ? 394 LEU   A O   1 
ATOM   2133 C  CB  . LEU   A 1 394 ? 129.731 145.237 124.392 1.00 40.98 ? 394 LEU   A CB  1 
ATOM   2134 C  CG  . LEU   A 1 394 ? 128.446 145.972 124.804 1.00 40.99 ? 394 LEU   A CG  1 
ATOM   2135 C  CD1 . LEU   A 1 394 ? 127.342 145.873 123.749 1.00 41.00 ? 394 LEU   A CD1 1 
ATOM   2136 C  CD2 . LEU   A 1 394 ? 127.945 145.460 126.153 1.00 41.00 ? 394 LEU   A CD2 1 
ATOM   2137 N  N   . GLN   A 1 395 ? 132.405 147.094 124.346 1.00 41.01 ? 395 GLN   A N   1 
ATOM   2138 C  CA  . GLN   A 1 395 ? 133.153 148.268 124.772 1.00 41.04 ? 395 GLN   A CA  1 
ATOM   2139 C  C   . GLN   A 1 395 ? 133.522 149.123 123.559 1.00 41.05 ? 395 GLN   A C   1 
ATOM   2140 O  O   . GLN   A 1 395 ? 133.456 150.349 123.632 1.00 41.06 ? 395 GLN   A O   1 
ATOM   2141 C  CB  . GLN   A 1 395 ? 134.410 147.877 125.552 1.00 41.04 ? 395 GLN   A CB  1 
ATOM   2142 N  N   . VAL   A 1 396 ? 133.914 148.469 122.455 1.00 41.04 ? 396 VAL   A N   1 
ATOM   2143 C  CA  . VAL   A 1 396 ? 134.223 149.162 121.211 1.00 41.06 ? 396 VAL   A CA  1 
ATOM   2144 C  C   . VAL   A 1 396 ? 132.919 149.698 120.619 1.00 41.07 ? 396 VAL   A C   1 
ATOM   2145 O  O   . VAL   A 1 396 ? 132.815 150.893 120.343 1.00 41.07 ? 396 VAL   A O   1 
ATOM   2146 C  CB  . VAL   A 1 396 ? 134.986 148.274 120.201 1.00 41.07 ? 396 VAL   A CB  1 
ATOM   2147 C  CG1 . VAL   A 1 396 ? 135.099 148.921 118.820 1.00 41.07 ? 396 VAL   A CG1 1 
ATOM   2148 C  CG2 . VAL   A 1 396 ? 136.368 147.874 120.715 1.00 41.07 ? 396 VAL   A CG2 1 
ATOM   2149 N  N   . LEU   A 1 397 ? 131.930 148.810 120.436 1.00 41.06 ? 397 LEU   A N   1 
ATOM   2150 C  CA  . LEU   A 1 397 ? 130.646 149.182 119.861 1.00 41.08 ? 397 LEU   A CA  1 
ATOM   2151 C  C   . LEU   A 1 397 ? 129.808 149.912 120.924 1.00 41.09 ? 397 LEU   A C   1 
ATOM   2152 O  O   . LEU   A 1 397 ? 129.843 151.162 120.921 1.00 41.08 ? 397 LEU   A O   1 
ATOM   2153 C  CB  . LEU   A 1 397 ? 129.921 147.945 119.331 1.00 41.09 ? 397 LEU   A CB  1 
HETATM 2154 C  C1  . A1LYD B 2 .   ? 116.051 124.037 100.862 1.00 40.34 ? 501 A1LYD A C1  1 
HETATM 2155 C  C2  . A1LYD B 2 .   ? 115.130 123.000 101.574 1.00 40.32 ? 501 A1LYD A C2  1 
HETATM 2156 C  C3  . A1LYD B 2 .   ? 116.141 122.963 102.732 1.00 40.31 ? 501 A1LYD A C3  1 
HETATM 2157 C  C4  . A1LYD B 2 .   ? 116.481 123.761 99.417  1.00 40.39 ? 501 A1LYD A C4  1 
HETATM 2158 C  C5  . A1LYD B 2 .   ? 115.718 125.511 101.072 1.00 40.34 ? 501 A1LYD A C5  1 
HETATM 2159 C  C6  . A1LYD B 2 .   ? 118.445 123.656 101.785 1.00 40.30 ? 501 A1LYD A C6  1 
HETATM 2160 O  O1  . A1LYD B 2 .   ? 117.644 123.419 99.206  1.00 40.38 ? 501 A1LYD A O1  1 
HETATM 2161 N  N2  . A1LYD B 2 .   ? 115.617 123.981 98.375  1.00 40.49 ? 501 A1LYD A N2  1 
HETATM 2162 O  O3  . A1LYD B 2 .   ? 111.071 125.852 98.365  1.00 40.64 ? 501 A1LYD A O3  1 
HETATM 2163 O  O4  . A1LYD B 2 .   ? 110.223 123.900 97.805  1.00 40.63 ? 501 A1LYD A O4  1 
HETATM 2164 CL CL1 . A1LYD B 2 .   ? 120.647 126.396 95.224  1.00 40.66 ? 501 A1LYD A CL1 1 
HETATM 2165 S  S1  . A1LYD B 2 .   ? 120.732 126.600 100.356 1.00 40.30 ? 501 A1LYD A S1  1 
HETATM 2166 O  O2  . A1LYD B 2 .   ? 119.070 122.612 101.958 1.00 40.31 ? 501 A1LYD A O2  1 
HETATM 2167 N  N1  . A1LYD B 2 .   ? 117.097 123.591 101.804 1.00 40.31 ? 501 A1LYD A N1  1 
HETATM 2168 C  C7  . A1LYD B 2 .   ? 114.143 124.097 98.450  1.00 40.54 ? 501 A1LYD A C7  1 
HETATM 2169 C  C8  . A1LYD B 2 .   ? 116.278 124.202 97.075  1.00 40.54 ? 501 A1LYD A C8  1 
HETATM 2170 C  C9  . A1LYD B 2 .   ? 119.184 124.879 101.523 1.00 40.29 ? 501 A1LYD A C9  1 
HETATM 2171 C  C10 . A1LYD B 2 .   ? 113.301 123.550 97.291  1.00 40.58 ? 501 A1LYD A C10 1 
HETATM 2172 C  C11 . A1LYD B 2 .   ? 119.227 126.022 102.407 1.00 40.25 ? 501 A1LYD A C11 1 
HETATM 2173 C  C12 . A1LYD B 2 .   ? 117.263 125.354 97.082  1.00 40.57 ? 501 A1LYD A C12 1 
HETATM 2174 C  C13 . A1LYD B 2 .   ? 119.956 125.071 100.408 1.00 40.29 ? 501 A1LYD A C13 1 
HETATM 2175 C  C14 . A1LYD B 2 .   ? 112.276 124.540 96.786  1.00 40.62 ? 501 A1LYD A C14 1 
HETATM 2176 C  C15 . A1LYD B 2 .   ? 120.046 127.042 101.885 1.00 40.24 ? 501 A1LYD A C15 1 
HETATM 2177 C  C16 . A1LYD B 2 .   ? 118.601 126.239 103.643 1.00 40.22 ? 501 A1LYD A C16 1 
HETATM 2178 C  C17 . A1LYD B 2 .   ? 118.375 125.346 96.250  1.00 40.59 ? 501 A1LYD A C17 1 
HETATM 2179 C  C18 . A1LYD B 2 .   ? 117.068 126.444 97.923  1.00 40.57 ? 501 A1LYD A C18 1 
HETATM 2180 C  C19 . A1LYD B 2 .   ? 120.246 128.248 102.560 1.00 40.21 ? 501 A1LYD A C19 1 
HETATM 2181 C  C20 . A1LYD B 2 .   ? 111.104 124.783 97.720  1.00 40.63 ? 501 A1LYD A C20 1 
HETATM 2182 C  C21 . A1LYD B 2 .   ? 118.803 127.432 104.309 1.00 40.19 ? 501 A1LYD A C21 1 
HETATM 2183 C  C22 . A1LYD B 2 .   ? 119.619 128.426 103.771 1.00 40.19 ? 501 A1LYD A C22 1 
HETATM 2184 C  C23 . A1LYD B 2 .   ? 119.260 126.408 96.275  1.00 40.61 ? 501 A1LYD A C23 1 
HETATM 2185 C  C24 . A1LYD B 2 .   ? 117.973 127.489 97.940  1.00 40.58 ? 501 A1LYD A C24 1 
HETATM 2186 C  C25 . A1LYD B 2 .   ? 119.071 127.483 97.110  1.00 40.60 ? 501 A1LYD A C25 1 
# 
