data_8SC1
# 
_entry.id   8SC1 
# 
_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   8SC1         pdb_00008sc1 10.2210/pdb8sc1/pdb 
WWPDB D_1000273406 ?            ?                   
EMDB  EMD-40334    ?            ?                   
# 
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 2023-10-18 ? 
2  'EM metadata'     1 0 2023-10-18 ? 
3  FSC               1 0 2023-10-18 ? 
4  'Half map'        1 0 2023-10-18 1 
5  'Half map'        1 0 2023-10-18 2 
6  Image             1 0 2023-10-18 ? 
7  'Primary map'     1 0 2023-10-18 ? 
8  'Structure model' 1 1 2023-10-25 ? 
9  FSC               1 0 2023-10-18 ? 
10 'Half map'        1 0 2023-10-18 1 
11 'Half map'        1 0 2023-10-18 2 
12 Image             1 0 2023-10-18 ? 
13 'Primary map'     1 0 2023-10-18 ? 
14 'Structure model' 1 2 2024-11-06 ? 
15 FSC               1 0 2023-10-18 ? 
16 'Half map'        1 0 2023-10-18 1 
17 'Half map'        1 0 2023-10-18 2 
18 Image             1 0 2023-10-18 ? 
19 'Primary map'     1 0 2023-10-18 ? 
20 'Structure model' 1 3 2025-06-04 ? 
21 'EM metadata'     1 1 2025-06-04 ? 
# 
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' ? ? 
8  9  FSC               repository 'Initial release' ? ? 
9  10 'Half map'        repository 'Initial release' ? ? 
10 11 'Half map'        repository 'Initial release' ? ? 
11 12 Image             repository 'Initial release' ? ? 
12 13 'Primary map'     repository 'Initial release' ? ? 
13 15 FSC               repository 'Initial release' ? ? 
14 16 'Half map'        repository 'Initial release' ? ? 
15 17 'Half map'        repository 'Initial release' ? ? 
16 18 Image             repository 'Initial release' ? ? 
17 19 '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' 'Database references'  
2 14 'Structure model' 'Data collection'      
3 14 'Structure model' 'Structure summary'    
4 20 'Structure model' 'Data collection'      
5 21 'EM metadata'     'Data processing'      
6 21 'EM metadata'     'Experimental summary' 
# 
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 14 'Structure model' em_admin                  
4 14 'Structure model' pdbx_entry_details        
5 14 'Structure model' pdbx_modification_feature 
6 20 'Structure model' em_admin                  
7 20 'Structure model' em_software               
8 21 'EM metadata'     em_admin                  
9 21 'EM metadata'     em_software               
# 
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' '_citation_author.identifier_ORCID' 
13 8  'Structure model' '_citation_author.name'             
14 14 'Structure model' '_em_admin.last_update'             
15 20 'Structure model' '_em_admin.last_update'             
16 20 'Structure model' '_em_software.name'                 
17 21 'EM metadata'     '_em_admin.last_update'             
18 21 'EM metadata'     '_em_software.name'                 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  ? 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8SC1 
_pdbx_database_status.recvd_initial_deposition_date   2023-04-04 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_database_related.db_name        EMDB 
_pdbx_database_related.details        'Human OCT1 (Apo) in inward-open conformation' 
_pdbx_database_related.db_id          EMD-40334 
_pdbx_database_related.content_type   'associated EM volume' 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              a.stewart@victorchang.edu.au 
_pdbx_contact_author.name_first         Alastair 
_pdbx_contact_author.name_last          Stewart 
_pdbx_contact_author.name_mi            G 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-2070-6030 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Zeng, Y.C.'    1 0000-0001-9964-0929 
'Sobti, M.'     2 0000-0001-7086-3467 
'Stewart, A.G.' 3 0000-0002-2070-6030 
# 
_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            14 
_citation.language                  ? 
_citation.page_first                6374 
_citation.page_last                 6374 
_citation.title                     'Structural basis of promiscuous substrate transport by Organic Cation Transporter 1.' 
_citation.year                      2023 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1038/s41467-023-42086-9 
_citation.pdbx_database_id_PubMed   37821493 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Zeng, Y.C.'       1 0000-0001-9964-0929 
primary 'Sobti, M.'        2 ?                   
primary 'Quinn, A.'        3 0009-0003-1862-0750 
primary 'Smith, N.J.'      4 0000-0002-7247-9562 
primary 'Brown, S.H.J.'    5 0000-0003-3997-4614 
primary 'Vandenberg, J.I.' 6 0000-0002-3859-3716 
primary 'Ryan, R.M.'       7 0000-0002-8680-4610 
primary 
;O'Mara, M.L.
;
8 0000-0002-8764-1585 
primary 'Stewart, A.G.'    9 0000-0002-2070-6030 
# 
_entity.id                         1 
_entity.type                       polymer 
_entity.src_method                 man 
_entity.pdbx_description           'Solute carrier family 22 member 1' 
_entity.formula_weight             61200.664 
_entity.pdbx_number_of_molecules   1 
_entity.pdbx_ec                    ? 
_entity.pdbx_mutation              ? 
_entity.pdbx_fragment              ? 
_entity.details                    ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Organic cation transporter 1,hOCT1' 
# 
_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       
;MPTVDDILEQVGESGWFQKQAFLILCLLSAAFAPICVGIVFLGFTPDHHCQSPGVAELSQRCGWSPAEELNYTVPGLGPA
GEAFLGQCRRYEVDWNQSALSCVDPLASLATNRSHLPLGPCQDGWVYDTPGSSIVTEFNLVCADSWKLDLFQSCLNAGFL
FGSLGVGYFADRFGRKLCLLGTVLVNAVSGVLMAFSPNYMSMLLFRLLQGLVSKGNWMAGYTLITEFVGSGSRRTVAIMY
QMAFTVGLVALTGLAYALPHWRWLQLAVSLPTFLFLLYYWCVPESPRWLLSQKRNTEAIKIMDHIAQKNGKLPPADLKML
SLEEDVTEKLSPSFADLFRTPRLRKRTFILMYLWFTDSVLYQGLILHMGATSGNLYLDFLYSALVEIPGAFIALITIDRV
GRIYPMAMSNLLAGAACLVMIFISPDLHWLNIIIMCVGRMGITIAIQMICLVNAELYPTFVRNLGVMVCSSLCDIGGIIT
PFIVFRLREVWQALPLILFAVLGLLAAGVTLLLPETKGVALPETMKDAENLGRKAKPKENTIYLKVQTSEPSGT
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MPTVDDILEQVGESGWFQKQAFLILCLLSAAFAPICVGIVFLGFTPDHHCQSPGVAELSQRCGWSPAEELNYTVPGLGPA
GEAFLGQCRRYEVDWNQSALSCVDPLASLATNRSHLPLGPCQDGWVYDTPGSSIVTEFNLVCADSWKLDLFQSCLNAGFL
FGSLGVGYFADRFGRKLCLLGTVLVNAVSGVLMAFSPNYMSMLLFRLLQGLVSKGNWMAGYTLITEFVGSGSRRTVAIMY
QMAFTVGLVALTGLAYALPHWRWLQLAVSLPTFLFLLYYWCVPESPRWLLSQKRNTEAIKIMDHIAQKNGKLPPADLKML
SLEEDVTEKLSPSFADLFRTPRLRKRTFILMYLWFTDSVLYQGLILHMGATSGNLYLDFLYSALVEIPGAFIALITIDRV
GRIYPMAMSNLLAGAACLVMIFISPDLHWLNIIIMCVGRMGITIAIQMICLVNAELYPTFVRNLGVMVCSSLCDIGGIIT
PFIVFRLREVWQALPLILFAVLGLLAAGVTLLLPETKGVALPETMKDAENLGRKAKPKENTIYLKVQTSEPSGT
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
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   PRO n 
1 3   THR n 
1 4   VAL n 
1 5   ASP n 
1 6   ASP n 
1 7   ILE n 
1 8   LEU n 
1 9   GLU n 
1 10  GLN n 
1 11  VAL n 
1 12  GLY n 
1 13  GLU n 
1 14  SER n 
1 15  GLY n 
1 16  TRP n 
1 17  PHE n 
1 18  GLN n 
1 19  LYS n 
1 20  GLN n 
1 21  ALA n 
1 22  PHE n 
1 23  LEU n 
1 24  ILE n 
1 25  LEU n 
1 26  CYS n 
1 27  LEU n 
1 28  LEU n 
1 29  SER n 
1 30  ALA n 
1 31  ALA n 
1 32  PHE n 
1 33  ALA n 
1 34  PRO n 
1 35  ILE n 
1 36  CYS n 
1 37  VAL n 
1 38  GLY n 
1 39  ILE n 
1 40  VAL n 
1 41  PHE n 
1 42  LEU n 
1 43  GLY n 
1 44  PHE n 
1 45  THR n 
1 46  PRO n 
1 47  ASP n 
1 48  HIS n 
1 49  HIS n 
1 50  CYS n 
1 51  GLN n 
1 52  SER n 
1 53  PRO n 
1 54  GLY n 
1 55  VAL n 
1 56  ALA n 
1 57  GLU n 
1 58  LEU n 
1 59  SER n 
1 60  GLN n 
1 61  ARG n 
1 62  CYS n 
1 63  GLY n 
1 64  TRP n 
1 65  SER n 
1 66  PRO n 
1 67  ALA n 
1 68  GLU n 
1 69  GLU n 
1 70  LEU n 
1 71  ASN n 
1 72  TYR n 
1 73  THR n 
1 74  VAL n 
1 75  PRO n 
1 76  GLY n 
1 77  LEU n 
1 78  GLY n 
1 79  PRO n 
1 80  ALA n 
1 81  GLY n 
1 82  GLU n 
1 83  ALA n 
1 84  PHE n 
1 85  LEU n 
1 86  GLY n 
1 87  GLN n 
1 88  CYS n 
1 89  ARG n 
1 90  ARG n 
1 91  TYR n 
1 92  GLU n 
1 93  VAL n 
1 94  ASP n 
1 95  TRP n 
1 96  ASN n 
1 97  GLN n 
1 98  SER n 
1 99  ALA n 
1 100 LEU n 
1 101 SER n 
1 102 CYS n 
1 103 VAL n 
1 104 ASP n 
1 105 PRO n 
1 106 LEU n 
1 107 ALA n 
1 108 SER n 
1 109 LEU n 
1 110 ALA n 
1 111 THR n 
1 112 ASN n 
1 113 ARG n 
1 114 SER n 
1 115 HIS n 
1 116 LEU n 
1 117 PRO n 
1 118 LEU n 
1 119 GLY n 
1 120 PRO n 
1 121 CYS n 
1 122 GLN n 
1 123 ASP n 
1 124 GLY n 
1 125 TRP n 
1 126 VAL n 
1 127 TYR n 
1 128 ASP n 
1 129 THR n 
1 130 PRO n 
1 131 GLY n 
1 132 SER n 
1 133 SER n 
1 134 ILE n 
1 135 VAL n 
1 136 THR n 
1 137 GLU n 
1 138 PHE n 
1 139 ASN n 
1 140 LEU n 
1 141 VAL n 
1 142 CYS n 
1 143 ALA n 
1 144 ASP n 
1 145 SER n 
1 146 TRP n 
1 147 LYS n 
1 148 LEU n 
1 149 ASP n 
1 150 LEU n 
1 151 PHE n 
1 152 GLN n 
1 153 SER n 
1 154 CYS n 
1 155 LEU n 
1 156 ASN n 
1 157 ALA n 
1 158 GLY n 
1 159 PHE n 
1 160 LEU n 
1 161 PHE n 
1 162 GLY n 
1 163 SER n 
1 164 LEU n 
1 165 GLY n 
1 166 VAL n 
1 167 GLY n 
1 168 TYR n 
1 169 PHE n 
1 170 ALA n 
1 171 ASP n 
1 172 ARG n 
1 173 PHE n 
1 174 GLY n 
1 175 ARG n 
1 176 LYS n 
1 177 LEU n 
1 178 CYS n 
1 179 LEU n 
1 180 LEU n 
1 181 GLY n 
1 182 THR n 
1 183 VAL n 
1 184 LEU n 
1 185 VAL n 
1 186 ASN n 
1 187 ALA n 
1 188 VAL n 
1 189 SER n 
1 190 GLY n 
1 191 VAL n 
1 192 LEU n 
1 193 MET n 
1 194 ALA n 
1 195 PHE n 
1 196 SER n 
1 197 PRO n 
1 198 ASN n 
1 199 TYR n 
1 200 MET n 
1 201 SER n 
1 202 MET n 
1 203 LEU n 
1 204 LEU n 
1 205 PHE n 
1 206 ARG n 
1 207 LEU n 
1 208 LEU n 
1 209 GLN n 
1 210 GLY n 
1 211 LEU n 
1 212 VAL n 
1 213 SER n 
1 214 LYS n 
1 215 GLY n 
1 216 ASN n 
1 217 TRP n 
1 218 MET n 
1 219 ALA n 
1 220 GLY n 
1 221 TYR n 
1 222 THR n 
1 223 LEU n 
1 224 ILE n 
1 225 THR n 
1 226 GLU n 
1 227 PHE n 
1 228 VAL n 
1 229 GLY n 
1 230 SER n 
1 231 GLY n 
1 232 SER n 
1 233 ARG n 
1 234 ARG n 
1 235 THR n 
1 236 VAL n 
1 237 ALA n 
1 238 ILE n 
1 239 MET n 
1 240 TYR n 
1 241 GLN n 
1 242 MET n 
1 243 ALA n 
1 244 PHE n 
1 245 THR n 
1 246 VAL n 
1 247 GLY n 
1 248 LEU n 
1 249 VAL n 
1 250 ALA n 
1 251 LEU n 
1 252 THR n 
1 253 GLY n 
1 254 LEU n 
1 255 ALA n 
1 256 TYR n 
1 257 ALA n 
1 258 LEU n 
1 259 PRO n 
1 260 HIS n 
1 261 TRP n 
1 262 ARG n 
1 263 TRP n 
1 264 LEU n 
1 265 GLN n 
1 266 LEU n 
1 267 ALA n 
1 268 VAL n 
1 269 SER n 
1 270 LEU n 
1 271 PRO n 
1 272 THR n 
1 273 PHE n 
1 274 LEU n 
1 275 PHE n 
1 276 LEU n 
1 277 LEU n 
1 278 TYR n 
1 279 TYR n 
1 280 TRP n 
1 281 CYS n 
1 282 VAL n 
1 283 PRO n 
1 284 GLU n 
1 285 SER n 
1 286 PRO n 
1 287 ARG n 
1 288 TRP n 
1 289 LEU n 
1 290 LEU n 
1 291 SER n 
1 292 GLN n 
1 293 LYS n 
1 294 ARG n 
1 295 ASN n 
1 296 THR n 
1 297 GLU n 
1 298 ALA n 
1 299 ILE n 
1 300 LYS n 
1 301 ILE n 
1 302 MET n 
1 303 ASP n 
1 304 HIS n 
1 305 ILE n 
1 306 ALA n 
1 307 GLN n 
1 308 LYS n 
1 309 ASN n 
1 310 GLY n 
1 311 LYS n 
1 312 LEU n 
1 313 PRO n 
1 314 PRO n 
1 315 ALA n 
1 316 ASP n 
1 317 LEU n 
1 318 LYS n 
1 319 MET n 
1 320 LEU n 
1 321 SER n 
1 322 LEU n 
1 323 GLU n 
1 324 GLU n 
1 325 ASP n 
1 326 VAL n 
1 327 THR n 
1 328 GLU n 
1 329 LYS n 
1 330 LEU n 
1 331 SER n 
1 332 PRO n 
1 333 SER n 
1 334 PHE n 
1 335 ALA n 
1 336 ASP n 
1 337 LEU n 
1 338 PHE n 
1 339 ARG n 
1 340 THR n 
1 341 PRO n 
1 342 ARG n 
1 343 LEU n 
1 344 ARG n 
1 345 LYS n 
1 346 ARG n 
1 347 THR n 
1 348 PHE n 
1 349 ILE n 
1 350 LEU n 
1 351 MET n 
1 352 TYR n 
1 353 LEU n 
1 354 TRP n 
1 355 PHE n 
1 356 THR n 
1 357 ASP n 
1 358 SER n 
1 359 VAL n 
1 360 LEU n 
1 361 TYR n 
1 362 GLN n 
1 363 GLY n 
1 364 LEU n 
1 365 ILE n 
1 366 LEU n 
1 367 HIS n 
1 368 MET n 
1 369 GLY n 
1 370 ALA n 
1 371 THR n 
1 372 SER n 
1 373 GLY n 
1 374 ASN n 
1 375 LEU n 
1 376 TYR n 
1 377 LEU n 
1 378 ASP n 
1 379 PHE n 
1 380 LEU n 
1 381 TYR n 
1 382 SER n 
1 383 ALA n 
1 384 LEU n 
1 385 VAL n 
1 386 GLU n 
1 387 ILE n 
1 388 PRO n 
1 389 GLY n 
1 390 ALA n 
1 391 PHE n 
1 392 ILE n 
1 393 ALA n 
1 394 LEU n 
1 395 ILE n 
1 396 THR n 
1 397 ILE n 
1 398 ASP n 
1 399 ARG n 
1 400 VAL n 
1 401 GLY n 
1 402 ARG n 
1 403 ILE n 
1 404 TYR n 
1 405 PRO n 
1 406 MET n 
1 407 ALA n 
1 408 MET n 
1 409 SER n 
1 410 ASN n 
1 411 LEU n 
1 412 LEU n 
1 413 ALA n 
1 414 GLY n 
1 415 ALA n 
1 416 ALA n 
1 417 CYS n 
1 418 LEU n 
1 419 VAL n 
1 420 MET n 
1 421 ILE n 
1 422 PHE n 
1 423 ILE n 
1 424 SER n 
1 425 PRO n 
1 426 ASP n 
1 427 LEU n 
1 428 HIS n 
1 429 TRP n 
1 430 LEU n 
1 431 ASN n 
1 432 ILE n 
1 433 ILE n 
1 434 ILE n 
1 435 MET n 
1 436 CYS n 
1 437 VAL n 
1 438 GLY n 
1 439 ARG n 
1 440 MET n 
1 441 GLY n 
1 442 ILE n 
1 443 THR n 
1 444 ILE n 
1 445 ALA n 
1 446 ILE n 
1 447 GLN n 
1 448 MET n 
1 449 ILE n 
1 450 CYS n 
1 451 LEU n 
1 452 VAL n 
1 453 ASN n 
1 454 ALA n 
1 455 GLU n 
1 456 LEU n 
1 457 TYR n 
1 458 PRO n 
1 459 THR n 
1 460 PHE n 
1 461 VAL n 
1 462 ARG n 
1 463 ASN n 
1 464 LEU n 
1 465 GLY n 
1 466 VAL n 
1 467 MET n 
1 468 VAL n 
1 469 CYS n 
1 470 SER n 
1 471 SER n 
1 472 LEU n 
1 473 CYS n 
1 474 ASP n 
1 475 ILE n 
1 476 GLY n 
1 477 GLY n 
1 478 ILE n 
1 479 ILE n 
1 480 THR n 
1 481 PRO n 
1 482 PHE n 
1 483 ILE n 
1 484 VAL n 
1 485 PHE n 
1 486 ARG n 
1 487 LEU n 
1 488 ARG n 
1 489 GLU n 
1 490 VAL n 
1 491 TRP n 
1 492 GLN n 
1 493 ALA n 
1 494 LEU n 
1 495 PRO n 
1 496 LEU n 
1 497 ILE n 
1 498 LEU n 
1 499 PHE n 
1 500 ALA n 
1 501 VAL n 
1 502 LEU n 
1 503 GLY n 
1 504 LEU n 
1 505 LEU n 
1 506 ALA n 
1 507 ALA n 
1 508 GLY n 
1 509 VAL n 
1 510 THR n 
1 511 LEU n 
1 512 LEU n 
1 513 LEU n 
1 514 PRO n 
1 515 GLU n 
1 516 THR n 
1 517 LYS n 
1 518 GLY n 
1 519 VAL n 
1 520 ALA n 
1 521 LEU n 
1 522 PRO n 
1 523 GLU n 
1 524 THR n 
1 525 MET n 
1 526 LYS n 
1 527 ASP n 
1 528 ALA n 
1 529 GLU n 
1 530 ASN n 
1 531 LEU n 
1 532 GLY n 
1 533 ARG n 
1 534 LYS n 
1 535 ALA n 
1 536 LYS n 
1 537 PRO n 
1 538 LYS n 
1 539 GLU n 
1 540 ASN n 
1 541 THR n 
1 542 ILE n 
1 543 TYR n 
1 544 LEU n 
1 545 LYS n 
1 546 VAL n 
1 547 GLN n 
1 548 THR n 
1 549 SER n 
1 550 GLU n 
1 551 PRO n 
1 552 SER n 
1 553 GLY n 
1 554 THR n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   554 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'SLC22A1, OCT1' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     9606 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE         ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE        ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE      ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE        ? 'C3 H7 N O2 S'   121.158 
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   PRO 2   2   ?   ?   ?   A . n 
A 1 3   THR 3   3   ?   ?   ?   A . n 
A 1 4   VAL 4   4   ?   ?   ?   A . n 
A 1 5   ASP 5   5   ?   ?   ?   A . n 
A 1 6   ASP 6   6   ?   ?   ?   A . n 
A 1 7   ILE 7   7   ?   ?   ?   A . n 
A 1 8   LEU 8   8   ?   ?   ?   A . n 
A 1 9   GLU 9   9   ?   ?   ?   A . n 
A 1 10  GLN 10  10  ?   ?   ?   A . n 
A 1 11  VAL 11  11  ?   ?   ?   A . n 
A 1 12  GLY 12  12  ?   ?   ?   A . n 
A 1 13  GLU 13  13  ?   ?   ?   A . n 
A 1 14  SER 14  14  ?   ?   ?   A . n 
A 1 15  GLY 15  15  ?   ?   ?   A . n 
A 1 16  TRP 16  16  ?   ?   ?   A . n 
A 1 17  PHE 17  17  ?   ?   ?   A . n 
A 1 18  GLN 18  18  ?   ?   ?   A . n 
A 1 19  LYS 19  19  19  LYS LYS A . n 
A 1 20  GLN 20  20  20  GLN GLN A . n 
A 1 21  ALA 21  21  21  ALA ALA A . n 
A 1 22  PHE 22  22  22  PHE PHE A . n 
A 1 23  LEU 23  23  23  LEU LEU A . n 
A 1 24  ILE 24  24  24  ILE ILE A . n 
A 1 25  LEU 25  25  25  LEU LEU A . n 
A 1 26  CYS 26  26  26  CYS CYS A . n 
A 1 27  LEU 27  27  27  LEU LEU A . n 
A 1 28  LEU 28  28  28  LEU LEU A . n 
A 1 29  SER 29  29  29  SER SER A . n 
A 1 30  ALA 30  30  30  ALA ALA 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  ALA 33  33  33  ALA ALA A . n 
A 1 34  PRO 34  34  34  PRO PRO A . n 
A 1 35  ILE 35  35  35  ILE ILE A . n 
A 1 36  CYS 36  36  36  CYS CYS A . n 
A 1 37  VAL 37  37  37  VAL VAL A . n 
A 1 38  GLY 38  38  38  GLY GLY A . n 
A 1 39  ILE 39  39  39  ILE ILE A . n 
A 1 40  VAL 40  40  40  VAL VAL A . n 
A 1 41  PHE 41  41  41  PHE PHE A . n 
A 1 42  LEU 42  42  42  LEU LEU A . n 
A 1 43  GLY 43  43  43  GLY GLY A . n 
A 1 44  PHE 44  44  44  PHE PHE A . n 
A 1 45  THR 45  45  45  THR THR A . n 
A 1 46  PRO 46  46  46  PRO PRO A . n 
A 1 47  ASP 47  47  47  ASP ASP A . n 
A 1 48  HIS 48  48  48  HIS HIS A . n 
A 1 49  HIS 49  49  49  HIS HIS A . n 
A 1 50  CYS 50  50  50  CYS CYS A . n 
A 1 51  GLN 51  51  51  GLN GLN A . n 
A 1 52  SER 52  52  52  SER SER A . n 
A 1 53  PRO 53  53  53  PRO PRO A . n 
A 1 54  GLY 54  54  54  GLY GLY A . n 
A 1 55  VAL 55  55  55  VAL VAL A . n 
A 1 56  ALA 56  56  56  ALA ALA A . n 
A 1 57  GLU 57  57  57  GLU GLU A . n 
A 1 58  LEU 58  58  58  LEU LEU A . n 
A 1 59  SER 59  59  59  SER SER A . n 
A 1 60  GLN 60  60  60  GLN GLN A . n 
A 1 61  ARG 61  61  61  ARG ARG A . n 
A 1 62  CYS 62  62  62  CYS CYS A . n 
A 1 63  GLY 63  63  63  GLY GLY A . n 
A 1 64  TRP 64  64  64  TRP TRP A . n 
A 1 65  SER 65  65  65  SER SER A . n 
A 1 66  PRO 66  66  66  PRO PRO A . n 
A 1 67  ALA 67  67  67  ALA ALA A . n 
A 1 68  GLU 68  68  68  GLU GLU A . n 
A 1 69  GLU 69  69  69  GLU GLU A . n 
A 1 70  LEU 70  70  70  LEU LEU A . n 
A 1 71  ASN 71  71  71  ASN ASN A . n 
A 1 72  TYR 72  72  72  TYR TYR A . n 
A 1 73  THR 73  73  73  THR THR A . n 
A 1 74  VAL 74  74  74  VAL VAL A . n 
A 1 75  PRO 75  75  75  PRO PRO A . n 
A 1 76  GLY 76  76  76  GLY GLY A . n 
A 1 77  LEU 77  77  77  LEU LEU A . n 
A 1 78  GLY 78  78  78  GLY GLY A . n 
A 1 79  PRO 79  79  79  PRO PRO A . n 
A 1 80  ALA 80  80  80  ALA ALA A . n 
A 1 81  GLY 81  81  81  GLY GLY A . n 
A 1 82  GLU 82  82  82  GLU GLU A . n 
A 1 83  ALA 83  83  83  ALA ALA A . n 
A 1 84  PHE 84  84  84  PHE PHE A . n 
A 1 85  LEU 85  85  85  LEU LEU A . n 
A 1 86  GLY 86  86  86  GLY GLY A . n 
A 1 87  GLN 87  87  87  GLN GLN A . n 
A 1 88  CYS 88  88  88  CYS CYS A . n 
A 1 89  ARG 89  89  89  ARG ARG A . n 
A 1 90  ARG 90  90  90  ARG ARG A . n 
A 1 91  TYR 91  91  91  TYR TYR A . n 
A 1 92  GLU 92  92  92  GLU GLU A . n 
A 1 93  VAL 93  93  93  VAL VAL A . n 
A 1 94  ASP 94  94  94  ASP ASP A . n 
A 1 95  TRP 95  95  95  TRP TRP A . n 
A 1 96  ASN 96  96  96  ASN ASN A . n 
A 1 97  GLN 97  97  97  GLN GLN A . n 
A 1 98  SER 98  98  98  SER SER A . n 
A 1 99  ALA 99  99  99  ALA ALA A . n 
A 1 100 LEU 100 100 100 LEU LEU A . n 
A 1 101 SER 101 101 101 SER SER A . n 
A 1 102 CYS 102 102 102 CYS CYS A . n 
A 1 103 VAL 103 103 103 VAL VAL A . n 
A 1 104 ASP 104 104 104 ASP ASP A . n 
A 1 105 PRO 105 105 105 PRO PRO A . n 
A 1 106 LEU 106 106 106 LEU LEU A . n 
A 1 107 ALA 107 107 107 ALA ALA A . n 
A 1 108 SER 108 108 108 SER SER A . n 
A 1 109 LEU 109 109 109 LEU LEU A . n 
A 1 110 ALA 110 110 110 ALA ALA A . n 
A 1 111 THR 111 111 111 THR THR A . n 
A 1 112 ASN 112 112 112 ASN ASN A . n 
A 1 113 ARG 113 113 113 ARG ARG A . n 
A 1 114 SER 114 114 114 SER SER A . n 
A 1 115 HIS 115 115 115 HIS HIS A . n 
A 1 116 LEU 116 116 116 LEU LEU A . n 
A 1 117 PRO 117 117 117 PRO PRO A . n 
A 1 118 LEU 118 118 118 LEU LEU A . n 
A 1 119 GLY 119 119 119 GLY GLY A . n 
A 1 120 PRO 120 120 120 PRO PRO A . n 
A 1 121 CYS 121 121 121 CYS CYS A . n 
A 1 122 GLN 122 122 122 GLN GLN A . n 
A 1 123 ASP 123 123 123 ASP ASP A . n 
A 1 124 GLY 124 124 124 GLY GLY A . n 
A 1 125 TRP 125 125 125 TRP TRP A . n 
A 1 126 VAL 126 126 126 VAL VAL A . n 
A 1 127 TYR 127 127 127 TYR TYR A . n 
A 1 128 ASP 128 128 128 ASP ASP A . n 
A 1 129 THR 129 129 129 THR THR A . n 
A 1 130 PRO 130 130 130 PRO PRO A . n 
A 1 131 GLY 131 131 131 GLY GLY A . n 
A 1 132 SER 132 132 132 SER SER A . n 
A 1 133 SER 133 133 133 SER SER A . n 
A 1 134 ILE 134 134 134 ILE ILE A . n 
A 1 135 VAL 135 135 135 VAL VAL A . n 
A 1 136 THR 136 136 136 THR THR A . n 
A 1 137 GLU 137 137 137 GLU GLU A . n 
A 1 138 PHE 138 138 138 PHE PHE A . n 
A 1 139 ASN 139 139 139 ASN ASN A . n 
A 1 140 LEU 140 140 140 LEU LEU A . n 
A 1 141 VAL 141 141 141 VAL VAL A . n 
A 1 142 CYS 142 142 142 CYS CYS A . n 
A 1 143 ALA 143 143 143 ALA ALA A . n 
A 1 144 ASP 144 144 144 ASP ASP A . n 
A 1 145 SER 145 145 145 SER SER A . n 
A 1 146 TRP 146 146 146 TRP TRP A . n 
A 1 147 LYS 147 147 147 LYS LYS A . n 
A 1 148 LEU 148 148 148 LEU LEU A . n 
A 1 149 ASP 149 149 149 ASP ASP A . n 
A 1 150 LEU 150 150 150 LEU LEU A . n 
A 1 151 PHE 151 151 151 PHE PHE A . n 
A 1 152 GLN 152 152 152 GLN GLN A . n 
A 1 153 SER 153 153 153 SER SER A . n 
A 1 154 CYS 154 154 154 CYS CYS A . n 
A 1 155 LEU 155 155 155 LEU LEU A . n 
A 1 156 ASN 156 156 156 ASN ASN A . n 
A 1 157 ALA 157 157 157 ALA ALA A . n 
A 1 158 GLY 158 158 158 GLY GLY A . n 
A 1 159 PHE 159 159 159 PHE PHE A . n 
A 1 160 LEU 160 160 160 LEU LEU A . n 
A 1 161 PHE 161 161 161 PHE PHE A . n 
A 1 162 GLY 162 162 162 GLY GLY A . n 
A 1 163 SER 163 163 163 SER SER A . n 
A 1 164 LEU 164 164 164 LEU LEU A . n 
A 1 165 GLY 165 165 165 GLY GLY A . n 
A 1 166 VAL 166 166 166 VAL VAL A . n 
A 1 167 GLY 167 167 167 GLY GLY A . n 
A 1 168 TYR 168 168 168 TYR TYR A . n 
A 1 169 PHE 169 169 169 PHE PHE A . n 
A 1 170 ALA 170 170 170 ALA ALA A . n 
A 1 171 ASP 171 171 171 ASP ASP A . n 
A 1 172 ARG 172 172 172 ARG ARG A . n 
A 1 173 PHE 173 173 173 PHE PHE A . n 
A 1 174 GLY 174 174 174 GLY GLY A . n 
A 1 175 ARG 175 175 175 ARG ARG A . n 
A 1 176 LYS 176 176 176 LYS LYS A . n 
A 1 177 LEU 177 177 177 LEU LEU A . n 
A 1 178 CYS 178 178 178 CYS CYS A . n 
A 1 179 LEU 179 179 179 LEU LEU A . n 
A 1 180 LEU 180 180 180 LEU LEU A . n 
A 1 181 GLY 181 181 181 GLY GLY A . n 
A 1 182 THR 182 182 182 THR THR A . n 
A 1 183 VAL 183 183 183 VAL VAL A . n 
A 1 184 LEU 184 184 184 LEU LEU A . n 
A 1 185 VAL 185 185 185 VAL VAL A . n 
A 1 186 ASN 186 186 186 ASN ASN A . n 
A 1 187 ALA 187 187 187 ALA ALA A . n 
A 1 188 VAL 188 188 188 VAL VAL A . n 
A 1 189 SER 189 189 189 SER SER A . n 
A 1 190 GLY 190 190 190 GLY GLY A . n 
A 1 191 VAL 191 191 191 VAL VAL A . n 
A 1 192 LEU 192 192 192 LEU LEU A . n 
A 1 193 MET 193 193 193 MET MET A . n 
A 1 194 ALA 194 194 194 ALA ALA A . n 
A 1 195 PHE 195 195 195 PHE PHE A . n 
A 1 196 SER 196 196 196 SER SER A . n 
A 1 197 PRO 197 197 197 PRO PRO A . n 
A 1 198 ASN 198 198 198 ASN ASN A . n 
A 1 199 TYR 199 199 199 TYR TYR A . n 
A 1 200 MET 200 200 200 MET MET A . n 
A 1 201 SER 201 201 201 SER SER A . n 
A 1 202 MET 202 202 202 MET MET A . n 
A 1 203 LEU 203 203 203 LEU LEU A . n 
A 1 204 LEU 204 204 204 LEU LEU A . n 
A 1 205 PHE 205 205 205 PHE PHE A . n 
A 1 206 ARG 206 206 206 ARG ARG A . n 
A 1 207 LEU 207 207 207 LEU LEU A . n 
A 1 208 LEU 208 208 208 LEU LEU A . n 
A 1 209 GLN 209 209 209 GLN GLN A . n 
A 1 210 GLY 210 210 210 GLY GLY A . n 
A 1 211 LEU 211 211 211 LEU LEU A . n 
A 1 212 VAL 212 212 212 VAL VAL A . n 
A 1 213 SER 213 213 213 SER SER A . n 
A 1 214 LYS 214 214 214 LYS LYS A . n 
A 1 215 GLY 215 215 215 GLY GLY A . n 
A 1 216 ASN 216 216 216 ASN ASN A . n 
A 1 217 TRP 217 217 217 TRP TRP A . n 
A 1 218 MET 218 218 218 MET MET A . n 
A 1 219 ALA 219 219 219 ALA ALA A . n 
A 1 220 GLY 220 220 220 GLY GLY A . n 
A 1 221 TYR 221 221 221 TYR TYR A . n 
A 1 222 THR 222 222 222 THR THR A . n 
A 1 223 LEU 223 223 223 LEU LEU A . n 
A 1 224 ILE 224 224 224 ILE ILE A . n 
A 1 225 THR 225 225 225 THR THR A . n 
A 1 226 GLU 226 226 226 GLU GLU A . n 
A 1 227 PHE 227 227 227 PHE PHE A . n 
A 1 228 VAL 228 228 228 VAL VAL A . n 
A 1 229 GLY 229 229 229 GLY GLY A . n 
A 1 230 SER 230 230 230 SER SER A . n 
A 1 231 GLY 231 231 231 GLY GLY A . n 
A 1 232 SER 232 232 232 SER SER A . n 
A 1 233 ARG 233 233 233 ARG ARG A . n 
A 1 234 ARG 234 234 234 ARG ARG A . n 
A 1 235 THR 235 235 235 THR THR A . n 
A 1 236 VAL 236 236 236 VAL VAL A . n 
A 1 237 ALA 237 237 237 ALA ALA A . n 
A 1 238 ILE 238 238 238 ILE ILE A . n 
A 1 239 MET 239 239 239 MET MET A . n 
A 1 240 TYR 240 240 240 TYR TYR A . n 
A 1 241 GLN 241 241 241 GLN GLN A . n 
A 1 242 MET 242 242 242 MET MET A . n 
A 1 243 ALA 243 243 243 ALA ALA A . n 
A 1 244 PHE 244 244 244 PHE PHE A . n 
A 1 245 THR 245 245 245 THR THR A . n 
A 1 246 VAL 246 246 246 VAL VAL A . n 
A 1 247 GLY 247 247 247 GLY GLY A . n 
A 1 248 LEU 248 248 248 LEU LEU A . n 
A 1 249 VAL 249 249 249 VAL VAL A . n 
A 1 250 ALA 250 250 250 ALA ALA A . n 
A 1 251 LEU 251 251 251 LEU LEU A . n 
A 1 252 THR 252 252 252 THR THR A . n 
A 1 253 GLY 253 253 253 GLY GLY A . n 
A 1 254 LEU 254 254 254 LEU LEU A . n 
A 1 255 ALA 255 255 255 ALA ALA A . n 
A 1 256 TYR 256 256 256 TYR TYR A . n 
A 1 257 ALA 257 257 257 ALA ALA A . n 
A 1 258 LEU 258 258 258 LEU LEU A . n 
A 1 259 PRO 259 259 259 PRO PRO A . n 
A 1 260 HIS 260 260 260 HIS HIS A . n 
A 1 261 TRP 261 261 261 TRP TRP A . n 
A 1 262 ARG 262 262 262 ARG ARG A . n 
A 1 263 TRP 263 263 263 TRP TRP A . n 
A 1 264 LEU 264 264 264 LEU LEU A . n 
A 1 265 GLN 265 265 265 GLN GLN A . n 
A 1 266 LEU 266 266 266 LEU LEU A . n 
A 1 267 ALA 267 267 267 ALA ALA A . n 
A 1 268 VAL 268 268 268 VAL VAL A . n 
A 1 269 SER 269 269 269 SER SER A . n 
A 1 270 LEU 270 270 270 LEU LEU A . n 
A 1 271 PRO 271 271 271 PRO PRO A . n 
A 1 272 THR 272 272 272 THR THR A . n 
A 1 273 PHE 273 273 273 PHE PHE A . n 
A 1 274 LEU 274 274 274 LEU LEU A . n 
A 1 275 PHE 275 275 275 PHE PHE A . n 
A 1 276 LEU 276 276 276 LEU LEU A . n 
A 1 277 LEU 277 277 277 LEU LEU A . n 
A 1 278 TYR 278 278 278 TYR TYR A . n 
A 1 279 TYR 279 279 279 TYR TYR A . n 
A 1 280 TRP 280 280 ?   ?   ?   A . n 
A 1 281 CYS 281 281 ?   ?   ?   A . n 
A 1 282 VAL 282 282 ?   ?   ?   A . n 
A 1 283 PRO 283 283 ?   ?   ?   A . n 
A 1 284 GLU 284 284 ?   ?   ?   A . n 
A 1 285 SER 285 285 ?   ?   ?   A . n 
A 1 286 PRO 286 286 ?   ?   ?   A . n 
A 1 287 ARG 287 287 ?   ?   ?   A . n 
A 1 288 TRP 288 288 ?   ?   ?   A . n 
A 1 289 LEU 289 289 ?   ?   ?   A . n 
A 1 290 LEU 290 290 ?   ?   ?   A . n 
A 1 291 SER 291 291 ?   ?   ?   A . n 
A 1 292 GLN 292 292 ?   ?   ?   A . n 
A 1 293 LYS 293 293 ?   ?   ?   A . n 
A 1 294 ARG 294 294 ?   ?   ?   A . n 
A 1 295 ASN 295 295 ?   ?   ?   A . n 
A 1 296 THR 296 296 ?   ?   ?   A . n 
A 1 297 GLU 297 297 ?   ?   ?   A . n 
A 1 298 ALA 298 298 ?   ?   ?   A . n 
A 1 299 ILE 299 299 ?   ?   ?   A . n 
A 1 300 LYS 300 300 ?   ?   ?   A . n 
A 1 301 ILE 301 301 ?   ?   ?   A . n 
A 1 302 MET 302 302 ?   ?   ?   A . n 
A 1 303 ASP 303 303 ?   ?   ?   A . n 
A 1 304 HIS 304 304 ?   ?   ?   A . n 
A 1 305 ILE 305 305 ?   ?   ?   A . n 
A 1 306 ALA 306 306 ?   ?   ?   A . n 
A 1 307 GLN 307 307 ?   ?   ?   A . n 
A 1 308 LYS 308 308 ?   ?   ?   A . n 
A 1 309 ASN 309 309 ?   ?   ?   A . n 
A 1 310 GLY 310 310 ?   ?   ?   A . n 
A 1 311 LYS 311 311 ?   ?   ?   A . n 
A 1 312 LEU 312 312 ?   ?   ?   A . n 
A 1 313 PRO 313 313 ?   ?   ?   A . n 
A 1 314 PRO 314 314 ?   ?   ?   A . n 
A 1 315 ALA 315 315 ?   ?   ?   A . n 
A 1 316 ASP 316 316 ?   ?   ?   A . n 
A 1 317 LEU 317 317 ?   ?   ?   A . n 
A 1 318 LYS 318 318 ?   ?   ?   A . n 
A 1 319 MET 319 319 ?   ?   ?   A . n 
A 1 320 LEU 320 320 ?   ?   ?   A . n 
A 1 321 SER 321 321 ?   ?   ?   A . n 
A 1 322 LEU 322 322 ?   ?   ?   A . n 
A 1 323 GLU 323 323 ?   ?   ?   A . n 
A 1 324 GLU 324 324 ?   ?   ?   A . n 
A 1 325 ASP 325 325 ?   ?   ?   A . n 
A 1 326 VAL 326 326 ?   ?   ?   A . n 
A 1 327 THR 327 327 ?   ?   ?   A . n 
A 1 328 GLU 328 328 ?   ?   ?   A . n 
A 1 329 LYS 329 329 ?   ?   ?   A . n 
A 1 330 LEU 330 330 ?   ?   ?   A . n 
A 1 331 SER 331 331 331 SER SER A . n 
A 1 332 PRO 332 332 332 PRO PRO A . n 
A 1 333 SER 333 333 333 SER SER A . n 
A 1 334 PHE 334 334 334 PHE PHE A . n 
A 1 335 ALA 335 335 335 ALA ALA A . n 
A 1 336 ASP 336 336 336 ASP ASP A . n 
A 1 337 LEU 337 337 337 LEU LEU A . n 
A 1 338 PHE 338 338 338 PHE PHE A . n 
A 1 339 ARG 339 339 339 ARG ARG A . n 
A 1 340 THR 340 340 340 THR THR A . n 
A 1 341 PRO 341 341 341 PRO PRO A . n 
A 1 342 ARG 342 342 342 ARG ARG A . n 
A 1 343 LEU 343 343 343 LEU LEU A . n 
A 1 344 ARG 344 344 344 ARG ARG A . n 
A 1 345 LYS 345 345 345 LYS LYS A . n 
A 1 346 ARG 346 346 346 ARG ARG A . n 
A 1 347 THR 347 347 347 THR THR A . n 
A 1 348 PHE 348 348 348 PHE PHE A . n 
A 1 349 ILE 349 349 349 ILE ILE A . n 
A 1 350 LEU 350 350 350 LEU LEU A . n 
A 1 351 MET 351 351 351 MET MET A . n 
A 1 352 TYR 352 352 352 TYR TYR A . n 
A 1 353 LEU 353 353 353 LEU LEU A . n 
A 1 354 TRP 354 354 354 TRP TRP A . n 
A 1 355 PHE 355 355 355 PHE PHE A . n 
A 1 356 THR 356 356 356 THR THR A . n 
A 1 357 ASP 357 357 357 ASP ASP A . n 
A 1 358 SER 358 358 358 SER SER A . n 
A 1 359 VAL 359 359 359 VAL VAL A . n 
A 1 360 LEU 360 360 360 LEU LEU A . n 
A 1 361 TYR 361 361 361 TYR TYR A . n 
A 1 362 GLN 362 362 362 GLN GLN A . n 
A 1 363 GLY 363 363 363 GLY GLY A . n 
A 1 364 LEU 364 364 364 LEU LEU A . n 
A 1 365 ILE 365 365 365 ILE ILE A . n 
A 1 366 LEU 366 366 366 LEU LEU A . n 
A 1 367 HIS 367 367 367 HIS HIS A . n 
A 1 368 MET 368 368 368 MET MET A . n 
A 1 369 GLY 369 369 369 GLY GLY A . n 
A 1 370 ALA 370 370 370 ALA ALA A . n 
A 1 371 THR 371 371 371 THR THR A . n 
A 1 372 SER 372 372 372 SER SER A . n 
A 1 373 GLY 373 373 373 GLY GLY A . n 
A 1 374 ASN 374 374 374 ASN ASN A . n 
A 1 375 LEU 375 375 375 LEU LEU A . n 
A 1 376 TYR 376 376 376 TYR TYR A . n 
A 1 377 LEU 377 377 377 LEU LEU A . n 
A 1 378 ASP 378 378 378 ASP ASP A . n 
A 1 379 PHE 379 379 379 PHE PHE A . n 
A 1 380 LEU 380 380 380 LEU LEU A . n 
A 1 381 TYR 381 381 381 TYR TYR A . n 
A 1 382 SER 382 382 382 SER SER A . n 
A 1 383 ALA 383 383 383 ALA ALA A . n 
A 1 384 LEU 384 384 384 LEU LEU A . n 
A 1 385 VAL 385 385 385 VAL VAL A . n 
A 1 386 GLU 386 386 386 GLU GLU A . n 
A 1 387 ILE 387 387 387 ILE ILE A . n 
A 1 388 PRO 388 388 388 PRO PRO A . n 
A 1 389 GLY 389 389 389 GLY GLY A . n 
A 1 390 ALA 390 390 390 ALA ALA A . n 
A 1 391 PHE 391 391 391 PHE PHE A . n 
A 1 392 ILE 392 392 392 ILE ILE A . n 
A 1 393 ALA 393 393 393 ALA ALA A . n 
A 1 394 LEU 394 394 394 LEU LEU A . n 
A 1 395 ILE 395 395 395 ILE ILE A . n 
A 1 396 THR 396 396 396 THR THR A . n 
A 1 397 ILE 397 397 397 ILE ILE A . n 
A 1 398 ASP 398 398 398 ASP ASP A . n 
A 1 399 ARG 399 399 399 ARG ARG A . n 
A 1 400 VAL 400 400 400 VAL VAL A . n 
A 1 401 GLY 401 401 401 GLY GLY A . n 
A 1 402 ARG 402 402 402 ARG ARG A . n 
A 1 403 ILE 403 403 403 ILE ILE A . n 
A 1 404 TYR 404 404 404 TYR TYR A . n 
A 1 405 PRO 405 405 405 PRO PRO A . n 
A 1 406 MET 406 406 406 MET MET A . n 
A 1 407 ALA 407 407 407 ALA ALA A . n 
A 1 408 MET 408 408 408 MET MET A . n 
A 1 409 SER 409 409 409 SER SER A . n 
A 1 410 ASN 410 410 410 ASN ASN A . n 
A 1 411 LEU 411 411 411 LEU LEU A . n 
A 1 412 LEU 412 412 412 LEU LEU A . n 
A 1 413 ALA 413 413 413 ALA ALA A . n 
A 1 414 GLY 414 414 414 GLY GLY A . n 
A 1 415 ALA 415 415 415 ALA ALA A . n 
A 1 416 ALA 416 416 416 ALA ALA A . n 
A 1 417 CYS 417 417 417 CYS CYS A . n 
A 1 418 LEU 418 418 418 LEU LEU A . n 
A 1 419 VAL 419 419 419 VAL VAL A . n 
A 1 420 MET 420 420 420 MET MET A . n 
A 1 421 ILE 421 421 421 ILE ILE A . n 
A 1 422 PHE 422 422 422 PHE PHE A . n 
A 1 423 ILE 423 423 423 ILE ILE A . n 
A 1 424 SER 424 424 424 SER SER A . n 
A 1 425 PRO 425 425 425 PRO PRO A . n 
A 1 426 ASP 426 426 426 ASP ASP A . n 
A 1 427 LEU 427 427 427 LEU LEU A . n 
A 1 428 HIS 428 428 428 HIS HIS A . n 
A 1 429 TRP 429 429 429 TRP TRP A . n 
A 1 430 LEU 430 430 430 LEU LEU A . n 
A 1 431 ASN 431 431 431 ASN ASN A . n 
A 1 432 ILE 432 432 432 ILE ILE A . n 
A 1 433 ILE 433 433 433 ILE ILE A . n 
A 1 434 ILE 434 434 434 ILE ILE A . n 
A 1 435 MET 435 435 435 MET MET A . n 
A 1 436 CYS 436 436 436 CYS CYS A . n 
A 1 437 VAL 437 437 437 VAL VAL A . n 
A 1 438 GLY 438 438 438 GLY GLY A . n 
A 1 439 ARG 439 439 439 ARG ARG A . n 
A 1 440 MET 440 440 440 MET MET A . n 
A 1 441 GLY 441 441 441 GLY GLY A . n 
A 1 442 ILE 442 442 442 ILE ILE A . n 
A 1 443 THR 443 443 443 THR THR A . n 
A 1 444 ILE 444 444 444 ILE ILE A . n 
A 1 445 ALA 445 445 445 ALA ALA A . n 
A 1 446 ILE 446 446 446 ILE ILE A . n 
A 1 447 GLN 447 447 447 GLN GLN A . n 
A 1 448 MET 448 448 448 MET MET A . n 
A 1 449 ILE 449 449 449 ILE ILE A . n 
A 1 450 CYS 450 450 450 CYS CYS A . n 
A 1 451 LEU 451 451 451 LEU LEU A . n 
A 1 452 VAL 452 452 452 VAL VAL A . n 
A 1 453 ASN 453 453 453 ASN ASN A . n 
A 1 454 ALA 454 454 454 ALA ALA A . n 
A 1 455 GLU 455 455 455 GLU GLU A . n 
A 1 456 LEU 456 456 456 LEU LEU A . n 
A 1 457 TYR 457 457 457 TYR TYR A . n 
A 1 458 PRO 458 458 458 PRO PRO A . n 
A 1 459 THR 459 459 459 THR THR A . n 
A 1 460 PHE 460 460 460 PHE PHE A . n 
A 1 461 VAL 461 461 461 VAL VAL A . n 
A 1 462 ARG 462 462 462 ARG ARG A . n 
A 1 463 ASN 463 463 463 ASN ASN A . n 
A 1 464 LEU 464 464 464 LEU LEU A . n 
A 1 465 GLY 465 465 465 GLY GLY A . n 
A 1 466 VAL 466 466 466 VAL VAL A . n 
A 1 467 MET 467 467 467 MET MET A . n 
A 1 468 VAL 468 468 468 VAL VAL A . n 
A 1 469 CYS 469 469 469 CYS CYS A . n 
A 1 470 SER 470 470 470 SER SER A . n 
A 1 471 SER 471 471 471 SER SER A . n 
A 1 472 LEU 472 472 472 LEU LEU A . n 
A 1 473 CYS 473 473 473 CYS CYS A . n 
A 1 474 ASP 474 474 474 ASP ASP A . n 
A 1 475 ILE 475 475 475 ILE ILE A . n 
A 1 476 GLY 476 476 476 GLY GLY A . n 
A 1 477 GLY 477 477 477 GLY GLY A . n 
A 1 478 ILE 478 478 478 ILE ILE A . n 
A 1 479 ILE 479 479 479 ILE ILE A . n 
A 1 480 THR 480 480 480 THR THR A . n 
A 1 481 PRO 481 481 481 PRO PRO A . n 
A 1 482 PHE 482 482 482 PHE PHE A . n 
A 1 483 ILE 483 483 483 ILE ILE A . n 
A 1 484 VAL 484 484 484 VAL VAL A . n 
A 1 485 PHE 485 485 485 PHE PHE A . n 
A 1 486 ARG 486 486 486 ARG ARG A . n 
A 1 487 LEU 487 487 487 LEU LEU A . n 
A 1 488 ARG 488 488 488 ARG ARG A . n 
A 1 489 GLU 489 489 489 GLU GLU A . n 
A 1 490 VAL 490 490 490 VAL VAL A . n 
A 1 491 TRP 491 491 491 TRP TRP A . n 
A 1 492 GLN 492 492 492 GLN GLN A . n 
A 1 493 ALA 493 493 493 ALA ALA A . n 
A 1 494 LEU 494 494 494 LEU LEU A . n 
A 1 495 PRO 495 495 495 PRO PRO A . n 
A 1 496 LEU 496 496 496 LEU LEU A . n 
A 1 497 ILE 497 497 497 ILE ILE A . n 
A 1 498 LEU 498 498 498 LEU LEU A . n 
A 1 499 PHE 499 499 499 PHE PHE A . n 
A 1 500 ALA 500 500 500 ALA ALA A . n 
A 1 501 VAL 501 501 501 VAL VAL A . n 
A 1 502 LEU 502 502 502 LEU LEU A . n 
A 1 503 GLY 503 503 503 GLY GLY A . n 
A 1 504 LEU 504 504 504 LEU LEU A . n 
A 1 505 LEU 505 505 505 LEU LEU A . n 
A 1 506 ALA 506 506 506 ALA ALA A . n 
A 1 507 ALA 507 507 507 ALA ALA A . n 
A 1 508 GLY 508 508 508 GLY GLY A . n 
A 1 509 VAL 509 509 509 VAL VAL A . n 
A 1 510 THR 510 510 510 THR THR A . n 
A 1 511 LEU 511 511 511 LEU LEU A . n 
A 1 512 LEU 512 512 512 LEU LEU A . n 
A 1 513 LEU 513 513 513 LEU LEU A . n 
A 1 514 PRO 514 514 514 PRO PRO A . n 
A 1 515 GLU 515 515 515 GLU GLU A . n 
A 1 516 THR 516 516 ?   ?   ?   A . n 
A 1 517 LYS 517 517 ?   ?   ?   A . n 
A 1 518 GLY 518 518 ?   ?   ?   A . n 
A 1 519 VAL 519 519 ?   ?   ?   A . n 
A 1 520 ALA 520 520 ?   ?   ?   A . n 
A 1 521 LEU 521 521 ?   ?   ?   A . n 
A 1 522 PRO 522 522 ?   ?   ?   A . n 
A 1 523 GLU 523 523 ?   ?   ?   A . n 
A 1 524 THR 524 524 ?   ?   ?   A . n 
A 1 525 MET 525 525 ?   ?   ?   A . n 
A 1 526 LYS 526 526 ?   ?   ?   A . n 
A 1 527 ASP 527 527 ?   ?   ?   A . n 
A 1 528 ALA 528 528 ?   ?   ?   A . n 
A 1 529 GLU 529 529 ?   ?   ?   A . n 
A 1 530 ASN 530 530 ?   ?   ?   A . n 
A 1 531 LEU 531 531 ?   ?   ?   A . n 
A 1 532 GLY 532 532 ?   ?   ?   A . n 
A 1 533 ARG 533 533 ?   ?   ?   A . n 
A 1 534 LYS 534 534 ?   ?   ?   A . n 
A 1 535 ALA 535 535 ?   ?   ?   A . n 
A 1 536 LYS 536 536 ?   ?   ?   A . n 
A 1 537 PRO 537 537 ?   ?   ?   A . n 
A 1 538 LYS 538 538 ?   ?   ?   A . n 
A 1 539 GLU 539 539 ?   ?   ?   A . n 
A 1 540 ASN 540 540 ?   ?   ?   A . n 
A 1 541 THR 541 541 ?   ?   ?   A . n 
A 1 542 ILE 542 542 ?   ?   ?   A . n 
A 1 543 TYR 543 543 ?   ?   ?   A . n 
A 1 544 LEU 544 544 ?   ?   ?   A . n 
A 1 545 LYS 545 545 ?   ?   ?   A . n 
A 1 546 VAL 546 546 ?   ?   ?   A . n 
A 1 547 GLN 547 547 ?   ?   ?   A . n 
A 1 548 THR 548 548 ?   ?   ?   A . n 
A 1 549 SER 549 549 ?   ?   ?   A . n 
A 1 550 GLU 550 550 ?   ?   ?   A . n 
A 1 551 PRO 551 551 ?   ?   ?   A . n 
A 1 552 SER 552 552 ?   ?   ?   A . n 
A 1 553 GLY 553 553 ?   ?   ?   A . n 
A 1 554 THR 554 554 ?   ?   ?   A . n 
# 
_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                     8SC1 
_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                         8SC1 
_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                   8SC1 
_exptl.crystals_number            ? 
_exptl.details                    ? 
_exptl.method                     'ELECTRON MICROSCOPY' 
_exptl.method_details             ? 
# 
_struct.entry_id                     8SC1 
_struct.title                        'Human OCT1 (Apo) in inward-open conformation' 
_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        8SC1 
_struct_keywords.text            'membrane protein, MFS, drug transporter, TRANSPORT PROTEIN' 
_struct_keywords.pdbx_keywords   'TRANSPORT PROTEIN' 
# 
_struct_asym.id                            A 
_struct_asym.pdbx_blank_PDB_chainid_flag   N 
_struct_asym.pdbx_modified                 N 
_struct_asym.entity_id                     1 
_struct_asym.details                       ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    S22A1_HUMAN 
_struct_ref.pdbx_db_accession          O15245 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MPTVDDILEQVGESGWFQKQAFLILCLLSAAFAPICVGIVFLGFTPDHHCQSPGVAELSQRCGWSPAEELNYTVPGLGPA
GEAFLGQCRRYEVDWNQSALSCVDPLASLATNRSHLPLGPCQDGWVYDTPGSSIVTEFNLVCADSWKLDLFQSCLNAGFL
FGSLGVGYFADRFGRKLCLLGTVLVNAVSGVLMAFSPNYMSMLLFRLLQGLVSKGNWMAGYTLITEFVGSGSRRTVAIMY
QMAFTVGLVALTGLAYALPHWRWLQLAVSLPTFLFLLYYWCVPESPRWLLSQKRNTEAIKIMDHIAQKNGKLPPADLKML
SLEEDVTEKLSPSFADLFRTPRLRKRTFILMYLWFTDSVLYQGLILHMGATSGNLYLDFLYSALVEIPGAFIALITIDRV
GRIYPMAMSNLLAGAACLVMIFISPDLHWLNIIIMCVGRMGITIAIQMICLVNAELYPTFVRNLGVMVCSSLCDIGGIIT
PFIVFRLREVWQALPLILFAVLGLLAAGVTLLLPETKGVALPETMKDAENLGRKAKPKENTIYLKVQTSEPSGT
;
_struct_ref.pdbx_align_begin           1 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              8SC1 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 554 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             O15245 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  554 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       554 
# 
_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 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0 
_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 LYS A 19  ? ALA A 31  ? LYS A 19  ALA A 31  1 ? 13 
HELX_P HELX_P2  AA2 PHE A 32  ? GLY A 38  ? PHE A 32  GLY A 38  1 ? 7  
HELX_P HELX_P3  AA3 GLY A 38  ? GLY A 43  ? GLY A 38  GLY A 43  1 ? 6  
HELX_P HELX_P4  AA4 GLY A 54  ? GLY A 63  ? GLY A 54  GLY A 63  1 ? 10 
HELX_P HELX_P5  AA5 SER A 65  ? VAL A 74  ? SER A 65  VAL A 74  1 ? 10 
HELX_P HELX_P6  AA6 ALA A 83  ? CYS A 88  ? ALA A 83  CYS A 88  1 ? 6  
HELX_P HELX_P7  AA7 ASP A 104 ? LEU A 109 ? ASP A 104 LEU A 109 5 ? 6  
HELX_P HELX_P8  AA8 ASN A 112 ? LEU A 116 ? ASN A 112 LEU A 116 5 ? 5  
HELX_P HELX_P9  AA9 SER A 133 ? ASN A 139 ? SER A 133 ASN A 139 1 ? 7  
HELX_P HELX_P10 AB1 VAL A 141 ? SER A 145 ? VAL A 141 SER A 145 5 ? 5  
HELX_P HELX_P11 AB2 TRP A 146 ? PHE A 173 ? TRP A 146 PHE A 173 1 ? 28 
HELX_P HELX_P12 AB3 GLY A 174 ? ALA A 194 ? GLY A 174 ALA A 194 1 ? 21 
HELX_P HELX_P13 AB4 ASN A 198 ? VAL A 228 ? ASN A 198 VAL A 228 1 ? 31 
HELX_P HELX_P14 AB5 SER A 232 ? LEU A 258 ? SER A 232 LEU A 258 1 ? 27 
HELX_P HELX_P15 AB6 HIS A 260 ? TYR A 279 ? HIS A 260 TYR A 279 1 ? 20 
HELX_P HELX_P16 AB7 SER A 333 ? ARG A 339 ? SER A 333 ARG A 339 5 ? 7  
HELX_P HELX_P17 AB8 THR A 340 ? SER A 372 ? THR A 340 SER A 372 1 ? 33 
HELX_P HELX_P18 AB9 ASN A 374 ? VAL A 385 ? ASN A 374 VAL A 385 1 ? 12 
HELX_P HELX_P19 AC1 VAL A 385 ? VAL A 400 ? VAL A 385 VAL A 400 1 ? 16 
HELX_P HELX_P20 AC2 ARG A 402 ? MET A 420 ? ARG A 402 MET A 420 1 ? 19 
HELX_P HELX_P21 AC3 LEU A 427 ? LEU A 456 ? LEU A 427 LEU A 456 1 ? 30 
HELX_P HELX_P22 AC4 PRO A 458 ? SER A 471 ? PRO A 458 SER A 471 1 ? 14 
HELX_P HELX_P23 AC5 SER A 471 ? LEU A 487 ? SER A 471 LEU A 487 1 ? 17 
HELX_P HELX_P24 AC6 ARG A 488 ? VAL A 490 ? ARG A 488 VAL A 490 5 ? 3  
HELX_P HELX_P25 AC7 ALA A 493 ? LEU A 511 ? ALA A 493 LEU A 511 1 ? 19 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
disulf1 disulf ? ? A CYS 50 SG ? ? ? 1_555 A CYS 121 SG ? ? A CYS 50 A CYS 121 1_555 ? ? ? ? ? ? ? 2.027 ? ? 
disulf2 disulf ? ? A CYS 62 SG ? ? ? 1_555 A CYS 102 SG ? ? A CYS 62 A CYS 102 1_555 ? ? ? ? ? ? ? 2.032 ? ? 
disulf3 disulf ? ? A CYS 88 SG ? ? ? 1_555 A CYS 142 SG ? ? A CYS 88 A CYS 142 1_555 ? ? ? ? ? ? ? 2.041 ? ? 
# 
_struct_conn_type.id          disulf 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 CYS A 50 ? CYS A 121 ? CYS A 50 ? 1_555 CYS A 121 ? 1_555 SG SG . . . None 'Disulfide bridge' 
2 CYS A 62 ? CYS A 102 ? CYS A 62 ? 1_555 CYS A 102 ? 1_555 SG SG . . . None 'Disulfide bridge' 
3 CYS A 88 ? CYS A 142 ? CYS A 88 ? 1_555 CYS A 142 ? 1_555 SG SG . . . None 'Disulfide bridge' 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2 ? 
AA2 ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA2 1 2 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 HIS A 48  ? CYS A 50  ? HIS A 48  CYS A 50  
AA1 2 TRP A 125 ? TYR A 127 ? TRP A 125 TYR A 127 
AA2 1 ARG A 90  ? TYR A 91  ? ARG A 90  TYR A 91  
AA2 2 LEU A 118 ? GLY A 119 ? LEU A 118 GLY A 119 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N HIS A 49 ? N HIS A 49 O VAL A 126 ? O VAL A 126 
AA2 1 2 N ARG A 90 ? N ARG A 90 O GLY A 119 ? O GLY A 119 
# 
_pdbx_entry_details.entry_id                   8SC1 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     ? 
_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 THR A 73  ? ? -130.38 -32.89  
2 1 ASP A 104 ? ? -160.04 90.63   
3 1 CYS A 142 ? ? 56.01   -123.26 
4 1 VAL A 400 ? ? -116.41 -72.48  
5 1 ARG A 402 ? ? -137.36 -31.83  
6 1 LEU A 427 ? ? -81.44  48.93   
# 
_em_3d_fitting.id                1 
_em_3d_fitting.entry_id          8SC1 
_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                    8SC1 
_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                  2.92 
_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               1398918 
_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            8.0 
# 
_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                 'Human OCT1' 
_em_entity_assembly.details              ? 
_em_entity_assembly.synonym              ? 
_em_entity_assembly.oligomeric_details   ? 
_em_entity_assembly.entity_id_list       1 
# 
_em_imaging.entry_id                        8SC1 
_em_imaging.id                              1 
_em_imaging.astigmatism                     ? 
_em_imaging.electron_beam_tilt_params       ? 
_em_imaging.residual_tilt                   ? 
_em_imaging.microscope_model                'FEI TITAN 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               'FLOOD BEAM' 
_em_imaging.mode                            'BRIGHT FIELD' 
_em_imaging.nominal_cs                      ? 
_em_imaging.nominal_defocus_min             500 
_em_imaging.nominal_defocus_max             2000 
_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_vitrification.entry_id              8SC1 
_em_vitrification.id                    1 
_em_vitrification.specimen_id           1 
_em_vitrification.cryogen_name          ETHANE 
_em_vitrification.humidity              ? 
_em_vitrification.temp                  ? 
_em_vitrification.chamber_temperature   ? 
_em_vitrification.instrument            ? 
_em_vitrification.method                ? 
_em_vitrification.time_resolved_state   ? 
_em_vitrification.citation_id           ? 
_em_vitrification.details               ? 
# 
_em_experiment.entry_id                8SC1 
_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 PRO 2   ? A PRO 2   
3   1 Y 1 A THR 3   ? A THR 3   
4   1 Y 1 A VAL 4   ? A VAL 4   
5   1 Y 1 A ASP 5   ? A ASP 5   
6   1 Y 1 A ASP 6   ? A ASP 6   
7   1 Y 1 A ILE 7   ? A ILE 7   
8   1 Y 1 A LEU 8   ? A LEU 8   
9   1 Y 1 A GLU 9   ? A GLU 9   
10  1 Y 1 A GLN 10  ? A GLN 10  
11  1 Y 1 A VAL 11  ? A VAL 11  
12  1 Y 1 A GLY 12  ? A GLY 12  
13  1 Y 1 A GLU 13  ? A GLU 13  
14  1 Y 1 A SER 14  ? A SER 14  
15  1 Y 1 A GLY 15  ? A GLY 15  
16  1 Y 1 A TRP 16  ? A TRP 16  
17  1 Y 1 A PHE 17  ? A PHE 17  
18  1 Y 1 A GLN 18  ? A GLN 18  
19  1 Y 1 A TRP 280 ? A TRP 280 
20  1 Y 1 A CYS 281 ? A CYS 281 
21  1 Y 1 A VAL 282 ? A VAL 282 
22  1 Y 1 A PRO 283 ? A PRO 283 
23  1 Y 1 A GLU 284 ? A GLU 284 
24  1 Y 1 A SER 285 ? A SER 285 
25  1 Y 1 A PRO 286 ? A PRO 286 
26  1 Y 1 A ARG 287 ? A ARG 287 
27  1 Y 1 A TRP 288 ? A TRP 288 
28  1 Y 1 A LEU 289 ? A LEU 289 
29  1 Y 1 A LEU 290 ? A LEU 290 
30  1 Y 1 A SER 291 ? A SER 291 
31  1 Y 1 A GLN 292 ? A GLN 292 
32  1 Y 1 A LYS 293 ? A LYS 293 
33  1 Y 1 A ARG 294 ? A ARG 294 
34  1 Y 1 A ASN 295 ? A ASN 295 
35  1 Y 1 A THR 296 ? A THR 296 
36  1 Y 1 A GLU 297 ? A GLU 297 
37  1 Y 1 A ALA 298 ? A ALA 298 
38  1 Y 1 A ILE 299 ? A ILE 299 
39  1 Y 1 A LYS 300 ? A LYS 300 
40  1 Y 1 A ILE 301 ? A ILE 301 
41  1 Y 1 A MET 302 ? A MET 302 
42  1 Y 1 A ASP 303 ? A ASP 303 
43  1 Y 1 A HIS 304 ? A HIS 304 
44  1 Y 1 A ILE 305 ? A ILE 305 
45  1 Y 1 A ALA 306 ? A ALA 306 
46  1 Y 1 A GLN 307 ? A GLN 307 
47  1 Y 1 A LYS 308 ? A LYS 308 
48  1 Y 1 A ASN 309 ? A ASN 309 
49  1 Y 1 A GLY 310 ? A GLY 310 
50  1 Y 1 A LYS 311 ? A LYS 311 
51  1 Y 1 A LEU 312 ? A LEU 312 
52  1 Y 1 A PRO 313 ? A PRO 313 
53  1 Y 1 A PRO 314 ? A PRO 314 
54  1 Y 1 A ALA 315 ? A ALA 315 
55  1 Y 1 A ASP 316 ? A ASP 316 
56  1 Y 1 A LEU 317 ? A LEU 317 
57  1 Y 1 A LYS 318 ? A LYS 318 
58  1 Y 1 A MET 319 ? A MET 319 
59  1 Y 1 A LEU 320 ? A LEU 320 
60  1 Y 1 A SER 321 ? A SER 321 
61  1 Y 1 A LEU 322 ? A LEU 322 
62  1 Y 1 A GLU 323 ? A GLU 323 
63  1 Y 1 A GLU 324 ? A GLU 324 
64  1 Y 1 A ASP 325 ? A ASP 325 
65  1 Y 1 A VAL 326 ? A VAL 326 
66  1 Y 1 A THR 327 ? A THR 327 
67  1 Y 1 A GLU 328 ? A GLU 328 
68  1 Y 1 A LYS 329 ? A LYS 329 
69  1 Y 1 A LEU 330 ? A LEU 330 
70  1 Y 1 A THR 516 ? A THR 516 
71  1 Y 1 A LYS 517 ? A LYS 517 
72  1 Y 1 A GLY 518 ? A GLY 518 
73  1 Y 1 A VAL 519 ? A VAL 519 
74  1 Y 1 A ALA 520 ? A ALA 520 
75  1 Y 1 A LEU 521 ? A LEU 521 
76  1 Y 1 A PRO 522 ? A PRO 522 
77  1 Y 1 A GLU 523 ? A GLU 523 
78  1 Y 1 A THR 524 ? A THR 524 
79  1 Y 1 A MET 525 ? A MET 525 
80  1 Y 1 A LYS 526 ? A LYS 526 
81  1 Y 1 A ASP 527 ? A ASP 527 
82  1 Y 1 A ALA 528 ? A ALA 528 
83  1 Y 1 A GLU 529 ? A GLU 529 
84  1 Y 1 A ASN 530 ? A ASN 530 
85  1 Y 1 A LEU 531 ? A LEU 531 
86  1 Y 1 A GLY 532 ? A GLY 532 
87  1 Y 1 A ARG 533 ? A ARG 533 
88  1 Y 1 A LYS 534 ? A LYS 534 
89  1 Y 1 A ALA 535 ? A ALA 535 
90  1 Y 1 A LYS 536 ? A LYS 536 
91  1 Y 1 A PRO 537 ? A PRO 537 
92  1 Y 1 A LYS 538 ? A LYS 538 
93  1 Y 1 A GLU 539 ? A GLU 539 
94  1 Y 1 A ASN 540 ? A ASN 540 
95  1 Y 1 A THR 541 ? A THR 541 
96  1 Y 1 A ILE 542 ? A ILE 542 
97  1 Y 1 A TYR 543 ? A TYR 543 
98  1 Y 1 A LEU 544 ? A LEU 544 
99  1 Y 1 A LYS 545 ? A LYS 545 
100 1 Y 1 A VAL 546 ? A VAL 546 
101 1 Y 1 A GLN 547 ? A GLN 547 
102 1 Y 1 A THR 548 ? A THR 548 
103 1 Y 1 A SER 549 ? A SER 549 
104 1 Y 1 A GLU 550 ? A GLU 550 
105 1 Y 1 A PRO 551 ? A PRO 551 
106 1 Y 1 A SER 552 ? A SER 552 
107 1 Y 1 A GLY 553 ? A GLY 553 
108 1 Y 1 A THR 554 ? A THR 554 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
CYS N    N N N 74  
CYS CA   C N R 75  
CYS C    C N N 76  
CYS O    O N N 77  
CYS CB   C N N 78  
CYS SG   S N N 79  
CYS OXT  O N N 80  
CYS H    H N N 81  
CYS H2   H N N 82  
CYS HA   H N N 83  
CYS HB2  H N N 84  
CYS HB3  H N N 85  
CYS HG   H N N 86  
CYS HXT  H N N 87  
GLN N    N N N 88  
GLN CA   C N S 89  
GLN C    C N N 90  
GLN O    O N N 91  
GLN CB   C N N 92  
GLN CG   C N N 93  
GLN CD   C N N 94  
GLN OE1  O N N 95  
GLN NE2  N N N 96  
GLN OXT  O N N 97  
GLN H    H N N 98  
GLN H2   H N N 99  
GLN HA   H N N 100 
GLN HB2  H N N 101 
GLN HB3  H N N 102 
GLN HG2  H N N 103 
GLN HG3  H N N 104 
GLN HE21 H N N 105 
GLN HE22 H N N 106 
GLN HXT  H N N 107 
GLU N    N N N 108 
GLU CA   C N S 109 
GLU C    C N N 110 
GLU O    O N N 111 
GLU CB   C N N 112 
GLU CG   C N N 113 
GLU CD   C N N 114 
GLU OE1  O N N 115 
GLU OE2  O N N 116 
GLU OXT  O N N 117 
GLU H    H N N 118 
GLU H2   H N N 119 
GLU HA   H N N 120 
GLU HB2  H N N 121 
GLU HB3  H N N 122 
GLU HG2  H N N 123 
GLU HG3  H N N 124 
GLU HE2  H N N 125 
GLU HXT  H N N 126 
GLY N    N N N 127 
GLY CA   C N N 128 
GLY C    C N N 129 
GLY O    O N N 130 
GLY OXT  O N N 131 
GLY H    H N N 132 
GLY H2   H N N 133 
GLY HA2  H N N 134 
GLY HA3  H N N 135 
GLY HXT  H N N 136 
HIS N    N N N 137 
HIS CA   C N S 138 
HIS C    C N N 139 
HIS O    O N N 140 
HIS CB   C N N 141 
HIS CG   C Y N 142 
HIS ND1  N Y N 143 
HIS CD2  C Y N 144 
HIS CE1  C Y N 145 
HIS NE2  N Y N 146 
HIS OXT  O N N 147 
HIS H    H N N 148 
HIS H2   H N N 149 
HIS HA   H N N 150 
HIS HB2  H N N 151 
HIS HB3  H N N 152 
HIS HD1  H N N 153 
HIS HD2  H N N 154 
HIS HE1  H N N 155 
HIS HE2  H N N 156 
HIS HXT  H N N 157 
ILE N    N N N 158 
ILE CA   C N S 159 
ILE C    C N N 160 
ILE O    O N N 161 
ILE CB   C N S 162 
ILE CG1  C N N 163 
ILE CG2  C N N 164 
ILE CD1  C N N 165 
ILE OXT  O N N 166 
ILE H    H N N 167 
ILE H2   H N N 168 
ILE HA   H N N 169 
ILE HB   H N N 170 
ILE HG12 H N N 171 
ILE HG13 H N N 172 
ILE HG21 H N N 173 
ILE HG22 H N N 174 
ILE HG23 H N N 175 
ILE HD11 H N N 176 
ILE HD12 H N N 177 
ILE HD13 H N N 178 
ILE HXT  H N N 179 
LEU N    N N N 180 
LEU CA   C N S 181 
LEU C    C N N 182 
LEU O    O N N 183 
LEU CB   C N N 184 
LEU CG   C N N 185 
LEU CD1  C N N 186 
LEU CD2  C N N 187 
LEU OXT  O N N 188 
LEU H    H N N 189 
LEU H2   H N N 190 
LEU HA   H N N 191 
LEU HB2  H N N 192 
LEU HB3  H N N 193 
LEU HG   H N N 194 
LEU HD11 H N N 195 
LEU HD12 H N N 196 
LEU HD13 H N N 197 
LEU HD21 H N N 198 
LEU HD22 H N N 199 
LEU HD23 H N N 200 
LEU HXT  H N N 201 
LYS N    N N N 202 
LYS CA   C N S 203 
LYS C    C N N 204 
LYS O    O N N 205 
LYS CB   C N N 206 
LYS CG   C N N 207 
LYS CD   C N N 208 
LYS CE   C N N 209 
LYS NZ   N N N 210 
LYS OXT  O N N 211 
LYS H    H N N 212 
LYS H2   H N N 213 
LYS HA   H N N 214 
LYS HB2  H N N 215 
LYS HB3  H N N 216 
LYS HG2  H N N 217 
LYS HG3  H N N 218 
LYS HD2  H N N 219 
LYS HD3  H N N 220 
LYS HE2  H N N 221 
LYS HE3  H N N 222 
LYS HZ1  H N N 223 
LYS HZ2  H N N 224 
LYS HZ3  H N N 225 
LYS HXT  H N N 226 
MET N    N N N 227 
MET CA   C N S 228 
MET C    C N N 229 
MET O    O N N 230 
MET CB   C N N 231 
MET CG   C N N 232 
MET SD   S N N 233 
MET CE   C N N 234 
MET OXT  O N N 235 
MET H    H N N 236 
MET H2   H N N 237 
MET HA   H N N 238 
MET HB2  H N N 239 
MET HB3  H N N 240 
MET HG2  H N N 241 
MET HG3  H N N 242 
MET HE1  H N N 243 
MET HE2  H N N 244 
MET HE3  H N N 245 
MET HXT  H N N 246 
PHE N    N N N 247 
PHE CA   C N S 248 
PHE C    C N N 249 
PHE O    O N N 250 
PHE CB   C N N 251 
PHE CG   C Y N 252 
PHE CD1  C Y N 253 
PHE CD2  C Y N 254 
PHE CE1  C Y N 255 
PHE CE2  C Y N 256 
PHE CZ   C Y N 257 
PHE OXT  O N N 258 
PHE H    H N N 259 
PHE H2   H N N 260 
PHE HA   H N N 261 
PHE HB2  H N N 262 
PHE HB3  H N N 263 
PHE HD1  H N N 264 
PHE HD2  H N N 265 
PHE HE1  H N N 266 
PHE HE2  H N N 267 
PHE HZ   H N N 268 
PHE HXT  H N N 269 
PRO N    N N N 270 
PRO CA   C N S 271 
PRO C    C N N 272 
PRO O    O N N 273 
PRO CB   C N N 274 
PRO CG   C N N 275 
PRO CD   C N N 276 
PRO OXT  O N N 277 
PRO H    H N N 278 
PRO HA   H N N 279 
PRO HB2  H N N 280 
PRO HB3  H N N 281 
PRO HG2  H N N 282 
PRO HG3  H N N 283 
PRO HD2  H N N 284 
PRO HD3  H N N 285 
PRO HXT  H N N 286 
SER N    N N N 287 
SER CA   C N S 288 
SER C    C N N 289 
SER O    O N N 290 
SER CB   C N N 291 
SER OG   O N N 292 
SER OXT  O N N 293 
SER H    H N N 294 
SER H2   H N N 295 
SER HA   H N N 296 
SER HB2  H N N 297 
SER HB3  H N N 298 
SER HG   H N N 299 
SER HXT  H N N 300 
THR N    N N N 301 
THR CA   C N S 302 
THR C    C N N 303 
THR O    O N N 304 
THR CB   C N R 305 
THR OG1  O N N 306 
THR CG2  C N N 307 
THR OXT  O N N 308 
THR H    H N N 309 
THR H2   H N N 310 
THR HA   H N N 311 
THR HB   H N N 312 
THR HG1  H N N 313 
THR HG21 H N N 314 
THR HG22 H N N 315 
THR HG23 H N N 316 
THR HXT  H N N 317 
TRP N    N N N 318 
TRP CA   C N S 319 
TRP C    C N N 320 
TRP O    O N N 321 
TRP CB   C N N 322 
TRP CG   C Y N 323 
TRP CD1  C Y N 324 
TRP CD2  C Y N 325 
TRP NE1  N Y N 326 
TRP CE2  C Y N 327 
TRP CE3  C Y N 328 
TRP CZ2  C Y N 329 
TRP CZ3  C Y N 330 
TRP CH2  C Y N 331 
TRP OXT  O N N 332 
TRP H    H N N 333 
TRP H2   H N N 334 
TRP HA   H N N 335 
TRP HB2  H N N 336 
TRP HB3  H N N 337 
TRP HD1  H N N 338 
TRP HE1  H N N 339 
TRP HE3  H N N 340 
TRP HZ2  H N N 341 
TRP HZ3  H N N 342 
TRP HH2  H N N 343 
TRP HXT  H N N 344 
TYR N    N N N 345 
TYR CA   C N S 346 
TYR C    C N N 347 
TYR O    O N N 348 
TYR CB   C N N 349 
TYR CG   C Y N 350 
TYR CD1  C Y N 351 
TYR CD2  C Y N 352 
TYR CE1  C Y N 353 
TYR CE2  C Y N 354 
TYR CZ   C Y N 355 
TYR OH   O N N 356 
TYR OXT  O N N 357 
TYR H    H N N 358 
TYR H2   H N N 359 
TYR HA   H N N 360 
TYR HB2  H N N 361 
TYR HB3  H N N 362 
TYR HD1  H N N 363 
TYR HD2  H N N 364 
TYR HE1  H N N 365 
TYR HE2  H N N 366 
TYR HH   H N N 367 
TYR HXT  H N N 368 
VAL N    N N N 369 
VAL CA   C N S 370 
VAL C    C N N 371 
VAL O    O N N 372 
VAL CB   C N N 373 
VAL CG1  C N N 374 
VAL CG2  C N N 375 
VAL OXT  O N N 376 
VAL H    H N N 377 
VAL H2   H N N 378 
VAL HA   H N N 379 
VAL HB   H N N 380 
VAL HG11 H N N 381 
VAL HG12 H N N 382 
VAL HG13 H N N 383 
VAL HG21 H N N 384 
VAL HG22 H N N 385 
VAL HG23 H N N 386 
VAL HXT  H N N 387 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
HIS N   CA   sing N N 129 
HIS N   H    sing N N 130 
HIS N   H2   sing N N 131 
HIS CA  C    sing N N 132 
HIS CA  CB   sing N N 133 
HIS CA  HA   sing N N 134 
HIS C   O    doub N N 135 
HIS C   OXT  sing N N 136 
HIS CB  CG   sing N N 137 
HIS CB  HB2  sing N N 138 
HIS CB  HB3  sing N N 139 
HIS CG  ND1  sing Y N 140 
HIS CG  CD2  doub Y N 141 
HIS ND1 CE1  doub Y N 142 
HIS ND1 HD1  sing N N 143 
HIS CD2 NE2  sing Y N 144 
HIS CD2 HD2  sing N N 145 
HIS CE1 NE2  sing Y N 146 
HIS CE1 HE1  sing N N 147 
HIS NE2 HE2  sing N N 148 
HIS OXT HXT  sing N N 149 
ILE N   CA   sing N N 150 
ILE N   H    sing N N 151 
ILE N   H2   sing N N 152 
ILE CA  C    sing N N 153 
ILE CA  CB   sing N N 154 
ILE CA  HA   sing N N 155 
ILE C   O    doub N N 156 
ILE C   OXT  sing N N 157 
ILE CB  CG1  sing N N 158 
ILE CB  CG2  sing N N 159 
ILE CB  HB   sing N N 160 
ILE CG1 CD1  sing N N 161 
ILE CG1 HG12 sing N N 162 
ILE CG1 HG13 sing N N 163 
ILE CG2 HG21 sing N N 164 
ILE CG2 HG22 sing N N 165 
ILE CG2 HG23 sing N N 166 
ILE CD1 HD11 sing N N 167 
ILE CD1 HD12 sing N N 168 
ILE CD1 HD13 sing N N 169 
ILE OXT HXT  sing N N 170 
LEU N   CA   sing N N 171 
LEU N   H    sing N N 172 
LEU N   H2   sing N N 173 
LEU CA  C    sing N N 174 
LEU CA  CB   sing N N 175 
LEU CA  HA   sing N N 176 
LEU C   O    doub N N 177 
LEU C   OXT  sing N N 178 
LEU CB  CG   sing N N 179 
LEU CB  HB2  sing N N 180 
LEU CB  HB3  sing N N 181 
LEU CG  CD1  sing N N 182 
LEU CG  CD2  sing N N 183 
LEU CG  HG   sing N N 184 
LEU CD1 HD11 sing N N 185 
LEU CD1 HD12 sing N N 186 
LEU CD1 HD13 sing N N 187 
LEU CD2 HD21 sing N N 188 
LEU CD2 HD22 sing N N 189 
LEU CD2 HD23 sing N N 190 
LEU OXT HXT  sing N N 191 
LYS N   CA   sing N N 192 
LYS N   H    sing N N 193 
LYS N   H2   sing N N 194 
LYS CA  C    sing N N 195 
LYS CA  CB   sing N N 196 
LYS CA  HA   sing N N 197 
LYS C   O    doub N N 198 
LYS C   OXT  sing N N 199 
LYS CB  CG   sing N N 200 
LYS CB  HB2  sing N N 201 
LYS CB  HB3  sing N N 202 
LYS CG  CD   sing N N 203 
LYS CG  HG2  sing N N 204 
LYS CG  HG3  sing N N 205 
LYS CD  CE   sing N N 206 
LYS CD  HD2  sing N N 207 
LYS CD  HD3  sing N N 208 
LYS CE  NZ   sing N N 209 
LYS CE  HE2  sing N N 210 
LYS CE  HE3  sing N N 211 
LYS NZ  HZ1  sing N N 212 
LYS NZ  HZ2  sing N N 213 
LYS NZ  HZ3  sing N N 214 
LYS OXT HXT  sing N N 215 
MET N   CA   sing N N 216 
MET N   H    sing N N 217 
MET N   H2   sing N N 218 
MET CA  C    sing N N 219 
MET CA  CB   sing N N 220 
MET CA  HA   sing N N 221 
MET C   O    doub N N 222 
MET C   OXT  sing N N 223 
MET CB  CG   sing N N 224 
MET CB  HB2  sing N N 225 
MET CB  HB3  sing N N 226 
MET CG  SD   sing N N 227 
MET CG  HG2  sing N N 228 
MET CG  HG3  sing N N 229 
MET SD  CE   sing N N 230 
MET CE  HE1  sing N N 231 
MET CE  HE2  sing N N 232 
MET CE  HE3  sing N N 233 
MET OXT HXT  sing N N 234 
PHE N   CA   sing N N 235 
PHE N   H    sing N N 236 
PHE N   H2   sing N N 237 
PHE CA  C    sing N N 238 
PHE CA  CB   sing N N 239 
PHE CA  HA   sing N N 240 
PHE C   O    doub N N 241 
PHE C   OXT  sing N N 242 
PHE CB  CG   sing N N 243 
PHE CB  HB2  sing N N 244 
PHE CB  HB3  sing N N 245 
PHE CG  CD1  doub Y N 246 
PHE CG  CD2  sing Y N 247 
PHE CD1 CE1  sing Y N 248 
PHE CD1 HD1  sing N N 249 
PHE CD2 CE2  doub Y N 250 
PHE CD2 HD2  sing N N 251 
PHE CE1 CZ   doub Y N 252 
PHE CE1 HE1  sing N N 253 
PHE CE2 CZ   sing Y N 254 
PHE CE2 HE2  sing N N 255 
PHE CZ  HZ   sing N N 256 
PHE OXT HXT  sing N N 257 
PRO N   CA   sing N N 258 
PRO N   CD   sing N N 259 
PRO N   H    sing N N 260 
PRO CA  C    sing N N 261 
PRO CA  CB   sing N N 262 
PRO CA  HA   sing N N 263 
PRO C   O    doub N N 264 
PRO C   OXT  sing N N 265 
PRO CB  CG   sing N N 266 
PRO CB  HB2  sing N N 267 
PRO CB  HB3  sing N N 268 
PRO CG  CD   sing N N 269 
PRO CG  HG2  sing N N 270 
PRO CG  HG3  sing N N 271 
PRO CD  HD2  sing N N 272 
PRO CD  HD3  sing N N 273 
PRO OXT HXT  sing N N 274 
SER N   CA   sing N N 275 
SER N   H    sing N N 276 
SER N   H2   sing N N 277 
SER CA  C    sing N N 278 
SER CA  CB   sing N N 279 
SER CA  HA   sing N N 280 
SER C   O    doub N N 281 
SER C   OXT  sing N N 282 
SER CB  OG   sing N N 283 
SER CB  HB2  sing N N 284 
SER CB  HB3  sing N N 285 
SER OG  HG   sing N N 286 
SER OXT HXT  sing N N 287 
THR N   CA   sing N N 288 
THR N   H    sing N N 289 
THR N   H2   sing N N 290 
THR CA  C    sing N N 291 
THR CA  CB   sing N N 292 
THR CA  HA   sing N N 293 
THR C   O    doub N N 294 
THR C   OXT  sing N N 295 
THR CB  OG1  sing N N 296 
THR CB  CG2  sing N N 297 
THR CB  HB   sing N N 298 
THR OG1 HG1  sing N N 299 
THR CG2 HG21 sing N N 300 
THR CG2 HG22 sing N N 301 
THR CG2 HG23 sing N N 302 
THR OXT HXT  sing N N 303 
TRP N   CA   sing N N 304 
TRP N   H    sing N N 305 
TRP N   H2   sing N N 306 
TRP CA  C    sing N N 307 
TRP CA  CB   sing N N 308 
TRP CA  HA   sing N N 309 
TRP C   O    doub N N 310 
TRP C   OXT  sing N N 311 
TRP CB  CG   sing N N 312 
TRP CB  HB2  sing N N 313 
TRP CB  HB3  sing N N 314 
TRP CG  CD1  doub Y N 315 
TRP CG  CD2  sing Y N 316 
TRP CD1 NE1  sing Y N 317 
TRP CD1 HD1  sing N N 318 
TRP CD2 CE2  doub Y N 319 
TRP CD2 CE3  sing Y N 320 
TRP NE1 CE2  sing Y N 321 
TRP NE1 HE1  sing N N 322 
TRP CE2 CZ2  sing Y N 323 
TRP CE3 CZ3  doub Y N 324 
TRP CE3 HE3  sing N N 325 
TRP CZ2 CH2  doub Y N 326 
TRP CZ2 HZ2  sing N N 327 
TRP CZ3 CH2  sing Y N 328 
TRP CZ3 HZ3  sing N N 329 
TRP CH2 HH2  sing N N 330 
TRP OXT HXT  sing N N 331 
TYR N   CA   sing N N 332 
TYR N   H    sing N N 333 
TYR N   H2   sing N N 334 
TYR CA  C    sing N N 335 
TYR CA  CB   sing N N 336 
TYR CA  HA   sing N N 337 
TYR C   O    doub N N 338 
TYR C   OXT  sing N N 339 
TYR CB  CG   sing N N 340 
TYR CB  HB2  sing N N 341 
TYR CB  HB3  sing N N 342 
TYR CG  CD1  doub Y N 343 
TYR CG  CD2  sing Y N 344 
TYR CD1 CE1  sing Y N 345 
TYR CD1 HD1  sing N N 346 
TYR CD2 CE2  doub Y N 347 
TYR CD2 HD2  sing N N 348 
TYR CE1 CZ   doub Y N 349 
TYR CE1 HE1  sing N N 350 
TYR CE2 CZ   sing Y N 351 
TYR CE2 HE2  sing N N 352 
TYR CZ  OH   sing N N 353 
TYR OH  HH   sing N N 354 
TYR OXT HXT  sing N N 355 
VAL N   CA   sing N N 356 
VAL N   H    sing N N 357 
VAL N   H2   sing N N 358 
VAL CA  C    sing N N 359 
VAL CA  CB   sing N N 360 
VAL CA  HA   sing N N 361 
VAL C   O    doub N N 362 
VAL C   OXT  sing N N 363 
VAL CB  CG1  sing N N 364 
VAL CB  CG2  sing N N 365 
VAL CB  HB   sing N N 366 
VAL CG1 HG11 sing N N 367 
VAL CG1 HG12 sing N N 368 
VAL CG1 HG13 sing N N 369 
VAL CG2 HG21 sing N N 370 
VAL CG2 HG22 sing N N 371 
VAL CG2 HG23 sing N N 372 
VAL OXT HXT  sing N N 373 
# 
_em_admin.current_status     REL 
_em_admin.deposition_date    2023-04-04 
_em_admin.deposition_site    RCSB 
_em_admin.entry_id           8SC1 
_em_admin.last_update        2025-06-04 
_em_admin.map_release_date   2023-10-18 
_em_admin.title              'Human OCT1 (Apo) in inward-open conformation' 
# 
_em_ctf_correction.details                  ? 
_em_ctf_correction.em_image_processing_id   1 
_em_ctf_correction.id                       1 
_em_ctf_correction.type                     'PHASE FLIPPING ONLY' 
# 
_em_entity_assembly_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         88 
_em_image_recording.details                             ? 
_em_image_recording.detector_mode                       ? 
_em_image_recording.film_or_detector_model              'GATAN K3 (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  ? ? ? PHENIX ? 
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 
# 
_pdbx_audit_support.funding_organization   'National Health and Medical Research Council (NHMRC, Australia)' 
_pdbx_audit_support.country                Australia 
_pdbx_audit_support.grant_number           APP2016308 
_pdbx_audit_support.ordinal                1 
# 
_atom_sites.entry_id                    8SC1 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   1.000000 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   1.000000 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   0.000000 
_atom_sites.fract_transf_matrix[3][3]   1.000000 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM 1    N N   . LYS A 1 19  ? 112.331 83.106  124.361 1.00 100.82 ? 19  LYS A N   1 
ATOM 2    C CA  . LYS A 1 19  ? 113.520 83.874  124.014 1.00 100.67 ? 19  LYS A CA  1 
ATOM 3    C C   . LYS A 1 19  ? 113.481 85.245  124.679 1.00 100.88 ? 19  LYS A C   1 
ATOM 4    O O   . LYS A 1 19  ? 113.162 86.247  124.039 1.00 100.68 ? 19  LYS A O   1 
ATOM 5    C CB  . LYS A 1 19  ? 113.636 84.020  122.497 1.00 102.29 ? 19  LYS A CB  1 
ATOM 6    C CG  . LYS A 1 19  ? 113.881 82.708  121.770 1.00 103.38 ? 19  LYS A CG  1 
ATOM 7    C CD  . LYS A 1 19  ? 114.218 82.937  120.306 1.00 101.96 ? 19  LYS A CD  1 
ATOM 8    C CE  . LYS A 1 19  ? 114.492 81.624  119.595 1.00 100.71 ? 19  LYS A CE  1 
ATOM 9    N NZ  . LYS A 1 19  ? 115.050 81.841  118.233 1.00 103.39 ? 19  LYS A NZ  1 
ATOM 10   N N   . GLN A 1 20  ? 113.802 85.270  125.976 1.00 99.00  ? 20  GLN A N   1 
ATOM 11   C CA  . GLN A 1 20  ? 113.661 86.490  126.764 1.00 99.43  ? 20  GLN A CA  1 
ATOM 12   C C   . GLN A 1 20  ? 114.524 87.624  126.222 1.00 100.03 ? 20  GLN A C   1 
ATOM 13   O O   . GLN A 1 20  ? 114.120 88.792  126.279 1.00 98.74  ? 20  GLN A O   1 
ATOM 14   C CB  . GLN A 1 20  ? 114.008 86.198  128.223 1.00 99.65  ? 20  GLN A CB  1 
ATOM 15   C CG  . GLN A 1 20  ? 113.006 85.282  128.911 1.00 99.81  ? 20  GLN A CG  1 
ATOM 16   C CD  . GLN A 1 20  ? 113.558 84.650  130.172 1.00 101.87 ? 20  GLN A CD  1 
ATOM 17   O OE1 . GLN A 1 20  ? 114.722 84.848  130.522 1.00 100.66 ? 20  GLN A OE1 1 
ATOM 18   N NE2 . GLN A 1 20  ? 112.724 83.879  130.861 1.00 100.49 ? 20  GLN A NE2 1 
ATOM 19   N N   . ALA A 1 21  ? 115.707 87.304  125.695 1.00 97.08  ? 21  ALA A N   1 
ATOM 20   C CA  . ALA A 1 21  ? 116.636 88.332  125.237 1.00 96.54  ? 21  ALA A CA  1 
ATOM 21   C C   . ALA A 1 21  ? 116.203 88.941  123.910 1.00 95.26  ? 21  ALA A C   1 
ATOM 22   O O   . ALA A 1 21  ? 116.535 90.095  123.620 1.00 96.19  ? 21  ALA A O   1 
ATOM 23   C CB  . ALA A 1 21  ? 118.045 87.752  125.112 1.00 95.91  ? 21  ALA A CB  1 
ATOM 24   N N   . PHE A 1 22  ? 115.478 88.176  123.096 1.00 87.82  ? 22  PHE A N   1 
ATOM 25   C CA  . PHE A 1 22  ? 114.976 88.679  121.822 1.00 89.03  ? 22  PHE A CA  1 
ATOM 26   C C   . PHE A 1 22  ? 113.838 89.675  122.028 1.00 90.50  ? 22  PHE A C   1 
ATOM 27   O O   . PHE A 1 22  ? 113.875 90.797  121.501 1.00 86.52  ? 22  PHE A O   1 
ATOM 28   C CB  . PHE A 1 22  ? 114.546 87.478  120.971 1.00 88.25  ? 22  PHE A CB  1 
ATOM 29   C CG  . PHE A 1 22  ? 113.512 87.780  119.925 1.00 89.76  ? 22  PHE A CG  1 
ATOM 30   C CD1 . PHE A 1 22  ? 113.888 88.227  118.671 1.00 90.84  ? 22  PHE A CD1 1 
ATOM 31   C CD2 . PHE A 1 22  ? 112.167 87.570  120.180 1.00 88.11  ? 22  PHE A CD2 1 
ATOM 32   C CE1 . PHE A 1 22  ? 112.940 88.478  117.699 1.00 91.36  ? 22  PHE A CE1 1 
ATOM 33   C CE2 . PHE A 1 22  ? 111.215 87.829  119.217 1.00 90.92  ? 22  PHE A CE2 1 
ATOM 34   C CZ  . PHE A 1 22  ? 111.601 88.283  117.975 1.00 91.53  ? 22  PHE A CZ  1 
ATOM 35   N N   . LEU A 1 23  ? 112.808 89.273  122.782 1.00 90.69  ? 23  LEU A N   1 
ATOM 36   C CA  . LEU A 1 23  ? 111.633 90.118  122.980 1.00 88.76  ? 23  LEU A CA  1 
ATOM 37   C C   . LEU A 1 23  ? 111.984 91.495  123.531 1.00 88.09  ? 23  LEU A C   1 
ATOM 38   O O   . LEU A 1 23  ? 111.348 92.490  123.165 1.00 87.76  ? 23  LEU A O   1 
ATOM 39   C CB  . LEU A 1 23  ? 110.647 89.416  123.914 1.00 87.37  ? 23  LEU A CB  1 
ATOM 40   C CG  . LEU A 1 23  ? 110.019 88.129  123.375 1.00 87.96  ? 23  LEU A CG  1 
ATOM 41   C CD1 . LEU A 1 23  ? 109.269 87.393  124.473 1.00 87.96  ? 23  LEU A CD1 1 
ATOM 42   C CD2 . LEU A 1 23  ? 109.102 88.428  122.199 1.00 88.95  ? 23  LEU A CD2 1 
ATOM 43   N N   . ILE A 1 24  ? 113.010 91.588  124.378 1.00 85.14  ? 24  ILE A N   1 
ATOM 44   C CA  . ILE A 1 24  ? 113.318 92.879  124.988 1.00 85.94  ? 24  ILE A CA  1 
ATOM 45   C C   . ILE A 1 24  ? 113.993 93.813  123.990 1.00 84.98  ? 24  ILE A C   1 
ATOM 46   O O   . ILE A 1 24  ? 113.725 95.023  123.981 1.00 88.66  ? 24  ILE A O   1 
ATOM 47   C CB  . ILE A 1 24  ? 114.168 92.686  126.256 1.00 87.96  ? 24  ILE A CB  1 
ATOM 48   C CG1 . ILE A 1 24  ? 115.516 92.046  125.921 1.00 85.78  ? 24  ILE A CG1 1 
ATOM 49   C CG2 . ILE A 1 24  ? 113.410 91.850  127.279 1.00 86.75  ? 24  ILE A CG2 1 
ATOM 50   C CD1 . ILE A 1 24  ? 116.357 91.721  127.133 1.00 86.10  ? 24  ILE A CD1 1 
ATOM 51   N N   . LEU A 1 25  ? 114.812 93.281  123.083 1.00 75.45  ? 25  LEU A N   1 
ATOM 52   C CA  . LEU A 1 25  ? 115.362 94.157  122.061 1.00 78.89  ? 25  LEU A CA  1 
ATOM 53   C C   . LEU A 1 25  ? 114.306 94.510  121.024 1.00 77.94  ? 25  LEU A C   1 
ATOM 54   O O   . LEU A 1 25  ? 114.353 95.600  120.442 1.00 81.55  ? 25  LEU A O   1 
ATOM 55   C CB  . LEU A 1 25  ? 116.585 93.507  121.417 1.00 79.59  ? 25  LEU A CB  1 
ATOM 56   C CG  . LEU A 1 25  ? 117.718 93.261  122.418 1.00 77.48  ? 25  LEU A CG  1 
ATOM 57   C CD1 . LEU A 1 25  ? 118.881 92.521  121.782 1.00 76.21  ? 25  LEU A CD1 1 
ATOM 58   C CD2 . LEU A 1 25  ? 118.188 94.573  123.025 1.00 78.64  ? 25  LEU A CD2 1 
ATOM 59   N N   . CYS A 1 26  ? 113.334 93.622  120.787 1.00 67.39  ? 26  CYS A N   1 
ATOM 60   C CA  . CYS A 1 26  ? 112.245 94.022  119.904 1.00 68.42  ? 26  CYS A CA  1 
ATOM 61   C C   . CYS A 1 26  ? 111.377 95.086  120.561 1.00 67.43  ? 26  CYS A C   1 
ATOM 62   O O   . CYS A 1 26  ? 110.750 95.893  119.866 1.00 63.07  ? 26  CYS A O   1 
ATOM 63   C CB  . CYS A 1 26  ? 111.405 92.812  119.508 1.00 74.84  ? 26  CYS A CB  1 
ATOM 64   S SG  . CYS A 1 26  ? 112.335 91.587  118.585 1.00 77.47  ? 26  CYS A SG  1 
ATOM 65   N N   . LEU A 1 27  ? 111.329 95.096  121.897 1.00 64.35  ? 27  LEU A N   1 
ATOM 66   C CA  . LEU A 1 27  ? 110.634 96.163  122.609 1.00 61.49  ? 27  LEU A CA  1 
ATOM 67   C C   . LEU A 1 27  ? 111.413 97.465  122.509 1.00 60.27  ? 27  LEU A C   1 
ATOM 68   O O   . LEU A 1 27  ? 110.822 98.550  122.491 1.00 62.83  ? 27  LEU A O   1 
ATOM 69   C CB  . LEU A 1 27  ? 110.423 95.770  124.072 1.00 63.31  ? 27  LEU A CB  1 
ATOM 70   C CG  . LEU A 1 27  ? 109.873 96.832  125.029 1.00 65.29  ? 27  LEU A CG  1 
ATOM 71   C CD1 . LEU A 1 27  ? 108.481 97.277  124.607 1.00 65.28  ? 27  LEU A CD1 1 
ATOM 72   C CD2 . LEU A 1 27  ? 109.865 96.320  126.462 1.00 60.12  ? 27  LEU A CD2 1 
ATOM 73   N N   . LEU A 1 28  ? 112.742 97.365  122.441 1.00 54.38  ? 28  LEU A N   1 
ATOM 74   C CA  . LEU A 1 28  ? 113.586 98.541  122.266 1.00 51.28  ? 28  LEU A CA  1 
ATOM 75   C C   . LEU A 1 28  ? 113.533 99.079  120.841 1.00 52.31  ? 28  LEU A C   1 
ATOM 76   O O   . LEU A 1 28  ? 113.783 100.270 120.629 1.00 59.33  ? 28  LEU A O   1 
ATOM 77   C CB  . LEU A 1 28  ? 115.030 98.204  122.647 1.00 56.74  ? 28  LEU A CB  1 
ATOM 78   C CG  . LEU A 1 28  ? 116.062 99.334  122.687 1.00 59.30  ? 28  LEU A CG  1 
ATOM 79   C CD1 . LEU A 1 28  ? 115.683 100.372 123.732 1.00 59.08  ? 28  LEU A CD1 1 
ATOM 80   C CD2 . LEU A 1 28  ? 117.452 98.783  122.956 1.00 55.10  ? 28  LEU A CD2 1 
ATOM 81   N N   . SER A 1 29  ? 113.208 98.228  119.864 1.00 51.22  ? 29  SER A N   1 
ATOM 82   C CA  . SER A 1 29  ? 113.031 98.668  118.481 1.00 45.77  ? 29  SER A CA  1 
ATOM 83   C C   . SER A 1 29  ? 111.658 99.293  118.243 1.00 46.07  ? 29  SER A C   1 
ATOM 84   O O   . SER A 1 29  ? 111.536 100.254 117.477 1.00 42.79  ? 29  SER A O   1 
ATOM 85   C CB  . SER A 1 29  ? 113.250 97.493  117.529 1.00 44.94  ? 29  SER A CB  1 
ATOM 86   O OG  . SER A 1 29  ? 113.287 97.930  116.183 1.00 47.50  ? 29  SER A OG  1 
ATOM 87   N N   . ALA A 1 30  ? 110.617 98.751  118.875 1.00 39.66  ? 30  ALA A N   1 
ATOM 88   C CA  . ALA A 1 30  ? 109.273 99.306  118.737 1.00 38.62  ? 30  ALA A CA  1 
ATOM 89   C C   . ALA A 1 30  ? 109.171 100.709 119.326 1.00 48.90  ? 30  ALA A C   1 
ATOM 90   O O   . ALA A 1 30  ? 108.529 101.587 118.739 1.00 49.41  ? 30  ALA A O   1 
ATOM 91   C CB  . ALA A 1 30  ? 108.257 98.376  119.399 1.00 39.94  ? 30  ALA A CB  1 
ATOM 92   N N   . ALA A 1 31  ? 109.789 100.938 120.485 1.00 49.28  ? 31  ALA A N   1 
ATOM 93   C CA  . ALA A 1 31  ? 109.717 102.220 121.180 1.00 42.97  ? 31  ALA A CA  1 
ATOM 94   C C   . ALA A 1 31  ? 110.449 103.350 120.464 1.00 44.14  ? 31  ALA A C   1 
ATOM 95   O O   . ALA A 1 31  ? 110.284 104.510 120.856 1.00 46.82  ? 31  ALA A O   1 
ATOM 96   C CB  . ALA A 1 31  ? 110.272 102.073 122.597 1.00 41.41  ? 31  ALA A CB  1 
ATOM 97   N N   . PHE A 1 32  ? 111.249 103.052 119.440 1.00 39.68  ? 32  PHE A N   1 
ATOM 98   C CA  . PHE A 1 32  ? 111.907 104.099 118.666 1.00 35.94  ? 32  PHE A CA  1 
ATOM 99   C C   . PHE A 1 32  ? 110.960 104.801 117.693 1.00 40.81  ? 32  PHE A C   1 
ATOM 100  O O   . PHE A 1 32  ? 111.131 105.996 117.432 1.00 50.17  ? 32  PHE A O   1 
ATOM 101  C CB  . PHE A 1 32  ? 113.091 103.486 117.914 1.00 39.33  ? 32  PHE A CB  1 
ATOM 102  C CG  . PHE A 1 32  ? 113.967 104.483 117.215 1.00 44.04  ? 32  PHE A CG  1 
ATOM 103  C CD1 . PHE A 1 32  ? 114.450 105.594 117.883 1.00 45.56  ? 32  PHE A CD1 1 
ATOM 104  C CD2 . PHE A 1 32  ? 114.341 104.288 115.897 1.00 41.95  ? 32  PHE A CD2 1 
ATOM 105  C CE1 . PHE A 1 32  ? 115.268 106.502 117.242 1.00 44.17  ? 32  PHE A CE1 1 
ATOM 106  C CE2 . PHE A 1 32  ? 115.160 105.193 115.253 1.00 39.94  ? 32  PHE A CE2 1 
ATOM 107  C CZ  . PHE A 1 32  ? 115.624 106.300 115.927 1.00 42.95  ? 32  PHE A CZ  1 
ATOM 108  N N   . ALA A 1 33  ? 109.981 104.084 117.141 1.00 38.79  ? 33  ALA A N   1 
ATOM 109  C CA  . ALA A 1 33  ? 109.089 104.664 116.137 1.00 39.55  ? 33  ALA A CA  1 
ATOM 110  C C   . ALA A 1 33  ? 108.310 105.900 116.592 1.00 44.93  ? 33  ALA A C   1 
ATOM 111  O O   . ALA A 1 33  ? 108.208 106.856 115.797 1.00 40.31  ? 33  ALA A O   1 
ATOM 112  C CB  . ALA A 1 33  ? 108.125 103.583 115.633 1.00 43.95  ? 33  ALA A CB  1 
ATOM 113  N N   . PRO A 1 34  ? 107.742 105.959 117.805 1.00 44.15  ? 34  PRO A N   1 
ATOM 114  C CA  . PRO A 1 34  ? 107.090 107.205 118.243 1.00 42.72  ? 34  PRO A CA  1 
ATOM 115  C C   . PRO A 1 34  ? 108.018 108.400 118.303 1.00 41.44  ? 34  PRO A C   1 
ATOM 116  O O   . PRO A 1 34  ? 107.539 109.537 118.218 1.00 44.24  ? 34  PRO A O   1 
ATOM 117  C CB  . PRO A 1 34  ? 106.554 106.840 119.632 1.00 38.79  ? 34  PRO A CB  1 
ATOM 118  C CG  . PRO A 1 34  ? 106.319 105.380 119.542 1.00 33.62  ? 34  PRO A CG  1 
ATOM 119  C CD  . PRO A 1 34  ? 107.508 104.880 118.783 1.00 34.78  ? 34  PRO A CD  1 
ATOM 120  N N   . ILE A 1 35  ? 109.325 108.192 118.457 1.00 35.45  ? 35  ILE A N   1 
ATOM 121  C CA  . ILE A 1 35  ? 110.235 109.326 118.549 1.00 32.88  ? 35  ILE A CA  1 
ATOM 122  C C   . ILE A 1 35  ? 110.421 109.946 117.172 1.00 32.63  ? 35  ILE A C   1 
ATOM 123  O O   . ILE A 1 35  ? 110.461 111.173 117.022 1.00 37.57  ? 35  ILE A O   1 
ATOM 124  C CB  . ILE A 1 35  ? 111.576 108.892 119.168 1.00 40.12  ? 35  ILE A CB  1 
ATOM 125  C CG1 . ILE A 1 35  ? 111.369 108.411 120.605 1.00 39.17  ? 35  ILE A CG1 1 
ATOM 126  C CG2 . ILE A 1 35  ? 112.584 110.027 119.125 1.00 45.69  ? 35  ILE A CG2 1 
ATOM 127  C CD1 . ILE A 1 35  ? 112.605 107.812 121.230 1.00 41.44  ? 35  ILE A CD1 1 
ATOM 128  N N   . CYS A 1 36  ? 110.530 109.104 116.144 1.00 38.92  ? 36  CYS A N   1 
ATOM 129  C CA  . CYS A 1 36  ? 110.734 109.578 114.781 1.00 39.77  ? 36  CYS A CA  1 
ATOM 130  C C   . CYS A 1 36  ? 109.459 110.143 114.163 1.00 42.73  ? 36  CYS A C   1 
ATOM 131  O O   . CYS A 1 36  ? 109.513 111.158 113.460 1.00 44.30  ? 36  CYS A O   1 
ATOM 132  C CB  . CYS A 1 36  ? 111.276 108.445 113.909 1.00 37.04  ? 36  CYS A CB  1 
ATOM 133  S SG  . CYS A 1 36  ? 112.774 107.671 114.536 1.00 52.31  ? 36  CYS A SG  1 
ATOM 134  N N   . VAL A 1 37  ? 108.306 109.515 114.401 1.00 45.30  ? 37  VAL A N   1 
ATOM 135  C CA  . VAL A 1 37  ? 107.097 109.845 113.646 1.00 38.70  ? 37  VAL A CA  1 
ATOM 136  C C   . VAL A 1 37  ? 106.014 110.508 114.500 1.00 39.56  ? 37  VAL A C   1 
ATOM 137  O O   . VAL A 1 37  ? 105.059 111.070 113.937 1.00 36.06  ? 37  VAL A O   1 
ATOM 138  C CB  . VAL A 1 37  ? 106.546 108.584 112.936 1.00 34.07  ? 37  VAL A CB  1 
ATOM 139  C CG1 . VAL A 1 37  ? 105.219 108.817 112.221 1.00 36.72  ? 37  VAL A CG1 1 
ATOM 140  C CG2 . VAL A 1 37  ? 107.578 108.038 111.958 1.00 36.18  ? 37  VAL A CG2 1 
ATOM 141  N N   . GLY A 1 38  ? 106.176 110.554 115.823 1.00 38.32  ? 38  GLY A N   1 
ATOM 142  C CA  . GLY A 1 38  ? 105.156 111.113 116.701 1.00 31.50  ? 38  GLY A CA  1 
ATOM 143  C C   . GLY A 1 38  ? 104.771 112.558 116.434 1.00 37.46  ? 38  GLY A C   1 
ATOM 144  O O   . GLY A 1 38  ? 103.705 112.991 116.883 1.00 30.35  ? 38  GLY A O   1 
ATOM 145  N N   . ILE A 1 39  ? 105.616 113.321 115.733 1.00 43.06  ? 39  ILE A N   1 
ATOM 146  C CA  . ILE A 1 39  ? 105.277 114.697 115.358 1.00 28.15  ? 39  ILE A CA  1 
ATOM 147  C C   . ILE A 1 39  ? 103.967 114.777 114.579 1.00 29.50  ? 39  ILE A C   1 
ATOM 148  O O   . ILE A 1 39  ? 103.275 115.802 114.619 1.00 30.90  ? 39  ILE A O   1 
ATOM 149  C CB  . ILE A 1 39  ? 106.440 115.333 114.567 1.00 30.81  ? 39  ILE A CB  1 
ATOM 150  C CG1 . ILE A 1 39  ? 106.202 116.834 114.380 1.00 35.73  ? 39  ILE A CG1 1 
ATOM 151  C CG2 . ILE A 1 39  ? 106.624 114.646 113.223 1.00 33.13  ? 39  ILE A CG2 1 
ATOM 152  C CD1 . ILE A 1 39  ? 107.368 117.571 113.768 1.00 32.24  ? 39  ILE A CD1 1 
ATOM 153  N N   . VAL A 1 40  ? 103.602 113.712 113.863 1.00 36.21  ? 40  VAL A N   1 
ATOM 154  C CA  . VAL A 1 40  ? 102.359 113.696 113.094 1.00 34.07  ? 40  VAL A CA  1 
ATOM 155  C C   . VAL A 1 40  ? 101.141 113.875 113.993 1.00 32.29  ? 40  VAL A C   1 
ATOM 156  O O   . VAL A 1 40  ? 100.150 114.499 113.593 1.00 28.22  ? 40  VAL A O   1 
ATOM 157  C CB  . VAL A 1 40  ? 102.282 112.394 112.270 1.00 29.19  ? 40  VAL A CB  1 
ATOM 158  C CG1 . VAL A 1 40  ? 100.915 112.224 111.645 1.00 27.23  ? 40  VAL A CG1 1 
ATOM 159  C CG2 . VAL A 1 40  ? 103.358 112.388 111.199 1.00 36.41  ? 40  VAL A CG2 1 
ATOM 160  N N   . PHE A 1 41  ? 101.199 113.366 115.221 1.00 32.10  ? 41  PHE A N   1 
ATOM 161  C CA  . PHE A 1 41  ? 100.078 113.427 116.152 1.00 22.67  ? 41  PHE A CA  1 
ATOM 162  C C   . PHE A 1 41  ? 100.243 114.480 117.238 1.00 26.70  ? 41  PHE A C   1 
ATOM 163  O O   . PHE A 1 41  ? 99.240  115.004 117.731 1.00 38.71  ? 41  PHE A O   1 
ATOM 164  C CB  . PHE A 1 41  ? 99.858  112.059 116.806 1.00 27.61  ? 41  PHE A CB  1 
ATOM 165  C CG  . PHE A 1 41  ? 99.463  110.982 115.838 1.00 38.94  ? 41  PHE A CG  1 
ATOM 166  C CD1 . PHE A 1 41  ? 98.231  111.019 115.207 1.00 39.06  ? 41  PHE A CD1 1 
ATOM 167  C CD2 . PHE A 1 41  ? 100.323 109.937 115.552 1.00 28.80  ? 41  PHE A CD2 1 
ATOM 168  C CE1 . PHE A 1 41  ? 97.863  110.033 114.315 1.00 24.58  ? 41  PHE A CE1 1 
ATOM 169  C CE2 . PHE A 1 41  ? 99.960  108.949 114.661 1.00 32.64  ? 41  PHE A CE2 1 
ATOM 170  C CZ  . PHE A 1 41  ? 98.728  108.997 114.042 1.00 34.45  ? 41  PHE A CZ  1 
ATOM 171  N N   . LEU A 1 42  ? 101.476 114.799 117.626 1.00 28.26  ? 42  LEU A N   1 
ATOM 172  C CA  . LEU A 1 42  ? 101.710 115.799 118.660 1.00 28.45  ? 42  LEU A CA  1 
ATOM 173  C C   . LEU A 1 42  ? 101.630 117.227 118.136 1.00 29.59  ? 42  LEU A C   1 
ATOM 174  O O   . LEU A 1 42  ? 101.482 118.155 118.937 1.00 26.85  ? 42  LEU A O   1 
ATOM 175  C CB  . LEU A 1 42  ? 103.080 115.575 119.306 1.00 28.18  ? 42  LEU A CB  1 
ATOM 176  C CG  . LEU A 1 42  ? 103.310 114.261 120.055 1.00 36.04  ? 42  LEU A CG  1 
ATOM 177  C CD1 . LEU A 1 42  ? 104.784 114.087 120.376 1.00 30.93  ? 42  LEU A CD1 1 
ATOM 178  C CD2 . LEU A 1 42  ? 102.479 114.204 121.324 1.00 32.46  ? 42  LEU A CD2 1 
ATOM 179  N N   . GLY A 1 43  ? 101.723 117.428 116.823 1.00 30.26  ? 43  GLY A N   1 
ATOM 180  C CA  . GLY A 1 43  ? 101.794 118.764 116.265 1.00 16.81  ? 43  GLY A CA  1 
ATOM 181  C C   . GLY A 1 43  ? 100.862 119.044 115.101 1.00 22.37  ? 43  GLY A C   1 
ATOM 182  O O   . GLY A 1 43  ? 101.284 119.632 114.102 1.00 30.79  ? 43  GLY A O   1 
ATOM 183  N N   . PHE A 1 44  ? 99.604  118.624 115.205 1.00 29.95  ? 44  PHE A N   1 
ATOM 184  C CA  . PHE A 1 44  ? 98.620  118.920 114.171 1.00 19.18  ? 44  PHE A CA  1 
ATOM 185  C C   . PHE A 1 44  ? 98.125  120.361 114.279 1.00 27.50  ? 44  PHE A C   1 
ATOM 186  O O   . PHE A 1 44  ? 98.061  120.941 115.367 1.00 36.92  ? 44  PHE A O   1 
ATOM 187  C CB  . PHE A 1 44  ? 97.457  117.925 114.248 1.00 18.73  ? 44  PHE A CB  1 
ATOM 188  C CG  . PHE A 1 44  ? 96.645  118.016 115.513 1.00 20.74  ? 44  PHE A CG  1 
ATOM 189  C CD1 . PHE A 1 44  ? 95.625  118.944 115.644 1.00 30.57  ? 44  PHE A CD1 1 
ATOM 190  C CD2 . PHE A 1 44  ? 96.909  117.168 116.574 1.00 15.69  ? 44  PHE A CD2 1 
ATOM 191  C CE1 . PHE A 1 44  ? 94.886  119.022 116.807 1.00 28.43  ? 44  PHE A CE1 1 
ATOM 192  C CE2 . PHE A 1 44  ? 96.173  117.242 117.738 1.00 27.67  ? 44  PHE A CE2 1 
ATOM 193  C CZ  . PHE A 1 44  ? 95.161  118.171 117.854 1.00 32.40  ? 44  PHE A CZ  1 
ATOM 194  N N   . THR A 1 45  ? 97.780  120.941 113.128 1.00 25.46  ? 45  THR A N   1 
ATOM 195  C CA  . THR A 1 45  ? 97.252  122.301 113.053 1.00 17.68  ? 45  THR A CA  1 
ATOM 196  C C   . THR A 1 45  ? 95.763  122.307 112.734 1.00 29.22  ? 45  THR A C   1 
ATOM 197  O O   . THR A 1 45  ? 95.374  121.936 111.616 1.00 38.65  ? 45  THR A O   1 
ATOM 198  C CB  . THR A 1 45  ? 98.015  123.103 111.995 1.00 24.07  ? 45  THR A CB  1 
ATOM 199  O OG1 . THR A 1 45  ? 99.422  123.021 112.249 1.00 29.39  ? 45  THR A OG1 1 
ATOM 200  C CG2 . THR A 1 45  ? 97.588  124.560 112.018 1.00 19.70  ? 45  THR A CG2 1 
ATOM 201  N N   . PRO A 1 46  ? 94.899  122.709 113.660 1.00 31.05  ? 46  PRO A N   1 
ATOM 202  C CA  . PRO A 1 46  ? 93.475  122.854 113.345 1.00 25.25  ? 46  PRO A CA  1 
ATOM 203  C C   . PRO A 1 46  ? 93.169  124.211 112.716 1.00 26.44  ? 46  PRO A C   1 
ATOM 204  O O   . PRO A 1 46  ? 94.017  125.098 112.629 1.00 39.89  ? 46  PRO A O   1 
ATOM 205  C CB  . PRO A 1 46  ? 92.811  122.711 114.715 1.00 26.54  ? 46  PRO A CB  1 
ATOM 206  C CG  . PRO A 1 46  ? 93.806  123.304 115.646 1.00 37.55  ? 46  PRO A CG  1 
ATOM 207  C CD  . PRO A 1 46  ? 95.172  122.972 115.084 1.00 30.39  ? 46  PRO A CD  1 
ATOM 208  N N   . ASP A 1 47  ? 91.922  124.350 112.267 1.00 27.09  ? 47  ASP A N   1 
ATOM 209  C CA  . ASP A 1 47  ? 91.439  125.621 111.736 1.00 25.50  ? 47  ASP A CA  1 
ATOM 210  C C   . ASP A 1 47  ? 91.408  126.692 112.820 1.00 26.73  ? 47  ASP A C   1 
ATOM 211  O O   . ASP A 1 47  ? 91.075  126.418 113.976 1.00 34.82  ? 47  ASP A O   1 
ATOM 212  C CB  . ASP A 1 47  ? 90.045  125.450 111.133 1.00 32.47  ? 47  ASP A CB  1 
ATOM 213  C CG  . ASP A 1 47  ? 90.051  124.592 109.884 1.00 42.45  ? 47  ASP A CG  1 
ATOM 214  O OD1 . ASP A 1 47  ? 91.143  124.351 109.330 1.00 47.96  ? 47  ASP A OD1 1 
ATOM 215  O OD2 . ASP A 1 47  ? 88.961  124.159 109.455 1.00 38.36  ? 47  ASP A OD2 1 
ATOM 216  N N   . HIS A 1 48  ? 91.756  127.923 112.442 1.00 31.15  ? 48  HIS A N   1 
ATOM 217  C CA  . HIS A 1 48  ? 91.920  128.998 113.410 1.00 18.57  ? 48  HIS A CA  1 
ATOM 218  C C   . HIS A 1 48  ? 91.575  130.338 112.770 1.00 22.79  ? 48  HIS A C   1 
ATOM 219  O O   . HIS A 1 48  ? 91.606  130.495 111.548 1.00 33.07  ? 48  HIS A O   1 
ATOM 220  C CB  . HIS A 1 48  ? 93.344  129.022 113.978 1.00 25.75  ? 48  HIS A CB  1 
ATOM 221  C CG  . HIS A 1 48  ? 94.414  129.025 112.932 1.00 24.28  ? 48  HIS A CG  1 
ATOM 222  N ND1 . HIS A 1 48  ? 94.809  127.883 112.269 1.00 19.72  ? 48  HIS A ND1 1 
ATOM 223  C CD2 . HIS A 1 48  ? 95.181  130.027 112.443 1.00 29.76  ? 48  HIS A CD2 1 
ATOM 224  C CE1 . HIS A 1 48  ? 95.767  128.184 111.411 1.00 27.81  ? 48  HIS A CE1 1 
ATOM 225  N NE2 . HIS A 1 48  ? 96.012  129.478 111.497 1.00 29.04  ? 48  HIS A NE2 1 
ATOM 226  N N   . HIS A 1 49  ? 91.235  131.300 113.627 1.00 29.93  ? 49  HIS A N   1 
ATOM 227  C CA  . HIS A 1 49  ? 91.012  132.692 113.252 1.00 30.37  ? 49  HIS A CA  1 
ATOM 228  C C   . HIS A 1 49  ? 91.267  133.551 114.482 1.00 31.27  ? 49  HIS A C   1 
ATOM 229  O O   . HIS A 1 49  ? 91.337  133.041 115.602 1.00 44.63  ? 49  HIS A O   1 
ATOM 230  C CB  . HIS A 1 49  ? 89.602  132.923 112.692 1.00 40.74  ? 49  HIS A CB  1 
ATOM 231  C CG  . HIS A 1 49  ? 88.500  132.522 113.624 1.00 38.81  ? 49  HIS A CG  1 
ATOM 232  N ND1 . HIS A 1 49  ? 88.033  131.229 113.713 1.00 36.90  ? 49  HIS A ND1 1 
ATOM 233  C CD2 . HIS A 1 49  ? 87.763  133.249 114.496 1.00 38.38  ? 49  HIS A CD2 1 
ATOM 234  C CE1 . HIS A 1 49  ? 87.061  131.175 114.605 1.00 38.65  ? 49  HIS A CE1 1 
ATOM 235  N NE2 . HIS A 1 49  ? 86.878  132.387 115.096 1.00 36.44  ? 49  HIS A NE2 1 
ATOM 236  N N   . CYS A 1 50  ? 91.418  134.862 114.276 1.00 38.05  ? 50  CYS A N   1 
ATOM 237  C CA  . CYS A 1 50  ? 91.699  135.732 115.413 1.00 39.07  ? 50  CYS A CA  1 
ATOM 238  C C   . CYS A 1 50  ? 90.534  135.729 116.394 1.00 44.70  ? 50  CYS A C   1 
ATOM 239  O O   . CYS A 1 50  ? 89.365  135.683 116.003 1.00 49.71  ? 50  CYS A O   1 
ATOM 240  C CB  . CYS A 1 50  ? 91.949  137.179 114.970 1.00 45.51  ? 50  CYS A CB  1 
ATOM 241  S SG  . CYS A 1 50  ? 93.142  137.544 113.657 1.00 57.94  ? 50  CYS A SG  1 
ATOM 242  N N   . GLN A 1 51  ? 90.868  135.782 117.680 1.00 55.43  ? 51  GLN A N   1 
ATOM 243  C CA  . GLN A 1 51  ? 89.908  136.151 118.710 1.00 53.04  ? 51  GLN A CA  1 
ATOM 244  C C   . GLN A 1 51  ? 89.581  137.638 118.639 1.00 55.01  ? 51  GLN A C   1 
ATOM 245  O O   . GLN A 1 51  ? 90.455  138.469 118.381 1.00 54.38  ? 51  GLN A O   1 
ATOM 246  C CB  . GLN A 1 51  ? 90.459  135.795 120.089 1.00 49.28  ? 51  GLN A CB  1 
ATOM 247  C CG  . GLN A 1 51  ? 89.499  136.049 121.232 1.00 52.33  ? 51  GLN A CG  1 
ATOM 248  C CD  . GLN A 1 51  ? 90.016  135.514 122.549 1.00 62.04  ? 51  GLN A CD  1 
ATOM 249  O OE1 . GLN A 1 51  ? 90.968  134.734 122.584 1.00 61.59  ? 51  GLN A OE1 1 
ATOM 250  N NE2 . GLN A 1 51  ? 89.393  135.933 123.644 1.00 65.04  ? 51  GLN A NE2 1 
ATOM 251  N N   . SER A 1 52  ? 88.313  137.975 118.874 1.00 68.26  ? 52  SER A N   1 
ATOM 252  C CA  . SER A 1 52  ? 87.894  139.366 118.922 1.00 65.16  ? 52  SER A CA  1 
ATOM 253  C C   . SER A 1 52  ? 86.937  139.564 120.090 1.00 70.12  ? 52  SER A C   1 
ATOM 254  O O   . SER A 1 52  ? 86.038  138.738 120.304 1.00 73.65  ? 52  SER A O   1 
ATOM 255  C CB  . SER A 1 52  ? 87.210  139.800 117.619 1.00 66.01  ? 52  SER A CB  1 
ATOM 256  O OG  . SER A 1 52  ? 88.109  139.756 116.526 1.00 74.14  ? 52  SER A OG  1 
ATOM 257  N N   . PRO A 1 53  ? 87.102  140.640 120.854 1.00 76.76  ? 53  PRO A N   1 
ATOM 258  C CA  . PRO A 1 53  ? 86.103  140.993 121.865 1.00 77.39  ? 53  PRO A CA  1 
ATOM 259  C C   . PRO A 1 53  ? 84.792  141.449 121.241 1.00 80.39  ? 53  PRO A C   1 
ATOM 260  O O   . PRO A 1 53  ? 84.736  141.904 120.096 1.00 81.48  ? 53  PRO A O   1 
ATOM 261  C CB  . PRO A 1 53  ? 86.776  142.129 122.641 1.00 77.18  ? 53  PRO A CB  1 
ATOM 262  C CG  . PRO A 1 53  ? 87.640  142.787 121.622 1.00 75.30  ? 53  PRO A CG  1 
ATOM 263  C CD  . PRO A 1 53  ? 88.161  141.658 120.755 1.00 75.23  ? 53  PRO A CD  1 
ATOM 264  N N   . GLY A 1 54  ? 83.721  141.322 122.023 1.00 82.98  ? 54  GLY A N   1 
ATOM 265  C CA  . GLY A 1 54  ? 82.407  141.753 121.585 1.00 83.32  ? 54  GLY A CA  1 
ATOM 266  C C   . GLY A 1 54  ? 81.713  140.846 120.588 1.00 83.43  ? 54  GLY A C   1 
ATOM 267  O O   . GLY A 1 54  ? 80.480  140.823 120.524 1.00 85.58  ? 54  GLY A O   1 
ATOM 268  N N   . VAL A 1 55  ? 82.490  140.105 119.797 1.00 84.19  ? 55  VAL A N   1 
ATOM 269  C CA  . VAL A 1 55  ? 81.911  139.180 118.826 1.00 83.79  ? 55  VAL A CA  1 
ATOM 270  C C   . VAL A 1 55  ? 81.067  138.118 119.523 1.00 85.60  ? 55  VAL A C   1 
ATOM 271  O O   . VAL A 1 55  ? 79.958  137.803 119.085 1.00 85.58  ? 55  VAL A O   1 
ATOM 272  C CB  . VAL A 1 55  ? 83.016  138.544 117.963 1.00 84.54  ? 55  VAL A CB  1 
ATOM 273  C CG1 . VAL A 1 55  ? 82.452  137.409 117.127 1.00 81.99  ? 55  VAL A CG1 1 
ATOM 274  C CG2 . VAL A 1 55  ? 83.645  139.589 117.067 1.00 87.12  ? 55  VAL A CG2 1 
ATOM 275  N N   . ALA A 1 56  ? 81.591  137.530 120.600 1.00 87.57  ? 56  ALA A N   1 
ATOM 276  C CA  . ALA A 1 56  ? 80.835  136.515 121.333 1.00 87.73  ? 56  ALA A CA  1 
ATOM 277  C C   . ALA A 1 56  ? 79.554  137.075 121.948 1.00 86.81  ? 56  ALA A C   1 
ATOM 278  O O   . ALA A 1 56  ? 78.499  136.433 121.891 1.00 87.61  ? 56  ALA A O   1 
ATOM 279  C CB  . ALA A 1 56  ? 81.716  135.892 122.415 1.00 85.75  ? 56  ALA A CB  1 
ATOM 280  N N   . GLU A 1 57  ? 79.620  138.276 122.528 1.00 86.57  ? 57  GLU A N   1 
ATOM 281  C CA  . GLU A 1 57  ? 78.421  138.914 123.073 1.00 88.81  ? 57  GLU A CA  1 
ATOM 282  C C   . GLU A 1 57  ? 77.388  139.231 121.995 1.00 87.71  ? 57  GLU A C   1 
ATOM 283  O O   . GLU A 1 57  ? 76.190  139.000 122.191 1.00 87.03  ? 57  GLU A O   1 
ATOM 284  C CB  . GLU A 1 57  ? 78.803  140.182 123.840 1.00 89.02  ? 57  GLU A CB  1 
ATOM 285  C CG  . GLU A 1 57  ? 79.559  139.938 125.144 1.00 88.99  ? 57  GLU A CG  1 
ATOM 286  C CD  . GLU A 1 57  ? 80.993  139.488 124.935 1.00 91.16  ? 57  GLU A CD  1 
ATOM 287  O OE1 . GLU A 1 57  ? 81.518  139.664 123.817 1.00 90.67  ? 57  GLU A OE1 1 
ATOM 288  O OE2 . GLU A 1 57  ? 81.595  138.959 125.893 1.00 92.66  ? 57  GLU A OE2 1 
ATOM 289  N N   . LEU A 1 58  ? 77.827  139.772 120.858 1.00 88.61  ? 58  LEU A N   1 
ATOM 290  C CA  . LEU A 1 58  ? 76.910  140.020 119.747 1.00 89.32  ? 58  LEU A CA  1 
ATOM 291  C C   . LEU A 1 58  ? 76.303  138.726 119.212 1.00 89.10  ? 58  LEU A C   1 
ATOM 292  O O   . LEU A 1 58  ? 75.109  138.675 118.904 1.00 88.81  ? 58  LEU A O   1 
ATOM 293  C CB  . LEU A 1 58  ? 77.634  140.776 118.632 1.00 89.64  ? 58  LEU A CB  1 
ATOM 294  C CG  . LEU A 1 58  ? 76.834  141.054 117.359 1.00 89.17  ? 58  LEU A CG  1 
ATOM 295  C CD1 . LEU A 1 58  ? 75.602  141.885 117.675 1.00 89.43  ? 58  LEU A CD1 1 
ATOM 296  C CD2 . LEU A 1 58  ? 77.701  141.756 116.328 1.00 87.78  ? 58  LEU A CD2 1 
ATOM 297  N N   . SER A 1 59  ? 77.120  137.686 119.060 1.00 89.15  ? 59  SER A N   1 
ATOM 298  C CA  . SER A 1 59  ? 76.635  136.376 118.631 1.00 89.13  ? 59  SER A CA  1 
ATOM 299  C C   . SER A 1 59  ? 75.612  135.789 119.598 1.00 91.09  ? 59  SER A C   1 
ATOM 300  O O   . SER A 1 59  ? 74.645  135.148 119.172 1.00 90.03  ? 59  SER A O   1 
ATOM 301  C CB  . SER A 1 59  ? 77.812  135.418 118.466 1.00 90.17  ? 59  SER A CB  1 
ATOM 302  O OG  . SER A 1 59  ? 77.372  134.136 118.055 1.00 90.59  ? 59  SER A OG  1 
ATOM 303  N N   . GLN A 1 60  ? 75.811  135.980 120.901 1.00 98.53  ? 60  GLN A N   1 
ATOM 304  C CA  . GLN A 1 60  ? 74.811  135.548 121.876 1.00 97.72  ? 60  GLN A CA  1 
ATOM 305  C C   . GLN A 1 60  ? 73.531  136.374 121.791 1.00 98.30  ? 60  GLN A C   1 
ATOM 306  O O   . GLN A 1 60  ? 72.425  135.822 121.827 1.00 98.08  ? 60  GLN A O   1 
ATOM 307  C CB  . GLN A 1 60  ? 75.399  135.618 123.285 1.00 95.42  ? 60  GLN A CB  1 
ATOM 308  C CG  . GLN A 1 60  ? 74.458  135.137 124.377 1.00 96.13  ? 60  GLN A CG  1 
ATOM 309  C CD  . GLN A 1 60  ? 75.090  135.190 125.754 1.00 97.56  ? 60  GLN A CD  1 
ATOM 310  O OE1 . GLN A 1 60  ? 76.191  135.713 125.926 1.00 98.68  ? 60  GLN A OE1 1 
ATOM 311  N NE2 . GLN A 1 60  ? 74.393  134.647 126.745 1.00 97.74  ? 60  GLN A NE2 1 
ATOM 312  N N   . ARG A 1 61  ? 73.654  137.698 121.688 1.00 95.67  ? 61  ARG A N   1 
ATOM 313  C CA  . ARG A 1 61  ? 72.470  138.550 121.600 1.00 96.22  ? 61  ARG A CA  1 
ATOM 314  C C   . ARG A 1 61  ? 71.655  138.265 120.340 1.00 96.90  ? 61  ARG A C   1 
ATOM 315  O O   . ARG A 1 61  ? 70.424  138.161 120.395 1.00 97.56  ? 61  ARG A O   1 
ATOM 316  C CB  . ARG A 1 61  ? 72.890  140.020 121.650 1.00 96.45  ? 61  ARG A CB  1 
ATOM 317  C CG  . ARG A 1 61  ? 71.737  141.003 121.761 1.00 96.55  ? 61  ARG A CG  1 
ATOM 318  C CD  . ARG A 1 61  ? 72.240  142.439 121.733 1.00 96.47  ? 61  ARG A CD  1 
ATOM 319  N NE  . ARG A 1 61  ? 72.679  142.841 120.402 1.00 97.20  ? 61  ARG A NE  1 
ATOM 320  C CZ  . ARG A 1 61  ? 72.490  144.045 119.881 1.00 97.62  ? 61  ARG A CZ  1 
ATOM 321  N NH1 . ARG A 1 61  ? 71.882  145.005 120.561 1.00 95.13  ? 61  ARG A NH1 1 
ATOM 322  N NH2 . ARG A 1 61  ? 72.926  144.296 118.651 1.00 98.30  ? 61  ARG A NH2 1 
ATOM 323  N N   . CYS A 1 62  ? 72.322  138.138 119.194 1.00 96.16  ? 62  CYS A N   1 
ATOM 324  C CA  . CYS A 1 62  ? 71.654  137.870 117.925 1.00 96.62  ? 62  CYS A CA  1 
ATOM 325  C C   . CYS A 1 62  ? 71.406  136.387 117.667 1.00 96.86  ? 62  CYS A C   1 
ATOM 326  O O   . CYS A 1 62  ? 70.486  136.050 116.913 1.00 96.16  ? 62  CYS A O   1 
ATOM 327  C CB  . CYS A 1 62  ? 72.481  138.484 116.787 1.00 96.12  ? 62  CYS A CB  1 
ATOM 328  S SG  . CYS A 1 62  ? 71.946  138.174 115.088 1.00 100.96 ? 62  CYS A SG  1 
ATOM 329  N N   . GLY A 1 63  ? 72.188  135.500 118.276 1.00 92.35  ? 63  GLY A N   1 
ATOM 330  C CA  . GLY A 1 63  ? 71.943  134.070 118.182 1.00 89.69  ? 63  GLY A CA  1 
ATOM 331  C C   . GLY A 1 63  ? 72.508  133.373 116.962 1.00 89.89  ? 63  GLY A C   1 
ATOM 332  O O   . GLY A 1 63  ? 71.838  132.509 116.383 1.00 90.58  ? 63  GLY A O   1 
ATOM 333  N N   . TRP A 1 64  ? 73.723  133.726 116.549 1.00 90.61  ? 64  TRP A N   1 
ATOM 334  C CA  . TRP A 1 64  ? 74.329  133.105 115.378 1.00 90.63  ? 64  TRP A CA  1 
ATOM 335  C C   . TRP A 1 64  ? 74.607  131.625 115.620 1.00 90.42  ? 64  TRP A C   1 
ATOM 336  O O   . TRP A 1 64  ? 74.960  131.214 116.729 1.00 90.50  ? 64  TRP A O   1 
ATOM 337  C CB  . TRP A 1 64  ? 75.624  133.822 114.996 1.00 90.26  ? 64  TRP A CB  1 
ATOM 338  C CG  . TRP A 1 64  ? 75.449  135.285 114.743 1.00 89.51  ? 64  TRP A CG  1 
ATOM 339  C CD1 . TRP A 1 64  ? 74.286  135.930 114.450 1.00 89.58  ? 64  TRP A CD1 1 
ATOM 340  C CD2 . TRP A 1 64  ? 76.473  136.285 114.744 1.00 89.68  ? 64  TRP A CD2 1 
ATOM 341  N NE1 . TRP A 1 64  ? 74.517  137.272 114.279 1.00 89.65  ? 64  TRP A NE1 1 
ATOM 342  C CE2 . TRP A 1 64  ? 75.854  137.516 114.452 1.00 90.69  ? 64  TRP A CE2 1 
ATOM 343  C CE3 . TRP A 1 64  ? 77.853  136.260 114.966 1.00 90.05  ? 64  TRP A CE3 1 
ATOM 344  C CZ2 . TRP A 1 64  ? 76.566  138.711 114.377 1.00 89.47  ? 64  TRP A CZ2 1 
ATOM 345  C CZ3 . TRP A 1 64  ? 78.558  137.447 114.892 1.00 92.58  ? 64  TRP A CZ3 1 
ATOM 346  C CH2 . TRP A 1 64  ? 77.914  138.655 114.599 1.00 91.91  ? 64  TRP A CH2 1 
ATOM 347  N N   . SER A 1 65  ? 74.440  130.822 114.573 1.00 93.00  ? 65  SER A N   1 
ATOM 348  C CA  . SER A 1 65  ? 74.913  129.448 114.581 1.00 93.56  ? 65  SER A CA  1 
ATOM 349  C C   . SER A 1 65  ? 76.412  129.414 114.286 1.00 95.36  ? 65  SER A C   1 
ATOM 350  O O   . SER A 1 65  ? 76.969  130.379 113.757 1.00 95.46  ? 65  SER A O   1 
ATOM 351  C CB  . SER A 1 65  ? 74.135  128.623 113.558 1.00 92.92  ? 65  SER A CB  1 
ATOM 352  O OG  . SER A 1 65  ? 74.298  129.133 112.249 1.00 92.96  ? 65  SER A OG  1 
ATOM 353  N N   . PRO A 1 66  ? 77.097  128.313 114.626 1.00 91.41  ? 66  PRO A N   1 
ATOM 354  C CA  . PRO A 1 66  ? 78.572  128.343 114.598 1.00 90.30  ? 66  PRO A CA  1 
ATOM 355  C C   . PRO A 1 66  ? 79.166  128.582 113.218 1.00 90.16  ? 66  PRO A C   1 
ATOM 356  O O   . PRO A 1 66  ? 80.197  129.256 113.105 1.00 88.91  ? 66  PRO A O   1 
ATOM 357  C CB  . PRO A 1 66  ? 78.957  126.961 115.148 1.00 91.12  ? 66  PRO A CB  1 
ATOM 358  C CG  . PRO A 1 66  ? 77.808  126.571 116.003 1.00 92.67  ? 66  PRO A CG  1 
ATOM 359  C CD  . PRO A 1 66  ? 76.600  127.085 115.269 1.00 90.71  ? 66  PRO A CD  1 
ATOM 360  N N   . ALA A 1 67  ? 78.552  128.045 112.163 1.00 90.41  ? 67  ALA A N   1 
ATOM 361  C CA  . ALA A 1 67  ? 79.017  128.300 110.804 1.00 89.98  ? 67  ALA A CA  1 
ATOM 362  C C   . ALA A 1 67  ? 78.561  129.650 110.266 1.00 88.41  ? 67  ALA A C   1 
ATOM 363  O O   . ALA A 1 67  ? 79.191  130.181 109.345 1.00 87.93  ? 67  ALA A O   1 
ATOM 364  C CB  . ALA A 1 67  ? 78.541  127.188 109.867 1.00 89.83  ? 67  ALA A CB  1 
ATOM 365  N N   . GLU A 1 68  ? 77.481  130.204 110.812 1.00 86.98  ? 68  GLU A N   1 
ATOM 366  C CA  . GLU A 1 68  ? 76.974  131.507 110.396 1.00 87.56  ? 68  GLU A CA  1 
ATOM 367  C C   . GLU A 1 68  ? 77.795  132.650 110.991 1.00 88.47  ? 68  GLU A C   1 
ATOM 368  O O   . GLU A 1 68  ? 77.958  133.701 110.357 1.00 88.91  ? 68  GLU A O   1 
ATOM 369  C CB  . GLU A 1 68  ? 75.500  131.617 110.786 1.00 87.97  ? 68  GLU A CB  1 
ATOM 370  C CG  . GLU A 1 68  ? 74.871  132.972 110.597 1.00 88.80  ? 68  GLU A CG  1 
ATOM 371  C CD  . GLU A 1 68  ? 73.407  132.979 110.992 1.00 91.25  ? 68  GLU A CD  1 
ATOM 372  O OE1 . GLU A 1 68  ? 73.017  132.149 111.840 1.00 91.22  ? 68  GLU A OE1 1 
ATOM 373  O OE2 . GLU A 1 68  ? 72.642  133.804 110.449 1.00 90.03  ? 68  GLU A OE2 1 
ATOM 374  N N   . GLU A 1 69  ? 78.275  132.475 112.225 1.00 82.92  ? 69  GLU A N   1 
ATOM 375  C CA  . GLU A 1 69  ? 79.175  133.447 112.841 1.00 80.78  ? 69  GLU A CA  1 
ATOM 376  C C   . GLU A 1 69  ? 80.414  133.697 111.988 1.00 78.69  ? 69  GLU A C   1 
ATOM 377  O O   . GLU A 1 69  ? 80.845  134.847 111.825 1.00 84.08  ? 69  GLU A O   1 
ATOM 378  C CB  . GLU A 1 69  ? 79.584  132.953 114.228 1.00 81.27  ? 69  GLU A CB  1 
ATOM 379  C CG  . GLU A 1 69  ? 80.722  133.725 114.865 1.00 81.83  ? 69  GLU A CG  1 
ATOM 380  C CD  . GLU A 1 69  ? 80.913  133.369 116.325 1.00 82.75  ? 69  GLU A CD  1 
ATOM 381  O OE1 . GLU A 1 69  ? 79.989  133.614 117.125 1.00 83.09  ? 69  GLU A OE1 1 
ATOM 382  O OE2 . GLU A 1 69  ? 81.988  132.837 116.671 1.00 81.72  ? 69  GLU A OE2 1 
ATOM 383  N N   . LEU A 1 70  ? 80.972  132.642 111.391 1.00 72.35  ? 70  LEU A N   1 
ATOM 384  C CA  . LEU A 1 70  ? 82.079  132.831 110.459 1.00 72.55  ? 70  LEU A CA  1 
ATOM 385  C C   . LEU A 1 70  ? 81.642  133.663 109.263 1.00 75.26  ? 70  LEU A C   1 
ATOM 386  O O   . LEU A 1 70  ? 82.324  134.620 108.879 1.00 79.55  ? 70  LEU A O   1 
ATOM 387  C CB  . LEU A 1 70  ? 82.623  131.477 110.003 1.00 72.49  ? 70  LEU A CB  1 
ATOM 388  C CG  . LEU A 1 70  ? 83.116  130.523 111.090 1.00 71.91  ? 70  LEU A CG  1 
ATOM 389  C CD1 . LEU A 1 70  ? 83.733  129.286 110.463 1.00 74.99  ? 70  LEU A CD1 1 
ATOM 390  C CD2 . LEU A 1 70  ? 84.109  131.212 112.004 1.00 73.71  ? 70  LEU A CD2 1 
ATOM 391  N N   . ASN A 1 71  ? 80.518  133.300 108.644 1.00 84.21  ? 71  ASN A N   1 
ATOM 392  C CA  . ASN A 1 71  ? 80.089  133.994 107.435 1.00 84.70  ? 71  ASN A CA  1 
ATOM 393  C C   . ASN A 1 71  ? 79.866  135.479 107.704 1.00 81.92  ? 71  ASN A C   1 
ATOM 394  O O   . ASN A 1 71  ? 80.155  136.322 106.848 1.00 81.76  ? 71  ASN A O   1 
ATOM 395  C CB  . ASN A 1 71  ? 78.817  133.348 106.885 1.00 85.08  ? 71  ASN A CB  1 
ATOM 396  C CG  . ASN A 1 71  ? 78.405  133.919 105.543 1.00 87.69  ? 71  ASN A CG  1 
ATOM 397  O OD1 . ASN A 1 71  ? 77.623  134.867 105.472 1.00 87.40  ? 71  ASN A OD1 1 
ATOM 398  N ND2 . ASN A 1 71  ? 78.928  133.341 104.467 1.00 86.56  ? 71  ASN A ND2 1 
ATOM 399  N N   . TYR A 1 72  ? 79.352  135.818 108.890 1.00 77.68  ? 72  TYR A N   1 
ATOM 400  C CA  . TYR A 1 72  ? 79.176  137.223 109.251 1.00 80.77  ? 72  TYR A CA  1 
ATOM 401  C C   . TYR A 1 72  ? 80.440  137.917 109.746 1.00 80.85  ? 72  TYR A C   1 
ATOM 402  O O   . TYR A 1 72  ? 80.458  139.151 109.785 1.00 81.82  ? 72  TYR A O   1 
ATOM 403  C CB  . TYR A 1 72  ? 78.079  137.407 110.304 1.00 81.14  ? 72  TYR A CB  1 
ATOM 404  C CG  . TYR A 1 72  ? 76.697  136.994 109.862 1.00 83.92  ? 72  TYR A CG  1 
ATOM 405  C CD1 . TYR A 1 72  ? 76.340  137.024 108.522 1.00 84.36  ? 72  TYR A CD1 1 
ATOM 406  C CD2 . TYR A 1 72  ? 75.731  136.635 110.789 1.00 84.03  ? 72  TYR A CD2 1 
ATOM 407  C CE1 . TYR A 1 72  ? 75.059  136.713 108.118 1.00 83.96  ? 72  TYR A CE1 1 
ATOM 408  C CE2 . TYR A 1 72  ? 74.456  136.292 110.392 1.00 84.08  ? 72  TYR A CE2 1 
ATOM 409  C CZ  . TYR A 1 72  ? 74.123  136.337 109.055 1.00 85.05  ? 72  TYR A CZ  1 
ATOM 410  O OH  . TYR A 1 72  ? 72.867  135.950 108.650 1.00 85.63  ? 72  TYR A OH  1 
ATOM 411  N N   . THR A 1 73  ? 81.494  137.192 110.122 1.00 72.72  ? 73  THR A N   1 
ATOM 412  C CA  . THR A 1 73  ? 82.458  137.816 111.025 1.00 68.67  ? 73  THR A CA  1 
ATOM 413  C C   . THR A 1 73  ? 83.903  137.678 110.554 1.00 67.67  ? 73  THR A C   1 
ATOM 414  O O   . THR A 1 73  ? 84.714  138.580 110.783 1.00 69.48  ? 73  THR A O   1 
ATOM 415  C CB  . THR A 1 73  ? 82.312  137.233 112.433 1.00 70.14  ? 73  THR A CB  1 
ATOM 416  O OG1 . THR A 1 73  ? 80.930  137.238 112.810 1.00 75.27  ? 73  THR A OG1 1 
ATOM 417  C CG2 . THR A 1 73  ? 83.093  138.058 113.437 1.00 71.74  ? 73  THR A CG2 1 
ATOM 418  N N   . VAL A 1 74  ? 84.241  136.583 109.892 1.00 57.23  ? 74  VAL A N   1 
ATOM 419  C CA  . VAL A 1 74  ? 85.624  136.272 109.538 1.00 56.05  ? 74  VAL A CA  1 
ATOM 420  C C   . VAL A 1 74  ? 85.835  136.638 108.073 1.00 59.61  ? 74  VAL A C   1 
ATOM 421  O O   . VAL A 1 74  ? 84.968  136.328 107.243 1.00 59.18  ? 74  VAL A O   1 
ATOM 422  C CB  . VAL A 1 74  ? 85.949  134.787 109.788 1.00 54.85  ? 74  VAL A CB  1 
ATOM 423  C CG1 . VAL A 1 74  ? 87.375  134.468 109.381 1.00 51.34  ? 74  VAL A CG1 1 
ATOM 424  C CG2 . VAL A 1 74  ? 85.729  134.443 111.249 1.00 53.87  ? 74  VAL A CG2 1 
ATOM 425  N N   . PRO A 1 75  ? 86.933  137.312 107.723 1.00 65.84  ? 75  PRO A N   1 
ATOM 426  C CA  . PRO A 1 75  ? 87.164  137.692 106.324 1.00 60.23  ? 75  PRO A CA  1 
ATOM 427  C C   . PRO A 1 75  ? 87.108  136.498 105.380 1.00 65.62  ? 75  PRO A C   1 
ATOM 428  O O   . PRO A 1 75  ? 87.653  135.429 105.660 1.00 71.86  ? 75  PRO A O   1 
ATOM 429  C CB  . PRO A 1 75  ? 88.559  138.325 106.357 1.00 56.36  ? 75  PRO A CB  1 
ATOM 430  C CG  . PRO A 1 75  ? 88.682  138.859 107.736 1.00 58.57  ? 75  PRO A CG  1 
ATOM 431  C CD  . PRO A 1 75  ? 87.967  137.865 108.613 1.00 63.24  ? 75  PRO A CD  1 
ATOM 432  N N   . GLY A 1 76  ? 86.436  136.697 104.248 1.00 72.04  ? 76  GLY A N   1 
ATOM 433  C CA  . GLY A 1 76  ? 86.200  135.611 103.321 1.00 73.38  ? 76  GLY A CA  1 
ATOM 434  C C   . GLY A 1 76  ? 87.455  135.162 102.599 1.00 72.67  ? 76  GLY A C   1 
ATOM 435  O O   . GLY A 1 76  ? 88.469  135.858 102.542 1.00 74.86  ? 76  GLY A O   1 
ATOM 436  N N   . LEU A 1 77  ? 87.367  133.953 102.038 1.00 83.01  ? 77  LEU A N   1 
ATOM 437  C CA  . LEU A 1 77  ? 88.486  133.380 101.294 1.00 85.29  ? 77  LEU A CA  1 
ATOM 438  C C   . LEU A 1 77  ? 88.825  134.218 100.067 1.00 86.69  ? 77  LEU A C   1 
ATOM 439  O O   . LEU A 1 77  ? 89.993  134.541 99.825  1.00 86.43  ? 77  LEU A O   1 
ATOM 440  C CB  . LEU A 1 77  ? 88.159  131.942 100.888 1.00 84.45  ? 77  LEU A CB  1 
ATOM 441  C CG  . LEU A 1 77  ? 88.004  130.917 102.011 1.00 85.56  ? 77  LEU A CG  1 
ATOM 442  C CD1 . LEU A 1 77  ? 87.649  129.553 101.441 1.00 86.11  ? 77  LEU A CD1 1 
ATOM 443  C CD2 . LEU A 1 77  ? 89.275  130.836 102.840 1.00 87.87  ? 77  LEU A CD2 1 
ATOM 444  N N   . GLY A 1 78  ? 87.815  134.578 99.280  1.00 93.34  ? 78  GLY A N   1 
ATOM 445  C CA  . GLY A 1 78  ? 88.029  135.263 98.029  1.00 93.71  ? 78  GLY A CA  1 
ATOM 446  C C   . GLY A 1 78  ? 88.725  134.393 97.001  1.00 95.51  ? 78  GLY A C   1 
ATOM 447  O O   . GLY A 1 78  ? 88.725  133.162 97.096  1.00 95.57  ? 78  GLY A O   1 
ATOM 448  N N   . PRO A 1 79  ? 89.331  135.019 95.995  1.00 97.16  ? 79  PRO A N   1 
ATOM 449  C CA  . PRO A 1 79  ? 89.948  134.241 94.915  1.00 96.10  ? 79  PRO A CA  1 
ATOM 450  C C   . PRO A 1 79  ? 91.218  133.536 95.363  1.00 94.03  ? 79  PRO A C   1 
ATOM 451  O O   . PRO A 1 79  ? 91.923  133.982 96.270  1.00 93.60  ? 79  PRO A O   1 
ATOM 452  C CB  . PRO A 1 79  ? 90.252  135.298 93.847  1.00 94.60  ? 79  PRO A CB  1 
ATOM 453  C CG  . PRO A 1 79  ? 90.389  136.571 94.613  1.00 94.66  ? 79  PRO A CG  1 
ATOM 454  C CD  . PRO A 1 79  ? 89.430  136.471 95.764  1.00 93.00  ? 79  PRO A CD  1 
ATOM 455  N N   . ALA A 1 80  ? 91.493  132.409 94.703  1.00 91.55  ? 80  ALA A N   1 
ATOM 456  C CA  . ALA A 1 80  ? 92.711  131.619 94.897  1.00 92.11  ? 80  ALA A CA  1 
ATOM 457  C C   . ALA A 1 80  ? 92.874  131.144 96.340  1.00 93.33  ? 80  ALA A C   1 
ATOM 458  O O   . ALA A 1 80  ? 93.995  130.941 96.814  1.00 95.60  ? 80  ALA A O   1 
ATOM 459  C CB  . ALA A 1 80  ? 93.953  132.396 94.450  1.00 93.43  ? 80  ALA A CB  1 
ATOM 460  N N   . GLY A 1 81  ? 91.765  130.964 97.051  1.00 89.56  ? 81  GLY A N   1 
ATOM 461  C CA  . GLY A 1 81  ? 91.817  130.489 98.420  1.00 90.00  ? 81  GLY A CA  1 
ATOM 462  C C   . GLY A 1 81  ? 92.200  131.542 99.440  1.00 89.57  ? 81  GLY A C   1 
ATOM 463  O O   . GLY A 1 81  ? 91.360  131.997 100.223 1.00 87.47  ? 81  GLY A O   1 
ATOM 464  N N   . GLU A 1 82  ? 93.475  131.941 99.415  1.00 84.81  ? 82  GLU A N   1 
ATOM 465  C CA  . GLU A 1 82  ? 94.019  133.059 100.182 1.00 84.08  ? 82  GLU A CA  1 
ATOM 466  C C   . GLU A 1 82  ? 93.533  133.090 101.627 1.00 84.85  ? 82  GLU A C   1 
ATOM 467  O O   . GLU A 1 82  ? 93.173  134.154 102.142 1.00 84.90  ? 82  GLU A O   1 
ATOM 468  C CB  . GLU A 1 82  ? 93.691  134.386 99.493  1.00 84.92  ? 82  GLU A CB  1 
ATOM 469  C CG  . GLU A 1 82  ? 94.345  134.566 98.126  1.00 85.67  ? 82  GLU A CG  1 
ATOM 470  C CD  . GLU A 1 82  ? 95.809  134.973 98.200  1.00 88.66  ? 82  GLU A CD  1 
ATOM 471  O OE1 . GLU A 1 82  ? 96.507  134.577 99.157  1.00 88.19  ? 82  GLU A OE1 1 
ATOM 472  O OE2 . GLU A 1 82  ? 96.265  135.697 97.289  1.00 87.76  ? 82  GLU A OE2 1 
ATOM 473  N N   . ALA A 1 83  ? 93.510  131.925 102.282 1.00 71.69  ? 83  ALA A N   1 
ATOM 474  C CA  . ALA A 1 83  ? 92.948  131.811 103.625 1.00 71.01  ? 83  ALA A CA  1 
ATOM 475  C C   . ALA A 1 83  ? 93.655  132.706 104.636 1.00 71.71  ? 83  ALA A C   1 
ATOM 476  O O   . ALA A 1 83  ? 93.115  132.940 105.722 1.00 71.79  ? 83  ALA A O   1 
ATOM 477  C CB  . ALA A 1 83  ? 93.002  130.357 104.094 1.00 65.42  ? 83  ALA A CB  1 
ATOM 478  N N   . PHE A 1 84  ? 94.853  133.192 104.306 1.00 61.55  ? 84  PHE A N   1 
ATOM 479  C CA  . PHE A 1 84  ? 95.602  134.160 105.101 1.00 55.72  ? 84  PHE A CA  1 
ATOM 480  C C   . PHE A 1 84  ? 94.757  135.293 105.673 1.00 55.97  ? 84  PHE A C   1 
ATOM 481  O O   . PHE A 1 84  ? 94.914  135.650 106.845 1.00 64.26  ? 84  PHE A O   1 
ATOM 482  C CB  . PHE A 1 84  ? 96.737  134.743 104.254 1.00 61.27  ? 84  PHE A CB  1 
ATOM 483  C CG  . PHE A 1 84  ? 97.363  135.976 104.839 1.00 63.83  ? 84  PHE A CG  1 
ATOM 484  C CD1 . PHE A 1 84  ? 98.216  135.887 105.926 1.00 62.98  ? 84  PHE A CD1 1 
ATOM 485  C CD2 . PHE A 1 84  ? 97.107  137.223 104.296 1.00 61.91  ? 84  PHE A CD2 1 
ATOM 486  C CE1 . PHE A 1 84  ? 98.794  137.020 106.464 1.00 61.80  ? 84  PHE A CE1 1 
ATOM 487  C CE2 . PHE A 1 84  ? 97.681  138.359 104.830 1.00 61.37  ? 84  PHE A CE2 1 
ATOM 488  C CZ  . PHE A 1 84  ? 98.527  138.257 105.915 1.00 60.78  ? 84  PHE A CZ  1 
ATOM 489  N N   . LEU A 1 85  ? 93.866  135.872 104.867 1.00 51.60  ? 85  LEU A N   1 
ATOM 490  C CA  . LEU A 1 85  ? 93.071  136.999 105.349 1.00 54.57  ? 85  LEU A CA  1 
ATOM 491  C C   . LEU A 1 85  ? 92.097  136.596 106.450 1.00 57.47  ? 85  LEU A C   1 
ATOM 492  O O   . LEU A 1 85  ? 91.732  137.432 107.283 1.00 62.85  ? 85  LEU A O   1 
ATOM 493  C CB  . LEU A 1 85  ? 92.316  137.644 104.188 1.00 60.77  ? 85  LEU A CB  1 
ATOM 494  C CG  . LEU A 1 85  ? 93.176  138.312 103.116 1.00 60.05  ? 85  LEU A CG  1 
ATOM 495  C CD1 . LEU A 1 85  ? 92.303  138.924 102.036 1.00 57.61  ? 85  LEU A CD1 1 
ATOM 496  C CD2 . LEU A 1 85  ? 94.079  139.364 103.735 1.00 57.08  ? 85  LEU A CD2 1 
ATOM 497  N N   . GLY A 1 86  ? 91.664  135.340 106.474 1.00 51.93  ? 86  GLY A N   1 
ATOM 498  C CA  . GLY A 1 86  ? 90.869  134.836 107.577 1.00 47.74  ? 86  GLY A CA  1 
ATOM 499  C C   . GLY A 1 86  ? 91.667  134.323 108.758 1.00 49.42  ? 86  GLY A C   1 
ATOM 500  O O   . GLY A 1 86  ? 91.272  134.505 109.913 1.00 48.40  ? 86  GLY A O   1 
ATOM 501  N N   . GLN A 1 87  ? 92.798  133.679 108.474 1.00 51.27  ? 87  GLN A N   1 
ATOM 502  C CA  . GLN A 1 87  ? 93.611  133.055 109.512 1.00 43.09  ? 87  GLN A CA  1 
ATOM 503  C C   . GLN A 1 87  ? 94.420  134.056 110.328 1.00 45.69  ? 87  GLN A C   1 
ATOM 504  O O   . GLN A 1 87  ? 94.627  133.838 111.526 1.00 49.69  ? 87  GLN A O   1 
ATOM 505  C CB  . GLN A 1 87  ? 94.550  132.026 108.884 1.00 37.33  ? 87  GLN A CB  1 
ATOM 506  C CG  . GLN A 1 87  ? 93.845  130.791 108.361 1.00 45.85  ? 87  GLN A CG  1 
ATOM 507  C CD  . GLN A 1 87  ? 94.805  129.766 107.798 1.00 51.23  ? 87  GLN A CD  1 
ATOM 508  O OE1 . GLN A 1 87  ? 95.955  130.078 107.496 1.00 47.64  ? 87  GLN A OE1 1 
ATOM 509  N NE2 . GLN A 1 87  ? 94.337  128.533 107.655 1.00 51.92  ? 87  GLN A NE2 1 
ATOM 510  N N   . CYS A 1 88  ? 94.886  135.148 109.718 1.00 40.86  ? 88  CYS A N   1 
ATOM 511  C CA  . CYS A 1 88  ? 95.879  136.010 110.347 1.00 34.00  ? 88  CYS A CA  1 
ATOM 512  C C   . CYS A 1 88  ? 95.481  137.485 110.378 1.00 41.68  ? 88  CYS A C   1 
ATOM 513  O O   . CYS A 1 88  ? 96.313  138.323 110.741 1.00 59.42  ? 88  CYS A O   1 
ATOM 514  C CB  . CYS A 1 88  ? 97.248  135.842 109.669 1.00 44.16  ? 88  CYS A CB  1 
ATOM 515  S SG  . CYS A 1 88  ? 97.928  134.138 109.725 1.00 73.65  ? 88  CYS A SG  1 
ATOM 516  N N   . ARG A 1 89  ? 94.243  137.831 110.017 1.00 42.88  ? 89  ARG A N   1 
ATOM 517  C CA  . ARG A 1 89  ? 93.784  139.216 110.056 1.00 42.14  ? 89  ARG A CA  1 
ATOM 518  C C   . ARG A 1 89  ? 92.360  139.272 110.593 1.00 43.89  ? 89  ARG A C   1 
ATOM 519  O O   . ARG A 1 89  ? 91.653  138.263 110.641 1.00 60.86  ? 89  ARG A O   1 
ATOM 520  C CB  . ARG A 1 89  ? 93.830  139.875 108.670 1.00 52.26  ? 89  ARG A CB  1 
ATOM 521  C CG  . ARG A 1 89  ? 95.222  140.107 108.105 1.00 55.48  ? 89  ARG A CG  1 
ATOM 522  C CD  . ARG A 1 89  ? 95.991  141.131 108.921 1.00 53.76  ? 89  ARG A CD  1 
ATOM 523  N NE  . ARG A 1 89  ? 97.327  141.359 108.387 1.00 54.34  ? 89  ARG A NE  1 
ATOM 524  C CZ  . ARG A 1 89  ? 98.400  140.659 108.728 1.00 57.65  ? 89  ARG A CZ  1 
ATOM 525  N NH1 . ARG A 1 89  ? 98.322  139.635 109.560 1.00 57.09  ? 89  ARG A NH1 1 
ATOM 526  N NH2 . ARG A 1 89  ? 99.579  140.983 108.204 1.00 60.67  ? 89  ARG A NH2 1 
ATOM 527  N N   . ARG A 1 90  ? 91.945  140.472 111.006 1.00 46.25  ? 90  ARG A N   1 
ATOM 528  C CA  . ARG A 1 90  ? 90.581  140.706 111.463 1.00 56.13  ? 90  ARG A CA  1 
ATOM 529  C C   . ARG A 1 90  ? 90.122  142.114 111.104 1.00 54.03  ? 90  ARG A C   1 
ATOM 530  O O   . ARG A 1 90  ? 90.935  143.027 110.949 1.00 60.12  ? 90  ARG A O   1 
ATOM 531  C CB  . ARG A 1 90  ? 90.473  140.505 112.978 1.00 57.00  ? 90  ARG A CB  1 
ATOM 532  C CG  . ARG A 1 90  ? 91.294  141.503 113.774 1.00 54.03  ? 90  ARG A CG  1 
ATOM 533  C CD  . ARG A 1 90  ? 91.218  141.247 115.265 1.00 55.44  ? 90  ARG A CD  1 
ATOM 534  N NE  . ARG A 1 90  ? 91.883  142.302 116.020 1.00 60.65  ? 90  ARG A NE  1 
ATOM 535  C CZ  . ARG A 1 90  ? 91.857  142.410 117.341 1.00 61.02  ? 90  ARG A CZ  1 
ATOM 536  N NH1 . ARG A 1 90  ? 91.334  141.464 118.102 1.00 62.10  ? 90  ARG A NH1 1 
ATOM 537  N NH2 . ARG A 1 90  ? 92.411  143.474 117.915 1.00 58.66  ? 90  ARG A NH2 1 
ATOM 538  N N   . TYR A 1 91  ? 88.804  142.276 110.972 1.00 68.09  ? 91  TYR A N   1 
ATOM 539  C CA  . TYR A 1 91  ? 88.219  143.591 110.730 1.00 68.94  ? 91  TYR A CA  1 
ATOM 540  C C   . TYR A 1 91  ? 88.309  144.458 111.980 1.00 71.37  ? 91  TYR A C   1 
ATOM 541  O O   . TYR A 1 91  ? 87.942  144.026 113.076 1.00 72.64  ? 91  TYR A O   1 
ATOM 542  C CB  . TYR A 1 91  ? 86.755  143.471 110.305 1.00 69.98  ? 91  TYR A CB  1 
ATOM 543  C CG  . TYR A 1 91  ? 86.510  142.746 109.003 1.00 73.03  ? 91  TYR A CG  1 
ATOM 544  C CD1 . TYR A 1 91  ? 86.999  143.245 107.804 1.00 71.59  ? 91  TYR A CD1 1 
ATOM 545  C CD2 . TYR A 1 91  ? 85.767  141.575 108.970 1.00 71.31  ? 91  TYR A CD2 1 
ATOM 546  C CE1 . TYR A 1 91  ? 86.760  142.593 106.611 1.00 71.70  ? 91  TYR A CE1 1 
ATOM 547  C CE2 . TYR A 1 91  ? 85.531  140.913 107.784 1.00 69.02  ? 91  TYR A CE2 1 
ATOM 548  C CZ  . TYR A 1 91  ? 86.027  141.427 106.608 1.00 69.08  ? 91  TYR A CZ  1 
ATOM 549  O OH  . TYR A 1 91  ? 85.799  140.762 105.427 1.00 71.20  ? 91  TYR A OH  1 
ATOM 550  N N   . GLU A 1 92  ? 88.791  145.690 111.810 1.00 81.53  ? 92  GLU A N   1 
ATOM 551  C CA  . GLU A 1 92  ? 88.819  146.685 112.885 1.00 81.23  ? 92  GLU A CA  1 
ATOM 552  C C   . GLU A 1 92  ? 87.458  147.378 112.986 1.00 82.77  ? 92  GLU A C   1 
ATOM 553  O O   . GLU A 1 92  ? 87.288  148.554 112.657 1.00 83.37  ? 92  GLU A O   1 
ATOM 554  C CB  . GLU A 1 92  ? 89.940  147.688 112.656 1.00 81.17  ? 92  GLU A CB  1 
ATOM 555  C CG  . GLU A 1 92  ? 91.334  147.100 112.772 1.00 82.40  ? 92  GLU A CG  1 
ATOM 556  C CD  . GLU A 1 92  ? 92.420  148.125 112.516 1.00 84.90  ? 92  GLU A CD  1 
ATOM 557  O OE1 . GLU A 1 92  ? 92.086  149.255 112.103 1.00 84.23  ? 92  GLU A OE1 1 
ATOM 558  O OE2 . GLU A 1 92  ? 93.607  147.801 112.727 1.00 86.37  ? 92  GLU A OE2 1 
ATOM 559  N N   . VAL A 1 93  ? 86.471  146.620 113.457 1.00 86.06  ? 93  VAL A N   1 
ATOM 560  C CA  . VAL A 1 93  ? 85.097  147.095 113.567 1.00 86.28  ? 93  VAL A CA  1 
ATOM 561  C C   . VAL A 1 93  ? 84.679  147.051 115.031 1.00 89.33  ? 93  VAL A C   1 
ATOM 562  O O   . VAL A 1 93  ? 85.087  146.154 115.776 1.00 90.36  ? 93  VAL A O   1 
ATOM 563  C CB  . VAL A 1 93  ? 84.147  146.250 112.690 1.00 89.27  ? 93  VAL A CB  1 
ATOM 564  C CG1 . VAL A 1 93  ? 82.689  146.586 112.968 1.00 89.09  ? 93  VAL A CG1 1 
ATOM 565  C CG2 . VAL A 1 93  ? 84.473  146.447 111.221 1.00 89.76  ? 93  VAL A CG2 1 
ATOM 566  N N   . ASP A 1 94  ? 83.867  148.029 115.439 1.00 92.64  ? 94  ASP A N   1 
ATOM 567  C CA  . ASP A 1 94  ? 83.446  148.189 116.831 1.00 94.14  ? 94  ASP A CA  1 
ATOM 568  C C   . ASP A 1 94  ? 82.236  147.298 117.115 1.00 94.30  ? 94  ASP A C   1 
ATOM 569  O O   . ASP A 1 94  ? 81.084  147.738 117.134 1.00 93.86  ? 94  ASP A O   1 
ATOM 570  C CB  . ASP A 1 94  ? 83.145  149.653 117.128 1.00 95.32  ? 94  ASP A CB  1 
ATOM 571  C CG  . ASP A 1 94  ? 82.944  149.920 118.606 1.00 96.24  ? 94  ASP A CG  1 
ATOM 572  O OD1 . ASP A 1 94  ? 83.211  149.012 119.421 1.00 94.05  ? 94  ASP A OD1 1 
ATOM 573  O OD2 . ASP A 1 94  ? 82.521  151.042 118.955 1.00 95.52  ? 94  ASP A OD2 1 
ATOM 574  N N   . TRP A 1 95  ? 82.512  146.010 117.335 1.00 87.92  ? 95  TRP A N   1 
ATOM 575  C CA  . TRP A 1 95  ? 81.459  145.026 117.571 1.00 88.32  ? 95  TRP A CA  1 
ATOM 576  C C   . TRP A 1 95  ? 80.632  145.320 118.817 1.00 90.60  ? 95  TRP A C   1 
ATOM 577  O O   . TRP A 1 95  ? 79.564  144.722 118.985 1.00 91.01  ? 95  TRP A O   1 
ATOM 578  C CB  . TRP A 1 95  ? 82.053  143.621 117.690 1.00 86.05  ? 95  TRP A CB  1 
ATOM 579  C CG  . TRP A 1 95  ? 82.846  143.181 116.504 1.00 85.31  ? 95  TRP A CG  1 
ATOM 580  C CD1 . TRP A 1 95  ? 84.184  142.930 116.460 1.00 86.08  ? 95  TRP A CD1 1 
ATOM 581  C CD2 . TRP A 1 95  ? 82.344  142.913 115.190 1.00 83.32  ? 95  TRP A CD2 1 
ATOM 582  N NE1 . TRP A 1 95  ? 84.550  142.532 115.199 1.00 83.76  ? 95  TRP A NE1 1 
ATOM 583  C CE2 . TRP A 1 95  ? 83.437  142.514 114.400 1.00 82.08  ? 95  TRP A CE2 1 
ATOM 584  C CE3 . TRP A 1 95  ? 81.077  142.979 114.605 1.00 85.21  ? 95  TRP A CE3 1 
ATOM 585  C CZ2 . TRP A 1 95  ? 83.303  142.181 113.055 1.00 82.68  ? 95  TRP A CZ2 1 
ATOM 586  C CZ3 . TRP A 1 95  ? 80.946  142.649 113.271 1.00 85.21  ? 95  TRP A CZ3 1 
ATOM 587  C CH2 . TRP A 1 95  ? 82.052  142.255 112.511 1.00 84.08  ? 95  TRP A CH2 1 
ATOM 588  N N   . ASN A 1 96  ? 81.094  146.218 119.689 1.00 95.73  ? 96  ASN A N   1 
ATOM 589  C CA  . ASN A 1 96  ? 80.302  146.674 120.825 1.00 96.43  ? 96  ASN A CA  1 
ATOM 590  C C   . ASN A 1 96  ? 79.154  147.594 120.426 1.00 97.50  ? 96  ASN A C   1 
ATOM 591  O O   . ASN A 1 96  ? 78.297  147.881 121.269 1.00 95.56  ? 96  ASN A O   1 
ATOM 592  C CB  . ASN A 1 96  ? 81.213  147.381 121.833 1.00 96.30  ? 96  ASN A CB  1 
ATOM 593  C CG  . ASN A 1 96  ? 80.520  147.664 123.152 1.00 97.09  ? 96  ASN A CG  1 
ATOM 594  O OD1 . ASN A 1 96  ? 79.864  146.792 123.721 1.00 96.58  ? 96  ASN A OD1 1 
ATOM 595  N ND2 . ASN A 1 96  ? 80.662  148.889 123.645 1.00 96.47  ? 96  ASN A ND2 1 
ATOM 596  N N   . GLN A 1 97  ? 79.109  148.058 119.179 1.00 99.47  ? 97  GLN A N   1 
ATOM 597  C CA  . GLN A 1 97  ? 77.990  148.879 118.728 1.00 100.37 ? 97  GLN A CA  1 
ATOM 598  C C   . GLN A 1 97  ? 76.680  148.104 118.824 1.00 101.63 ? 97  GLN A C   1 
ATOM 599  O O   . GLN A 1 97  ? 76.536  147.026 118.240 1.00 101.75 ? 97  GLN A O   1 
ATOM 600  C CB  . GLN A 1 97  ? 78.231  149.345 117.294 1.00 100.77 ? 97  GLN A CB  1 
ATOM 601  C CG  . GLN A 1 97  ? 77.116  150.204 116.722 1.00 100.64 ? 97  GLN A CG  1 
ATOM 602  C CD  . GLN A 1 97  ? 77.457  150.766 115.355 1.00 101.88 ? 97  GLN A CD  1 
ATOM 603  O OE1 . GLN A 1 97  ? 78.531  150.503 114.814 1.00 102.98 ? 97  GLN A OE1 1 
ATOM 604  N NE2 . GLN A 1 97  ? 76.541  151.543 114.789 1.00 101.76 ? 97  GLN A NE2 1 
ATOM 605  N N   . SER A 1 98  ? 75.727  148.667 119.571 1.00 104.11 ? 98  SER A N   1 
ATOM 606  C CA  . SER A 1 98  ? 74.459  147.993 119.837 1.00 103.72 ? 98  SER A CA  1 
ATOM 607  C C   . SER A 1 98  ? 73.545  147.982 118.618 1.00 103.86 ? 98  SER A C   1 
ATOM 608  O O   . SER A 1 98  ? 72.746  147.053 118.452 1.00 102.00 ? 98  SER A O   1 
ATOM 609  C CB  . SER A 1 98  ? 73.752  148.656 121.019 1.00 102.65 ? 98  SER A CB  1 
ATOM 610  O OG  . SER A 1 98  ? 73.491  150.024 120.755 1.00 103.85 ? 98  SER A OG  1 
ATOM 611  N N   . ALA A 1 99  ? 73.647  148.995 117.761 1.00 100.41 ? 99  ALA A N   1 
ATOM 612  C CA  . ALA A 1 99  ? 72.728  149.196 116.647 1.00 100.35 ? 99  ALA A CA  1 
ATOM 613  C C   . ALA A 1 99  ? 73.027  148.320 115.438 1.00 100.78 ? 99  ALA A C   1 
ATOM 614  O O   . ALA A 1 99  ? 72.361  148.479 114.409 1.00 100.65 ? 99  ALA A O   1 
ATOM 615  C CB  . ALA A 1 99  ? 72.735  150.668 116.225 1.00 99.04  ? 99  ALA A CB  1 
ATOM 616  N N   . LEU A 1 100 ? 74.006  147.421 115.520 1.00 98.52  ? 100 LEU A N   1 
ATOM 617  C CA  . LEU A 1 100 ? 74.358  146.601 114.369 1.00 100.54 ? 100 LEU A CA  1 
ATOM 618  C C   . LEU A 1 100 ? 73.181  145.727 113.943 1.00 100.06 ? 100 LEU A C   1 
ATOM 619  O O   . LEU A 1 100 ? 72.387  145.261 114.764 1.00 98.02  ? 100 LEU A O   1 
ATOM 620  C CB  . LEU A 1 100 ? 75.568  145.724 114.689 1.00 98.70  ? 100 LEU A CB  1 
ATOM 621  C CG  . LEU A 1 100 ? 76.891  146.452 114.925 1.00 99.20  ? 100 LEU A CG  1 
ATOM 622  C CD1 . LEU A 1 100 ? 77.965  145.471 115.361 1.00 98.06  ? 100 LEU A CD1 1 
ATOM 623  C CD2 . LEU A 1 100 ? 77.319  147.199 113.673 1.00 98.51  ? 100 LEU A CD2 1 
ATOM 624  N N   . SER A 1 101 ? 73.080  145.515 112.633 1.00 99.83  ? 101 SER A N   1 
ATOM 625  C CA  . SER A 1 101 ? 72.086  144.613 112.062 1.00 98.03  ? 101 SER A CA  1 
ATOM 626  C C   . SER A 1 101 ? 72.365  143.169 112.464 1.00 97.57  ? 101 SER A C   1 
ATOM 627  O O   . SER A 1 101 ? 73.464  142.652 112.237 1.00 98.86  ? 101 SER A O   1 
ATOM 628  C CB  . SER A 1 101 ? 72.068  144.750 110.542 1.00 98.24  ? 101 SER A CB  1 
ATOM 629  O OG  . SER A 1 101 ? 71.202  143.795 109.954 1.00 96.70  ? 101 SER A OG  1 
ATOM 630  N N   . CYS A 1 102 ? 71.364  142.520 113.060 1.00 97.82  ? 102 CYS A N   1 
ATOM 631  C CA  . CYS A 1 102 ? 71.435  141.096 113.367 1.00 97.72  ? 102 CYS A CA  1 
ATOM 632  C C   . CYS A 1 102 ? 71.280  140.229 112.123 1.00 99.45  ? 102 CYS A C   1 
ATOM 633  O O   . CYS A 1 102 ? 71.524  139.020 112.194 1.00 99.63  ? 102 CYS A O   1 
ATOM 634  C CB  . CYS A 1 102 ? 70.367  140.761 114.418 1.00 98.66  ? 102 CYS A CB  1 
ATOM 635  S SG  . CYS A 1 102 ? 70.107  139.021 114.913 1.00 110.26 ? 102 CYS A SG  1 
ATOM 636  N N   . VAL A 1 103 ? 70.908  140.811 110.985 1.00 98.90  ? 103 VAL A N   1 
ATOM 637  C CA  . VAL A 1 103 ? 70.855  140.056 109.737 1.00 99.60  ? 103 VAL A CA  1 
ATOM 638  C C   . VAL A 1 103 ? 72.214  140.026 109.045 1.00 96.67  ? 103 VAL A C   1 
ATOM 639  O O   . VAL A 1 103 ? 72.653  138.972 108.580 1.00 95.18  ? 103 VAL A O   1 
ATOM 640  C CB  . VAL A 1 103 ? 69.766  140.639 108.815 1.00 97.38  ? 103 VAL A CB  1 
ATOM 641  C CG1 . VAL A 1 103 ? 69.720  139.878 107.500 1.00 95.37  ? 103 VAL A CG1 1 
ATOM 642  C CG2 . VAL A 1 103 ? 68.412  140.600 109.506 1.00 96.35  ? 103 VAL A CG2 1 
ATOM 643  N N   . ASP A 1 104 ? 72.903  141.169 108.969 1.00 91.54  ? 104 ASP A N   1 
ATOM 644  C CA  . ASP A 1 104 ? 74.242  141.217 108.390 1.00 92.77  ? 104 ASP A CA  1 
ATOM 645  C C   . ASP A 1 104 ? 74.957  142.476 108.871 1.00 93.93  ? 104 ASP A C   1 
ATOM 646  O O   . ASP A 1 104 ? 74.854  143.533 108.235 1.00 93.84  ? 104 ASP A O   1 
ATOM 647  C CB  . ASP A 1 104 ? 74.170  141.182 106.861 1.00 93.13  ? 104 ASP A CB  1 
ATOM 648  C CG  . ASP A 1 104 ? 75.540  141.104 106.205 1.00 93.16  ? 104 ASP A CG  1 
ATOM 649  O OD1 . ASP A 1 104 ? 76.560  141.078 106.925 1.00 93.55  ? 104 ASP A OD1 1 
ATOM 650  O OD2 . ASP A 1 104 ? 75.595  141.066 104.958 1.00 91.01  ? 104 ASP A OD2 1 
ATOM 651  N N   . PRO A 1 105 ? 75.685  142.401 109.989 1.00 91.76  ? 105 PRO A N   1 
ATOM 652  C CA  . PRO A 1 105 ? 76.113  143.634 110.669 1.00 89.31  ? 105 PRO A CA  1 
ATOM 653  C C   . PRO A 1 105 ? 77.111  144.472 109.884 1.00 91.20  ? 105 PRO A C   1 
ATOM 654  O O   . PRO A 1 105 ? 77.132  145.697 110.053 1.00 92.94  ? 105 PRO A O   1 
ATOM 655  C CB  . PRO A 1 105 ? 76.726  143.116 111.980 1.00 89.27  ? 105 PRO A CB  1 
ATOM 656  C CG  . PRO A 1 105 ? 77.129  141.711 111.675 1.00 91.31  ? 105 PRO A CG  1 
ATOM 657  C CD  . PRO A 1 105 ? 76.075  141.197 110.737 1.00 92.01  ? 105 PRO A CD  1 
ATOM 658  N N   . LEU A 1 106 ? 77.937  143.858 109.034 1.00 88.04  ? 106 LEU A N   1 
ATOM 659  C CA  . LEU A 1 106 ? 78.914  144.612 108.255 1.00 88.18  ? 106 LEU A CA  1 
ATOM 660  C C   . LEU A 1 106 ? 78.307  145.380 107.087 1.00 87.52  ? 106 LEU A C   1 
ATOM 661  O O   . LEU A 1 106 ? 78.954  146.296 106.570 1.00 86.27  ? 106 LEU A O   1 
ATOM 662  C CB  . LEU A 1 106 ? 80.000  143.671 107.729 1.00 86.50  ? 106 LEU A CB  1 
ATOM 663  C CG  . LEU A 1 106 ? 80.942  143.066 108.770 1.00 87.42  ? 106 LEU A CG  1 
ATOM 664  C CD1 . LEU A 1 106 ? 81.847  142.026 108.135 1.00 85.85  ? 106 LEU A CD1 1 
ATOM 665  C CD2 . LEU A 1 106 ? 81.766  144.156 109.434 1.00 86.49  ? 106 LEU A CD2 1 
ATOM 666  N N   . ALA A 1 107 ? 77.095  145.026 106.655 1.00 89.72  ? 107 ALA A N   1 
ATOM 667  C CA  . ALA A 1 107 ? 76.558  145.580 105.415 1.00 90.65  ? 107 ALA A CA  1 
ATOM 668  C C   . ALA A 1 107 ? 76.357  147.090 105.496 1.00 91.47  ? 107 ALA A C   1 
ATOM 669  O O   . ALA A 1 107 ? 76.411  147.778 104.470 1.00 90.01  ? 107 ALA A O   1 
ATOM 670  C CB  . ALA A 1 107 ? 75.240  144.891 105.061 1.00 88.64  ? 107 ALA A CB  1 
ATOM 671  N N   . SER A 1 108 ? 76.129  147.624 106.698 1.00 93.30  ? 108 SER A N   1 
ATOM 672  C CA  . SER A 1 108 ? 75.929  149.060 106.856 1.00 93.33  ? 108 SER A CA  1 
ATOM 673  C C   . SER A 1 108 ? 77.216  149.870 106.743 1.00 93.05  ? 108 SER A C   1 
ATOM 674  O O   . SER A 1 108 ? 77.144  151.086 106.537 1.00 92.71  ? 108 SER A O   1 
ATOM 675  C CB  . SER A 1 108 ? 75.261  149.348 108.202 1.00 93.40  ? 108 SER A CB  1 
ATOM 676  O OG  . SER A 1 108 ? 74.055  148.618 108.339 1.00 92.28  ? 108 SER A OG  1 
ATOM 677  N N   . LEU A 1 109 ? 78.384  149.241 106.869 1.00 90.41  ? 109 LEU A N   1 
ATOM 678  C CA  . LEU A 1 109 ? 79.610  150.005 107.078 1.00 90.55  ? 109 LEU A CA  1 
ATOM 679  C C   . LEU A 1 109 ? 80.258  150.485 105.787 1.00 92.90  ? 109 LEU A C   1 
ATOM 680  O O   . LEU A 1 109 ? 80.827  151.582 105.766 1.00 94.45  ? 109 LEU A O   1 
ATOM 681  C CB  . LEU A 1 109 ? 80.622  149.173 107.869 1.00 90.93  ? 109 LEU A CB  1 
ATOM 682  C CG  . LEU A 1 109 ? 80.138  148.614 109.205 1.00 92.94  ? 109 LEU A CG  1 
ATOM 683  C CD1 . LEU A 1 109 ? 81.252  147.841 109.883 1.00 92.16  ? 109 LEU A CD1 1 
ATOM 684  C CD2 . LEU A 1 109 ? 79.635  149.734 110.101 1.00 91.68  ? 109 LEU A CD2 1 
ATOM 685  N N   . ALA A 1 110 ? 80.187  149.705 104.711 1.00 91.36  ? 110 ALA A N   1 
ATOM 686  C CA  . ALA A 1 110 ? 80.841  150.095 103.469 1.00 90.82  ? 110 ALA A CA  1 
ATOM 687  C C   . ALA A 1 110 ? 80.157  149.399 102.304 1.00 90.77  ? 110 ALA A C   1 
ATOM 688  O O   . ALA A 1 110 ? 79.399  148.442 102.486 1.00 90.18  ? 110 ALA A O   1 
ATOM 689  C CB  . ALA A 1 110 ? 82.337  149.762 103.493 1.00 89.60  ? 110 ALA A CB  1 
ATOM 690  N N   . THR A 1 111 ? 80.435  149.900 101.098 1.00 90.58  ? 111 THR A N   1 
ATOM 691  C CA  . THR A 1 111 ? 79.901  149.268 99.896  1.00 90.65  ? 111 THR A CA  1 
ATOM 692  C C   . THR A 1 111 ? 80.439  147.852 99.719  1.00 90.64  ? 111 THR A C   1 
ATOM 693  O O   . THR A 1 111 ? 79.726  146.976 99.215  1.00 89.86  ? 111 THR A O   1 
ATOM 694  C CB  . THR A 1 111 ? 80.229  150.129 98.672  1.00 91.72  ? 111 THR A CB  1 
ATOM 695  O OG1 . THR A 1 111 ? 79.536  151.380 98.768  1.00 91.78  ? 111 THR A OG1 1 
ATOM 696  C CG2 . THR A 1 111 ? 79.811  149.434 97.382  1.00 90.66  ? 111 THR A CG2 1 
ATOM 697  N N   . ASN A 1 112 ? 81.672  147.596 100.156 1.00 88.80  ? 112 ASN A N   1 
ATOM 698  C CA  . ASN A 1 112 ? 82.231  146.253 100.121 1.00 90.23  ? 112 ASN A CA  1 
ATOM 699  C C   . ASN A 1 112 ? 83.097  146.027 101.352 1.00 90.00  ? 112 ASN A C   1 
ATOM 700  O O   . ASN A 1 112 ? 83.785  146.942 101.815 1.00 88.47  ? 112 ASN A O   1 
ATOM 701  C CB  . ASN A 1 112 ? 83.054  146.025 98.846  1.00 88.65  ? 112 ASN A CB  1 
ATOM 702  C CG  . ASN A 1 112 ? 83.488  144.580 98.680  1.00 89.90  ? 112 ASN A CG  1 
ATOM 703  O OD1 . ASN A 1 112 ? 84.256  144.051 99.483  1.00 89.38  ? 112 ASN A OD1 1 
ATOM 704  N ND2 . ASN A 1 112 ? 82.995  143.934 97.630  1.00 87.92  ? 112 ASN A ND2 1 
ATOM 705  N N   . ARG A 1 113 ? 83.046  144.802 101.881 1.00 87.51  ? 113 ARG A N   1 
ATOM 706  C CA  . ARG A 1 113 ? 83.870  144.431 103.029 1.00 84.09  ? 113 ARG A CA  1 
ATOM 707  C C   . ARG A 1 113 ? 85.360  144.626 102.763 1.00 86.62  ? 113 ARG A C   1 
ATOM 708  O O   . ARG A 1 113 ? 86.137  144.805 103.708 1.00 87.81  ? 113 ARG A O   1 
ATOM 709  C CB  . ARG A 1 113 ? 83.590  142.981 103.420 1.00 85.01  ? 113 ARG A CB  1 
ATOM 710  C CG  . ARG A 1 113 ? 82.209  142.758 104.007 1.00 84.77  ? 113 ARG A CG  1 
ATOM 711  C CD  . ARG A 1 113 ? 82.039  141.332 104.495 1.00 85.52  ? 113 ARG A CD  1 
ATOM 712  N NE  . ARG A 1 113 ? 80.703  141.099 105.030 1.00 86.43  ? 113 ARG A NE  1 
ATOM 713  C CZ  . ARG A 1 113 ? 80.281  139.938 105.512 1.00 87.40  ? 113 ARG A CZ  1 
ATOM 714  N NH1 . ARG A 1 113 ? 81.078  138.885 105.574 1.00 87.38  ? 113 ARG A NH1 1 
ATOM 715  N NH2 . ARG A 1 113 ? 79.029  139.835 105.950 1.00 87.13  ? 113 ARG A NH2 1 
ATOM 716  N N   . SER A 1 114 ? 85.778  144.587 101.495 1.00 86.91  ? 114 SER A N   1 
ATOM 717  C CA  . SER A 1 114 ? 87.182  144.801 101.151 1.00 89.96  ? 114 SER A CA  1 
ATOM 718  C C   . SER A 1 114 ? 87.676  146.201 101.496 1.00 88.28  ? 114 SER A C   1 
ATOM 719  O O   . SER A 1 114 ? 88.891  146.418 101.555 1.00 85.63  ? 114 SER A O   1 
ATOM 720  C CB  . SER A 1 114 ? 87.405  144.530 99.661  1.00 86.36  ? 114 SER A CB  1 
ATOM 721  O OG  . SER A 1 114 ? 86.867  143.275 99.285  1.00 84.11  ? 114 SER A OG  1 
ATOM 722  N N   . HIS A 1 115 ? 86.772  147.152 101.722 1.00 87.66  ? 115 HIS A N   1 
ATOM 723  C CA  . HIS A 1 115 ? 87.168  148.499 102.110 1.00 87.15  ? 115 HIS A CA  1 
ATOM 724  C C   . HIS A 1 115 ? 87.469  148.630 103.600 1.00 87.96  ? 115 HIS A C   1 
ATOM 725  O O   . HIS A 1 115 ? 88.074  149.627 104.008 1.00 90.67  ? 115 HIS A O   1 
ATOM 726  C CB  . HIS A 1 115 ? 86.074  149.493 101.713 1.00 87.36  ? 115 HIS A CB  1 
ATOM 727  C CG  . HIS A 1 115 ? 86.485  150.928 101.833 1.00 91.21  ? 115 HIS A CG  1 
ATOM 728  N ND1 . HIS A 1 115 ? 87.433  151.501 101.014 1.00 89.65  ? 115 HIS A ND1 1 
ATOM 729  C CD2 . HIS A 1 115 ? 86.071  151.907 102.672 1.00 91.63  ? 115 HIS A CD2 1 
ATOM 730  C CE1 . HIS A 1 115 ? 87.589  152.771 101.345 1.00 88.88  ? 115 HIS A CE1 1 
ATOM 731  N NE2 . HIS A 1 115 ? 86.773  153.042 102.348 1.00 90.91  ? 115 HIS A NE2 1 
ATOM 732  N N   . LEU A 1 116 ? 87.069  147.658 104.415 1.00 80.46  ? 116 LEU A N   1 
ATOM 733  C CA  . LEU A 1 116 ? 87.287  147.756 105.850 1.00 80.92  ? 116 LEU A CA  1 
ATOM 734  C C   . LEU A 1 116 ? 88.771  147.631 106.208 1.00 83.32  ? 116 LEU A C   1 
ATOM 735  O O   . LEU A 1 116 ? 89.530  146.933 105.530 1.00 81.94  ? 116 LEU A O   1 
ATOM 736  C CB  . LEU A 1 116 ? 86.489  146.681 106.587 1.00 81.50  ? 116 LEU A CB  1 
ATOM 737  C CG  . LEU A 1 116 ? 85.012  146.949 106.903 1.00 83.08  ? 116 LEU A CG  1 
ATOM 738  C CD1 . LEU A 1 116 ? 84.883  148.050 107.946 1.00 81.31  ? 116 LEU A CD1 1 
ATOM 739  C CD2 . LEU A 1 116 ? 84.189  147.277 105.663 1.00 85.25  ? 116 LEU A CD2 1 
ATOM 740  N N   . PRO A 1 117 ? 89.202  148.307 107.274 1.00 81.87  ? 117 PRO A N   1 
ATOM 741  C CA  . PRO A 1 117 ? 90.570  148.127 107.778 1.00 80.76  ? 117 PRO A CA  1 
ATOM 742  C C   . PRO A 1 117 ? 90.791  146.747 108.382 1.00 76.28  ? 117 PRO A C   1 
ATOM 743  O O   . PRO A 1 117 ? 89.925  146.206 109.073 1.00 78.42  ? 117 PRO A O   1 
ATOM 744  C CB  . PRO A 1 117 ? 90.704  149.230 108.835 1.00 78.87  ? 117 PRO A CB  1 
ATOM 745  C CG  . PRO A 1 117 ? 89.310  149.458 109.306 1.00 76.81  ? 117 PRO A CG  1 
ATOM 746  C CD  . PRO A 1 117 ? 88.439  149.267 108.090 1.00 78.54  ? 117 PRO A CD  1 
ATOM 747  N N   . LEU A 1 118 ? 91.965  146.180 108.115 1.00 63.66  ? 118 LEU A N   1 
ATOM 748  C CA  . LEU A 1 118 ? 92.366  144.891 108.662 1.00 64.69  ? 118 LEU A CA  1 
ATOM 749  C C   . LEU A 1 118 ? 93.459  145.081 109.709 1.00 67.00  ? 118 LEU A C   1 
ATOM 750  O O   . LEU A 1 118 ? 94.370  145.894 109.526 1.00 69.86  ? 118 LEU A O   1 
ATOM 751  C CB  . LEU A 1 118 ? 92.869  143.963 107.552 1.00 62.85  ? 118 LEU A CB  1 
ATOM 752  C CG  . LEU A 1 118 ? 91.858  143.032 106.877 1.00 66.39  ? 118 LEU A CG  1 
ATOM 753  C CD1 . LEU A 1 118 ? 90.761  143.822 106.187 1.00 68.71  ? 118 LEU A CD1 1 
ATOM 754  C CD2 . LEU A 1 118 ? 92.556  142.111 105.890 1.00 66.81  ? 118 LEU A CD2 1 
ATOM 755  N N   . GLY A 1 119 ? 93.364  144.328 110.807 1.00 61.20  ? 119 GLY A N   1 
ATOM 756  C CA  . GLY A 1 119 ? 94.424  144.255 111.789 1.00 60.45  ? 119 GLY A CA  1 
ATOM 757  C C   . GLY A 1 119 ? 94.865  142.839 112.113 1.00 64.77  ? 119 GLY A C   1 
ATOM 758  O O   . GLY A 1 119 ? 94.189  141.862 111.783 1.00 72.80  ? 119 GLY A O   1 
ATOM 759  N N   . PRO A 1 120 ? 96.011  142.705 112.776 1.00 57.04  ? 120 PRO A N   1 
ATOM 760  C CA  . PRO A 1 120 ? 96.509  141.383 113.170 1.00 53.06  ? 120 PRO A CA  1 
ATOM 761  C C   . PRO A 1 120 ? 95.812  140.833 114.411 1.00 55.47  ? 120 PRO A C   1 
ATOM 762  O O   . PRO A 1 120 ? 95.063  141.522 115.103 1.00 56.15  ? 120 PRO A O   1 
ATOM 763  C CB  . PRO A 1 120 ? 97.992  141.647 113.441 1.00 57.77  ? 120 PRO A CB  1 
ATOM 764  C CG  . PRO A 1 120 ? 98.007  143.042 113.963 1.00 57.80  ? 120 PRO A CG  1 
ATOM 765  C CD  . PRO A 1 120 ? 96.930  143.779 113.191 1.00 57.76  ? 120 PRO A CD  1 
ATOM 766  N N   . CYS A 1 121 ? 96.083  139.551 114.683 1.00 51.86  ? 121 CYS A N   1 
ATOM 767  C CA  . CYS A 1 121 ? 95.455  138.819 115.788 1.00 51.01  ? 121 CYS A CA  1 
ATOM 768  C C   . CYS A 1 121 ? 96.084  139.204 117.131 1.00 53.04  ? 121 CYS A C   1 
ATOM 769  O O   . CYS A 1 121 ? 96.711  138.394 117.813 1.00 53.64  ? 121 CYS A O   1 
ATOM 770  C CB  . CYS A 1 121 ? 95.568  137.313 115.577 1.00 47.37  ? 121 CYS A CB  1 
ATOM 771  S SG  . CYS A 1 121 ? 94.840  136.531 114.105 1.00 47.33  ? 121 CYS A SG  1 
ATOM 772  N N   . GLN A 1 122 ? 95.916  140.474 117.506 1.00 57.42  ? 122 GLN A N   1 
ATOM 773  C CA  . GLN A 1 122 ? 96.548  140.976 118.725 1.00 51.75  ? 122 GLN A CA  1 
ATOM 774  C C   . GLN A 1 122 ? 96.044  140.278 119.986 1.00 52.54  ? 122 GLN A C   1 
ATOM 775  O O   . GLN A 1 122 ? 96.781  140.188 120.974 1.00 59.52  ? 122 GLN A O   1 
ATOM 776  C CB  . GLN A 1 122 ? 96.336  142.485 118.846 1.00 50.62  ? 122 GLN A CB  1 
ATOM 777  C CG  . GLN A 1 122 ? 97.018  143.294 117.760 1.00 57.82  ? 122 GLN A CG  1 
ATOM 778  C CD  . GLN A 1 122 ? 96.993  144.780 118.043 1.00 61.56  ? 122 GLN A CD  1 
ATOM 779  O OE1 . GLN A 1 122 ? 96.118  145.274 118.754 1.00 61.99  ? 122 GLN A OE1 1 
ATOM 780  N NE2 . GLN A 1 122 ? 97.959  145.504 117.491 1.00 60.93  ? 122 GLN A NE2 1 
ATOM 781  N N   . ASP A 1 123 ? 94.807  139.781 119.983 1.00 55.96  ? 123 ASP A N   1 
ATOM 782  C CA  . ASP A 1 123 ? 94.265  139.092 121.150 1.00 53.18  ? 123 ASP A CA  1 
ATOM 783  C C   . ASP A 1 123 ? 94.501  137.587 121.161 1.00 54.83  ? 123 ASP A C   1 
ATOM 784  O O   . ASP A 1 123 ? 94.368  136.968 122.223 1.00 54.82  ? 123 ASP A O   1 
ATOM 785  C CB  . ASP A 1 123 ? 92.761  139.358 121.273 1.00 52.57  ? 123 ASP A CB  1 
ATOM 786  C CG  . ASP A 1 123 ? 92.450  140.808 121.579 1.00 58.60  ? 123 ASP A CG  1 
ATOM 787  O OD1 . ASP A 1 123 ? 92.945  141.317 122.605 1.00 54.71  ? 123 ASP A OD1 1 
ATOM 788  O OD2 . ASP A 1 123 ? 91.706  141.437 120.799 1.00 64.84  ? 123 ASP A OD2 1 
ATOM 789  N N   . GLY A 1 124 ? 94.843  136.982 120.034 1.00 50.27  ? 124 GLY A N   1 
ATOM 790  C CA  . GLY A 1 124 ? 95.114  135.560 119.980 1.00 40.54  ? 124 GLY A CA  1 
ATOM 791  C C   . GLY A 1 124 ? 94.257  134.863 118.945 1.00 39.69  ? 124 GLY A C   1 
ATOM 792  O O   . GLY A 1 124 ? 93.527  135.490 118.172 1.00 44.44  ? 124 GLY A O   1 
ATOM 793  N N   . TRP A 1 125 ? 94.349  133.535 118.938 1.00 36.28  ? 125 TRP A N   1 
ATOM 794  C CA  . TRP A 1 125 ? 93.628  132.694 117.995 1.00 33.01  ? 125 TRP A CA  1 
ATOM 795  C C   . TRP A 1 125 ? 92.651  131.772 118.712 1.00 37.87  ? 125 TRP A C   1 
ATOM 796  O O   . TRP A 1 125 ? 92.839  131.422 119.880 1.00 47.75  ? 125 TRP A O   1 
ATOM 797  C CB  . TRP A 1 125 ? 94.600  131.863 117.157 1.00 24.67  ? 125 TRP A CB  1 
ATOM 798  C CG  . TRP A 1 125 ? 95.361  132.682 116.173 1.00 37.69  ? 125 TRP A CG  1 
ATOM 799  C CD1 . TRP A 1 125 ? 95.046  132.897 114.866 1.00 38.09  ? 125 TRP A CD1 1 
ATOM 800  C CD2 . TRP A 1 125 ? 96.560  133.423 116.424 1.00 48.87  ? 125 TRP A CD2 1 
ATOM 801  N NE1 . TRP A 1 125 ? 95.980  133.716 114.283 1.00 34.00  ? 125 TRP A NE1 1 
ATOM 802  C CE2 . TRP A 1 125 ? 96.920  134.054 115.220 1.00 40.73  ? 125 TRP A CE2 1 
ATOM 803  C CE3 . TRP A 1 125 ? 97.367  133.609 117.550 1.00 41.45  ? 125 TRP A CE3 1 
ATOM 804  C CZ2 . TRP A 1 125 ? 98.051  134.856 115.108 1.00 36.39  ? 125 TRP A CZ2 1 
ATOM 805  C CZ3 . TRP A 1 125 ? 98.487  134.405 117.437 1.00 37.47  ? 125 TRP A CZ3 1 
ATOM 806  C CH2 . TRP A 1 125 ? 98.819  135.019 116.227 1.00 37.23  ? 125 TRP A CH2 1 
ATOM 807  N N   . VAL A 1 126 ? 91.596  131.394 117.994 1.00 23.18  ? 126 VAL A N   1 
ATOM 808  C CA  . VAL A 1 126 ? 90.601  130.430 118.452 1.00 23.07  ? 126 VAL A CA  1 
ATOM 809  C C   . VAL A 1 126 ? 90.782  129.160 117.633 1.00 26.28  ? 126 VAL A C   1 
ATOM 810  O O   . VAL A 1 126 ? 90.648  129.185 116.404 1.00 32.99  ? 126 VAL A O   1 
ATOM 811  C CB  . VAL A 1 126 ? 89.175  130.979 118.308 1.00 26.49  ? 126 VAL A CB  1 
ATOM 812  C CG1 . VAL A 1 126 ? 88.159  129.941 118.740 1.00 31.52  ? 126 VAL A CG1 1 
ATOM 813  C CG2 . VAL A 1 126 ? 89.014  132.255 119.113 1.00 28.78  ? 126 VAL A CG2 1 
ATOM 814  N N   . TYR A 1 127 ? 91.076  128.049 118.304 1.00 26.35  ? 127 TYR A N   1 
ATOM 815  C CA  . TYR A 1 127 ? 91.371  126.790 117.632 1.00 24.22  ? 127 TYR A CA  1 
ATOM 816  C C   . TYR A 1 127 ? 90.182  125.843 117.736 1.00 37.77  ? 127 TYR A C   1 
ATOM 817  O O   . TYR A 1 127 ? 89.628  125.648 118.823 1.00 38.12  ? 127 TYR A O   1 
ATOM 818  C CB  . TYR A 1 127 ? 92.612  126.134 118.238 1.00 22.56  ? 127 TYR A CB  1 
ATOM 819  C CG  . TYR A 1 127 ? 93.870  126.960 118.114 1.00 30.79  ? 127 TYR A CG  1 
ATOM 820  C CD1 . TYR A 1 127 ? 94.569  127.024 116.918 1.00 34.71  ? 127 TYR A CD1 1 
ATOM 821  C CD2 . TYR A 1 127 ? 94.355  127.682 119.195 1.00 27.31  ? 127 TYR A CD2 1 
ATOM 822  C CE1 . TYR A 1 127 ? 95.718  127.781 116.805 1.00 30.25  ? 127 TYR A CE1 1 
ATOM 823  C CE2 . TYR A 1 127 ? 95.500  128.441 119.089 1.00 10.47  ? 127 TYR A CE2 1 
ATOM 824  C CZ  . TYR A 1 127 ? 96.176  128.486 117.894 1.00 16.60  ? 127 TYR A CZ  1 
ATOM 825  O OH  . TYR A 1 127 ? 97.317  129.241 117.789 1.00 25.84  ? 127 TYR A OH  1 
ATOM 826  N N   . ASP A 1 128 ? 89.795  125.260 116.600 1.00 38.65  ? 128 ASP A N   1 
ATOM 827  C CA  . ASP A 1 128 ? 88.635  124.370 116.521 1.00 34.48  ? 128 ASP A CA  1 
ATOM 828  C C   . ASP A 1 128 ? 89.093  122.927 116.722 1.00 39.81  ? 128 ASP A C   1 
ATOM 829  O O   . ASP A 1 128 ? 89.318  122.173 115.774 1.00 40.77  ? 128 ASP A O   1 
ATOM 830  C CB  . ASP A 1 128 ? 87.914  124.553 115.192 1.00 34.89  ? 128 ASP A CB  1 
ATOM 831  C CG  . ASP A 1 128 ? 86.573  123.848 115.155 1.00 47.34  ? 128 ASP A CG  1 
ATOM 832  O OD1 . ASP A 1 128 ? 86.121  123.363 116.213 1.00 45.91  ? 128 ASP A OD1 1 
ATOM 833  O OD2 . ASP A 1 128 ? 85.968  123.780 114.065 1.00 50.19  ? 128 ASP A OD2 1 
ATOM 834  N N   . THR A 1 129 ? 89.228  122.536 117.994 1.00 41.51  ? 129 THR A N   1 
ATOM 835  C CA  . THR A 1 129 ? 89.678  121.185 118.305 1.00 38.04  ? 129 THR A CA  1 
ATOM 836  C C   . THR A 1 129 ? 89.230  120.808 119.706 1.00 41.51  ? 129 THR A C   1 
ATOM 837  O O   . THR A 1 129 ? 89.168  121.685 120.578 1.00 44.16  ? 129 THR A O   1 
ATOM 838  C CB  . THR A 1 129 ? 91.203  121.061 118.183 1.00 36.00  ? 129 THR A CB  1 
ATOM 839  O OG1 . THR A 1 129 ? 91.595  119.700 118.395 1.00 38.64  ? 129 THR A OG1 1 
ATOM 840  C CG2 . THR A 1 129 ? 91.913  121.960 119.186 1.00 32.38  ? 129 THR A CG2 1 
ATOM 841  N N   . PRO A 1 130 ? 88.880  119.540 119.954 1.00 37.94  ? 130 PRO A N   1 
ATOM 842  C CA  . PRO A 1 130 ? 88.617  119.109 121.334 1.00 30.73  ? 130 PRO A CA  1 
ATOM 843  C C   . PRO A 1 130 ? 89.860  118.726 122.119 1.00 36.33  ? 130 PRO A C   1 
ATOM 844  O O   . PRO A 1 130 ? 89.780  118.631 123.351 1.00 41.47  ? 130 PRO A O   1 
ATOM 845  C CB  . PRO A 1 130 ? 87.695  117.900 121.143 1.00 32.66  ? 130 PRO A CB  1 
ATOM 846  C CG  . PRO A 1 130 ? 88.175  117.305 119.859 1.00 32.91  ? 130 PRO A CG  1 
ATOM 847  C CD  . PRO A 1 130 ? 88.578  118.474 118.982 1.00 34.12  ? 130 PRO A CD  1 
ATOM 848  N N   . GLY A 1 131 ? 90.990  118.501 121.464 1.00 32.49  ? 131 GLY A N   1 
ATOM 849  C CA  . GLY A 1 131 ? 92.232  118.148 122.134 1.00 24.52  ? 131 GLY A CA  1 
ATOM 850  C C   . GLY A 1 131 ? 93.196  119.312 122.200 1.00 33.93  ? 131 GLY A C   1 
ATOM 851  O O   . GLY A 1 131 ? 92.796  120.467 122.383 1.00 39.67  ? 131 GLY A O   1 
ATOM 852  N N   . SER A 1 132 ? 94.483  119.008 122.052 1.00 27.99  ? 132 SER A N   1 
ATOM 853  C CA  . SER A 1 132 ? 95.508  120.041 122.080 1.00 25.75  ? 132 SER A CA  1 
ATOM 854  C C   . SER A 1 132 ? 96.763  119.521 121.398 1.00 24.81  ? 132 SER A C   1 
ATOM 855  O O   . SER A 1 132 ? 96.960  118.313 121.249 1.00 28.70  ? 132 SER A O   1 
ATOM 856  C CB  . SER A 1 132 ? 95.822  120.485 123.513 1.00 35.56  ? 132 SER A CB  1 
ATOM 857  O OG  . SER A 1 132 ? 96.510  119.473 124.225 1.00 40.61  ? 132 SER A OG  1 
ATOM 858  N N   . SER A 1 133 ? 97.611  120.460 120.987 1.00 24.63  ? 133 SER A N   1 
ATOM 859  C CA  . SER A 1 133 ? 98.886  120.158 120.357 1.00 17.01  ? 133 SER A CA  1 
ATOM 860  C C   . SER A 1 133 ? 99.859  121.275 120.703 1.00 25.10  ? 133 SER A C   1 
ATOM 861  O O   . SER A 1 133 ? 99.472  122.317 121.236 1.00 39.72  ? 133 SER A O   1 
ATOM 862  C CB  . SER A 1 133 ? 98.744  119.984 118.842 1.00 15.01  ? 133 SER A CB  1 
ATOM 863  O OG  . SER A 1 133 ? 98.534  121.225 118.197 1.00 26.36  ? 133 SER A OG  1 
ATOM 864  N N   . ILE A 1 134 ? 101.143 121.036 120.424 1.00 28.26  ? 134 ILE A N   1 
ATOM 865  C CA  . ILE A 1 134 ? 102.151 122.069 120.652 1.00 24.09  ? 134 ILE A CA  1 
ATOM 866  C C   . ILE A 1 134 ? 101.855 123.314 119.823 1.00 28.83  ? 134 ILE A C   1 
ATOM 867  O O   . ILE A 1 134 ? 102.166 124.435 120.243 1.00 41.30  ? 134 ILE A O   1 
ATOM 868  C CB  . ILE A 1 134 ? 103.564 121.518 120.371 1.00 19.34  ? 134 ILE A CB  1 
ATOM 869  C CG1 . ILE A 1 134 ? 103.719 121.121 118.903 1.00 31.33  ? 134 ILE A CG1 1 
ATOM 870  C CG2 . ILE A 1 134 ? 103.874 120.343 121.283 1.00 16.61  ? 134 ILE A CG2 1 
ATOM 871  C CD1 . ILE A 1 134 ? 105.144 120.829 118.500 1.00 33.10  ? 134 ILE A CD1 1 
ATOM 872  N N   . VAL A 1 135 ? 101.264 123.144 118.638 1.00 34.83  ? 135 VAL A N   1 
ATOM 873  C CA  . VAL A 1 135 ? 100.889 124.286 117.807 1.00 21.06  ? 135 VAL A CA  1 
ATOM 874  C C   . VAL A 1 135 ? 99.868  125.164 118.522 1.00 18.19  ? 135 VAL A C   1 
ATOM 875  O O   . VAL A 1 135 ? 99.961  126.396 118.497 1.00 23.75  ? 135 VAL A O   1 
ATOM 876  C CB  . VAL A 1 135 ? 100.364 123.801 116.444 1.00 11.04  ? 135 VAL A CB  1 
ATOM 877  C CG1 . VAL A 1 135 ? 99.760  124.954 115.661 1.00 15.33  ? 135 VAL A CG1 1 
ATOM 878  C CG2 . VAL A 1 135 ? 101.480 123.145 115.653 1.00 19.09  ? 135 VAL A CG2 1 
ATOM 879  N N   . THR A 1 136 ? 98.886  124.546 119.177 1.00 20.50  ? 136 THR A N   1 
ATOM 880  C CA  . THR A 1 136 ? 97.804  125.301 119.798 1.00 20.99  ? 136 THR A CA  1 
ATOM 881  C C   . THR A 1 136 ? 98.223  125.924 121.123 1.00 26.58  ? 136 THR A C   1 
ATOM 882  O O   . THR A 1 136 ? 97.658  126.945 121.528 1.00 33.39  ? 136 THR A O   1 
ATOM 883  C CB  . THR A 1 136 ? 96.584  124.405 120.010 1.00 17.60  ? 136 THR A CB  1 
ATOM 884  O OG1 . THR A 1 136 ? 96.882  123.421 121.005 1.00 32.99  ? 136 THR A OG1 1 
ATOM 885  C CG2 . THR A 1 136 ? 96.211  123.706 118.717 1.00 11.23  ? 136 THR A CG2 1 
ATOM 886  N N   . GLU A 1 137 ? 99.197  125.331 121.809 1.00 31.36  ? 137 GLU A N   1 
ATOM 887  C CA  . GLU A 1 137 ? 99.609  125.813 123.120 1.00 33.96  ? 137 GLU A CA  1 
ATOM 888  C C   . GLU A 1 137 ? 100.648 126.923 123.031 1.00 34.18  ? 137 GLU A C   1 
ATOM 889  O O   . GLU A 1 137 ? 100.568 127.904 123.777 1.00 41.61  ? 137 GLU A O   1 
ATOM 890  C CB  . GLU A 1 137 ? 100.158 124.654 123.953 1.00 31.18  ? 137 GLU A CB  1 
ATOM 891  C CG  . GLU A 1 137 ? 100.585 125.045 125.352 1.00 40.90  ? 137 GLU A CG  1 
ATOM 892  C CD  . GLU A 1 137 ? 100.604 123.868 126.299 1.00 45.99  ? 137 GLU A CD  1 
ATOM 893  O OE1 . GLU A 1 137 ? 100.189 122.768 125.883 1.00 50.09  ? 137 GLU A OE1 1 
ATOM 894  O OE2 . GLU A 1 137 ? 101.033 124.043 127.458 1.00 46.72  ? 137 GLU A OE2 1 
ATOM 895  N N   . PHE A 1 138 ? 101.629 126.784 122.144 1.00 32.65  ? 138 PHE A N   1 
ATOM 896  C CA  . PHE A 1 138 ? 102.664 127.792 121.969 1.00 21.78  ? 138 PHE A CA  1 
ATOM 897  C C   . PHE A 1 138 ? 102.338 128.793 120.866 1.00 22.69  ? 138 PHE A C   1 
ATOM 898  O O   . PHE A 1 138 ? 103.116 129.729 120.655 1.00 47.01  ? 138 PHE A O   1 
ATOM 899  C CB  . PHE A 1 138 ? 104.007 127.113 121.690 1.00 26.48  ? 138 PHE A CB  1 
ATOM 900  C CG  . PHE A 1 138 ? 104.406 126.111 122.740 1.00 36.18  ? 138 PHE A CG  1 
ATOM 901  C CD1 . PHE A 1 138 ? 104.396 126.455 124.082 1.00 33.21  ? 138 PHE A CD1 1 
ATOM 902  C CD2 . PHE A 1 138 ? 104.788 124.828 122.388 1.00 26.12  ? 138 PHE A CD2 1 
ATOM 903  C CE1 . PHE A 1 138 ? 104.758 125.539 125.051 1.00 23.27  ? 138 PHE A CE1 1 
ATOM 904  C CE2 . PHE A 1 138 ? 105.151 123.909 123.354 1.00 29.82  ? 138 PHE A CE2 1 
ATOM 905  C CZ  . PHE A 1 138 ? 105.135 124.266 124.686 1.00 24.33  ? 138 PHE A CZ  1 
ATOM 906  N N   . ASN A 1 139 ? 101.217 128.610 120.161 1.00 19.79  ? 139 ASN A N   1 
ATOM 907  C CA  . ASN A 1 139 ? 100.734 129.535 119.130 1.00 19.74  ? 139 ASN A CA  1 
ATOM 908  C C   . ASN A 1 139 ? 101.687 129.615 117.936 1.00 22.66  ? 139 ASN A C   1 
ATOM 909  O O   . ASN A 1 139 ? 102.095 130.695 117.506 1.00 29.16  ? 139 ASN A O   1 
ATOM 910  C CB  . ASN A 1 139 ? 100.472 130.924 119.716 1.00 19.04  ? 139 ASN A CB  1 
ATOM 911  C CG  . ASN A 1 139 ? 99.281  130.947 120.648 1.00 16.79  ? 139 ASN A CG  1 
ATOM 912  O OD1 . ASN A 1 139 ? 98.230  130.392 120.341 1.00 31.03  ? 139 ASN A OD1 1 
ATOM 913  N ND2 . ASN A 1 139 ? 99.439  131.594 121.793 1.00 24.55  ? 139 ASN A ND2 1 
ATOM 914  N N   . LEU A 1 140 ? 102.043 128.448 117.400 1.00 11.14  ? 140 LEU A N   1 
ATOM 915  C CA  . LEU A 1 140 ? 103.002 128.342 116.300 1.00 18.94  ? 140 LEU A CA  1 
ATOM 916  C C   . LEU A 1 140 ? 102.318 128.552 114.944 1.00 16.16  ? 140 LEU A C   1 
ATOM 917  O O   . LEU A 1 140 ? 102.324 127.687 114.070 1.00 13.86  ? 140 LEU A O   1 
ATOM 918  C CB  . LEU A 1 140 ? 103.719 126.999 116.361 1.00 27.14  ? 140 LEU A CB  1 
ATOM 919  C CG  . LEU A 1 140 ? 104.424 126.651 117.674 1.00 17.31  ? 140 LEU A CG  1 
ATOM 920  C CD1 . LEU A 1 140 ? 104.996 125.250 117.619 1.00 15.13  ? 140 LEU A CD1 1 
ATOM 921  C CD2 . LEU A 1 140 ? 105.518 127.659 117.977 1.00 11.11  ? 140 LEU A CD2 1 
ATOM 922  N N   . VAL A 1 141 ? 101.716 129.733 114.777 1.00 32.34  ? 141 VAL A N   1 
ATOM 923  C CA  . VAL A 1 141 ? 100.903 130.042 113.606 1.00 35.16  ? 141 VAL A CA  1 
ATOM 924  C C   . VAL A 1 141 ? 101.300 131.400 113.035 1.00 31.13  ? 141 VAL A C   1 
ATOM 925  O O   . VAL A 1 141 ? 101.948 132.216 113.693 1.00 35.62  ? 141 VAL A O   1 
ATOM 926  C CB  . VAL A 1 141 ? 99.389  130.021 113.921 1.00 27.63  ? 141 VAL A CB  1 
ATOM 927  C CG1 . VAL A 1 141 ? 98.944  128.627 114.324 1.00 23.01  ? 141 VAL A CG1 1 
ATOM 928  C CG2 . VAL A 1 141 ? 99.057  131.019 115.012 1.00 23.50  ? 141 VAL A CG2 1 
ATOM 929  N N   . CYS A 1 142 ? 100.883 131.630 111.786 1.00 27.49  ? 142 CYS A N   1 
ATOM 930  C CA  . CYS A 1 142 ? 101.192 132.838 111.006 1.00 32.83  ? 142 CYS A CA  1 
ATOM 931  C C   . CYS A 1 142 ? 102.704 133.029 110.925 1.00 40.84  ? 142 CYS A C   1 
ATOM 932  O O   . CYS A 1 142 ? 103.395 132.118 110.439 1.00 48.59  ? 142 CYS A O   1 
ATOM 933  C CB  . CYS A 1 142 ? 100.400 134.030 111.561 1.00 27.52  ? 142 CYS A CB  1 
ATOM 934  S SG  . CYS A 1 142 ? 98.590  133.814 111.628 1.00 48.33  ? 142 CYS A SG  1 
ATOM 935  N N   . ALA A 1 143 ? 103.255 134.167 111.354 1.00 34.78  ? 143 ALA A N   1 
ATOM 936  C CA  . ALA A 1 143 ? 104.692 134.424 111.281 1.00 26.00  ? 143 ALA A CA  1 
ATOM 937  C C   . ALA A 1 143 ? 105.547 133.483 112.126 1.00 37.11  ? 143 ALA A C   1 
ATOM 938  O O   . ALA A 1 143 ? 106.737 133.328 111.832 1.00 38.91  ? 143 ALA A O   1 
ATOM 939  C CB  . ALA A 1 143 ? 104.974 135.869 111.691 1.00 17.64  ? 143 ALA A CB  1 
ATOM 940  N N   . ASP A 1 144 ? 104.992 132.858 113.160 1.00 29.11  ? 144 ASP A N   1 
ATOM 941  C CA  . ASP A 1 144 ? 105.737 131.886 113.953 1.00 17.79  ? 144 ASP A CA  1 
ATOM 942  C C   . ASP A 1 144 ? 105.678 130.466 113.403 1.00 27.07  ? 144 ASP A C   1 
ATOM 943  O O   . ASP A 1 144 ? 106.264 129.563 114.007 1.00 44.11  ? 144 ASP A O   1 
ATOM 944  C CB  . ASP A 1 144 ? 105.237 131.893 115.398 1.00 22.07  ? 144 ASP A CB  1 
ATOM 945  C CG  . ASP A 1 144 ? 105.651 133.141 116.149 1.00 36.41  ? 144 ASP A CG  1 
ATOM 946  O OD1 . ASP A 1 144 ? 106.865 133.328 116.366 1.00 34.34  ? 144 ASP A OD1 1 
ATOM 947  O OD2 . ASP A 1 144 ? 104.765 133.935 116.523 1.00 50.35  ? 144 ASP A OD2 1 
ATOM 948  N N   . SER A 1 145 ? 104.989 130.243 112.283 1.00 21.12  ? 145 SER A N   1 
ATOM 949  C CA  . SER A 1 145 ? 104.723 128.890 111.805 1.00 19.34  ? 145 SER A CA  1 
ATOM 950  C C   . SER A 1 145 ? 105.974 128.158 111.332 1.00 28.59  ? 145 SER A C   1 
ATOM 951  O O   . SER A 1 145 ? 105.929 126.935 111.168 1.00 36.33  ? 145 SER A O   1 
ATOM 952  C CB  . SER A 1 145 ? 103.695 128.929 110.677 1.00 20.28  ? 145 SER A CB  1 
ATOM 953  O OG  . SER A 1 145 ? 104.157 129.723 109.602 1.00 35.18  ? 145 SER A OG  1 
ATOM 954  N N   . TRP A 1 146 ? 107.082 128.866 111.102 1.00 34.76  ? 146 TRP A N   1 
ATOM 955  C CA  . TRP A 1 146 ? 108.334 128.206 110.738 1.00 32.00  ? 146 TRP A CA  1 
ATOM 956  C C   . TRP A 1 146 ? 108.993 127.486 111.909 1.00 28.16  ? 146 TRP A C   1 
ATOM 957  O O   . TRP A 1 146 ? 109.864 126.640 111.685 1.00 30.71  ? 146 TRP A O   1 
ATOM 958  C CB  . TRP A 1 146 ? 109.302 129.225 110.124 1.00 21.51  ? 146 TRP A CB  1 
ATOM 959  C CG  . TRP A 1 146 ? 109.722 130.328 111.054 1.00 19.50  ? 146 TRP A CG  1 
ATOM 960  C CD1 . TRP A 1 146 ? 109.110 131.534 111.219 1.00 16.12  ? 146 TRP A CD1 1 
ATOM 961  C CD2 . TRP A 1 146 ? 110.865 130.339 111.918 1.00 29.35  ? 146 TRP A CD2 1 
ATOM 962  N NE1 . TRP A 1 146 ? 109.786 132.287 112.146 1.00 16.61  ? 146 TRP A NE1 1 
ATOM 963  C CE2 . TRP A 1 146 ? 110.868 131.575 112.590 1.00 21.97  ? 146 TRP A CE2 1 
ATOM 964  C CE3 . TRP A 1 146 ? 111.879 129.418 112.196 1.00 29.52  ? 146 TRP A CE3 1 
ATOM 965  C CZ2 . TRP A 1 146 ? 111.846 131.915 113.520 1.00 23.31  ? 146 TRP A CZ2 1 
ATOM 966  C CZ3 . TRP A 1 146 ? 112.848 129.758 113.120 1.00 19.04  ? 146 TRP A CZ3 1 
ATOM 967  C CH2 . TRP A 1 146 ? 112.824 130.996 113.770 1.00 19.72  ? 146 TRP A CH2 1 
ATOM 968  N N   . LYS A 1 147 ? 108.603 127.798 113.145 1.00 29.66  ? 147 LYS A N   1 
ATOM 969  C CA  . LYS A 1 147 ? 109.227 127.198 114.321 1.00 18.86  ? 147 LYS A CA  1 
ATOM 970  C C   . LYS A 1 147 ? 108.811 125.748 114.554 1.00 27.84  ? 147 LYS A C   1 
ATOM 971  O O   . LYS A 1 147 ? 109.461 125.054 115.341 1.00 40.46  ? 147 LYS A O   1 
ATOM 972  C CB  . LYS A 1 147 ? 108.919 128.036 115.559 1.00 16.15  ? 147 LYS A CB  1 
ATOM 973  C CG  . LYS A 1 147 ? 109.474 129.442 115.485 1.00 13.41  ? 147 LYS A CG  1 
ATOM 974  C CD  . LYS A 1 147 ? 109.000 130.289 116.644 1.00 23.24  ? 147 LYS A CD  1 
ATOM 975  C CE  . LYS A 1 147 ? 109.672 131.647 116.635 1.00 30.99  ? 147 LYS A CE  1 
ATOM 976  N NZ  . LYS A 1 147 ? 109.333 132.439 117.847 1.00 38.18  ? 147 LYS A NZ  1 
ATOM 977  N N   . LEU A 1 148 ? 107.744 125.278 113.905 1.00 36.98  ? 148 LEU A N   1 
ATOM 978  C CA  . LEU A 1 148 ? 107.425 123.852 113.929 1.00 33.61  ? 148 LEU A CA  1 
ATOM 979  C C   . LEU A 1 148 ? 108.463 123.011 113.187 1.00 35.91  ? 148 LEU A C   1 
ATOM 980  O O   . LEU A 1 148 ? 108.665 121.840 113.528 1.00 39.18  ? 148 LEU A O   1 
ATOM 981  C CB  . LEU A 1 148 ? 106.031 123.626 113.342 1.00 26.59  ? 148 LEU A CB  1 
ATOM 982  C CG  . LEU A 1 148 ? 105.481 122.199 113.344 1.00 34.67  ? 148 LEU A CG  1 
ATOM 983  C CD1 . LEU A 1 148 ? 105.281 121.713 114.767 1.00 34.90  ? 148 LEU A CD1 1 
ATOM 984  C CD2 . LEU A 1 148 ? 104.180 122.122 112.566 1.00 33.28  ? 148 LEU A CD2 1 
ATOM 985  N N   . ASP A 1 149 ? 109.127 123.581 112.179 1.00 41.86  ? 149 ASP A N   1 
ATOM 986  C CA  . ASP A 1 149 ? 110.138 122.847 111.418 1.00 40.08  ? 149 ASP A CA  1 
ATOM 987  C C   . ASP A 1 149 ? 111.390 122.590 112.252 1.00 42.09  ? 149 ASP A C   1 
ATOM 988  O O   . ASP A 1 149 ? 112.090 121.580 112.057 1.00 38.88  ? 149 ASP A O   1 
ATOM 989  C CB  . ASP A 1 149 ? 110.494 123.636 110.161 1.00 39.78  ? 149 ASP A CB  1 
ATOM 990  C CG  . ASP A 1 149 ? 109.275 123.999 109.339 1.00 47.78  ? 149 ASP A CG  1 
ATOM 991  O OD1 . ASP A 1 149 ? 108.147 123.761 109.817 1.00 46.33  ? 149 ASP A OD1 1 
ATOM 992  O OD2 . ASP A 1 149 ? 109.441 124.534 108.224 1.00 46.35  ? 149 ASP A OD2 1 
ATOM 993  N N   . LEU A 1 150 ? 111.644 123.456 113.228 1.00 41.94  ? 150 LEU A N   1 
ATOM 994  C CA  . LEU A 1 150 ? 112.829 123.359 114.061 1.00 31.59  ? 150 LEU A CA  1 
ATOM 995  C C   . LEU A 1 150 ? 112.693 122.263 115.104 1.00 34.78  ? 150 LEU A C   1 
ATOM 996  O O   . LEU A 1 150 ? 113.710 121.746 115.573 1.00 43.33  ? 150 LEU A O   1 
ATOM 997  C CB  . LEU A 1 150 ? 113.090 124.712 114.727 1.00 27.99  ? 150 LEU A CB  1 
ATOM 998  C CG  . LEU A 1 150 ? 114.342 124.915 115.574 1.00 37.90  ? 150 LEU A CG  1 
ATOM 999  C CD1 . LEU A 1 150 ? 115.585 124.619 114.758 1.00 37.78  ? 150 LEU A CD1 1 
ATOM 1000 C CD2 . LEU A 1 150 ? 114.374 126.338 116.100 1.00 32.14  ? 150 LEU A CD2 1 
ATOM 1001 N N   . PHE A 1 151 ? 111.465 121.844 115.409 1.00 34.53  ? 151 PHE A N   1 
ATOM 1002 C CA  . PHE A 1 151 ? 111.258 120.741 116.340 1.00 35.68  ? 151 PHE A CA  1 
ATOM 1003 C C   . PHE A 1 151 ? 111.805 119.438 115.765 1.00 37.48  ? 151 PHE A C   1 
ATOM 1004 O O   . PHE A 1 151 ? 112.417 118.643 116.487 1.00 37.08  ? 151 PHE A O   1 
ATOM 1005 C CB  . PHE A 1 151 ? 109.762 120.628 116.649 1.00 31.67  ? 151 PHE A CB  1 
ATOM 1006 C CG  . PHE A 1 151 ? 109.421 119.651 117.736 1.00 44.08  ? 151 PHE A CG  1 
ATOM 1007 C CD1 . PHE A 1 151 ? 109.551 120.001 119.069 1.00 42.01  ? 151 PHE A CD1 1 
ATOM 1008 C CD2 . PHE A 1 151 ? 108.925 118.396 117.425 1.00 41.06  ? 151 PHE A CD2 1 
ATOM 1009 C CE1 . PHE A 1 151 ? 109.220 119.110 120.069 1.00 33.36  ? 151 PHE A CE1 1 
ATOM 1010 C CE2 . PHE A 1 151 ? 108.593 117.500 118.422 1.00 31.82  ? 151 PHE A CE2 1 
ATOM 1011 C CZ  . PHE A 1 151 ? 108.741 117.858 119.745 1.00 33.99  ? 151 PHE A CZ  1 
ATOM 1012 N N   . GLN A 1 152 ? 111.592 119.201 114.468 1.00 36.90  ? 152 GLN A N   1 
ATOM 1013 C CA  . GLN A 1 152 ? 112.122 118.012 113.806 1.00 33.87  ? 152 GLN A CA  1 
ATOM 1014 C C   . GLN A 1 152 ? 113.581 118.192 113.386 1.00 41.07  ? 152 GLN A C   1 
ATOM 1015 O O   . GLN A 1 152 ? 114.363 117.223 113.398 1.00 45.70  ? 152 GLN A O   1 
ATOM 1016 C CB  . GLN A 1 152 ? 111.258 117.679 112.586 1.00 34.16  ? 152 GLN A CB  1 
ATOM 1017 C CG  . GLN A 1 152 ? 111.451 116.289 111.982 1.00 43.24  ? 152 GLN A CG  1 
ATOM 1018 C CD  . GLN A 1 152 ? 110.961 115.154 112.871 1.00 45.30  ? 152 GLN A CD  1 
ATOM 1019 O OE1 . GLN A 1 152 ? 110.614 115.352 114.034 1.00 43.02  ? 152 GLN A OE1 1 
ATOM 1020 N NE2 . GLN A 1 152 ? 110.929 113.950 112.314 1.00 39.34  ? 152 GLN A NE2 1 
ATOM 1021 N N   . SER A 1 153 ? 113.994 119.436 113.111 1.00 33.63  ? 153 SER A N   1 
ATOM 1022 C CA  . SER A 1 153 ? 115.393 119.661 112.760 1.00 31.50  ? 153 SER A CA  1 
ATOM 1023 C C   . SER A 1 153 ? 116.319 119.476 113.958 1.00 34.31  ? 153 SER A C   1 
ATOM 1024 O O   . SER A 1 153 ? 117.431 118.960 113.803 1.00 34.31  ? 153 SER A O   1 
ATOM 1025 C CB  . SER A 1 153 ? 115.566 121.055 112.162 1.00 44.42  ? 153 SER A CB  1 
ATOM 1026 O OG  . SER A 1 153 ? 114.760 121.216 111.010 1.00 50.65  ? 153 SER A OG  1 
ATOM 1027 N N   . CYS A 1 154 ? 115.912 119.926 115.149 1.00 35.73  ? 154 CYS A N   1 
ATOM 1028 C CA  . CYS A 1 154 ? 116.733 119.703 116.336 1.00 35.61  ? 154 CYS A CA  1 
ATOM 1029 C C   . CYS A 1 154 ? 116.939 118.215 116.600 1.00 38.77  ? 154 CYS A C   1 
ATOM 1030 O O   . CYS A 1 154 ? 118.043 117.785 116.957 1.00 37.54  ? 154 CYS A O   1 
ATOM 1031 C CB  . CYS A 1 154 ? 116.096 120.379 117.549 1.00 31.99  ? 154 CYS A CB  1 
ATOM 1032 S SG  . CYS A 1 154 ? 116.262 122.176 117.576 1.00 62.05  ? 154 CYS A SG  1 
ATOM 1033 N N   . LEU A 1 155 ? 115.883 117.414 116.433 1.00 38.47  ? 155 LEU A N   1 
ATOM 1034 C CA  . LEU A 1 155 ? 116.003 115.966 116.576 1.00 34.13  ? 155 LEU A CA  1 
ATOM 1035 C C   . LEU A 1 155 ? 117.016 115.390 115.596 1.00 30.09  ? 155 LEU A C   1 
ATOM 1036 O O   . LEU A 1 155 ? 117.866 114.572 115.970 1.00 33.26  ? 155 LEU A O   1 
ATOM 1037 C CB  . LEU A 1 155 ? 114.640 115.302 116.384 1.00 36.49  ? 155 LEU A CB  1 
ATOM 1038 C CG  . LEU A 1 155 ? 114.640 113.778 116.525 1.00 39.08  ? 155 LEU A CG  1 
ATOM 1039 C CD1 . LEU A 1 155 ? 114.661 113.371 117.988 1.00 41.14  ? 155 LEU A CD1 1 
ATOM 1040 C CD2 . LEU A 1 155 ? 113.450 113.166 115.808 1.00 32.61  ? 155 LEU A CD2 1 
ATOM 1041 N N   . ASN A 1 156 ? 116.939 115.797 114.327 1.00 33.72  ? 156 ASN A N   1 
ATOM 1042 C CA  . ASN A 1 156 ? 117.860 115.216 113.351 1.00 32.22  ? 156 ASN A CA  1 
ATOM 1043 C C   . ASN A 1 156 ? 119.300 115.693 113.554 1.00 37.06  ? 156 ASN A C   1 
ATOM 1044 O O   . ASN A 1 156 ? 120.245 114.926 113.331 1.00 37.12  ? 156 ASN A O   1 
ATOM 1045 C CB  . ASN A 1 156 ? 117.372 115.511 111.937 1.00 41.49  ? 156 ASN A CB  1 
ATOM 1046 C CG  . ASN A 1 156 ? 116.142 114.704 111.575 1.00 47.47  ? 156 ASN A CG  1 
ATOM 1047 O OD1 . ASN A 1 156 ? 116.242 113.536 111.202 1.00 46.68  ? 156 ASN A OD1 1 
ATOM 1048 N ND2 . ASN A 1 156 ? 114.973 115.320 111.692 1.00 46.09  ? 156 ASN A ND2 1 
ATOM 1049 N N   . ALA A 1 157 ? 119.490 116.936 114.001 1.00 39.98  ? 157 ALA A N   1 
ATOM 1050 C CA  . ALA A 1 157 ? 120.821 117.397 114.390 1.00 36.12  ? 157 ALA A CA  1 
ATOM 1051 C C   . ALA A 1 157 ? 121.378 116.594 115.563 1.00 45.28  ? 157 ALA A C   1 
ATOM 1052 O O   . ALA A 1 157 ? 122.568 116.242 115.578 1.00 45.02  ? 157 ALA A O   1 
ATOM 1053 C CB  . ALA A 1 157 ? 120.781 118.885 114.733 1.00 33.42  ? 157 ALA A CB  1 
ATOM 1054 N N   . GLY A 1 158 ? 120.541 116.324 116.570 1.00 40.77  ? 158 GLY A N   1 
ATOM 1055 C CA  . GLY A 1 158 ? 120.962 115.441 117.645 1.00 25.08  ? 158 GLY A CA  1 
ATOM 1056 C C   . GLY A 1 158 ? 121.351 114.062 117.152 1.00 36.60  ? 158 GLY A C   1 
ATOM 1057 O O   . GLY A 1 158 ? 122.328 113.483 117.626 1.00 34.39  ? 158 GLY A O   1 
ATOM 1058 N N   . PHE A 1 159 ? 120.593 113.515 116.197 1.00 45.60  ? 159 PHE A N   1 
ATOM 1059 C CA  . PHE A 1 159 ? 120.985 112.245 115.583 1.00 33.96  ? 159 PHE A CA  1 
ATOM 1060 C C   . PHE A 1 159 ? 122.371 112.348 114.962 1.00 43.05  ? 159 PHE A C   1 
ATOM 1061 O O   . PHE A 1 159 ? 123.204 111.446 115.114 1.00 50.09  ? 159 PHE A O   1 
ATOM 1062 C CB  . PHE A 1 159 ? 119.974 111.807 114.522 1.00 33.19  ? 159 PHE A CB  1 
ATOM 1063 C CG  . PHE A 1 159 ? 118.689 111.267 115.076 1.00 38.94  ? 159 PHE A CG  1 
ATOM 1064 C CD1 . PHE A 1 159 ? 118.521 111.080 116.435 1.00 44.75  ? 159 PHE A CD1 1 
ATOM 1065 C CD2 . PHE A 1 159 ? 117.654 110.924 114.225 1.00 40.38  ? 159 PHE A CD2 1 
ATOM 1066 C CE1 . PHE A 1 159 ? 117.339 110.574 116.936 1.00 44.58  ? 159 PHE A CE1 1 
ATOM 1067 C CE2 . PHE A 1 159 ? 116.471 110.420 114.720 1.00 44.24  ? 159 PHE A CE2 1 
ATOM 1068 C CZ  . PHE A 1 159 ? 116.313 110.244 116.078 1.00 45.69  ? 159 PHE A CZ  1 
ATOM 1069 N N   . LEU A 1 160 ? 122.620 113.434 114.229 1.00 45.15  ? 160 LEU A N   1 
ATOM 1070 C CA  . LEU A 1 160 ? 123.899 113.608 113.545 1.00 43.82  ? 160 LEU A CA  1 
ATOM 1071 C C   . LEU A 1 160 ? 125.069 113.624 114.525 1.00 44.87  ? 160 LEU A C   1 
ATOM 1072 O O   . LEU A 1 160 ? 126.049 112.891 114.350 1.00 46.83  ? 160 LEU A O   1 
ATOM 1073 C CB  . LEU A 1 160 ? 123.878 114.893 112.718 1.00 50.80  ? 160 LEU A CB  1 
ATOM 1074 C CG  . LEU A 1 160 ? 125.139 115.214 111.913 1.00 44.46  ? 160 LEU A CG  1 
ATOM 1075 C CD1 . LEU A 1 160 ? 125.387 114.155 110.855 1.00 48.26  ? 160 LEU A CD1 1 
ATOM 1076 C CD2 . LEU A 1 160 ? 125.039 116.592 111.282 1.00 41.90  ? 160 LEU A CD2 1 
ATOM 1077 N N   . PHE A 1 161 ? 124.989 114.464 115.560 1.00 54.65  ? 161 PHE A N   1 
ATOM 1078 C CA  . PHE A 1 161 ? 126.038 114.477 116.585 1.00 50.07  ? 161 PHE A CA  1 
ATOM 1079 C C   . PHE A 1 161 ? 126.157 113.145 117.328 1.00 54.73  ? 161 PHE A C   1 
ATOM 1080 O O   . PHE A 1 161 ? 127.274 112.688 117.615 1.00 57.76  ? 161 PHE A O   1 
ATOM 1081 C CB  . PHE A 1 161 ? 125.809 115.621 117.572 1.00 44.38  ? 161 PHE A CB  1 
ATOM 1082 C CG  . PHE A 1 161 ? 125.861 116.981 116.942 1.00 52.92  ? 161 PHE A CG  1 
ATOM 1083 C CD1 . PHE A 1 161 ? 127.035 117.444 116.374 1.00 52.67  ? 161 PHE A CD1 1 
ATOM 1084 C CD2 . PHE A 1 161 ? 124.750 117.801 116.930 1.00 56.90  ? 161 PHE A CD2 1 
ATOM 1085 C CE1 . PHE A 1 161 ? 127.096 118.691 115.793 1.00 47.84  ? 161 PHE A CE1 1 
ATOM 1086 C CE2 . PHE A 1 161 ? 124.804 119.051 116.350 1.00 57.81  ? 161 PHE A CE2 1 
ATOM 1087 C CZ  . PHE A 1 161 ? 125.979 119.497 115.781 1.00 52.45  ? 161 PHE A CZ  1 
ATOM 1088 N N   . GLY A 1 162 ? 125.027 112.521 117.669 1.00 48.50  ? 162 GLY A N   1 
ATOM 1089 C CA  . GLY A 1 162 ? 125.069 111.225 118.328 1.00 51.71  ? 162 GLY A CA  1 
ATOM 1090 C C   . GLY A 1 162 ? 125.787 110.161 117.523 1.00 57.55  ? 162 GLY A C   1 
ATOM 1091 O O   . GLY A 1 162 ? 126.584 109.396 118.070 1.00 57.89  ? 162 GLY A O   1 
ATOM 1092 N N   . SER A 1 163 ? 125.546 110.121 116.209 1.00 65.31  ? 163 SER A N   1 
ATOM 1093 C CA  . SER A 1 163 ? 126.127 109.069 115.380 1.00 65.73  ? 163 SER A CA  1 
ATOM 1094 C C   . SER A 1 163 ? 127.647 109.108 115.432 1.00 65.70  ? 163 SER A C   1 
ATOM 1095 O O   . SER A 1 163 ? 128.305 108.062 115.387 1.00 71.47  ? 163 SER A O   1 
ATOM 1096 C CB  . SER A 1 163 ? 125.637 109.200 113.938 1.00 66.93  ? 163 SER A CB  1 
ATOM 1097 O OG  . SER A 1 163 ? 124.231 109.045 113.859 1.00 63.84  ? 163 SER A OG  1 
ATOM 1098 N N   . LEU A 1 164 ? 128.223 110.302 115.525 1.00 66.89  ? 164 LEU A N   1 
ATOM 1099 C CA  . LEU A 1 164 ? 129.672 110.437 115.550 1.00 71.52  ? 164 LEU A CA  1 
ATOM 1100 C C   . LEU A 1 164 ? 130.227 110.270 116.959 1.00 75.31  ? 164 LEU A C   1 
ATOM 1101 O O   . LEU A 1 164 ? 131.305 109.691 117.133 1.00 77.60  ? 164 LEU A O   1 
ATOM 1102 C CB  . LEU A 1 164 ? 130.092 111.793 114.977 1.00 76.52  ? 164 LEU A CB  1 
ATOM 1103 C CG  . LEU A 1 164 ? 129.612 112.124 113.562 1.00 75.59  ? 164 LEU A CG  1 
ATOM 1104 C CD1 . LEU A 1 164 ? 130.030 113.531 113.171 1.00 72.28  ? 164 LEU A CD1 1 
ATOM 1105 C CD2 . LEU A 1 164 ? 130.135 111.109 112.561 1.00 72.20  ? 164 LEU A CD2 1 
ATOM 1106 N N   . GLY A 1 165 ? 129.517 110.765 117.973 1.00 89.12  ? 165 GLY A N   1 
ATOM 1107 C CA  . GLY A 1 165 ? 130.033 110.730 119.330 1.00 89.98  ? 165 GLY A CA  1 
ATOM 1108 C C   . GLY A 1 165 ? 129.809 109.466 120.142 1.00 89.80  ? 165 GLY A C   1 
ATOM 1109 O O   . GLY A 1 165 ? 130.731 108.995 120.820 1.00 89.12  ? 165 GLY A O   1 
ATOM 1110 N N   . VAL A 1 166 ? 128.583 108.934 120.118 1.00 88.30  ? 166 VAL A N   1 
ATOM 1111 C CA  . VAL A 1 166 ? 128.199 107.883 121.056 1.00 90.50  ? 166 VAL A CA  1 
ATOM 1112 C C   . VAL A 1 166 ? 128.966 106.591 120.793 1.00 91.56  ? 166 VAL A C   1 
ATOM 1113 O O   . VAL A 1 166 ? 129.318 105.870 121.730 1.00 90.01  ? 166 VAL A O   1 
ATOM 1114 C CB  . VAL A 1 166 ? 126.675 107.661 120.999 1.00 90.22  ? 166 VAL A CB  1 
ATOM 1115 C CG1 . VAL A 1 166 ? 126.264 106.478 121.865 1.00 89.85  ? 166 VAL A CG1 1 
ATOM 1116 C CG2 . VAL A 1 166 ? 125.940 108.920 121.430 1.00 88.52  ? 166 VAL A CG2 1 
ATOM 1117 N N   . GLY A 1 167 ? 129.230 106.268 119.525 1.00 97.15  ? 167 GLY A N   1 
ATOM 1118 C CA  . GLY A 1 167 ? 130.018 105.078 119.229 1.00 97.98  ? 167 GLY A CA  1 
ATOM 1119 C C   . GLY A 1 167 ? 131.447 105.154 119.735 1.00 97.52  ? 167 GLY A C   1 
ATOM 1120 O O   . GLY A 1 167 ? 131.989 104.175 120.258 1.00 96.77  ? 167 GLY A O   1 
ATOM 1121 N N   . TYR A 1 168 ? 132.045 106.343 119.676 1.00 102.82 ? 168 TYR A N   1 
ATOM 1122 C CA  . TYR A 1 168 ? 133.389 106.517 120.213 1.00 104.32 ? 168 TYR A CA  1 
ATOM 1123 C C   . TYR A 1 168 ? 133.386 106.497 121.736 1.00 104.20 ? 168 TYR A C   1 
ATOM 1124 O O   . TYR A 1 168 ? 134.304 105.946 122.355 1.00 102.92 ? 168 TYR A O   1 
ATOM 1125 C CB  . TYR A 1 168 ? 133.991 107.817 119.679 1.00 103.98 ? 168 TYR A CB  1 
ATOM 1126 C CG  . TYR A 1 168 ? 135.441 108.037 120.042 1.00 105.50 ? 168 TYR A CG  1 
ATOM 1127 C CD1 . TYR A 1 168 ? 136.366 107.005 119.938 1.00 104.94 ? 168 TYR A CD1 1 
ATOM 1128 C CD2 . TYR A 1 168 ? 135.894 109.284 120.453 1.00 105.00 ? 168 TYR A CD2 1 
ATOM 1129 C CE1 . TYR A 1 168 ? 137.695 107.201 120.263 1.00 105.70 ? 168 TYR A CE1 1 
ATOM 1130 C CE2 . TYR A 1 168 ? 137.223 109.492 120.771 1.00 104.98 ? 168 TYR A CE2 1 
ATOM 1131 C CZ  . TYR A 1 168 ? 138.119 108.446 120.677 1.00 106.08 ? 168 TYR A CZ  1 
ATOM 1132 O OH  . TYR A 1 168 ? 139.444 108.647 120.988 1.00 104.69 ? 168 TYR A OH  1 
ATOM 1133 N N   . PHE A 1 169 ? 132.375 107.105 122.357 1.00 107.70 ? 169 PHE A N   1 
ATOM 1134 C CA  . PHE A 1 169 ? 132.229 106.989 123.807 1.00 108.43 ? 169 PHE A CA  1 
ATOM 1135 C C   . PHE A 1 169 ? 132.045 105.537 124.245 1.00 106.04 ? 169 PHE A C   1 
ATOM 1136 O O   . PHE A 1 169 ? 132.634 105.104 125.243 1.00 103.39 ? 169 PHE A O   1 
ATOM 1137 C CB  . PHE A 1 169 ? 131.057 107.847 124.281 1.00 108.41 ? 169 PHE A CB  1 
ATOM 1138 C CG  . PHE A 1 169 ? 130.793 107.754 125.756 1.00 108.83 ? 169 PHE A CG  1 
ATOM 1139 C CD1 . PHE A 1 169 ? 131.789 108.051 126.670 1.00 107.66 ? 169 PHE A CD1 1 
ATOM 1140 C CD2 . PHE A 1 169 ? 129.547 107.380 126.228 1.00 109.41 ? 169 PHE A CD2 1 
ATOM 1141 C CE1 . PHE A 1 169 ? 131.550 107.969 128.028 1.00 108.95 ? 169 PHE A CE1 1 
ATOM 1142 C CE2 . PHE A 1 169 ? 129.300 107.297 127.585 1.00 108.95 ? 169 PHE A CE2 1 
ATOM 1143 C CZ  . PHE A 1 169 ? 130.303 107.592 128.487 1.00 109.61 ? 169 PHE A CZ  1 
ATOM 1144 N N   . ALA A 1 170 ? 131.228 104.771 123.516 1.00 105.64 ? 170 ALA A N   1 
ATOM 1145 C CA  . ALA A 1 170 ? 131.045 103.349 123.797 1.00 106.73 ? 170 ALA A CA  1 
ATOM 1146 C C   . ALA A 1 170 ? 132.298 102.527 123.534 1.00 107.02 ? 170 ALA A C   1 
ATOM 1147 O O   . ALA A 1 170 ? 132.440 101.441 124.104 1.00 106.84 ? 170 ALA A O   1 
ATOM 1148 C CB  . ALA A 1 170 ? 129.884 102.795 122.970 1.00 106.39 ? 170 ALA A CB  1 
ATOM 1149 N N   . ASP A 1 171 ? 133.207 103.016 122.691 1.00 108.35 ? 171 ASP A N   1 
ATOM 1150 C CA  . ASP A 1 171 ? 134.477 102.319 122.513 1.00 107.50 ? 171 ASP A CA  1 
ATOM 1151 C C   . ASP A 1 171 ? 135.481 102.692 123.597 1.00 106.49 ? 171 ASP A C   1 
ATOM 1152 O O   . ASP A 1 171 ? 136.326 101.869 123.964 1.00 106.14 ? 171 ASP A O   1 
ATOM 1153 C CB  . ASP A 1 171 ? 135.057 102.619 121.131 1.00 109.34 ? 171 ASP A CB  1 
ATOM 1154 C CG  . ASP A 1 171 ? 136.138 101.634 120.727 1.00 110.19 ? 171 ASP A CG  1 
ATOM 1155 O OD1 . ASP A 1 171 ? 136.145 100.506 121.264 1.00 109.10 ? 171 ASP A OD1 1 
ATOM 1156 O OD2 . ASP A 1 171 ? 136.979 101.987 119.874 1.00 109.85 ? 171 ASP A OD2 1 
ATOM 1157 N N   . ARG A 1 172 ? 135.405 103.920 124.112 1.00 110.59 ? 172 ARG A N   1 
ATOM 1158 C CA  . ARG A 1 172 ? 136.287 104.352 125.191 1.00 110.42 ? 172 ARG A CA  1 
ATOM 1159 C C   . ARG A 1 172 ? 135.811 103.853 126.552 1.00 110.32 ? 172 ARG A C   1 
ATOM 1160 O O   . ARG A 1 172 ? 136.619 103.378 127.357 1.00 108.02 ? 172 ARG A O   1 
ATOM 1161 C CB  . ARG A 1 172 ? 136.397 105.877 125.201 1.00 111.77 ? 172 ARG A CB  1 
ATOM 1162 C CG  . ARG A 1 172 ? 137.128 106.461 124.006 1.00 109.72 ? 172 ARG A CG  1 
ATOM 1163 C CD  . ARG A 1 172 ? 136.817 107.940 123.848 1.00 109.62 ? 172 ARG A CD  1 
ATOM 1164 N NE  . ARG A 1 172 ? 137.325 108.734 124.960 1.00 110.65 ? 172 ARG A NE  1 
ATOM 1165 C CZ  . ARG A 1 172 ? 136.902 109.954 125.262 1.00 109.96 ? 172 ARG A CZ  1 
ATOM 1166 N NH1 . ARG A 1 172 ? 135.958 110.553 124.556 1.00 109.65 ? 172 ARG A NH1 1 
ATOM 1167 N NH2 . ARG A 1 172 ? 137.442 110.590 126.298 1.00 108.12 ? 172 ARG A NH2 1 
ATOM 1168 N N   . PHE A 1 173 ? 134.512 103.952 126.826 1.00 108.21 ? 173 PHE A N   1 
ATOM 1169 C CA  . PHE A 1 173 ? 133.940 103.473 128.075 1.00 108.36 ? 173 PHE A CA  1 
ATOM 1170 C C   . PHE A 1 173 ? 133.473 102.022 127.917 1.00 107.15 ? 173 PHE A C   1 
ATOM 1171 O O   . PHE A 1 173 ? 133.498 101.450 126.825 1.00 105.38 ? 173 PHE A O   1 
ATOM 1172 C CB  . PHE A 1 173 ? 132.795 104.399 128.500 1.00 107.51 ? 173 PHE A CB  1 
ATOM 1173 C CG  . PHE A 1 173 ? 132.275 104.146 129.888 1.00 107.82 ? 173 PHE A CG  1 
ATOM 1174 C CD1 . PHE A 1 173 ? 133.147 103.895 130.936 1.00 107.14 ? 173 PHE A CD1 1 
ATOM 1175 C CD2 . PHE A 1 173 ? 130.916 104.192 130.151 1.00 108.00 ? 173 PHE A CD2 1 
ATOM 1176 C CE1 . PHE A 1 173 ? 132.671 103.674 132.215 1.00 106.77 ? 173 PHE A CE1 1 
ATOM 1177 C CE2 . PHE A 1 173 ? 130.435 103.974 131.428 1.00 107.04 ? 173 PHE A CE2 1 
ATOM 1178 C CZ  . PHE A 1 173 ? 131.314 103.713 132.461 1.00 106.80 ? 173 PHE A CZ  1 
ATOM 1179 N N   . GLY A 1 174 ? 133.046 101.424 129.026 1.00 103.77 ? 174 GLY A N   1 
ATOM 1180 C CA  . GLY A 1 174 ? 132.521 100.067 128.978 1.00 105.40 ? 174 GLY A CA  1 
ATOM 1181 C C   . GLY A 1 174 ? 131.182 99.983  128.264 1.00 105.67 ? 174 GLY A C   1 
ATOM 1182 O O   . GLY A 1 174 ? 130.254 100.749 128.550 1.00 105.68 ? 174 GLY A O   1 
ATOM 1183 N N   . ARG A 1 175 ? 131.086 99.040  127.322 1.00 95.93  ? 175 ARG A N   1 
ATOM 1184 C CA  . ARG A 1 175 ? 129.938 98.943  126.422 1.00 96.91  ? 175 ARG A CA  1 
ATOM 1185 C C   . ARG A 1 175 ? 128.620 98.779  127.175 1.00 97.96  ? 175 ARG A C   1 
ATOM 1186 O O   . ARG A 1 175 ? 127.626 99.449  126.861 1.00 97.84  ? 175 ARG A O   1 
ATOM 1187 C CB  . ARG A 1 175 ? 130.153 97.780  125.456 1.00 96.91  ? 175 ARG A CB  1 
ATOM 1188 C CG  . ARG A 1 175 ? 129.224 97.760  124.259 1.00 98.59  ? 175 ARG A CG  1 
ATOM 1189 C CD  . ARG A 1 175 ? 129.426 96.483  123.461 1.00 99.11  ? 175 ARG A CD  1 
ATOM 1190 N NE  . ARG A 1 175 ? 128.776 96.533  122.158 1.00 98.27  ? 175 ARG A NE  1 
ATOM 1191 C CZ  . ARG A 1 175 ? 128.645 95.491  121.348 1.00 98.96  ? 175 ARG A CZ  1 
ATOM 1192 N NH1 . ARG A 1 175 ? 128.955 94.267  121.742 1.00 97.62  ? 175 ARG A NH1 1 
ATOM 1193 N NH2 . ARG A 1 175 ? 128.144 95.676  120.131 1.00 98.12  ? 175 ARG A NH2 1 
ATOM 1194 N N   . LYS A 1 176 ? 128.603 97.917  128.196 1.00 90.58  ? 176 LYS A N   1 
ATOM 1195 C CA  . LYS A 1 176 ? 127.376 97.669  128.949 1.00 90.50  ? 176 LYS A CA  1 
ATOM 1196 C C   . LYS A 1 176 ? 126.977 98.878  129.783 1.00 90.73  ? 176 LYS A C   1 
ATOM 1197 O O   . LYS A 1 176 ? 125.814 99.298  129.764 1.00 88.57  ? 176 LYS A O   1 
ATOM 1198 C CB  . LYS A 1 176 ? 127.551 96.438  129.840 1.00 88.96  ? 176 LYS A CB  1 
ATOM 1199 C CG  . LYS A 1 176 ? 127.931 95.167  129.092 1.00 91.06  ? 176 LYS A CG  1 
ATOM 1200 C CD  . LYS A 1 176 ? 126.941 94.832  127.986 1.00 91.69  ? 176 LYS A CD  1 
ATOM 1201 C CE  . LYS A 1 176 ? 125.540 94.611  128.533 1.00 89.27  ? 176 LYS A CE  1 
ATOM 1202 N NZ  . LYS A 1 176 ? 124.596 94.180  127.466 1.00 87.86  ? 176 LYS A NZ  1 
ATOM 1203 N N   . LEU A 1 177 ? 127.916 99.426  130.554 1.00 89.99  ? 177 LEU A N   1 
ATOM 1204 C CA  . LEU A 1 177 ? 127.618 100.616 131.343 1.00 88.88  ? 177 LEU A CA  1 
ATOM 1205 C C   . LEU A 1 177 ? 127.206 101.776 130.447 1.00 90.90  ? 177 LEU A C   1 
ATOM 1206 O O   . LEU A 1 177 ? 126.292 102.536 130.783 1.00 92.98  ? 177 LEU A O   1 
ATOM 1207 C CB  . LEU A 1 177 ? 128.826 100.994 132.199 1.00 89.76  ? 177 LEU A CB  1 
ATOM 1208 C CG  . LEU A 1 177 ? 129.240 99.977  133.263 1.00 91.99  ? 177 LEU A CG  1 
ATOM 1209 C CD1 . LEU A 1 177 ? 130.420 100.498 134.070 1.00 90.89  ? 177 LEU A CD1 1 
ATOM 1210 C CD2 . LEU A 1 177 ? 128.065 99.645  134.172 1.00 90.99  ? 177 LEU A CD2 1 
ATOM 1211 N N   . CYS A 1 178 ? 127.880 101.928 129.305 1.00 83.63  ? 178 CYS A N   1 
ATOM 1212 C CA  . CYS A 1 178 ? 127.512 102.943 128.320 1.00 81.91  ? 178 CYS A CA  1 
ATOM 1213 C C   . CYS A 1 178 ? 126.064 102.798 127.856 1.00 82.71  ? 178 CYS A C   1 
ATOM 1214 O O   . CYS A 1 178 ? 125.292 103.766 127.887 1.00 83.52  ? 178 CYS A O   1 
ATOM 1215 C CB  . CYS A 1 178 ? 128.462 102.876 127.124 1.00 80.97  ? 178 CYS A CB  1 
ATOM 1216 S SG  . CYS A 1 178 ? 128.227 104.193 125.912 1.00 94.49  ? 178 CYS A SG  1 
ATOM 1217 N N   . LEU A 1 179 ? 125.683 101.601 127.400 1.00 65.34  ? 179 LEU A N   1 
ATOM 1218 C CA  . LEU A 1 179 ? 124.301 101.389 126.972 1.00 66.64  ? 179 LEU A CA  1 
ATOM 1219 C C   . LEU A 1 179 ? 123.307 101.612 128.110 1.00 68.91  ? 179 LEU A C   1 
ATOM 1220 O O   . LEU A 1 179 ? 122.257 102.236 127.906 1.00 72.32  ? 179 LEU A O   1 
ATOM 1221 C CB  . LEU A 1 179 ? 124.154 99.980  126.389 1.00 65.56  ? 179 LEU A CB  1 
ATOM 1222 C CG  . LEU A 1 179 ? 122.855 99.573  125.685 1.00 64.35  ? 179 LEU A CG  1 
ATOM 1223 C CD1 . LEU A 1 179 ? 123.149 98.547  124.609 1.00 64.22  ? 179 LEU A CD1 1 
ATOM 1224 C CD2 . LEU A 1 179 ? 121.841 99.008  126.664 1.00 66.61  ? 179 LEU A CD2 1 
ATOM 1225 N N   . LEU A 1 180 ? 123.613 101.121 129.313 1.00 61.07  ? 180 LEU A N   1 
ATOM 1226 C CA  . LEU A 1 180 ? 122.694 101.310 130.433 1.00 61.39  ? 180 LEU A CA  1 
ATOM 1227 C C   . LEU A 1 180 ? 122.512 102.791 130.748 1.00 62.82  ? 180 LEU A C   1 
ATOM 1228 O O   . LEU A 1 180 ? 121.386 103.256 130.984 1.00 61.64  ? 180 LEU A O   1 
ATOM 1229 C CB  . LEU A 1 180 ? 123.208 100.558 131.661 1.00 63.79  ? 180 LEU A CB  1 
ATOM 1230 C CG  . LEU A 1 180 ? 122.344 100.590 132.922 1.00 63.14  ? 180 LEU A CG  1 
ATOM 1231 C CD1 . LEU A 1 180 ? 121.010 99.917  132.665 1.00 61.89  ? 180 LEU A CD1 1 
ATOM 1232 C CD2 . LEU A 1 180 ? 123.062 99.927  134.086 1.00 61.52  ? 180 LEU A CD2 1 
ATOM 1233 N N   . GLY A 1 181 ? 123.607 103.551 130.712 1.00 50.27  ? 181 GLY A N   1 
ATOM 1234 C CA  . GLY A 1 181 ? 123.523 104.978 130.957 1.00 39.54  ? 181 GLY A CA  1 
ATOM 1235 C C   . GLY A 1 181 ? 122.710 105.699 129.904 1.00 44.49  ? 181 GLY A C   1 
ATOM 1236 O O   . GLY A 1 181 ? 121.884 106.554 130.227 1.00 47.56  ? 181 GLY A O   1 
ATOM 1237 N N   . THR A 1 182 ? 122.934 105.372 128.629 1.00 47.74  ? 182 THR A N   1 
ATOM 1238 C CA  . THR A 1 182 ? 122.219 106.093 127.584 1.00 46.31  ? 182 THR A CA  1 
ATOM 1239 C C   . THR A 1 182 ? 120.757 105.679 127.495 1.00 43.70  ? 182 THR A C   1 
ATOM 1240 O O   . THR A 1 182 ? 119.924 106.494 127.090 1.00 47.37  ? 182 THR A O   1 
ATOM 1241 C CB  . THR A 1 182 ? 122.899 105.882 126.230 1.00 46.03  ? 182 THR A CB  1 
ATOM 1242 O OG1 . THR A 1 182 ? 122.916 104.486 125.913 1.00 45.44  ? 182 THR A OG1 1 
ATOM 1243 C CG2 . THR A 1 182 ? 124.325 106.407 126.262 1.00 46.85  ? 182 THR A CG2 1 
ATOM 1244 N N   . VAL A 1 183 ? 120.399 104.514 128.036 1.00 43.56  ? 183 VAL A N   1 
ATOM 1245 C CA  . VAL A 1 183 ? 118.988 104.141 128.097 1.00 42.98  ? 183 VAL A CA  1 
ATOM 1246 C C   . VAL A 1 183 ? 118.301 104.829 129.269 1.00 43.06  ? 183 VAL A C   1 
ATOM 1247 O O   . VAL A 1 183 ? 117.164 105.304 129.146 1.00 39.44  ? 183 VAL A O   1 
ATOM 1248 C CB  . VAL A 1 183 ? 118.841 102.610 128.164 1.00 46.79  ? 183 VAL A CB  1 
ATOM 1249 C CG1 . VAL A 1 183 ? 117.399 102.223 128.443 1.00 47.22  ? 183 VAL A CG1 1 
ATOM 1250 C CG2 . VAL A 1 183 ? 119.303 101.979 126.864 1.00 50.26  ? 183 VAL A CG2 1 
ATOM 1251 N N   . LEU A 1 184 ? 118.983 104.924 130.412 1.00 40.34  ? 184 LEU A N   1 
ATOM 1252 C CA  . LEU A 1 184 ? 118.430 105.687 131.526 1.00 37.87  ? 184 LEU A CA  1 
ATOM 1253 C C   . LEU A 1 184 ? 118.271 107.164 131.169 1.00 44.33  ? 184 LEU A C   1 
ATOM 1254 O O   . LEU A 1 184 ? 117.243 107.779 131.485 1.00 47.54  ? 184 LEU A O   1 
ATOM 1255 C CB  . LEU A 1 184 ? 119.325 105.522 132.754 1.00 37.97  ? 184 LEU A CB  1 
ATOM 1256 C CG  . LEU A 1 184 ? 118.980 106.309 134.017 1.00 38.48  ? 184 LEU A CG  1 
ATOM 1257 C CD1 . LEU A 1 184 ? 117.578 105.986 134.492 1.00 43.84  ? 184 LEU A CD1 1 
ATOM 1258 C CD2 . LEU A 1 184 ? 119.994 106.007 135.104 1.00 46.00  ? 184 LEU A CD2 1 
ATOM 1259 N N   . VAL A 1 185 ? 119.256 107.739 130.473 1.00 38.73  ? 185 VAL A N   1 
ATOM 1260 C CA  . VAL A 1 185 ? 119.144 109.128 130.035 1.00 26.06  ? 185 VAL A CA  1 
ATOM 1261 C C   . VAL A 1 185 ? 118.053 109.300 128.985 1.00 28.38  ? 185 VAL A C   1 
ATOM 1262 O O   . VAL A 1 185 ? 117.322 110.298 129.010 1.00 37.18  ? 185 VAL A O   1 
ATOM 1263 C CB  . VAL A 1 185 ? 120.504 109.633 129.520 1.00 31.40  ? 185 VAL A CB  1 
ATOM 1264 C CG1 . VAL A 1 185 ? 120.365 111.020 128.914 1.00 34.75  ? 185 VAL A CG1 1 
ATOM 1265 C CG2 . VAL A 1 185 ? 121.513 109.663 130.651 1.00 38.76  ? 185 VAL A CG2 1 
ATOM 1266 N N   . ASN A 1 186 ? 117.857 108.313 128.104 1.00 29.22  ? 186 ASN A N   1 
ATOM 1267 C CA  . ASN A 1 186 ? 116.789 108.430 127.117 1.00 30.03  ? 186 ASN A CA  1 
ATOM 1268 C C   . ASN A 1 186 ? 115.423 108.410 127.788 1.00 41.05  ? 186 ASN A C   1 
ATOM 1269 O O   . ASN A 1 186 ? 114.560 109.244 127.480 1.00 39.14  ? 186 ASN A O   1 
ATOM 1270 C CB  . ASN A 1 186 ? 116.908 107.305 126.092 1.00 27.85  ? 186 ASN A CB  1 
ATOM 1271 C CG  . ASN A 1 186 ? 115.931 107.451 124.948 1.00 35.89  ? 186 ASN A CG  1 
ATOM 1272 O OD1 . ASN A 1 186 ? 115.532 108.558 124.596 1.00 39.69  ? 186 ASN A OD1 1 
ATOM 1273 N ND2 . ASN A 1 186 ? 115.544 106.330 124.357 1.00 36.77  ? 186 ASN A ND2 1 
ATOM 1274 N N   . ALA A 1 187 ? 115.224 107.496 128.739 1.00 40.93  ? 187 ALA A N   1 
ATOM 1275 C CA  . ALA A 1 187 ? 113.951 107.429 129.449 1.00 29.24  ? 187 ALA A CA  1 
ATOM 1276 C C   . ALA A 1 187 ? 113.683 108.718 130.220 1.00 31.96  ? 187 ALA A C   1 
ATOM 1277 O O   . ALA A 1 187 ? 112.601 109.312 130.106 1.00 37.06  ? 187 ALA A O   1 
ATOM 1278 C CB  . ALA A 1 187 ? 113.940 106.224 130.388 1.00 29.74  ? 187 ALA A CB  1 
ATOM 1279 N N   . VAL A 1 188 ? 114.659 109.164 131.019 1.00 28.47  ? 188 VAL A N   1 
ATOM 1280 C CA  . VAL A 1 188 ? 114.443 110.339 131.861 1.00 20.21  ? 188 VAL A CA  1 
ATOM 1281 C C   . VAL A 1 188 ? 114.204 111.584 131.012 1.00 32.94  ? 188 VAL A C   1 
ATOM 1282 O O   . VAL A 1 188 ? 113.359 112.423 131.348 1.00 32.72  ? 188 VAL A O   1 
ATOM 1283 C CB  . VAL A 1 188 ? 115.626 110.526 132.829 1.00 29.49  ? 188 VAL A CB  1 
ATOM 1284 C CG1 . VAL A 1 188 ? 115.480 111.820 133.607 1.00 29.84  ? 188 VAL A CG1 1 
ATOM 1285 C CG2 . VAL A 1 188 ? 115.713 109.351 133.784 1.00 37.48  ? 188 VAL A CG2 1 
ATOM 1286 N N   . SER A 1 189 ? 114.934 111.733 129.901 1.00 32.36  ? 189 SER A N   1 
ATOM 1287 C CA  . SER A 1 189 ? 114.717 112.893 129.042 1.00 25.26  ? 189 SER A CA  1 
ATOM 1288 C C   . SER A 1 189 ? 113.356 112.836 128.358 1.00 40.05  ? 189 SER A C   1 
ATOM 1289 O O   . SER A 1 189 ? 112.716 113.874 128.154 1.00 37.86  ? 189 SER A O   1 
ATOM 1290 C CB  . SER A 1 189 ? 115.834 112.998 128.006 1.00 19.06  ? 189 SER A CB  1 
ATOM 1291 O OG  . SER A 1 189 ? 115.905 111.825 127.218 1.00 32.63  ? 189 SER A OG  1 
ATOM 1292 N N   . GLY A 1 190 ? 112.902 111.636 127.986 1.00 38.52  ? 190 GLY A N   1 
ATOM 1293 C CA  . GLY A 1 190 ? 111.580 111.506 127.392 1.00 27.61  ? 190 GLY A CA  1 
ATOM 1294 C C   . GLY A 1 190 ? 110.442 111.822 128.346 1.00 25.67  ? 190 GLY A C   1 
ATOM 1295 O O   . GLY A 1 190 ? 109.428 112.398 127.943 1.00 21.41  ? 190 GLY A O   1 
ATOM 1296 N N   . VAL A 1 191 ? 110.588 111.451 129.619 1.00 26.80  ? 191 VAL A N   1 
ATOM 1297 C CA  . VAL A 1 191 ? 109.556 111.768 130.607 1.00 26.16  ? 191 VAL A CA  1 
ATOM 1298 C C   . VAL A 1 191 ? 109.546 113.253 130.967 1.00 35.12  ? 191 VAL A C   1 
ATOM 1299 O O   . VAL A 1 191 ? 108.476 113.867 131.070 1.00 45.17  ? 191 VAL A O   1 
ATOM 1300 C CB  . VAL A 1 191 ? 109.731 110.884 131.855 1.00 30.96  ? 191 VAL A CB  1 
ATOM 1301 C CG1 . VAL A 1 191 ? 108.869 111.392 132.998 1.00 28.17  ? 191 VAL A CG1 1 
ATOM 1302 C CG2 . VAL A 1 191 ? 109.370 109.450 131.527 1.00 29.68  ? 191 VAL A CG2 1 
ATOM 1303 N N   . LEU A 1 192 ? 110.720 113.857 131.165 1.00 27.43  ? 192 LEU A N   1 
ATOM 1304 C CA  . LEU A 1 192 ? 110.783 115.281 131.501 1.00 25.56  ? 192 LEU A CA  1 
ATOM 1305 C C   . LEU A 1 192 ? 110.217 116.184 130.409 1.00 24.48  ? 192 LEU A C   1 
ATOM 1306 O O   . LEU A 1 192 ? 109.655 117.239 130.720 1.00 26.08  ? 192 LEU A O   1 
ATOM 1307 C CB  . LEU A 1 192 ? 112.222 115.687 131.817 1.00 29.71  ? 192 LEU A CB  1 
ATOM 1308 C CG  . LEU A 1 192 ? 112.775 115.235 133.169 1.00 34.10  ? 192 LEU A CG  1 
ATOM 1309 C CD1 . LEU A 1 192 ? 114.276 115.446 133.236 1.00 30.88  ? 192 LEU A CD1 1 
ATOM 1310 C CD2 . LEU A 1 192 ? 112.082 115.982 134.292 1.00 30.24  ? 192 LEU A CD2 1 
ATOM 1311 N N   . MET A 1 193 ? 110.365 115.809 129.136 1.00 28.06  ? 193 MET A N   1 
ATOM 1312 C CA  . MET A 1 193 ? 109.803 116.614 128.051 1.00 29.47  ? 193 MET A CA  1 
ATOM 1313 C C   . MET A 1 193 ? 108.292 116.798 128.175 1.00 38.76  ? 193 MET A C   1 
ATOM 1314 O O   . MET A 1 193 ? 107.766 117.849 127.791 1.00 36.40  ? 193 MET A O   1 
ATOM 1315 C CB  . MET A 1 193 ? 110.153 115.995 126.697 1.00 24.12  ? 193 MET A CB  1 
ATOM 1316 C CG  . MET A 1 193 ? 109.475 116.674 125.517 1.00 32.41  ? 193 MET A CG  1 
ATOM 1317 S SD  . MET A 1 193 ? 110.397 116.546 123.977 1.00 39.38  ? 193 MET A SD  1 
ATOM 1318 C CE  . MET A 1 193 ? 110.476 114.774 123.781 1.00 30.87  ? 193 MET A CE  1 
ATOM 1319 N N   . ALA A 1 194 ? 107.580 115.806 128.713 1.00 46.31  ? 194 ALA A N   1 
ATOM 1320 C CA  . ALA A 1 194 ? 106.148 115.965 128.959 1.00 20.07  ? 194 ALA A CA  1 
ATOM 1321 C C   . ALA A 1 194 ? 105.844 117.102 129.929 1.00 28.97  ? 194 ALA A C   1 
ATOM 1322 O O   . ALA A 1 194 ? 104.752 117.676 129.881 1.00 36.72  ? 194 ALA A O   1 
ATOM 1323 C CB  . ALA A 1 194 ? 105.562 114.657 129.486 1.00 16.78  ? 194 ALA A CB  1 
ATOM 1324 N N   . PHE A 1 195 ? 106.781 117.440 130.814 1.00 27.66  ? 195 PHE A N   1 
ATOM 1325 C CA  . PHE A 1 195 ? 106.612 118.535 131.761 1.00 27.52  ? 195 PHE A CA  1 
ATOM 1326 C C   . PHE A 1 195 ? 107.317 119.815 131.324 1.00 38.05  ? 195 PHE A C   1 
ATOM 1327 O O   . PHE A 1 195 ? 107.487 120.723 132.144 1.00 42.48  ? 195 PHE A O   1 
ATOM 1328 C CB  . PHE A 1 195 ? 107.113 118.122 133.147 1.00 32.63  ? 195 PHE A CB  1 
ATOM 1329 C CG  . PHE A 1 195 ? 106.408 116.928 133.720 1.00 38.54  ? 195 PHE A CG  1 
ATOM 1330 C CD1 . PHE A 1 195 ? 105.188 117.069 134.357 1.00 33.64  ? 195 PHE A CD1 1 
ATOM 1331 C CD2 . PHE A 1 195 ? 106.967 115.665 133.627 1.00 38.51  ? 195 PHE A CD2 1 
ATOM 1332 C CE1 . PHE A 1 195 ? 104.538 115.974 134.888 1.00 32.15  ? 195 PHE A CE1 1 
ATOM 1333 C CE2 . PHE A 1 195 ? 106.320 114.566 134.157 1.00 32.17  ? 195 PHE A CE2 1 
ATOM 1334 C CZ  . PHE A 1 195 ? 105.104 114.722 134.787 1.00 28.16  ? 195 PHE A CZ  1 
ATOM 1335 N N   . SER A 1 196 ? 107.751 119.894 130.069 1.00 42.12  ? 196 SER A N   1 
ATOM 1336 C CA  . SER A 1 196 ? 108.414 121.084 129.554 1.00 33.08  ? 196 SER A CA  1 
ATOM 1337 C C   . SER A 1 196 ? 107.569 122.336 129.789 1.00 32.27  ? 196 SER A C   1 
ATOM 1338 O O   . SER A 1 196 ? 106.390 122.364 129.409 1.00 33.54  ? 196 SER A O   1 
ATOM 1339 C CB  . SER A 1 196 ? 108.690 120.922 128.059 1.00 32.74  ? 196 SER A CB  1 
ATOM 1340 O OG  . SER A 1 196 ? 109.467 121.997 127.565 1.00 36.53  ? 196 SER A OG  1 
ATOM 1341 N N   . PRO A 1 197 ? 108.130 123.384 130.405 1.00 31.87  ? 197 PRO A N   1 
ATOM 1342 C CA  . PRO A 1 197 ? 107.344 124.600 130.660 1.00 29.66  ? 197 PRO A CA  1 
ATOM 1343 C C   . PRO A 1 197 ? 107.297 125.567 129.487 1.00 34.15  ? 197 PRO A C   1 
ATOM 1344 O O   . PRO A 1 197 ? 106.405 126.425 129.458 1.00 40.88  ? 197 PRO A O   1 
ATOM 1345 C CB  . PRO A 1 197 ? 108.056 125.224 131.864 1.00 23.92  ? 197 PRO A CB  1 
ATOM 1346 C CG  . PRO A 1 197 ? 109.471 124.821 131.676 1.00 32.88  ? 197 PRO A CG  1 
ATOM 1347 C CD  . PRO A 1 197 ? 109.438 123.430 131.081 1.00 32.12  ? 197 PRO A CD  1 
ATOM 1348 N N   . ASN A 1 198 ? 108.218 125.463 128.529 1.00 35.98  ? 198 ASN A N   1 
ATOM 1349 C CA  . ASN A 1 198 ? 108.260 126.373 127.393 1.00 25.87  ? 198 ASN A CA  1 
ATOM 1350 C C   . ASN A 1 198 ? 108.881 125.661 126.196 1.00 32.97  ? 198 ASN A C   1 
ATOM 1351 O O   . ASN A 1 198 ? 109.370 124.534 126.300 1.00 38.26  ? 198 ASN A O   1 
ATOM 1352 C CB  . ASN A 1 198 ? 108.996 127.675 127.746 1.00 30.43  ? 198 ASN A CB  1 
ATOM 1353 C CG  . ASN A 1 198 ? 110.404 127.443 128.267 1.00 39.10  ? 198 ASN A CG  1 
ATOM 1354 O OD1 . ASN A 1 198 ? 111.100 126.520 127.848 1.00 41.96  ? 198 ASN A OD1 1 
ATOM 1355 N ND2 . ASN A 1 198 ? 110.829 128.293 129.193 1.00 36.50  ? 198 ASN A ND2 1 
ATOM 1356 N N   . TYR A 1 199 ? 108.837 126.336 125.045 1.00 24.02  ? 199 TYR A N   1 
ATOM 1357 C CA  . TYR A 1 199 ? 109.327 125.753 123.797 1.00 25.01  ? 199 TYR A CA  1 
ATOM 1358 C C   . TYR A 1 199 ? 110.844 125.560 123.789 1.00 39.21  ? 199 TYR A C   1 
ATOM 1359 O O   . TYR A 1 199 ? 111.342 124.578 123.224 1.00 39.54  ? 199 TYR A O   1 
ATOM 1360 C CB  . TYR A 1 199 ? 108.890 126.641 122.630 1.00 18.12  ? 199 TYR A CB  1 
ATOM 1361 C CG  . TYR A 1 199 ? 109.031 126.022 121.259 1.00 28.86  ? 199 TYR A CG  1 
ATOM 1362 C CD1 . TYR A 1 199 ? 108.360 124.853 120.934 1.00 35.44  ? 199 TYR A CD1 1 
ATOM 1363 C CD2 . TYR A 1 199 ? 109.819 126.617 120.284 1.00 22.82  ? 199 TYR A CD2 1 
ATOM 1364 C CE1 . TYR A 1 199 ? 108.477 124.287 119.682 1.00 32.51  ? 199 TYR A CE1 1 
ATOM 1365 C CE2 . TYR A 1 199 ? 109.944 126.057 119.029 1.00 18.70  ? 199 TYR A CE2 1 
ATOM 1366 C CZ  . TYR A 1 199 ? 109.270 124.894 118.735 1.00 30.90  ? 199 TYR A CZ  1 
ATOM 1367 O OH  . TYR A 1 199 ? 109.389 124.331 117.487 1.00 37.99  ? 199 TYR A OH  1 
ATOM 1368 N N   . MET A 1 200 ? 111.596 126.477 124.405 1.00 33.37  ? 200 MET A N   1 
ATOM 1369 C CA  . MET A 1 200 ? 113.051 126.331 124.479 1.00 27.65  ? 200 MET A CA  1 
ATOM 1370 C C   . MET A 1 200 ? 113.458 125.052 125.205 1.00 36.36  ? 200 MET A C   1 
ATOM 1371 O O   . MET A 1 200 ? 114.312 124.288 124.729 1.00 36.73  ? 200 MET A O   1 
ATOM 1372 C CB  . MET A 1 200 ? 113.659 127.554 125.164 1.00 33.23  ? 200 MET A CB  1 
ATOM 1373 C CG  . MET A 1 200 ? 114.032 128.679 124.214 1.00 41.49  ? 200 MET A CG  1 
ATOM 1374 S SD  . MET A 1 200 ? 115.321 128.209 123.045 1.00 64.00  ? 200 MET A SD  1 
ATOM 1375 C CE  . MET A 1 200 ? 114.394 128.177 121.514 1.00 36.85  ? 200 MET A CE  1 
ATOM 1376 N N   . SER A 1 201 ? 112.869 124.814 126.376 1.00 36.90  ? 201 SER A N   1 
ATOM 1377 C CA  . SER A 1 201 ? 113.197 123.619 127.142 1.00 33.59  ? 201 SER A CA  1 
ATOM 1378 C C   . SER A 1 201 ? 112.801 122.358 126.387 1.00 36.13  ? 201 SER A C   1 
ATOM 1379 O O   . SER A 1 201 ? 113.528 121.357 126.409 1.00 42.67  ? 201 SER A O   1 
ATOM 1380 C CB  . SER A 1 201 ? 112.514 123.673 128.504 1.00 28.20  ? 201 SER A CB  1 
ATOM 1381 O OG  . SER A 1 201 ? 111.115 123.815 128.351 1.00 28.60  ? 201 SER A OG  1 
ATOM 1382 N N   . MET A 1 202 ? 111.632 122.375 125.743 1.00 34.34  ? 202 MET A N   1 
ATOM 1383 C CA  . MET A 1 202 ? 111.249 121.260 124.886 1.00 30.38  ? 202 MET A CA  1 
ATOM 1384 C C   . MET A 1 202 ? 112.253 121.022 123.767 1.00 36.41  ? 202 MET A C   1 
ATOM 1385 O O   . MET A 1 202 ? 112.525 119.867 123.421 1.00 46.11  ? 202 MET A O   1 
ATOM 1386 C CB  . MET A 1 202 ? 109.863 121.515 124.297 1.00 30.18  ? 202 MET A CB  1 
ATOM 1387 C CG  . MET A 1 202 ? 109.210 120.289 123.706 1.00 34.80  ? 202 MET A CG  1 
ATOM 1388 S SD  . MET A 1 202 ? 107.479 120.555 123.299 1.00 54.72  ? 202 MET A SD  1 
ATOM 1389 C CE  . MET A 1 202 ? 106.937 118.863 123.095 1.00 44.35  ? 202 MET A CE  1 
ATOM 1390 N N   . LEU A 1 203 ? 112.866 122.080 123.231 1.00 29.19  ? 203 LEU A N   1 
ATOM 1391 C CA  . LEU A 1 203 ? 113.847 121.864 122.172 1.00 27.85  ? 203 LEU A CA  1 
ATOM 1392 C C   . LEU A 1 203 ? 115.165 121.331 122.715 1.00 35.96  ? 203 LEU A C   1 
ATOM 1393 O O   . LEU A 1 203 ? 115.836 120.535 122.044 1.00 43.78  ? 203 LEU A O   1 
ATOM 1394 C CB  . LEU A 1 203 ? 114.092 123.162 121.401 1.00 30.63  ? 203 LEU A CB  1 
ATOM 1395 C CG  . LEU A 1 203 ? 112.996 123.627 120.443 1.00 31.09  ? 203 LEU A CG  1 
ATOM 1396 C CD1 . LEU A 1 203 ? 113.470 124.829 119.648 1.00 29.75  ? 203 LEU A CD1 1 
ATOM 1397 C CD2 . LEU A 1 203 ? 112.579 122.500 119.515 1.00 31.21  ? 203 LEU A CD2 1 
ATOM 1398 N N   . LEU A 1 204 ? 115.483 121.645 123.970 1.00 35.67  ? 204 LEU A N   1 
ATOM 1399 C CA  . LEU A 1 204 ? 116.704 121.090 124.546 1.00 24.17  ? 204 LEU A CA  1 
ATOM 1400 C C   . LEU A 1 204 ? 116.519 119.629 124.936 1.00 33.92  ? 204 LEU A C   1 
ATOM 1401 O O   . LEU A 1 204 ? 117.433 118.814 124.752 1.00 41.23  ? 204 LEU A O   1 
ATOM 1402 C CB  . LEU A 1 204 ? 117.152 121.914 125.753 1.00 21.33  ? 204 LEU A CB  1 
ATOM 1403 C CG  . LEU A 1 204 ? 117.484 123.384 125.496 1.00 40.59  ? 204 LEU A CG  1 
ATOM 1404 C CD1 . LEU A 1 204 ? 118.146 123.999 126.715 1.00 42.06  ? 204 LEU A CD1 1 
ATOM 1405 C CD2 . LEU A 1 204 ? 118.371 123.540 124.272 1.00 40.38  ? 204 LEU A CD2 1 
ATOM 1406 N N   . PHE A 1 205 ? 115.336 119.268 125.434 1.00 30.55  ? 205 PHE A N   1 
ATOM 1407 C CA  . PHE A 1 205 ? 115.052 117.857 125.679 1.00 9.05   ? 205 PHE A CA  1 
ATOM 1408 C C   . PHE A 1 205 ? 114.964 117.067 124.378 1.00 14.87  ? 205 PHE A C   1 
ATOM 1409 O O   . PHE A 1 205 ? 115.396 115.912 124.325 1.00 31.44  ? 205 PHE A O   1 
ATOM 1410 C CB  . PHE A 1 205 ? 113.765 117.694 126.486 1.00 24.22  ? 205 PHE A CB  1 
ATOM 1411 C CG  . PHE A 1 205 ? 113.858 118.205 127.894 1.00 24.96  ? 205 PHE A CG  1 
ATOM 1412 C CD1 . PHE A 1 205 ? 114.841 117.739 128.746 1.00 23.43  ? 205 PHE A CD1 1 
ATOM 1413 C CD2 . PHE A 1 205 ? 112.942 119.122 128.377 1.00 25.94  ? 205 PHE A CD2 1 
ATOM 1414 C CE1 . PHE A 1 205 ? 114.926 118.196 130.042 1.00 22.01  ? 205 PHE A CE1 1 
ATOM 1415 C CE2 . PHE A 1 205 ? 113.023 119.584 129.673 1.00 25.22  ? 205 PHE A CE2 1 
ATOM 1416 C CZ  . PHE A 1 205 ? 114.016 119.120 130.506 1.00 26.52  ? 205 PHE A CZ  1 
ATOM 1417 N N   . ARG A 1 206 ? 114.421 117.666 123.315 1.00 34.96  ? 206 ARG A N   1 
ATOM 1418 C CA  . ARG A 1 206 ? 114.386 116.988 122.022 1.00 35.36  ? 206 ARG A CA  1 
ATOM 1419 C C   . ARG A 1 206 ? 115.781 116.781 121.437 1.00 25.44  ? 206 ARG A C   1 
ATOM 1420 O O   . ARG A 1 206 ? 116.060 115.719 120.864 1.00 26.04  ? 206 ARG A O   1 
ATOM 1421 C CB  . ARG A 1 206 ? 113.523 117.803 121.058 1.00 30.34  ? 206 ARG A CB  1 
ATOM 1422 C CG  . ARG A 1 206 ? 113.180 117.124 119.752 1.00 33.70  ? 206 ARG A CG  1 
ATOM 1423 C CD  . ARG A 1 206 ? 112.122 116.060 119.955 1.00 28.07  ? 206 ARG A CD  1 
ATOM 1424 N NE  . ARG A 1 206 ? 111.660 115.509 118.688 1.00 30.59  ? 206 ARG A NE  1 
ATOM 1425 C CZ  . ARG A 1 206 ? 110.940 114.403 118.572 1.00 41.18  ? 206 ARG A CZ  1 
ATOM 1426 N NH1 . ARG A 1 206 ? 110.581 113.698 119.633 1.00 40.73  ? 206 ARG A NH1 1 
ATOM 1427 N NH2 . ARG A 1 206 ? 110.567 113.996 117.363 1.00 40.69  ? 206 ARG A NH2 1 
ATOM 1428 N N   . LEU A 1 207 ? 116.708 117.706 121.699 1.00 15.60  ? 207 LEU A N   1 
ATOM 1429 C CA  . LEU A 1 207 ? 118.090 117.501 121.268 1.00 23.85  ? 207 LEU A CA  1 
ATOM 1430 C C   . LEU A 1 207 ? 118.790 116.432 122.103 1.00 37.41  ? 207 LEU A C   1 
ATOM 1431 O O   . LEU A 1 207 ? 119.495 115.569 121.559 1.00 36.09  ? 207 LEU A O   1 
ATOM 1432 C CB  . LEU A 1 207 ? 118.849 118.827 121.339 1.00 31.73  ? 207 LEU A CB  1 
ATOM 1433 C CG  . LEU A 1 207 ? 120.341 118.854 121.007 1.00 32.06  ? 207 LEU A CG  1 
ATOM 1434 C CD1 . LEU A 1 207 ? 120.574 118.470 119.563 1.00 37.11  ? 207 LEU A CD1 1 
ATOM 1435 C CD2 . LEU A 1 207 ? 120.920 120.228 121.289 1.00 30.33  ? 207 LEU A CD2 1 
ATOM 1436 N N   . LEU A 1 208 ? 118.605 116.468 123.424 1.00 43.55  ? 208 LEU A N   1 
ATOM 1437 C CA  . LEU A 1 208 ? 119.263 115.493 124.286 1.00 28.82  ? 208 LEU A CA  1 
ATOM 1438 C C   . LEU A 1 208 ? 118.702 114.087 124.087 1.00 31.75  ? 208 LEU A C   1 
ATOM 1439 O O   . LEU A 1 208 ? 119.422 113.103 124.280 1.00 44.12  ? 208 LEU A O   1 
ATOM 1440 C CB  . LEU A 1 208 ? 119.131 115.934 125.743 1.00 21.72  ? 208 LEU A CB  1 
ATOM 1441 C CG  . LEU A 1 208 ? 119.785 115.087 126.828 1.00 34.73  ? 208 LEU A CG  1 
ATOM 1442 C CD1 . LEU A 1 208 ? 121.270 114.958 126.556 1.00 39.51  ? 208 LEU A CD1 1 
ATOM 1443 C CD2 . LEU A 1 208 ? 119.541 115.714 128.186 1.00 34.43  ? 208 LEU A CD2 1 
ATOM 1444 N N   . GLN A 1 209 ? 117.425 113.972 123.715 1.00 26.45  ? 209 GLN A N   1 
ATOM 1445 C CA  . GLN A 1 209 ? 116.855 112.679 123.346 1.00 26.83  ? 209 GLN A CA  1 
ATOM 1446 C C   . GLN A 1 209 ? 117.378 112.194 121.998 1.00 33.08  ? 209 GLN A C   1 
ATOM 1447 O O   . GLN A 1 209 ? 117.628 110.992 121.819 1.00 41.11  ? 209 GLN A O   1 
ATOM 1448 C CB  . GLN A 1 209 ? 115.332 112.770 123.325 1.00 28.75  ? 209 GLN A CB  1 
ATOM 1449 C CG  . GLN A 1 209 ? 114.636 111.463 123.017 1.00 36.20  ? 209 GLN A CG  1 
ATOM 1450 C CD  . GLN A 1 209 ? 113.243 111.403 123.600 1.00 41.77  ? 209 GLN A CD  1 
ATOM 1451 O OE1 . GLN A 1 209 ? 112.482 112.362 123.508 1.00 41.27  ? 209 GLN A OE1 1 
ATOM 1452 N NE2 . GLN A 1 209 ? 112.900 110.273 124.205 1.00 39.74  ? 209 GLN A NE2 1 
ATOM 1453 N N   . GLY A 1 210 ? 117.488 113.100 121.020 1.00 32.96  ? 210 GLY A N   1 
ATOM 1454 C CA  . GLY A 1 210 ? 118.086 112.732 119.748 1.00 26.84  ? 210 GLY A CA  1 
ATOM 1455 C C   . GLY A 1 210 ? 119.496 112.192 119.889 1.00 25.43  ? 210 GLY A C   1 
ATOM 1456 O O   . GLY A 1 210 ? 119.872 111.235 119.210 1.00 33.19  ? 210 GLY A O   1 
ATOM 1457 N N   . LEU A 1 211 ? 120.301 112.813 120.755 1.00 22.11  ? 211 LEU A N   1 
ATOM 1458 C CA  . LEU A 1 211 ? 121.685 112.371 120.931 1.00 24.15  ? 211 LEU A CA  1 
ATOM 1459 C C   . LEU A 1 211 ? 121.806 110.888 121.277 1.00 39.30  ? 211 LEU A C   1 
ATOM 1460 O O   . LEU A 1 211 ? 122.766 110.233 120.855 1.00 40.64  ? 211 LEU A O   1 
ATOM 1461 C CB  . LEU A 1 211 ? 122.372 113.192 122.024 1.00 22.37  ? 211 LEU A CB  1 
ATOM 1462 C CG  . LEU A 1 211 ? 122.683 114.668 121.786 1.00 30.98  ? 211 LEU A CG  1 
ATOM 1463 C CD1 . LEU A 1 211 ? 123.153 115.311 123.074 1.00 35.01  ? 211 LEU A CD1 1 
ATOM 1464 C CD2 . LEU A 1 211 ? 123.739 114.820 120.712 1.00 40.31  ? 211 LEU A CD2 1 
ATOM 1465 N N   . VAL A 1 212 ? 120.858 110.340 122.037 1.00 54.61  ? 212 VAL A N   1 
ATOM 1466 C CA  . VAL A 1 212 ? 120.958 108.974 122.551 1.00 34.10  ? 212 VAL A CA  1 
ATOM 1467 C C   . VAL A 1 212 ? 120.094 107.943 121.826 1.00 31.53  ? 212 VAL A C   1 
ATOM 1468 O O   . VAL A 1 212 ? 120.451 106.758 121.783 1.00 45.54  ? 212 VAL A O   1 
ATOM 1469 C CB  . VAL A 1 212 ? 120.644 108.956 124.058 1.00 28.80  ? 212 VAL A CB  1 
ATOM 1470 C CG1 . VAL A 1 212 ? 121.758 109.636 124.831 1.00 27.55  ? 212 VAL A CG1 1 
ATOM 1471 C CG2 . VAL A 1 212 ? 119.318 109.638 124.330 1.00 26.80  ? 212 VAL A CG2 1 
ATOM 1472 N N   . SER A 1 213 ? 118.931 108.362 121.310 1.00 29.37  ? 213 SER A N   1 
ATOM 1473 C CA  . SER A 1 213 ? 117.987 107.410 120.720 1.00 30.99  ? 213 SER A CA  1 
ATOM 1474 C C   . SER A 1 213 ? 118.617 106.544 119.630 1.00 40.71  ? 213 SER A C   1 
ATOM 1475 O O   . SER A 1 213 ? 118.520 105.307 119.665 1.00 48.29  ? 213 SER A O   1 
ATOM 1476 C CB  . SER A 1 213 ? 116.783 108.166 120.160 1.00 35.31  ? 213 SER A CB  1 
ATOM 1477 O OG  . SER A 1 213 ? 116.007 108.725 121.202 1.00 40.70  ? 213 SER A OG  1 
ATOM 1478 N N   . LYS A 1 214 ? 119.272 107.170 118.652 1.00 43.03  ? 214 LYS A N   1 
ATOM 1479 C CA  . LYS A 1 214 ? 119.736 106.402 117.503 1.00 44.23  ? 214 LYS A CA  1 
ATOM 1480 C C   . LYS A 1 214 ? 120.933 105.538 117.869 1.00 50.78  ? 214 LYS A C   1 
ATOM 1481 O O   . LYS A 1 214 ? 121.091 104.435 117.330 1.00 58.74  ? 214 LYS A O   1 
ATOM 1482 C CB  . LYS A 1 214 ? 120.077 107.334 116.343 1.00 50.17  ? 214 LYS A CB  1 
ATOM 1483 C CG  . LYS A 1 214 ? 120.129 106.637 114.995 1.00 50.00  ? 214 LYS A CG  1 
ATOM 1484 C CD  . LYS A 1 214 ? 120.590 107.582 113.905 1.00 54.18  ? 214 LYS A CD  1 
ATOM 1485 C CE  . LYS A 1 214 ? 120.620 106.892 112.555 1.00 56.49  ? 214 LYS A CE  1 
ATOM 1486 N NZ  . LYS A 1 214 ? 121.332 107.709 111.536 1.00 55.97  ? 214 LYS A NZ  1 
ATOM 1487 N N   . GLY A 1 215 ? 121.765 106.008 118.798 1.00 53.62  ? 215 GLY A N   1 
ATOM 1488 C CA  . GLY A 1 215 ? 122.848 105.175 119.287 1.00 51.36  ? 215 GLY A CA  1 
ATOM 1489 C C   . GLY A 1 215 ? 122.335 103.926 119.974 1.00 49.34  ? 215 GLY A C   1 
ATOM 1490 O O   . GLY A 1 215 ? 122.847 102.828 119.750 1.00 52.82  ? 215 GLY A O   1 
ATOM 1491 N N   . ASN A 1 216 ? 121.328 104.081 120.839 1.00 50.97  ? 216 ASN A N   1 
ATOM 1492 C CA  . ASN A 1 216 ? 120.703 102.919 121.469 1.00 49.40  ? 216 ASN A CA  1 
ATOM 1493 C C   . ASN A 1 216 ? 120.165 101.943 120.428 1.00 54.87  ? 216 ASN A C   1 
ATOM 1494 O O   . ASN A 1 216 ? 120.368 100.726 120.535 1.00 56.07  ? 216 ASN A O   1 
ATOM 1495 C CB  . ASN A 1 216 ? 119.585 103.357 122.415 1.00 45.72  ? 216 ASN A CB  1 
ATOM 1496 C CG  . ASN A 1 216 ? 120.089 104.212 123.552 1.00 53.81  ? 216 ASN A CG  1 
ATOM 1497 O OD1 . ASN A 1 216 ? 121.265 104.160 123.908 1.00 56.07  ? 216 ASN A OD1 1 
ATOM 1498 N ND2 . ASN A 1 216 ? 119.197 104.999 124.137 1.00 57.97  ? 216 ASN A ND2 1 
ATOM 1499 N N   . TRP A 1 217 ? 119.439 102.459 119.432 1.00 58.80  ? 217 TRP A N   1 
ATOM 1500 C CA  . TRP A 1 217 ? 118.841 101.585 118.424 1.00 56.02  ? 217 TRP A CA  1 
ATOM 1501 C C   . TRP A 1 217 ? 119.904 100.820 117.637 1.00 53.89  ? 217 TRP A C   1 
ATOM 1502 O O   . TRP A 1 217 ? 119.779 99.605  117.421 1.00 61.83  ? 217 TRP A O   1 
ATOM 1503 C CB  . TRP A 1 217 ? 117.955 102.410 117.491 1.00 53.63  ? 217 TRP A CB  1 
ATOM 1504 C CG  . TRP A 1 217 ? 117.127 101.600 116.541 1.00 56.97  ? 217 TRP A CG  1 
ATOM 1505 C CD1 . TRP A 1 217 ? 116.005 100.885 116.841 1.00 56.05  ? 217 TRP A CD1 1 
ATOM 1506 C CD2 . TRP A 1 217 ? 117.331 101.452 115.131 1.00 58.45  ? 217 TRP A CD2 1 
ATOM 1507 N NE1 . TRP A 1 217 ? 115.509 100.286 115.710 1.00 54.71  ? 217 TRP A NE1 1 
ATOM 1508 C CE2 . TRP A 1 217 ? 116.304 100.620 114.646 1.00 57.68  ? 217 TRP A CE2 1 
ATOM 1509 C CE3 . TRP A 1 217 ? 118.287 101.936 114.233 1.00 58.04  ? 217 TRP A CE3 1 
ATOM 1510 C CZ2 . TRP A 1 217 ? 116.206 100.260 113.305 1.00 58.41  ? 217 TRP A CZ2 1 
ATOM 1511 C CZ3 . TRP A 1 217 ? 118.188 101.577 112.902 1.00 57.31  ? 217 TRP A CZ3 1 
ATOM 1512 C CH2 . TRP A 1 217 ? 117.155 100.747 112.451 1.00 58.29  ? 217 TRP A CH2 1 
ATOM 1513 N N   . MET A 1 218 ? 120.995 101.495 117.267 1.00 60.49  ? 218 MET A N   1 
ATOM 1514 C CA  . MET A 1 218 ? 122.054 100.825 116.516 1.00 62.10  ? 218 MET A CA  1 
ATOM 1515 C C   . MET A 1 218 ? 122.821 99.840  117.390 1.00 64.59  ? 218 MET A C   1 
ATOM 1516 O O   . MET A 1 218 ? 123.245 98.783  116.913 1.00 63.01  ? 218 MET A O   1 
ATOM 1517 C CB  . MET A 1 218 ? 123.003 101.856 115.907 1.00 64.95  ? 218 MET A CB  1 
ATOM 1518 C CG  . MET A 1 218 ? 122.355 102.752 114.866 1.00 69.30  ? 218 MET A CG  1 
ATOM 1519 S SD  . MET A 1 218 ? 121.825 101.848 113.399 1.00 80.32  ? 218 MET A SD  1 
ATOM 1520 C CE  . MET A 1 218 ? 123.405 101.431 112.667 1.00 71.23  ? 218 MET A CE  1 
ATOM 1521 N N   . ALA A 1 219 ? 123.006 100.164 118.670 1.00 72.29  ? 219 ALA A N   1 
ATOM 1522 C CA  . ALA A 1 219 ? 123.653 99.237  119.593 1.00 72.13  ? 219 ALA A CA  1 
ATOM 1523 C C   . ALA A 1 219 ? 122.843 97.955  119.742 1.00 71.06  ? 219 ALA A C   1 
ATOM 1524 O O   . ALA A 1 219 ? 123.394 96.848  119.686 1.00 70.41  ? 219 ALA A O   1 
ATOM 1525 C CB  . ALA A 1 219 ? 123.858 99.906  120.952 1.00 66.78  ? 219 ALA A CB  1 
ATOM 1526 N N   . GLY A 1 220 ? 121.539 98.087  119.990 1.00 72.91  ? 220 GLY A N   1 
ATOM 1527 C CA  . GLY A 1 220 ? 120.688 96.908  120.038 1.00 70.92  ? 220 GLY A CA  1 
ATOM 1528 C C   . GLY A 1 220 ? 120.729 96.091  118.760 1.00 72.99  ? 220 GLY A C   1 
ATOM 1529 O O   . GLY A 1 220 ? 120.790 94.858  118.805 1.00 73.70  ? 220 GLY A O   1 
ATOM 1530 N N   . TYR A 1 221 ? 120.708 96.760  117.601 1.00 77.61  ? 221 TYR A N   1 
ATOM 1531 C CA  . TYR A 1 221 ? 120.803 96.027  116.339 1.00 76.06  ? 221 TYR A CA  1 
ATOM 1532 C C   . TYR A 1 221 ? 122.122 95.266  116.245 1.00 79.49  ? 221 TYR A C   1 
ATOM 1533 O O   . TYR A 1 221 ? 122.158 94.106  115.811 1.00 80.05  ? 221 TYR A O   1 
ATOM 1534 C CB  . TYR A 1 221 ? 120.646 96.984  115.159 1.00 76.68  ? 221 TYR A CB  1 
ATOM 1535 C CG  . TYR A 1 221 ? 120.753 96.313  113.808 1.00 79.76  ? 221 TYR A CG  1 
ATOM 1536 C CD1 . TYR A 1 221 ? 119.695 95.579  113.291 1.00 79.10  ? 221 TYR A CD1 1 
ATOM 1537 C CD2 . TYR A 1 221 ? 121.913 96.414  113.050 1.00 81.19  ? 221 TYR A CD2 1 
ATOM 1538 C CE1 . TYR A 1 221 ? 119.785 94.966  112.057 1.00 79.21  ? 221 TYR A CE1 1 
ATOM 1539 C CE2 . TYR A 1 221 ? 122.014 95.802  111.815 1.00 82.07  ? 221 TYR A CE2 1 
ATOM 1540 C CZ  . TYR A 1 221 ? 120.947 95.079  111.323 1.00 81.12  ? 221 TYR A CZ  1 
ATOM 1541 O OH  . TYR A 1 221 ? 121.044 94.466  110.095 1.00 79.78  ? 221 TYR A OH  1 
ATOM 1542 N N   . THR A 1 222 ? 123.219 95.917  116.633 1.00 82.92  ? 222 THR A N   1 
ATOM 1543 C CA  . THR A 1 222 ? 124.534 95.286  116.617 1.00 81.74  ? 222 THR A CA  1 
ATOM 1544 C C   . THR A 1 222 ? 124.553 94.034  117.485 1.00 78.98  ? 222 THR A C   1 
ATOM 1545 O O   . THR A 1 222 ? 124.975 92.964  117.039 1.00 75.49  ? 222 THR A O   1 
ATOM 1546 C CB  . THR A 1 222 ? 125.600 96.280  117.079 1.00 83.29  ? 222 THR A CB  1 
ATOM 1547 O OG1 . THR A 1 222 ? 125.577 97.435  116.232 1.00 86.02  ? 222 THR A OG1 1 
ATOM 1548 C CG2 . THR A 1 222 ? 126.977 95.643  117.015 1.00 81.85  ? 222 THR A CG2 1 
ATOM 1549 N N   . LEU A 1 223 ? 124.156 94.171  118.753 1.00 82.93  ? 223 LEU A N   1 
ATOM 1550 C CA  . LEU A 1 223 ? 124.104 93.020  119.655 1.00 80.63  ? 223 LEU A CA  1 
ATOM 1551 C C   . LEU A 1 223 ? 123.220 91.898  119.119 1.00 83.41  ? 223 LEU A C   1 
ATOM 1552 O O   . LEU A 1 223 ? 123.585 90.718  119.212 1.00 85.13  ? 223 LEU A O   1 
ATOM 1553 C CB  . LEU A 1 223 ? 123.626 93.446  121.044 1.00 80.92  ? 223 LEU A CB  1 
ATOM 1554 C CG  . LEU A 1 223 ? 124.674 93.932  122.049 1.00 81.91  ? 223 LEU A CG  1 
ATOM 1555 C CD1 . LEU A 1 223 ? 125.203 95.310  121.701 1.00 81.08  ? 223 LEU A CD1 1 
ATOM 1556 C CD2 . LEU A 1 223 ? 124.100 93.916  123.457 1.00 81.47  ? 223 LEU A CD2 1 
ATOM 1557 N N   . ILE A 1 224 ? 122.070 92.235  118.527 1.00 85.46  ? 224 ILE A N   1 
ATOM 1558 C CA  . ILE A 1 224 ? 121.157 91.186  118.077 1.00 81.74  ? 224 ILE A CA  1 
ATOM 1559 C C   . ILE A 1 224 ? 121.725 90.450  116.869 1.00 79.53  ? 224 ILE A C   1 
ATOM 1560 O O   . ILE A 1 224 ? 121.549 89.233  116.739 1.00 78.97  ? 224 ILE A O   1 
ATOM 1561 C CB  . ILE A 1 224 ? 119.744 91.748  117.813 1.00 83.18  ? 224 ILE A CB  1 
ATOM 1562 C CG1 . ILE A 1 224 ? 118.722 90.610  117.811 1.00 83.38  ? 224 ILE A CG1 1 
ATOM 1563 C CG2 . ILE A 1 224 ? 119.662 92.486  116.493 1.00 80.50  ? 224 ILE A CG2 1 
ATOM 1564 C CD1 . ILE A 1 224 ? 118.278 90.169  119.182 1.00 82.70  ? 224 ILE A CD1 1 
ATOM 1565 N N   . THR A 1 225 ? 122.415 91.153  115.969 1.00 86.30  ? 225 THR A N   1 
ATOM 1566 C CA  . THR A 1 225 ? 122.982 90.459  114.818 1.00 87.59  ? 225 THR A CA  1 
ATOM 1567 C C   . THR A 1 225 ? 124.337 89.829  115.118 1.00 89.65  ? 225 THR A C   1 
ATOM 1568 O O   . THR A 1 225 ? 124.781 88.956  114.363 1.00 91.15  ? 225 THR A O   1 
ATOM 1569 C CB  . THR A 1 225 ? 123.127 91.413  113.628 1.00 87.77  ? 225 THR A CB  1 
ATOM 1570 O OG1 . THR A 1 225 ? 123.961 92.519  113.994 1.00 89.97  ? 225 THR A OG1 1 
ATOM 1571 C CG2 . THR A 1 225 ? 121.765 91.930  113.189 1.00 86.57  ? 225 THR A CG2 1 
ATOM 1572 N N   . GLU A 1 226 ? 124.998 90.250  116.197 1.00 91.61  ? 226 GLU A N   1 
ATOM 1573 C CA  . GLU A 1 226 ? 126.271 89.670  116.611 1.00 92.61  ? 226 GLU A CA  1 
ATOM 1574 C C   . GLU A 1 226 ? 126.068 88.373  117.384 1.00 90.75  ? 226 GLU A C   1 
ATOM 1575 O O   . GLU A 1 226 ? 126.749 87.374  117.127 1.00 89.05  ? 226 GLU A O   1 
ATOM 1576 C CB  . GLU A 1 226 ? 127.061 90.677  117.449 1.00 93.56  ? 226 GLU A CB  1 
ATOM 1577 C CG  . GLU A 1 226 ? 128.329 90.112  118.069 1.00 93.36  ? 226 GLU A CG  1 
ATOM 1578 C CD  . GLU A 1 226 ? 129.012 91.095  119.001 1.00 93.40  ? 226 GLU A CD  1 
ATOM 1579 O OE1 . GLU A 1 226 ? 129.134 92.281  118.629 1.00 92.32  ? 226 GLU A OE1 1 
ATOM 1580 O OE2 . GLU A 1 226 ? 129.428 90.680  120.103 1.00 93.12  ? 226 GLU A OE2 1 
ATOM 1581 N N   . PHE A 1 227 ? 125.138 88.377  118.343 1.00 92.68  ? 227 PHE A N   1 
ATOM 1582 C CA  . PHE A 1 227 ? 124.809 87.150  119.063 1.00 93.01  ? 227 PHE A CA  1 
ATOM 1583 C C   . PHE A 1 227 ? 124.252 86.087  118.124 1.00 94.05  ? 227 PHE A C   1 
ATOM 1584 O O   . PHE A 1 227 ? 124.604 84.907  118.235 1.00 95.25  ? 227 PHE A O   1 
ATOM 1585 C CB  . PHE A 1 227 ? 123.813 87.461  120.183 1.00 92.19  ? 227 PHE A CB  1 
ATOM 1586 C CG  . PHE A 1 227 ? 123.180 86.243  120.796 1.00 91.82  ? 227 PHE A CG  1 
ATOM 1587 C CD1 . PHE A 1 227 ? 123.960 85.197  121.264 1.00 92.40  ? 227 PHE A CD1 1 
ATOM 1588 C CD2 . PHE A 1 227 ? 121.803 86.146  120.904 1.00 93.33  ? 227 PHE A CD2 1 
ATOM 1589 C CE1 . PHE A 1 227 ? 123.377 84.078  121.828 1.00 94.13  ? 227 PHE A CE1 1 
ATOM 1590 C CE2 . PHE A 1 227 ? 121.214 85.029  121.466 1.00 93.41  ? 227 PHE A CE2 1 
ATOM 1591 C CZ  . PHE A 1 227 ? 122.002 83.994  121.929 1.00 94.24  ? 227 PHE A CZ  1 
ATOM 1592 N N   . VAL A 1 228 ? 123.393 86.478  117.190 1.00 91.42  ? 228 VAL A N   1 
ATOM 1593 C CA  . VAL A 1 228 ? 122.799 85.518  116.269 1.00 89.23  ? 228 VAL A CA  1 
ATOM 1594 C C   . VAL A 1 228 ? 123.806 85.182  115.175 1.00 93.44  ? 228 VAL A C   1 
ATOM 1595 O O   . VAL A 1 228 ? 124.608 86.023  114.754 1.00 91.43  ? 228 VAL A O   1 
ATOM 1596 C CB  . VAL A 1 228 ? 121.482 86.079  115.693 1.00 89.44  ? 228 VAL A CB  1 
ATOM 1597 C CG1 . VAL A 1 228 ? 120.953 85.209  114.562 1.00 90.40  ? 228 VAL A CG1 1 
ATOM 1598 C CG2 . VAL A 1 228 ? 120.441 86.204  116.793 1.00 90.81  ? 228 VAL A CG2 1 
ATOM 1599 N N   . GLY A 1 229 ? 123.764 83.931  114.707 1.00 92.51  ? 229 GLY A N   1 
ATOM 1600 C CA  . GLY A 1 229 ? 124.691 83.463  113.701 1.00 90.62  ? 229 GLY A CA  1 
ATOM 1601 C C   . GLY A 1 229 ? 124.329 83.898  112.292 1.00 92.74  ? 229 GLY A C   1 
ATOM 1602 O O   . GLY A 1 229 ? 123.231 84.382  112.015 1.00 91.71  ? 229 GLY A O   1 
ATOM 1603 N N   . SER A 1 230 ? 125.298 83.720  111.389 1.00 95.37  ? 230 SER A N   1 
ATOM 1604 C CA  . SER A 1 230 ? 125.157 84.187  110.014 1.00 96.11  ? 230 SER A CA  1 
ATOM 1605 C C   . SER A 1 230 ? 124.026 83.485  109.272 1.00 95.97  ? 230 SER A C   1 
ATOM 1606 O O   . SER A 1 230 ? 123.557 84.000  108.250 1.00 95.11  ? 230 SER A O   1 
ATOM 1607 C CB  . SER A 1 230 ? 126.473 83.993  109.259 1.00 94.06  ? 230 SER A CB  1 
ATOM 1608 O OG  . SER A 1 230 ? 126.825 82.622  109.193 1.00 92.54  ? 230 SER A OG  1 
ATOM 1609 N N   . GLY A 1 231 ? 123.578 82.326  109.758 1.00 96.77  ? 231 GLY A N   1 
ATOM 1610 C CA  . GLY A 1 231 ? 122.501 81.602  109.106 1.00 96.33  ? 231 GLY A CA  1 
ATOM 1611 C C   . GLY A 1 231 ? 121.139 82.240  109.281 1.00 97.16  ? 231 GLY A C   1 
ATOM 1612 O O   . GLY A 1 231 ? 120.221 81.938  108.511 1.00 95.68  ? 231 GLY A O   1 
ATOM 1613 N N   . SER A 1 232 ? 120.987 83.114  110.276 1.00 97.69  ? 232 SER A N   1 
ATOM 1614 C CA  . SER A 1 232 ? 119.703 83.715  110.600 1.00 99.13  ? 232 SER A CA  1 
ATOM 1615 C C   . SER A 1 232 ? 119.768 85.232  110.703 1.00 98.48  ? 232 SER A C   1 
ATOM 1616 O O   . SER A 1 232 ? 118.762 85.853  111.063 1.00 99.62  ? 232 SER A O   1 
ATOM 1617 C CB  . SER A 1 232 ? 119.157 83.139  111.916 1.00 96.77  ? 232 SER A CB  1 
ATOM 1618 O OG  . SER A 1 232 ? 117.865 83.647  112.198 1.00 97.57  ? 232 SER A OG  1 
ATOM 1619 N N   . ARG A 1 233 ? 120.923 85.837  110.413 1.00 95.41  ? 233 ARG A N   1 
ATOM 1620 C CA  . ARG A 1 233 ? 121.096 87.280  110.563 1.00 97.93  ? 233 ARG A CA  1 
ATOM 1621 C C   . ARG A 1 233 ? 120.047 88.062  109.778 1.00 95.65  ? 233 ARG A C   1 
ATOM 1622 O O   . ARG A 1 233 ? 119.424 88.989  110.306 1.00 92.54  ? 233 ARG A O   1 
ATOM 1623 C CB  . ARG A 1 233 ? 122.506 87.678  110.123 1.00 96.20  ? 233 ARG A CB  1 
ATOM 1624 C CG  . ARG A 1 233 ? 122.797 89.165  110.223 1.00 95.06  ? 233 ARG A CG  1 
ATOM 1625 C CD  . ARG A 1 233 ? 124.231 89.472  109.823 1.00 95.11  ? 233 ARG A CD  1 
ATOM 1626 N NE  . ARG A 1 233 ? 124.519 90.901  109.864 1.00 98.26  ? 233 ARG A NE  1 
ATOM 1627 C CZ  . ARG A 1 233 ? 124.195 91.760  108.906 1.00 98.98  ? 233 ARG A CZ  1 
ATOM 1628 N NH1 . ARG A 1 233 ? 123.565 91.368  107.811 1.00 98.35  ? 233 ARG A NH1 1 
ATOM 1629 N NH2 . ARG A 1 233 ? 124.511 93.044  109.052 1.00 97.62  ? 233 ARG A NH2 1 
ATOM 1630 N N   . ARG A 1 234 ? 119.855 87.712  108.504 1.00 88.72  ? 234 ARG A N   1 
ATOM 1631 C CA  . ARG A 1 234 ? 118.845 88.381  107.685 1.00 89.84  ? 234 ARG A CA  1 
ATOM 1632 C C   . ARG A 1 234 ? 117.443 88.217  108.263 1.00 87.00  ? 234 ARG A C   1 
ATOM 1633 O O   . ARG A 1 234 ? 116.644 89.164  108.257 1.00 88.34  ? 234 ARG A O   1 
ATOM 1634 C CB  . ARG A 1 234 ? 118.907 87.843  106.257 1.00 88.43  ? 234 ARG A CB  1 
ATOM 1635 C CG  . ARG A 1 234 ? 118.146 88.664  105.237 1.00 86.99  ? 234 ARG A CG  1 
ATOM 1636 C CD  . ARG A 1 234 ? 118.323 88.073  103.851 1.00 89.18  ? 234 ARG A CD  1 
ATOM 1637 N NE  . ARG A 1 234 ? 119.723 88.086  103.444 1.00 90.63  ? 234 ARG A NE  1 
ATOM 1638 C CZ  . ARG A 1 234 ? 120.432 87.002  103.160 1.00 90.19  ? 234 ARG A CZ  1 
ATOM 1639 N NH1 . ARG A 1 234 ? 119.896 85.794  103.207 1.00 89.13  ? 234 ARG A NH1 1 
ATOM 1640 N NH2 . ARG A 1 234 ? 121.710 87.135  102.816 1.00 88.92  ? 234 ARG A NH2 1 
ATOM 1641 N N   . THR A 1 235 ? 117.138 87.040  108.813 1.00 86.11  ? 235 THR A N   1 
ATOM 1642 C CA  . THR A 1 235 ? 115.799 86.817  109.345 1.00 88.49  ? 235 THR A CA  1 
ATOM 1643 C C   . THR A 1 235 ? 115.573 87.638  110.607 1.00 91.65  ? 235 THR A C   1 
ATOM 1644 O O   . THR A 1 235 ? 114.493 88.215  110.800 1.00 94.11  ? 235 THR A O   1 
ATOM 1645 C CB  . THR A 1 235 ? 115.586 85.329  109.623 1.00 87.48  ? 235 THR A CB  1 
ATOM 1646 O OG1 . THR A 1 235 ? 115.935 84.570  108.459 1.00 86.95  ? 235 THR A OG1 1 
ATOM 1647 C CG2 . THR A 1 235 ? 114.133 85.055  109.974 1.00 88.02  ? 235 THR A CG2 1 
ATOM 1648 N N   . VAL A 1 236 ? 116.591 87.736  111.463 1.00 84.31  ? 236 VAL A N   1 
ATOM 1649 C CA  . VAL A 1 236 ? 116.419 88.500  112.689 1.00 81.76  ? 236 VAL A CA  1 
ATOM 1650 C C   . VAL A 1 236 ? 116.404 89.990  112.371 1.00 80.71  ? 236 VAL A C   1 
ATOM 1651 O O   . VAL A 1 236 ? 115.703 90.767  113.028 1.00 81.99  ? 236 VAL A O   1 
ATOM 1652 C CB  . VAL A 1 236 ? 117.528 88.135  113.693 1.00 79.43  ? 236 VAL A CB  1 
ATOM 1653 C CG1 . VAL A 1 236 ? 117.489 89.053  114.895 1.00 80.70  ? 236 VAL A CG1 1 
ATOM 1654 C CG2 . VAL A 1 236 ? 117.398 86.682  114.121 1.00 79.52  ? 236 VAL A CG2 1 
ATOM 1655 N N   . ALA A 1 237 ? 117.126 90.404  111.327 1.00 69.58  ? 237 ALA A N   1 
ATOM 1656 C CA  . ALA A 1 237 ? 117.053 91.787  110.865 1.00 73.13  ? 237 ALA A CA  1 
ATOM 1657 C C   . ALA A 1 237 ? 115.655 92.135  110.367 1.00 75.45  ? 237 ALA A C   1 
ATOM 1658 O O   . ALA A 1 237 ? 115.140 93.228  110.637 1.00 76.49  ? 237 ALA A O   1 
ATOM 1659 C CB  . ALA A 1 237 ? 118.088 92.028  109.768 1.00 75.88  ? 237 ALA A CB  1 
ATOM 1660 N N   . ILE A 1 238 ? 115.020 91.213  109.639 1.00 70.30  ? 238 ILE A N   1 
ATOM 1661 C CA  . ILE A 1 238 ? 113.667 91.483  109.163 1.00 65.96  ? 238 ILE A CA  1 
ATOM 1662 C C   . ILE A 1 238 ? 112.662 91.464  110.311 1.00 66.11  ? 238 ILE A C   1 
ATOM 1663 O O   . ILE A 1 238 ? 111.706 92.251  110.316 1.00 70.02  ? 238 ILE A O   1 
ATOM 1664 C CB  . ILE A 1 238 ? 113.304 90.482  108.052 1.00 66.16  ? 238 ILE A CB  1 
ATOM 1665 C CG1 . ILE A 1 238 ? 114.101 90.810  106.790 1.00 67.23  ? 238 ILE A CG1 1 
ATOM 1666 C CG2 . ILE A 1 238 ? 111.816 90.508  107.754 1.00 69.76  ? 238 ILE A CG2 1 
ATOM 1667 C CD1 . ILE A 1 238 ? 114.113 89.710  105.775 1.00 67.52  ? 238 ILE A CD1 1 
ATOM 1668 N N   . MET A 1 239 ? 112.894 90.643  111.340 1.00 60.25  ? 239 MET A N   1 
ATOM 1669 C CA  . MET A 1 239 ? 112.018 90.708  112.508 1.00 61.79  ? 239 MET A CA  1 
ATOM 1670 C C   . MET A 1 239 ? 112.244 92.001  113.283 1.00 62.75  ? 239 MET A C   1 
ATOM 1671 O O   . MET A 1 239 ? 111.302 92.565  113.862 1.00 70.99  ? 239 MET A O   1 
ATOM 1672 C CB  . MET A 1 239 ? 112.251 89.496  113.409 1.00 63.20  ? 239 MET A CB  1 
ATOM 1673 C CG  . MET A 1 239 ? 111.381 89.469  114.654 1.00 66.36  ? 239 MET A CG  1 
ATOM 1674 S SD  . MET A 1 239 ? 109.615 89.450  114.291 1.00 78.27  ? 239 MET A SD  1 
ATOM 1675 C CE  . MET A 1 239 ? 109.406 87.763  113.728 1.00 67.17  ? 239 MET A CE  1 
ATOM 1676 N N   . TYR A 1 240 ? 113.454 92.546  113.188 1.00 55.47  ? 240 TYR A N   1 
ATOM 1677 C CA  . TYR A 1 240 ? 113.791 93.773  113.894 1.00 58.21  ? 240 TYR A CA  1 
ATOM 1678 C C   . TYR A 1 240 ? 113.134 94.960  113.207 1.00 53.59  ? 240 TYR A C   1 
ATOM 1679 O O   . TYR A 1 240 ? 112.697 95.910  113.866 1.00 57.12  ? 240 TYR A O   1 
ATOM 1680 C CB  . TYR A 1 240 ? 115.315 93.918  113.933 1.00 59.83  ? 240 TYR A CB  1 
ATOM 1681 C CG  . TYR A 1 240 ? 115.872 94.863  114.971 1.00 62.67  ? 240 TYR A CG  1 
ATOM 1682 C CD1 . TYR A 1 240 ? 116.100 94.434  116.271 1.00 58.01  ? 240 TYR A CD1 1 
ATOM 1683 C CD2 . TYR A 1 240 ? 116.208 96.169  114.645 1.00 61.87  ? 240 TYR A CD2 1 
ATOM 1684 C CE1 . TYR A 1 240 ? 116.624 95.284  117.222 1.00 58.82  ? 240 TYR A CE1 1 
ATOM 1685 C CE2 . TYR A 1 240 ? 116.732 97.029  115.592 1.00 57.08  ? 240 TYR A CE2 1 
ATOM 1686 C CZ  . TYR A 1 240 ? 116.939 96.580  116.877 1.00 59.93  ? 240 TYR A CZ  1 
ATOM 1687 O OH  . TYR A 1 240 ? 117.456 97.431  117.825 1.00 61.35  ? 240 TYR A OH  1 
ATOM 1688 N N   . GLN A 1 241 ? 113.065 94.918  111.876 1.00 51.85  ? 241 GLN A N   1 
ATOM 1689 C CA  . GLN A 1 241 ? 112.357 95.954  111.131 1.00 52.36  ? 241 GLN A CA  1 
ATOM 1690 C C   . GLN A 1 241 ? 110.839 95.832  111.268 1.00 52.39  ? 241 GLN A C   1 
ATOM 1691 O O   . GLN A 1 241 ? 110.140 96.851  111.261 1.00 51.98  ? 241 GLN A O   1 
ATOM 1692 C CB  . GLN A 1 241 ? 112.759 95.908  109.658 1.00 55.79  ? 241 GLN A CB  1 
ATOM 1693 C CG  . GLN A 1 241 ? 114.222 96.236  109.403 1.00 56.68  ? 241 GLN A CG  1 
ATOM 1694 C CD  . GLN A 1 241 ? 114.456 97.717  109.176 1.00 60.28  ? 241 GLN A CD  1 
ATOM 1695 O OE1 . GLN A 1 241 ? 113.553 98.444  108.762 1.00 58.57  ? 241 GLN A OE1 1 
ATOM 1696 N NE2 . GLN A 1 241 ? 115.675 98.171  109.444 1.00 58.25  ? 241 GLN A NE2 1 
ATOM 1697 N N   . MET A 1 242 ? 110.304 94.608  111.377 1.00 45.06  ? 242 MET A N   1 
ATOM 1698 C CA  . MET A 1 242 ? 108.867 94.444  111.609 1.00 39.94  ? 242 MET A CA  1 
ATOM 1699 C C   . MET A 1 242 ? 108.438 94.899  113.004 1.00 44.07  ? 242 MET A C   1 
ATOM 1700 O O   . MET A 1 242 ? 107.281 95.313  113.197 1.00 47.30  ? 242 MET A O   1 
ATOM 1701 C CB  . MET A 1 242 ? 108.459 92.990  111.373 1.00 41.03  ? 242 MET A CB  1 
ATOM 1702 C CG  . MET A 1 242 ? 108.572 92.558  109.918 1.00 48.82  ? 242 MET A CG  1 
ATOM 1703 S SD  . MET A 1 242 ? 107.607 91.091  109.508 1.00 66.81  ? 242 MET A SD  1 
ATOM 1704 C CE  . MET A 1 242 ? 108.392 89.858  110.539 1.00 51.56  ? 242 MET A CE  1 
ATOM 1705 N N   . ALA A 1 243 ? 109.341 94.843  113.987 1.00 48.48  ? 243 ALA A N   1 
ATOM 1706 C CA  . ALA A 1 243 ? 108.987 95.397  115.290 1.00 35.77  ? 243 ALA A CA  1 
ATOM 1707 C C   . ALA A 1 243 ? 108.795 96.911  115.241 1.00 34.79  ? 243 ALA A C   1 
ATOM 1708 O O   . ALA A 1 243 ? 108.005 97.453  116.025 1.00 40.50  ? 243 ALA A O   1 
ATOM 1709 C CB  . ALA A 1 243 ? 110.053 95.035  116.321 1.00 31.56  ? 243 ALA A CB  1 
ATOM 1710 N N   . PHE A 1 244 ? 109.421 97.591  114.279 1.00 28.47  ? 244 PHE A N   1 
ATOM 1711 C CA  . PHE A 1 244 ? 109.157 99.013  114.079 1.00 31.36  ? 244 PHE A CA  1 
ATOM 1712 C C   . PHE A 1 244 ? 107.731 99.238  113.582 1.00 42.26  ? 244 PHE A C   1 
ATOM 1713 O O   . PHE A 1 244 ? 107.062 100.192 113.997 1.00 40.81  ? 244 PHE A O   1 
ATOM 1714 C CB  . PHE A 1 244 ? 110.188 99.575  113.097 1.00 37.34  ? 244 PHE A CB  1 
ATOM 1715 C CG  . PHE A 1 244 ? 110.118 101.064 112.900 1.00 44.93  ? 244 PHE A CG  1 
ATOM 1716 C CD1 . PHE A 1 244 ? 109.250 101.623 111.978 1.00 43.33  ? 244 PHE A CD1 1 
ATOM 1717 C CD2 . PHE A 1 244 ? 110.955 101.903 113.616 1.00 41.59  ? 244 PHE A CD2 1 
ATOM 1718 C CE1 . PHE A 1 244 ? 109.202 102.991 111.794 1.00 42.91  ? 244 PHE A CE1 1 
ATOM 1719 C CE2 . PHE A 1 244 ? 110.912 103.269 113.434 1.00 32.87  ? 244 PHE A CE2 1 
ATOM 1720 C CZ  . PHE A 1 244 ? 110.034 103.814 112.524 1.00 32.53  ? 244 PHE A CZ  1 
ATOM 1721 N N   . THR A 1 245 ? 107.251 98.370  112.687 1.00 42.48  ? 245 THR A N   1 
ATOM 1722 C CA  . THR A 1 245 ? 105.878 98.476  112.202 1.00 29.95  ? 245 THR A CA  1 
ATOM 1723 C C   . THR A 1 245 ? 104.879 98.238  113.329 1.00 25.53  ? 245 THR A C   1 
ATOM 1724 O O   . THR A 1 245 ? 103.856 98.932  113.431 1.00 38.39  ? 245 THR A O   1 
ATOM 1725 C CB  . THR A 1 245 ? 105.648 97.488  111.059 1.00 31.78  ? 245 THR A CB  1 
ATOM 1726 O OG1 . THR A 1 245 ? 106.648 97.681  110.053 1.00 39.10  ? 245 THR A OG1 1 
ATOM 1727 C CG2 . THR A 1 245 ? 104.277 97.693  110.439 1.00 31.86  ? 245 THR A CG2 1 
ATOM 1728 N N   . VAL A 1 246 ? 105.153 97.244  114.178 1.00 27.66  ? 246 VAL A N   1 
ATOM 1729 C CA  . VAL A 1 246 ? 104.296 97.021  115.343 1.00 26.98  ? 246 VAL A CA  1 
ATOM 1730 C C   . VAL A 1 246 ? 104.289 98.249  116.252 1.00 29.14  ? 246 VAL A C   1 
ATOM 1731 O O   . VAL A 1 246 ? 103.243 98.635  116.799 1.00 33.60  ? 246 VAL A O   1 
ATOM 1732 C CB  . VAL A 1 246 ? 104.744 95.757  116.100 1.00 30.63  ? 246 VAL A CB  1 
ATOM 1733 C CG1 . VAL A 1 246 ? 103.927 95.574  117.366 1.00 37.42  ? 246 VAL A CG1 1 
ATOM 1734 C CG2 . VAL A 1 246 ? 104.626 94.535  115.205 1.00 33.08  ? 246 VAL A CG2 1 
ATOM 1735 N N   . GLY A 1 247 ? 105.445 98.900  116.405 1.00 31.18  ? 247 GLY A N   1 
ATOM 1736 C CA  . GLY A 1 247 ? 105.487 100.140 117.167 1.00 25.79  ? 247 GLY A CA  1 
ATOM 1737 C C   . GLY A 1 247 ? 104.660 101.251 116.546 1.00 24.74  ? 247 GLY A C   1 
ATOM 1738 O O   . GLY A 1 247 ? 104.011 102.026 117.254 1.00 26.30  ? 247 GLY A O   1 
ATOM 1739 N N   . LEU A 1 248 ? 104.654 101.330 115.213 1.00 39.96  ? 248 LEU A N   1 
ATOM 1740 C CA  . LEU A 1 248 ? 103.824 102.323 114.531 1.00 31.68  ? 248 LEU A CA  1 
ATOM 1741 C C   . LEU A 1 248 ? 102.337 102.054 114.735 1.00 26.51  ? 248 LEU A C   1 
ATOM 1742 O O   . LEU A 1 248 ? 101.548 102.992 114.898 1.00 32.31  ? 248 LEU A O   1 
ATOM 1743 C CB  . LEU A 1 248 ? 104.147 102.351 113.037 1.00 27.61  ? 248 LEU A CB  1 
ATOM 1744 C CG  . LEU A 1 248 ? 105.527 102.814 112.577 1.00 31.94  ? 248 LEU A CG  1 
ATOM 1745 C CD1 . LEU A 1 248 ? 105.658 102.640 111.075 1.00 33.73  ? 248 LEU A CD1 1 
ATOM 1746 C CD2 . LEU A 1 248 ? 105.750 104.263 112.959 1.00 29.74  ? 248 LEU A CD2 1 
ATOM 1747 N N   . VAL A 1 249 ? 101.939 100.782 114.773 1.00 23.28  ? 249 VAL A N   1 
ATOM 1748 C CA  . VAL A 1 249 ? 100.518 100.485 114.965 1.00 17.33  ? 249 VAL A CA  1 
ATOM 1749 C C   . VAL A 1 249 ? 100.101 100.760 116.408 1.00 28.55  ? 249 VAL A C   1 
ATOM 1750 O O   . VAL A 1 249 ? 98.993  101.265 116.667 1.00 43.57  ? 249 VAL A O   1 
ATOM 1751 C CB  . VAL A 1 249 ? 100.217 99.033  114.548 1.00 31.19  ? 249 VAL A CB  1 
ATOM 1752 C CG1 . VAL A 1 249 ? 98.790  98.656  114.906 1.00 23.36  ? 249 VAL A CG1 1 
ATOM 1753 C CG2 . VAL A 1 249 ? 100.461 98.849  113.057 1.00 27.17  ? 249 VAL A CG2 1 
ATOM 1754 N N   . ALA A 1 250 ? 101.009 100.541 117.361 1.00 30.76  ? 250 ALA A N   1 
ATOM 1755 C CA  . ALA A 1 250 ? 100.705 100.891 118.745 1.00 20.00  ? 250 ALA A CA  1 
ATOM 1756 C C   . ALA A 1 250 ? 100.583 102.402 118.904 1.00 24.32  ? 250 ALA A C   1 
ATOM 1757 O O   . ALA A 1 250 ? 99.682  102.892 119.597 1.00 29.43  ? 250 ALA A O   1 
ATOM 1758 C CB  . ALA A 1 250 ? 101.775 100.329 119.680 1.00 25.77  ? 250 ALA A CB  1 
ATOM 1759 N N   . LEU A 1 251 ? 101.535 103.150 118.340 1.00 30.28  ? 251 LEU A N   1 
ATOM 1760 C CA  . LEU A 1 251 ? 101.434 104.606 118.305 1.00 15.09  ? 251 LEU A CA  1 
ATOM 1761 C C   . LEU A 1 251 ? 100.094 105.061 117.736 1.00 24.19  ? 251 LEU A C   1 
ATOM 1762 O O   . LEU A 1 251 ? 99.443  105.954 118.288 1.00 30.37  ? 251 LEU A O   1 
ATOM 1763 C CB  . LEU A 1 251 ? 102.586 105.190 117.486 1.00 24.29  ? 251 LEU A CB  1 
ATOM 1764 C CG  . LEU A 1 251 ? 102.485 106.673 117.122 1.00 40.31  ? 251 LEU A CG  1 
ATOM 1765 C CD1 . LEU A 1 251 ? 102.550 107.547 118.363 1.00 29.92  ? 251 LEU A CD1 1 
ATOM 1766 C CD2 . LEU A 1 251 ? 103.568 107.061 116.129 1.00 29.44  ? 251 LEU A CD2 1 
ATOM 1767 N N   . THR A 1 252 ? 99.692  104.486 116.596 1.00 33.38  ? 252 THR A N   1 
ATOM 1768 C CA  . THR A 1 252 ? 98.403  104.824 115.992 1.00 35.77  ? 252 THR A CA  1 
ATOM 1769 C C   . THR A 1 252 ? 97.242  104.597 116.954 1.00 29.54  ? 252 THR A C   1 
ATOM 1770 O O   . THR A 1 252 ? 96.278  105.371 116.964 1.00 35.41  ? 252 THR A O   1 
ATOM 1771 C CB  . THR A 1 252 ? 98.194  104.009 114.715 1.00 34.52  ? 252 THR A CB  1 
ATOM 1772 O OG1 . THR A 1 252 ? 99.377  104.065 113.912 1.00 40.22  ? 252 THR A OG1 1 
ATOM 1773 C CG2 . THR A 1 252 ? 97.024  104.561 113.918 1.00 21.87  ? 252 THR A CG2 1 
ATOM 1774 N N   . GLY A 1 253 ? 97.309  103.547 117.767 1.00 20.97  ? 253 GLY A N   1 
ATOM 1775 C CA  . GLY A 1 253 ? 96.201  103.278 118.672 1.00 8.59   ? 253 GLY A CA  1 
ATOM 1776 C C   . GLY A 1 253 ? 96.157  104.170 119.903 1.00 28.10  ? 253 GLY A C   1 
ATOM 1777 O O   . GLY A 1 253 ? 95.088  104.641 120.333 1.00 28.51  ? 253 GLY A O   1 
ATOM 1778 N N   . LEU A 1 254 ? 97.339  104.446 120.458 1.00 35.73  ? 254 LEU A N   1 
ATOM 1779 C CA  . LEU A 1 254 ? 97.425  105.355 121.598 1.00 15.50  ? 254 LEU A CA  1 
ATOM 1780 C C   . LEU A 1 254 ? 97.073  106.784 121.208 1.00 25.23  ? 254 LEU A C   1 
ATOM 1781 O O   . LEU A 1 254 ? 96.357  107.470 121.946 1.00 31.57  ? 254 LEU A O   1 
ATOM 1782 C CB  . LEU A 1 254 ? 98.822  105.298 122.214 1.00 24.80  ? 254 LEU A CB  1 
ATOM 1783 C CG  . LEU A 1 254 ? 99.155  104.040 123.014 1.00 27.36  ? 254 LEU A CG  1 
ATOM 1784 C CD1 . LEU A 1 254 ? 100.626 104.020 123.390 1.00 17.88  ? 254 LEU A CD1 1 
ATOM 1785 C CD2 . LEU A 1 254 ? 98.277  103.956 124.251 1.00 25.77  ? 254 LEU A CD2 1 
ATOM 1786 N N   . ALA A 1 255 ? 97.565  107.259 120.059 1.00 34.80  ? 255 ALA A N   1 
ATOM 1787 C CA  . ALA A 1 255 ? 97.204  108.593 119.592 1.00 27.37  ? 255 ALA A CA  1 
ATOM 1788 C C   . ALA A 1 255 ? 95.701  108.751 119.419 1.00 25.83  ? 255 ALA A C   1 
ATOM 1789 O O   . ALA A 1 255 ? 95.203  109.882 119.406 1.00 32.48  ? 255 ALA A O   1 
ATOM 1790 C CB  . ALA A 1 255 ? 97.915  108.899 118.275 1.00 19.57  ? 255 ALA A CB  1 
ATOM 1791 N N   . TYR A 1 256 ? 94.972  107.645 119.298 1.00 33.96  ? 256 TYR A N   1 
ATOM 1792 C CA  . TYR A 1 256 ? 93.522  107.661 119.173 1.00 26.02  ? 256 TYR A CA  1 
ATOM 1793 C C   . TYR A 1 256 ? 92.845  107.667 120.534 1.00 30.37  ? 256 TYR A C   1 
ATOM 1794 O O   . TYR A 1 256 ? 91.861  108.387 120.730 1.00 32.39  ? 256 TYR A O   1 
ATOM 1795 C CB  . TYR A 1 256 ? 93.039  106.461 118.354 1.00 20.18  ? 256 TYR A CB  1 
ATOM 1796 C CG  . TYR A 1 256 ? 91.533  106.388 118.215 1.00 26.58  ? 256 TYR A CG  1 
ATOM 1797 C CD1 . TYR A 1 256 ? 90.861  107.181 117.297 1.00 34.09  ? 256 TYR A CD1 1 
ATOM 1798 C CD2 . TYR A 1 256 ? 90.784  105.529 119.007 1.00 26.51  ? 256 TYR A CD2 1 
ATOM 1799 C CE1 . TYR A 1 256 ? 89.488  107.121 117.172 1.00 33.16  ? 256 TYR A CE1 1 
ATOM 1800 C CE2 . TYR A 1 256 ? 89.411  105.462 118.889 1.00 21.36  ? 256 TYR A CE2 1 
ATOM 1801 C CZ  . TYR A 1 256 ? 88.768  106.260 117.970 1.00 30.73  ? 256 TYR A CZ  1 
ATOM 1802 O OH  . TYR A 1 256 ? 87.400  106.195 117.848 1.00 37.59  ? 256 TYR A OH  1 
ATOM 1803 N N   . ALA A 1 257 ? 93.347  106.876 121.485 1.00 32.40  ? 257 ALA A N   1 
ATOM 1804 C CA  . ALA A 1 257 ? 92.695  106.848 122.792 1.00 14.31  ? 257 ALA A CA  1 
ATOM 1805 C C   . ALA A 1 257 ? 93.085  108.025 123.687 1.00 29.80  ? 257 ALA A C   1 
ATOM 1806 O O   . ALA A 1 257 ? 92.288  108.427 124.541 1.00 40.08  ? 257 ALA A O   1 
ATOM 1807 C CB  . ALA A 1 257 ? 93.006  105.534 123.506 1.00 23.12  ? 257 ALA A CB  1 
ATOM 1808 N N   . LEU A 1 258 ? 94.288  108.585 123.521 1.00 35.76  ? 258 LEU A N   1 
ATOM 1809 C CA  . LEU A 1 258 ? 94.780  109.723 124.301 1.00 19.11  ? 258 LEU A CA  1 
ATOM 1810 C C   . LEU A 1 258 ? 94.793  111.019 123.494 1.00 24.76  ? 258 LEU A C   1 
ATOM 1811 O O   . LEU A 1 258 ? 95.768  111.305 122.784 1.00 33.54  ? 258 LEU A O   1 
ATOM 1812 C CB  . LEU A 1 258 ? 96.172  109.416 124.854 1.00 15.82  ? 258 LEU A CB  1 
ATOM 1813 C CG  . LEU A 1 258 ? 96.183  108.196 125.773 1.00 25.22  ? 258 LEU A CG  1 
ATOM 1814 C CD1 . LEU A 1 258 ? 97.595  107.802 126.113 1.00 25.47  ? 258 LEU A CD1 1 
ATOM 1815 C CD2 . LEU A 1 258 ? 95.388  108.473 127.037 1.00 25.14  ? 258 LEU A CD2 1 
ATOM 1816 N N   . PRO A 1 259 ? 93.743  111.841 123.570 1.00 25.33  ? 259 PRO A N   1 
ATOM 1817 C CA  . PRO A 1 259 ? 93.641  113.025 122.704 1.00 32.71  ? 259 PRO A CA  1 
ATOM 1818 C C   . PRO A 1 259 ? 94.499  114.224 123.100 1.00 35.18  ? 259 PRO A C   1 
ATOM 1819 O O   . PRO A 1 259 ? 94.431  115.247 122.410 1.00 28.72  ? 259 PRO A O   1 
ATOM 1820 C CB  . PRO A 1 259 ? 92.150  113.377 122.802 1.00 29.27  ? 259 PRO A CB  1 
ATOM 1821 C CG  . PRO A 1 259 ? 91.762  112.926 124.159 1.00 33.26  ? 259 PRO A CG  1 
ATOM 1822 C CD  . PRO A 1 259 ? 92.558  111.679 124.430 1.00 26.70  ? 259 PRO A CD  1 
ATOM 1823 N N   . HIS A 1 260 ? 95.296  114.163 124.167 1.00 40.90  ? 260 HIS A N   1 
ATOM 1824 C CA  . HIS A 1 260 ? 96.125  115.289 124.588 1.00 27.52  ? 260 HIS A CA  1 
ATOM 1825 C C   . HIS A 1 260 ? 97.603  114.936 124.478 1.00 41.14  ? 260 HIS A C   1 
ATOM 1826 O O   . HIS A 1 260 ? 98.006  113.810 124.782 1.00 47.85  ? 260 HIS A O   1 
ATOM 1827 C CB  . HIS A 1 260 ? 95.792  115.724 126.017 1.00 28.56  ? 260 HIS A CB  1 
ATOM 1828 C CG  . HIS A 1 260 ? 94.436  116.342 126.161 1.00 31.79  ? 260 HIS A CG  1 
ATOM 1829 N ND1 . HIS A 1 260 ? 93.304  115.605 126.433 1.00 40.87  ? 260 HIS A ND1 1 
ATOM 1830 C CD2 . HIS A 1 260 ? 94.032  117.631 126.075 1.00 38.06  ? 260 HIS A CD2 1 
ATOM 1831 C CE1 . HIS A 1 260 ? 92.261  116.413 126.505 1.00 42.17  ? 260 HIS A CE1 1 
ATOM 1832 N NE2 . HIS A 1 260 ? 92.676  117.648 126.292 1.00 37.02  ? 260 HIS A NE2 1 
ATOM 1833 N N   . TRP A 1 261 ? 98.405  115.911 124.034 1.00 30.28  ? 261 TRP A N   1 
ATOM 1834 C CA  . TRP A 1 261 ? 99.801  115.643 123.685 1.00 29.90  ? 261 TRP A CA  1 
ATOM 1835 C C   . TRP A 1 261 ? 100.640 115.246 124.899 1.00 31.11  ? 261 TRP A C   1 
ATOM 1836 O O   . TRP A 1 261 ? 101.512 114.378 124.788 1.00 33.43  ? 261 TRP A O   1 
ATOM 1837 C CB  . TRP A 1 261 ? 100.395 116.844 122.934 1.00 30.86  ? 261 TRP A CB  1 
ATOM 1838 C CG  . TRP A 1 261 ? 100.825 118.048 123.742 1.00 32.73  ? 261 TRP A CG  1 
ATOM 1839 C CD1 . TRP A 1 261 ? 100.111 119.194 123.941 1.00 27.96  ? 261 TRP A CD1 1 
ATOM 1840 C CD2 . TRP A 1 261 ? 102.093 118.256 124.378 1.00 33.53  ? 261 TRP A CD2 1 
ATOM 1841 N NE1 . TRP A 1 261 ? 100.836 120.082 124.694 1.00 9.91   ? 261 TRP A NE1 1 
ATOM 1842 C CE2 . TRP A 1 261 ? 102.057 119.531 124.974 1.00 20.42  ? 261 TRP A CE2 1 
ATOM 1843 C CE3 . TRP A 1 261 ? 103.247 117.478 124.520 1.00 34.53  ? 261 TRP A CE3 1 
ATOM 1844 C CZ2 . TRP A 1 261 ? 103.127 120.045 125.700 1.00 26.75  ? 261 TRP A CZ2 1 
ATOM 1845 C CZ3 . TRP A 1 261 ? 104.306 117.990 125.241 1.00 25.61  ? 261 TRP A CZ3 1 
ATOM 1846 C CH2 . TRP A 1 261 ? 104.240 119.261 125.821 1.00 25.17  ? 261 TRP A CH2 1 
ATOM 1847 N N   . ARG A 1 262 ? 100.414 115.869 126.058 1.00 45.31  ? 262 ARG A N   1 
ATOM 1848 C CA  . ARG A 1 262 ? 101.190 115.507 127.244 1.00 37.95  ? 262 ARG A CA  1 
ATOM 1849 C C   . ARG A 1 262 ? 100.857 114.095 127.721 1.00 49.02  ? 262 ARG A C   1 
ATOM 1850 O O   . ARG A 1 262 ? 101.747 113.344 128.147 1.00 51.58  ? 262 ARG A O   1 
ATOM 1851 C CB  . ARG A 1 262 ? 100.933 116.511 128.365 1.00 38.97  ? 262 ARG A CB  1 
ATOM 1852 C CG  . ARG A 1 262 ? 101.423 117.916 128.082 1.00 45.62  ? 262 ARG A CG  1 
ATOM 1853 C CD  . ARG A 1 262 ? 101.354 118.786 129.326 1.00 48.49  ? 262 ARG A CD  1 
ATOM 1854 N NE  . ARG A 1 262 ? 101.520 120.200 129.013 1.00 47.51  ? 262 ARG A NE  1 
ATOM 1855 C CZ  . ARG A 1 262 ? 102.627 120.896 129.233 1.00 45.81  ? 262 ARG A CZ  1 
ATOM 1856 N NH1 . ARG A 1 262 ? 103.752 120.306 129.599 1.00 50.60  ? 262 ARG A NH1 1 
ATOM 1857 N NH2 . ARG A 1 262 ? 102.620 122.208 129.022 1.00 48.30  ? 262 ARG A NH2 1 
ATOM 1858 N N   . TRP A 1 263 ? 99.587  113.702 127.600 1.00 44.65  ? 263 TRP A N   1 
ATOM 1859 C CA  . TRP A 1 263 ? 99.181  112.339 127.928 1.00 31.09  ? 263 TRP A CA  1 
ATOM 1860 C C   . TRP A 1 263 ? 99.828  111.324 126.997 1.00 30.30  ? 263 TRP A C   1 
ATOM 1861 O O   . TRP A 1 263 ? 100.294 110.268 127.443 1.00 25.20  ? 263 TRP A O   1 
ATOM 1862 C CB  . TRP A 1 263 ? 97.660  112.220 127.843 1.00 30.26  ? 263 TRP A CB  1 
ATOM 1863 C CG  . TRP A 1 263 ? 96.903  113.073 128.812 1.00 31.11  ? 263 TRP A CG  1 
ATOM 1864 C CD1 . TRP A 1 263 ? 97.420  113.951 129.715 1.00 29.87  ? 263 TRP A CD1 1 
ATOM 1865 C CD2 . TRP A 1 263 ? 95.481  113.142 128.954 1.00 38.14  ? 263 TRP A CD2 1 
ATOM 1866 N NE1 . TRP A 1 263 ? 96.409  114.554 130.421 1.00 33.49  ? 263 TRP A NE1 1 
ATOM 1867 C CE2 . TRP A 1 263 ? 95.208  114.074 129.971 1.00 37.06  ? 263 TRP A CE2 1 
ATOM 1868 C CE3 . TRP A 1 263 ? 94.411  112.500 128.322 1.00 40.10  ? 263 TRP A CE3 1 
ATOM 1869 C CZ2 . TRP A 1 263 ? 93.910  114.383 130.371 1.00 35.98  ? 263 TRP A CZ2 1 
ATOM 1870 C CZ3 . TRP A 1 263 ? 93.126  112.807 128.721 1.00 38.47  ? 263 TRP A CZ3 1 
ATOM 1871 C CH2 . TRP A 1 263 ? 92.886  113.740 129.736 1.00 35.47  ? 263 TRP A CH2 1 
ATOM 1872 N N   . LEU A 1 264 ? 99.896  111.639 125.703 1.00 21.21  ? 264 LEU A N   1 
ATOM 1873 C CA  . LEU A 1 264 ? 100.534 110.725 124.767 1.00 21.16  ? 264 LEU A CA  1 
ATOM 1874 C C   . LEU A 1 264 ? 102.043 110.681 124.965 1.00 31.76  ? 264 LEU A C   1 
ATOM 1875 O O   . LEU A 1 264 ? 102.655 109.626 124.780 1.00 35.56  ? 264 LEU A O   1 
ATOM 1876 C CB  . LEU A 1 264 ? 100.185 111.131 123.335 1.00 27.08  ? 264 LEU A CB  1 
ATOM 1877 C CG  . LEU A 1 264 ? 100.684 110.257 122.185 1.00 32.78  ? 264 LEU A CG  1 
ATOM 1878 C CD1 . LEU A 1 264 ? 100.037 108.888 122.239 1.00 32.72  ? 264 LEU A CD1 1 
ATOM 1879 C CD2 . LEU A 1 264 ? 100.408 110.929 120.852 1.00 17.49  ? 264 LEU A CD2 1 
ATOM 1880 N N   . GLN A 1 265 ? 102.650 111.788 125.399 1.00 42.99  ? 265 GLN A N   1 
ATOM 1881 C CA  . GLN A 1 265 ? 104.089 111.791 125.646 1.00 33.43  ? 265 GLN A CA  1 
ATOM 1882 C C   . GLN A 1 265 ? 104.429 110.951 126.872 1.00 35.08  ? 265 GLN A C   1 
ATOM 1883 O O   . GLN A 1 265 ? 105.413 110.194 126.867 1.00 32.94  ? 265 GLN A O   1 
ATOM 1884 C CB  . GLN A 1 265 ? 104.579 113.230 125.814 1.00 31.46  ? 265 GLN A CB  1 
ATOM 1885 C CG  . GLN A 1 265 ? 106.075 113.386 126.037 1.00 43.58  ? 265 GLN A CG  1 
ATOM 1886 C CD  . GLN A 1 265 ? 106.900 112.860 124.881 1.00 44.10  ? 265 GLN A CD  1 
ATOM 1887 O OE1 . GLN A 1 265 ? 106.470 112.896 123.730 1.00 42.80  ? 265 GLN A OE1 1 
ATOM 1888 N NE2 . GLN A 1 265 ? 108.097 112.373 125.181 1.00 38.71  ? 265 GLN A NE2 1 
ATOM 1889 N N   . LEU A 1 266 ? 103.572 110.997 127.895 1.00 33.14  ? 266 LEU A N   1 
ATOM 1890 C CA  . LEU A 1 266 ? 103.770 110.122 129.046 1.00 28.06  ? 266 LEU A CA  1 
ATOM 1891 C C   . LEU A 1 266 ? 103.577 108.666 128.650 1.00 39.93  ? 266 LEU A C   1 
ATOM 1892 O O   . LEU A 1 266 ? 104.417 107.816 128.962 1.00 49.49  ? 266 LEU A O   1 
ATOM 1893 C CB  . LEU A 1 266 ? 102.813 110.500 130.175 1.00 37.41  ? 266 LEU A CB  1 
ATOM 1894 C CG  . LEU A 1 266 ? 103.133 111.755 130.984 1.00 42.33  ? 266 LEU A CG  1 
ATOM 1895 C CD1 . LEU A 1 266 ? 101.981 112.087 131.912 1.00 42.76  ? 266 LEU A CD1 1 
ATOM 1896 C CD2 . LEU A 1 266 ? 104.416 111.562 131.772 1.00 37.02  ? 266 LEU A CD2 1 
ATOM 1897 N N   . ALA A 1 267 ? 102.462 108.354 127.985 1.00 40.86  ? 267 ALA A N   1 
ATOM 1898 C CA  . ALA A 1 267 ? 102.184 106.969 127.616 1.00 38.31  ? 267 ALA A CA  1 
ATOM 1899 C C   . ALA A 1 267 ? 103.303 106.387 126.762 1.00 31.32  ? 267 ALA A C   1 
ATOM 1900 O O   . ALA A 1 267 ? 103.697 105.232 126.947 1.00 33.83  ? 267 ALA A O   1 
ATOM 1901 C CB  . ALA A 1 267 ? 100.851 106.875 126.883 1.00 36.69  ? 267 ALA A CB  1 
ATOM 1902 N N   . VAL A 1 268 ? 103.808 107.166 125.802 1.00 30.61  ? 268 VAL A N   1 
ATOM 1903 C CA  . VAL A 1 268 ? 104.904 106.724 124.946 1.00 27.16  ? 268 VAL A CA  1 
ATOM 1904 C C   . VAL A 1 268 ? 106.207 106.566 125.726 1.00 42.56  ? 268 VAL A C   1 
ATOM 1905 O O   . VAL A 1 268 ? 107.025 105.695 125.404 1.00 41.76  ? 268 VAL A O   1 
ATOM 1906 C CB  . VAL A 1 268 ? 105.053 107.709 123.770 1.00 31.76  ? 268 VAL A CB  1 
ATOM 1907 C CG1 . VAL A 1 268 ? 106.422 107.596 123.125 1.00 36.02  ? 268 VAL A CG1 1 
ATOM 1908 C CG2 . VAL A 1 268 ? 103.960 107.469 122.744 1.00 39.25  ? 268 VAL A CG2 1 
ATOM 1909 N N   . SER A 1 269 ? 106.412 107.358 126.779 1.00 54.08  ? 269 SER A N   1 
ATOM 1910 C CA  . SER A 1 269 ? 107.700 107.321 127.469 1.00 39.98  ? 269 SER A CA  1 
ATOM 1911 C C   . SER A 1 269 ? 107.806 106.226 128.530 1.00 44.77  ? 269 SER A C   1 
ATOM 1912 O O   . SER A 1 269 ? 108.857 105.586 128.641 1.00 44.07  ? 269 SER A O   1 
ATOM 1913 C CB  . SER A 1 269 ? 107.984 108.681 128.105 1.00 40.36  ? 269 SER A CB  1 
ATOM 1914 O OG  . SER A 1 269 ? 107.991 109.700 127.123 1.00 41.34  ? 269 SER A OG  1 
ATOM 1915 N N   . LEU A 1 270 ? 106.758 106.007 129.321 1.00 53.86  ? 270 LEU A N   1 
ATOM 1916 C CA  . LEU A 1 270 ? 106.826 105.061 130.436 1.00 56.31  ? 270 LEU A CA  1 
ATOM 1917 C C   . LEU A 1 270 ? 107.306 103.649 130.092 1.00 65.07  ? 270 LEU A C   1 
ATOM 1918 O O   . LEU A 1 270 ? 108.034 103.069 130.915 1.00 66.61  ? 270 LEU A O   1 
ATOM 1919 C CB  . LEU A 1 270 ? 105.451 104.986 131.115 1.00 55.68  ? 270 LEU A CB  1 
ATOM 1920 C CG  . LEU A 1 270 ? 105.008 106.227 131.891 1.00 60.88  ? 270 LEU A CG  1 
ATOM 1921 C CD1 . LEU A 1 270 ? 103.573 106.076 132.371 1.00 59.07  ? 270 LEU A CD1 1 
ATOM 1922 C CD2 . LEU A 1 270 ? 105.944 106.499 133.058 1.00 57.40  ? 270 LEU A CD2 1 
ATOM 1923 N N   . PRO A 1 271 ? 106.945 103.033 128.957 1.00 68.86  ? 271 PRO A N   1 
ATOM 1924 C CA  . PRO A 1 271 ? 107.473 101.687 128.654 1.00 62.38  ? 271 PRO A CA  1 
ATOM 1925 C C   . PRO A 1 271 ? 108.989 101.562 128.696 1.00 65.85  ? 271 PRO A C   1 
ATOM 1926 O O   . PRO A 1 271 ? 109.499 100.483 129.023 1.00 64.98  ? 271 PRO A O   1 
ATOM 1927 C CB  . PRO A 1 271 ? 106.928 101.418 127.246 1.00 60.84  ? 271 PRO A CB  1 
ATOM 1928 C CG  . PRO A 1 271 ? 105.661 102.164 127.212 1.00 62.49  ? 271 PRO A CG  1 
ATOM 1929 C CD  . PRO A 1 271 ? 105.932 103.435 127.964 1.00 63.26  ? 271 PRO A CD  1 
ATOM 1930 N N   . THR A 1 272 ? 109.727 102.623 128.359 1.00 69.07  ? 272 THR A N   1 
ATOM 1931 C CA  . THR A 1 272 ? 111.186 102.551 128.374 1.00 67.48  ? 272 THR A CA  1 
ATOM 1932 C C   . THR A 1 272 ? 111.741 102.294 129.772 1.00 63.95  ? 272 THR A C   1 
ATOM 1933 O O   . THR A 1 272 ? 112.780 101.638 129.910 1.00 63.05  ? 272 THR A O   1 
ATOM 1934 C CB  . THR A 1 272 ? 111.781 103.836 127.797 1.00 65.89  ? 272 THR A CB  1 
ATOM 1935 O OG1 . THR A 1 272 ? 111.412 104.950 128.619 1.00 69.71  ? 272 THR A OG1 1 
ATOM 1936 C CG2 . THR A 1 272 ? 111.276 104.067 126.381 1.00 64.39  ? 272 THR A CG2 1 
ATOM 1937 N N   . PHE A 1 273 ? 111.074 102.795 130.816 1.00 60.95  ? 273 PHE A N   1 
ATOM 1938 C CA  . PHE A 1 273 ? 111.495 102.482 132.179 1.00 63.42  ? 273 PHE A CA  1 
ATOM 1939 C C   . PHE A 1 273 ? 111.390 100.999 132.508 1.00 69.86  ? 273 PHE A C   1 
ATOM 1940 O O   . PHE A 1 273 ? 112.078 100.533 133.421 1.00 70.05  ? 273 PHE A O   1 
ATOM 1941 C CB  . PHE A 1 273 ? 110.674 103.278 133.194 1.00 65.20  ? 273 PHE A CB  1 
ATOM 1942 C CG  . PHE A 1 273 ? 111.214 104.649 133.469 1.00 69.28  ? 273 PHE A CG  1 
ATOM 1943 C CD1 . PHE A 1 273 ? 112.443 104.808 134.086 1.00 67.83  ? 273 PHE A CD1 1 
ATOM 1944 C CD2 . PHE A 1 273 ? 110.489 105.776 133.132 1.00 68.75  ? 273 PHE A CD2 1 
ATOM 1945 C CE1 . PHE A 1 273 ? 112.944 106.066 134.348 1.00 66.14  ? 273 PHE A CE1 1 
ATOM 1946 C CE2 . PHE A 1 273 ? 110.985 107.035 133.394 1.00 65.99  ? 273 PHE A CE2 1 
ATOM 1947 C CZ  . PHE A 1 273 ? 112.213 107.180 134.002 1.00 67.64  ? 273 PHE A CZ  1 
ATOM 1948 N N   . LEU A 1 274 ? 110.549 100.248 131.796 1.00 81.29  ? 274 LEU A N   1 
ATOM 1949 C CA  . LEU A 1 274 ? 110.377 98.835  132.107 1.00 79.06  ? 274 LEU A CA  1 
ATOM 1950 C C   . LEU A 1 274 ? 111.533 97.983  131.602 1.00 77.98  ? 274 LEU A C   1 
ATOM 1951 O O   . LEU A 1 274 ? 111.741 96.878  132.114 1.00 77.86  ? 274 LEU A O   1 
ATOM 1952 C CB  . LEU A 1 274 ? 109.057 98.325  131.526 1.00 83.71  ? 274 LEU A CB  1 
ATOM 1953 C CG  . LEU A 1 274 ? 107.826 99.153  131.902 1.00 82.76  ? 274 LEU A CG  1 
ATOM 1954 C CD1 . LEU A 1 274 ? 106.555 98.509  131.367 1.00 80.90  ? 274 LEU A CD1 1 
ATOM 1955 C CD2 . LEU A 1 274 ? 107.746 99.345  133.410 1.00 78.13  ? 274 LEU A CD2 1 
ATOM 1956 N N   . PHE A 1 275 ? 112.283 98.471  130.613 1.00 82.38  ? 275 PHE A N   1 
ATOM 1957 C CA  . PHE A 1 275 ? 113.494 97.780  130.184 1.00 85.96  ? 275 PHE A CA  1 
ATOM 1958 C C   . PHE A 1 275 ? 114.546 97.808  131.287 1.00 85.94  ? 275 PHE A C   1 
ATOM 1959 O O   . PHE A 1 275 ? 115.199 96.794  131.559 1.00 85.86  ? 275 PHE A O   1 
ATOM 1960 C CB  . PHE A 1 275 ? 114.020 98.418  128.893 1.00 86.25  ? 275 PHE A CB  1 
ATOM 1961 C CG  . PHE A 1 275 ? 115.187 97.693  128.267 1.00 87.62  ? 275 PHE A CG  1 
ATOM 1962 C CD1 . PHE A 1 275 ? 116.454 97.746  128.827 1.00 87.79  ? 275 PHE A CD1 1 
ATOM 1963 C CD2 . PHE A 1 275 ? 115.012 96.968  127.101 1.00 86.03  ? 275 PHE A CD2 1 
ATOM 1964 C CE1 . PHE A 1 275 ? 117.515 97.082  128.243 1.00 86.68  ? 275 PHE A CE1 1 
ATOM 1965 C CE2 . PHE A 1 275 ? 116.069 96.304  126.514 1.00 86.57  ? 275 PHE A CE2 1 
ATOM 1966 C CZ  . PHE A 1 275 ? 117.322 96.361  127.085 1.00 85.49  ? 275 PHE A CZ  1 
ATOM 1967 N N   . LEU A 1 276 ? 114.724 98.967  131.924 1.00 80.00  ? 276 LEU A N   1 
ATOM 1968 C CA  . LEU A 1 276 ? 115.611 99.067  133.079 1.00 77.96  ? 276 LEU A CA  1 
ATOM 1969 C C   . LEU A 1 276 ? 115.152 98.159  134.214 1.00 79.69  ? 276 LEU A C   1 
ATOM 1970 O O   . LEU A 1 276 ? 115.979 97.589  134.935 1.00 81.61  ? 276 LEU A O   1 
ATOM 1971 C CB  . LEU A 1 276 ? 115.673 100.517 133.558 1.00 81.61  ? 276 LEU A CB  1 
ATOM 1972 C CG  . LEU A 1 276 ? 116.248 101.550 132.589 1.00 76.75  ? 276 LEU A CG  1 
ATOM 1973 C CD1 . LEU A 1 276 ? 115.955 102.956 133.081 1.00 74.86  ? 276 LEU A CD1 1 
ATOM 1974 C CD2 . LEU A 1 276 ? 117.736 101.345 132.417 1.00 79.22  ? 276 LEU A CD2 1 
ATOM 1975 N N   . LEU A 1 277 ? 113.837 98.011  134.386 1.00 89.57  ? 277 LEU A N   1 
ATOM 1976 C CA  . LEU A 1 277 ? 113.315 97.176  135.463 1.00 91.98  ? 277 LEU A CA  1 
ATOM 1977 C C   . LEU A 1 277 ? 113.514 95.693  135.182 1.00 93.04  ? 277 LEU A C   1 
ATOM 1978 O O   . LEU A 1 277 ? 113.719 94.912  136.118 1.00 90.54  ? 277 LEU A O   1 
ATOM 1979 C CB  . LEU A 1 277 ? 111.835 97.484  135.690 1.00 92.97  ? 277 LEU A CB  1 
ATOM 1980 C CG  . LEU A 1 277 ? 111.155 96.787  136.869 1.00 94.14  ? 277 LEU A CG  1 
ATOM 1981 C CD1 . LEU A 1 277 ? 111.857 97.134  138.173 1.00 92.92  ? 277 LEU A CD1 1 
ATOM 1982 C CD2 . LEU A 1 277 ? 109.688 97.171  136.934 1.00 94.28  ? 277 LEU A CD2 1 
ATOM 1983 N N   . TYR A 1 278 ? 113.443 95.283  133.912 1.00 107.11 ? 278 TYR A N   1 
ATOM 1984 C CA  . TYR A 1 278 ? 113.766 93.903  133.560 1.00 106.82 ? 278 TYR A CA  1 
ATOM 1985 C C   . TYR A 1 278 ? 115.180 93.541  134.000 1.00 106.82 ? 278 TYR A C   1 
ATOM 1986 O O   . TYR A 1 278 ? 115.406 92.462  134.561 1.00 105.77 ? 278 TYR A O   1 
ATOM 1987 C CB  . TYR A 1 278 ? 113.592 93.695  132.053 1.00 105.39 ? 278 TYR A CB  1 
ATOM 1988 C CG  . TYR A 1 278 ? 114.017 92.333  131.539 1.00 107.35 ? 278 TYR A CG  1 
ATOM 1989 C CD1 . TYR A 1 278 ? 115.343 92.065  131.218 1.00 105.39 ? 278 TYR A CD1 1 
ATOM 1990 C CD2 . TYR A 1 278 ? 113.087 91.314  131.370 1.00 108.47 ? 278 TYR A CD2 1 
ATOM 1991 C CE1 . TYR A 1 278 ? 115.731 90.824  130.749 1.00 106.80 ? 278 TYR A CE1 1 
ATOM 1992 C CE2 . TYR A 1 278 ? 113.466 90.069  130.900 1.00 107.94 ? 278 TYR A CE2 1 
ATOM 1993 C CZ  . TYR A 1 278 ? 114.788 89.830  130.593 1.00 108.39 ? 278 TYR A CZ  1 
ATOM 1994 O OH  . TYR A 1 278 ? 115.171 88.595  130.125 1.00 105.99 ? 278 TYR A OH  1 
ATOM 1995 N N   . TYR A 1 279 ? 116.141 94.425  133.753 1.00 111.33 ? 279 TYR A N   1 
ATOM 1996 C CA  . TYR A 1 279 ? 117.474 94.283  134.327 1.00 111.98 ? 279 TYR A CA  1 
ATOM 1997 C C   . TYR A 1 279 ? 117.547 94.936  135.704 1.00 111.70 ? 279 TYR A C   1 
ATOM 1998 O O   . TYR A 1 279 ? 116.958 94.446  136.667 1.00 111.91 ? 279 TYR A O   1 
ATOM 1999 C CB  . TYR A 1 279 ? 118.527 94.890  133.400 1.00 110.50 ? 279 TYR A CB  1 
ATOM 2000 C CG  . TYR A 1 279 ? 118.727 94.121  132.115 1.00 112.76 ? 279 TYR A CG  1 
ATOM 2001 C CD1 . TYR A 1 279 ? 119.351 92.881  132.117 1.00 112.47 ? 279 TYR A CD1 1 
ATOM 2002 C CD2 . TYR A 1 279 ? 118.295 94.636  130.901 1.00 112.64 ? 279 TYR A CD2 1 
ATOM 2003 C CE1 . TYR A 1 279 ? 119.530 92.169  130.946 1.00 112.77 ? 279 TYR A CE1 1 
ATOM 2004 C CE2 . TYR A 1 279 ? 118.476 93.935  129.724 1.00 113.01 ? 279 TYR A CE2 1 
ATOM 2005 C CZ  . TYR A 1 279 ? 119.092 92.702  129.752 1.00 113.06 ? 279 TYR A CZ  1 
ATOM 2006 O OH  . TYR A 1 279 ? 119.282 92.005  128.582 1.00 111.79 ? 279 TYR A OH  1 
ATOM 2007 N N   . SER A 1 331 ? 144.384 99.428  111.040 1.00 92.31  ? 331 SER A N   1 
ATOM 2008 C CA  . SER A 1 331 ? 143.212 100.216 111.401 1.00 93.57  ? 331 SER A CA  1 
ATOM 2009 C C   . SER A 1 331 ? 142.689 100.991 110.194 1.00 94.67  ? 331 SER A C   1 
ATOM 2010 O O   . SER A 1 331 ? 143.453 101.312 109.283 1.00 92.58  ? 331 SER A O   1 
ATOM 2011 C CB  . SER A 1 331 ? 143.552 101.175 112.546 1.00 93.69  ? 331 SER A CB  1 
ATOM 2012 O OG  . SER A 1 331 ? 144.574 102.081 112.168 1.00 93.85  ? 331 SER A OG  1 
ATOM 2013 N N   . PRO A 1 332 ? 141.396 101.301 110.186 1.00 101.78 ? 332 PRO A N   1 
ATOM 2014 C CA  . PRO A 1 332 ? 140.825 102.059 109.071 1.00 100.98 ? 332 PRO A CA  1 
ATOM 2015 C C   . PRO A 1 332 ? 141.177 103.537 109.156 1.00 98.56  ? 332 PRO A C   1 
ATOM 2016 O O   . PRO A 1 332 ? 141.580 104.055 110.199 1.00 99.11  ? 332 PRO A O   1 
ATOM 2017 C CB  . PRO A 1 332 ? 139.317 101.840 109.230 1.00 100.98 ? 332 PRO A CB  1 
ATOM 2018 C CG  . PRO A 1 332 ? 139.132 101.615 110.686 1.00 100.32 ? 332 PRO A CG  1 
ATOM 2019 C CD  . PRO A 1 332 ? 140.370 100.905 111.168 1.00 100.06 ? 332 PRO A CD  1 
ATOM 2020 N N   . SER A 1 333 ? 141.015 104.215 108.022 1.00 100.69 ? 333 SER A N   1 
ATOM 2021 C CA  . SER A 1 333 ? 141.236 105.651 107.960 1.00 101.12 ? 333 SER A CA  1 
ATOM 2022 C C   . SER A 1 333 ? 140.305 106.265 106.926 1.00 104.07 ? 333 SER A C   1 
ATOM 2023 O O   . SER A 1 333 ? 139.992 105.649 105.903 1.00 104.87 ? 333 SER A O   1 
ATOM 2024 C CB  . SER A 1 333 ? 142.694 105.982 107.622 1.00 99.94  ? 333 SER A CB  1 
ATOM 2025 O OG  . SER A 1 333 ? 142.898 107.383 107.571 1.00 101.00 ? 333 SER A OG  1 
ATOM 2026 N N   . PHE A 1 334 ? 139.859 107.490 107.221 1.00 101.02 ? 334 PHE A N   1 
ATOM 2027 C CA  . PHE A 1 334 ? 138.845 108.157 106.409 1.00 99.64  ? 334 PHE A CA  1 
ATOM 2028 C C   . PHE A 1 334 ? 139.282 108.296 104.955 1.00 99.33  ? 334 PHE A C   1 
ATOM 2029 O O   . PHE A 1 334 ? 138.444 108.247 104.048 1.00 100.37 ? 334 PHE A O   1 
ATOM 2030 C CB  . PHE A 1 334 ? 138.526 109.524 107.017 1.00 99.12  ? 334 PHE A CB  1 
ATOM 2031 C CG  . PHE A 1 334 ? 137.514 110.318 106.246 1.00 98.86  ? 334 PHE A CG  1 
ATOM 2032 C CD1 . PHE A 1 334 ? 136.161 110.154 106.488 1.00 97.31  ? 334 PHE A CD1 1 
ATOM 2033 C CD2 . PHE A 1 334 ? 137.913 111.250 105.303 1.00 99.14  ? 334 PHE A CD2 1 
ATOM 2034 C CE1 . PHE A 1 334 ? 135.224 110.888 105.790 1.00 97.76  ? 334 PHE A CE1 1 
ATOM 2035 C CE2 . PHE A 1 334 ? 136.980 111.987 104.601 1.00 100.63 ? 334 PHE A CE2 1 
ATOM 2036 C CZ  . PHE A 1 334 ? 135.634 111.806 104.846 1.00 98.58  ? 334 PHE A CZ  1 
ATOM 2037 N N   . ALA A 1 335 ? 140.584 108.473 104.717 1.00 98.74  ? 335 ALA A N   1 
ATOM 2038 C CA  . ALA A 1 335 ? 141.094 108.749 103.377 1.00 101.67 ? 335 ALA A CA  1 
ATOM 2039 C C   . ALA A 1 335 ? 140.831 107.613 102.396 1.00 101.36 ? 335 ALA A C   1 
ATOM 2040 O O   . ALA A 1 335 ? 140.794 107.856 101.184 1.00 99.59  ? 335 ALA A O   1 
ATOM 2041 C CB  . ALA A 1 335 ? 142.594 109.043 103.439 1.00 101.06 ? 335 ALA A CB  1 
ATOM 2042 N N   . ASP A 1 336 ? 140.658 106.384 102.886 1.00 102.21 ? 336 ASP A N   1 
ATOM 2043 C CA  . ASP A 1 336 ? 140.613 105.220 102.004 1.00 102.62 ? 336 ASP A CA  1 
ATOM 2044 C C   . ASP A 1 336 ? 139.389 105.243 101.095 1.00 103.56 ? 336 ASP A C   1 
ATOM 2045 O O   . ASP A 1 336 ? 139.469 104.832 99.932  1.00 102.24 ? 336 ASP A O   1 
ATOM 2046 C CB  . ASP A 1 336 ? 140.637 103.937 102.833 1.00 101.40 ? 336 ASP A CB  1 
ATOM 2047 C CG  . ASP A 1 336 ? 140.998 102.717 102.011 1.00 102.01 ? 336 ASP A CG  1 
ATOM 2048 O OD1 . ASP A 1 336 ? 141.899 102.821 101.154 1.00 101.13 ? 336 ASP A OD1 1 
ATOM 2049 O OD2 . ASP A 1 336 ? 140.378 101.654 102.221 1.00 102.46 ? 336 ASP A OD2 1 
ATOM 2050 N N   . LEU A 1 337 ? 138.249 105.722 101.600 1.00 99.96  ? 337 LEU A N   1 
ATOM 2051 C CA  . LEU A 1 337 ? 136.991 105.660 100.860 1.00 98.60  ? 337 LEU A CA  1 
ATOM 2052 C C   . LEU A 1 337 ? 137.018 106.449 99.555  1.00 98.51  ? 337 LEU A C   1 
ATOM 2053 O O   . LEU A 1 337 ? 136.120 106.268 98.726  1.00 98.82  ? 337 LEU A O   1 
ATOM 2054 C CB  . LEU A 1 337 ? 135.844 106.162 101.737 1.00 98.58  ? 337 LEU A CB  1 
ATOM 2055 C CG  . LEU A 1 337 ? 135.705 105.513 103.115 1.00 100.77 ? 337 LEU A CG  1 
ATOM 2056 C CD1 . LEU A 1 337 ? 134.514 106.092 103.857 1.00 102.19 ? 337 LEU A CD1 1 
ATOM 2057 C CD2 . LEU A 1 337 ? 135.583 104.004 102.994 1.00 98.20  ? 337 LEU A CD2 1 
ATOM 2058 N N   . PHE A 1 338 ? 138.013 107.311 99.352  1.00 97.65  ? 338 PHE A N   1 
ATOM 2059 C CA  . PHE A 1 338 ? 138.093 108.171 98.180  1.00 98.62  ? 338 PHE A CA  1 
ATOM 2060 C C   . PHE A 1 338 ? 139.369 107.963 97.378  1.00 99.32  ? 338 PHE A C   1 
ATOM 2061 O O   . PHE A 1 338 ? 139.565 108.641 96.362  1.00 98.74  ? 338 PHE A O   1 
ATOM 2062 C CB  . PHE A 1 338 ? 137.960 109.644 98.587  1.00 96.86  ? 338 PHE A CB  1 
ATOM 2063 C CG  . PHE A 1 338 ? 136.847 109.898 99.560  1.00 99.68  ? 338 PHE A CG  1 
ATOM 2064 C CD1 . PHE A 1 338 ? 135.536 109.980 99.120  1.00 98.17  ? 338 PHE A CD1 1 
ATOM 2065 C CD2 . PHE A 1 338 ? 137.105 110.038 100.912 1.00 98.19  ? 338 PHE A CD2 1 
ATOM 2066 C CE1 . PHE A 1 338 ? 134.505 110.207 100.010 1.00 98.06  ? 338 PHE A CE1 1 
ATOM 2067 C CE2 . PHE A 1 338 ? 136.077 110.263 101.806 1.00 97.91  ? 338 PHE A CE2 1 
ATOM 2068 C CZ  . PHE A 1 338 ? 134.776 110.349 101.355 1.00 98.37  ? 338 PHE A CZ  1 
ATOM 2069 N N   . ARG A 1 339 ? 140.240 107.048 97.806  1.00 105.16 ? 339 ARG A N   1 
ATOM 2070 C CA  . ARG A 1 339 ? 141.583 106.931 97.253  1.00 106.76 ? 339 ARG A CA  1 
ATOM 2071 C C   . ARG A 1 339 ? 141.583 106.349 95.843  1.00 107.50 ? 339 ARG A C   1 
ATOM 2072 O O   . ARG A 1 339 ? 142.529 106.594 95.086  1.00 105.85 ? 339 ARG A O   1 
ATOM 2073 C CB  . ARG A 1 339 ? 142.451 106.077 98.179  1.00 105.48 ? 339 ARG A CB  1 
ATOM 2074 C CG  . ARG A 1 339 ? 143.936 106.113 97.862  1.00 105.58 ? 339 ARG A CG  1 
ATOM 2075 C CD  . ARG A 1 339 ? 144.744 105.406 98.934  1.00 105.69 ? 339 ARG A CD  1 
ATOM 2076 N NE  . ARG A 1 339 ? 146.175 105.466 98.662  1.00 106.31 ? 339 ARG A NE  1 
ATOM 2077 C CZ  . ARG A 1 339 ? 146.962 106.471 99.019  1.00 106.98 ? 339 ARG A CZ  1 
ATOM 2078 N NH1 . ARG A 1 339 ? 146.487 107.530 99.655  1.00 106.96 ? 339 ARG A NH1 1 
ATOM 2079 N NH2 . ARG A 1 339 ? 148.258 106.416 98.727  1.00 107.05 ? 339 ARG A NH2 1 
ATOM 2080 N N   . THR A 1 340 ? 140.548 105.599 95.469  1.00 105.72 ? 340 THR A N   1 
ATOM 2081 C CA  . THR A 1 340 ? 140.469 104.981 94.155  1.00 103.74 ? 340 THR A CA  1 
ATOM 2082 C C   . THR A 1 340 ? 139.137 105.329 93.502  1.00 103.08 ? 340 THR A C   1 
ATOM 2083 O O   . THR A 1 340 ? 138.098 105.343 94.175  1.00 99.72  ? 340 THR A O   1 
ATOM 2084 C CB  . THR A 1 340 ? 140.617 103.451 94.294  1.00 101.40 ? 340 THR A CB  1 
ATOM 2085 O OG1 . THR A 1 340 ? 141.855 103.148 94.949  1.00 102.01 ? 340 THR A OG1 1 
ATOM 2086 C CG2 . THR A 1 340 ? 140.586 102.746 92.947  1.00 99.92  ? 340 THR A CG2 1 
ATOM 2087 N N   . PRO A 1 341 ? 139.138 105.632 92.198  1.00 103.40 ? 341 PRO A N   1 
ATOM 2088 C CA  . PRO A 1 341 ? 137.905 106.118 91.553  1.00 102.90 ? 341 PRO A CA  1 
ATOM 2089 C C   . PRO A 1 341 ? 136.739 105.143 91.590  1.00 102.08 ? 341 PRO A C   1 
ATOM 2090 O O   . PRO A 1 341 ? 135.588 105.589 91.625  1.00 102.18 ? 341 PRO A O   1 
ATOM 2091 C CB  . PRO A 1 341 ? 138.354 106.417 90.114  1.00 100.65 ? 341 PRO A CB  1 
ATOM 2092 C CG  . PRO A 1 341 ? 139.612 105.644 89.923  1.00 99.34  ? 341 PRO A CG  1 
ATOM 2093 C CD  . PRO A 1 341 ? 140.277 105.656 91.266  1.00 101.28 ? 341 PRO A CD  1 
ATOM 2094 N N   . ARG A 1 342 ? 136.988 103.834 91.557  1.00 98.17  ? 342 ARG A N   1 
ATOM 2095 C CA  . ARG A 1 342 ? 135.898 102.869 91.690  1.00 98.81  ? 342 ARG A CA  1 
ATOM 2096 C C   . ARG A 1 342 ? 135.250 102.943 93.070  1.00 97.89  ? 342 ARG A C   1 
ATOM 2097 O O   . ARG A 1 342 ? 134.018 103.006 93.193  1.00 97.85  ? 342 ARG A O   1 
ATOM 2098 C CB  . ARG A 1 342 ? 136.416 101.459 91.410  1.00 98.46  ? 342 ARG A CB  1 
ATOM 2099 C CG  . ARG A 1 342 ? 136.882 101.253 89.979  1.00 99.96  ? 342 ARG A CG  1 
ATOM 2100 C CD  . ARG A 1 342 ? 137.335 99.824  89.738  1.00 100.47 ? 342 ARG A CD  1 
ATOM 2101 N NE  . ARG A 1 342 ? 137.881 99.648  88.397  1.00 101.06 ? 342 ARG A NE  1 
ATOM 2102 C CZ  . ARG A 1 342 ? 138.427 98.526  87.951  1.00 100.75 ? 342 ARG A CZ  1 
ATOM 2103 N NH1 . ARG A 1 342 ? 138.473 97.435  88.697  1.00 99.11  ? 342 ARG A NH1 1 
ATOM 2104 N NH2 . ARG A 1 342 ? 138.927 98.493  86.719  1.00 99.37  ? 342 ARG A NH2 1 
ATOM 2105 N N   . LEU A 1 343 ? 136.071 102.933 94.121  1.00 94.63  ? 343 LEU A N   1 
ATOM 2106 C CA  . LEU A 1 343 ? 135.565 103.068 95.483  1.00 93.22  ? 343 LEU A CA  1 
ATOM 2107 C C   . LEU A 1 343 ? 134.954 104.441 95.730  1.00 94.61  ? 343 LEU A C   1 
ATOM 2108 O O   . LEU A 1 343 ? 133.953 104.549 96.447  1.00 94.49  ? 343 LEU A O   1 
ATOM 2109 C CB  . LEU A 1 343 ? 136.686 102.790 96.484  1.00 91.10  ? 343 LEU A CB  1 
ATOM 2110 C CG  . LEU A 1 343 ? 136.317 102.835 97.967  1.00 94.01  ? 343 LEU A CG  1 
ATOM 2111 C CD1 . LEU A 1 343 ? 135.196 101.854 98.269  1.00 94.65  ? 343 LEU A CD1 1 
ATOM 2112 C CD2 . LEU A 1 343 ? 137.534 102.527 98.819  1.00 94.11  ? 343 LEU A CD2 1 
ATOM 2113 N N   . ARG A 1 344 ? 135.493 105.485 95.096  1.00 87.76  ? 344 ARG A N   1 
ATOM 2114 C CA  . ARG A 1 344 ? 134.837 106.790 95.117  1.00 88.62  ? 344 ARG A CA  1 
ATOM 2115 C C   . ARG A 1 344 ? 133.447 106.722 94.494  1.00 87.59  ? 344 ARG A C   1 
ATOM 2116 O O   . ARG A 1 344 ? 132.479 107.247 95.056  1.00 85.27  ? 344 ARG A O   1 
ATOM 2117 C CB  . ARG A 1 344 ? 135.700 107.808 94.373  1.00 86.38  ? 344 ARG A CB  1 
ATOM 2118 C CG  . ARG A 1 344 ? 135.217 109.237 94.490  1.00 85.19  ? 344 ARG A CG  1 
ATOM 2119 C CD  . ARG A 1 344 ? 136.020 110.172 93.601  1.00 86.96  ? 344 ARG A CD  1 
ATOM 2120 N NE  . ARG A 1 344 ? 137.448 110.128 93.892  1.00 89.23  ? 344 ARG A NE  1 
ATOM 2121 C CZ  . ARG A 1 344 ? 138.395 110.500 93.042  1.00 89.72  ? 344 ARG A CZ  1 
ATOM 2122 N NH1 . ARG A 1 344 ? 138.099 111.013 91.859  1.00 88.10  ? 344 ARG A NH1 1 
ATOM 2123 N NH2 . ARG A 1 344 ? 139.671 110.371 93.395  1.00 90.61  ? 344 ARG A NH2 1 
ATOM 2124 N N   . LYS A 1 345 ? 133.351 106.165 93.288  1.00 83.64  ? 345 LYS A N   1 
ATOM 2125 C CA  . LYS A 1 345 ? 132.075 106.048 92.590  1.00 83.74  ? 345 LYS A CA  1 
ATOM 2126 C C   . LYS A 1 345 ? 131.035 105.338 93.450  1.00 82.60  ? 345 LYS A C   1 
ATOM 2127 O O   . LYS A 1 345 ? 129.920 105.839 93.653  1.00 83.39  ? 345 LYS A O   1 
ATOM 2128 C CB  . LYS A 1 345 ? 132.286 105.299 91.272  1.00 80.61  ? 345 LYS A CB  1 
ATOM 2129 C CG  . LYS A 1 345 ? 131.030 105.058 90.457  1.00 81.79  ? 345 LYS A CG  1 
ATOM 2130 C CD  . LYS A 1 345 ? 131.373 104.375 89.141  1.00 81.25  ? 345 LYS A CD  1 
ATOM 2131 C CE  . LYS A 1 345 ? 130.133 104.119 88.302  1.00 82.19  ? 345 LYS A CE  1 
ATOM 2132 N NZ  . LYS A 1 345 ? 130.470 103.530 86.977  1.00 81.37  ? 345 LYS A NZ  1 
ATOM 2133 N N   . ARG A 1 346 ? 131.394 104.155 93.954  1.00 78.25  ? 346 ARG A N   1 
ATOM 2134 C CA  . ARG A 1 346 ? 130.522 103.405 94.856  1.00 79.21  ? 346 ARG A CA  1 
ATOM 2135 C C   . ARG A 1 346 ? 130.118 104.220 96.082  1.00 79.87  ? 346 ARG A C   1 
ATOM 2136 O O   . ARG A 1 346 ? 128.942 104.240 96.463  1.00 79.13  ? 346 ARG A O   1 
ATOM 2137 C CB  . ARG A 1 346 ? 131.207 102.105 95.277  1.00 80.94  ? 346 ARG A CB  1 
ATOM 2138 C CG  . ARG A 1 346 ? 131.409 101.127 94.134  1.00 80.30  ? 346 ARG A CG  1 
ATOM 2139 C CD  . ARG A 1 346 ? 132.319 99.979  94.535  1.00 80.98  ? 346 ARG A CD  1 
ATOM 2140 N NE  . ARG A 1 346 ? 132.760 99.218  93.373  1.00 84.13  ? 346 ARG A NE  1 
ATOM 2141 C CZ  . ARG A 1 346 ? 133.829 98.434  93.351  1.00 83.35  ? 346 ARG A CZ  1 
ATOM 2142 N NH1 . ARG A 1 346 ? 134.524 98.183  94.449  1.00 80.97  ? 346 ARG A NH1 1 
ATOM 2143 N NH2 . ARG A 1 346 ? 134.187 97.858  92.208  1.00 82.66  ? 346 ARG A NH2 1 
ATOM 2144 N N   . THR A 1 347 ? 131.080 104.886 96.725  1.00 75.43  ? 347 THR A N   1 
ATOM 2145 C CA  . THR A 1 347 ? 130.778 105.682 97.911  1.00 76.63  ? 347 THR A CA  1 
ATOM 2146 C C   . THR A 1 347 ? 129.789 106.806 97.615  1.00 77.10  ? 347 THR A C   1 
ATOM 2147 O O   . THR A 1 347 ? 128.815 106.992 98.350  1.00 78.99  ? 347 THR A O   1 
ATOM 2148 C CB  . THR A 1 347 ? 132.073 106.247 98.497  1.00 77.12  ? 347 THR A CB  1 
ATOM 2149 O OG1 . THR A 1 347 ? 132.942 105.169 98.864  1.00 78.32  ? 347 THR A OG1 1 
ATOM 2150 C CG2 . THR A 1 347 ? 131.779 107.090 99.727  1.00 76.66  ? 347 THR A CG2 1 
ATOM 2151 N N   . PHE A 1 348 ? 130.041 107.587 96.564  1.00 67.83  ? 348 PHE A N   1 
ATOM 2152 C CA  . PHE A 1 348 ? 129.143 108.689 96.217  1.00 66.87  ? 348 PHE A CA  1 
ATOM 2153 C C   . PHE A 1 348 ? 127.751 108.214 95.803  1.00 71.24  ? 348 PHE A C   1 
ATOM 2154 O O   . PHE A 1 348 ? 126.745 108.830 96.179  1.00 69.25  ? 348 PHE A O   1 
ATOM 2155 C CB  . PHE A 1 348 ? 129.751 109.542 95.103  1.00 67.59  ? 348 PHE A CB  1 
ATOM 2156 C CG  . PHE A 1 348 ? 130.970 110.314 95.517  1.00 68.38  ? 348 PHE A CG  1 
ATOM 2157 C CD1 . PHE A 1 348 ? 131.297 110.464 96.854  1.00 70.64  ? 348 PHE A CD1 1 
ATOM 2158 C CD2 . PHE A 1 348 ? 131.772 110.920 94.566  1.00 69.01  ? 348 PHE A CD2 1 
ATOM 2159 C CE1 . PHE A 1 348 ? 132.414 111.184 97.231  1.00 70.29  ? 348 PHE A CE1 1 
ATOM 2160 C CE2 . PHE A 1 348 ? 132.886 111.645 94.938  1.00 70.05  ? 348 PHE A CE2 1 
ATOM 2161 C CZ  . PHE A 1 348 ? 133.210 111.774 96.272  1.00 70.70  ? 348 PHE A CZ  1 
ATOM 2162 N N   . ILE A 1 349 ? 127.660 107.082 95.101  1.00 61.44  ? 349 ILE A N   1 
ATOM 2163 C CA  . ILE A 1 349 ? 126.345 106.526 94.785  1.00 54.51  ? 349 ILE A CA  1 
ATOM 2164 C C   . ILE A 1 349 ? 125.613 106.052 96.038  1.00 53.19  ? 349 ILE A C   1 
ATOM 2165 O O   . ILE A 1 349 ? 124.408 106.289 96.187  1.00 59.01  ? 349 ILE A O   1 
ATOM 2166 C CB  . ILE A 1 349 ? 126.482 105.402 93.742  1.00 56.40  ? 349 ILE A CB  1 
ATOM 2167 C CG1 . ILE A 1 349 ? 126.946 105.980 92.404  1.00 55.91  ? 349 ILE A CG1 1 
ATOM 2168 C CG2 . ILE A 1 349 ? 125.165 104.671 93.564  1.00 54.55  ? 349 ILE A CG2 1 
ATOM 2169 C CD1 . ILE A 1 349 ? 127.273 104.939 91.362  1.00 55.27  ? 349 ILE A CD1 1 
ATOM 2170 N N   . LEU A 1 350 ? 126.300 105.352 96.941  1.00 52.40  ? 350 LEU A N   1 
ATOM 2171 C CA  . LEU A 1 350 ? 125.637 104.901 98.163  1.00 56.96  ? 350 LEU A CA  1 
ATOM 2172 C C   . LEU A 1 350 ? 125.218 106.067 99.057  1.00 58.05  ? 350 LEU A C   1 
ATOM 2173 O O   . LEU A 1 350 ? 124.130 106.044 99.646  1.00 60.97  ? 350 LEU A O   1 
ATOM 2174 C CB  . LEU A 1 350 ? 126.548 103.940 98.926  1.00 58.53  ? 350 LEU A CB  1 
ATOM 2175 C CG  . LEU A 1 350 ? 126.743 102.568 98.278  1.00 59.27  ? 350 LEU A CG  1 
ATOM 2176 C CD1 . LEU A 1 350 ? 127.853 101.798 98.972  1.00 58.25  ? 350 LEU A CD1 1 
ATOM 2177 C CD2 . LEU A 1 350 ? 125.445 101.776 98.290  1.00 57.83  ? 350 LEU A CD2 1 
ATOM 2178 N N   . MET A 1 351 ? 126.063 107.096 99.165  1.00 56.65  ? 351 MET A N   1 
ATOM 2179 C CA  . MET A 1 351 ? 125.674 108.339 99.826  1.00 53.15  ? 351 MET A CA  1 
ATOM 2180 C C   . MET A 1 351 ? 124.411 108.936 99.218  1.00 58.35  ? 351 MET A C   1 
ATOM 2181 O O   . MET A 1 351 ? 123.485 109.332 99.939  1.00 58.95  ? 351 MET A O   1 
ATOM 2182 C CB  . MET A 1 351 ? 126.815 109.352 99.729  1.00 52.49  ? 351 MET A CB  1 
ATOM 2183 C CG  . MET A 1 351 ? 128.010 109.095 100.620 1.00 52.56  ? 351 MET A CG  1 
ATOM 2184 S SD  . MET A 1 351 ? 129.324 110.270 100.234 1.00 58.52  ? 351 MET A SD  1 
ATOM 2185 C CE  . MET A 1 351 ? 130.439 110.020 101.607 1.00 60.37  ? 351 MET A CE  1 
ATOM 2186 N N   . TYR A 1 352 ? 124.344 108.980 97.886  1.00 46.60  ? 352 TYR A N   1 
ATOM 2187 C CA  . TYR A 1 352 ? 123.195 109.584 97.221  1.00 34.42  ? 352 TYR A CA  1 
ATOM 2188 C C   . TYR A 1 352 ? 121.918 108.778 97.426  1.00 37.80  ? 352 TYR A C   1 
ATOM 2189 O O   . TYR A 1 352 ? 120.849 109.354 97.646  1.00 39.35  ? 352 TYR A O   1 
ATOM 2190 C CB  . TYR A 1 352 ? 123.482 109.753 95.730  1.00 37.70  ? 352 TYR A CB  1 
ATOM 2191 C CG  . TYR A 1 352 ? 122.302 110.287 94.957  1.00 45.72  ? 352 TYR A CG  1 
ATOM 2192 C CD1 . TYR A 1 352 ? 121.807 111.559 95.204  1.00 45.23  ? 352 TYR A CD1 1 
ATOM 2193 C CD2 . TYR A 1 352 ? 121.677 109.519 93.985  1.00 39.10  ? 352 TYR A CD2 1 
ATOM 2194 C CE1 . TYR A 1 352 ? 120.717 112.044 94.518  1.00 43.91  ? 352 TYR A CE1 1 
ATOM 2195 C CE2 . TYR A 1 352 ? 120.594 110.003 93.285  1.00 40.51  ? 352 TYR A CE2 1 
ATOM 2196 C CZ  . TYR A 1 352 ? 120.116 111.263 93.557  1.00 43.67  ? 352 TYR A CZ  1 
ATOM 2197 O OH  . TYR A 1 352 ? 119.048 111.756 92.849  1.00 51.61  ? 352 TYR A OH  1 
ATOM 2198 N N   . LEU A 1 353 ? 122.006 107.451 97.361  1.00 34.05  ? 353 LEU A N   1 
ATOM 2199 C CA  . LEU A 1 353 ? 120.833 106.616 97.618  1.00 27.52  ? 353 LEU A CA  1 
ATOM 2200 C C   . LEU A 1 353 ? 120.363 106.670 99.072  1.00 30.23  ? 353 LEU A C   1 
ATOM 2201 O O   . LEU A 1 353 ? 119.155 106.730 99.326  1.00 36.47  ? 353 LEU A O   1 
ATOM 2202 C CB  . LEU A 1 353 ? 121.126 105.174 97.208  1.00 34.98  ? 353 LEU A CB  1 
ATOM 2203 C CG  . LEU A 1 353 ? 121.385 104.929 95.720  1.00 33.35  ? 353 LEU A CG  1 
ATOM 2204 C CD1 . LEU A 1 353 ? 121.654 103.459 95.461  1.00 32.23  ? 353 LEU A CD1 1 
ATOM 2205 C CD2 . LEU A 1 353 ? 120.216 105.414 94.883  1.00 31.54  ? 353 LEU A CD2 1 
ATOM 2206 N N   . TRP A 1 354 ? 121.284 106.650 100.040 1.00 44.29  ? 354 TRP A N   1 
ATOM 2207 C CA  . TRP A 1 354 ? 120.893 106.860 101.436 1.00 42.29  ? 354 TRP A CA  1 
ATOM 2208 C C   . TRP A 1 354 ? 120.213 108.210 101.661 1.00 48.44  ? 354 TRP A C   1 
ATOM 2209 O O   . TRP A 1 354 ? 119.143 108.278 102.286 1.00 56.44  ? 354 TRP A O   1 
ATOM 2210 C CB  . TRP A 1 354 ? 122.120 106.741 102.340 1.00 46.51  ? 354 TRP A CB  1 
ATOM 2211 C CG  . TRP A 1 354 ? 122.411 105.353 102.815 1.00 51.65  ? 354 TRP A CG  1 
ATOM 2212 C CD1 . TRP A 1 354 ? 123.470 104.570 102.461 1.00 50.09  ? 354 TRP A CD1 1 
ATOM 2213 C CD2 . TRP A 1 354 ? 121.645 104.589 103.754 1.00 55.67  ? 354 TRP A CD2 1 
ATOM 2214 N NE1 . TRP A 1 354 ? 123.405 103.362 103.110 1.00 45.27  ? 354 TRP A NE1 1 
ATOM 2215 C CE2 . TRP A 1 354 ? 122.294 103.349 103.911 1.00 53.55  ? 354 TRP A CE2 1 
ATOM 2216 C CE3 . TRP A 1 354 ? 120.470 104.832 104.472 1.00 53.21  ? 354 TRP A CE3 1 
ATOM 2217 C CZ2 . TRP A 1 354 ? 121.808 102.355 104.755 1.00 53.43  ? 354 TRP A CZ2 1 
ATOM 2218 C CZ3 . TRP A 1 354 ? 119.989 103.844 105.309 1.00 52.25  ? 354 TRP A CZ3 1 
ATOM 2219 C CH2 . TRP A 1 354 ? 120.657 102.621 105.444 1.00 54.37  ? 354 TRP A CH2 1 
ATOM 2220 N N   . PHE A 1 355 ? 120.763 109.274 101.072 1.00 39.79  ? 355 PHE A N   1 
ATOM 2221 C CA  . PHE A 1 355 ? 120.129 110.588 101.115 1.00 34.81  ? 355 PHE A CA  1 
ATOM 2222 C C   . PHE A 1 355 ? 118.725 110.558 100.521 1.00 42.12  ? 355 PHE A C   1 
ATOM 2223 O O   . PHE A 1 355 ? 117.756 110.991 101.160 1.00 37.20  ? 355 PHE A O   1 
ATOM 2224 C CB  . PHE A 1 355 ? 121.017 111.596 100.380 1.00 38.02  ? 355 PHE A CB  1 
ATOM 2225 C CG  . PHE A 1 355 ? 120.495 113.005 100.394 1.00 41.39  ? 355 PHE A CG  1 
ATOM 2226 C CD1 . PHE A 1 355 ? 120.702 113.823 101.489 1.00 43.63  ? 355 PHE A CD1 1 
ATOM 2227 C CD2 . PHE A 1 355 ? 119.819 113.517 99.302  1.00 37.20  ? 355 PHE A CD2 1 
ATOM 2228 C CE1 . PHE A 1 355 ? 120.230 115.119 101.501 1.00 39.57  ? 355 PHE A CE1 1 
ATOM 2229 C CE2 . PHE A 1 355 ? 119.344 114.810 99.308  1.00 40.37  ? 355 PHE A CE2 1 
ATOM 2230 C CZ  . PHE A 1 355 ? 119.549 115.612 100.409 1.00 42.43  ? 355 PHE A CZ  1 
ATOM 2231 N N   . THR A 1 356 ? 118.604 110.080 99.281  1.00 47.55  ? 356 THR A N   1 
ATOM 2232 C CA  . THR A 1 356 ? 117.323 110.083 98.584  1.00 35.90  ? 356 THR A CA  1 
ATOM 2233 C C   . THR A 1 356 ? 116.263 109.288 99.338  1.00 33.16  ? 356 THR A C   1 
ATOM 2234 O O   . THR A 1 356 ? 115.136 109.762 99.519  1.00 45.72  ? 356 THR A O   1 
ATOM 2235 C CB  . THR A 1 356 ? 117.500 109.528 97.172  1.00 33.02  ? 356 THR A CB  1 
ATOM 2236 O OG1 . THR A 1 356 ? 118.477 110.306 96.471  1.00 37.69  ? 356 THR A OG1 1 
ATOM 2237 C CG2 . THR A 1 356 ? 116.187 109.569 96.414  1.00 37.63  ? 356 THR A CG2 1 
ATOM 2238 N N   . ASP A 1 357 ? 116.587 108.060 99.752  1.00 24.84  ? 357 ASP A N   1 
ATOM 2239 C CA  . ASP A 1 357 ? 115.590 107.242 100.436 1.00 33.66  ? 357 ASP A CA  1 
ATOM 2240 C C   . ASP A 1 357 ? 115.188 107.823 101.789 1.00 38.16  ? 357 ASP A C   1 
ATOM 2241 O O   . ASP A 1 357 ? 114.006 107.777 102.151 1.00 42.27  ? 357 ASP A O   1 
ATOM 2242 C CB  . ASP A 1 357 ? 116.104 105.812 100.599 1.00 39.15  ? 357 ASP A CB  1 
ATOM 2243 C CG  . ASP A 1 357 ? 116.157 105.058 99.283  1.00 46.07  ? 357 ASP A CG  1 
ATOM 2244 O OD1 . ASP A 1 357 ? 115.353 105.375 98.384  1.00 44.90  ? 357 ASP A OD1 1 
ATOM 2245 O OD2 . ASP A 1 357 ? 116.998 104.145 99.149  1.00 47.31  ? 357 ASP A OD2 1 
ATOM 2246 N N   . SER A 1 358 ? 116.128 108.415 102.532 1.00 42.53  ? 358 SER A N   1 
ATOM 2247 C CA  . SER A 1 358 ? 115.753 109.105 103.766 1.00 36.01  ? 358 SER A CA  1 
ATOM 2248 C C   . SER A 1 358 ? 114.804 110.272 103.505 1.00 41.60  ? 358 SER A C   1 
ATOM 2249 O O   . SER A 1 358 ? 113.755 110.403 104.159 1.00 42.72  ? 358 SER A O   1 
ATOM 2250 C CB  . SER A 1 358 ? 117.009 109.590 104.487 1.00 36.52  ? 358 SER A CB  1 
ATOM 2251 O OG  . SER A 1 358 ? 116.679 110.263 105.687 1.00 46.37  ? 358 SER A OG  1 
ATOM 2252 N N   . VAL A 1 359 ? 115.158 111.129 102.543 1.00 44.02  ? 359 VAL A N   1 
ATOM 2253 C CA  . VAL A 1 359 ? 114.323 112.278 102.201 1.00 40.88  ? 359 VAL A CA  1 
ATOM 2254 C C   . VAL A 1 359 ? 112.931 111.848 101.758 1.00 40.02  ? 359 VAL A C   1 
ATOM 2255 O O   . VAL A 1 359 ? 111.930 112.417 102.202 1.00 42.52  ? 359 VAL A O   1 
ATOM 2256 C CB  . VAL A 1 359 ? 115.017 113.137 101.126 1.00 35.06  ? 359 VAL A CB  1 
ATOM 2257 C CG1 . VAL A 1 359 ? 114.080 114.218 100.621 1.00 34.80  ? 359 VAL A CG1 1 
ATOM 2258 C CG2 . VAL A 1 359 ? 116.277 113.763 101.685 1.00 40.58  ? 359 VAL A CG2 1 
ATOM 2259 N N   . LEU A 1 360 ? 112.833 110.795 100.945 1.00 35.01  ? 360 LEU A N   1 
ATOM 2260 C CA  . LEU A 1 360 ? 111.518 110.361 100.475 1.00 29.14  ? 360 LEU A CA  1 
ATOM 2261 C C   . LEU A 1 360 ? 110.694 109.738 101.593 1.00 33.02  ? 360 LEU A C   1 
ATOM 2262 O O   . LEU A 1 360 ? 109.496 110.030 101.722 1.00 38.26  ? 360 LEU A O   1 
ATOM 2263 C CB  . LEU A 1 360 ? 111.661 109.377 99.314  1.00 28.83  ? 360 LEU A CB  1 
ATOM 2264 C CG  . LEU A 1 360 ? 112.238 109.903 98.001  1.00 36.83  ? 360 LEU A CG  1 
ATOM 2265 C CD1 . LEU A 1 360 ? 112.064 108.870 96.903  1.00 36.46  ? 360 LEU A CD1 1 
ATOM 2266 C CD2 . LEU A 1 360 ? 111.582 111.212 97.614  1.00 34.89  ? 360 LEU A CD2 1 
ATOM 2267 N N   . TYR A 1 361 ? 111.311 108.889 102.417 1.00 38.45  ? 361 TYR A N   1 
ATOM 2268 C CA  . TYR A 1 361 ? 110.571 108.227 103.484 1.00 36.48  ? 361 TYR A CA  1 
ATOM 2269 C C   . TYR A 1 361 ? 109.997 109.240 104.466 1.00 43.48  ? 361 TYR A C   1 
ATOM 2270 O O   . TYR A 1 361 ? 108.819 109.163 104.829 1.00 50.10  ? 361 TYR A O   1 
ATOM 2271 C CB  . TYR A 1 361 ? 111.475 107.218 104.195 1.00 38.25  ? 361 TYR A CB  1 
ATOM 2272 C CG  . TYR A 1 361 ? 110.754 106.315 105.174 1.00 43.16  ? 361 TYR A CG  1 
ATOM 2273 C CD1 . TYR A 1 361 ? 110.533 106.712 106.486 1.00 41.55  ? 361 TYR A CD1 1 
ATOM 2274 C CD2 . TYR A 1 361 ? 110.282 105.070 104.780 1.00 42.42  ? 361 TYR A CD2 1 
ATOM 2275 C CE1 . TYR A 1 361 ? 109.873 105.891 107.379 1.00 41.63  ? 361 TYR A CE1 1 
ATOM 2276 C CE2 . TYR A 1 361 ? 109.621 104.243 105.666 1.00 48.01  ? 361 TYR A CE2 1 
ATOM 2277 C CZ  . TYR A 1 361 ? 109.418 104.659 106.963 1.00 46.04  ? 361 TYR A CZ  1 
ATOM 2278 O OH  . TYR A 1 361 ? 108.760 103.839 107.849 1.00 38.35  ? 361 TYR A OH  1 
ATOM 2279 N N   . GLN A 1 362 ? 110.813 110.197 104.919 1.00 41.34  ? 362 GLN A N   1 
ATOM 2280 C CA  . GLN A 1 362 ? 110.277 111.214 105.826 1.00 34.79  ? 362 GLN A CA  1 
ATOM 2281 C C   . GLN A 1 362 ? 109.303 112.166 105.127 1.00 42.18  ? 362 GLN A C   1 
ATOM 2282 O O   . GLN A 1 362 ? 108.282 112.557 105.713 1.00 42.19  ? 362 GLN A O   1 
ATOM 2283 C CB  . GLN A 1 362 ? 111.419 111.995 106.471 1.00 44.94  ? 362 GLN A CB  1 
ATOM 2284 C CG  . GLN A 1 362 ? 112.307 111.154 107.370 1.00 44.61  ? 362 GLN A CG  1 
ATOM 2285 C CD  . GLN A 1 362 ? 113.200 111.998 108.256 1.00 50.76  ? 362 GLN A CD  1 
ATOM 2286 O OE1 . GLN A 1 362 ? 112.857 113.128 108.603 1.00 49.60  ? 362 GLN A OE1 1 
ATOM 2287 N NE2 . GLN A 1 362 ? 114.352 111.453 108.627 1.00 44.98  ? 362 GLN A NE2 1 
ATOM 2288 N N   . GLY A 1 363 ? 109.607 112.561 103.887 1.00 42.65  ? 363 GLY A N   1 
ATOM 2289 C CA  . GLY A 1 363 ? 108.752 113.485 103.159 1.00 35.88  ? 363 GLY A CA  1 
ATOM 2290 C C   . GLY A 1 363 ? 107.345 112.984 102.901 1.00 39.12  ? 363 GLY A C   1 
ATOM 2291 O O   . GLY A 1 363 ? 106.381 113.739 103.036 1.00 40.91  ? 363 GLY A O   1 
ATOM 2292 N N   . LEU A 1 364 ? 107.197 111.706 102.545 1.00 40.12  ? 364 LEU A N   1 
ATOM 2293 C CA  . LEU A 1 364 ? 105.854 111.186 102.293 1.00 39.22  ? 364 LEU A CA  1 
ATOM 2294 C C   . LEU A 1 364 ? 105.023 111.088 103.567 1.00 36.13  ? 364 LEU A C   1 
ATOM 2295 O O   . LEU A 1 364 ? 103.821 111.379 103.549 1.00 42.49  ? 364 LEU A O   1 
ATOM 2296 C CB  . LEU A 1 364 ? 105.939 109.822 101.609 1.00 43.46  ? 364 LEU A CB  1 
ATOM 2297 C CG  . LEU A 1 364 ? 106.412 109.831 100.155 1.00 40.97  ? 364 LEU A CG  1 
ATOM 2298 C CD1 . LEU A 1 364 ? 106.504 108.416 99.611  1.00 38.25  ? 364 LEU A CD1 1 
ATOM 2299 C CD2 . LEU A 1 364 ? 105.486 110.679 99.301  1.00 38.45  ? 364 LEU A CD2 1 
ATOM 2300 N N   . ILE A 1 365 ? 105.647 110.754 104.695 1.00 36.65  ? 365 ILE A N   1 
ATOM 2301 C CA  . ILE A 1 365 ? 104.900 110.699 105.948 1.00 42.50  ? 365 ILE A CA  1 
ATOM 2302 C C   . ILE A 1 365 ? 104.496 112.099 106.399 1.00 48.24  ? 365 ILE A C   1 
ATOM 2303 O O   . ILE A 1 365 ? 103.359 112.319 106.836 1.00 49.00  ? 365 ILE A O   1 
ATOM 2304 C CB  . ILE A 1 365 ? 105.711 109.962 107.029 1.00 44.21  ? 365 ILE A CB  1 
ATOM 2305 C CG1 . ILE A 1 365 ? 105.922 108.502 106.629 1.00 40.71  ? 365 ILE A CG1 1 
ATOM 2306 C CG2 . ILE A 1 365 ? 105.006 110.036 108.371 1.00 40.29  ? 365 ILE A CG2 1 
ATOM 2307 C CD1 . ILE A 1 365 ? 106.818 107.738 107.571 1.00 38.60  ? 365 ILE A CD1 1 
ATOM 2308 N N   . LEU A 1 366 ? 105.410 113.068 106.295 1.00 38.90  ? 366 LEU A N   1 
ATOM 2309 C CA  . LEU A 1 366 ? 105.064 114.441 106.657 1.00 33.87  ? 366 LEU A CA  1 
ATOM 2310 C C   . LEU A 1 366 ? 103.991 115.029 105.742 1.00 43.82  ? 366 LEU A C   1 
ATOM 2311 O O   . LEU A 1 366 ? 103.079 115.718 106.212 1.00 39.71  ? 366 LEU A O   1 
ATOM 2312 C CB  . LEU A 1 366 ? 106.316 115.318 106.640 1.00 41.90  ? 366 LEU A CB  1 
ATOM 2313 C CG  . LEU A 1 366 ? 107.355 115.062 107.734 1.00 46.33  ? 366 LEU A CG  1 
ATOM 2314 C CD1 . LEU A 1 366 ? 108.606 115.890 107.488 1.00 43.65  ? 366 LEU A CD1 1 
ATOM 2315 C CD2 . LEU A 1 366 ? 106.778 115.356 109.109 1.00 43.08  ? 366 LEU A CD2 1 
ATOM 2316 N N   . HIS A 1 367 ? 104.071 114.756 104.436 1.00 52.45  ? 367 HIS A N   1 
ATOM 2317 C CA  . HIS A 1 367 ? 103.033 115.197 103.505 1.00 44.76  ? 367 HIS A CA  1 
ATOM 2318 C C   . HIS A 1 367 ? 101.676 114.564 103.804 1.00 44.46  ? 367 HIS A C   1 
ATOM 2319 O O   . HIS A 1 367 ? 100.646 115.254 103.786 1.00 47.98  ? 367 HIS A O   1 
ATOM 2320 C CB  . HIS A 1 367 ? 103.467 114.883 102.073 1.00 44.98  ? 367 HIS A CB  1 
ATOM 2321 C CG  . HIS A 1 367 ? 102.521 115.385 101.027 1.00 52.55  ? 367 HIS A CG  1 
ATOM 2322 N ND1 . HIS A 1 367 ? 102.424 116.717 100.688 1.00 49.83  ? 367 HIS A ND1 1 
ATOM 2323 C CD2 . HIS A 1 367 ? 101.634 114.731 100.239 1.00 50.30  ? 367 HIS A CD2 1 
ATOM 2324 C CE1 . HIS A 1 367 ? 101.516 116.863 99.740  1.00 48.02  ? 367 HIS A CE1 1 
ATOM 2325 N NE2 . HIS A 1 367 ? 101.022 115.673 99.450  1.00 50.77  ? 367 HIS A NE2 1 
ATOM 2326 N N   . MET A 1 368 ? 101.653 113.266 104.122 1.00 45.87  ? 368 MET A N   1 
ATOM 2327 C CA  . MET A 1 368 ? 100.385 112.635 104.475 1.00 46.11  ? 368 MET A CA  1 
ATOM 2328 C C   . MET A 1 368 ? 99.813  113.221 105.756 1.00 45.25  ? 368 MET A C   1 
ATOM 2329 O O   . MET A 1 368 ? 98.608  113.483 105.836 1.00 43.73  ? 368 MET A O   1 
ATOM 2330 C CB  . MET A 1 368 ? 100.566 111.124 104.614 1.00 50.75  ? 368 MET A CB  1 
ATOM 2331 C CG  . MET A 1 368 ? 99.313  110.395 105.072 1.00 50.67  ? 368 MET A CG  1 
ATOM 2332 S SD  . MET A 1 368 ? 99.581  108.634 105.335 1.00 58.51  ? 368 MET A SD  1 
ATOM 2333 C CE  . MET A 1 368 ? 100.628 108.668 106.786 1.00 44.60  ? 368 MET A CE  1 
ATOM 2334 N N   . GLY A 1 369 ? 100.652 113.433 106.769 1.00 50.47  ? 369 GLY A N   1 
ATOM 2335 C CA  . GLY A 1 369 ? 100.155 114.031 107.996 1.00 49.66  ? 369 GLY A CA  1 
ATOM 2336 C C   . GLY A 1 369 ? 99.617  115.433 107.777 1.00 51.95  ? 369 GLY A C   1 
ATOM 2337 O O   . GLY A 1 369 ? 98.583  115.807 108.334 1.00 54.97  ? 369 GLY A O   1 
ATOM 2338 N N   . ALA A 1 370 ? 100.317 116.228 106.964 1.00 56.62  ? 370 ALA A N   1 
ATOM 2339 C CA  . ALA A 1 370 ? 99.891  117.596 106.693 1.00 50.29  ? 370 ALA A CA  1 
ATOM 2340 C C   . ALA A 1 370 ? 98.612  117.669 105.865 1.00 56.47  ? 370 ALA A C   1 
ATOM 2341 O O   . ALA A 1 370 ? 97.865  118.647 105.982 1.00 56.98  ? 370 ALA A O   1 
ATOM 2342 C CB  . ALA A 1 370 ? 101.010 118.362 105.990 1.00 50.54  ? 370 ALA A CB  1 
ATOM 2343 N N   . THR A 1 371 ? 98.329  116.663 105.027 1.00 61.51  ? 371 THR A N   1 
ATOM 2344 C CA  . THR A 1 371 ? 97.271  116.815 104.033 1.00 53.66  ? 371 THR A CA  1 
ATOM 2345 C C   . THR A 1 371 ? 96.101  115.841 104.133 1.00 55.66  ? 371 THR A C   1 
ATOM 2346 O O   . THR A 1 371 ? 95.048  116.132 103.557 1.00 56.94  ? 371 THR A O   1 
ATOM 2347 C CB  . THR A 1 371 ? 97.850  116.708 102.612 1.00 52.53  ? 371 THR A CB  1 
ATOM 2348 O OG1 . THR A 1 371 ? 98.395  115.398 102.411 1.00 56.16  ? 371 THR A OG1 1 
ATOM 2349 C CG2 . THR A 1 371 ? 98.936  117.747 102.396 1.00 52.56  ? 371 THR A CG2 1 
ATOM 2350 N N   . SER A 1 372 ? 96.235  114.714 104.827 1.00 56.84  ? 372 SER A N   1 
ATOM 2351 C CA  . SER A 1 372 ? 95.133  113.758 104.866 1.00 54.73  ? 372 SER A CA  1 
ATOM 2352 C C   . SER A 1 372 ? 93.932  114.304 105.633 1.00 50.86  ? 372 SER A C   1 
ATOM 2353 O O   . SER A 1 372 ? 94.066  115.050 106.606 1.00 53.22  ? 372 SER A O   1 
ATOM 2354 C CB  . SER A 1 372 ? 95.588  112.442 105.494 1.00 54.48  ? 372 SER A CB  1 
ATOM 2355 O OG  . SER A 1 372 ? 96.189  112.662 106.756 1.00 63.01  ? 372 SER A OG  1 
ATOM 2356 N N   . GLY A 1 373 ? 92.742  113.921 105.168 1.00 50.32  ? 373 GLY A N   1 
ATOM 2357 C CA  . GLY A 1 373 ? 91.479  114.243 105.807 1.00 50.24  ? 373 GLY A CA  1 
ATOM 2358 C C   . GLY A 1 373 ? 90.976  113.247 106.835 1.00 54.24  ? 373 GLY A C   1 
ATOM 2359 O O   . GLY A 1 373 ? 90.099  113.574 107.640 1.00 53.69  ? 373 GLY A O   1 
ATOM 2360 N N   . ASN A 1 374 ? 91.520  112.019 106.820 1.00 53.47  ? 374 ASN A N   1 
ATOM 2361 C CA  . ASN A 1 374 ? 91.287  111.021 107.872 1.00 45.26  ? 374 ASN A CA  1 
ATOM 2362 C C   . ASN A 1 374 ? 92.642  110.380 108.174 1.00 42.39  ? 374 ASN A C   1 
ATOM 2363 O O   . ASN A 1 374 ? 92.984  109.311 107.666 1.00 51.46  ? 374 ASN A O   1 
ATOM 2364 C CB  . ASN A 1 374 ? 90.245  109.986 107.447 1.00 42.46  ? 374 ASN A CB  1 
ATOM 2365 C CG  . ASN A 1 374 ? 89.815  109.081 108.589 1.00 51.99  ? 374 ASN A CG  1 
ATOM 2366 O OD1 . ASN A 1 374 ? 90.473  109.008 109.626 1.00 47.63  ? 374 ASN A OD1 1 
ATOM 2367 N ND2 . ASN A 1 374 ? 88.701  108.384 108.400 1.00 52.40  ? 374 ASN A ND2 1 
ATOM 2368 N N   . LEU A 1 375 ? 93.417  111.066 109.013 1.00 32.17  ? 375 LEU A N   1 
ATOM 2369 C CA  . LEU A 1 375 ? 94.791  110.665 109.291 1.00 29.88  ? 375 LEU A CA  1 
ATOM 2370 C C   . LEU A 1 375 ? 94.885  109.312 109.990 1.00 36.33  ? 375 LEU A C   1 
ATOM 2371 O O   . LEU A 1 375 ? 95.851  108.576 109.769 1.00 40.83  ? 375 LEU A O   1 
ATOM 2372 C CB  . LEU A 1 375 ? 95.471  111.749 110.126 1.00 32.86  ? 375 LEU A CB  1 
ATOM 2373 C CG  . LEU A 1 375 ? 96.932  111.571 110.526 1.00 40.62  ? 375 LEU A CG  1 
ATOM 2374 C CD1 . LEU A 1 375 ? 97.809  111.409 109.299 1.00 41.29  ? 375 LEU A CD1 1 
ATOM 2375 C CD2 . LEU A 1 375 ? 97.374  112.765 111.346 1.00 39.84  ? 375 LEU A CD2 1 
ATOM 2376 N N   . TYR A 1 376 ? 93.905  108.961 110.825 1.00 38.95  ? 376 TYR A N   1 
ATOM 2377 C CA  . TYR A 1 376 ? 93.996  107.718 111.591 1.00 33.93  ? 376 TYR A CA  1 
ATOM 2378 C C   . TYR A 1 376 ? 93.952  106.480 110.698 1.00 41.73  ? 376 TYR A C   1 
ATOM 2379 O O   . TYR A 1 376 ? 94.865  105.644 110.732 1.00 49.99  ? 376 TYR A O   1 
ATOM 2380 C CB  . TYR A 1 376 ? 92.876  107.658 112.629 1.00 27.88  ? 376 TYR A CB  1 
ATOM 2381 C CG  . TYR A 1 376 ? 93.031  108.645 113.761 1.00 35.79  ? 376 TYR A CG  1 
ATOM 2382 C CD1 . TYR A 1 376 ? 94.158  108.632 114.570 1.00 36.31  ? 376 TYR A CD1 1 
ATOM 2383 C CD2 . TYR A 1 376 ? 92.043  109.580 114.031 1.00 46.46  ? 376 TYR A CD2 1 
ATOM 2384 C CE1 . TYR A 1 376 ? 94.303  109.531 115.606 1.00 36.23  ? 376 TYR A CE1 1 
ATOM 2385 C CE2 . TYR A 1 376 ? 92.179  110.482 115.066 1.00 41.21  ? 376 TYR A CE2 1 
ATOM 2386 C CZ  . TYR A 1 376 ? 93.310  110.453 115.850 1.00 36.61  ? 376 TYR A CZ  1 
ATOM 2387 O OH  . TYR A 1 376 ? 93.447  111.350 116.883 1.00 41.90  ? 376 TYR A OH  1 
ATOM 2388 N N   . LEU A 1 377 ? 92.916  106.357 109.865 1.00 30.88  ? 377 LEU A N   1 
ATOM 2389 C CA  . LEU A 1 377 ? 92.826  105.198 108.982 1.00 29.44  ? 377 LEU A CA  1 
ATOM 2390 C C   . LEU A 1 377 ? 93.842  105.242 107.848 1.00 33.70  ? 377 LEU A C   1 
ATOM 2391 O O   . LEU A 1 377 ? 94.329  104.188 107.423 1.00 45.06  ? 377 LEU A O   1 
ATOM 2392 C CB  . LEU A 1 377 ? 91.409  105.079 108.422 1.00 34.02  ? 377 LEU A CB  1 
ATOM 2393 C CG  . LEU A 1 377 ? 90.365  104.505 109.381 1.00 34.56  ? 377 LEU A CG  1 
ATOM 2394 C CD1 . LEU A 1 377 ? 88.966  104.659 108.820 1.00 36.57  ? 377 LEU A CD1 1 
ATOM 2395 C CD2 . LEU A 1 377 ? 90.661  103.047 109.674 1.00 33.06  ? 377 LEU A CD2 1 
ATOM 2396 N N   . ASP A 1 378 ? 94.191  106.431 107.356 1.00 32.62  ? 378 ASP A N   1 
ATOM 2397 C CA  . ASP A 1 378 ? 95.236  106.516 106.340 1.00 33.86  ? 378 ASP A CA  1 
ATOM 2398 C C   . ASP A 1 378 ? 96.590  106.091 106.894 1.00 37.42  ? 378 ASP A C   1 
ATOM 2399 O O   . ASP A 1 378 ? 97.338  105.363 106.228 1.00 36.38  ? 378 ASP A O   1 
ATOM 2400 C CB  . ASP A 1 378 ? 95.309  107.935 105.780 1.00 37.87  ? 378 ASP A CB  1 
ATOM 2401 C CG  . ASP A 1 378 ? 94.113  108.283 104.919 1.00 49.74  ? 378 ASP A CG  1 
ATOM 2402 O OD1 . ASP A 1 378 ? 93.212  107.432 104.779 1.00 47.45  ? 378 ASP A OD1 1 
ATOM 2403 O OD2 . ASP A 1 378 ? 94.076  109.406 104.377 1.00 54.75  ? 378 ASP A OD2 1 
ATOM 2404 N N   . PHE A 1 379 ? 96.866  106.428 108.155 1.00 34.38  ? 379 PHE A N   1 
ATOM 2405 C CA  . PHE A 1 379 ? 98.113  106.017 108.790 1.00 25.92  ? 379 PHE A CA  1 
ATOM 2406 C C   . PHE A 1 379 ? 98.098  104.527 109.097 1.00 28.57  ? 379 PHE A C   1 
ATOM 2407 O O   . PHE A 1 379 ? 99.130  103.854 108.963 1.00 37.22  ? 379 PHE A O   1 
ATOM 2408 C CB  . PHE A 1 379 ? 98.322  106.859 110.055 1.00 24.48  ? 379 PHE A CB  1 
ATOM 2409 C CG  . PHE A 1 379 ? 99.700  106.762 110.651 1.00 35.95  ? 379 PHE A CG  1 
ATOM 2410 C CD1 . PHE A 1 379 ? 100.087 105.660 111.391 1.00 43.30  ? 379 PHE A CD1 1 
ATOM 2411 C CD2 . PHE A 1 379 ? 100.607 107.793 110.476 1.00 35.52  ? 379 PHE A CD2 1 
ATOM 2412 C CE1 . PHE A 1 379 ? 101.354 105.585 111.939 1.00 37.01  ? 379 PHE A CE1 1 
ATOM 2413 C CE2 . PHE A 1 379 ? 101.875 107.722 111.019 1.00 38.72  ? 379 PHE A CE2 1 
ATOM 2414 C CZ  . PHE A 1 379 ? 102.248 106.618 111.752 1.00 39.30  ? 379 PHE A CZ  1 
ATOM 2415 N N   . LEU A 1 380 ? 96.929  103.983 109.441 1.00 23.22  ? 380 LEU A N   1 
ATOM 2416 C CA  . LEU A 1 380 ? 96.837  102.556 109.724 1.00 20.14  ? 380 LEU A CA  1 
ATOM 2417 C C   . LEU A 1 380 ? 97.064  101.747 108.453 1.00 31.85  ? 380 LEU A C   1 
ATOM 2418 O O   . LEU A 1 380 ? 97.885  100.823 108.434 1.00 39.00  ? 380 LEU A O   1 
ATOM 2419 C CB  . LEU A 1 380 ? 95.479  102.229 110.342 1.00 31.45  ? 380 LEU A CB  1 
ATOM 2420 C CG  . LEU A 1 380 ? 95.233  100.778 110.757 1.00 27.49  ? 380 LEU A CG  1 
ATOM 2421 C CD1 . LEU A 1 380 ? 96.109  100.407 111.937 1.00 25.60  ? 380 LEU A CD1 1 
ATOM 2422 C CD2 . LEU A 1 380 ? 93.768  100.557 111.084 1.00 20.95  ? 380 LEU A CD2 1 
ATOM 2423 N N   . TYR A 1 381 ? 96.334  102.071 107.381 1.00 37.17  ? 381 TYR A N   1 
ATOM 2424 C CA  . TYR A 1 381 ? 96.496  101.337 106.129 1.00 23.90  ? 381 TYR A CA  1 
ATOM 2425 C C   . TYR A 1 381 ? 97.901  101.508 105.566 1.00 35.66  ? 381 TYR A C   1 
ATOM 2426 O O   . TYR A 1 381 ? 98.455  100.576 104.973 1.00 43.76  ? 381 TYR A O   1 
ATOM 2427 C CB  . TYR A 1 381 ? 95.457  101.783 105.102 1.00 26.50  ? 381 TYR A CB  1 
ATOM 2428 C CG  . TYR A 1 381 ? 94.024  101.518 105.495 1.00 35.25  ? 381 TYR A CG  1 
ATOM 2429 C CD1 . TYR A 1 381 ? 93.700  100.488 106.367 1.00 34.58  ? 381 TYR A CD1 1 
ATOM 2430 C CD2 . TYR A 1 381 ? 92.991  102.287 104.979 1.00 37.08  ? 381 TYR A CD2 1 
ATOM 2431 C CE1 . TYR A 1 381 ? 92.390  100.240 106.720 1.00 34.45  ? 381 TYR A CE1 1 
ATOM 2432 C CE2 . TYR A 1 381 ? 91.678  102.048 105.328 1.00 34.49  ? 381 TYR A CE2 1 
ATOM 2433 C CZ  . TYR A 1 381 ? 91.383  101.023 106.198 1.00 38.54  ? 381 TYR A CZ  1 
ATOM 2434 O OH  . TYR A 1 381 ? 90.074  100.783 106.547 1.00 40.92  ? 381 TYR A OH  1 
ATOM 2435 N N   . SER A 1 382 ? 98.490  102.697 105.726 1.00 39.23  ? 382 SER A N   1 
ATOM 2436 C CA  . SER A 1 382 ? 99.848  102.925 105.246 1.00 28.87  ? 382 SER A CA  1 
ATOM 2437 C C   . SER A 1 382 ? 100.871 102.095 106.014 1.00 36.90  ? 382 SER A C   1 
ATOM 2438 O O   . SER A 1 382 ? 101.853 101.621 105.432 1.00 36.64  ? 382 SER A O   1 
ATOM 2439 C CB  . SER A 1 382 ? 100.185 104.412 105.336 1.00 33.10  ? 382 SER A CB  1 
ATOM 2440 O OG  . SER A 1 382 ? 101.502 104.667 104.884 1.00 48.41  ? 382 SER A OG  1 
ATOM 2441 N N   . ALA A 1 383 ? 100.664 101.908 107.321 1.00 39.74  ? 383 ALA A N   1 
ATOM 2442 C CA  . ALA A 1 383 ? 101.606 101.121 108.115 1.00 31.35  ? 383 ALA A CA  1 
ATOM 2443 C C   . ALA A 1 383 ? 101.551 99.629  107.785 1.00 34.67  ? 383 ALA A C   1 
ATOM 2444 O O   . ALA A 1 383 ? 102.594 98.988  107.614 1.00 41.47  ? 383 ALA A O   1 
ATOM 2445 C CB  . ALA A 1 383 ? 101.344 101.347 109.604 1.00 24.46  ? 383 ALA A CB  1 
ATOM 2446 N N   . LEU A 1 384 ? 100.347 99.055  107.700 1.00 27.45  ? 384 LEU A N   1 
ATOM 2447 C CA  . LEU A 1 384 ? 100.212 97.617  107.459 1.00 20.93  ? 384 LEU A CA  1 
ATOM 2448 C C   . LEU A 1 384 ? 100.872 97.156  106.164 1.00 29.57  ? 384 LEU A C   1 
ATOM 2449 O O   . LEU A 1 384 ? 101.337 96.014  106.083 1.00 43.70  ? 384 LEU A O   1 
ATOM 2450 C CB  . LEU A 1 384 ? 98.735  97.226  107.441 1.00 26.79  ? 384 LEU A CB  1 
ATOM 2451 C CG  . LEU A 1 384 ? 97.961  97.280  108.756 1.00 34.22  ? 384 LEU A CG  1 
ATOM 2452 C CD1 . LEU A 1 384 ? 96.466  97.236  108.490 1.00 29.42  ? 384 LEU A CD1 1 
ATOM 2453 C CD2 . LEU A 1 384 ? 98.379  96.135  109.660 1.00 34.19  ? 384 LEU A CD2 1 
ATOM 2454 N N   . VAL A 1 385 ? 100.916 98.012  105.142 1.00 36.71  ? 385 VAL A N   1 
ATOM 2455 C CA  . VAL A 1 385 ? 101.529 97.658  103.864 1.00 36.02  ? 385 VAL A CA  1 
ATOM 2456 C C   . VAL A 1 385 ? 103.025 97.349  103.964 1.00 41.03  ? 385 VAL A C   1 
ATOM 2457 O O   . VAL A 1 385 ? 103.569 96.648  103.104 1.00 41.41  ? 385 VAL A O   1 
ATOM 2458 C CB  . VAL A 1 385 ? 101.236 98.803  102.864 1.00 32.43  ? 385 VAL A CB  1 
ATOM 2459 C CG1 . VAL A 1 385 ? 102.121 98.735  101.633 1.00 37.80  ? 385 VAL A CG1 1 
ATOM 2460 C CG2 . VAL A 1 385 ? 99.773  98.781  102.463 1.00 35.85  ? 385 VAL A CG2 1 
ATOM 2461 N N   . GLU A 1 386 ? 103.696 97.790  105.030 1.00 39.48  ? 386 GLU A N   1 
ATOM 2462 C CA  . GLU A 1 386 ? 105.094 97.423  105.254 1.00 32.62  ? 386 GLU A CA  1 
ATOM 2463 C C   . GLU A 1 386 ? 105.328 95.940  105.538 1.00 35.27  ? 386 GLU A C   1 
ATOM 2464 O O   . GLU A 1 386 ? 106.485 95.511  105.521 1.00 40.55  ? 386 GLU A O   1 
ATOM 2465 C CB  . GLU A 1 386 ? 105.671 98.252  106.402 1.00 33.82  ? 386 GLU A CB  1 
ATOM 2466 C CG  . GLU A 1 386 ? 105.659 99.750  106.151 1.00 39.68  ? 386 GLU A CG  1 
ATOM 2467 C CD  . GLU A 1 386 ? 106.353 100.530 107.250 1.00 49.84  ? 386 GLU A CD  1 
ATOM 2468 O OE1 . GLU A 1 386 ? 106.736 99.916  108.268 1.00 48.77  ? 386 GLU A OE1 1 
ATOM 2469 O OE2 . GLU A 1 386 ? 106.517 101.758 107.097 1.00 49.99  ? 386 GLU A OE2 1 
ATOM 2470 N N   . ILE A 1 387 ? 104.294 95.153  105.814 1.00 30.82  ? 387 ILE A N   1 
ATOM 2471 C CA  . ILE A 1 387 ? 104.469 93.721  106.064 1.00 30.79  ? 387 ILE A CA  1 
ATOM 2472 C C   . ILE A 1 387 ? 104.655 92.951  104.754 1.00 44.28  ? 387 ILE A C   1 
ATOM 2473 O O   . ILE A 1 387 ? 105.658 92.220  104.607 1.00 46.91  ? 387 ILE A O   1 
ATOM 2474 C CB  . ILE A 1 387 ? 103.308 93.162  106.905 1.00 32.43  ? 387 ILE A CB  1 
ATOM 2475 C CG1 . ILE A 1 387 ? 103.295 93.814  108.289 1.00 37.06  ? 387 ILE A CG1 1 
ATOM 2476 C CG2 . ILE A 1 387 ? 103.411 91.657  107.023 1.00 43.39  ? 387 ILE A CG2 1 
ATOM 2477 C CD1 . ILE A 1 387 ? 102.092 93.449  109.118 1.00 47.27  ? 387 ILE A CD1 1 
ATOM 2478 N N   . PRO A 1 388 ? 103.746 93.070  103.772 1.00 45.74  ? 388 PRO A N   1 
ATOM 2479 C CA  . PRO A 1 388 ? 104.050 92.486  102.459 1.00 30.36  ? 388 PRO A CA  1 
ATOM 2480 C C   . PRO A 1 388 ? 105.326 93.026  101.855 1.00 34.23  ? 388 PRO A C   1 
ATOM 2481 O O   . PRO A 1 388 ? 106.012 92.283  101.152 1.00 47.07  ? 388 PRO A O   1 
ATOM 2482 C CB  . PRO A 1 388 ? 102.829 92.871  101.618 1.00 37.51  ? 388 PRO A CB  1 
ATOM 2483 C CG  . PRO A 1 388 ? 101.737 92.958  102.592 1.00 42.39  ? 388 PRO A CG  1 
ATOM 2484 C CD  . PRO A 1 388 ? 102.369 93.603  103.792 1.00 40.48  ? 388 PRO A CD  1 
ATOM 2485 N N   . GLY A 1 389 ? 105.659 94.296  102.086 1.00 35.97  ? 389 GLY A N   1 
ATOM 2486 C CA  . GLY A 1 389 ? 106.913 94.818  101.568 1.00 36.73  ? 389 GLY A CA  1 
ATOM 2487 C C   . GLY A 1 389 ? 108.110 94.044  102.086 1.00 45.07  ? 389 GLY A C   1 
ATOM 2488 O O   . GLY A 1 389 ? 109.020 93.697  101.326 1.00 50.71  ? 389 GLY A O   1 
ATOM 2489 N N   . ALA A 1 390 ? 108.088 93.705  103.376 1.00 42.81  ? 390 ALA A N   1 
ATOM 2490 C CA  . ALA A 1 390 ? 109.170 92.931  103.971 1.00 39.79  ? 390 ALA A CA  1 
ATOM 2491 C C   . ALA A 1 390 ? 109.225 91.521  103.400 1.00 42.80  ? 390 ALA A C   1 
ATOM 2492 O O   . ALA A 1 390 ? 110.306 91.029  103.051 1.00 48.50  ? 390 ALA A O   1 
ATOM 2493 C CB  . ALA A 1 390 ? 109.011 92.890  105.491 1.00 41.04  ? 390 ALA A CB  1 
ATOM 2494 N N   . PHE A 1 391 ? 108.080 90.834  103.325 1.00 46.52  ? 391 PHE A N   1 
ATOM 2495 C CA  . PHE A 1 391 ? 108.121 89.472  102.790 1.00 41.30  ? 391 PHE A CA  1 
ATOM 2496 C C   . PHE A 1 391 ? 108.533 89.449  101.318 1.00 46.75  ? 391 PHE A C   1 
ATOM 2497 O O   . PHE A 1 391 ? 109.285 88.560  100.891 1.00 54.20  ? 391 PHE A O   1 
ATOM 2498 C CB  . PHE A 1 391 ? 106.776 88.775  102.987 1.00 47.04  ? 391 PHE A CB  1 
ATOM 2499 C CG  . PHE A 1 391 ? 106.474 88.437  104.418 1.00 55.76  ? 391 PHE A CG  1 
ATOM 2500 C CD1 . PHE A 1 391 ? 107.227 87.483  105.085 1.00 54.00  ? 391 PHE A CD1 1 
ATOM 2501 C CD2 . PHE A 1 391 ? 105.437 89.054  105.094 1.00 52.11  ? 391 PHE A CD2 1 
ATOM 2502 C CE1 . PHE A 1 391 ? 106.957 87.160  106.399 1.00 52.62  ? 391 PHE A CE1 1 
ATOM 2503 C CE2 . PHE A 1 391 ? 105.162 88.731  106.410 1.00 52.19  ? 391 PHE A CE2 1 
ATOM 2504 C CZ  . PHE A 1 391 ? 105.923 87.785  107.062 1.00 52.54  ? 391 PHE A CZ  1 
ATOM 2505 N N   . ILE A 1 392 ? 108.082 90.432  100.533 1.00 49.45  ? 392 ILE A N   1 
ATOM 2506 C CA  . ILE A 1 392 ? 108.480 90.513  99.130  1.00 50.16  ? 392 ILE A CA  1 
ATOM 2507 C C   . ILE A 1 392 ? 109.976 90.759  99.012  1.00 51.01  ? 392 ILE A C   1 
ATOM 2508 O O   . ILE A 1 392 ? 110.645 90.169  98.159  1.00 53.18  ? 392 ILE A O   1 
ATOM 2509 C CB  . ILE A 1 392 ? 107.664 91.591  98.391  1.00 47.61  ? 392 ILE A CB  1 
ATOM 2510 C CG1 . ILE A 1 392 ? 106.193 91.189  98.304  1.00 51.01  ? 392 ILE A CG1 1 
ATOM 2511 C CG2 . ILE A 1 392 ? 108.219 91.824  96.997  1.00 50.31  ? 392 ILE A CG2 1 
ATOM 2512 C CD1 . ILE A 1 392 ? 105.271 92.336  97.956  1.00 46.67  ? 392 ILE A CD1 1 
ATOM 2513 N N   . ALA A 1 393 ? 110.531 91.615  99.873  1.00 50.79  ? 393 ALA A N   1 
ATOM 2514 C CA  . ALA A 1 393 ? 111.969 91.858  99.820  1.00 49.48  ? 393 ALA A CA  1 
ATOM 2515 C C   . ALA A 1 393 ? 112.736 90.588  100.166 1.00 52.21  ? 393 ALA A C   1 
ATOM 2516 O O   . ALA A 1 393 ? 113.695 90.217  99.475  1.00 59.69  ? 393 ALA A O   1 
ATOM 2517 C CB  . ALA A 1 393 ? 112.346 92.998  100.766 1.00 48.29  ? 393 ALA A CB  1 
ATOM 2518 N N   . LEU A 1 394 ? 112.332 89.918  101.248 1.00 58.17  ? 394 LEU A N   1 
ATOM 2519 C CA  . LEU A 1 394 ? 112.985 88.679  101.659 1.00 59.07  ? 394 LEU A CA  1 
ATOM 2520 C C   . LEU A 1 394 ? 112.993 87.648  100.535 1.00 60.66  ? 394 LEU A C   1 
ATOM 2521 O O   . LEU A 1 394 ? 114.016 87.003  100.280 1.00 59.82  ? 394 LEU A O   1 
ATOM 2522 C CB  . LEU A 1 394 ? 112.301 88.112  102.903 1.00 57.80  ? 394 LEU A CB  1 
ATOM 2523 C CG  . LEU A 1 394 ? 112.777 86.735  103.375 1.00 58.47  ? 394 LEU A CG  1 
ATOM 2524 C CD1 . LEU A 1 394 ? 114.227 86.763  103.823 1.00 61.07  ? 394 LEU A CD1 1 
ATOM 2525 C CD2 . LEU A 1 394 ? 111.884 86.225  104.493 1.00 61.43  ? 394 LEU A CD2 1 
ATOM 2526 N N   . ILE A 1 395 ? 111.858 87.466  99.855  1.00 57.93  ? 395 ILE A N   1 
ATOM 2527 C CA  . ILE A 1 395 ? 111.815 86.463  98.793  1.00 57.16  ? 395 ILE A CA  1 
ATOM 2528 C C   . ILE A 1 395 ? 112.613 86.922  97.575  1.00 59.39  ? 395 ILE A C   1 
ATOM 2529 O O   . ILE A 1 395 ? 113.320 86.127  96.945  1.00 61.06  ? 395 ILE A O   1 
ATOM 2530 C CB  . ILE A 1 395 ? 110.359 86.132  98.425  1.00 63.68  ? 395 ILE A CB  1 
ATOM 2531 C CG1 . ILE A 1 395 ? 109.622 85.551  99.632  1.00 63.10  ? 395 ILE A CG1 1 
ATOM 2532 C CG2 . ILE A 1 395 ? 110.312 85.150  97.266  1.00 61.05  ? 395 ILE A CG2 1 
ATOM 2533 C CD1 . ILE A 1 395 ? 108.118 85.656  99.535  1.00 61.15  ? 395 ILE A CD1 1 
ATOM 2534 N N   . THR A 1 396 ? 112.515 88.208  97.225  1.00 63.04  ? 396 THR A N   1 
ATOM 2535 C CA  . THR A 1 396 ? 113.186 88.728  96.037  1.00 62.54  ? 396 THR A CA  1 
ATOM 2536 C C   . THR A 1 396 ? 114.700 88.620  96.156  1.00 61.76  ? 396 THR A C   1 
ATOM 2537 O O   . THR A 1 396 ? 115.391 88.325  95.173  1.00 66.81  ? 396 THR A O   1 
ATOM 2538 C CB  . THR A 1 396 ? 112.770 90.179  95.796  1.00 60.30  ? 396 THR A CB  1 
ATOM 2539 O OG1 . THR A 1 396 ? 111.345 90.254  95.665  1.00 61.75  ? 396 THR A OG1 1 
ATOM 2540 C CG2 . THR A 1 396 ? 113.408 90.713  94.528  1.00 63.86  ? 396 THR A CG2 1 
ATOM 2541 N N   . ILE A 1 397 ? 115.232 88.861  97.356  1.00 67.04  ? 397 ILE A N   1 
ATOM 2542 C CA  . ILE A 1 397 ? 116.663 88.693  97.608  1.00 65.19  ? 397 ILE A CA  1 
ATOM 2543 C C   . ILE A 1 397 ? 117.134 87.296  97.220  1.00 70.39  ? 397 ILE A C   1 
ATOM 2544 O O   . ILE A 1 397 ? 118.215 87.128  96.643  1.00 70.42  ? 397 ILE A O   1 
ATOM 2545 C CB  . ILE A 1 397 ? 116.969 88.999  99.087  1.00 68.55  ? 397 ILE A CB  1 
ATOM 2546 C CG1 . ILE A 1 397 ? 116.911 90.505  99.344  1.00 69.94  ? 397 ILE A CG1 1 
ATOM 2547 C CG2 . ILE A 1 397 ? 118.319 88.431  99.493  1.00 73.75  ? 397 ILE A CG2 1 
ATOM 2548 C CD1 . ILE A 1 397 ? 116.755 90.864  100.805 1.00 70.85  ? 397 ILE A CD1 1 
ATOM 2549 N N   . ASP A 1 398 ? 116.327 86.275  97.508  1.00 76.02  ? 398 ASP A N   1 
ATOM 2550 C CA  . ASP A 1 398 ? 116.732 84.907  97.202  1.00 74.99  ? 398 ASP A CA  1 
ATOM 2551 C C   . ASP A 1 398 ? 116.583 84.569  95.721  1.00 75.67  ? 398 ASP A C   1 
ATOM 2552 O O   . ASP A 1 398 ? 117.450 83.899  95.149  1.00 75.93  ? 398 ASP A O   1 
ATOM 2553 C CB  . ASP A 1 398 ? 115.922 83.925  98.048  1.00 75.36  ? 398 ASP A CB  1 
ATOM 2554 C CG  . ASP A 1 398 ? 116.221 84.049  99.527  1.00 80.39  ? 398 ASP A CG  1 
ATOM 2555 O OD1 . ASP A 1 398 ? 117.231 84.694  99.878  1.00 80.11  ? 398 ASP A OD1 1 
ATOM 2556 O OD2 . ASP A 1 398 ? 115.446 83.504  100.341 1.00 80.99  ? 398 ASP A OD2 1 
ATOM 2557 N N   . ARG A 1 399 ? 115.502 85.015  95.083  1.00 73.93  ? 399 ARG A N   1 
ATOM 2558 C CA  . ARG A 1 399 ? 115.199 84.573  93.727  1.00 72.58  ? 399 ARG A CA  1 
ATOM 2559 C C   . ARG A 1 399 ? 115.884 85.395  92.642  1.00 74.60  ? 399 ARG A C   1 
ATOM 2560 O O   . ARG A 1 399 ? 116.216 84.846  91.586  1.00 72.71  ? 399 ARG A O   1 
ATOM 2561 C CB  . ARG A 1 399 ? 113.686 84.599  93.491  1.00 74.81  ? 399 ARG A CB  1 
ATOM 2562 C CG  . ARG A 1 399 ? 112.896 83.685  94.412  1.00 76.16  ? 399 ARG A CG  1 
ATOM 2563 C CD  . ARG A 1 399 ? 113.192 82.221  94.135  1.00 72.97  ? 399 ARG A CD  1 
ATOM 2564 N NE  . ARG A 1 399 ? 112.620 81.353  95.156  1.00 75.56  ? 399 ARG A NE  1 
ATOM 2565 C CZ  . ARG A 1 399 ? 113.317 80.764  96.118  1.00 77.55  ? 399 ARG A CZ  1 
ATOM 2566 N NH1 . ARG A 1 399 ? 114.636 80.848  96.167  1.00 75.93  ? 399 ARG A NH1 1 
ATOM 2567 N NH2 . ARG A 1 399 ? 112.676 80.049  97.039  1.00 77.63  ? 399 ARG A NH2 1 
ATOM 2568 N N   . VAL A 1 400 ? 116.111 86.689  92.867  1.00 76.23  ? 400 VAL A N   1 
ATOM 2569 C CA  . VAL A 1 400 ? 116.415 87.601  91.769  1.00 69.67  ? 400 VAL A CA  1 
ATOM 2570 C C   . VAL A 1 400 ? 117.818 88.172  91.921  1.00 72.50  ? 400 VAL A C   1 
ATOM 2571 O O   . VAL A 1 400 ? 118.734 87.797  91.180  1.00 75.49  ? 400 VAL A O   1 
ATOM 2572 C CB  . VAL A 1 400 ? 115.374 88.732  91.685  1.00 66.67  ? 400 VAL A CB  1 
ATOM 2573 C CG1 . VAL A 1 400 ? 115.572 89.538  90.414  1.00 70.08  ? 400 VAL A CG1 1 
ATOM 2574 C CG2 . VAL A 1 400 ? 113.966 88.168  91.748  1.00 68.16  ? 400 VAL A CG2 1 
ATOM 2575 N N   . GLY A 1 401 ? 118.003 89.069  92.878  1.00 73.13  ? 401 GLY A N   1 
ATOM 2576 C CA  . GLY A 1 401 ? 119.181 89.925  92.879  1.00 70.10  ? 401 GLY A CA  1 
ATOM 2577 C C   . GLY A 1 401 ? 118.932 91.191  93.684  1.00 71.76  ? 401 GLY A C   1 
ATOM 2578 O O   . GLY A 1 401 ? 118.103 91.208  94.593  1.00 78.24  ? 401 GLY A O   1 
ATOM 2579 N N   . ARG A 1 402 ? 119.671 92.247  93.327  1.00 67.72  ? 402 ARG A N   1 
ATOM 2580 C CA  . ARG A 1 402 ? 119.589 93.507  94.064  1.00 67.82  ? 402 ARG A CA  1 
ATOM 2581 C C   . ARG A 1 402 ? 119.556 94.766  93.206  1.00 69.43  ? 402 ARG A C   1 
ATOM 2582 O O   . ARG A 1 402 ? 118.936 95.747  93.627  1.00 70.09  ? 402 ARG A O   1 
ATOM 2583 C CB  . ARG A 1 402 ? 120.767 93.617  95.043  1.00 69.37  ? 402 ARG A CB  1 
ATOM 2584 C CG  . ARG A 1 402 ? 120.875 92.461  96.017  1.00 69.24  ? 402 ARG A CG  1 
ATOM 2585 C CD  . ARG A 1 402 ? 122.025 92.645  96.981  1.00 73.25  ? 402 ARG A CD  1 
ATOM 2586 N NE  . ARG A 1 402 ? 122.267 91.432  97.753  1.00 77.79  ? 402 ARG A NE  1 
ATOM 2587 C CZ  . ARG A 1 402 ? 123.379 91.184  98.430  1.00 77.60  ? 402 ARG A CZ  1 
ATOM 2588 N NH1 . ARG A 1 402 ? 124.358 92.071  98.499  1.00 72.94  ? 402 ARG A NH1 1 
ATOM 2589 N NH2 . ARG A 1 402 ? 123.507 90.023  99.065  1.00 74.81  ? 402 ARG A NH2 1 
ATOM 2590 N N   . ILE A 1 403 ? 120.200 94.796  92.039  1.00 58.76  ? 403 ILE A N   1 
ATOM 2591 C CA  . ILE A 1 403 ? 120.234 96.018  91.236  1.00 58.84  ? 403 ILE A CA  1 
ATOM 2592 C C   . ILE A 1 403 ? 118.863 96.334  90.645  1.00 61.70  ? 403 ILE A C   1 
ATOM 2593 O O   . ILE A 1 403 ? 118.295 97.403  90.895  1.00 66.20  ? 403 ILE A O   1 
ATOM 2594 C CB  . ILE A 1 403 ? 121.303 95.905  90.134  1.00 60.51  ? 403 ILE A CB  1 
ATOM 2595 C CG1 . ILE A 1 403 ? 122.701 95.824  90.751  1.00 63.00  ? 403 ILE A CG1 1 
ATOM 2596 C CG2 . ILE A 1 403 ? 121.204 97.076  89.173  1.00 61.50  ? 403 ILE A CG2 1 
ATOM 2597 C CD1 . ILE A 1 403 ? 123.074 97.034  91.575  1.00 61.07  ? 403 ILE A CD1 1 
ATOM 2598 N N   . TYR A 1 404 ? 118.319 95.421  89.848  1.00 59.12  ? 404 TYR A N   1 
ATOM 2599 C CA  . TYR A 1 404 ? 117.011 95.621  89.227  1.00 52.79  ? 404 TYR A CA  1 
ATOM 2600 C C   . TYR A 1 404 ? 115.831 95.681  90.197  1.00 51.79  ? 404 TYR A C   1 
ATOM 2601 O O   . TYR A 1 404 ? 114.942 96.519  90.005  1.00 55.99  ? 404 TYR A O   1 
ATOM 2602 C CB  . TYR A 1 404 ? 116.772 94.534  88.175  1.00 52.85  ? 404 TYR A CB  1 
ATOM 2603 C CG  . TYR A 1 404 ? 117.883 94.435  87.155  1.00 59.54  ? 404 TYR A CG  1 
ATOM 2604 C CD1 . TYR A 1 404 ? 117.939 95.307  86.077  1.00 54.87  ? 404 TYR A CD1 1 
ATOM 2605 C CD2 . TYR A 1 404 ? 118.885 93.483  87.279  1.00 63.33  ? 404 TYR A CD2 1 
ATOM 2606 C CE1 . TYR A 1 404 ? 118.950 95.222  85.141  1.00 56.29  ? 404 TYR A CE1 1 
ATOM 2607 C CE2 . TYR A 1 404 ? 119.905 93.394  86.351  1.00 62.37  ? 404 TYR A CE2 1 
ATOM 2608 C CZ  . TYR A 1 404 ? 119.932 94.266  85.284  1.00 63.66  ? 404 TYR A CZ  1 
ATOM 2609 O OH  . TYR A 1 404 ? 120.949 94.187  84.360  1.00 63.54  ? 404 TYR A OH  1 
ATOM 2610 N N   . PRO A 1 405 ? 115.762 94.835  91.234  1.00 52.19  ? 405 PRO A N   1 
ATOM 2611 C CA  . PRO A 1 405 ? 114.723 95.045  92.260  1.00 50.99  ? 405 PRO A CA  1 
ATOM 2612 C C   . PRO A 1 405 ? 114.746 96.415  92.920  1.00 53.19  ? 405 PRO A C   1 
ATOM 2613 O O   . PRO A 1 405 ? 113.682 97.019  93.120  1.00 59.42  ? 405 PRO A O   1 
ATOM 2614 C CB  . PRO A 1 405 ? 115.017 93.929  93.271  1.00 52.10  ? 405 PRO A CB  1 
ATOM 2615 C CG  . PRO A 1 405 ? 115.564 92.841  92.438  1.00 53.22  ? 405 PRO A CG  1 
ATOM 2616 C CD  . PRO A 1 405 ? 116.445 93.546  91.436  1.00 54.52  ? 405 PRO A CD  1 
ATOM 2617 N N   . MET A 1 406 ? 115.930 96.971  93.179  1.00 45.56  ? 406 MET A N   1 
ATOM 2618 C CA  . MET A 1 406 ? 115.996 98.279  93.820  1.00 45.80  ? 406 MET A CA  1 
ATOM 2619 C C   . MET A 1 406 ? 115.760 99.420  92.840  1.00 49.58  ? 406 MET A C   1 
ATOM 2620 O O   . MET A 1 406 ? 115.144 100.428 93.207  1.00 47.03  ? 406 MET A O   1 
ATOM 2621 C CB  . MET A 1 406 ? 117.347 98.442  94.519  1.00 46.88  ? 406 MET A CB  1 
ATOM 2622 C CG  . MET A 1 406 ? 117.486 99.711  95.340  1.00 55.80  ? 406 MET A CG  1 
ATOM 2623 S SD  . MET A 1 406 ? 118.836 99.614  96.529  1.00 68.20  ? 406 MET A SD  1 
ATOM 2624 C CE  . MET A 1 406 ? 120.236 99.380  95.439  1.00 50.18  ? 406 MET A CE  1 
ATOM 2625 N N   . ALA A 1 407 ? 116.176 99.260  91.584  1.00 42.22  ? 407 ALA A N   1 
ATOM 2626 C CA  . ALA A 1 407 ? 115.801 100.228 90.560  1.00 34.42  ? 407 ALA A CA  1 
ATOM 2627 C C   . ALA A 1 407 ? 114.289 100.273 90.382  1.00 41.94  ? 407 ALA A C   1 
ATOM 2628 O O   . ALA A 1 407 ? 113.696 101.354 90.307  1.00 50.66  ? 407 ALA A O   1 
ATOM 2629 C CB  . ALA A 1 407 ? 116.492 99.890  89.240  1.00 32.75  ? 407 ALA A CB  1 
ATOM 2630 N N   . MET A 1 408 ? 113.653 99.104  90.268  1.00 36.52  ? 408 MET A N   1 
ATOM 2631 C CA  . MET A 1 408 ? 112.201 99.046  90.121  1.00 25.14  ? 408 MET A CA  1 
ATOM 2632 C C   . MET A 1 408 ? 111.470 99.626  91.328  1.00 29.54  ? 408 MET A C   1 
ATOM 2633 O O   . MET A 1 408 ? 110.470 100.335 91.168  1.00 37.75  ? 408 MET A O   1 
ATOM 2634 C CB  . MET A 1 408 ? 111.759 97.602  89.882  1.00 34.27  ? 408 MET A CB  1 
ATOM 2635 C CG  . MET A 1 408 ? 112.145 97.044  88.523  1.00 42.54  ? 408 MET A CG  1 
ATOM 2636 S SD  . MET A 1 408 ? 111.528 98.043  87.156  1.00 62.17  ? 408 MET A SD  1 
ATOM 2637 C CE  . MET A 1 408 ? 109.766 97.991  87.473  1.00 47.61  ? 408 MET A CE  1 
ATOM 2638 N N   . SER A 1 409 ? 111.963 99.365  92.542  1.00 27.80  ? 409 SER A N   1 
ATOM 2639 C CA  . SER A 1 409 ? 111.322 99.934  93.727  1.00 27.87  ? 409 SER A CA  1 
ATOM 2640 C C   . SER A 1 409 ? 111.549 101.437 93.882  1.00 35.24  ? 409 SER A C   1 
ATOM 2641 O O   . SER A 1 409 ? 110.714 102.119 94.488  1.00 34.13  ? 409 SER A O   1 
ATOM 2642 C CB  . SER A 1 409 ? 111.805 99.199  94.975  1.00 38.85  ? 409 SER A CB  1 
ATOM 2643 O OG  . SER A 1 409 ? 113.213 99.266  95.091  1.00 44.83  ? 409 SER A OG  1 
ATOM 2644 N N   . ASN A 1 410 ? 112.654 101.977 93.364  1.00 40.72  ? 410 ASN A N   1 
ATOM 2645 C CA  . ASN A 1 410 ? 112.808 103.431 93.304  1.00 32.08  ? 410 ASN A CA  1 
ATOM 2646 C C   . ASN A 1 410 ? 111.895 104.060 92.252  1.00 29.40  ? 410 ASN A C   1 
ATOM 2647 O O   . ASN A 1 410 ? 111.206 105.055 92.520  1.00 35.08  ? 410 ASN A O   1 
ATOM 2648 C CB  . ASN A 1 410 ? 114.267 103.793 93.028  1.00 35.30  ? 410 ASN A CB  1 
ATOM 2649 C CG  . ASN A 1 410 ? 115.102 103.864 94.293  1.00 41.40  ? 410 ASN A CG  1 
ATOM 2650 O OD1 . ASN A 1 410 ? 114.941 104.773 95.106  1.00 37.62  ? 410 ASN A OD1 1 
ATOM 2651 N ND2 . ASN A 1 410 ? 116.009 102.910 94.457  1.00 31.86  ? 410 ASN A ND2 1 
ATOM 2652 N N   . LEU A 1 411 ? 111.910 103.506 91.039  1.00 23.47  ? 411 LEU A N   1 
ATOM 2653 C CA  . LEU A 1 411 ? 111.039 103.968 89.962  1.00 27.41  ? 411 LEU A CA  1 
ATOM 2654 C C   . LEU A 1 411 ? 109.562 103.931 90.346  1.00 34.80  ? 411 LEU A C   1 
ATOM 2655 O O   . LEU A 1 411 ? 108.797 104.819 89.956  1.00 36.70  ? 411 LEU A O   1 
ATOM 2656 C CB  . LEU A 1 411 ? 111.288 103.116 88.717  1.00 32.88  ? 411 LEU A CB  1 
ATOM 2657 C CG  . LEU A 1 411 ? 110.491 103.383 87.442  1.00 38.51  ? 411 LEU A CG  1 
ATOM 2658 C CD1 . LEU A 1 411 ? 110.740 104.789 86.942  1.00 33.82  ? 411 LEU A CD1 1 
ATOM 2659 C CD2 . LEU A 1 411 ? 110.848 102.364 86.374  1.00 35.15  ? 411 LEU A CD2 1 
ATOM 2660 N N   . LEU A 1 412 ? 109.138 102.915 91.100  1.00 31.91  ? 412 LEU A N   1 
ATOM 2661 C CA  . LEU A 1 412 ? 107.735 102.826 91.502  1.00 26.24  ? 412 LEU A CA  1 
ATOM 2662 C C   . LEU A 1 412 ? 107.320 103.958 92.440  1.00 26.37  ? 412 LEU A C   1 
ATOM 2663 O O   . LEU A 1 412 ? 106.243 104.544 92.271  1.00 24.82  ? 412 LEU A O   1 
ATOM 2664 C CB  . LEU A 1 412 ? 107.480 101.469 92.158  1.00 31.31  ? 412 LEU A CB  1 
ATOM 2665 C CG  . LEU A 1 412 ? 106.039 101.083 92.492  1.00 34.23  ? 412 LEU A CG  1 
ATOM 2666 C CD1 . LEU A 1 412 ? 105.247 100.811 91.224  1.00 26.23  ? 412 LEU A CD1 1 
ATOM 2667 C CD2 . LEU A 1 412 ? 106.016 99.875  93.413  1.00 23.56  ? 412 LEU A CD2 1 
ATOM 2668 N N   . ALA A 1 413 ? 108.176 104.326 93.395  1.00 25.32  ? 413 ALA A N   1 
ATOM 2669 C CA  . ALA A 1 413 ? 107.861 105.461 94.259  1.00 29.33  ? 413 ALA A CA  1 
ATOM 2670 C C   . ALA A 1 413 ? 107.950 106.790 93.517  1.00 39.87  ? 413 ALA A C   1 
ATOM 2671 O O   . ALA A 1 413 ? 107.133 107.691 93.753  1.00 35.85  ? 413 ALA A O   1 
ATOM 2672 C CB  . ALA A 1 413 ? 108.788 105.467 95.472  1.00 27.78  ? 413 ALA A CB  1 
ATOM 2673 N N   . GLY A 1 414 ? 108.893 106.919 92.581  1.00 29.23  ? 414 GLY A N   1 
ATOM 2674 C CA  . GLY A 1 414 ? 108.928 108.122 91.763  1.00 7.31   ? 414 GLY A CA  1 
ATOM 2675 C C   . GLY A 1 414 ? 107.676 108.292 90.924  1.00 21.48  ? 414 GLY A C   1 
ATOM 2676 O O   . GLY A 1 414 ? 107.099 109.382 90.859  1.00 34.03  ? 414 GLY A O   1 
ATOM 2677 N N   . ALA A 1 415 ? 107.224 107.208 90.291  1.00 29.68  ? 415 ALA A N   1 
ATOM 2678 C CA  . ALA A 1 415 ? 106.032 107.266 89.453  1.00 23.39  ? 415 ALA A CA  1 
ATOM 2679 C C   . ALA A 1 415 ? 104.775 107.499 90.281  1.00 28.56  ? 415 ALA A C   1 
ATOM 2680 O O   . ALA A 1 415 ? 103.857 108.197 89.836  1.00 30.04  ? 415 ALA A O   1 
ATOM 2681 C CB  . ALA A 1 415 ? 105.908 105.984 88.634  1.00 26.18  ? 415 ALA A CB  1 
ATOM 2682 N N   . ALA A 1 416 ? 104.703 106.918 91.482  1.00 34.08  ? 416 ALA A N   1 
ATOM 2683 C CA  . ALA A 1 416 ? 103.566 107.196 92.354  1.00 24.21  ? 416 ALA A CA  1 
ATOM 2684 C C   . ALA A 1 416 ? 103.529 108.657 92.780  1.00 27.05  ? 416 ALA A C   1 
ATOM 2685 O O   . ALA A 1 416 ? 102.455 109.268 92.822  1.00 34.78  ? 416 ALA A O   1 
ATOM 2686 C CB  . ALA A 1 416 ? 103.609 106.284 93.578  1.00 35.85  ? 416 ALA A CB  1 
ATOM 2687 N N   . CYS A 1 417 ? 104.686 109.235 93.116  1.00 43.58  ? 417 CYS A N   1 
ATOM 2688 C CA  . CYS A 1 417 ? 104.727 110.663 93.428  1.00 34.86  ? 417 CYS A CA  1 
ATOM 2689 C C   . CYS A 1 417 ? 104.311 111.516 92.234  1.00 32.28  ? 417 CYS A C   1 
ATOM 2690 O O   . CYS A 1 417 ? 103.639 112.540 92.397  1.00 24.74  ? 417 CYS A O   1 
ATOM 2691 C CB  . CYS A 1 417 ? 106.122 111.062 93.909  1.00 37.19  ? 417 CYS A CB  1 
ATOM 2692 S SG  . CYS A 1 417 ? 106.639 110.300 95.460  1.00 53.31  ? 417 CYS A SG  1 
ATOM 2693 N N   . LEU A 1 418 ? 104.711 111.114 91.025  1.00 43.18  ? 418 LEU A N   1 
ATOM 2694 C CA  . LEU A 1 418 ? 104.319 111.840 89.817  1.00 37.53  ? 418 LEU A CA  1 
ATOM 2695 C C   . LEU A 1 418 ? 102.811 111.804 89.570  1.00 41.85  ? 418 LEU A C   1 
ATOM 2696 O O   . LEU A 1 418 ? 102.196 112.839 89.292  1.00 51.45  ? 418 LEU A O   1 
ATOM 2697 C CB  . LEU A 1 418 ? 105.066 111.272 88.611  1.00 40.00  ? 418 LEU A CB  1 
ATOM 2698 C CG  . LEU A 1 418 ? 104.792 111.929 87.258  1.00 43.88  ? 418 LEU A CG  1 
ATOM 2699 C CD1 . LEU A 1 418 ? 105.187 113.395 87.280  1.00 39.83  ? 418 LEU A CD1 1 
ATOM 2700 C CD2 . LEU A 1 418 ? 105.526 111.192 86.151  1.00 46.84  ? 418 LEU A CD2 1 
ATOM 2701 N N   . VAL A 1 419 ? 102.199 110.621 89.657  1.00 44.98  ? 419 VAL A N   1 
ATOM 2702 C CA  . VAL A 1 419 ? 100.755 110.491 89.446  1.00 39.28  ? 419 VAL A CA  1 
ATOM 2703 C C   . VAL A 1 419 ? 99.959  111.283 90.480  1.00 40.84  ? 419 VAL A C   1 
ATOM 2704 O O   . VAL A 1 419 ? 98.920  111.872 90.160  1.00 47.63  ? 419 VAL A O   1 
ATOM 2705 C CB  . VAL A 1 419 ? 100.354 109.004 89.440  1.00 38.71  ? 419 VAL A CB  1 
ATOM 2706 C CG1 . VAL A 1 419 ? 98.846  108.851 89.430  1.00 39.92  ? 419 VAL A CG1 1 
ATOM 2707 C CG2 . VAL A 1 419 ? 100.961 108.300 88.243  1.00 44.98  ? 419 VAL A CG2 1 
ATOM 2708 N N   . MET A 1 420 ? 100.432 111.323 91.727  1.00 41.90  ? 420 MET A N   1 
ATOM 2709 C CA  . MET A 1 420 ? 99.726  112.058 92.774  1.00 39.57  ? 420 MET A CA  1 
ATOM 2710 C C   . MET A 1 420 ? 99.561  113.545 92.475  1.00 48.28  ? 420 MET A C   1 
ATOM 2711 O O   . MET A 1 420 ? 98.695  114.187 93.079  1.00 50.91  ? 420 MET A O   1 
ATOM 2712 C CB  . MET A 1 420 ? 100.434 111.879 94.117  1.00 43.30  ? 420 MET A CB  1 
ATOM 2713 C CG  . MET A 1 420 ? 100.120 110.561 94.806  1.00 47.61  ? 420 MET A CG  1 
ATOM 2714 S SD  . MET A 1 420 ? 100.621 110.527 96.536  1.00 50.55  ? 420 MET A SD  1 
ATOM 2715 C CE  . MET A 1 420 ? 102.380 110.247 96.379  1.00 45.04  ? 420 MET A CE  1 
ATOM 2716 N N   . ILE A 1 421 ? 100.362 114.114 91.571  1.00 55.88  ? 421 ILE A N   1 
ATOM 2717 C CA  . ILE A 1 421 ? 100.180 115.520 91.218  1.00 50.56  ? 421 ILE A CA  1 
ATOM 2718 C C   . ILE A 1 421 ? 98.868  115.736 90.468  1.00 50.61  ? 421 ILE A C   1 
ATOM 2719 O O   . ILE A 1 421 ? 98.233  116.789 90.604  1.00 55.01  ? 421 ILE A O   1 
ATOM 2720 C CB  . ILE A 1 421 ? 101.386 116.013 90.394  1.00 47.81  ? 421 ILE A CB  1 
ATOM 2721 C CG1 . ILE A 1 421 ? 102.662 115.976 91.233  1.00 46.02  ? 421 ILE A CG1 1 
ATOM 2722 C CG2 . ILE A 1 421 ? 101.155 117.424 89.872  1.00 50.07  ? 421 ILE A CG2 1 
ATOM 2723 C CD1 . ILE A 1 421 ? 103.924 116.002 90.406  1.00 48.45  ? 421 ILE A CD1 1 
ATOM 2724 N N   . PHE A 1 422 ? 98.423  114.745 89.695  1.00 54.78  ? 422 PHE A N   1 
ATOM 2725 C CA  . PHE A 1 422 ? 97.316  114.919 88.762  1.00 55.34  ? 422 PHE A CA  1 
ATOM 2726 C C   . PHE A 1 422 ? 95.990  114.363 89.268  1.00 58.54  ? 422 PHE A C   1 
ATOM 2727 O O   . PHE A 1 422 ? 94.952  114.643 88.659  1.00 60.36  ? 422 PHE A O   1 
ATOM 2728 C CB  . PHE A 1 422 ? 97.658  114.276 87.413  1.00 53.52  ? 422 PHE A CB  1 
ATOM 2729 C CG  . PHE A 1 422 ? 98.902  114.828 86.777  1.00 55.82  ? 422 PHE A CG  1 
ATOM 2730 C CD1 . PHE A 1 422 ? 98.854  115.994 86.031  1.00 55.10  ? 422 PHE A CD1 1 
ATOM 2731 C CD2 . PHE A 1 422 ? 100.119 114.188 86.928  1.00 56.97  ? 422 PHE A CD2 1 
ATOM 2732 C CE1 . PHE A 1 422 ? 99.994  116.506 85.445  1.00 53.93  ? 422 PHE A CE1 1 
ATOM 2733 C CE2 . PHE A 1 422 ? 101.263 114.698 86.344  1.00 57.50  ? 422 PHE A CE2 1 
ATOM 2734 C CZ  . PHE A 1 422 ? 101.199 115.859 85.602  1.00 55.83  ? 422 PHE A CZ  1 
ATOM 2735 N N   . ILE A 1 423 ? 95.994  113.587 90.352  1.00 69.10  ? 423 ILE A N   1 
ATOM 2736 C CA  . ILE A 1 423 ? 94.762  112.987 90.854  1.00 69.53  ? 423 ILE A CA  1 
ATOM 2737 C C   . ILE A 1 423 ? 93.835  114.076 91.377  1.00 70.62  ? 423 ILE A C   1 
ATOM 2738 O O   . ILE A 1 423 ? 94.253  114.967 92.128  1.00 69.45  ? 423 ILE A O   1 
ATOM 2739 C CB  . ILE A 1 423 ? 95.072  111.949 91.943  1.00 66.90  ? 423 ILE A CB  1 
ATOM 2740 C CG1 . ILE A 1 423 ? 95.754  110.724 91.332  1.00 65.97  ? 423 ILE A CG1 1 
ATOM 2741 C CG2 . ILE A 1 423 ? 93.804  111.534 92.666  1.00 66.63  ? 423 ILE A CG2 1 
ATOM 2742 C CD1 . ILE A 1 423 ? 96.254  109.735 92.357  1.00 63.36  ? 423 ILE A CD1 1 
ATOM 2743 N N   . SER A 1 424 ? 92.572  114.013 90.968  1.00 84.69  ? 424 SER A N   1 
ATOM 2744 C CA  . SER A 1 424 ? 91.575  114.956 91.450  1.00 84.99  ? 424 SER A CA  1 
ATOM 2745 C C   . SER A 1 424 ? 91.365  114.788 92.955  1.00 85.21  ? 424 SER A C   1 
ATOM 2746 O O   . SER A 1 424 ? 91.373  113.660 93.463  1.00 82.42  ? 424 SER A O   1 
ATOM 2747 C CB  . SER A 1 424 ? 90.253  114.758 90.709  1.00 84.74  ? 424 SER A CB  1 
ATOM 2748 O OG  . SER A 1 424 ? 90.442  114.809 89.306  1.00 83.22  ? 424 SER A OG  1 
ATOM 2749 N N   . PRO A 1 425 ? 91.182  115.887 93.694  1.00 92.53  ? 425 PRO A N   1 
ATOM 2750 C CA  . PRO A 1 425 ? 91.223  115.812 95.165  1.00 92.89  ? 425 PRO A CA  1 
ATOM 2751 C C   . PRO A 1 425 ? 90.091  115.006 95.782  1.00 90.96  ? 425 PRO A C   1 
ATOM 2752 O O   . PRO A 1 425 ? 90.194  114.632 96.957  1.00 90.33  ? 425 PRO A O   1 
ATOM 2753 C CB  . PRO A 1 425 ? 91.151  117.285 95.593  1.00 91.51  ? 425 PRO A CB  1 
ATOM 2754 C CG  . PRO A 1 425 ? 90.452  117.963 94.460  1.00 92.16  ? 425 PRO A CG  1 
ATOM 2755 C CD  . PRO A 1 425 ? 90.951  117.261 93.224  1.00 88.99  ? 425 PRO A CD  1 
ATOM 2756 N N   . ASP A 1 426 ? 89.021  114.727 95.040  1.00 91.55  ? 426 ASP A N   1 
ATOM 2757 C CA  . ASP A 1 426 ? 87.938  113.877 95.518  1.00 92.89  ? 426 ASP A CA  1 
ATOM 2758 C C   . ASP A 1 426 ? 88.178  112.390 95.290  1.00 93.72  ? 426 ASP A C   1 
ATOM 2759 O O   . ASP A 1 426 ? 87.460  111.571 95.873  1.00 95.24  ? 426 ASP A O   1 
ATOM 2760 C CB  . ASP A 1 426 ? 86.616  114.284 94.855  1.00 92.23  ? 426 ASP A CB  1 
ATOM 2761 C CG  . ASP A 1 426 ? 86.735  114.419 93.350  1.00 93.49  ? 426 ASP A CG  1 
ATOM 2762 O OD1 . ASP A 1 426 ? 87.873  114.381 92.837  1.00 95.03  ? 426 ASP A OD1 1 
ATOM 2763 O OD2 . ASP A 1 426 ? 85.691  114.566 92.681  1.00 92.81  ? 426 ASP A OD2 1 
ATOM 2764 N N   . LEU A 1 427 ? 89.157  112.015 94.468  1.00 85.94  ? 427 LEU A N   1 
ATOM 2765 C CA  . LEU A 1 427 ? 89.474  110.605 94.261  1.00 84.65  ? 427 LEU A CA  1 
ATOM 2766 C C   . LEU A 1 427 ? 90.355  110.070 95.387  1.00 85.54  ? 427 LEU A C   1 
ATOM 2767 O O   . LEU A 1 427 ? 91.386  109.436 95.139  1.00 86.57  ? 427 LEU A O   1 
ATOM 2768 C CB  . LEU A 1 427 ? 90.148  110.404 92.902  1.00 84.48  ? 427 LEU A CB  1 
ATOM 2769 C CG  . LEU A 1 427 ? 89.227  110.071 91.724  1.00 84.22  ? 427 LEU A CG  1 
ATOM 2770 C CD1 . LEU A 1 427 ? 88.155  111.134 91.533  1.00 83.77  ? 427 LEU A CD1 1 
ATOM 2771 C CD2 . LEU A 1 427 ? 90.031  109.892 90.446  1.00 83.71  ? 427 LEU A CD2 1 
ATOM 2772 N N   . HIS A 1 428 ? 89.944  110.341 96.630  1.00 79.94  ? 428 HIS A N   1 
ATOM 2773 C CA  . HIS A 1 428 ? 90.650  109.861 97.817  1.00 80.59  ? 428 HIS A CA  1 
ATOM 2774 C C   . HIS A 1 428 ? 90.860  108.350 97.801  1.00 79.82  ? 428 HIS A C   1 
ATOM 2775 O O   . HIS A 1 428 ? 91.920  107.856 98.209  1.00 78.64  ? 428 HIS A O   1 
ATOM 2776 C CB  . HIS A 1 428 ? 89.877  110.278 99.071  1.00 80.77  ? 428 HIS A CB  1 
ATOM 2777 C CG  . HIS A 1 428 ? 90.402  109.678 100.337 1.00 82.60  ? 428 HIS A CG  1 
ATOM 2778 N ND1 . HIS A 1 428 ? 91.575  110.094 100.929 1.00 83.68  ? 428 HIS A ND1 1 
ATOM 2779 C CD2 . HIS A 1 428 ? 89.909  108.697 101.130 1.00 81.35  ? 428 HIS A CD2 1 
ATOM 2780 C CE1 . HIS A 1 428 ? 91.784  109.392 102.029 1.00 79.77  ? 428 HIS A CE1 1 
ATOM 2781 N NE2 . HIS A 1 428 ? 90.787  108.538 102.173 1.00 81.79  ? 428 HIS A NE2 1 
ATOM 2782 N N   . TRP A 1 429 ? 89.860  107.599 97.330  1.00 73.65  ? 429 TRP A N   1 
ATOM 2783 C CA  . TRP A 1 429 ? 89.981  106.146 97.254  1.00 74.79  ? 429 TRP A CA  1 
ATOM 2784 C C   . TRP A 1 429 ? 91.069  105.692 96.291  1.00 76.66  ? 429 TRP A C   1 
ATOM 2785 O O   . TRP A 1 429 ? 91.565  104.569 96.428  1.00 74.03  ? 429 TRP A O   1 
ATOM 2786 C CB  . TRP A 1 429 ? 88.631  105.530 96.873  1.00 72.75  ? 429 TRP A CB  1 
ATOM 2787 C CG  . TRP A 1 429 ? 88.063  106.013 95.570  1.00 73.35  ? 429 TRP A CG  1 
ATOM 2788 C CD1 . TRP A 1 429 ? 87.143  107.004 95.399  1.00 74.63  ? 429 TRP A CD1 1 
ATOM 2789 C CD2 . TRP A 1 429 ? 88.347  105.500 94.262  1.00 74.45  ? 429 TRP A CD2 1 
ATOM 2790 N NE1 . TRP A 1 429 ? 86.849  107.155 94.067  1.00 75.84  ? 429 TRP A NE1 1 
ATOM 2791 C CE2 . TRP A 1 429 ? 87.574  106.242 93.347  1.00 73.06  ? 429 TRP A CE2 1 
ATOM 2792 C CE3 . TRP A 1 429 ? 89.184  104.492 93.776  1.00 73.71  ? 429 TRP A CE3 1 
ATOM 2793 C CZ2 . TRP A 1 429 ? 87.614  106.009 91.976  1.00 68.16  ? 429 TRP A CZ2 1 
ATOM 2794 C CZ3 . TRP A 1 429 ? 89.222  104.262 92.414  1.00 75.54  ? 429 TRP A CZ3 1 
ATOM 2795 C CH2 . TRP A 1 429 ? 88.442  105.018 91.530  1.00 73.36  ? 429 TRP A CH2 1 
ATOM 2796 N N   . LEU A 1 430 ? 91.450  106.522 95.323  1.00 70.02  ? 430 LEU A N   1 
ATOM 2797 C CA  . LEU A 1 430 ? 92.625  106.231 94.509  1.00 67.49  ? 430 LEU A CA  1 
ATOM 2798 C C   . LEU A 1 430 ? 93.890  106.775 95.164  1.00 64.49  ? 430 LEU A C   1 
ATOM 2799 O O   . LEU A 1 430 ? 94.968  106.171 95.051  1.00 69.94  ? 430 LEU A O   1 
ATOM 2800 C CB  . LEU A 1 430 ? 92.448  106.820 93.107  1.00 66.40  ? 430 LEU A CB  1 
ATOM 2801 C CG  . LEU A 1 430 ? 93.503  106.483 92.054  1.00 66.94  ? 430 LEU A CG  1 
ATOM 2802 C CD1 . LEU A 1 430 ? 93.533  104.987 91.798  1.00 64.78  ? 430 LEU A CD1 1 
ATOM 2803 C CD2 . LEU A 1 430 ? 93.222  107.238 90.768  1.00 65.57  ? 430 LEU A CD2 1 
ATOM 2804 N N   . ASN A 1 431 ? 93.769  107.953 95.779  1.00 60.10  ? 431 ASN A N   1 
ATOM 2805 C CA  . ASN A 1 431 ? 94.910  108.624 96.392  1.00 62.91  ? 431 ASN A CA  1 
ATOM 2806 C C   . ASN A 1 431 ? 95.571  107.751 97.453  1.00 66.79  ? 431 ASN A C   1 
ATOM 2807 O O   . ASN A 1 431 ? 96.805  107.654 97.509  1.00 66.95  ? 431 ASN A O   1 
ATOM 2808 C CB  . ASN A 1 431 ? 94.460  109.956 96.993  1.00 62.52  ? 431 ASN A CB  1 
ATOM 2809 C CG  . ASN A 1 431 ? 95.613  110.766 97.546  1.00 67.68  ? 431 ASN A CG  1 
ATOM 2810 O OD1 . ASN A 1 431 ? 95.978  110.631 98.713  1.00 71.08  ? 431 ASN A OD1 1 
ATOM 2811 N ND2 . ASN A 1 431 ? 96.191  111.619 96.709  1.00 66.55  ? 431 ASN A ND2 1 
ATOM 2812 N N   . ILE A 1 432 ? 94.766  107.075 98.279  1.00 58.94  ? 432 ILE A N   1 
ATOM 2813 C CA  . ILE A 1 432 ? 95.349  106.181 99.277  1.00 58.67  ? 432 ILE A CA  1 
ATOM 2814 C C   . ILE A 1 432 ? 96.010  104.972 98.624  1.00 58.77  ? 432 ILE A C   1 
ATOM 2815 O O   . ILE A 1 432 ? 97.032  104.480 99.118  1.00 62.96  ? 432 ILE A O   1 
ATOM 2816 C CB  . ILE A 1 432 ? 94.283  105.764 100.310 1.00 56.12  ? 432 ILE A CB  1 
ATOM 2817 C CG1 . ILE A 1 432 ? 94.926  104.996 101.466 1.00 56.07  ? 432 ILE A CG1 1 
ATOM 2818 C CG2 . ILE A 1 432 ? 93.181  104.940 99.664  1.00 55.26  ? 432 ILE A CG2 1 
ATOM 2819 C CD1 . ILE A 1 432 ? 95.999  105.775 102.195 1.00 55.51  ? 432 ILE A CD1 1 
ATOM 2820 N N   . ILE A 1 433 ? 95.464  104.475 97.513  1.00 49.23  ? 433 ILE A N   1 
ATOM 2821 C CA  . ILE A 1 433 ? 96.073  103.326 96.847  1.00 48.56  ? 433 ILE A CA  1 
ATOM 2822 C C   . ILE A 1 433 ? 97.464  103.693 96.347  1.00 53.81  ? 433 ILE A C   1 
ATOM 2823 O O   . ILE A 1 433 ? 98.440  102.957 96.548  1.00 58.96  ? 433 ILE A O   1 
ATOM 2824 C CB  . ILE A 1 433 ? 95.175  102.816 95.705  1.00 48.26  ? 433 ILE A CB  1 
ATOM 2825 C CG1 . ILE A 1 433 ? 93.834  102.333 96.253  1.00 53.59  ? 433 ILE A CG1 1 
ATOM 2826 C CG2 . ILE A 1 433 ? 95.859  101.695 94.949  1.00 52.64  ? 433 ILE A CG2 1 
ATOM 2827 C CD1 . ILE A 1 433 ? 92.849  101.935 95.178  1.00 55.93  ? 433 ILE A CD1 1 
ATOM 2828 N N   . ILE A 1 434 ? 97.570  104.848 95.686  1.00 46.27  ? 434 ILE A N   1 
ATOM 2829 C CA  . ILE A 1 434 ? 98.865  105.303 95.183  1.00 40.31  ? 434 ILE A CA  1 
ATOM 2830 C C   . ILE A 1 434 ? 99.831  105.620 96.324  1.00 44.44  ? 434 ILE A C   1 
ATOM 2831 O O   . ILE A 1 434 ? 101.040 105.354 96.218  1.00 45.05  ? 434 ILE A O   1 
ATOM 2832 C CB  . ILE A 1 434 ? 98.665  106.517 94.257  1.00 42.62  ? 434 ILE A CB  1 
ATOM 2833 C CG1 . ILE A 1 434 ? 97.713  106.161 93.115  1.00 45.16  ? 434 ILE A CG1 1 
ATOM 2834 C CG2 . ILE A 1 434 ? 99.992  106.984 93.692  1.00 48.85  ? 434 ILE A CG2 1 
ATOM 2835 C CD1 . ILE A 1 434 ? 98.173  104.987 92.283  1.00 45.42  ? 434 ILE A CD1 1 
ATOM 2836 N N   . MET A 1 435 ? 99.322  106.123 97.453  1.00 46.93  ? 435 MET A N   1 
ATOM 2837 C CA  . MET A 1 435 ? 100.190 106.363 98.604  1.00 47.13  ? 435 MET A CA  1 
ATOM 2838 C C   . MET A 1 435 ? 100.726 105.057 99.180  1.00 50.81  ? 435 MET A C   1 
ATOM 2839 O O   . MET A 1 435 ? 101.906 104.969 99.545  1.00 51.50  ? 435 MET A O   1 
ATOM 2840 C CB  . MET A 1 435 ? 99.431  107.148 99.672  1.00 44.55  ? 435 MET A CB  1 
ATOM 2841 C CG  . MET A 1 435 ? 100.255 107.497 100.899 1.00 55.78  ? 435 MET A CG  1 
ATOM 2842 S SD  . MET A 1 435 ? 101.519 108.743 100.580 1.00 71.09  ? 435 MET A SD  1 
ATOM 2843 C CE  . MET A 1 435 ? 100.518 110.225 100.488 1.00 50.88  ? 435 MET A CE  1 
ATOM 2844 N N   . CYS A 1 436 ? 99.894  104.015 99.217  1.00 45.08  ? 436 CYS A N   1 
ATOM 2845 C CA  . CYS A 1 436 ? 100.355 102.724 99.712  1.00 39.39  ? 436 CYS A CA  1 
ATOM 2846 C C   . CYS A 1 436 ? 101.349 102.080 98.755  1.00 42.20  ? 436 CYS A C   1 
ATOM 2847 O O   . CYS A 1 436 ? 102.290 101.409 99.198  1.00 46.99  ? 436 CYS A O   1 
ATOM 2848 C CB  . CYS A 1 436 ? 99.163  101.797 99.945  1.00 38.83  ? 436 CYS A CB  1 
ATOM 2849 S SG  . CYS A 1 436 ? 98.122  102.249 101.354 1.00 35.69  ? 436 CYS A SG  1 
ATOM 2850 N N   . VAL A 1 437 ? 101.178 102.293 97.449  1.00 39.81  ? 437 VAL A N   1 
ATOM 2851 C CA  . VAL A 1 437 ? 102.118 101.721 96.489  1.00 39.33  ? 437 VAL A CA  1 
ATOM 2852 C C   . VAL A 1 437 ? 103.479 102.406 96.593  1.00 40.73  ? 437 VAL A C   1 
ATOM 2853 O O   . VAL A 1 437 ? 104.528 101.744 96.576  1.00 46.54  ? 437 VAL A O   1 
ATOM 2854 C CB  . VAL A 1 437 ? 101.539 101.817 95.065  1.00 32.88  ? 437 VAL A CB  1 
ATOM 2855 C CG1 . VAL A 1 437 ? 102.603 101.501 94.031  1.00 36.85  ? 437 VAL A CG1 1 
ATOM 2856 C CG2 . VAL A 1 437 ? 100.349 100.884 94.911  1.00 31.75  ? 437 VAL A CG2 1 
ATOM 2857 N N   . GLY A 1 438 ? 103.486 103.727 96.791  1.00 33.11  ? 438 GLY A N   1 
ATOM 2858 C CA  . GLY A 1 438 ? 104.747 104.411 97.040  1.00 25.85  ? 438 GLY A CA  1 
ATOM 2859 C C   . GLY A 1 438 ? 105.405 103.985 98.341  1.00 35.36  ? 438 GLY A C   1 
ATOM 2860 O O   . GLY A 1 438 ? 106.633 103.827 98.406  1.00 41.82  ? 438 GLY A O   1 
ATOM 2861 N N   . ARG A 1 439 ? 104.604 103.795 99.393  1.00 37.52  ? 439 ARG A N   1 
ATOM 2862 C CA  . ARG A 1 439 ? 105.152 103.346 100.670 1.00 32.14  ? 439 ARG A CA  1 
ATOM 2863 C C   . ARG A 1 439 ? 105.816 101.981 100.531 1.00 35.49  ? 439 ARG A C   1 
ATOM 2864 O O   . ARG A 1 439 ? 106.939 101.775 101.006 1.00 42.77  ? 439 ARG A O   1 
ATOM 2865 C CB  . ARG A 1 439 ? 104.056 103.317 101.735 1.00 36.31  ? 439 ARG A CB  1 
ATOM 2866 C CG  . ARG A 1 439 ? 103.660 104.701 102.223 1.00 42.93  ? 439 ARG A CG  1 
ATOM 2867 C CD  . ARG A 1 439 ? 104.567 105.216 103.332 1.00 45.37  ? 439 ARG A CD  1 
ATOM 2868 N NE  . ARG A 1 439 ? 104.200 104.706 104.648 1.00 42.99  ? 439 ARG A NE  1 
ATOM 2869 C CZ  . ARG A 1 439 ? 104.945 103.881 105.370 1.00 40.12  ? 439 ARG A CZ  1 
ATOM 2870 N NH1 . ARG A 1 439 ? 106.095 103.415 104.916 1.00 47.09  ? 439 ARG A NH1 1 
ATOM 2871 N NH2 . ARG A 1 439 ? 104.524 103.516 106.577 1.00 30.33  ? 439 ARG A NH2 1 
ATOM 2872 N N   . MET A 1 440 ? 105.110 101.017 99.933  1.00 34.04  ? 440 MET A N   1 
ATOM 2873 C CA  . MET A 1 440 ? 105.698 99.693  99.738  1.00 38.19  ? 440 MET A CA  1 
ATOM 2874 C C   . MET A 1 440 ? 106.971 99.760  98.899  1.00 43.01  ? 440 MET A C   1 
ATOM 2875 O O   . MET A 1 440 ? 107.948 99.050  99.181  1.00 49.79  ? 440 MET A O   1 
ATOM 2876 C CB  . MET A 1 440 ? 104.679 98.760  99.086  1.00 34.88  ? 440 MET A CB  1 
ATOM 2877 C CG  . MET A 1 440 ? 105.020 97.287  99.212  1.00 42.67  ? 440 MET A CG  1 
ATOM 2878 S SD  . MET A 1 440 ? 103.653 96.211  98.750  1.00 51.73  ? 440 MET A SD  1 
ATOM 2879 C CE  . MET A 1 440 ? 103.784 96.256  96.966  1.00 49.45  ? 440 MET A CE  1 
ATOM 2880 N N   . GLY A 1 441 ? 106.988 100.621 97.875  1.00 32.57  ? 441 GLY A N   1 
ATOM 2881 C CA  . GLY A 1 441 ? 108.201 100.787 97.087  1.00 24.72  ? 441 GLY A CA  1 
ATOM 2882 C C   . GLY A 1 441 ? 109.391 101.248 97.908  1.00 33.60  ? 441 GLY A C   1 
ATOM 2883 O O   . GLY A 1 441 ? 110.475 100.653 97.851  1.00 40.81  ? 441 GLY A O   1 
ATOM 2884 N N   . ILE A 1 442 ? 109.205 102.308 98.701  1.00 39.34  ? 442 ILE A N   1 
ATOM 2885 C CA  . ILE A 1 442 ? 110.343 102.819 99.465  1.00 37.73  ? 442 ILE A CA  1 
ATOM 2886 C C   . ILE A 1 442 ? 110.731 101.859 100.583 1.00 44.31  ? 442 ILE A C   1 
ATOM 2887 O O   . ILE A 1 442 ? 111.908 101.778 100.954 1.00 49.12  ? 442 ILE A O   1 
ATOM 2888 C CB  . ILE A 1 442 ? 110.064 104.233 100.011 1.00 40.09  ? 442 ILE A CB  1 
ATOM 2889 C CG1 . ILE A 1 442 ? 108.826 104.247 100.905 1.00 40.14  ? 442 ILE A CG1 1 
ATOM 2890 C CG2 . ILE A 1 442 ? 109.925 105.229 98.876  1.00 47.46  ? 442 ILE A CG2 1 
ATOM 2891 C CD1 . ILE A 1 442 ? 108.455 105.624 101.404 1.00 46.67  ? 442 ILE A CD1 1 
ATOM 2892 N N   . THR A 1 443 ? 109.776 101.089 101.108 1.00 45.87  ? 443 THR A N   1 
ATOM 2893 C CA  . THR A 1 443 ? 110.105 100.066 102.097 1.00 37.42  ? 443 THR A CA  1 
ATOM 2894 C C   . THR A 1 443 ? 111.006 98.989  101.504 1.00 35.61  ? 443 THR A C   1 
ATOM 2895 O O   . THR A 1 443 ? 112.031 98.622  102.094 1.00 43.67  ? 443 THR A O   1 
ATOM 2896 C CB  . THR A 1 443 ? 108.824 99.446  102.655 1.00 42.35  ? 443 THR A CB  1 
ATOM 2897 O OG1 . THR A 1 443 ? 108.022 100.467 103.259 1.00 55.59  ? 443 THR A OG1 1 
ATOM 2898 C CG2 . THR A 1 443 ? 109.155 98.389  103.694 1.00 48.34  ? 443 THR A CG2 1 
ATOM 2899 N N   . ILE A 1 444 ? 110.641 98.472  100.329 1.00 39.95  ? 444 ILE A N   1 
ATOM 2900 C CA  . ILE A 1 444 ? 111.468 97.458  99.678  1.00 42.84  ? 444 ILE A CA  1 
ATOM 2901 C C   . ILE A 1 444 ? 112.849 98.014  99.342  1.00 46.47  ? 444 ILE A C   1 
ATOM 2902 O O   . ILE A 1 444 ? 113.866 97.328  99.508  1.00 52.04  ? 444 ILE A O   1 
ATOM 2903 C CB  . ILE A 1 444 ? 110.756 96.910  98.427  1.00 44.89  ? 444 ILE A CB  1 
ATOM 2904 C CG1 . ILE A 1 444 ? 109.483 96.163  98.824  1.00 40.61  ? 444 ILE A CG1 1 
ATOM 2905 C CG2 . ILE A 1 444 ? 111.676 95.989  97.644  1.00 44.09  ? 444 ILE A CG2 1 
ATOM 2906 C CD1 . ILE A 1 444 ? 108.515 95.964  97.682  1.00 43.36  ? 444 ILE A CD1 1 
ATOM 2907 N N   . ALA A 1 445 ? 112.917 99.274  98.900  1.00 44.17  ? 445 ALA A N   1 
ATOM 2908 C CA  . ALA A 1 445 ? 114.218 99.852  98.564  1.00 39.91  ? 445 ALA A CA  1 
ATOM 2909 C C   . ALA A 1 445 ? 115.102 100.033 99.798  1.00 44.85  ? 445 ALA A C   1 
ATOM 2910 O O   . ALA A 1 445 ? 116.310 99.760  99.748  1.00 51.02  ? 445 ALA A O   1 
ATOM 2911 C CB  . ALA A 1 445 ? 114.029 101.186 97.845  1.00 45.34  ? 445 ALA A CB  1 
ATOM 2912 N N   . ILE A 1 446 ? 114.529 100.514 100.904 1.00 47.47  ? 446 ILE A N   1 
ATOM 2913 C CA  . ILE A 1 446 ? 115.287 100.634 102.147 1.00 46.08  ? 446 ILE A CA  1 
ATOM 2914 C C   . ILE A 1 446 ? 115.778 99.273  102.630 1.00 53.65  ? 446 ILE A C   1 
ATOM 2915 O O   . ILE A 1 446 ? 116.916 99.143  103.095 1.00 54.80  ? 446 ILE A O   1 
ATOM 2916 C CB  . ILE A 1 446 ? 114.449 101.347 103.224 1.00 45.16  ? 446 ILE A CB  1 
ATOM 2917 C CG1 . ILE A 1 446 ? 114.282 102.825 102.876 1.00 50.11  ? 446 ILE A CG1 1 
ATOM 2918 C CG2 . ILE A 1 446 ? 115.090 101.199 104.592 1.00 47.18  ? 446 ILE A CG2 1 
ATOM 2919 C CD1 . ILE A 1 446 ? 113.217 103.514 103.682 1.00 49.66  ? 446 ILE A CD1 1 
ATOM 2920 N N   . GLN A 1 447 ? 114.939 98.238  102.534 1.00 61.51  ? 447 GLN A N   1 
ATOM 2921 C CA  . GLN A 1 447 ? 115.408 96.905  102.911 1.00 54.66  ? 447 GLN A CA  1 
ATOM 2922 C C   . GLN A 1 447 ? 116.547 96.426  102.015 1.00 55.90  ? 447 GLN A C   1 
ATOM 2923 O O   . GLN A 1 447 ? 117.486 95.779  102.491 1.00 62.34  ? 447 GLN A O   1 
ATOM 2924 C CB  . GLN A 1 447 ? 114.251 95.905  102.873 1.00 57.53  ? 447 GLN A CB  1 
ATOM 2925 C CG  . GLN A 1 447 ? 113.120 96.198  103.848 1.00 59.41  ? 447 GLN A CG  1 
ATOM 2926 C CD  . GLN A 1 447 ? 113.614 96.563  105.232 1.00 62.64  ? 447 GLN A CD  1 
ATOM 2927 O OE1 . GLN A 1 447 ? 114.454 95.871  105.807 1.00 62.45  ? 447 GLN A OE1 1 
ATOM 2928 N NE2 . GLN A 1 447 ? 113.093 97.655  105.776 1.00 61.57  ? 447 GLN A NE2 1 
ATOM 2929 N N   . MET A 1 448 ? 116.483 96.726  100.716 1.00 54.80  ? 448 MET A N   1 
ATOM 2930 C CA  . MET A 1 448 ? 117.540 96.289  99.804  1.00 54.68  ? 448 MET A CA  1 
ATOM 2931 C C   . MET A 1 448 ? 118.870 96.981  100.093 1.00 58.00  ? 448 MET A C   1 
ATOM 2932 O O   . MET A 1 448 ? 119.933 96.340  100.101 1.00 63.52  ? 448 MET A O   1 
ATOM 2933 C CB  . MET A 1 448 ? 117.118 96.526  98.355  1.00 62.87  ? 448 MET A CB  1 
ATOM 2934 C CG  . MET A 1 448 ? 116.005 95.617  97.871  1.00 65.68  ? 448 MET A CG  1 
ATOM 2935 S SD  . MET A 1 448 ? 116.615 93.998  97.372  1.00 71.46  ? 448 MET A SD  1 
ATOM 2936 C CE  . MET A 1 448 ? 115.082 93.179  96.951  1.00 62.13  ? 448 MET A CE  1 
ATOM 2937 N N   . ILE A 1 449 ? 118.838 98.300  100.305 1.00 64.94  ? 449 ILE A N   1 
ATOM 2938 C CA  . ILE A 1 449 ? 120.093 99.028  100.485 1.00 65.64  ? 449 ILE A CA  1 
ATOM 2939 C C   . ILE A 1 449 ? 120.825 98.606  101.757 1.00 66.63  ? 449 ILE A C   1 
ATOM 2940 O O   . ILE A 1 449 ? 122.057 98.700  101.824 1.00 68.87  ? 449 ILE A O   1 
ATOM 2941 C CB  . ILE A 1 449 ? 119.839 100.549 100.457 1.00 63.86  ? 449 ILE A CB  1 
ATOM 2942 C CG1 . ILE A 1 449 ? 121.162 101.310 100.380 1.00 63.14  ? 449 ILE A CG1 1 
ATOM 2943 C CG2 . ILE A 1 449 ? 119.056 100.995 101.675 1.00 62.99  ? 449 ILE A CG2 1 
ATOM 2944 C CD1 . ILE A 1 449 ? 121.014 102.740 99.932  1.00 62.03  ? 449 ILE A CD1 1 
ATOM 2945 N N   . CYS A 1 450 ? 120.106 98.133  102.780 1.00 65.66  ? 450 CYS A N   1 
ATOM 2946 C CA  . CYS A 1 450 ? 120.784 97.639  103.977 1.00 67.66  ? 450 CYS A CA  1 
ATOM 2947 C C   . CYS A 1 450 ? 121.669 96.433  103.683 1.00 70.97  ? 450 CYS A C   1 
ATOM 2948 O O   . CYS A 1 450 ? 122.683 96.228  104.360 1.00 68.77  ? 450 CYS A O   1 
ATOM 2949 C CB  . CYS A 1 450 ? 119.762 97.294  105.059 1.00 68.78  ? 450 CYS A CB  1 
ATOM 2950 S SG  . CYS A 1 450 ? 118.771 98.694  105.624 1.00 78.90  ? 450 CYS A SG  1 
ATOM 2951 N N   . LEU A 1 451 ? 121.311 95.629  102.681 1.00 76.44  ? 451 LEU A N   1 
ATOM 2952 C CA  . LEU A 1 451 ? 122.197 94.571  102.206 1.00 73.72  ? 451 LEU A CA  1 
ATOM 2953 C C   . LEU A 1 451 ? 123.282 95.110  101.282 1.00 74.36  ? 451 LEU A C   1 
ATOM 2954 O O   . LEU A 1 451 ? 124.466 94.804  101.461 1.00 75.95  ? 451 LEU A O   1 
ATOM 2955 C CB  . LEU A 1 451 ? 121.397 93.473  101.502 1.00 73.10  ? 451 LEU A CB  1 
ATOM 2956 C CG  . LEU A 1 451 ? 120.664 92.447  102.374 1.00 75.25  ? 451 LEU A CG  1 
ATOM 2957 C CD1 . LEU A 1 451 ? 119.439 93.041  103.060 1.00 73.23  ? 451 LEU A CD1 1 
ATOM 2958 C CD2 . LEU A 1 451 ? 120.294 91.220  101.553 1.00 74.44  ? 451 LEU A CD2 1 
ATOM 2959 N N   . VAL A 1 452 ? 122.890 95.901  100.280 1.00 76.42  ? 452 VAL A N   1 
ATOM 2960 C CA  . VAL A 1 452 ? 123.845 96.366  99.272  1.00 76.63  ? 452 VAL A CA  1 
ATOM 2961 C C   . VAL A 1 452 ? 124.968 97.183  99.908  1.00 78.95  ? 452 VAL A C   1 
ATOM 2962 O O   . VAL A 1 452 ? 126.127 97.110  99.482  1.00 78.94  ? 452 VAL A O   1 
ATOM 2963 C CB  . VAL A 1 452 ? 123.110 97.165  98.179  1.00 78.64  ? 452 VAL A CB  1 
ATOM 2964 C CG1 . VAL A 1 452 ? 124.094 97.711  97.157  1.00 78.26  ? 452 VAL A CG1 1 
ATOM 2965 C CG2 . VAL A 1 452 ? 122.062 96.298  97.503  1.00 79.32  ? 452 VAL A CG2 1 
ATOM 2966 N N   . ASN A 1 453 ? 124.644 97.965  100.939 1.00 79.10  ? 453 ASN A N   1 
ATOM 2967 C CA  . ASN A 1 453 ? 125.651 98.753  101.651 1.00 77.74  ? 453 ASN A CA  1 
ATOM 2968 C C   . ASN A 1 453 ? 126.707 97.896  102.346 1.00 80.03  ? 453 ASN A C   1 
ATOM 2969 O O   . ASN A 1 453 ? 127.830 98.363  102.564 1.00 80.46  ? 453 ASN A O   1 
ATOM 2970 C CB  . ASN A 1 453 ? 124.972 99.666  102.672 1.00 76.07  ? 453 ASN A CB  1 
ATOM 2971 C CG  . ASN A 1 453 ? 125.927 100.674 103.278 1.00 78.58  ? 453 ASN A CG  1 
ATOM 2972 O OD1 . ASN A 1 453 ? 126.915 101.064 102.656 1.00 80.69  ? 453 ASN A OD1 1 
ATOM 2973 N ND2 . ASN A 1 453 ? 125.635 101.103 104.501 1.00 79.66  ? 453 ASN A ND2 1 
ATOM 2974 N N   . ALA A 1 454 ? 126.384 96.651  102.696 1.00 87.59  ? 454 ALA A N   1 
ATOM 2975 C CA  . ALA A 1 454 ? 127.346 95.814  103.411 1.00 88.07  ? 454 ALA A CA  1 
ATOM 2976 C C   . ALA A 1 454 ? 128.389 95.187  102.488 1.00 87.28  ? 454 ALA A C   1 
ATOM 2977 O O   . ALA A 1 454 ? 129.590 95.261  102.767 1.00 85.32  ? 454 ALA A O   1 
ATOM 2978 C CB  . ALA A 1 454 ? 126.608 94.725  104.190 1.00 86.02  ? 454 ALA A CB  1 
ATOM 2979 N N   . GLU A 1 455 ? 127.962 94.564  101.390 1.00 91.93  ? 455 GLU A N   1 
ATOM 2980 C CA  . GLU A 1 455 ? 128.887 93.782  100.576 1.00 91.78  ? 455 GLU A CA  1 
ATOM 2981 C C   . GLU A 1 455 ? 129.754 94.625  99.648  1.00 90.66  ? 455 GLU A C   1 
ATOM 2982 O O   . GLU A 1 455 ? 130.781 94.130  99.172  1.00 90.04  ? 455 GLU A O   1 
ATOM 2983 C CB  . GLU A 1 455 ? 128.127 92.742  99.750  1.00 89.83  ? 455 GLU A CB  1 
ATOM 2984 C CG  . GLU A 1 455 ? 127.447 91.670  100.579 1.00 89.32  ? 455 GLU A CG  1 
ATOM 2985 C CD  . GLU A 1 455 ? 126.959 90.510  99.736  1.00 90.29  ? 455 GLU A CD  1 
ATOM 2986 O OE1 . GLU A 1 455 ? 127.779 89.924  98.998  1.00 90.41  ? 455 GLU A OE1 1 
ATOM 2987 O OE2 . GLU A 1 455 ? 125.762 90.172  99.823  1.00 90.89  ? 455 GLU A OE2 1 
ATOM 2988 N N   . LEU A 1 456 ? 129.374 95.873  99.372  1.00 89.31  ? 456 LEU A N   1 
ATOM 2989 C CA  . LEU A 1 456 ? 130.233 96.739  98.571  1.00 89.80  ? 456 LEU A CA  1 
ATOM 2990 C C   . LEU A 1 456 ? 131.461 97.239  99.325  1.00 90.75  ? 456 LEU A C   1 
ATOM 2991 O O   . LEU A 1 456 ? 132.379 97.764  98.686  1.00 90.03  ? 456 LEU A O   1 
ATOM 2992 C CB  . LEU A 1 456 ? 129.432 97.930  98.043  1.00 91.40  ? 456 LEU A CB  1 
ATOM 2993 C CG  . LEU A 1 456 ? 128.357 97.604  97.004  1.00 89.73  ? 456 LEU A CG  1 
ATOM 2994 C CD1 . LEU A 1 456 ? 127.541 98.840  96.675  1.00 88.73  ? 456 LEU A CD1 1 
ATOM 2995 C CD2 . LEU A 1 456 ? 128.984 97.025  95.746  1.00 88.12  ? 456 LEU A CD2 1 
ATOM 2996 N N   . TYR A 1 457 ? 131.511 97.089  100.657 1.00 90.50  ? 457 TYR A N   1 
ATOM 2997 C CA  . TYR A 1 457 ? 132.714 97.466  101.384 1.00 92.08  ? 457 TYR A CA  1 
ATOM 2998 C C   . TYR A 1 457 ? 133.376 96.248  102.016 1.00 93.30  ? 457 TYR A C   1 
ATOM 2999 O O   . TYR A 1 457 ? 132.685 95.372  102.548 1.00 93.04  ? 457 TYR A O   1 
ATOM 3000 C CB  . TYR A 1 457 ? 132.413 98.491  102.485 1.00 91.90  ? 457 TYR A CB  1 
ATOM 3001 C CG  . TYR A 1 457 ? 132.026 99.864  101.985 1.00 94.93  ? 457 TYR A CG  1 
ATOM 3002 C CD1 . TYR A 1 457 ? 132.844 100.559 101.105 1.00 92.74  ? 457 TYR A CD1 1 
ATOM 3003 C CD2 . TYR A 1 457 ? 130.860 100.479 102.421 1.00 93.96  ? 457 TYR A CD2 1 
ATOM 3004 C CE1 . TYR A 1 457 ? 132.491 101.809 100.640 1.00 92.78  ? 457 TYR A CE1 1 
ATOM 3005 C CE2 . TYR A 1 457 ? 130.508 101.737 101.975 1.00 91.33  ? 457 TYR A CE2 1 
ATOM 3006 C CZ  . TYR A 1 457 ? 131.325 102.395 101.082 1.00 92.24  ? 457 TYR A CZ  1 
ATOM 3007 O OH  . TYR A 1 457 ? 130.987 103.656 100.650 1.00 92.13  ? 457 TYR A OH  1 
ATOM 3008 N N   . PRO A 1 458 ? 134.704 96.166  101.976 1.00 98.91  ? 458 PRO A N   1 
ATOM 3009 C CA  . PRO A 1 458 ? 135.401 95.102  102.702 1.00 97.92  ? 458 PRO A CA  1 
ATOM 3010 C C   . PRO A 1 458 ? 135.385 95.327  104.208 1.00 98.42  ? 458 PRO A C   1 
ATOM 3011 O O   . PRO A 1 458 ? 135.234 96.445  104.706 1.00 95.82  ? 458 PRO A O   1 
ATOM 3012 C CB  . PRO A 1 458 ? 136.825 95.169  102.141 1.00 95.18  ? 458 PRO A CB  1 
ATOM 3013 C CG  . PRO A 1 458 ? 137.001 96.598  101.775 1.00 96.56  ? 458 PRO A CG  1 
ATOM 3014 C CD  . PRO A 1 458 ? 135.643 97.068  101.289 1.00 96.74  ? 458 PRO A CD  1 
ATOM 3015 N N   . THR A 1 459 ? 135.539 94.214  104.932 1.00 101.24 ? 459 THR A N   1 
ATOM 3016 C CA  . THR A 1 459 ? 135.391 94.209  106.386 1.00 100.98 ? 459 THR A CA  1 
ATOM 3017 C C   . THR A 1 459 ? 136.389 95.138  107.074 1.00 99.58  ? 459 THR A C   1 
ATOM 3018 O O   . THR A 1 459 ? 136.108 95.654  108.163 1.00 99.03  ? 459 THR A O   1 
ATOM 3019 C CB  . THR A 1 459 ? 135.541 92.777  106.908 1.00 101.25 ? 459 THR A CB  1 
ATOM 3020 O OG1 . THR A 1 459 ? 134.564 91.937  106.281 1.00 99.13  ? 459 THR A OG1 1 
ATOM 3021 C CG2 . THR A 1 459 ? 135.340 92.716  108.416 1.00 100.24 ? 459 THR A CG2 1 
ATOM 3022 N N   . PHE A 1 460 ? 137.542 95.387  106.448 1.00 97.62  ? 460 PHE A N   1 
ATOM 3023 C CA  . PHE A 1 460 ? 138.512 96.318  107.020 1.00 98.64  ? 460 PHE A CA  1 
ATOM 3024 C C   . PHE A 1 460 ? 137.964 97.736  107.134 1.00 97.88  ? 460 PHE A C   1 
ATOM 3025 O O   . PHE A 1 460 ? 138.328 98.464  108.065 1.00 97.51  ? 460 PHE A O   1 
ATOM 3026 C CB  . PHE A 1 460 ? 139.787 96.312  106.175 1.00 97.42  ? 460 PHE A CB  1 
ATOM 3027 C CG  . PHE A 1 460 ? 140.910 97.117  106.760 1.00 96.84  ? 460 PHE A CG  1 
ATOM 3028 C CD1 . PHE A 1 460 ? 141.677 96.611  107.795 1.00 96.16  ? 460 PHE A CD1 1 
ATOM 3029 C CD2 . PHE A 1 460 ? 141.205 98.378  106.269 1.00 97.18  ? 460 PHE A CD2 1 
ATOM 3030 C CE1 . PHE A 1 460 ? 142.713 97.347  108.332 1.00 97.34  ? 460 PHE A CE1 1 
ATOM 3031 C CE2 . PHE A 1 460 ? 142.240 99.119  106.802 1.00 96.76  ? 460 PHE A CE2 1 
ATOM 3032 C CZ  . PHE A 1 460 ? 142.995 98.602  107.834 1.00 96.56  ? 460 PHE A CZ  1 
ATOM 3033 N N   . VAL A 1 461 ? 137.099 98.149  106.213 1.00 96.34  ? 461 VAL A N   1 
ATOM 3034 C CA  . VAL A 1 461 ? 136.572 99.508  106.216 1.00 97.48  ? 461 VAL A CA  1 
ATOM 3035 C C   . VAL A 1 461 ? 135.077 99.563  106.504 1.00 96.28  ? 461 VAL A C   1 
ATOM 3036 O O   . VAL A 1 461 ? 134.563 100.655 106.795 1.00 97.46  ? 461 VAL A O   1 
ATOM 3037 C CB  . VAL A 1 461 ? 136.884 100.233 104.891 1.00 98.25  ? 461 VAL A CB  1 
ATOM 3038 C CG1 . VAL A 1 461 ? 138.368 100.137 104.568 1.00 95.49  ? 461 VAL A CG1 1 
ATOM 3039 C CG2 . VAL A 1 461 ? 136.046 99.662  103.763 1.00 97.21  ? 461 VAL A CG2 1 
ATOM 3040 N N   . ARG A 1 462 ? 134.365 98.436  106.416 1.00 92.42  ? 462 ARG A N   1 
ATOM 3041 C CA  . ARG A 1 462 ? 132.907 98.433  106.510 1.00 96.37  ? 462 ARG A CA  1 
ATOM 3042 C C   . ARG A 1 462 ? 132.395 99.124  107.769 1.00 94.75  ? 462 ARG A C   1 
ATOM 3043 O O   . ARG A 1 462 ? 131.404 99.862  107.719 1.00 94.32  ? 462 ARG A O   1 
ATOM 3044 C CB  . ARG A 1 462 ? 132.393 96.994  106.449 1.00 95.77  ? 462 ARG A CB  1 
ATOM 3045 C CG  . ARG A 1 462 ? 130.890 96.872  106.294 1.00 93.96  ? 462 ARG A CG  1 
ATOM 3046 C CD  . ARG A 1 462 ? 130.467 95.414  106.269 1.00 95.68  ? 462 ARG A CD  1 
ATOM 3047 N NE  . ARG A 1 462 ? 131.092 94.689  105.169 1.00 96.17  ? 462 ARG A NE  1 
ATOM 3048 C CZ  . ARG A 1 462 ? 131.927 93.670  105.321 1.00 94.90  ? 462 ARG A CZ  1 
ATOM 3049 N NH1 . ARG A 1 462 ? 132.162 93.142  106.511 1.00 94.38  ? 462 ARG A NH1 1 
ATOM 3050 N NH2 . ARG A 1 462 ? 132.509 93.143  104.248 1.00 94.55  ? 462 ARG A NH2 1 
ATOM 3051 N N   . ASN A 1 463 ? 133.077 98.927  108.902 1.00 89.38  ? 463 ASN A N   1 
ATOM 3052 C CA  . ASN A 1 463 ? 132.638 99.554  110.146 1.00 90.37  ? 463 ASN A CA  1 
ATOM 3053 C C   . ASN A 1 463 ? 132.675 101.074 110.065 1.00 91.60  ? 463 ASN A C   1 
ATOM 3054 O O   . ASN A 1 463 ? 131.858 101.748 110.703 1.00 92.26  ? 463 ASN A O   1 
ATOM 3055 C CB  . ASN A 1 463 ? 133.500 99.065  111.311 1.00 92.92  ? 463 ASN A CB  1 
ATOM 3056 C CG  . ASN A 1 463 ? 132.976 99.525  112.657 1.00 93.27  ? 463 ASN A CG  1 
ATOM 3057 O OD1 . ASN A 1 463 ? 131.794 99.367  112.962 1.00 92.59  ? 463 ASN A OD1 1 
ATOM 3058 N ND2 . ASN A 1 463 ? 133.856 100.093 113.474 1.00 91.56  ? 463 ASN A ND2 1 
ATOM 3059 N N   . LEU A 1 464 ? 133.607 101.633 109.296 1.00 90.85  ? 464 LEU A N   1 
ATOM 3060 C CA  . LEU A 1 464 ? 133.655 103.074 109.086 1.00 89.61  ? 464 LEU A CA  1 
ATOM 3061 C C   . LEU A 1 464 ? 132.739 103.495 107.940 1.00 89.16  ? 464 LEU A C   1 
ATOM 3062 O O   . LEU A 1 464 ? 131.978 104.460 108.067 1.00 88.91  ? 464 LEU A O   1 
ATOM 3063 C CB  . LEU A 1 464 ? 135.097 103.512 108.814 1.00 90.91  ? 464 LEU A CB  1 
ATOM 3064 C CG  . LEU A 1 464 ? 135.336 104.971 108.428 1.00 91.07  ? 464 LEU A CG  1 
ATOM 3065 C CD1 . LEU A 1 464 ? 134.893 105.893 109.548 1.00 90.86  ? 464 LEU A CD1 1 
ATOM 3066 C CD2 . LEU A 1 464 ? 136.800 105.198 108.094 1.00 90.18  ? 464 LEU A CD2 1 
ATOM 3067 N N   . GLY A 1 465 ? 132.828 102.784 106.815 1.00 87.26  ? 465 GLY A N   1 
ATOM 3068 C CA  . GLY A 1 465 ? 132.067 103.151 105.631 1.00 87.52  ? 465 GLY A CA  1 
ATOM 3069 C C   . GLY A 1 465 ? 130.563 103.163 105.842 1.00 88.66  ? 465 GLY A C   1 
ATOM 3070 O O   . GLY A 1 465 ? 129.856 103.996 105.270 1.00 87.58  ? 465 GLY A O   1 
ATOM 3071 N N   . VAL A 1 466 ? 130.052 102.239 106.661 1.00 86.34  ? 466 VAL A N   1 
ATOM 3072 C CA  . VAL A 1 466 ? 128.636 102.274 107.027 1.00 86.41  ? 466 VAL A CA  1 
ATOM 3073 C C   . VAL A 1 466 ? 128.293 103.542 107.801 1.00 87.57  ? 466 VAL A C   1 
ATOM 3074 O O   . VAL A 1 466 ? 127.246 104.158 107.569 1.00 88.12  ? 466 VAL A O   1 
ATOM 3075 C CB  . VAL A 1 466 ? 128.259 101.007 107.816 1.00 86.37  ? 466 VAL A CB  1 
ATOM 3076 C CG1 . VAL A 1 466 ? 126.861 101.136 108.397 1.00 84.77  ? 466 VAL A CG1 1 
ATOM 3077 C CG2 . VAL A 1 466 ? 128.339 99.787  106.915 1.00 86.21  ? 466 VAL A CG2 1 
ATOM 3078 N N   . MET A 1 467 ? 129.162 103.961 108.719 1.00 85.50  ? 467 MET A N   1 
ATOM 3079 C CA  . MET A 1 467 ? 128.923 105.211 109.438 1.00 83.62  ? 467 MET A CA  1 
ATOM 3080 C C   . MET A 1 467 ? 128.943 106.412 108.497 1.00 84.81  ? 467 MET A C   1 
ATOM 3081 O O   . MET A 1 467 ? 128.104 107.313 108.607 1.00 87.10  ? 467 MET A O   1 
ATOM 3082 C CB  . MET A 1 467 ? 129.960 105.383 110.546 1.00 84.10  ? 467 MET A CB  1 
ATOM 3083 C CG  . MET A 1 467 ? 129.791 106.651 111.363 1.00 85.00  ? 467 MET A CG  1 
ATOM 3084 S SD  . MET A 1 467 ? 131.301 107.124 112.226 1.00 95.49  ? 467 MET A SD  1 
ATOM 3085 C CE  . MET A 1 467 ? 132.176 107.984 110.923 1.00 85.82  ? 467 MET A CE  1 
ATOM 3086 N N   . VAL A 1 468 ? 129.903 106.440 107.573 1.00 81.78  ? 468 VAL A N   1 
ATOM 3087 C CA  . VAL A 1 468 ? 130.060 107.570 106.657 1.00 78.50  ? 468 VAL A CA  1 
ATOM 3088 C C   . VAL A 1 468 ? 128.831 107.736 105.765 1.00 79.30  ? 468 VAL A C   1 
ATOM 3089 O O   . VAL A 1 468 ? 128.175 108.784 105.768 1.00 80.46  ? 468 VAL A O   1 
ATOM 3090 C CB  . VAL A 1 468 ? 131.339 107.403 105.819 1.00 78.18  ? 468 VAL A CB  1 
ATOM 3091 C CG1 . VAL A 1 468 ? 131.386 108.436 104.712 1.00 76.07  ? 468 VAL A CG1 1 
ATOM 3092 C CG2 . VAL A 1 468 ? 132.566 107.510 106.706 1.00 82.39  ? 468 VAL A CG2 1 
ATOM 3093 N N   . CYS A 1 469 ? 128.505 106.701 104.987 1.00 78.41  ? 469 CYS A N   1 
ATOM 3094 C CA  . CYS A 1 469 ? 127.385 106.772 104.046 1.00 76.99  ? 469 CYS A CA  1 
ATOM 3095 C C   . CYS A 1 469 ? 126.032 106.937 104.735 1.00 74.62  ? 469 CYS A C   1 
ATOM 3096 O O   . CYS A 1 469 ? 125.162 107.649 104.224 1.00 74.49  ? 469 CYS A O   1 
ATOM 3097 C CB  . CYS A 1 469 ? 127.375 105.529 103.158 1.00 70.77  ? 469 CYS A CB  1 
ATOM 3098 S SG  . CYS A 1 469 ? 128.764 105.424 102.007 1.00 77.41  ? 469 CYS A SG  1 
ATOM 3099 N N   . SER A 1 470 ? 125.824 106.293 105.884 1.00 68.63  ? 470 SER A N   1 
ATOM 3100 C CA  . SER A 1 470 ? 124.538 106.428 106.565 1.00 67.47  ? 470 SER A CA  1 
ATOM 3101 C C   . SER A 1 470 ? 124.334 107.795 107.210 1.00 71.13  ? 470 SER A C   1 
ATOM 3102 O O   . SER A 1 470 ? 123.185 108.173 107.462 1.00 72.76  ? 470 SER A O   1 
ATOM 3103 C CB  . SER A 1 470 ? 124.382 105.339 107.627 1.00 70.23  ? 470 SER A CB  1 
ATOM 3104 O OG  . SER A 1 470 ? 125.290 105.535 108.697 1.00 71.53  ? 470 SER A OG  1 
ATOM 3105 N N   . SER A 1 471 ? 125.405 108.538 107.495 1.00 67.32  ? 471 SER A N   1 
ATOM 3106 C CA  . SER A 1 471 ? 125.257 109.877 108.061 1.00 66.83  ? 471 SER A CA  1 
ATOM 3107 C C   . SER A 1 471 ? 124.530 110.851 107.136 1.00 71.70  ? 471 SER A C   1 
ATOM 3108 O O   . SER A 1 471 ? 124.002 111.858 107.619 1.00 73.06  ? 471 SER A O   1 
ATOM 3109 C CB  . SER A 1 471 ? 126.626 110.447 108.430 1.00 66.96  ? 471 SER A CB  1 
ATOM 3110 O OG  . SER A 1 471 ? 127.198 109.734 109.512 1.00 71.48  ? 471 SER A OG  1 
ATOM 3111 N N   . LEU A 1 472 ? 124.497 110.590 105.826 1.00 59.26  ? 472 LEU A N   1 
ATOM 3112 C CA  . LEU A 1 472 ? 123.723 111.441 104.922 1.00 55.87  ? 472 LEU A CA  1 
ATOM 3113 C C   . LEU A 1 472 ? 122.230 111.406 105.234 1.00 55.18  ? 472 LEU A C   1 
ATOM 3114 O O   . LEU A 1 472 ? 121.514 112.378 104.953 1.00 55.53  ? 472 LEU A O   1 
ATOM 3115 C CB  . LEU A 1 472 ? 123.965 111.023 103.470 1.00 55.40  ? 472 LEU A CB  1 
ATOM 3116 C CG  . LEU A 1 472 ? 125.204 111.547 102.732 1.00 58.96  ? 472 LEU A CG  1 
ATOM 3117 C CD1 . LEU A 1 472 ? 125.150 113.060 102.580 1.00 56.71  ? 472 LEU A CD1 1 
ATOM 3118 C CD2 . LEU A 1 472 ? 126.502 111.112 103.400 1.00 59.73  ? 472 LEU A CD2 1 
ATOM 3119 N N   . CYS A 1 473 ? 121.744 110.302 105.808 1.00 50.56  ? 473 CYS A N   1 
ATOM 3120 C CA  . CYS A 1 473 ? 120.367 110.244 106.290 1.00 49.83  ? 473 CYS A CA  1 
ATOM 3121 C C   . CYS A 1 473 ? 120.051 111.376 107.259 1.00 56.37  ? 473 CYS A C   1 
ATOM 3122 O O   . CYS A 1 473 ? 118.938 111.916 107.247 1.00 58.08  ? 473 CYS A O   1 
ATOM 3123 C CB  . CYS A 1 473 ? 120.110 108.890 106.954 1.00 54.48  ? 473 CYS A CB  1 
ATOM 3124 S SG  . CYS A 1 473 ? 118.431 108.648 107.572 1.00 75.37  ? 473 CYS A SG  1 
ATOM 3125 N N   . ASP A 1 474 ? 121.038 111.814 108.042 1.00 54.10  ? 474 ASP A N   1 
ATOM 3126 C CA  . ASP A 1 474 ? 120.773 112.829 109.054 1.00 49.05  ? 474 ASP A CA  1 
ATOM 3127 C C   . ASP A 1 474 ? 120.697 114.221 108.442 1.00 53.60  ? 474 ASP A C   1 
ATOM 3128 O O   . ASP A 1 474 ? 119.854 115.029 108.845 1.00 59.39  ? 474 ASP A O   1 
ATOM 3129 C CB  . ASP A 1 474 ? 121.847 112.775 110.140 1.00 55.01  ? 474 ASP A CB  1 
ATOM 3130 C CG  . ASP A 1 474 ? 121.877 111.441 110.860 1.00 59.25  ? 474 ASP A CG  1 
ATOM 3131 O OD1 . ASP A 1 474 ? 120.855 110.727 110.827 1.00 55.94  ? 474 ASP A OD1 1 
ATOM 3132 O OD2 . ASP A 1 474 ? 122.920 111.106 111.458 1.00 60.82  ? 474 ASP A OD2 1 
ATOM 3133 N N   . ILE A 1 475 ? 121.542 114.517 107.454 1.00 51.02  ? 475 ILE A N   1 
ATOM 3134 C CA  . ILE A 1 475 ? 121.433 115.811 106.789 1.00 53.07  ? 475 ILE A CA  1 
ATOM 3135 C C   . ILE A 1 475 ? 120.160 115.864 105.953 1.00 51.69  ? 475 ILE A C   1 
ATOM 3136 O O   . ILE A 1 475 ? 119.502 116.914 105.867 1.00 48.23  ? 475 ILE A O   1 
ATOM 3137 C CB  . ILE A 1 475 ? 122.691 116.079 105.943 1.00 48.81  ? 475 ILE A CB  1 
ATOM 3138 C CG1 . ILE A 1 475 ? 123.921 116.167 106.847 1.00 52.60  ? 475 ILE A CG1 1 
ATOM 3139 C CG2 . ILE A 1 475 ? 122.537 117.354 105.136 1.00 47.48  ? 475 ILE A CG2 1 
ATOM 3140 C CD1 . ILE A 1 475 ? 125.230 116.187 106.100 1.00 55.01  ? 475 ILE A CD1 1 
ATOM 3141 N N   . GLY A 1 476 ? 119.765 114.734 105.361 1.00 45.78  ? 476 GLY A N   1 
ATOM 3142 C CA  . GLY A 1 476 ? 118.479 114.686 104.686 1.00 43.74  ? 476 GLY A CA  1 
ATOM 3143 C C   . GLY A 1 476 ? 117.321 114.943 105.630 1.00 48.48  ? 476 GLY A C   1 
ATOM 3144 O O   . GLY A 1 476 ? 116.370 115.649 105.285 1.00 53.43  ? 476 GLY A O   1 
ATOM 3145 N N   . GLY A 1 477 ? 117.388 114.381 106.840 1.00 45.54  ? 477 GLY A N   1 
ATOM 3146 C CA  . GLY A 1 477 ? 116.342 114.628 107.817 1.00 44.17  ? 477 GLY A CA  1 
ATOM 3147 C C   . GLY A 1 477 ? 116.338 116.045 108.357 1.00 44.26  ? 477 GLY A C   1 
ATOM 3148 O O   . GLY A 1 477 ? 115.288 116.553 108.758 1.00 48.18  ? 477 GLY A O   1 
ATOM 3149 N N   . ILE A 1 478 ? 117.505 116.688 108.406 1.00 36.47  ? 478 ILE A N   1 
ATOM 3150 C CA  . ILE A 1 478 ? 117.562 118.096 108.795 1.00 43.61  ? 478 ILE A CA  1 
ATOM 3151 C C   . ILE A 1 478 ? 116.924 118.983 107.731 1.00 49.54  ? 478 ILE A C   1 
ATOM 3152 O O   . ILE A 1 478 ? 116.181 119.920 108.048 1.00 45.95  ? 478 ILE A O   1 
ATOM 3153 C CB  . ILE A 1 478 ? 119.015 118.526 109.074 1.00 41.49  ? 478 ILE A CB  1 
ATOM 3154 C CG1 . ILE A 1 478 ? 119.598 117.772 110.265 1.00 46.84  ? 478 ILE A CG1 1 
ATOM 3155 C CG2 . ILE A 1 478 ? 119.096 120.020 109.325 1.00 41.89  ? 478 ILE A CG2 1 
ATOM 3156 C CD1 . ILE A 1 478 ? 121.082 117.998 110.452 1.00 38.18  ? 478 ILE A CD1 1 
ATOM 3157 N N   . ILE A 1 479 ? 117.192 118.698 106.456 1.00 52.98  ? 479 ILE A N   1 
ATOM 3158 C CA  . ILE A 1 479 ? 116.698 119.557 105.379 1.00 47.94  ? 479 ILE A CA  1 
ATOM 3159 C C   . ILE A 1 479 ? 115.219 119.318 105.070 1.00 45.32  ? 479 ILE A C   1 
ATOM 3160 O O   . ILE A 1 479 ? 114.486 120.262 104.754 1.00 47.10  ? 479 ILE A O   1 
ATOM 3161 C CB  . ILE A 1 479 ? 117.583 119.373 104.132 1.00 50.43  ? 479 ILE A CB  1 
ATOM 3162 C CG1 . ILE A 1 479 ? 118.953 120.010 104.364 1.00 50.12  ? 479 ILE A CG1 1 
ATOM 3163 C CG2 . ILE A 1 479 ? 116.932 119.974 102.901 1.00 52.05  ? 479 ILE A CG2 1 
ATOM 3164 C CD1 . ILE A 1 479 ? 119.977 119.654 103.313 1.00 51.62  ? 479 ILE A CD1 1 
ATOM 3165 N N   . THR A 1 480 ? 114.751 118.075 105.171 1.00 46.96  ? 480 THR A N   1 
ATOM 3166 C CA  . THR A 1 480 ? 113.395 117.731 104.737 1.00 46.12  ? 480 THR A CA  1 
ATOM 3167 C C   . THR A 1 480 ? 112.253 118.570 105.322 1.00 47.02  ? 480 THR A C   1 
ATOM 3168 O O   . THR A 1 480 ? 111.352 118.940 104.550 1.00 42.69  ? 480 THR A O   1 
ATOM 3169 C CB  . THR A 1 480 ? 113.149 116.242 105.032 1.00 48.75  ? 480 THR A CB  1 
ATOM 3170 O OG1 . THR A 1 480 ? 114.101 115.449 104.315 1.00 57.18  ? 480 THR A OG1 1 
ATOM 3171 C CG2 . THR A 1 480 ? 111.747 115.832 104.611 1.00 46.13  ? 480 THR A CG2 1 
ATOM 3172 N N   . PRO A 1 481 ? 112.209 118.905 106.620 1.00 50.83  ? 481 PRO A N   1 
ATOM 3173 C CA  . PRO A 1 481 ? 111.037 119.643 107.136 1.00 48.68  ? 481 PRO A CA  1 
ATOM 3174 C C   . PRO A 1 481 ? 110.798 121.009 106.507 1.00 48.16  ? 481 PRO A C   1 
ATOM 3175 O O   . PRO A 1 481 ? 109.640 121.387 106.273 1.00 42.16  ? 481 PRO A O   1 
ATOM 3176 C CB  . PRO A 1 481 ? 111.345 119.770 108.636 1.00 46.34  ? 481 PRO A CB  1 
ATOM 3177 C CG  . PRO A 1 481 ? 112.233 118.633 108.933 1.00 45.03  ? 481 PRO A CG  1 
ATOM 3178 C CD  . PRO A 1 481 ? 113.103 118.505 107.718 1.00 43.75  ? 481 PRO A CD  1 
ATOM 3179 N N   . PHE A 1 482 ? 111.862 121.750 106.198 1.00 46.56  ? 482 PHE A N   1 
ATOM 3180 C CA  . PHE A 1 482 ? 111.711 123.053 105.559 1.00 42.45  ? 482 PHE A CA  1 
ATOM 3181 C C   . PHE A 1 482 ? 111.215 122.947 104.123 1.00 49.22  ? 482 PHE A C   1 
ATOM 3182 O O   . PHE A 1 482 ? 110.461 123.814 103.671 1.00 51.82  ? 482 PHE A O   1 
ATOM 3183 C CB  . PHE A 1 482 ? 113.036 123.812 105.617 1.00 46.19  ? 482 PHE A CB  1 
ATOM 3184 C CG  . PHE A 1 482 ? 113.466 124.166 107.013 1.00 50.13  ? 482 PHE A CG  1 
ATOM 3185 C CD1 . PHE A 1 482 ? 112.865 125.213 107.692 1.00 49.30  ? 482 PHE A CD1 1 
ATOM 3186 C CD2 . PHE A 1 482 ? 114.456 123.443 107.653 1.00 51.45  ? 482 PHE A CD2 1 
ATOM 3187 C CE1 . PHE A 1 482 ? 113.253 125.538 108.976 1.00 47.97  ? 482 PHE A CE1 1 
ATOM 3188 C CE2 . PHE A 1 482 ? 114.846 123.764 108.939 1.00 43.99  ? 482 PHE A CE2 1 
ATOM 3189 C CZ  . PHE A 1 482 ? 114.244 124.812 109.601 1.00 40.83  ? 482 PHE A CZ  1 
ATOM 3190 N N   . ILE A 1 483 ? 111.578 121.883 103.410 1.00 51.10  ? 483 ILE A N   1 
ATOM 3191 C CA  . ILE A 1 483 ? 111.021 121.653 102.078 1.00 47.28  ? 483 ILE A CA  1 
ATOM 3192 C C   . ILE A 1 483 ? 109.516 121.419 102.159 1.00 49.92  ? 483 ILE A C   1 
ATOM 3193 O O   . ILE A 1 483 ? 108.728 122.092 101.487 1.00 49.79  ? 483 ILE A O   1 
ATOM 3194 C CB  . ILE A 1 483 ? 111.735 120.479 101.388 1.00 53.96  ? 483 ILE A CB  1 
ATOM 3195 C CG1 . ILE A 1 483 ? 113.199 120.829 101.114 1.00 48.50  ? 483 ILE A CG1 1 
ATOM 3196 C CG2 . ILE A 1 483 ? 111.018 120.104 100.099 1.00 53.49  ? 483 ILE A CG2 1 
ATOM 3197 C CD1 . ILE A 1 483 ? 114.026 119.661 100.631 1.00 45.29  ? 483 ILE A CD1 1 
ATOM 3198 N N   . VAL A 1 484 ? 109.096 120.453 102.976 1.00 48.25  ? 484 VAL A N   1 
ATOM 3199 C CA  . VAL A 1 484 ? 107.678 120.108 103.049 1.00 44.47  ? 484 VAL A CA  1 
ATOM 3200 C C   . VAL A 1 484 ? 106.842 121.288 103.540 1.00 50.16  ? 484 VAL A C   1 
ATOM 3201 O O   . VAL A 1 484 ? 105.779 121.579 102.979 1.00 49.28  ? 484 VAL A O   1 
ATOM 3202 C CB  . VAL A 1 484 ? 107.475 118.865 103.933 1.00 44.55  ? 484 VAL A CB  1 
ATOM 3203 C CG1 . VAL A 1 484 ? 105.998 118.546 104.060 1.00 41.09  ? 484 VAL A CG1 1 
ATOM 3204 C CG2 . VAL A 1 484 ? 108.223 117.680 103.357 1.00 45.37  ? 484 VAL A CG2 1 
ATOM 3205 N N   . PHE A 1 485 ? 107.296 121.989 104.583 1.00 51.26  ? 485 PHE A N   1 
ATOM 3206 C CA  . PHE A 1 485 ? 106.437 123.026 105.155 1.00 44.80  ? 485 PHE A CA  1 
ATOM 3207 C C   . PHE A 1 485 ? 106.584 124.409 104.518 1.00 45.77  ? 485 PHE A C   1 
ATOM 3208 O O   . PHE A 1 485 ? 105.576 125.101 104.343 1.00 46.78  ? 485 PHE A O   1 
ATOM 3209 C CB  . PHE A 1 485 ? 106.662 123.124 106.667 1.00 44.41  ? 485 PHE A CB  1 
ATOM 3210 C CG  . PHE A 1 485 ? 106.354 121.853 107.410 1.00 46.95  ? 485 PHE A CG  1 
ATOM 3211 C CD1 . PHE A 1 485 ? 105.125 121.234 107.258 1.00 49.69  ? 485 PHE A CD1 1 
ATOM 3212 C CD2 . PHE A 1 485 ? 107.278 121.288 108.270 1.00 48.14  ? 485 PHE A CD2 1 
ATOM 3213 C CE1 . PHE A 1 485 ? 104.828 120.071 107.941 1.00 49.72  ? 485 PHE A CE1 1 
ATOM 3214 C CE2 . PHE A 1 485 ? 106.987 120.124 108.957 1.00 46.86  ? 485 PHE A CE2 1 
ATOM 3215 C CZ  . PHE A 1 485 ? 105.761 119.516 108.791 1.00 51.38  ? 485 PHE A CZ  1 
ATOM 3216 N N   . ARG A 1 486 ? 107.792 124.847 104.157 1.00 43.58  ? 486 ARG A N   1 
ATOM 3217 C CA  . ARG A 1 486 ? 107.919 126.169 103.547 1.00 43.26  ? 486 ARG A CA  1 
ATOM 3218 C C   . ARG A 1 486 ? 107.549 126.146 102.069 1.00 50.71  ? 486 ARG A C   1 
ATOM 3219 O O   . ARG A 1 486 ? 106.742 126.962 101.610 1.00 57.76  ? 486 ARG A O   1 
ATOM 3220 C CB  . ARG A 1 486 ? 109.343 126.698 103.728 1.00 47.14  ? 486 ARG A CB  1 
ATOM 3221 C CG  . ARG A 1 486 ? 109.819 126.807 105.171 1.00 50.29  ? 486 ARG A CG  1 
ATOM 3222 C CD  . ARG A 1 486 ? 108.893 127.678 106.011 1.00 45.52  ? 486 ARG A CD  1 
ATOM 3223 N NE  . ARG A 1 486 ? 108.053 126.909 106.918 1.00 41.15  ? 486 ARG A NE  1 
ATOM 3224 C CZ  . ARG A 1 486 ? 106.776 127.175 107.158 1.00 48.31  ? 486 ARG A CZ  1 
ATOM 3225 N NH1 . ARG A 1 486 ? 106.163 128.195 106.583 1.00 43.36  ? 486 ARG A NH1 1 
ATOM 3226 N NH2 . ARG A 1 486 ? 106.100 126.399 108.000 1.00 48.67  ? 486 ARG A NH2 1 
ATOM 3227 N N   . LEU A 1 487 ? 108.142 125.223 101.309 1.00 61.29  ? 487 LEU A N   1 
ATOM 3228 C CA  . LEU A 1 487 ? 108.024 125.244 99.853  1.00 56.84  ? 487 LEU A CA  1 
ATOM 3229 C C   . LEU A 1 487 ? 106.588 125.010 99.398  1.00 53.94  ? 487 LEU A C   1 
ATOM 3230 O O   . LEU A 1 487 ? 106.184 125.498 98.338  1.00 56.00  ? 487 LEU A O   1 
ATOM 3231 C CB  . LEU A 1 487 ? 108.958 124.199 99.246  1.00 54.44  ? 487 LEU A CB  1 
ATOM 3232 C CG  . LEU A 1 487 ? 109.266 124.314 97.759  1.00 56.86  ? 487 LEU A CG  1 
ATOM 3233 C CD1 . LEU A 1 487 ? 109.927 125.650 97.481  1.00 58.60  ? 487 LEU A CD1 1 
ATOM 3234 C CD2 . LEU A 1 487 ? 110.160 123.169 97.318  1.00 56.23  ? 487 LEU A CD2 1 
ATOM 3235 N N   . ARG A 1 488 ? 105.816 124.258 100.185 1.00 58.29  ? 488 ARG A N   1 
ATOM 3236 C CA  . ARG A 1 488 ? 104.384 124.093 99.947  1.00 58.59  ? 488 ARG A CA  1 
ATOM 3237 C C   . ARG A 1 488 ? 103.635 125.421 99.892  1.00 60.28  ? 488 ARG A C   1 
ATOM 3238 O O   . ARG A 1 488 ? 102.620 125.525 99.195  1.00 64.62  ? 488 ARG A O   1 
ATOM 3239 C CB  . ARG A 1 488 ? 103.792 123.195 101.034 1.00 58.72  ? 488 ARG A CB  1 
ATOM 3240 C CG  . ARG A 1 488 ? 102.301 122.940 100.924 1.00 66.04  ? 488 ARG A CG  1 
ATOM 3241 C CD  . ARG A 1 488 ? 101.844 121.945 101.982 1.00 65.68  ? 488 ARG A CD  1 
ATOM 3242 N NE  . ARG A 1 488 ? 100.407 121.707 101.933 1.00 66.82  ? 488 ARG A NE  1 
ATOM 3243 C CZ  . ARG A 1 488 ? 99.582  121.894 102.954 1.00 66.75  ? 488 ARG A CZ  1 
ATOM 3244 N NH1 . ARG A 1 488 ? 100.027 122.269 104.143 1.00 63.27  ? 488 ARG A NH1 1 
ATOM 3245 N NH2 . ARG A 1 488 ? 98.281  121.681 102.784 1.00 66.64  ? 488 ARG A NH2 1 
ATOM 3246 N N   . GLU A 1 489 ? 104.112 126.447 100.597 1.00 67.69  ? 489 GLU A N   1 
ATOM 3247 C CA  . GLU A 1 489 ? 103.449 127.744 100.534 1.00 64.38  ? 489 GLU A CA  1 
ATOM 3248 C C   . GLU A 1 489 ? 103.762 128.526 99.264  1.00 64.02  ? 489 GLU A C   1 
ATOM 3249 O O   . GLU A 1 489 ? 103.019 129.456 98.934  1.00 64.05  ? 489 GLU A O   1 
ATOM 3250 C CB  . GLU A 1 489 ? 103.826 128.590 101.752 1.00 64.22  ? 489 GLU A CB  1 
ATOM 3251 C CG  . GLU A 1 489 ? 103.457 127.965 103.086 1.00 65.81  ? 489 GLU A CG  1 
ATOM 3252 C CD  . GLU A 1 489 ? 103.673 128.912 104.250 1.00 71.21  ? 489 GLU A CD  1 
ATOM 3253 O OE1 . GLU A 1 489 ? 104.513 129.827 104.125 1.00 72.33  ? 489 GLU A OE1 1 
ATOM 3254 O OE2 . GLU A 1 489 ? 103.004 128.741 105.291 1.00 71.59  ? 489 GLU A OE2 1 
ATOM 3255 N N   . VAL A 1 490 ? 104.832 128.184 98.545  1.00 67.53  ? 490 VAL A N   1 
ATOM 3256 C CA  . VAL A 1 490 ? 105.049 128.785 97.232  1.00 67.11  ? 490 VAL A CA  1 
ATOM 3257 C C   . VAL A 1 490 ? 104.090 128.185 96.211  1.00 69.04  ? 490 VAL A C   1 
ATOM 3258 O O   . VAL A 1 490 ? 103.457 128.906 95.431  1.00 72.09  ? 490 VAL A O   1 
ATOM 3259 C CB  . VAL A 1 490 ? 106.515 128.615 96.797  1.00 71.05  ? 490 VAL A CB  1 
ATOM 3260 C CG1 . VAL A 1 490 ? 106.771 129.366 95.500  1.00 67.29  ? 490 VAL A CG1 1 
ATOM 3261 C CG2 . VAL A 1 490 ? 107.453 129.095 97.893  1.00 71.84  ? 490 VAL A CG2 1 
ATOM 3262 N N   . TRP A 1 491 ? 103.964 126.857 96.208  1.00 66.28  ? 491 TRP A N   1 
ATOM 3263 C CA  . TRP A 1 491 ? 103.016 126.152 95.352  1.00 65.06  ? 491 TRP A CA  1 
ATOM 3264 C C   . TRP A 1 491 ? 102.882 124.720 95.858  1.00 66.34  ? 491 TRP A C   1 
ATOM 3265 O O   . TRP A 1 491 ? 103.884 124.018 96.030  1.00 67.95  ? 491 TRP A O   1 
ATOM 3266 C CB  . TRP A 1 491 ? 103.470 126.202 93.889  1.00 65.75  ? 491 TRP A CB  1 
ATOM 3267 C CG  . TRP A 1 491 ? 102.607 125.435 92.934  1.00 68.09  ? 491 TRP A CG  1 
ATOM 3268 C CD1 . TRP A 1 491 ? 101.302 125.078 93.107  1.00 65.09  ? 491 TRP A CD1 1 
ATOM 3269 C CD2 . TRP A 1 491 ? 102.980 124.966 91.633  1.00 68.75  ? 491 TRP A CD2 1 
ATOM 3270 N NE1 . TRP A 1 491 ? 100.847 124.396 92.006  1.00 63.58  ? 491 TRP A NE1 1 
ATOM 3271 C CE2 . TRP A 1 491 ? 101.858 124.316 91.085  1.00 68.33  ? 491 TRP A CE2 1 
ATOM 3272 C CE3 . TRP A 1 491 ? 104.158 125.025 90.882  1.00 66.64  ? 491 TRP A CE3 1 
ATOM 3273 C CZ2 . TRP A 1 491 ? 101.878 123.730 89.823  1.00 69.88  ? 491 TRP A CZ2 1 
ATOM 3274 C CZ3 . TRP A 1 491 ? 104.177 124.442 89.630  1.00 67.56  ? 491 TRP A CZ3 1 
ATOM 3275 C CH2 . TRP A 1 491 ? 103.045 123.804 89.112  1.00 68.86  ? 491 TRP A CH2 1 
ATOM 3276 N N   . GLN A 1 492 ? 101.645 124.282 96.097  1.00 65.66  ? 492 GLN A N   1 
ATOM 3277 C CA  . GLN A 1 492 ? 101.391 123.018 96.782  1.00 67.68  ? 492 GLN A CA  1 
ATOM 3278 C C   . GLN A 1 492 ? 101.837 121.778 96.011  1.00 70.21  ? 492 GLN A C   1 
ATOM 3279 O O   . GLN A 1 492 ? 102.045 120.731 96.634  1.00 68.53  ? 492 GLN A O   1 
ATOM 3280 C CB  . GLN A 1 492 ? 99.901  122.900 97.106  1.00 69.34  ? 492 GLN A CB  1 
ATOM 3281 C CG  . GLN A 1 492 ? 99.395  123.956 98.074  1.00 70.26  ? 492 GLN A CG  1 
ATOM 3282 C CD  . GLN A 1 492 ? 97.984  123.679 98.549  1.00 75.15  ? 492 GLN A CD  1 
ATOM 3283 O OE1 . GLN A 1 492 ? 97.342  122.729 98.103  1.00 76.25  ? 492 GLN A OE1 1 
ATOM 3284 N NE2 . GLN A 1 492 ? 97.493  124.510 99.461  1.00 74.27  ? 492 GLN A NE2 1 
ATOM 3285 N N   . ALA A 1 493 ? 101.983 121.850 94.687  1.00 61.26  ? 493 ALA A N   1 
ATOM 3286 C CA  . ALA A 1 493 ? 102.499 120.701 93.950  1.00 58.95  ? 493 ALA A CA  1 
ATOM 3287 C C   . ALA A 1 493 ? 104.014 120.543 94.011  1.00 61.01  ? 493 ALA A C   1 
ATOM 3288 O O   . ALA A 1 493 ? 104.514 119.455 93.708  1.00 63.83  ? 493 ALA A O   1 
ATOM 3289 C CB  . ALA A 1 493 ? 102.064 120.785 92.486  1.00 55.89  ? 493 ALA A CB  1 
ATOM 3290 N N   . LEU A 1 494 ? 104.751 121.583 94.383  1.00 48.27  ? 494 LEU A N   1 
ATOM 3291 C CA  . LEU A 1 494 ? 106.192 121.611 94.144  1.00 44.52  ? 494 LEU A CA  1 
ATOM 3292 C C   . LEU A 1 494 ? 106.999 120.584 94.949  1.00 49.18  ? 494 LEU A C   1 
ATOM 3293 O O   . LEU A 1 494 ? 107.967 120.017 94.415  1.00 53.00  ? 494 LEU A O   1 
ATOM 3294 C CB  . LEU A 1 494 ? 106.717 123.023 94.409  1.00 49.10  ? 494 LEU A CB  1 
ATOM 3295 C CG  . LEU A 1 494 ? 108.146 123.328 93.965  1.00 52.96  ? 494 LEU A CG  1 
ATOM 3296 C CD1 . LEU A 1 494 ? 108.302 123.051 92.483  1.00 54.58  ? 494 LEU A CD1 1 
ATOM 3297 C CD2 . LEU A 1 494 ? 108.483 124.774 94.262  1.00 50.14  ? 494 LEU A CD2 1 
ATOM 3298 N N   . PRO A 1 495 ? 106.625 120.269 96.200  1.00 45.05  ? 495 PRO A N   1 
ATOM 3299 C CA  . PRO A 1 495 ? 107.301 119.149 96.881  1.00 45.28  ? 495 PRO A CA  1 
ATOM 3300 C C   . PRO A 1 495 ? 107.162 117.822 96.160  1.00 49.19  ? 495 PRO A C   1 
ATOM 3301 O O   . PRO A 1 495 ? 108.120 117.039 96.131  1.00 53.26  ? 495 PRO A O   1 
ATOM 3302 C CB  . PRO A 1 495 ? 106.630 119.120 98.263  1.00 40.08  ? 495 PRO A CB  1 
ATOM 3303 C CG  . PRO A 1 495 ? 106.138 120.491 98.468  1.00 43.84  ? 495 PRO A CG  1 
ATOM 3304 C CD  . PRO A 1 495 ? 105.705 120.965 97.117  1.00 40.56  ? 495 PRO A CD  1 
ATOM 3305 N N   . LEU A 1 496 ? 105.986 117.524 95.608  1.00 43.95  ? 496 LEU A N   1 
ATOM 3306 C CA  . LEU A 1 496 ? 105.825 116.274 94.878  1.00 37.27  ? 496 LEU A CA  1 
ATOM 3307 C C   . LEU A 1 496 ? 106.646 116.258 93.594  1.00 36.65  ? 496 LEU A C   1 
ATOM 3308 O O   . LEU A 1 496 ? 107.105 115.193 93.173  1.00 50.82  ? 496 LEU A O   1 
ATOM 3309 C CB  . LEU A 1 496 ? 104.348 116.038 94.567  1.00 44.18  ? 496 LEU A CB  1 
ATOM 3310 C CG  . LEU A 1 496 ? 103.434 115.777 95.764  1.00 41.23  ? 496 LEU A CG  1 
ATOM 3311 C CD1 . LEU A 1 496 ? 101.986 115.691 95.319  1.00 36.23  ? 496 LEU A CD1 1 
ATOM 3312 C CD2 . LEU A 1 496 ? 103.848 114.507 96.487  1.00 40.40  ? 496 LEU A CD2 1 
ATOM 3313 N N   . ILE A 1 497 ? 106.886 117.424 92.990  1.00 31.31  ? 497 ILE A N   1 
ATOM 3314 C CA  . ILE A 1 497 ? 107.791 117.506 91.845  1.00 40.57  ? 497 ILE A CA  1 
ATOM 3315 C C   . ILE A 1 497 ? 109.234 117.229 92.257  1.00 37.02  ? 497 ILE A C   1 
ATOM 3316 O O   . ILE A 1 497 ? 109.967 116.511 91.559  1.00 34.43  ? 497 ILE A O   1 
ATOM 3317 C CB  . ILE A 1 497 ? 107.651 118.878 91.159  1.00 34.21  ? 497 ILE A CB  1 
ATOM 3318 C CG1 . ILE A 1 497 ? 106.245 119.046 90.586  1.00 35.13  ? 497 ILE A CG1 1 
ATOM 3319 C CG2 . ILE A 1 497 ? 108.684 119.039 90.060  1.00 38.02  ? 497 ILE A CG2 1 
ATOM 3320 C CD1 . ILE A 1 497 ? 105.951 120.442 90.095  1.00 31.02  ? 497 ILE A CD1 1 
ATOM 3321 N N   . LEU A 1 498 ? 109.642 117.713 93.433  1.00 33.86  ? 498 LEU A N   1 
ATOM 3322 C CA  . LEU A 1 498 ? 110.963 117.343 93.941  1.00 31.25  ? 498 LEU A CA  1 
ATOM 3323 C C   . LEU A 1 498 ? 111.063 115.845 94.204  1.00 33.56  ? 498 LEU A C   1 
ATOM 3324 O O   . LEU A 1 498 ? 112.059 115.210 93.840  1.00 39.40  ? 498 LEU A O   1 
ATOM 3325 C CB  . LEU A 1 498 ? 111.301 118.133 95.206  1.00 36.32  ? 498 LEU A CB  1 
ATOM 3326 C CG  . LEU A 1 498 ? 111.940 119.519 95.061  1.00 43.73  ? 498 LEU A CG  1 
ATOM 3327 C CD1 . LEU A 1 498 ? 110.970 120.570 94.561  1.00 45.90  ? 498 LEU A CD1 1 
ATOM 3328 C CD2 . LEU A 1 498 ? 112.558 119.948 96.384  1.00 41.80  ? 498 LEU A CD2 1 
ATOM 3329 N N   . PHE A 1 499 ? 110.079 115.278 94.901  1.00 31.50  ? 499 PHE A N   1 
ATOM 3330 C CA  . PHE A 1 499 ? 110.121 113.850 95.211  1.00 27.91  ? 499 PHE A CA  1 
ATOM 3331 C C   . PHE A 1 499 ? 110.125 112.994 93.946  1.00 26.50  ? 499 PHE A C   1 
ATOM 3332 O O   . PHE A 1 499 ? 110.859 112.001 93.863  1.00 38.34  ? 499 PHE A O   1 
ATOM 3333 C CB  . PHE A 1 499 ? 108.942 113.463 96.106  1.00 33.48  ? 499 PHE A CB  1 
ATOM 3334 C CG  . PHE A 1 499 ? 108.937 114.137 97.452  1.00 33.96  ? 499 PHE A CG  1 
ATOM 3335 C CD1 . PHE A 1 499 ? 110.039 114.844 97.904  1.00 39.46  ? 499 PHE A CD1 1 
ATOM 3336 C CD2 . PHE A 1 499 ? 107.825 114.051 98.271  1.00 29.72  ? 499 PHE A CD2 1 
ATOM 3337 C CE1 . PHE A 1 499 ? 110.027 115.456 99.143  1.00 37.68  ? 499 PHE A CE1 1 
ATOM 3338 C CE2 . PHE A 1 499 ? 107.807 114.661 99.508  1.00 31.89  ? 499 PHE A CE2 1 
ATOM 3339 C CZ  . PHE A 1 499 ? 108.909 115.364 99.945  1.00 35.18  ? 499 PHE A CZ  1 
ATOM 3340 N N   . ALA A 1 500 ? 109.359 113.398 92.929  1.00 18.51  ? 500 ALA A N   1 
ATOM 3341 C CA  . ALA A 1 500 ? 109.380 112.703 91.645  1.00 15.40  ? 500 ALA A CA  1 
ATOM 3342 C C   . ALA A 1 500 ? 110.750 112.761 90.982  1.00 34.99  ? 500 ALA A C   1 
ATOM 3343 O O   . ALA A 1 500 ? 111.252 111.739 90.497  1.00 35.04  ? 500 ALA A O   1 
ATOM 3344 C CB  . ALA A 1 500 ? 108.318 113.292 90.719  1.00 19.67  ? 500 ALA A CB  1 
ATOM 3345 N N   . VAL A 1 501 ? 111.390 113.933 90.978  1.00 36.99  ? 501 VAL A N   1 
ATOM 3346 C CA  . VAL A 1 501 ? 112.680 114.047 90.300  1.00 23.63  ? 501 VAL A CA  1 
ATOM 3347 C C   . VAL A 1 501 ? 113.759 113.275 91.053  1.00 19.76  ? 501 VAL A C   1 
ATOM 3348 O O   . VAL A 1 501 ? 114.577 112.572 90.444  1.00 23.63  ? 501 VAL A O   1 
ATOM 3349 C CB  . VAL A 1 501 ? 113.060 115.526 90.115  1.00 29.28  ? 501 VAL A CB  1 
ATOM 3350 C CG1 . VAL A 1 501 ? 114.474 115.650 89.574  1.00 28.37  ? 501 VAL A CG1 1 
ATOM 3351 C CG2 . VAL A 1 501 ? 112.079 116.205 89.178  1.00 28.29  ? 501 VAL A CG2 1 
ATOM 3352 N N   . LEU A 1 502 ? 113.775 113.380 92.384  1.00 27.98  ? 502 LEU A N   1 
ATOM 3353 C CA  . LEU A 1 502 ? 114.722 112.603 93.181  1.00 25.14  ? 502 LEU A CA  1 
ATOM 3354 C C   . LEU A 1 502 ? 114.541 111.102 92.975  1.00 32.03  ? 502 LEU A C   1 
ATOM 3355 O O   . LEU A 1 502 ? 115.527 110.374 92.808  1.00 39.91  ? 502 LEU A O   1 
ATOM 3356 C CB  . LEU A 1 502 ? 114.582 112.955 94.661  1.00 30.05  ? 502 LEU A CB  1 
ATOM 3357 C CG  . LEU A 1 502 ? 115.087 114.334 95.087  1.00 31.25  ? 502 LEU A CG  1 
ATOM 3358 C CD1 . LEU A 1 502 ? 114.835 114.561 96.568  1.00 29.99  ? 502 LEU A CD1 1 
ATOM 3359 C CD2 . LEU A 1 502 ? 116.561 114.483 94.762  1.00 33.63  ? 502 LEU A CD2 1 
ATOM 3360 N N   . GLY A 1 503 ? 113.296 110.619 92.965  1.00 32.60  ? 503 GLY A N   1 
ATOM 3361 C CA  . GLY A 1 503 ? 113.079 109.192 92.787  1.00 22.50  ? 503 GLY A CA  1 
ATOM 3362 C C   . GLY A 1 503 ? 113.457 108.704 91.402  1.00 15.83  ? 503 GLY A C   1 
ATOM 3363 O O   . GLY A 1 503 ? 114.057 107.633 91.252  1.00 27.80  ? 503 GLY A O   1 
ATOM 3364 N N   . LEU A 1 504 ? 113.163 109.499 90.373  1.00 21.32  ? 504 LEU A N   1 
ATOM 3365 C CA  . LEU A 1 504 ? 113.485 109.077 89.019  1.00 18.39  ? 504 LEU A CA  1 
ATOM 3366 C C   . LEU A 1 504 ? 114.969 109.204 88.704  1.00 26.00  ? 504 LEU A C   1 
ATOM 3367 O O   . LEU A 1 504 ? 115.448 108.536 87.782  1.00 35.61  ? 504 LEU A O   1 
ATOM 3368 C CB  . LEU A 1 504 ? 112.667 109.883 88.008  1.00 34.67  ? 504 LEU A CB  1 
ATOM 3369 C CG  . LEU A 1 504 ? 111.147 109.690 88.067  1.00 32.37  ? 504 LEU A CG  1 
ATOM 3370 C CD1 . LEU A 1 504 ? 110.431 110.731 87.225  1.00 33.72  ? 504 LEU A CD1 1 
ATOM 3371 C CD2 . LEU A 1 504 ? 110.760 108.297 87.628  1.00 30.03  ? 504 LEU A CD2 1 
ATOM 3372 N N   . LEU A 1 505 ? 115.709 110.042 89.436  1.00 35.60  ? 505 LEU A N   1 
ATOM 3373 C CA  . LEU A 1 505 ? 117.164 110.022 89.305  1.00 32.20  ? 505 LEU A CA  1 
ATOM 3374 C C   . LEU A 1 505 ? 117.795 108.877 90.094  1.00 30.08  ? 505 LEU A C   1 
ATOM 3375 O O   . LEU A 1 505 ? 118.750 108.252 89.623  1.00 22.61  ? 505 LEU A O   1 
ATOM 3376 C CB  . LEU A 1 505 ? 117.756 111.359 89.749  1.00 30.26  ? 505 LEU A CB  1 
ATOM 3377 C CG  . LEU A 1 505 ? 117.630 112.522 88.766  1.00 33.29  ? 505 LEU A CG  1 
ATOM 3378 C CD1 . LEU A 1 505 ? 117.782 113.847 89.484  1.00 37.10  ? 505 LEU A CD1 1 
ATOM 3379 C CD2 . LEU A 1 505 ? 118.666 112.391 87.667  1.00 33.74  ? 505 LEU A CD2 1 
ATOM 3380 N N   . ALA A 1 506 ? 117.286 108.594 91.296  1.00 34.11  ? 506 ALA A N   1 
ATOM 3381 C CA  . ALA A 1 506 ? 117.769 107.447 92.063  1.00 30.94  ? 506 ALA A CA  1 
ATOM 3382 C C   . ALA A 1 506 ? 117.515 106.122 91.353  1.00 35.56  ? 506 ALA A C   1 
ATOM 3383 O O   . ALA A 1 506 ? 118.270 105.163 91.547  1.00 37.83  ? 506 ALA A O   1 
ATOM 3384 C CB  . ALA A 1 506 ? 117.122 107.435 93.447  1.00 30.00  ? 506 ALA A CB  1 
ATOM 3385 N N   . ALA A 1 507 ? 116.459 106.040 90.543  1.00 38.94  ? 507 ALA A N   1 
ATOM 3386 C CA  . ALA A 1 507 ? 116.211 104.824 89.770  1.00 19.25  ? 507 ALA A CA  1 
ATOM 3387 C C   . ALA A 1 507 ? 117.327 104.543 88.765  1.00 25.56  ? 507 ALA A C   1 
ATOM 3388 O O   . ALA A 1 507 ? 117.872 103.435 88.722  1.00 34.42  ? 507 ALA A O   1 
ATOM 3389 C CB  . ALA A 1 507 ? 114.863 104.924 89.059  1.00 25.46  ? 507 ALA A CB  1 
ATOM 3390 N N   . GLY A 1 508 ? 117.675 105.533 87.942  1.00 28.68  ? 508 GLY A N   1 
ATOM 3391 C CA  . GLY A 1 508 ? 118.719 105.334 86.944  1.00 34.59  ? 508 GLY A CA  1 
ATOM 3392 C C   . GLY A 1 508 ? 120.117 105.136 87.509  1.00 40.90  ? 508 GLY A C   1 
ATOM 3393 O O   . GLY A 1 508 ? 120.882 104.308 87.009  1.00 39.03  ? 508 GLY A O   1 
ATOM 3394 N N   . VAL A 1 509 ? 120.475 105.899 88.543  1.00 42.99  ? 509 VAL A N   1 
ATOM 3395 C CA  . VAL A 1 509 ? 121.824 105.843 89.108  1.00 33.93  ? 509 VAL A CA  1 
ATOM 3396 C C   . VAL A 1 509 ? 122.154 104.464 89.671  1.00 40.83  ? 509 VAL A C   1 
ATOM 3397 O O   . VAL A 1 509 ? 123.306 104.017 89.599  1.00 51.20  ? 509 VAL A O   1 
ATOM 3398 C CB  . VAL A 1 509 ? 121.978 106.947 90.176  1.00 41.12  ? 509 VAL A CB  1 
ATOM 3399 C CG1 . VAL A 1 509 ? 123.229 106.734 91.013  1.00 45.47  ? 509 VAL A CG1 1 
ATOM 3400 C CG2 . VAL A 1 509 ? 122.008 108.316 89.518  1.00 45.77  ? 509 VAL A CG2 1 
ATOM 3401 N N   . THR A 1 510 ? 121.159 103.763 90.218  1.00 42.16  ? 510 THR A N   1 
ATOM 3402 C CA  . THR A 1 510 ? 121.375 102.417 90.748  1.00 38.08  ? 510 THR A CA  1 
ATOM 3403 C C   . THR A 1 510 ? 121.987 101.474 89.714  1.00 43.33  ? 510 THR A C   1 
ATOM 3404 O O   . THR A 1 510 ? 122.826 100.633 90.056  1.00 41.17  ? 510 THR A O   1 
ATOM 3405 C CB  . THR A 1 510 ? 120.053 101.852 91.269  1.00 38.98  ? 510 THR A CB  1 
ATOM 3406 O OG1 . THR A 1 510 ? 119.575 102.673 92.340  1.00 50.87  ? 510 THR A OG1 1 
ATOM 3407 C CG2 . THR A 1 510 ? 120.238 100.438 91.784  1.00 39.36  ? 510 THR A CG2 1 
ATOM 3408 N N   . LEU A 1 511 ? 121.601 101.606 88.443  1.00 49.19  ? 511 LEU A N   1 
ATOM 3409 C CA  . LEU A 1 511 ? 122.125 100.719 87.406  1.00 47.79  ? 511 LEU A CA  1 
ATOM 3410 C C   . LEU A 1 511 ? 123.631 100.836 87.201  1.00 46.20  ? 511 LEU A C   1 
ATOM 3411 O O   . LEU A 1 511 ? 124.216 99.958  86.559  1.00 53.16  ? 511 LEU A O   1 
ATOM 3412 C CB  . LEU A 1 511 ? 121.417 100.988 86.077  1.00 41.66  ? 511 LEU A CB  1 
ATOM 3413 C CG  . LEU A 1 511 ? 119.921 100.693 86.013  1.00 41.57  ? 511 LEU A CG  1 
ATOM 3414 C CD1 . LEU A 1 511 ? 119.372 101.067 84.649  1.00 47.14  ? 511 LEU A CD1 1 
ATOM 3415 C CD2 . LEU A 1 511 ? 119.658 99.228  86.310  1.00 40.22  ? 511 LEU A CD2 1 
ATOM 3416 N N   . LEU A 1 512 ? 124.272 101.882 87.716  1.00 52.78  ? 512 LEU A N   1 
ATOM 3417 C CA  . LEU A 1 512 ? 125.713 102.040 87.557  1.00 54.21  ? 512 LEU A CA  1 
ATOM 3418 C C   . LEU A 1 512 ? 126.524 101.264 88.588  1.00 55.23  ? 512 LEU A C   1 
ATOM 3419 O O   . LEU A 1 512 ? 127.748 101.177 88.445  1.00 55.79  ? 512 LEU A O   1 
ATOM 3420 C CB  . LEU A 1 512 ? 126.093 103.522 87.617  1.00 54.02  ? 512 LEU A CB  1 
ATOM 3421 C CG  . LEU A 1 512 ? 125.446 104.422 86.565  1.00 51.97  ? 512 LEU A CG  1 
ATOM 3422 C CD1 . LEU A 1 512 ? 125.859 105.867 86.770  1.00 54.56  ? 512 LEU A CD1 1 
ATOM 3423 C CD2 . LEU A 1 512 ? 125.814 103.952 85.168  1.00 52.29  ? 512 LEU A CD2 1 
ATOM 3424 N N   . LEU A 1 513 ? 125.885 100.702 89.614  1.00 58.23  ? 513 LEU A N   1 
ATOM 3425 C CA  . LEU A 1 513 ? 126.601 99.840  90.541  1.00 61.37  ? 513 LEU A CA  1 
ATOM 3426 C C   . LEU A 1 513 ? 126.833 98.453  89.939  1.00 66.59  ? 513 LEU A C   1 
ATOM 3427 O O   . LEU A 1 513 ? 126.045 97.985  89.113  1.00 65.24  ? 513 LEU A O   1 
ATOM 3428 C CB  . LEU A 1 513 ? 125.824 99.707  91.846  1.00 58.12  ? 513 LEU A CB  1 
ATOM 3429 C CG  . LEU A 1 513 ? 125.685 100.978 92.684  1.00 58.99  ? 513 LEU A CG  1 
ATOM 3430 C CD1 . LEU A 1 513 ? 124.811 100.723 93.898  1.00 61.32  ? 513 LEU A CD1 1 
ATOM 3431 C CD2 . LEU A 1 513 ? 127.053 101.485 93.102  1.00 60.91  ? 513 LEU A CD2 1 
ATOM 3432 N N   . PRO A 1 514 ? 127.911 97.784  90.336  1.00 76.16  ? 514 PRO A N   1 
ATOM 3433 C CA  . PRO A 1 514 ? 128.139 96.403  89.905  1.00 74.13  ? 514 PRO A CA  1 
ATOM 3434 C C   . PRO A 1 514 ? 127.293 95.414  90.698  1.00 74.42  ? 514 PRO A C   1 
ATOM 3435 O O   . PRO A 1 514 ? 126.723 95.728  91.743  1.00 75.57  ? 514 PRO A O   1 
ATOM 3436 C CB  . PRO A 1 514 ? 129.632 96.203  90.177  1.00 74.87  ? 514 PRO A CB  1 
ATOM 3437 C CG  . PRO A 1 514 ? 129.873 97.032  91.389  1.00 74.63  ? 514 PRO A CG  1 
ATOM 3438 C CD  . PRO A 1 514 ? 128.990 98.259  91.220  1.00 73.19  ? 514 PRO A CD  1 
ATOM 3439 N N   . GLU A 1 515 ? 127.226 94.194  90.174  1.00 82.27  ? 515 GLU A N   1 
ATOM 3440 C CA  . GLU A 1 515 ? 126.565 93.092  90.866  1.00 83.47  ? 515 GLU A CA  1 
ATOM 3441 C C   . GLU A 1 515 ? 127.337 91.791  90.682  1.00 82.67  ? 515 GLU A C   1 
ATOM 3442 O O   . GLU A 1 515 ? 127.820 91.493  89.590  1.00 84.03  ? 515 GLU A O   1 
ATOM 3443 C CB  . GLU A 1 515 ? 125.132 92.919  90.361  1.00 81.66  ? 515 GLU A CB  1 
ATOM 3444 C CG  . GLU A 1 515 ? 124.297 91.955  91.188  1.00 82.75  ? 515 GLU A CG  1 
ATOM 3445 C CD  . GLU A 1 515 ? 122.897 91.769  90.633  1.00 85.74  ? 515 GLU A CD  1 
ATOM 3446 O OE1 . GLU A 1 515 ? 122.070 92.694  90.768  1.00 85.62  ? 515 GLU A OE1 1 
ATOM 3447 O OE2 . GLU A 1 515 ? 122.622 90.694  90.060  1.00 86.81  ? 515 GLU A OE2 1 
# 
