data_9J3J
# 
_entry.id   9J3J 
# 
_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   9J3J         pdb_00009j3j 10.2210/pdb9j3j/pdb 
WWPDB D_1300049905 ?            ?                   
EMDB  EMD-61117    ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1  'Structure model' 1 0 2025-03-19 ? 
2  'EM metadata'     1 0 2025-03-19 ? 
3  FSC               1 0 2025-03-19 ? 
4  'Half map'        1 0 2025-03-19 1 
5  'Half map'        1 0 2025-03-19 2 
6  Image             1 0 2025-03-19 ? 
7  Mask              1 0 2025-03-19 1 
8  'Primary map'     1 0 2025-03-19 ? 
9  'Structure model' 1 1 2025-03-26 ? 
10 'Structure model' 1 2 2025-05-21 ? 
# 
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 Mask              repository 'Initial release' ? ? 
8 8 '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 9  'Structure model' 'Data collection'     
2 9  'Structure model' 'Database references' 
3 10 'Structure model' 'Data collection'     
4 10 'Structure model' 'Database references' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 9  'Structure model' citation        
2 9  'Structure model' citation_author 
3 9  'Structure model' em_admin        
4 10 'Structure model' citation        
5 10 'Structure model' em_admin        
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 9  'Structure model' '_citation.pdbx_database_id_DOI'    
2 9  'Structure model' '_citation.pdbx_database_id_PubMed' 
3 9  'Structure model' '_citation.title'                   
4 9  'Structure model' '_em_admin.last_update'             
5 10 'Structure model' '_citation.journal_volume'          
6 10 'Structure model' '_citation.page_first'              
7 10 'Structure model' '_citation.page_last'               
8 10 'Structure model' '_em_admin.last_update'             
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  ? 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9J3J 
_pdbx_database_status.recvd_initial_deposition_date   2024-08-08 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBC 
_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        'Arabidopsis ATP/ADP translocator AtNTT1' 
_pdbx_database_related.db_id          EMD-61117 
_pdbx_database_related.content_type   'associated EM volume' 
# 
_pdbx_contact_author.id                 5 
_pdbx_contact_author.email              mrfan@cemps.ac.cn 
_pdbx_contact_author.name_first         Minrui 
_pdbx_contact_author.name_last          Fan 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0009-0002-8375-6972 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Lin, H.J.'   1 0000-0002-9847-0996 
'Huang, J.'   2 ?                   
'Li, T.M.'    3 0009-0002-1444-1707 
'Li, W.J.'    4 0009-0001-4333-9886 
'Su, N.N.'    5 0000-0002-8737-0412 
'Zhang, J.R.' 6 0009-0004-5131-2992 
'Wu, X.D.'    7 0000-0002-6492-2202 
'Fan, M.R.'   8 0009-0002-8375-6972 
# 
_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            Nature 
_citation.journal_id_ASTM           NATUAS 
_citation.journal_id_CSD            0006 
_citation.journal_id_ISSN           1476-4687 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            641 
_citation.language                  ? 
_citation.page_first                797 
_citation.page_last                 804 
_citation.title                     'Structure and mechanism of the plastid/parasite ATP/ADP translocator.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1038/s41586-025-08743-3 
_citation.pdbx_database_id_PubMed   40074904 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Lin, H.'   1  ?                   
primary 'Huang, J.' 2  ?                   
primary 'Li, T.'    3  ?                   
primary 'Li, W.'    4  ?                   
primary 'Wu, Y.'    5  ?                   
primary 'Yang, T.'  6  ?                   
primary 'Nian, Y.'  7  ?                   
primary 'Lin, X.'   8  ?                   
primary 'Wang, J.'  9  0000-0003-4643-3453 
primary 'Wang, R.'  10 ?                   
primary 'Zhao, X.'  11 ?                   
primary 'Su, N.'    12 0000-0002-8737-0412 
primary 'Zhang, J.' 13 0009-0004-5131-2992 
primary 'Wu, X.'    14 0000-0002-6492-2202 
primary 'Fan, M.'   15 0009-0002-8375-6972 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer man 'ADP,ATP carrier protein 1, chloroplastic' 66654.609 1 ? ? ? ? 
2 polymer man 'nanobody: B-C8'                           13700.997 1 ? ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'ADP/ATP translocase 1,Adenine nucleotide translocase 1' 
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)' no no 
;MAGAVFGEGDSAAVVASPKIFGVEVATLKKIIPLGLMFFCILFNYTILRDTKDVLVVTAKGSSAEIIPFLKTWVNLPMAI
GFMLLYTKLSNVLSKKALFYTVIVPFIIYFGAFGFVMYPLSNYIHPEALADKLLTTLGPRFMGPIAILRIWSFCLFYVMA
ELWGSVVVSVLFWGFANQITTVDEAKKFYPLFGLGANVALIFSGRTVKYFSNLRKNLGPGVDGWAVSLKAMMSIVVGMGL
AICLLYWWVNRYVPLPTRSKNKKEKPKMGTMESLKFLVSSPYIRDLATLVVAYGISINLVEVTWKSKLKAQFPSPNEYSA
FMGDFSTCTGVATFTMMLLSQYVFNKYGWGVAAKITPTVLLLTGVAFFSLILFGGPFAPLVAKLGMTPLLAAVYVGALQN
IFSKSAKYSLFDPCKEMAYIPLDEDTKVKGKAAIDVVCNPLGKSGGALIQQFMILSFGSLANSTPYLGMILLVIVTAWLA
AAKSLEGQFNSLRSEEELEKEMERASSVKIPVVSQDESGNGSLGESPSSSPEKSAPTNLVDELTSRGRGSGGLNDIFEAQ
KIEWHEGSGLEVLFQGPDYKDDDDKWSHPQFEKGGGGSGGSAWSHPQFEK
;
;MAGAVFGEGDSAAVVASPKIFGVEVATLKKIIPLGLMFFCILFNYTILRDTKDVLVVTAKGSSAEIIPFLKTWVNLPMAI
GFMLLYTKLSNVLSKKALFYTVIVPFIIYFGAFGFVMYPLSNYIHPEALADKLLTTLGPRFMGPIAILRIWSFCLFYVMA
ELWGSVVVSVLFWGFANQITTVDEAKKFYPLFGLGANVALIFSGRTVKYFSNLRKNLGPGVDGWAVSLKAMMSIVVGMGL
AICLLYWWVNRYVPLPTRSKNKKEKPKMGTMESLKFLVSSPYIRDLATLVVAYGISINLVEVTWKSKLKAQFPSPNEYSA
FMGDFSTCTGVATFTMMLLSQYVFNKYGWGVAAKITPTVLLLTGVAFFSLILFGGPFAPLVAKLGMTPLLAAVYVGALQN
IFSKSAKYSLFDPCKEMAYIPLDEDTKVKGKAAIDVVCNPLGKSGGALIQQFMILSFGSLANSTPYLGMILLVIVTAWLA
AAKSLEGQFNSLRSEEELEKEMERASSVKIPVVSQDESGNGSLGESPSSSPEKSAPTNLVDELTSRGRGSGGLNDIFEAQ
KIEWHEGSGLEVLFQGPDYKDDDDKWSHPQFEKGGGGSGGSAWSHPQFEK
;
A ? 
2 'polypeptide(L)' no no 
;EVQLVESGGGLVQAGGSLRLSCAASGFPVTEHEMYWYRQAPGKEREWVAAIDSYGYTEYADSVKGRFTISRDNSKNTVYL
QMNSLKPEDTAVYYCNVKDLGAWYNDYDYWGQGTQVTVSSLE
;
;EVQLVESGGGLVQAGGSLRLSCAASGFPVTEHEMYWYRQAPGKEREWVAAIDSYGYTEYADSVKGRFTISRDNSKNTVYL
QMNSLKPEDTAVYYCNVKDLGAWYNDYDYWGQGTQVTVSSLE
;
B ? 
# 
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   ALA n 
1 3   GLY n 
1 4   ALA n 
1 5   VAL n 
1 6   PHE n 
1 7   GLY n 
1 8   GLU n 
1 9   GLY n 
1 10  ASP n 
1 11  SER n 
1 12  ALA n 
1 13  ALA n 
1 14  VAL n 
1 15  VAL n 
1 16  ALA n 
1 17  SER n 
1 18  PRO n 
1 19  LYS n 
1 20  ILE n 
1 21  PHE n 
1 22  GLY n 
1 23  VAL n 
1 24  GLU n 
1 25  VAL n 
1 26  ALA n 
1 27  THR n 
1 28  LEU n 
1 29  LYS n 
1 30  LYS n 
1 31  ILE n 
1 32  ILE n 
1 33  PRO n 
1 34  LEU n 
1 35  GLY n 
1 36  LEU n 
1 37  MET n 
1 38  PHE n 
1 39  PHE n 
1 40  CYS n 
1 41  ILE n 
1 42  LEU n 
1 43  PHE n 
1 44  ASN n 
1 45  TYR n 
1 46  THR n 
1 47  ILE n 
1 48  LEU n 
1 49  ARG n 
1 50  ASP n 
1 51  THR n 
1 52  LYS n 
1 53  ASP n 
1 54  VAL n 
1 55  LEU n 
1 56  VAL n 
1 57  VAL n 
1 58  THR n 
1 59  ALA n 
1 60  LYS n 
1 61  GLY n 
1 62  SER n 
1 63  SER n 
1 64  ALA n 
1 65  GLU n 
1 66  ILE n 
1 67  ILE n 
1 68  PRO n 
1 69  PHE n 
1 70  LEU n 
1 71  LYS n 
1 72  THR n 
1 73  TRP n 
1 74  VAL n 
1 75  ASN n 
1 76  LEU n 
1 77  PRO n 
1 78  MET n 
1 79  ALA n 
1 80  ILE n 
1 81  GLY n 
1 82  PHE n 
1 83  MET n 
1 84  LEU n 
1 85  LEU n 
1 86  TYR n 
1 87  THR n 
1 88  LYS n 
1 89  LEU n 
1 90  SER n 
1 91  ASN n 
1 92  VAL n 
1 93  LEU n 
1 94  SER n 
1 95  LYS n 
1 96  LYS n 
1 97  ALA n 
1 98  LEU n 
1 99  PHE n 
1 100 TYR n 
1 101 THR n 
1 102 VAL n 
1 103 ILE n 
1 104 VAL n 
1 105 PRO n 
1 106 PHE n 
1 107 ILE n 
1 108 ILE n 
1 109 TYR n 
1 110 PHE n 
1 111 GLY n 
1 112 ALA n 
1 113 PHE n 
1 114 GLY n 
1 115 PHE n 
1 116 VAL n 
1 117 MET n 
1 118 TYR n 
1 119 PRO n 
1 120 LEU n 
1 121 SER n 
1 122 ASN n 
1 123 TYR n 
1 124 ILE n 
1 125 HIS n 
1 126 PRO n 
1 127 GLU n 
1 128 ALA n 
1 129 LEU n 
1 130 ALA n 
1 131 ASP n 
1 132 LYS n 
1 133 LEU n 
1 134 LEU n 
1 135 THR n 
1 136 THR n 
1 137 LEU n 
1 138 GLY n 
1 139 PRO n 
1 140 ARG n 
1 141 PHE n 
1 142 MET n 
1 143 GLY n 
1 144 PRO n 
1 145 ILE n 
1 146 ALA n 
1 147 ILE n 
1 148 LEU n 
1 149 ARG n 
1 150 ILE n 
1 151 TRP n 
1 152 SER n 
1 153 PHE n 
1 154 CYS n 
1 155 LEU n 
1 156 PHE n 
1 157 TYR n 
1 158 VAL n 
1 159 MET n 
1 160 ALA n 
1 161 GLU n 
1 162 LEU n 
1 163 TRP n 
1 164 GLY n 
1 165 SER n 
1 166 VAL n 
1 167 VAL n 
1 168 VAL n 
1 169 SER n 
1 170 VAL n 
1 171 LEU n 
1 172 PHE n 
1 173 TRP n 
1 174 GLY n 
1 175 PHE n 
1 176 ALA n 
1 177 ASN n 
1 178 GLN n 
1 179 ILE n 
1 180 THR n 
1 181 THR n 
1 182 VAL n 
1 183 ASP n 
1 184 GLU n 
1 185 ALA n 
1 186 LYS n 
1 187 LYS n 
1 188 PHE n 
1 189 TYR n 
1 190 PRO n 
1 191 LEU n 
1 192 PHE n 
1 193 GLY n 
1 194 LEU n 
1 195 GLY n 
1 196 ALA n 
1 197 ASN n 
1 198 VAL n 
1 199 ALA n 
1 200 LEU n 
1 201 ILE n 
1 202 PHE n 
1 203 SER n 
1 204 GLY n 
1 205 ARG n 
1 206 THR n 
1 207 VAL n 
1 208 LYS n 
1 209 TYR n 
1 210 PHE n 
1 211 SER n 
1 212 ASN n 
1 213 LEU n 
1 214 ARG n 
1 215 LYS n 
1 216 ASN n 
1 217 LEU n 
1 218 GLY n 
1 219 PRO n 
1 220 GLY n 
1 221 VAL n 
1 222 ASP n 
1 223 GLY n 
1 224 TRP n 
1 225 ALA n 
1 226 VAL n 
1 227 SER n 
1 228 LEU n 
1 229 LYS n 
1 230 ALA n 
1 231 MET n 
1 232 MET n 
1 233 SER n 
1 234 ILE n 
1 235 VAL n 
1 236 VAL n 
1 237 GLY n 
1 238 MET n 
1 239 GLY n 
1 240 LEU n 
1 241 ALA n 
1 242 ILE n 
1 243 CYS n 
1 244 LEU n 
1 245 LEU n 
1 246 TYR n 
1 247 TRP n 
1 248 TRP n 
1 249 VAL n 
1 250 ASN n 
1 251 ARG n 
1 252 TYR n 
1 253 VAL n 
1 254 PRO n 
1 255 LEU n 
1 256 PRO n 
1 257 THR n 
1 258 ARG n 
1 259 SER n 
1 260 LYS n 
1 261 ASN n 
1 262 LYS n 
1 263 LYS n 
1 264 GLU n 
1 265 LYS n 
1 266 PRO n 
1 267 LYS n 
1 268 MET n 
1 269 GLY n 
1 270 THR n 
1 271 MET n 
1 272 GLU n 
1 273 SER n 
1 274 LEU n 
1 275 LYS n 
1 276 PHE n 
1 277 LEU n 
1 278 VAL n 
1 279 SER n 
1 280 SER n 
1 281 PRO n 
1 282 TYR n 
1 283 ILE n 
1 284 ARG n 
1 285 ASP n 
1 286 LEU n 
1 287 ALA n 
1 288 THR n 
1 289 LEU n 
1 290 VAL n 
1 291 VAL n 
1 292 ALA n 
1 293 TYR n 
1 294 GLY n 
1 295 ILE n 
1 296 SER n 
1 297 ILE n 
1 298 ASN n 
1 299 LEU n 
1 300 VAL n 
1 301 GLU n 
1 302 VAL n 
1 303 THR n 
1 304 TRP n 
1 305 LYS n 
1 306 SER n 
1 307 LYS n 
1 308 LEU n 
1 309 LYS n 
1 310 ALA n 
1 311 GLN n 
1 312 PHE n 
1 313 PRO n 
1 314 SER n 
1 315 PRO n 
1 316 ASN n 
1 317 GLU n 
1 318 TYR n 
1 319 SER n 
1 320 ALA n 
1 321 PHE n 
1 322 MET n 
1 323 GLY n 
1 324 ASP n 
1 325 PHE n 
1 326 SER n 
1 327 THR n 
1 328 CYS n 
1 329 THR n 
1 330 GLY n 
1 331 VAL n 
1 332 ALA n 
1 333 THR n 
1 334 PHE n 
1 335 THR n 
1 336 MET n 
1 337 MET n 
1 338 LEU n 
1 339 LEU n 
1 340 SER n 
1 341 GLN n 
1 342 TYR n 
1 343 VAL n 
1 344 PHE n 
1 345 ASN n 
1 346 LYS n 
1 347 TYR n 
1 348 GLY n 
1 349 TRP n 
1 350 GLY n 
1 351 VAL n 
1 352 ALA n 
1 353 ALA n 
1 354 LYS n 
1 355 ILE n 
1 356 THR n 
1 357 PRO n 
1 358 THR n 
1 359 VAL n 
1 360 LEU n 
1 361 LEU n 
1 362 LEU n 
1 363 THR n 
1 364 GLY n 
1 365 VAL n 
1 366 ALA n 
1 367 PHE n 
1 368 PHE n 
1 369 SER n 
1 370 LEU n 
1 371 ILE n 
1 372 LEU n 
1 373 PHE n 
1 374 GLY n 
1 375 GLY n 
1 376 PRO n 
1 377 PHE n 
1 378 ALA n 
1 379 PRO n 
1 380 LEU n 
1 381 VAL n 
1 382 ALA n 
1 383 LYS n 
1 384 LEU n 
1 385 GLY n 
1 386 MET n 
1 387 THR n 
1 388 PRO n 
1 389 LEU n 
1 390 LEU n 
1 391 ALA n 
1 392 ALA n 
1 393 VAL n 
1 394 TYR n 
1 395 VAL n 
1 396 GLY n 
1 397 ALA n 
1 398 LEU n 
1 399 GLN n 
1 400 ASN n 
1 401 ILE n 
1 402 PHE n 
1 403 SER n 
1 404 LYS n 
1 405 SER n 
1 406 ALA n 
1 407 LYS n 
1 408 TYR n 
1 409 SER n 
1 410 LEU n 
1 411 PHE n 
1 412 ASP n 
1 413 PRO n 
1 414 CYS n 
1 415 LYS n 
1 416 GLU n 
1 417 MET n 
1 418 ALA n 
1 419 TYR n 
1 420 ILE n 
1 421 PRO n 
1 422 LEU n 
1 423 ASP n 
1 424 GLU n 
1 425 ASP n 
1 426 THR n 
1 427 LYS n 
1 428 VAL n 
1 429 LYS n 
1 430 GLY n 
1 431 LYS n 
1 432 ALA n 
1 433 ALA n 
1 434 ILE n 
1 435 ASP n 
1 436 VAL n 
1 437 VAL n 
1 438 CYS n 
1 439 ASN n 
1 440 PRO n 
1 441 LEU n 
1 442 GLY n 
1 443 LYS n 
1 444 SER n 
1 445 GLY n 
1 446 GLY n 
1 447 ALA n 
1 448 LEU n 
1 449 ILE n 
1 450 GLN n 
1 451 GLN n 
1 452 PHE n 
1 453 MET n 
1 454 ILE n 
1 455 LEU n 
1 456 SER n 
1 457 PHE n 
1 458 GLY n 
1 459 SER n 
1 460 LEU n 
1 461 ALA n 
1 462 ASN n 
1 463 SER n 
1 464 THR n 
1 465 PRO n 
1 466 TYR n 
1 467 LEU n 
1 468 GLY n 
1 469 MET n 
1 470 ILE n 
1 471 LEU n 
1 472 LEU n 
1 473 VAL n 
1 474 ILE n 
1 475 VAL n 
1 476 THR n 
1 477 ALA n 
1 478 TRP n 
1 479 LEU n 
1 480 ALA n 
1 481 ALA n 
1 482 ALA n 
1 483 LYS n 
1 484 SER n 
1 485 LEU n 
1 486 GLU n 
1 487 GLY n 
1 488 GLN n 
1 489 PHE n 
1 490 ASN n 
1 491 SER n 
1 492 LEU n 
1 493 ARG n 
1 494 SER n 
1 495 GLU n 
1 496 GLU n 
1 497 GLU n 
1 498 LEU n 
1 499 GLU n 
1 500 LYS n 
1 501 GLU n 
1 502 MET n 
1 503 GLU n 
1 504 ARG n 
1 505 ALA n 
1 506 SER n 
1 507 SER n 
1 508 VAL n 
1 509 LYS n 
1 510 ILE n 
1 511 PRO n 
1 512 VAL n 
1 513 VAL n 
1 514 SER n 
1 515 GLN n 
1 516 ASP n 
1 517 GLU n 
1 518 SER n 
1 519 GLY n 
1 520 ASN n 
1 521 GLY n 
1 522 SER n 
1 523 LEU n 
1 524 GLY n 
1 525 GLU n 
1 526 SER n 
1 527 PRO n 
1 528 SER n 
1 529 SER n 
1 530 SER n 
1 531 PRO n 
1 532 GLU n 
1 533 LYS n 
1 534 SER n 
1 535 ALA n 
1 536 PRO n 
1 537 THR n 
1 538 ASN n 
1 539 LEU n 
1 540 VAL n 
1 541 ASP n 
1 542 GLU n 
1 543 LEU n 
1 544 THR n 
1 545 SER n 
1 546 ARG n 
1 547 GLY n 
1 548 ARG n 
1 549 GLY n 
1 550 SER n 
1 551 GLY n 
1 552 GLY n 
1 553 LEU n 
1 554 ASN n 
1 555 ASP n 
1 556 ILE n 
1 557 PHE n 
1 558 GLU n 
1 559 ALA n 
1 560 GLN n 
1 561 LYS n 
1 562 ILE n 
1 563 GLU n 
1 564 TRP n 
1 565 HIS n 
1 566 GLU n 
1 567 GLY n 
1 568 SER n 
1 569 GLY n 
1 570 LEU n 
1 571 GLU n 
1 572 VAL n 
1 573 LEU n 
1 574 PHE n 
1 575 GLN n 
1 576 GLY n 
1 577 PRO n 
1 578 ASP n 
1 579 TYR n 
1 580 LYS n 
1 581 ASP n 
1 582 ASP n 
1 583 ASP n 
1 584 ASP n 
1 585 LYS n 
1 586 TRP n 
1 587 SER n 
1 588 HIS n 
1 589 PRO n 
1 590 GLN n 
1 591 PHE n 
1 592 GLU n 
1 593 LYS n 
1 594 GLY n 
1 595 GLY n 
1 596 GLY n 
1 597 GLY n 
1 598 SER n 
1 599 GLY n 
1 600 GLY n 
1 601 SER n 
1 602 ALA n 
1 603 TRP n 
1 604 SER n 
1 605 HIS n 
1 606 PRO n 
1 607 GLN n 
1 608 PHE n 
1 609 GLU n 
1 610 LYS n 
2 1   GLU n 
2 2   VAL n 
2 3   GLN n 
2 4   LEU n 
2 5   VAL n 
2 6   GLU n 
2 7   SER n 
2 8   GLY n 
2 9   GLY n 
2 10  GLY n 
2 11  LEU n 
2 12  VAL n 
2 13  GLN n 
2 14  ALA n 
2 15  GLY n 
2 16  GLY n 
2 17  SER n 
2 18  LEU n 
2 19  ARG n 
2 20  LEU n 
2 21  SER n 
2 22  CYS n 
2 23  ALA n 
2 24  ALA n 
2 25  SER n 
2 26  GLY n 
2 27  PHE n 
2 28  PRO n 
2 29  VAL n 
2 30  THR n 
2 31  GLU n 
2 32  HIS n 
2 33  GLU n 
2 34  MET n 
2 35  TYR n 
2 36  TRP n 
2 37  TYR n 
2 38  ARG n 
2 39  GLN n 
2 40  ALA n 
2 41  PRO n 
2 42  GLY n 
2 43  LYS n 
2 44  GLU n 
2 45  ARG n 
2 46  GLU n 
2 47  TRP n 
2 48  VAL n 
2 49  ALA n 
2 50  ALA n 
2 51  ILE n 
2 52  ASP n 
2 53  SER n 
2 54  TYR n 
2 55  GLY n 
2 56  TYR n 
2 57  THR n 
2 58  GLU n 
2 59  TYR n 
2 60  ALA n 
2 61  ASP n 
2 62  SER n 
2 63  VAL n 
2 64  LYS n 
2 65  GLY n 
2 66  ARG n 
2 67  PHE n 
2 68  THR n 
2 69  ILE n 
2 70  SER n 
2 71  ARG n 
2 72  ASP n 
2 73  ASN n 
2 74  SER n 
2 75  LYS n 
2 76  ASN n 
2 77  THR n 
2 78  VAL n 
2 79  TYR n 
2 80  LEU n 
2 81  GLN n 
2 82  MET n 
2 83  ASN n 
2 84  SER n 
2 85  LEU n 
2 86  LYS n 
2 87  PRO n 
2 88  GLU n 
2 89  ASP n 
2 90  THR n 
2 91  ALA n 
2 92  VAL n 
2 93  TYR n 
2 94  TYR n 
2 95  CYS n 
2 96  ASN n 
2 97  VAL n 
2 98  LYS n 
2 99  ASP n 
2 100 LEU n 
2 101 GLY n 
2 102 ALA n 
2 103 TRP n 
2 104 TYR n 
2 105 ASN n 
2 106 ASP n 
2 107 TYR n 
2 108 ASP n 
2 109 TYR n 
2 110 TRP n 
2 111 GLY n 
2 112 GLN n 
2 113 GLY n 
2 114 THR n 
2 115 GLN n 
2 116 VAL n 
2 117 THR n 
2 118 VAL n 
2 119 SER n 
2 120 SER n 
2 121 LEU n 
2 122 GLU n 
# 
loop_
_entity_src_gen.entity_id 
_entity_src_gen.pdbx_src_id 
_entity_src_gen.pdbx_alt_source_flag 
_entity_src_gen.pdbx_seq_type 
_entity_src_gen.pdbx_beg_seq_num 
_entity_src_gen.pdbx_end_seq_num 
_entity_src_gen.gene_src_common_name 
_entity_src_gen.gene_src_genus 
_entity_src_gen.pdbx_gene_src_gene 
_entity_src_gen.gene_src_species 
_entity_src_gen.gene_src_strain 
_entity_src_gen.gene_src_tissue 
_entity_src_gen.gene_src_tissue_fraction 
_entity_src_gen.gene_src_details 
_entity_src_gen.pdbx_gene_src_fragment 
_entity_src_gen.pdbx_gene_src_scientific_name 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 
_entity_src_gen.pdbx_gene_src_variant 
_entity_src_gen.pdbx_gene_src_cell_line 
_entity_src_gen.pdbx_gene_src_atcc 
_entity_src_gen.pdbx_gene_src_organ 
_entity_src_gen.pdbx_gene_src_organelle 
_entity_src_gen.pdbx_gene_src_cell 
_entity_src_gen.pdbx_gene_src_cellular_location 
_entity_src_gen.host_org_common_name 
_entity_src_gen.pdbx_host_org_scientific_name 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 
_entity_src_gen.host_org_genus 
_entity_src_gen.pdbx_host_org_gene 
_entity_src_gen.pdbx_host_org_organ 
_entity_src_gen.host_org_species 
_entity_src_gen.pdbx_host_org_tissue 
_entity_src_gen.pdbx_host_org_tissue_fraction 
_entity_src_gen.pdbx_host_org_strain 
_entity_src_gen.pdbx_host_org_variant 
_entity_src_gen.pdbx_host_org_cell_line 
_entity_src_gen.pdbx_host_org_atcc 
_entity_src_gen.pdbx_host_org_culture_collection 
_entity_src_gen.pdbx_host_org_cell 
_entity_src_gen.pdbx_host_org_organelle 
_entity_src_gen.pdbx_host_org_cellular_location 
_entity_src_gen.pdbx_host_org_vector_type 
_entity_src_gen.pdbx_host_org_vector 
_entity_src_gen.host_org_details 
_entity_src_gen.expression_system_id 
_entity_src_gen.plasmid_name 
_entity_src_gen.plasmid_details 
_entity_src_gen.pdbx_description 
1 1 sample 'Biological sequence' 1 610 'Mouse-ear cress' ? 'AATP1, At1g80300, F5I6.5' ? ? ? ? ? ? 'Arabidopsis thaliana' 3702  ? ? 
? ? ? ? ? ? 'Homo sapiens'     9606 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 122 ?                 ? ?                          ? ? ? ? ? ? 'Vicugna pacos'        30538 ? ? 
? ? ? ? ? ? 'Escherichia coli' 562  ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
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   86  ?   ?   ?   A . n 
A 1 2   ALA 2   87  ?   ?   ?   A . n 
A 1 3   GLY 3   88  ?   ?   ?   A . n 
A 1 4   ALA 4   89  ?   ?   ?   A . n 
A 1 5   VAL 5   90  ?   ?   ?   A . n 
A 1 6   PHE 6   91  ?   ?   ?   A . n 
A 1 7   GLY 7   92  ?   ?   ?   A . n 
A 1 8   GLU 8   93  ?   ?   ?   A . n 
A 1 9   GLY 9   94  ?   ?   ?   A . n 
A 1 10  ASP 10  95  ?   ?   ?   A . n 
A 1 11  SER 11  96  ?   ?   ?   A . n 
A 1 12  ALA 12  97  ?   ?   ?   A . n 
A 1 13  ALA 13  98  ?   ?   ?   A . n 
A 1 14  VAL 14  99  ?   ?   ?   A . n 
A 1 15  VAL 15  100 ?   ?   ?   A . n 
A 1 16  ALA 16  101 101 ALA ALA A . n 
A 1 17  SER 17  102 102 SER SER A . n 
A 1 18  PRO 18  103 103 PRO PRO A . n 
A 1 19  LYS 19  104 104 LYS LYS A . n 
A 1 20  ILE 20  105 105 ILE ILE A . n 
A 1 21  PHE 21  106 106 PHE PHE A . n 
A 1 22  GLY 22  107 107 GLY GLY A . n 
A 1 23  VAL 23  108 108 VAL VAL A . n 
A 1 24  GLU 24  109 109 GLU GLU A . n 
A 1 25  VAL 25  110 110 VAL VAL A . n 
A 1 26  ALA 26  111 111 ALA ALA A . n 
A 1 27  THR 27  112 112 THR THR A . n 
A 1 28  LEU 28  113 113 LEU LEU A . n 
A 1 29  LYS 29  114 114 LYS LYS A . n 
A 1 30  LYS 30  115 115 LYS LYS A . n 
A 1 31  ILE 31  116 116 ILE ILE A . n 
A 1 32  ILE 32  117 117 ILE ILE A . n 
A 1 33  PRO 33  118 118 PRO PRO A . n 
A 1 34  LEU 34  119 119 LEU LEU A . n 
A 1 35  GLY 35  120 120 GLY GLY A . n 
A 1 36  LEU 36  121 121 LEU LEU A . n 
A 1 37  MET 37  122 122 MET MET A . n 
A 1 38  PHE 38  123 123 PHE PHE A . n 
A 1 39  PHE 39  124 124 PHE PHE A . n 
A 1 40  CYS 40  125 125 CYS CYS A . n 
A 1 41  ILE 41  126 126 ILE ILE A . n 
A 1 42  LEU 42  127 127 LEU LEU A . n 
A 1 43  PHE 43  128 128 PHE PHE A . n 
A 1 44  ASN 44  129 129 ASN ASN A . n 
A 1 45  TYR 45  130 130 TYR TYR A . n 
A 1 46  THR 46  131 131 THR THR A . n 
A 1 47  ILE 47  132 132 ILE ILE A . n 
A 1 48  LEU 48  133 133 LEU LEU A . n 
A 1 49  ARG 49  134 134 ARG ARG A . n 
A 1 50  ASP 50  135 135 ASP ASP A . n 
A 1 51  THR 51  136 136 THR THR A . n 
A 1 52  LYS 52  137 137 LYS LYS A . n 
A 1 53  ASP 53  138 138 ASP ASP A . n 
A 1 54  VAL 54  139 139 VAL VAL A . n 
A 1 55  LEU 55  140 140 LEU LEU A . n 
A 1 56  VAL 56  141 141 VAL VAL A . n 
A 1 57  VAL 57  142 142 VAL VAL A . n 
A 1 58  THR 58  143 143 THR THR A . n 
A 1 59  ALA 59  144 144 ALA ALA A . n 
A 1 60  LYS 60  145 145 LYS LYS A . n 
A 1 61  GLY 61  146 146 GLY GLY A . n 
A 1 62  SER 62  147 147 SER SER A . n 
A 1 63  SER 63  148 148 SER SER A . n 
A 1 64  ALA 64  149 149 ALA ALA A . n 
A 1 65  GLU 65  150 150 GLU GLU A . n 
A 1 66  ILE 66  151 151 ILE ILE A . n 
A 1 67  ILE 67  152 152 ILE ILE A . n 
A 1 68  PRO 68  153 153 PRO PRO A . n 
A 1 69  PHE 69  154 154 PHE PHE A . n 
A 1 70  LEU 70  155 155 LEU LEU A . n 
A 1 71  LYS 71  156 156 LYS LYS A . n 
A 1 72  THR 72  157 157 THR THR A . n 
A 1 73  TRP 73  158 158 TRP TRP A . n 
A 1 74  VAL 74  159 159 VAL VAL A . n 
A 1 75  ASN 75  160 160 ASN ASN A . n 
A 1 76  LEU 76  161 161 LEU LEU A . n 
A 1 77  PRO 77  162 162 PRO PRO A . n 
A 1 78  MET 78  163 163 MET MET A . n 
A 1 79  ALA 79  164 164 ALA ALA A . n 
A 1 80  ILE 80  165 165 ILE ILE A . n 
A 1 81  GLY 81  166 166 GLY GLY A . n 
A 1 82  PHE 82  167 167 PHE PHE A . n 
A 1 83  MET 83  168 168 MET MET A . n 
A 1 84  LEU 84  169 169 LEU LEU A . n 
A 1 85  LEU 85  170 170 LEU LEU A . n 
A 1 86  TYR 86  171 171 TYR TYR A . n 
A 1 87  THR 87  172 172 THR THR A . n 
A 1 88  LYS 88  173 173 LYS LYS A . n 
A 1 89  LEU 89  174 174 LEU LEU A . n 
A 1 90  SER 90  175 175 SER SER A . n 
A 1 91  ASN 91  176 176 ASN ASN A . n 
A 1 92  VAL 92  177 177 VAL VAL A . n 
A 1 93  LEU 93  178 178 LEU LEU A . n 
A 1 94  SER 94  179 179 SER SER A . n 
A 1 95  LYS 95  180 180 LYS LYS A . n 
A 1 96  LYS 96  181 181 LYS LYS A . n 
A 1 97  ALA 97  182 182 ALA ALA A . n 
A 1 98  LEU 98  183 183 LEU LEU A . n 
A 1 99  PHE 99  184 184 PHE PHE A . n 
A 1 100 TYR 100 185 185 TYR TYR A . n 
A 1 101 THR 101 186 186 THR THR A . n 
A 1 102 VAL 102 187 187 VAL VAL A . n 
A 1 103 ILE 103 188 188 ILE ILE A . n 
A 1 104 VAL 104 189 189 VAL VAL A . n 
A 1 105 PRO 105 190 190 PRO PRO A . n 
A 1 106 PHE 106 191 191 PHE PHE A . n 
A 1 107 ILE 107 192 192 ILE ILE A . n 
A 1 108 ILE 108 193 193 ILE ILE A . n 
A 1 109 TYR 109 194 194 TYR TYR A . n 
A 1 110 PHE 110 195 195 PHE PHE A . n 
A 1 111 GLY 111 196 196 GLY GLY A . n 
A 1 112 ALA 112 197 197 ALA ALA A . n 
A 1 113 PHE 113 198 198 PHE PHE A . n 
A 1 114 GLY 114 199 199 GLY GLY A . n 
A 1 115 PHE 115 200 200 PHE PHE A . n 
A 1 116 VAL 116 201 201 VAL VAL A . n 
A 1 117 MET 117 202 202 MET MET A . n 
A 1 118 TYR 118 203 203 TYR TYR A . n 
A 1 119 PRO 119 204 204 PRO PRO A . n 
A 1 120 LEU 120 205 205 LEU LEU A . n 
A 1 121 SER 121 206 206 SER SER A . n 
A 1 122 ASN 122 207 207 ASN ASN A . n 
A 1 123 TYR 123 208 208 TYR TYR A . n 
A 1 124 ILE 124 209 209 ILE ILE A . n 
A 1 125 HIS 125 210 210 HIS HIS A . n 
A 1 126 PRO 126 211 211 PRO PRO A . n 
A 1 127 GLU 127 212 212 GLU GLU A . n 
A 1 128 ALA 128 213 213 ALA ALA A . n 
A 1 129 LEU 129 214 214 LEU LEU A . n 
A 1 130 ALA 130 215 215 ALA ALA A . n 
A 1 131 ASP 131 216 216 ASP ASP A . n 
A 1 132 LYS 132 217 217 LYS LYS A . n 
A 1 133 LEU 133 218 218 LEU LEU A . n 
A 1 134 LEU 134 219 219 LEU LEU A . n 
A 1 135 THR 135 220 220 THR THR A . n 
A 1 136 THR 136 221 221 THR THR A . n 
A 1 137 LEU 137 222 222 LEU LEU A . n 
A 1 138 GLY 138 223 223 GLY GLY A . n 
A 1 139 PRO 139 224 224 PRO PRO A . n 
A 1 140 ARG 140 225 225 ARG ARG A . n 
A 1 141 PHE 141 226 226 PHE PHE A . n 
A 1 142 MET 142 227 227 MET MET A . n 
A 1 143 GLY 143 228 228 GLY GLY A . n 
A 1 144 PRO 144 229 229 PRO PRO A . n 
A 1 145 ILE 145 230 230 ILE ILE A . n 
A 1 146 ALA 146 231 231 ALA ALA A . n 
A 1 147 ILE 147 232 232 ILE ILE A . n 
A 1 148 LEU 148 233 233 LEU LEU A . n 
A 1 149 ARG 149 234 234 ARG ARG A . n 
A 1 150 ILE 150 235 235 ILE ILE A . n 
A 1 151 TRP 151 236 236 TRP TRP A . n 
A 1 152 SER 152 237 237 SER SER A . n 
A 1 153 PHE 153 238 238 PHE PHE A . n 
A 1 154 CYS 154 239 239 CYS CYS A . n 
A 1 155 LEU 155 240 240 LEU LEU A . n 
A 1 156 PHE 156 241 241 PHE PHE A . n 
A 1 157 TYR 157 242 242 TYR TYR A . n 
A 1 158 VAL 158 243 243 VAL VAL A . n 
A 1 159 MET 159 244 244 MET MET A . n 
A 1 160 ALA 160 245 245 ALA ALA A . n 
A 1 161 GLU 161 246 246 GLU GLU A . n 
A 1 162 LEU 162 247 247 LEU LEU A . n 
A 1 163 TRP 163 248 248 TRP TRP A . n 
A 1 164 GLY 164 249 249 GLY GLY A . n 
A 1 165 SER 165 250 250 SER SER A . n 
A 1 166 VAL 166 251 251 VAL VAL A . n 
A 1 167 VAL 167 252 252 VAL VAL A . n 
A 1 168 VAL 168 253 253 VAL VAL A . n 
A 1 169 SER 169 254 254 SER SER A . n 
A 1 170 VAL 170 255 255 VAL VAL A . n 
A 1 171 LEU 171 256 256 LEU LEU A . n 
A 1 172 PHE 172 257 257 PHE PHE A . n 
A 1 173 TRP 173 258 258 TRP TRP A . n 
A 1 174 GLY 174 259 259 GLY GLY A . n 
A 1 175 PHE 175 260 260 PHE PHE A . n 
A 1 176 ALA 176 261 261 ALA ALA A . n 
A 1 177 ASN 177 262 262 ASN ASN A . n 
A 1 178 GLN 178 263 263 GLN GLN A . n 
A 1 179 ILE 179 264 264 ILE ILE A . n 
A 1 180 THR 180 265 265 THR THR A . n 
A 1 181 THR 181 266 266 THR THR A . n 
A 1 182 VAL 182 267 267 VAL VAL A . n 
A 1 183 ASP 183 268 268 ASP ASP A . n 
A 1 184 GLU 184 269 269 GLU GLU A . n 
A 1 185 ALA 185 270 270 ALA ALA A . n 
A 1 186 LYS 186 271 271 LYS LYS A . n 
A 1 187 LYS 187 272 272 LYS LYS A . n 
A 1 188 PHE 188 273 273 PHE PHE A . n 
A 1 189 TYR 189 274 274 TYR TYR A . n 
A 1 190 PRO 190 275 275 PRO PRO A . n 
A 1 191 LEU 191 276 276 LEU LEU A . n 
A 1 192 PHE 192 277 277 PHE PHE A . n 
A 1 193 GLY 193 278 278 GLY GLY A . n 
A 1 194 LEU 194 279 279 LEU LEU A . n 
A 1 195 GLY 195 280 280 GLY GLY A . n 
A 1 196 ALA 196 281 281 ALA ALA A . n 
A 1 197 ASN 197 282 282 ASN ASN A . n 
A 1 198 VAL 198 283 283 VAL VAL A . n 
A 1 199 ALA 199 284 284 ALA ALA A . n 
A 1 200 LEU 200 285 285 LEU LEU A . n 
A 1 201 ILE 201 286 286 ILE ILE A . n 
A 1 202 PHE 202 287 287 PHE PHE A . n 
A 1 203 SER 203 288 288 SER SER A . n 
A 1 204 GLY 204 289 289 GLY GLY A . n 
A 1 205 ARG 205 290 290 ARG ARG A . n 
A 1 206 THR 206 291 291 THR THR A . n 
A 1 207 VAL 207 292 292 VAL VAL A . n 
A 1 208 LYS 208 293 293 LYS LYS A . n 
A 1 209 TYR 209 294 294 TYR TYR A . n 
A 1 210 PHE 210 295 295 PHE PHE A . n 
A 1 211 SER 211 296 296 SER SER A . n 
A 1 212 ASN 212 297 297 ASN ASN A . n 
A 1 213 LEU 213 298 298 LEU LEU A . n 
A 1 214 ARG 214 299 299 ARG ARG A . n 
A 1 215 LYS 215 300 300 LYS LYS A . n 
A 1 216 ASN 216 301 301 ASN ASN A . n 
A 1 217 LEU 217 302 302 LEU LEU A . n 
A 1 218 GLY 218 303 303 GLY GLY A . n 
A 1 219 PRO 219 304 304 PRO PRO A . n 
A 1 220 GLY 220 305 305 GLY GLY A . n 
A 1 221 VAL 221 306 306 VAL VAL A . n 
A 1 222 ASP 222 307 307 ASP ASP A . n 
A 1 223 GLY 223 308 308 GLY GLY A . n 
A 1 224 TRP 224 309 309 TRP TRP A . n 
A 1 225 ALA 225 310 310 ALA ALA A . n 
A 1 226 VAL 226 311 311 VAL VAL A . n 
A 1 227 SER 227 312 312 SER SER A . n 
A 1 228 LEU 228 313 313 LEU LEU A . n 
A 1 229 LYS 229 314 314 LYS LYS A . n 
A 1 230 ALA 230 315 315 ALA ALA A . n 
A 1 231 MET 231 316 316 MET MET A . n 
A 1 232 MET 232 317 317 MET MET A . n 
A 1 233 SER 233 318 318 SER SER A . n 
A 1 234 ILE 234 319 319 ILE ILE A . n 
A 1 235 VAL 235 320 320 VAL VAL A . n 
A 1 236 VAL 236 321 321 VAL VAL A . n 
A 1 237 GLY 237 322 322 GLY GLY A . n 
A 1 238 MET 238 323 323 MET MET A . n 
A 1 239 GLY 239 324 324 GLY GLY A . n 
A 1 240 LEU 240 325 325 LEU LEU A . n 
A 1 241 ALA 241 326 326 ALA ALA A . n 
A 1 242 ILE 242 327 327 ILE ILE A . n 
A 1 243 CYS 243 328 328 CYS CYS A . n 
A 1 244 LEU 244 329 329 LEU LEU A . n 
A 1 245 LEU 245 330 330 LEU LEU A . n 
A 1 246 TYR 246 331 331 TYR TYR A . n 
A 1 247 TRP 247 332 332 TRP TRP A . n 
A 1 248 TRP 248 333 333 TRP TRP A . n 
A 1 249 VAL 249 334 334 VAL VAL A . n 
A 1 250 ASN 250 335 335 ASN ASN A . n 
A 1 251 ARG 251 336 336 ARG ARG A . n 
A 1 252 TYR 252 337 337 TYR TYR A . n 
A 1 253 VAL 253 338 338 VAL VAL A . n 
A 1 254 PRO 254 339 339 PRO PRO A . n 
A 1 255 LEU 255 340 340 LEU LEU A . n 
A 1 256 PRO 256 341 341 PRO PRO A . n 
A 1 257 THR 257 342 342 THR THR A . n 
A 1 258 ARG 258 343 343 ARG ARG A . n 
A 1 259 SER 259 344 344 SER SER A . n 
A 1 260 LYS 260 345 345 LYS LYS A . n 
A 1 261 ASN 261 346 346 ASN ASN A . n 
A 1 262 LYS 262 347 347 LYS LYS A . n 
A 1 263 LYS 263 348 348 LYS LYS A . n 
A 1 264 GLU 264 349 349 GLU GLU A . n 
A 1 265 LYS 265 350 350 LYS LYS A . n 
A 1 266 PRO 266 351 351 PRO PRO A . n 
A 1 267 LYS 267 352 352 LYS LYS A . n 
A 1 268 MET 268 353 353 MET MET A . n 
A 1 269 GLY 269 354 354 GLY GLY A . n 
A 1 270 THR 270 355 355 THR THR A . n 
A 1 271 MET 271 356 356 MET MET A . n 
A 1 272 GLU 272 357 357 GLU GLU A . n 
A 1 273 SER 273 358 358 SER SER A . n 
A 1 274 LEU 274 359 359 LEU LEU A . n 
A 1 275 LYS 275 360 360 LYS LYS A . n 
A 1 276 PHE 276 361 361 PHE PHE A . n 
A 1 277 LEU 277 362 362 LEU LEU A . n 
A 1 278 VAL 278 363 363 VAL VAL A . n 
A 1 279 SER 279 364 364 SER SER A . n 
A 1 280 SER 280 365 365 SER SER A . n 
A 1 281 PRO 281 366 366 PRO PRO A . n 
A 1 282 TYR 282 367 367 TYR TYR A . n 
A 1 283 ILE 283 368 368 ILE ILE A . n 
A 1 284 ARG 284 369 369 ARG ARG A . n 
A 1 285 ASP 285 370 370 ASP ASP A . n 
A 1 286 LEU 286 371 371 LEU LEU A . n 
A 1 287 ALA 287 372 372 ALA ALA A . n 
A 1 288 THR 288 373 373 THR THR A . n 
A 1 289 LEU 289 374 374 LEU LEU A . n 
A 1 290 VAL 290 375 375 VAL VAL A . n 
A 1 291 VAL 291 376 376 VAL VAL A . n 
A 1 292 ALA 292 377 377 ALA ALA A . n 
A 1 293 TYR 293 378 378 TYR TYR A . n 
A 1 294 GLY 294 379 379 GLY GLY A . n 
A 1 295 ILE 295 380 380 ILE ILE A . n 
A 1 296 SER 296 381 381 SER SER A . n 
A 1 297 ILE 297 382 382 ILE ILE A . n 
A 1 298 ASN 298 383 383 ASN ASN A . n 
A 1 299 LEU 299 384 384 LEU LEU A . n 
A 1 300 VAL 300 385 385 VAL VAL A . n 
A 1 301 GLU 301 386 386 GLU GLU A . n 
A 1 302 VAL 302 387 387 VAL VAL A . n 
A 1 303 THR 303 388 388 THR THR A . n 
A 1 304 TRP 304 389 389 TRP TRP A . n 
A 1 305 LYS 305 390 390 LYS LYS A . n 
A 1 306 SER 306 391 391 SER SER A . n 
A 1 307 LYS 307 392 392 LYS LYS A . n 
A 1 308 LEU 308 393 393 LEU LEU A . n 
A 1 309 LYS 309 394 394 LYS LYS A . n 
A 1 310 ALA 310 395 395 ALA ALA A . n 
A 1 311 GLN 311 396 396 GLN GLN A . n 
A 1 312 PHE 312 397 397 PHE PHE A . n 
A 1 313 PRO 313 398 398 PRO PRO A . n 
A 1 314 SER 314 399 399 SER SER A . n 
A 1 315 PRO 315 400 400 PRO PRO A . n 
A 1 316 ASN 316 401 401 ASN ASN A . n 
A 1 317 GLU 317 402 402 GLU GLU A . n 
A 1 318 TYR 318 403 403 TYR TYR A . n 
A 1 319 SER 319 404 404 SER SER A . n 
A 1 320 ALA 320 405 405 ALA ALA A . n 
A 1 321 PHE 321 406 406 PHE PHE A . n 
A 1 322 MET 322 407 407 MET MET A . n 
A 1 323 GLY 323 408 408 GLY GLY A . n 
A 1 324 ASP 324 409 409 ASP ASP A . n 
A 1 325 PHE 325 410 410 PHE PHE A . n 
A 1 326 SER 326 411 411 SER SER A . n 
A 1 327 THR 327 412 412 THR THR A . n 
A 1 328 CYS 328 413 413 CYS CYS A . n 
A 1 329 THR 329 414 414 THR THR A . n 
A 1 330 GLY 330 415 415 GLY GLY A . n 
A 1 331 VAL 331 416 416 VAL VAL A . n 
A 1 332 ALA 332 417 417 ALA ALA A . n 
A 1 333 THR 333 418 418 THR THR A . n 
A 1 334 PHE 334 419 419 PHE PHE A . n 
A 1 335 THR 335 420 420 THR THR A . n 
A 1 336 MET 336 421 421 MET MET A . n 
A 1 337 MET 337 422 422 MET MET A . n 
A 1 338 LEU 338 423 423 LEU LEU A . n 
A 1 339 LEU 339 424 424 LEU LEU A . n 
A 1 340 SER 340 425 425 SER SER A . n 
A 1 341 GLN 341 426 426 GLN GLN A . n 
A 1 342 TYR 342 427 427 TYR TYR A . n 
A 1 343 VAL 343 428 428 VAL VAL A . n 
A 1 344 PHE 344 429 429 PHE PHE A . n 
A 1 345 ASN 345 430 430 ASN ASN A . n 
A 1 346 LYS 346 431 431 LYS LYS A . n 
A 1 347 TYR 347 432 432 TYR TYR A . n 
A 1 348 GLY 348 433 433 GLY GLY A . n 
A 1 349 TRP 349 434 434 TRP TRP A . n 
A 1 350 GLY 350 435 435 GLY GLY A . n 
A 1 351 VAL 351 436 436 VAL VAL A . n 
A 1 352 ALA 352 437 437 ALA ALA A . n 
A 1 353 ALA 353 438 438 ALA ALA A . n 
A 1 354 LYS 354 439 439 LYS LYS A . n 
A 1 355 ILE 355 440 440 ILE ILE A . n 
A 1 356 THR 356 441 441 THR THR A . n 
A 1 357 PRO 357 442 442 PRO PRO A . n 
A 1 358 THR 358 443 443 THR THR A . n 
A 1 359 VAL 359 444 444 VAL VAL A . n 
A 1 360 LEU 360 445 445 LEU LEU A . n 
A 1 361 LEU 361 446 446 LEU LEU A . n 
A 1 362 LEU 362 447 447 LEU LEU A . n 
A 1 363 THR 363 448 448 THR THR A . n 
A 1 364 GLY 364 449 449 GLY GLY A . n 
A 1 365 VAL 365 450 450 VAL VAL A . n 
A 1 366 ALA 366 451 451 ALA ALA A . n 
A 1 367 PHE 367 452 452 PHE PHE A . n 
A 1 368 PHE 368 453 453 PHE PHE A . n 
A 1 369 SER 369 454 454 SER SER A . n 
A 1 370 LEU 370 455 455 LEU LEU A . n 
A 1 371 ILE 371 456 456 ILE ILE A . n 
A 1 372 LEU 372 457 457 LEU LEU A . n 
A 1 373 PHE 373 458 458 PHE PHE A . n 
A 1 374 GLY 374 459 459 GLY GLY A . n 
A 1 375 GLY 375 460 460 GLY GLY A . n 
A 1 376 PRO 376 461 461 PRO PRO A . n 
A 1 377 PHE 377 462 462 PHE PHE A . n 
A 1 378 ALA 378 463 463 ALA ALA A . n 
A 1 379 PRO 379 464 464 PRO PRO A . n 
A 1 380 LEU 380 465 465 LEU LEU A . n 
A 1 381 VAL 381 466 466 VAL VAL A . n 
A 1 382 ALA 382 467 467 ALA ALA A . n 
A 1 383 LYS 383 468 468 LYS LYS A . n 
A 1 384 LEU 384 469 469 LEU LEU A . n 
A 1 385 GLY 385 470 470 GLY GLY A . n 
A 1 386 MET 386 471 471 MET MET A . n 
A 1 387 THR 387 472 472 THR THR A . n 
A 1 388 PRO 388 473 473 PRO PRO A . n 
A 1 389 LEU 389 474 474 LEU LEU A . n 
A 1 390 LEU 390 475 475 LEU LEU A . n 
A 1 391 ALA 391 476 476 ALA ALA A . n 
A 1 392 ALA 392 477 477 ALA ALA A . n 
A 1 393 VAL 393 478 478 VAL VAL A . n 
A 1 394 TYR 394 479 479 TYR TYR A . n 
A 1 395 VAL 395 480 480 VAL VAL A . n 
A 1 396 GLY 396 481 481 GLY GLY A . n 
A 1 397 ALA 397 482 482 ALA ALA A . n 
A 1 398 LEU 398 483 483 LEU LEU A . n 
A 1 399 GLN 399 484 484 GLN GLN A . n 
A 1 400 ASN 400 485 485 ASN ASN A . n 
A 1 401 ILE 401 486 486 ILE ILE A . n 
A 1 402 PHE 402 487 487 PHE PHE A . n 
A 1 403 SER 403 488 488 SER SER A . n 
A 1 404 LYS 404 489 489 LYS LYS A . n 
A 1 405 SER 405 490 490 SER SER A . n 
A 1 406 ALA 406 491 491 ALA ALA A . n 
A 1 407 LYS 407 492 492 LYS LYS A . n 
A 1 408 TYR 408 493 493 TYR TYR A . n 
A 1 409 SER 409 494 494 SER SER A . n 
A 1 410 LEU 410 495 495 LEU LEU A . n 
A 1 411 PHE 411 496 496 PHE PHE A . n 
A 1 412 ASP 412 497 497 ASP ASP A . n 
A 1 413 PRO 413 498 498 PRO PRO A . n 
A 1 414 CYS 414 499 499 CYS CYS A . n 
A 1 415 LYS 415 500 500 LYS LYS A . n 
A 1 416 GLU 416 501 501 GLU GLU A . n 
A 1 417 MET 417 502 502 MET MET A . n 
A 1 418 ALA 418 503 503 ALA ALA A . n 
A 1 419 TYR 419 504 504 TYR TYR A . n 
A 1 420 ILE 420 505 505 ILE ILE A . n 
A 1 421 PRO 421 506 506 PRO PRO A . n 
A 1 422 LEU 422 507 507 LEU LEU A . n 
A 1 423 ASP 423 508 508 ASP ASP A . n 
A 1 424 GLU 424 509 509 GLU GLU A . n 
A 1 425 ASP 425 510 510 ASP ASP A . n 
A 1 426 THR 426 511 511 THR THR A . n 
A 1 427 LYS 427 512 512 LYS LYS A . n 
A 1 428 VAL 428 513 513 VAL VAL A . n 
A 1 429 LYS 429 514 514 LYS LYS A . n 
A 1 430 GLY 430 515 515 GLY GLY A . n 
A 1 431 LYS 431 516 516 LYS LYS A . n 
A 1 432 ALA 432 517 517 ALA ALA A . n 
A 1 433 ALA 433 518 518 ALA ALA A . n 
A 1 434 ILE 434 519 519 ILE ILE A . n 
A 1 435 ASP 435 520 520 ASP ASP A . n 
A 1 436 VAL 436 521 521 VAL VAL A . n 
A 1 437 VAL 437 522 522 VAL VAL A . n 
A 1 438 CYS 438 523 523 CYS CYS A . n 
A 1 439 ASN 439 524 524 ASN ASN A . n 
A 1 440 PRO 440 525 525 PRO PRO A . n 
A 1 441 LEU 441 526 526 LEU LEU A . n 
A 1 442 GLY 442 527 527 GLY GLY A . n 
A 1 443 LYS 443 528 528 LYS LYS A . n 
A 1 444 SER 444 529 529 SER SER A . n 
A 1 445 GLY 445 530 530 GLY GLY A . n 
A 1 446 GLY 446 531 531 GLY GLY A . n 
A 1 447 ALA 447 532 532 ALA ALA A . n 
A 1 448 LEU 448 533 533 LEU LEU A . n 
A 1 449 ILE 449 534 534 ILE ILE A . n 
A 1 450 GLN 450 535 535 GLN GLN A . n 
A 1 451 GLN 451 536 536 GLN GLN A . n 
A 1 452 PHE 452 537 537 PHE PHE A . n 
A 1 453 MET 453 538 538 MET MET A . n 
A 1 454 ILE 454 539 539 ILE ILE A . n 
A 1 455 LEU 455 540 540 LEU LEU A . n 
A 1 456 SER 456 541 541 SER SER A . n 
A 1 457 PHE 457 542 542 PHE PHE A . n 
A 1 458 GLY 458 543 543 GLY GLY A . n 
A 1 459 SER 459 544 544 SER SER A . n 
A 1 460 LEU 460 545 545 LEU LEU A . n 
A 1 461 ALA 461 546 546 ALA ALA A . n 
A 1 462 ASN 462 547 547 ASN ASN A . n 
A 1 463 SER 463 548 548 SER SER A . n 
A 1 464 THR 464 549 549 THR THR A . n 
A 1 465 PRO 465 550 550 PRO PRO A . n 
A 1 466 TYR 466 551 551 TYR TYR A . n 
A 1 467 LEU 467 552 552 LEU LEU A . n 
A 1 468 GLY 468 553 553 GLY GLY A . n 
A 1 469 MET 469 554 554 MET MET A . n 
A 1 470 ILE 470 555 555 ILE ILE A . n 
A 1 471 LEU 471 556 556 LEU LEU A . n 
A 1 472 LEU 472 557 557 LEU LEU A . n 
A 1 473 VAL 473 558 558 VAL VAL A . n 
A 1 474 ILE 474 559 559 ILE ILE A . n 
A 1 475 VAL 475 560 560 VAL VAL A . n 
A 1 476 THR 476 561 561 THR THR A . n 
A 1 477 ALA 477 562 562 ALA ALA A . n 
A 1 478 TRP 478 563 563 TRP TRP A . n 
A 1 479 LEU 479 564 564 LEU LEU A . n 
A 1 480 ALA 480 565 565 ALA ALA A . n 
A 1 481 ALA 481 566 566 ALA ALA A . n 
A 1 482 ALA 482 567 567 ALA ALA A . n 
A 1 483 LYS 483 568 568 LYS LYS A . n 
A 1 484 SER 484 569 569 SER SER A . n 
A 1 485 LEU 485 570 570 LEU LEU A . n 
A 1 486 GLU 486 571 571 GLU GLU A . n 
A 1 487 GLY 487 572 572 GLY GLY A . n 
A 1 488 GLN 488 573 573 GLN GLN A . n 
A 1 489 PHE 489 574 574 PHE PHE A . n 
A 1 490 ASN 490 575 575 ASN ASN A . n 
A 1 491 SER 491 576 576 SER SER A . n 
A 1 492 LEU 492 577 577 LEU LEU A . n 
A 1 493 ARG 493 578 578 ARG ARG A . n 
A 1 494 SER 494 579 579 SER SER A . n 
A 1 495 GLU 495 580 580 GLU GLU A . n 
A 1 496 GLU 496 581 581 GLU GLU A . n 
A 1 497 GLU 497 582 582 GLU GLU A . n 
A 1 498 LEU 498 583 583 LEU LEU A . n 
A 1 499 GLU 499 584 584 GLU GLU A . n 
A 1 500 LYS 500 585 585 LYS LYS A . n 
A 1 501 GLU 501 586 586 GLU GLU A . n 
A 1 502 MET 502 587 587 MET MET A . n 
A 1 503 GLU 503 588 588 GLU GLU A . n 
A 1 504 ARG 504 589 589 ARG ARG A . n 
A 1 505 ALA 505 590 590 ALA ALA A . n 
A 1 506 SER 506 591 ?   ?   ?   A . n 
A 1 507 SER 507 592 ?   ?   ?   A . n 
A 1 508 VAL 508 593 ?   ?   ?   A . n 
A 1 509 LYS 509 594 ?   ?   ?   A . n 
A 1 510 ILE 510 595 ?   ?   ?   A . n 
A 1 511 PRO 511 596 ?   ?   ?   A . n 
A 1 512 VAL 512 597 ?   ?   ?   A . n 
A 1 513 VAL 513 598 ?   ?   ?   A . n 
A 1 514 SER 514 599 ?   ?   ?   A . n 
A 1 515 GLN 515 600 ?   ?   ?   A . n 
A 1 516 ASP 516 601 ?   ?   ?   A . n 
A 1 517 GLU 517 602 ?   ?   ?   A . n 
A 1 518 SER 518 603 ?   ?   ?   A . n 
A 1 519 GLY 519 604 ?   ?   ?   A . n 
A 1 520 ASN 520 605 ?   ?   ?   A . n 
A 1 521 GLY 521 606 ?   ?   ?   A . n 
A 1 522 SER 522 607 ?   ?   ?   A . n 
A 1 523 LEU 523 608 ?   ?   ?   A . n 
A 1 524 GLY 524 609 ?   ?   ?   A . n 
A 1 525 GLU 525 610 ?   ?   ?   A . n 
A 1 526 SER 526 611 ?   ?   ?   A . n 
A 1 527 PRO 527 612 ?   ?   ?   A . n 
A 1 528 SER 528 613 ?   ?   ?   A . n 
A 1 529 SER 529 614 ?   ?   ?   A . n 
A 1 530 SER 530 615 ?   ?   ?   A . n 
A 1 531 PRO 531 616 ?   ?   ?   A . n 
A 1 532 GLU 532 617 ?   ?   ?   A . n 
A 1 533 LYS 533 618 ?   ?   ?   A . n 
A 1 534 SER 534 619 ?   ?   ?   A . n 
A 1 535 ALA 535 620 ?   ?   ?   A . n 
A 1 536 PRO 536 621 ?   ?   ?   A . n 
A 1 537 THR 537 622 ?   ?   ?   A . n 
A 1 538 ASN 538 623 ?   ?   ?   A . n 
A 1 539 LEU 539 624 ?   ?   ?   A . n 
A 1 540 VAL 540 625 ?   ?   ?   A . n 
A 1 541 ASP 541 626 ?   ?   ?   A . n 
A 1 542 GLU 542 627 ?   ?   ?   A . n 
A 1 543 LEU 543 628 ?   ?   ?   A . n 
A 1 544 THR 544 629 ?   ?   ?   A . n 
A 1 545 SER 545 630 ?   ?   ?   A . n 
A 1 546 ARG 546 631 ?   ?   ?   A . n 
A 1 547 GLY 547 632 ?   ?   ?   A . n 
A 1 548 ARG 548 633 ?   ?   ?   A . n 
A 1 549 GLY 549 634 ?   ?   ?   A . n 
A 1 550 SER 550 635 ?   ?   ?   A . n 
A 1 551 GLY 551 636 ?   ?   ?   A . n 
A 1 552 GLY 552 637 ?   ?   ?   A . n 
A 1 553 LEU 553 638 ?   ?   ?   A . n 
A 1 554 ASN 554 639 ?   ?   ?   A . n 
A 1 555 ASP 555 640 ?   ?   ?   A . n 
A 1 556 ILE 556 641 ?   ?   ?   A . n 
A 1 557 PHE 557 642 ?   ?   ?   A . n 
A 1 558 GLU 558 643 ?   ?   ?   A . n 
A 1 559 ALA 559 644 ?   ?   ?   A . n 
A 1 560 GLN 560 645 ?   ?   ?   A . n 
A 1 561 LYS 561 646 ?   ?   ?   A . n 
A 1 562 ILE 562 647 ?   ?   ?   A . n 
A 1 563 GLU 563 648 ?   ?   ?   A . n 
A 1 564 TRP 564 649 ?   ?   ?   A . n 
A 1 565 HIS 565 650 ?   ?   ?   A . n 
A 1 566 GLU 566 651 ?   ?   ?   A . n 
A 1 567 GLY 567 652 ?   ?   ?   A . n 
A 1 568 SER 568 653 ?   ?   ?   A . n 
A 1 569 GLY 569 654 ?   ?   ?   A . n 
A 1 570 LEU 570 655 ?   ?   ?   A . n 
A 1 571 GLU 571 656 ?   ?   ?   A . n 
A 1 572 VAL 572 657 ?   ?   ?   A . n 
A 1 573 LEU 573 658 ?   ?   ?   A . n 
A 1 574 PHE 574 659 ?   ?   ?   A . n 
A 1 575 GLN 575 660 ?   ?   ?   A . n 
A 1 576 GLY 576 661 ?   ?   ?   A . n 
A 1 577 PRO 577 662 ?   ?   ?   A . n 
A 1 578 ASP 578 663 ?   ?   ?   A . n 
A 1 579 TYR 579 664 ?   ?   ?   A . n 
A 1 580 LYS 580 665 ?   ?   ?   A . n 
A 1 581 ASP 581 666 ?   ?   ?   A . n 
A 1 582 ASP 582 667 ?   ?   ?   A . n 
A 1 583 ASP 583 668 ?   ?   ?   A . n 
A 1 584 ASP 584 669 ?   ?   ?   A . n 
A 1 585 LYS 585 670 ?   ?   ?   A . n 
A 1 586 TRP 586 671 ?   ?   ?   A . n 
A 1 587 SER 587 672 ?   ?   ?   A . n 
A 1 588 HIS 588 673 ?   ?   ?   A . n 
A 1 589 PRO 589 674 ?   ?   ?   A . n 
A 1 590 GLN 590 675 ?   ?   ?   A . n 
A 1 591 PHE 591 676 ?   ?   ?   A . n 
A 1 592 GLU 592 677 ?   ?   ?   A . n 
A 1 593 LYS 593 678 ?   ?   ?   A . n 
A 1 594 GLY 594 679 ?   ?   ?   A . n 
A 1 595 GLY 595 680 ?   ?   ?   A . n 
A 1 596 GLY 596 681 ?   ?   ?   A . n 
A 1 597 GLY 597 682 ?   ?   ?   A . n 
A 1 598 SER 598 683 ?   ?   ?   A . n 
A 1 599 GLY 599 684 ?   ?   ?   A . n 
A 1 600 GLY 600 685 ?   ?   ?   A . n 
A 1 601 SER 601 686 ?   ?   ?   A . n 
A 1 602 ALA 602 687 ?   ?   ?   A . n 
A 1 603 TRP 603 688 ?   ?   ?   A . n 
A 1 604 SER 604 689 ?   ?   ?   A . n 
A 1 605 HIS 605 690 ?   ?   ?   A . n 
A 1 606 PRO 606 691 ?   ?   ?   A . n 
A 1 607 GLN 607 692 ?   ?   ?   A . n 
A 1 608 PHE 608 693 ?   ?   ?   A . n 
A 1 609 GLU 609 694 ?   ?   ?   A . n 
A 1 610 LYS 610 695 ?   ?   ?   A . n 
B 2 1   GLU 1   1   1   GLU GLU B . n 
B 2 2   VAL 2   2   2   VAL VAL B . n 
B 2 3   GLN 3   3   3   GLN GLN B . n 
B 2 4   LEU 4   4   4   LEU LEU B . n 
B 2 5   VAL 5   5   5   VAL VAL B . n 
B 2 6   GLU 6   6   6   GLU GLU B . n 
B 2 7   SER 7   7   7   SER SER B . n 
B 2 8   GLY 8   8   8   GLY GLY B . n 
B 2 9   GLY 9   9   9   GLY GLY B . n 
B 2 10  GLY 10  10  10  GLY GLY B . n 
B 2 11  LEU 11  11  11  LEU LEU B . n 
B 2 12  VAL 12  12  12  VAL VAL B . n 
B 2 13  GLN 13  13  13  GLN GLN B . n 
B 2 14  ALA 14  14  14  ALA ALA B . n 
B 2 15  GLY 15  15  15  GLY GLY B . n 
B 2 16  GLY 16  16  16  GLY GLY B . n 
B 2 17  SER 17  17  17  SER SER B . n 
B 2 18  LEU 18  18  18  LEU LEU B . n 
B 2 19  ARG 19  19  19  ARG ARG B . n 
B 2 20  LEU 20  20  20  LEU LEU B . n 
B 2 21  SER 21  21  21  SER SER B . n 
B 2 22  CYS 22  22  22  CYS CYS B . n 
B 2 23  ALA 23  23  23  ALA ALA B . n 
B 2 24  ALA 24  24  24  ALA ALA B . n 
B 2 25  SER 25  25  25  SER SER B . n 
B 2 26  GLY 26  26  26  GLY GLY B . n 
B 2 27  PHE 27  27  27  PHE PHE B . n 
B 2 28  PRO 28  28  28  PRO PRO B . n 
B 2 29  VAL 29  29  29  VAL VAL B . n 
B 2 30  THR 30  30  30  THR THR B . n 
B 2 31  GLU 31  31  31  GLU GLU B . n 
B 2 32  HIS 32  32  32  HIS HIS B . n 
B 2 33  GLU 33  33  33  GLU GLU B . n 
B 2 34  MET 34  34  34  MET MET B . n 
B 2 35  TYR 35  35  35  TYR TYR B . n 
B 2 36  TRP 36  36  36  TRP TRP B . n 
B 2 37  TYR 37  37  37  TYR TYR B . n 
B 2 38  ARG 38  38  38  ARG ARG B . n 
B 2 39  GLN 39  39  39  GLN GLN B . n 
B 2 40  ALA 40  40  40  ALA ALA B . n 
B 2 41  PRO 41  41  41  PRO PRO B . n 
B 2 42  GLY 42  42  42  GLY GLY B . n 
B 2 43  LYS 43  43  43  LYS LYS B . n 
B 2 44  GLU 44  44  44  GLU GLU B . n 
B 2 45  ARG 45  45  45  ARG ARG B . n 
B 2 46  GLU 46  46  46  GLU GLU B . n 
B 2 47  TRP 47  47  47  TRP TRP B . n 
B 2 48  VAL 48  48  48  VAL VAL B . n 
B 2 49  ALA 49  49  49  ALA ALA B . n 
B 2 50  ALA 50  50  50  ALA ALA B . n 
B 2 51  ILE 51  51  51  ILE ILE B . n 
B 2 52  ASP 52  52  52  ASP ASP B . n 
B 2 53  SER 53  53  53  SER SER B . n 
B 2 54  TYR 54  54  54  TYR TYR B . n 
B 2 55  GLY 55  55  55  GLY GLY B . n 
B 2 56  TYR 56  56  56  TYR TYR B . n 
B 2 57  THR 57  57  57  THR THR B . n 
B 2 58  GLU 58  58  58  GLU GLU B . n 
B 2 59  TYR 59  59  59  TYR TYR B . n 
B 2 60  ALA 60  60  60  ALA ALA B . n 
B 2 61  ASP 61  61  61  ASP ASP B . n 
B 2 62  SER 62  62  62  SER SER B . n 
B 2 63  VAL 63  63  63  VAL VAL B . n 
B 2 64  LYS 64  64  64  LYS LYS B . n 
B 2 65  GLY 65  65  65  GLY GLY B . n 
B 2 66  ARG 66  66  66  ARG ARG B . n 
B 2 67  PHE 67  67  67  PHE PHE B . n 
B 2 68  THR 68  68  68  THR THR B . n 
B 2 69  ILE 69  69  69  ILE ILE B . n 
B 2 70  SER 70  70  70  SER SER B . n 
B 2 71  ARG 71  71  71  ARG ARG B . n 
B 2 72  ASP 72  72  72  ASP ASP B . n 
B 2 73  ASN 73  73  73  ASN ASN B . n 
B 2 74  SER 74  74  74  SER SER B . n 
B 2 75  LYS 75  75  75  LYS LYS B . n 
B 2 76  ASN 76  76  76  ASN ASN B . n 
B 2 77  THR 77  77  77  THR THR B . n 
B 2 78  VAL 78  78  78  VAL VAL B . n 
B 2 79  TYR 79  79  79  TYR TYR B . n 
B 2 80  LEU 80  80  80  LEU LEU B . n 
B 2 81  GLN 81  81  81  GLN GLN B . n 
B 2 82  MET 82  82  82  MET MET B . n 
B 2 83  ASN 83  83  83  ASN ASN B . n 
B 2 84  SER 84  84  84  SER SER B . n 
B 2 85  LEU 85  85  85  LEU LEU B . n 
B 2 86  LYS 86  86  86  LYS LYS B . n 
B 2 87  PRO 87  87  87  PRO PRO B . n 
B 2 88  GLU 88  88  88  GLU GLU B . n 
B 2 89  ASP 89  89  89  ASP ASP B . n 
B 2 90  THR 90  90  90  THR THR B . n 
B 2 91  ALA 91  91  91  ALA ALA B . n 
B 2 92  VAL 92  92  92  VAL VAL B . n 
B 2 93  TYR 93  93  93  TYR TYR B . n 
B 2 94  TYR 94  94  94  TYR TYR B . n 
B 2 95  CYS 95  95  95  CYS CYS B . n 
B 2 96  ASN 96  96  96  ASN ASN B . n 
B 2 97  VAL 97  97  97  VAL VAL B . n 
B 2 98  LYS 98  98  98  LYS LYS B . n 
B 2 99  ASP 99  99  99  ASP ASP B . n 
B 2 100 LEU 100 100 100 LEU LEU B . n 
B 2 101 GLY 101 101 101 GLY GLY B . n 
B 2 102 ALA 102 102 102 ALA ALA B . n 
B 2 103 TRP 103 103 103 TRP TRP B . n 
B 2 104 TYR 104 104 104 TYR TYR B . n 
B 2 105 ASN 105 105 105 ASN ASN B . n 
B 2 106 ASP 106 106 106 ASP ASP B . n 
B 2 107 TYR 107 107 107 TYR TYR B . n 
B 2 108 ASP 108 108 108 ASP ASP B . n 
B 2 109 TYR 109 109 109 TYR TYR B . n 
B 2 110 TRP 110 110 110 TRP TRP B . n 
B 2 111 GLY 111 111 111 GLY GLY B . n 
B 2 112 GLN 112 112 112 GLN GLN B . n 
B 2 113 GLY 113 113 113 GLY GLY B . n 
B 2 114 THR 114 114 114 THR THR B . n 
B 2 115 GLN 115 115 115 GLN GLN B . n 
B 2 116 VAL 116 116 116 VAL VAL B . n 
B 2 117 THR 117 117 117 THR THR B . n 
B 2 118 VAL 118 118 118 VAL VAL B . n 
B 2 119 SER 119 119 119 SER SER B . n 
B 2 120 SER 120 120 120 SER SER B . n 
B 2 121 LEU 121 121 121 LEU LEU B . n 
B 2 122 GLU 122 122 122 GLU GLU B . n 
# 
_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                   9J3J 
_exptl.crystals_number            ? 
_exptl.details                    ? 
_exptl.method                     'ELECTRON MICROSCOPY' 
_exptl.method_details             ? 
# 
_refine.pdbx_refine_id                           'ELECTRON MICROSCOPY' 
_refine.entry_id                                 9J3J 
_refine.pdbx_diffrn_id                           ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             ? 
_refine.ls_d_res_high                            . 
_refine.ls_percent_reflns_obs                    ? 
_refine.ls_R_factor_obs                          ? 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       ? 
_refine.ls_R_factor_R_free                       ? 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 ? 
_refine.ls_number_reflns_R_free                  ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.B_iso_mean                               ? 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.solvent_model_details                    ? 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.pdbx_ls_cross_valid_method               ? 
_refine.details                                  ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'ELECTRON MICROSCOPY' ? 0.003 ? 4903 ? f_bond_d           ? ? 
'ELECTRON MICROSCOPY' ? 0.695 ? 6658 ? f_angle_d          ? ? 
'ELECTRON MICROSCOPY' ? 5.073 ? 656  ? f_dihedral_angle_d ? ? 
'ELECTRON MICROSCOPY' ? 0.043 ? 755  ? f_chiral_restr     ? ? 
'ELECTRON MICROSCOPY' ? 0.005 ? 817  ? f_plane_restr      ? ? 
# 
_struct.entry_id                     9J3J 
_struct.title                        'Arabidopsis ATP/ADP translocator AtNTT1' 
_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        9J3J 
_struct_keywords.text            'ATP/ADP translocator;non-mitochondrial;antiporter, MEMBRANE PROTEIN' 
_struct_keywords.pdbx_keywords   'MEMBRANE PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP TLC1_ARATH Q39002 ? 1 
;GAVFGEGDSAAVVASPKIFGVEVATLKKIIPLGLMFFCILFNYTILRDTKDVLVVTAKGSSAEIIPFLKTWVNLPMAIGF
MLLYTKLSNVLSKKALFYTVIVPFIIYFGAFGFVMYPLSNYIHPEALADKLLTTLGPRFMGPIAILRIWSFCLFYVMAEL
WGSVVVSVLFWGFANQITTVDEAKKFYPLFGLGANVALIFSGRTVKYFSNLRKNLGPGVDGWAVSLKAMMSIVVGMGLAI
CLLYWWVNRYVPLPTRSKNKKEKPKMGTMESLKFLVSSPYIRDLATLVVAYGISINLVEVTWKSKLKAQFPSPNEYSAFM
GDFSTCTGVATFTMMLLSQYVFNKYGWGVAAKITPTVLLLTGVAFFSLILFGGPFAPLVAKLGMTPLLAAVYVGALQNIF
SKSAKYSLFDPCKEMAYIPLDEDTKVKGKAAIDVVCNPLGKSGGALIQQFMILSFGSLANSTPYLGMILLVIVTAWLAAA
KSLEGQFNSLRSEEELEKEMERASSVKIPVVSQDESGNGSLGESPSSSPEKSAPTNL
;
88 
2 PDB 9J3J       9J3J   ? 2 ? 1  
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 9J3J A 3 ? 539 ? Q39002 88 ? 624 ? 88 624 
2 2 9J3J B 1 ? 122 ? 9J3J   1  ? 122 ? 1  122 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 9J3J MET A 1   ? UNP Q39002 ? ? 'initiating methionine' 86  1  
1 9J3J ALA A 2   ? UNP Q39002 ? ? 'expression tag'        87  2  
1 9J3J VAL A 540 ? UNP Q39002 ? ? 'expression tag'        625 3  
1 9J3J ASP A 541 ? UNP Q39002 ? ? 'expression tag'        626 4  
1 9J3J GLU A 542 ? UNP Q39002 ? ? 'expression tag'        627 5  
1 9J3J LEU A 543 ? UNP Q39002 ? ? 'expression tag'        628 6  
1 9J3J THR A 544 ? UNP Q39002 ? ? 'expression tag'        629 7  
1 9J3J SER A 545 ? UNP Q39002 ? ? 'expression tag'        630 8  
1 9J3J ARG A 546 ? UNP Q39002 ? ? 'expression tag'        631 9  
1 9J3J GLY A 547 ? UNP Q39002 ? ? 'expression tag'        632 10 
1 9J3J ARG A 548 ? UNP Q39002 ? ? 'expression tag'        633 11 
1 9J3J GLY A 549 ? UNP Q39002 ? ? 'expression tag'        634 12 
1 9J3J SER A 550 ? UNP Q39002 ? ? 'expression tag'        635 13 
1 9J3J GLY A 551 ? UNP Q39002 ? ? 'expression tag'        636 14 
1 9J3J GLY A 552 ? UNP Q39002 ? ? 'expression tag'        637 15 
1 9J3J LEU A 553 ? UNP Q39002 ? ? 'expression tag'        638 16 
1 9J3J ASN A 554 ? UNP Q39002 ? ? 'expression tag'        639 17 
1 9J3J ASP A 555 ? UNP Q39002 ? ? 'expression tag'        640 18 
1 9J3J ILE A 556 ? UNP Q39002 ? ? 'expression tag'        641 19 
1 9J3J PHE A 557 ? UNP Q39002 ? ? 'expression tag'        642 20 
1 9J3J GLU A 558 ? UNP Q39002 ? ? 'expression tag'        643 21 
1 9J3J ALA A 559 ? UNP Q39002 ? ? 'expression tag'        644 22 
1 9J3J GLN A 560 ? UNP Q39002 ? ? 'expression tag'        645 23 
1 9J3J LYS A 561 ? UNP Q39002 ? ? 'expression tag'        646 24 
1 9J3J ILE A 562 ? UNP Q39002 ? ? 'expression tag'        647 25 
1 9J3J GLU A 563 ? UNP Q39002 ? ? 'expression tag'        648 26 
1 9J3J TRP A 564 ? UNP Q39002 ? ? 'expression tag'        649 27 
1 9J3J HIS A 565 ? UNP Q39002 ? ? 'expression tag'        650 28 
1 9J3J GLU A 566 ? UNP Q39002 ? ? 'expression tag'        651 29 
1 9J3J GLY A 567 ? UNP Q39002 ? ? 'expression tag'        652 30 
1 9J3J SER A 568 ? UNP Q39002 ? ? 'expression tag'        653 31 
1 9J3J GLY A 569 ? UNP Q39002 ? ? 'expression tag'        654 32 
1 9J3J LEU A 570 ? UNP Q39002 ? ? 'expression tag'        655 33 
1 9J3J GLU A 571 ? UNP Q39002 ? ? 'expression tag'        656 34 
1 9J3J VAL A 572 ? UNP Q39002 ? ? 'expression tag'        657 35 
1 9J3J LEU A 573 ? UNP Q39002 ? ? 'expression tag'        658 36 
1 9J3J PHE A 574 ? UNP Q39002 ? ? 'expression tag'        659 37 
1 9J3J GLN A 575 ? UNP Q39002 ? ? 'expression tag'        660 38 
1 9J3J GLY A 576 ? UNP Q39002 ? ? 'expression tag'        661 39 
1 9J3J PRO A 577 ? UNP Q39002 ? ? 'expression tag'        662 40 
1 9J3J ASP A 578 ? UNP Q39002 ? ? 'expression tag'        663 41 
1 9J3J TYR A 579 ? UNP Q39002 ? ? 'expression tag'        664 42 
1 9J3J LYS A 580 ? UNP Q39002 ? ? 'expression tag'        665 43 
1 9J3J ASP A 581 ? UNP Q39002 ? ? 'expression tag'        666 44 
1 9J3J ASP A 582 ? UNP Q39002 ? ? 'expression tag'        667 45 
1 9J3J ASP A 583 ? UNP Q39002 ? ? 'expression tag'        668 46 
1 9J3J ASP A 584 ? UNP Q39002 ? ? 'expression tag'        669 47 
1 9J3J LYS A 585 ? UNP Q39002 ? ? 'expression tag'        670 48 
1 9J3J TRP A 586 ? UNP Q39002 ? ? 'expression tag'        671 49 
1 9J3J SER A 587 ? UNP Q39002 ? ? 'expression tag'        672 50 
1 9J3J HIS A 588 ? UNP Q39002 ? ? 'expression tag'        673 51 
1 9J3J PRO A 589 ? UNP Q39002 ? ? 'expression tag'        674 52 
1 9J3J GLN A 590 ? UNP Q39002 ? ? 'expression tag'        675 53 
1 9J3J PHE A 591 ? UNP Q39002 ? ? 'expression tag'        676 54 
1 9J3J GLU A 592 ? UNP Q39002 ? ? 'expression tag'        677 55 
1 9J3J LYS A 593 ? UNP Q39002 ? ? 'expression tag'        678 56 
1 9J3J GLY A 594 ? UNP Q39002 ? ? 'expression tag'        679 57 
1 9J3J GLY A 595 ? UNP Q39002 ? ? 'expression tag'        680 58 
1 9J3J GLY A 596 ? UNP Q39002 ? ? 'expression tag'        681 59 
1 9J3J GLY A 597 ? UNP Q39002 ? ? 'expression tag'        682 60 
1 9J3J SER A 598 ? UNP Q39002 ? ? 'expression tag'        683 61 
1 9J3J GLY A 599 ? UNP Q39002 ? ? 'expression tag'        684 62 
1 9J3J GLY A 600 ? UNP Q39002 ? ? 'expression tag'        685 63 
1 9J3J SER A 601 ? UNP Q39002 ? ? 'expression tag'        686 64 
1 9J3J ALA A 602 ? UNP Q39002 ? ? 'expression tag'        687 65 
1 9J3J TRP A 603 ? UNP Q39002 ? ? 'expression tag'        688 66 
1 9J3J SER A 604 ? UNP Q39002 ? ? 'expression tag'        689 67 
1 9J3J HIS A 605 ? UNP Q39002 ? ? 'expression tag'        690 68 
1 9J3J PRO A 606 ? UNP Q39002 ? ? 'expression tag'        691 69 
1 9J3J GLN A 607 ? UNP Q39002 ? ? 'expression tag'        692 70 
1 9J3J PHE A 608 ? UNP Q39002 ? ? 'expression tag'        693 71 
1 9J3J GLU A 609 ? UNP Q39002 ? ? 'expression tag'        694 72 
1 9J3J LYS A 610 ? UNP Q39002 ? ? 'expression tag'        695 73 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'electron microscopy' 
_pdbx_struct_assembly_auth_evidence.details                'not applicable' 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0 
_pdbx_struct_oper_list.matrix[1][2]         0.0 
_pdbx_struct_oper_list.matrix[1][3]         0.0 
_pdbx_struct_oper_list.vector[1]            0.0 
_pdbx_struct_oper_list.matrix[2][1]         0.0 
_pdbx_struct_oper_list.matrix[2][2]         1.0 
_pdbx_struct_oper_list.matrix[2][3]         0.0 
_pdbx_struct_oper_list.vector[2]            0.0 
_pdbx_struct_oper_list.matrix[3][1]         0.0 
_pdbx_struct_oper_list.matrix[3][2]         0.0 
_pdbx_struct_oper_list.matrix[3][3]         1.0 
_pdbx_struct_oper_list.vector[3]            0.0 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 VAL A 25  ? VAL A 57  ? VAL A 110 VAL A 142 1 ? 33 
HELX_P HELX_P2  AA2 GLU A 65  ? TRP A 73  ? GLU A 150 TRP A 158 1 ? 9  
HELX_P HELX_P3  AA3 VAL A 74  ? LEU A 93  ? VAL A 159 LEU A 178 1 ? 20 
HELX_P HELX_P4  AA4 SER A 94  ? VAL A 116 ? SER A 179 VAL A 201 1 ? 23 
HELX_P HELX_P5  AA5 LEU A 120 ? HIS A 125 ? LEU A 205 HIS A 210 1 ? 6  
HELX_P HELX_P6  AA6 ASP A 131 ? LEU A 137 ? ASP A 216 LEU A 222 1 ? 7  
HELX_P HELX_P7  AA7 GLY A 138 ? ARG A 140 ? GLY A 223 ARG A 225 5 ? 3  
HELX_P HELX_P8  AA8 PHE A 141 ? ILE A 150 ? PHE A 226 ILE A 235 1 ? 10 
HELX_P HELX_P9  AA9 ILE A 150 ? VAL A 167 ? ILE A 235 VAL A 252 1 ? 18 
HELX_P HELX_P10 AB1 SER A 169 ? THR A 180 ? SER A 254 THR A 265 1 ? 12 
HELX_P HELX_P11 AB2 THR A 181 ? TYR A 189 ? THR A 266 TYR A 274 1 ? 9  
HELX_P HELX_P12 AB3 TYR A 189 ? LEU A 217 ? TYR A 274 LEU A 302 1 ? 29 
HELX_P HELX_P13 AB4 ASP A 222 ? VAL A 253 ? ASP A 307 VAL A 338 1 ? 32 
HELX_P HELX_P14 AB5 SER A 259 ? LYS A 263 ? SER A 344 LYS A 348 5 ? 5  
HELX_P HELX_P15 AB6 MET A 271 ? SER A 279 ? MET A 356 SER A 364 1 ? 9  
HELX_P HELX_P16 AB7 SER A 280 ? PHE A 312 ? SER A 365 PHE A 397 1 ? 33 
HELX_P HELX_P17 AB8 SER A 314 ? TYR A 347 ? SER A 399 TYR A 432 1 ? 34 
HELX_P HELX_P18 AB9 GLY A 348 ? PHE A 373 ? GLY A 433 PHE A 458 1 ? 26 
HELX_P HELX_P19 AC1 PHE A 373 ? LYS A 383 ? PHE A 458 LYS A 468 1 ? 11 
HELX_P HELX_P20 AC2 THR A 387 ? ALA A 406 ? THR A 472 ALA A 491 1 ? 20 
HELX_P HELX_P21 AC3 LEU A 410 ? ALA A 418 ? LEU A 495 ALA A 503 1 ? 9  
HELX_P HELX_P22 AC4 ASP A 423 ? VAL A 436 ? ASP A 508 VAL A 521 1 ? 14 
HELX_P HELX_P23 AC5 VAL A 437 ? GLY A 458 ? VAL A 522 GLY A 543 1 ? 22 
HELX_P HELX_P24 AC6 SER A 463 ? ALA A 505 ? SER A 548 ALA A 590 1 ? 43 
HELX_P HELX_P25 AC7 LYS B 86  ? THR B 90  ? LYS B 86  THR B 90  5 ? 5  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_struct_conn.id                            disulf1 
_struct_conn.conn_type_id                  disulf 
_struct_conn.pdbx_leaving_atom_flag        ? 
_struct_conn.pdbx_PDB_id                   ? 
_struct_conn.ptnr1_label_asym_id           B 
_struct_conn.ptnr1_label_comp_id           CYS 
_struct_conn.ptnr1_label_seq_id            22 
_struct_conn.ptnr1_label_atom_id           SG 
_struct_conn.pdbx_ptnr1_label_alt_id       ? 
_struct_conn.pdbx_ptnr1_PDB_ins_code       ? 
_struct_conn.pdbx_ptnr1_standard_comp_id   ? 
_struct_conn.ptnr1_symmetry                1_555 
_struct_conn.ptnr2_label_asym_id           B 
_struct_conn.ptnr2_label_comp_id           CYS 
_struct_conn.ptnr2_label_seq_id            95 
_struct_conn.ptnr2_label_atom_id           SG 
_struct_conn.pdbx_ptnr2_label_alt_id       ? 
_struct_conn.pdbx_ptnr2_PDB_ins_code       ? 
_struct_conn.ptnr1_auth_asym_id            B 
_struct_conn.ptnr1_auth_comp_id            CYS 
_struct_conn.ptnr1_auth_seq_id             22 
_struct_conn.ptnr2_auth_asym_id            B 
_struct_conn.ptnr2_auth_comp_id            CYS 
_struct_conn.ptnr2_auth_seq_id             95 
_struct_conn.ptnr2_symmetry                1_555 
_struct_conn.pdbx_ptnr3_label_atom_id      ? 
_struct_conn.pdbx_ptnr3_label_seq_id       ? 
_struct_conn.pdbx_ptnr3_label_comp_id      ? 
_struct_conn.pdbx_ptnr3_label_asym_id      ? 
_struct_conn.pdbx_ptnr3_label_alt_id       ? 
_struct_conn.pdbx_ptnr3_PDB_ins_code       ? 
_struct_conn.details                       ? 
_struct_conn.pdbx_dist_value               2.029 
_struct_conn.pdbx_value_order              ? 
_struct_conn.pdbx_role                     ? 
# 
_struct_conn_type.id          disulf 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
_pdbx_modification_feature.ordinal                            1 
_pdbx_modification_feature.label_comp_id                      CYS 
_pdbx_modification_feature.label_asym_id                      B 
_pdbx_modification_feature.label_seq_id                       22 
_pdbx_modification_feature.label_alt_id                       ? 
_pdbx_modification_feature.modified_residue_label_comp_id     CYS 
_pdbx_modification_feature.modified_residue_label_asym_id     B 
_pdbx_modification_feature.modified_residue_label_seq_id      95 
_pdbx_modification_feature.modified_residue_label_alt_id      ? 
_pdbx_modification_feature.auth_comp_id                       CYS 
_pdbx_modification_feature.auth_asym_id                       B 
_pdbx_modification_feature.auth_seq_id                        22 
_pdbx_modification_feature.PDB_ins_code                       ? 
_pdbx_modification_feature.symmetry                           1_555 
_pdbx_modification_feature.modified_residue_auth_comp_id      CYS 
_pdbx_modification_feature.modified_residue_auth_asym_id      B 
_pdbx_modification_feature.modified_residue_auth_seq_id       95 
_pdbx_modification_feature.modified_residue_PDB_ins_code      ? 
_pdbx_modification_feature.modified_residue_symmetry          1_555 
_pdbx_modification_feature.comp_id_linking_atom               SG 
_pdbx_modification_feature.modified_residue_id_linking_atom   SG 
_pdbx_modification_feature.modified_residue_id                . 
_pdbx_modification_feature.ref_pcm_id                         . 
_pdbx_modification_feature.ref_comp_id                        . 
_pdbx_modification_feature.type                               None 
_pdbx_modification_feature.category                           'Disulfide bridge' 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2 ? 
AA2 ? 4 ? 
AA3 ? 6 ? 
AA4 ? 4 ? 
# 
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 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA3 1 2 ? parallel      
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA3 4 5 ? anti-parallel 
AA3 5 6 ? anti-parallel 
AA4 1 2 ? parallel      
AA4 2 3 ? anti-parallel 
AA4 3 4 ? 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 LYS A 19  ? ILE A 20  ? LYS A 104 ILE A 105 
AA1 2 VAL A 23  ? GLU A 24  ? VAL A 108 GLU A 109 
AA2 1 GLN B 3   ? SER B 7   ? GLN B 3   SER B 7   
AA2 2 LEU B 18  ? SER B 25  ? LEU B 18  SER B 25  
AA2 3 THR B 77  ? MET B 82  ? THR B 77  MET B 82  
AA2 4 PHE B 67  ? ASP B 72  ? PHE B 67  ASP B 72  
AA3 1 LEU B 11  ? GLN B 13  ? LEU B 11  GLN B 13  
AA3 2 THR B 114 ? SER B 119 ? THR B 114 SER B 119 
AA3 3 ALA B 91  ? LYS B 98  ? ALA B 91  LYS B 98  
AA3 4 MET B 34  ? GLN B 39  ? MET B 34  GLN B 39  
AA3 5 GLU B 46  ? ILE B 51  ? GLU B 46  ILE B 51  
AA3 6 GLU B 58  ? TYR B 59  ? GLU B 58  TYR B 59  
AA4 1 LEU B 11  ? GLN B 13  ? LEU B 11  GLN B 13  
AA4 2 THR B 114 ? SER B 119 ? THR B 114 SER B 119 
AA4 3 ALA B 91  ? LYS B 98  ? ALA B 91  LYS B 98  
AA4 4 ASP B 108 ? TRP B 110 ? ASP B 108 TRP B 110 
# 
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 ILE A 20  ? N ILE A 105 O VAL A 23  ? O VAL A 108 
AA2 1 2 N VAL B 5   ? N VAL B 5   O ALA B 23  ? O ALA B 23  
AA2 2 3 N LEU B 20  ? N LEU B 20  O LEU B 80  ? O LEU B 80  
AA2 3 4 O THR B 77  ? O THR B 77  N ASP B 72  ? N ASP B 72  
AA3 1 2 N VAL B 12  ? N VAL B 12  O THR B 117 ? O THR B 117 
AA3 2 3 O THR B 114 ? O THR B 114 N TYR B 93  ? N TYR B 93  
AA3 3 4 O VAL B 92  ? O VAL B 92  N GLN B 39  ? N GLN B 39  
AA3 4 5 N TRP B 36  ? N TRP B 36  O VAL B 48  ? O VAL B 48  
AA3 5 6 N ALA B 50  ? N ALA B 50  O GLU B 58  ? O GLU B 58  
AA4 1 2 N VAL B 12  ? N VAL B 12  O THR B 117 ? O THR B 117 
AA4 2 3 O THR B 114 ? O THR B 114 N TYR B 93  ? N TYR B 93  
AA4 3 4 N VAL B 97  ? N VAL B 97  O TYR B 109 ? O TYR B 109 
# 
_pdbx_entry_details.entry_id                   9J3J 
_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 GLU A 150 ? ? -95.23  30.16  
2 1 VAL A 201 ? ? -125.51 -53.68 
3 1 LEU A 205 ? ? -95.83  51.24  
4 1 ALA A 215 ? ? -88.95  45.28  
5 1 ASP A 216 ? ? -131.96 -36.90 
6 1 SER A 254 ? ? -95.22  -61.82 
7 1 ARG A 343 ? ? 176.94  179.86 
8 1 TYR B 107 ? ? 72.19   -12.02 
9 1 SER B 120 ? ? -94.92  52.99  
# 
_em_3d_fitting.id                1 
_em_3d_fitting.entry_id          9J3J 
_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                    9J3J 
_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                  2.83 
_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               405184 
_em_3d_reconstruction.euler_angles_details        ? 
_em_3d_reconstruction.num_class_averages          ? 
_em_3d_reconstruction.refinement_type             ? 
_em_3d_reconstruction.image_processing_id         1 
_em_3d_reconstruction.symmetry_type               POINT 
# 
_em_buffer.id            1 
_em_buffer.specimen_id   1 
_em_buffer.name          ? 
_em_buffer.details       ? 
_em_buffer.pH            7.4 
# 
_em_entity_assembly.id                   1 
_em_entity_assembly.parent_id            0 
_em_entity_assembly.source               'MULTIPLE SOURCES' 
_em_entity_assembly.type                 COMPLEX 
_em_entity_assembly.name                 'Arabidopsis ATP/ADP translocator AtNTT1' 
_em_entity_assembly.details              ? 
_em_entity_assembly.synonym              ? 
_em_entity_assembly.oligomeric_details   ? 
_em_entity_assembly.entity_id_list       '1, 2' 
# 
_em_imaging.entry_id                        9J3J 
_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                            DIFFRACTION 
_em_imaging.nominal_cs                      ? 
_em_imaging.nominal_defocus_min             800 
_em_imaging.nominal_defocus_max             1600 
_em_imaging.calibrated_defocus_min          ? 
_em_imaging.calibrated_defocus_max          ? 
_em_imaging.tilt_angle_min                  ? 
_em_imaging.tilt_angle_max                  ? 
_em_imaging.nominal_magnification           130000 
_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              9J3J 
_em_vitrification.id                    1 
_em_vitrification.specimen_id           1 
_em_vitrification.cryogen_name          NITROGEN 
_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                9J3J 
_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 86  ? A MET 1   
2   1 Y 1 A ALA 87  ? A ALA 2   
3   1 Y 1 A GLY 88  ? A GLY 3   
4   1 Y 1 A ALA 89  ? A ALA 4   
5   1 Y 1 A VAL 90  ? A VAL 5   
6   1 Y 1 A PHE 91  ? A PHE 6   
7   1 Y 1 A GLY 92  ? A GLY 7   
8   1 Y 1 A GLU 93  ? A GLU 8   
9   1 Y 1 A GLY 94  ? A GLY 9   
10  1 Y 1 A ASP 95  ? A ASP 10  
11  1 Y 1 A SER 96  ? A SER 11  
12  1 Y 1 A ALA 97  ? A ALA 12  
13  1 Y 1 A ALA 98  ? A ALA 13  
14  1 Y 1 A VAL 99  ? A VAL 14  
15  1 Y 1 A VAL 100 ? A VAL 15  
16  1 Y 1 A SER 591 ? A SER 506 
17  1 Y 1 A SER 592 ? A SER 507 
18  1 Y 1 A VAL 593 ? A VAL 508 
19  1 Y 1 A LYS 594 ? A LYS 509 
20  1 Y 1 A ILE 595 ? A ILE 510 
21  1 Y 1 A PRO 596 ? A PRO 511 
22  1 Y 1 A VAL 597 ? A VAL 512 
23  1 Y 1 A VAL 598 ? A VAL 513 
24  1 Y 1 A SER 599 ? A SER 514 
25  1 Y 1 A GLN 600 ? A GLN 515 
26  1 Y 1 A ASP 601 ? A ASP 516 
27  1 Y 1 A GLU 602 ? A GLU 517 
28  1 Y 1 A SER 603 ? A SER 518 
29  1 Y 1 A GLY 604 ? A GLY 519 
30  1 Y 1 A ASN 605 ? A ASN 520 
31  1 Y 1 A GLY 606 ? A GLY 521 
32  1 Y 1 A SER 607 ? A SER 522 
33  1 Y 1 A LEU 608 ? A LEU 523 
34  1 Y 1 A GLY 609 ? A GLY 524 
35  1 Y 1 A GLU 610 ? A GLU 525 
36  1 Y 1 A SER 611 ? A SER 526 
37  1 Y 1 A PRO 612 ? A PRO 527 
38  1 Y 1 A SER 613 ? A SER 528 
39  1 Y 1 A SER 614 ? A SER 529 
40  1 Y 1 A SER 615 ? A SER 530 
41  1 Y 1 A PRO 616 ? A PRO 531 
42  1 Y 1 A GLU 617 ? A GLU 532 
43  1 Y 1 A LYS 618 ? A LYS 533 
44  1 Y 1 A SER 619 ? A SER 534 
45  1 Y 1 A ALA 620 ? A ALA 535 
46  1 Y 1 A PRO 621 ? A PRO 536 
47  1 Y 1 A THR 622 ? A THR 537 
48  1 Y 1 A ASN 623 ? A ASN 538 
49  1 Y 1 A LEU 624 ? A LEU 539 
50  1 Y 1 A VAL 625 ? A VAL 540 
51  1 Y 1 A ASP 626 ? A ASP 541 
52  1 Y 1 A GLU 627 ? A GLU 542 
53  1 Y 1 A LEU 628 ? A LEU 543 
54  1 Y 1 A THR 629 ? A THR 544 
55  1 Y 1 A SER 630 ? A SER 545 
56  1 Y 1 A ARG 631 ? A ARG 546 
57  1 Y 1 A GLY 632 ? A GLY 547 
58  1 Y 1 A ARG 633 ? A ARG 548 
59  1 Y 1 A GLY 634 ? A GLY 549 
60  1 Y 1 A SER 635 ? A SER 550 
61  1 Y 1 A GLY 636 ? A GLY 551 
62  1 Y 1 A GLY 637 ? A GLY 552 
63  1 Y 1 A LEU 638 ? A LEU 553 
64  1 Y 1 A ASN 639 ? A ASN 554 
65  1 Y 1 A ASP 640 ? A ASP 555 
66  1 Y 1 A ILE 641 ? A ILE 556 
67  1 Y 1 A PHE 642 ? A PHE 557 
68  1 Y 1 A GLU 643 ? A GLU 558 
69  1 Y 1 A ALA 644 ? A ALA 559 
70  1 Y 1 A GLN 645 ? A GLN 560 
71  1 Y 1 A LYS 646 ? A LYS 561 
72  1 Y 1 A ILE 647 ? A ILE 562 
73  1 Y 1 A GLU 648 ? A GLU 563 
74  1 Y 1 A TRP 649 ? A TRP 564 
75  1 Y 1 A HIS 650 ? A HIS 565 
76  1 Y 1 A GLU 651 ? A GLU 566 
77  1 Y 1 A GLY 652 ? A GLY 567 
78  1 Y 1 A SER 653 ? A SER 568 
79  1 Y 1 A GLY 654 ? A GLY 569 
80  1 Y 1 A LEU 655 ? A LEU 570 
81  1 Y 1 A GLU 656 ? A GLU 571 
82  1 Y 1 A VAL 657 ? A VAL 572 
83  1 Y 1 A LEU 658 ? A LEU 573 
84  1 Y 1 A PHE 659 ? A PHE 574 
85  1 Y 1 A GLN 660 ? A GLN 575 
86  1 Y 1 A GLY 661 ? A GLY 576 
87  1 Y 1 A PRO 662 ? A PRO 577 
88  1 Y 1 A ASP 663 ? A ASP 578 
89  1 Y 1 A TYR 664 ? A TYR 579 
90  1 Y 1 A LYS 665 ? A LYS 580 
91  1 Y 1 A ASP 666 ? A ASP 581 
92  1 Y 1 A ASP 667 ? A ASP 582 
93  1 Y 1 A ASP 668 ? A ASP 583 
94  1 Y 1 A ASP 669 ? A ASP 584 
95  1 Y 1 A LYS 670 ? A LYS 585 
96  1 Y 1 A TRP 671 ? A TRP 586 
97  1 Y 1 A SER 672 ? A SER 587 
98  1 Y 1 A HIS 673 ? A HIS 588 
99  1 Y 1 A PRO 674 ? A PRO 589 
100 1 Y 1 A GLN 675 ? A GLN 590 
101 1 Y 1 A PHE 676 ? A PHE 591 
102 1 Y 1 A GLU 677 ? A GLU 592 
103 1 Y 1 A LYS 678 ? A LYS 593 
104 1 Y 1 A GLY 679 ? A GLY 594 
105 1 Y 1 A GLY 680 ? A GLY 595 
106 1 Y 1 A GLY 681 ? A GLY 596 
107 1 Y 1 A GLY 682 ? A GLY 597 
108 1 Y 1 A SER 683 ? A SER 598 
109 1 Y 1 A GLY 684 ? A GLY 599 
110 1 Y 1 A GLY 685 ? A GLY 600 
111 1 Y 1 A SER 686 ? A SER 601 
112 1 Y 1 A ALA 687 ? A ALA 602 
113 1 Y 1 A TRP 688 ? A TRP 603 
114 1 Y 1 A SER 689 ? A SER 604 
115 1 Y 1 A HIS 690 ? A HIS 605 
116 1 Y 1 A PRO 691 ? A PRO 606 
117 1 Y 1 A GLN 692 ? A GLN 607 
118 1 Y 1 A PHE 693 ? A PHE 608 
119 1 Y 1 A GLU 694 ? A GLU 609 
120 1 Y 1 A LYS 695 ? A LYS 610 
# 
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    2024-08-08 
_em_admin.deposition_site    PDBJ 
_em_admin.entry_id           9J3J 
_em_admin.last_update        2025-05-21 
_em_admin.map_release_date   2025-03-19 
_em_admin.title              'Arabidopsis ATP/ADP translocator AtNTT1' 
# 
_em_ctf_correction.details                  ? 
_em_ctf_correction.em_image_processing_id   1 
_em_ctf_correction.id                       1 
_em_ctf_correction.type                     'PHASE FLIPPING AND AMPLITUDE CORRECTION' 
# 
_em_entity_assembly_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          3701 
_em_entity_assembly_naturalsource.organism             Arabidopsis 
_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         52 
_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  ? ? ? ? ? 
OTHER                      ? 9  ? ? ? ? ? 
'INITIAL EULER ASSIGNMENT' ? 10 1 ? ? ? ? 
'FINAL EULER ASSIGNMENT'   ? 11 1 ? ? ? ? 
CLASSIFICATION             ? 12 1 ? ? ? ? 
RECONSTRUCTION             ? 13 1 ? ? ? ? 
# 
_em_specimen.concentration           ? 
_em_specimen.details                 ? 
_em_specimen.embedding_applied       NO 
_em_specimen.experiment_id           1 
_em_specimen.id                      1 
_em_specimen.shadowing_applied       NO 
_em_specimen.staining_applied        NO 
_em_specimen.vitrification_applied   YES 
# 
_pdbx_audit_support.funding_organization   'Chinese Academy of Sciences' 
_pdbx_audit_support.country                China 
_pdbx_audit_support.grant_number           XDB0630101 
_pdbx_audit_support.ordinal                1 
# 
_atom_sites.entry_id                    9J3J 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   1.000000 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   1.000000 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   0.000000 
_atom_sites.fract_transf_matrix[3][3]   1.000000 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM 1    N N   . ALA A 1 16  ? 126.661 151.626 76.999  1.00 138.64 ? 101 ALA A N   1 
ATOM 2    C CA  . ALA A 1 16  ? 126.550 151.599 78.452  1.00 141.10 ? 101 ALA A CA  1 
ATOM 3    C C   . ALA A 1 16  ? 125.133 151.242 78.884  1.00 144.37 ? 101 ALA A C   1 
ATOM 4    O O   . ALA A 1 16  ? 124.262 152.108 78.965  1.00 144.42 ? 101 ALA A O   1 
ATOM 5    C CB  . ALA A 1 16  ? 126.964 152.939 79.042  1.00 134.18 ? 101 ALA A CB  1 
ATOM 6    N N   . SER A 1 17  ? 124.911 149.960 79.160  1.00 143.09 ? 102 SER A N   1 
ATOM 7    C CA  . SER A 1 17  ? 123.609 149.514 79.622  1.00 142.78 ? 102 SER A CA  1 
ATOM 8    C C   . SER A 1 17  ? 123.316 150.098 81.004  1.00 142.56 ? 102 SER A C   1 
ATOM 9    O O   . SER A 1 17  ? 124.238 150.377 81.776  1.00 140.88 ? 102 SER A O   1 
ATOM 10   C CB  . SER A 1 17  ? 123.557 147.989 79.677  1.00 141.17 ? 102 SER A CB  1 
ATOM 11   O OG  . SER A 1 17  ? 123.722 147.425 78.388  1.00 138.26 ? 102 SER A OG  1 
ATOM 12   N N   . PRO A 1 18  ? 122.041 150.301 81.336  1.00 141.05 ? 103 PRO A N   1 
ATOM 13   C CA  . PRO A 1 18  ? 121.709 150.851 82.655  1.00 140.02 ? 103 PRO A CA  1 
ATOM 14   C C   . PRO A 1 18  ? 122.152 149.914 83.767  1.00 137.61 ? 103 PRO A C   1 
ATOM 15   O O   . PRO A 1 18  ? 122.332 148.712 83.557  1.00 135.92 ? 103 PRO A O   1 
ATOM 16   C CB  . PRO A 1 18  ? 120.182 150.993 82.610  1.00 138.36 ? 103 PRO A CB  1 
ATOM 17   C CG  . PRO A 1 18  ? 119.744 150.022 81.562  1.00 137.61 ? 103 PRO A CG  1 
ATOM 18   C CD  . PRO A 1 18  ? 120.835 150.030 80.534  1.00 138.60 ? 103 PRO A CD  1 
ATOM 19   N N   . LYS A 1 19  ? 122.377 150.485 84.947  1.00 135.82 ? 104 LYS A N   1 
ATOM 20   C CA  . LYS A 1 19  ? 122.781 149.725 86.123  1.00 130.18 ? 104 LYS A CA  1 
ATOM 21   C C   . LYS A 1 19  ? 121.916 150.142 87.303  1.00 132.26 ? 104 LYS A C   1 
ATOM 22   O O   . LYS A 1 19  ? 121.881 151.324 87.664  1.00 133.12 ? 104 LYS A O   1 
ATOM 23   C CB  . LYS A 1 19  ? 124.264 149.941 86.437  1.00 127.44 ? 104 LYS A CB  1 
ATOM 24   C CG  . LYS A 1 19  ? 125.214 149.313 85.427  1.00 126.07 ? 104 LYS A CG  1 
ATOM 25   C CD  . LYS A 1 19  ? 126.664 149.652 85.740  1.00 126.64 ? 104 LYS A CD  1 
ATOM 26   C CE  . LYS A 1 19  ? 127.141 148.940 86.996  1.00 128.10 ? 104 LYS A CE  1 
ATOM 27   N NZ  . LYS A 1 19  ? 128.591 149.166 87.250  1.00 127.91 ? 104 LYS A NZ  1 
ATOM 28   N N   . ILE A 1 20  ? 121.223 149.175 87.899  1.00 133.02 ? 105 ILE A N   1 
ATOM 29   C CA  . ILE A 1 20  ? 120.440 149.384 89.112  1.00 133.34 ? 105 ILE A CA  1 
ATOM 30   C C   . ILE A 1 20  ? 121.165 148.719 90.272  1.00 134.78 ? 105 ILE A C   1 
ATOM 31   O O   . ILE A 1 20  ? 121.657 147.591 90.145  1.00 132.79 ? 105 ILE A O   1 
ATOM 32   C CB  . ILE A 1 20  ? 119.000 148.847 88.980  1.00 131.70 ? 105 ILE A CB  1 
ATOM 33   C CG1 . ILE A 1 20  ? 118.229 149.605 87.896  1.00 134.03 ? 105 ILE A CG1 1 
ATOM 34   C CG2 . ILE A 1 20  ? 118.264 148.929 90.309  1.00 127.74 ? 105 ILE A CG2 1 
ATOM 35   C CD1 . ILE A 1 20  ? 118.284 148.976 86.533  1.00 131.91 ? 105 ILE A CD1 1 
ATOM 36   N N   . PHE A 1 21  ? 121.247 149.433 91.396  1.00 136.51 ? 106 PHE A N   1 
ATOM 37   C CA  . PHE A 1 21  ? 121.895 148.963 92.619  1.00 137.33 ? 106 PHE A CA  1 
ATOM 38   C C   . PHE A 1 21  ? 123.388 148.715 92.403  1.00 136.60 ? 106 PHE A C   1 
ATOM 39   O O   . PHE A 1 21  ? 124.012 147.932 93.124  1.00 139.67 ? 106 PHE A O   1 
ATOM 40   C CB  . PHE A 1 21  ? 121.187 147.709 93.161  1.00 136.64 ? 106 PHE A CB  1 
ATOM 41   C CG  . PHE A 1 21  ? 121.618 147.300 94.544  1.00 138.86 ? 106 PHE A CG  1 
ATOM 42   C CD1 . PHE A 1 21  ? 121.270 148.069 95.642  1.00 136.62 ? 106 PHE A CD1 1 
ATOM 43   C CD2 . PHE A 1 21  ? 122.332 146.130 94.751  1.00 138.25 ? 106 PHE A CD2 1 
ATOM 44   C CE1 . PHE A 1 21  ? 121.651 147.697 96.917  1.00 133.21 ? 106 PHE A CE1 1 
ATOM 45   C CE2 . PHE A 1 21  ? 122.717 145.753 96.024  1.00 135.23 ? 106 PHE A CE2 1 
ATOM 46   C CZ  . PHE A 1 21  ? 122.375 146.537 97.108  1.00 132.07 ? 106 PHE A CZ  1 
ATOM 47   N N   . GLY A 1 22  ? 123.981 149.389 91.419  1.00 132.84 ? 107 GLY A N   1 
ATOM 48   C CA  . GLY A 1 22  ? 125.382 149.201 91.107  1.00 133.09 ? 107 GLY A CA  1 
ATOM 49   C C   . GLY A 1 22  ? 125.702 147.943 90.334  1.00 130.88 ? 107 GLY A C   1 
ATOM 50   O O   . GLY A 1 22  ? 126.883 147.605 90.195  1.00 129.14 ? 107 GLY A O   1 
ATOM 51   N N   . VAL A 1 23  ? 124.692 147.239 89.828  1.00 129.51 ? 108 VAL A N   1 
ATOM 52   C CA  . VAL A 1 23  ? 124.873 145.993 89.094  1.00 128.32 ? 108 VAL A CA  1 
ATOM 53   C C   . VAL A 1 23  ? 124.235 146.144 87.721  1.00 127.23 ? 108 VAL A C   1 
ATOM 54   O O   . VAL A 1 23  ? 123.170 146.757 87.586  1.00 126.21 ? 108 VAL A O   1 
ATOM 55   C CB  . VAL A 1 23  ? 124.266 144.793 89.852  1.00 122.24 ? 108 VAL A CB  1 
ATOM 56   C CG1 . VAL A 1 23  ? 124.642 143.484 89.172  1.00 107.02 ? 108 VAL A CG1 1 
ATOM 57   C CG2 . VAL A 1 23  ? 124.717 144.794 91.305  1.00 119.38 ? 108 VAL A CG2 1 
ATOM 58   N N   . GLU A 1 24  ? 124.892 145.591 86.704  1.00 126.14 ? 109 GLU A N   1 
ATOM 59   C CA  . GLU A 1 24  ? 124.377 145.668 85.343  1.00 120.06 ? 109 GLU A CA  1 
ATOM 60   C C   . GLU A 1 24  ? 123.040 144.944 85.232  1.00 111.47 ? 109 GLU A C   1 
ATOM 61   O O   . GLU A 1 24  ? 122.798 143.944 85.915  1.00 106.72 ? 109 GLU A O   1 
ATOM 62   C CB  . GLU A 1 24  ? 125.386 145.070 84.360  1.00 118.02 ? 109 GLU A CB  1 
ATOM 63   C CG  . GLU A 1 24  ? 126.683 145.861 84.226  1.00 127.60 ? 109 GLU A CG  1 
ATOM 64   C CD  . GLU A 1 24  ? 127.684 145.544 85.322  1.00 132.40 ? 109 GLU A CD  1 
ATOM 65   O OE1 . GLU A 1 24  ? 127.398 144.661 86.158  1.00 130.94 ? 109 GLU A OE1 1 
ATOM 66   O OE2 . GLU A 1 24  ? 128.759 146.180 85.348  1.00 134.62 ? 109 GLU A OE2 1 
ATOM 67   N N   . VAL A 1 25  ? 122.166 145.461 84.363  1.00 111.70 ? 110 VAL A N   1 
ATOM 68   C CA  . VAL A 1 25  ? 120.827 144.894 84.214  1.00 104.13 ? 110 VAL A CA  1 
ATOM 69   C C   . VAL A 1 25  ? 120.887 143.465 83.694  1.00 99.72  ? 110 VAL A C   1 
ATOM 70   O O   . VAL A 1 25  ? 120.035 142.642 84.038  1.00 97.59  ? 110 VAL A O   1 
ATOM 71   C CB  . VAL A 1 25  ? 119.958 145.789 83.305  1.00 107.61 ? 110 VAL A CB  1 
ATOM 72   C CG1 . VAL A 1 25  ? 118.598 145.152 83.060  1.00 101.95 ? 110 VAL A CG1 1 
ATOM 73   C CG2 . VAL A 1 25  ? 119.765 147.142 83.939  1.00 117.35 ? 110 VAL A CG2 1 
ATOM 74   N N   . ALA A 1 26  ? 121.875 143.142 82.856  1.00 100.04 ? 111 ALA A N   1 
ATOM 75   C CA  . ALA A 1 26  ? 121.980 141.776 82.348  1.00 95.24  ? 111 ALA A CA  1 
ATOM 76   C C   . ALA A 1 26  ? 122.345 140.794 83.457  1.00 94.41  ? 111 ALA A C   1 
ATOM 77   O O   . ALA A 1 26  ? 121.735 139.722 83.577  1.00 93.37  ? 111 ALA A O   1 
ATOM 78   C CB  . ALA A 1 26  ? 123.007 141.716 81.217  1.00 92.65  ? 111 ALA A CB  1 
ATOM 79   N N   . THR A 1 27  ? 123.335 141.143 84.281  1.00 96.08  ? 112 THR A N   1 
ATOM 80   C CA  . THR A 1 27  ? 123.687 140.288 85.409  1.00 91.03  ? 112 THR A CA  1 
ATOM 81   C C   . THR A 1 27  ? 122.530 140.190 86.394  1.00 89.26  ? 112 THR A C   1 
ATOM 82   O O   . THR A 1 27  ? 122.266 139.120 86.954  1.00 87.02  ? 112 THR A O   1 
ATOM 83   C CB  . THR A 1 27  ? 124.943 140.823 86.099  1.00 93.31  ? 112 THR A CB  1 
ATOM 84   O OG1 . THR A 1 27  ? 126.030 140.841 85.165  1.00 95.22  ? 112 THR A OG1 1 
ATOM 85   C CG2 . THR A 1 27  ? 125.321 139.939 87.271  1.00 85.97  ? 112 THR A CG2 1 
ATOM 86   N N   . LEU A 1 28  ? 121.820 141.299 86.607  1.00 91.87  ? 113 LEU A N   1 
ATOM 87   C CA  . LEU A 1 28  ? 120.661 141.290 87.491  1.00 87.93  ? 113 LEU A CA  1 
ATOM 88   C C   . LEU A 1 28  ? 119.578 140.364 86.944  1.00 82.21  ? 113 LEU A C   1 
ATOM 89   O O   . LEU A 1 28  ? 118.943 139.609 87.694  1.00 81.40  ? 113 LEU A O   1 
ATOM 90   C CB  . LEU A 1 28  ? 120.134 142.719 87.635  1.00 88.25  ? 113 LEU A CB  1 
ATOM 91   C CG  . LEU A 1 28  ? 118.820 142.955 88.364  1.00 86.33  ? 113 LEU A CG  1 
ATOM 92   C CD1 . LEU A 1 28  ? 118.956 142.313 89.723  1.00 86.38  ? 113 LEU A CD1 1 
ATOM 93   C CD2 . LEU A 1 28  ? 118.485 144.435 88.484  1.00 95.26  ? 113 LEU A CD2 1 
ATOM 94   N N   . LYS A 1 29  ? 119.367 140.414 85.626  1.00 83.61  ? 114 LYS A N   1 
ATOM 95   C CA  . LYS A 1 29  ? 118.395 139.593 84.914  1.00 79.72  ? 114 LYS A CA  1 
ATOM 96   C C   . LYS A 1 29  ? 118.763 138.119 84.929  1.00 78.21  ? 114 LYS A C   1 
ATOM 97   O O   . LYS A 1 29  ? 117.880 137.269 84.787  1.00 81.05  ? 114 LYS A O   1 
ATOM 98   C CB  . LYS A 1 29  ? 118.286 140.076 83.464  1.00 81.62  ? 114 LYS A CB  1 
ATOM 99   C CG  . LYS A 1 29  ? 117.144 139.482 82.656  1.00 85.08  ? 114 LYS A CG  1 
ATOM 100  C CD  . LYS A 1 29  ? 117.169 140.003 81.225  1.00 86.86  ? 114 LYS A CD  1 
ATOM 101  C CE  . LYS A 1 29  ? 116.721 141.453 81.144  1.00 90.85  ? 114 LYS A CE  1 
ATOM 102  N NZ  . LYS A 1 29  ? 116.626 141.924 79.733  1.00 86.67  ? 114 LYS A NZ  1 
ATOM 103  N N   . LYS A 1 30  ? 120.049 137.800 85.045  1.00 78.54  ? 115 LYS A N   1 
ATOM 104  C CA  . LYS A 1 30  ? 120.450 136.407 85.191  1.00 75.87  ? 115 LYS A CA  1 
ATOM 105  C C   . LYS A 1 30  ? 120.473 135.942 86.642  1.00 70.75  ? 115 LYS A C   1 
ATOM 106  O O   . LYS A 1 30  ? 120.385 134.734 86.891  1.00 68.04  ? 115 LYS A O   1 
ATOM 107  C CB  . LYS A 1 30  ? 121.828 136.171 84.561  1.00 76.23  ? 115 LYS A CB  1 
ATOM 108  C CG  . LYS A 1 30  ? 122.994 136.316 85.523  1.00 80.00  ? 115 LYS A CG  1 
ATOM 109  C CD  . LYS A 1 30  ? 124.321 136.240 84.793  1.00 80.97  ? 115 LYS A CD  1 
ATOM 110  C CE  . LYS A 1 30  ? 124.580 134.832 84.285  1.00 71.99  ? 115 LYS A CE  1 
ATOM 111  N NZ  . LYS A 1 30  ? 125.933 134.695 83.681  1.00 69.24  ? 115 LYS A NZ  1 
ATOM 112  N N   . ILE A 1 31  ? 120.581 136.862 87.599  1.00 74.76  ? 116 ILE A N   1 
ATOM 113  C CA  . ILE A 1 31  ? 120.731 136.474 88.999  1.00 66.33  ? 116 ILE A CA  1 
ATOM 114  C C   . ILE A 1 31  ? 119.386 136.379 89.716  1.00 67.55  ? 116 ILE A C   1 
ATOM 115  O O   . ILE A 1 31  ? 119.170 135.448 90.497  1.00 67.15  ? 116 ILE A O   1 
ATOM 116  C CB  . ILE A 1 31  ? 121.695 137.443 89.715  1.00 66.54  ? 116 ILE A CB  1 
ATOM 117  C CG1 . ILE A 1 31  ? 123.135 137.178 89.268  1.00 68.97  ? 116 ILE A CG1 1 
ATOM 118  C CG2 . ILE A 1 31  ? 121.582 137.308 91.225  1.00 65.03  ? 116 ILE A CG2 1 
ATOM 119  C CD1 . ILE A 1 31  ? 123.657 135.812 89.664  1.00 66.36  ? 116 ILE A CD1 1 
ATOM 120  N N   . ILE A 1 32  ? 118.456 137.318 89.486  1.00 69.98  ? 117 ILE A N   1 
ATOM 121  C CA  . ILE A 1 32  ? 117.142 137.223 90.135  1.00 62.72  ? 117 ILE A CA  1 
ATOM 122  C C   . ILE A 1 32  ? 116.430 135.912 89.823  1.00 65.21  ? 117 ILE A C   1 
ATOM 123  O O   . ILE A 1 32  ? 115.937 135.267 90.762  1.00 67.67  ? 117 ILE A O   1 
ATOM 124  C CB  . ILE A 1 32  ? 116.279 138.452 89.792  1.00 62.90  ? 117 ILE A CB  1 
ATOM 125  C CG1 . ILE A 1 32  ? 116.839 139.720 90.425  1.00 66.17  ? 117 ILE A CG1 1 
ATOM 126  C CG2 . ILE A 1 32  ? 114.835 138.228 90.228  1.00 63.69  ? 117 ILE A CG2 1 
ATOM 127  C CD1 . ILE A 1 32  ? 115.868 140.886 90.357  1.00 76.55  ? 117 ILE A CD1 1 
ATOM 128  N N   . PRO A 1 33  ? 116.313 135.473 88.564  1.00 63.02  ? 118 PRO A N   1 
ATOM 129  C CA  . PRO A 1 33  ? 115.699 134.158 88.328  1.00 57.86  ? 118 PRO A CA  1 
ATOM 130  C C   . PRO A 1 33  ? 116.460 133.016 88.975  1.00 59.52  ? 118 PRO A C   1 
ATOM 131  O O   . PRO A 1 33  ? 115.832 132.052 89.420  1.00 58.31  ? 118 PRO A O   1 
ATOM 132  C CB  . PRO A 1 33  ? 115.685 134.046 86.799  1.00 59.87  ? 118 PRO A CB  1 
ATOM 133  C CG  . PRO A 1 33  ? 115.719 135.448 86.321  1.00 62.08  ? 118 PRO A CG  1 
ATOM 134  C CD  . PRO A 1 33  ? 116.604 136.158 87.294  1.00 65.24  ? 118 PRO A CD  1 
ATOM 135  N N   . LEU A 1 34  ? 117.791 133.097 89.058  1.00 58.47  ? 119 LEU A N   1 
ATOM 136  C CA  . LEU A 1 34  ? 118.546 132.064 89.764  1.00 52.58  ? 119 LEU A CA  1 
ATOM 137  C C   . LEU A 1 34  ? 118.206 132.046 91.249  1.00 54.82  ? 119 LEU A C   1 
ATOM 138  O O   . LEU A 1 34  ? 118.018 130.974 91.838  1.00 60.06  ? 119 LEU A O   1 
ATOM 139  C CB  . LEU A 1 34  ? 120.046 132.279 89.568  1.00 50.56  ? 119 LEU A CB  1 
ATOM 140  C CG  . LEU A 1 34  ? 120.705 131.649 88.342  1.00 55.25  ? 119 LEU A CG  1 
ATOM 141  C CD1 . LEU A 1 34  ? 122.217 131.752 88.464  1.00 53.34  ? 119 LEU A CD1 1 
ATOM 142  C CD2 . LEU A 1 34  ? 120.269 130.202 88.174  1.00 52.91  ? 119 LEU A CD2 1 
ATOM 143  N N   . GLY A 1 35  ? 118.131 133.224 91.872  1.00 53.30  ? 120 GLY A N   1 
ATOM 144  C CA  . GLY A 1 35  ? 117.749 133.284 93.273  1.00 51.40  ? 120 GLY A CA  1 
ATOM 145  C C   . GLY A 1 35  ? 116.345 132.767 93.510  1.00 56.06  ? 120 GLY A C   1 
ATOM 146  O O   . GLY A 1 35  ? 116.090 132.064 94.490  1.00 59.54  ? 120 GLY A O   1 
ATOM 147  N N   . LEU A 1 36  ? 115.416 133.104 92.612  1.00 55.69  ? 121 LEU A N   1 
ATOM 148  C CA  . LEU A 1 36  ? 114.055 132.590 92.719  1.00 51.15  ? 121 LEU A CA  1 
ATOM 149  C C   . LEU A 1 36  ? 114.023 131.075 92.551  1.00 53.78  ? 121 LEU A C   1 
ATOM 150  O O   . LEU A 1 36  ? 113.291 130.381 93.267  1.00 58.72  ? 121 LEU A O   1 
ATOM 151  C CB  . LEU A 1 36  ? 113.159 133.267 91.683  1.00 53.27  ? 121 LEU A CB  1 
ATOM 152  C CG  . LEU A 1 36  ? 112.809 134.735 91.939  1.00 55.22  ? 121 LEU A CG  1 
ATOM 153  C CD1 . LEU A 1 36  ? 112.375 135.416 90.650  1.00 61.96  ? 121 LEU A CD1 1 
ATOM 154  C CD2 . LEU A 1 36  ? 111.729 134.854 93.003  1.00 60.81  ? 121 LEU A CD2 1 
ATOM 155  N N   . MET A 1 37  ? 114.810 130.546 91.610  1.00 52.52  ? 122 MET A N   1 
ATOM 156  C CA  . MET A 1 37  ? 114.895 129.101 91.431  1.00 50.51  ? 122 MET A CA  1 
ATOM 157  C C   . MET A 1 37  ? 115.403 128.423 92.691  1.00 49.51  ? 122 MET A C   1 
ATOM 158  O O   . MET A 1 37  ? 114.865 127.395 93.109  1.00 56.36  ? 122 MET A O   1 
ATOM 159  C CB  . MET A 1 37  ? 115.813 128.764 90.255  1.00 51.95  ? 122 MET A CB  1 
ATOM 160  C CG  . MET A 1 37  ? 115.209 128.994 88.888  1.00 52.88  ? 122 MET A CG  1 
ATOM 161  S SD  . MET A 1 37  ? 116.229 128.333 87.556  1.00 67.75  ? 122 MET A SD  1 
ATOM 162  C CE  . MET A 1 37  ? 116.959 126.906 88.356  1.00 53.77  ? 122 MET A CE  1 
ATOM 163  N N   . PHE A 1 38  ? 116.442 128.984 93.309  1.00 46.41  ? 123 PHE A N   1 
ATOM 164  C CA  . PHE A 1 38  ? 117.016 128.355 94.494  1.00 44.92  ? 123 PHE A CA  1 
ATOM 165  C C   . PHE A 1 38  ? 116.058 128.462 95.677  1.00 47.59  ? 123 PHE A C   1 
ATOM 166  O O   . PHE A 1 38  ? 115.928 127.518 96.469  1.00 55.26  ? 123 PHE A O   1 
ATOM 167  C CB  . PHE A 1 38  ? 118.372 128.994 94.794  1.00 49.74  ? 123 PHE A CB  1 
ATOM 168  C CG  . PHE A 1 38  ? 119.187 128.265 95.821  1.00 49.96  ? 123 PHE A CG  1 
ATOM 169  C CD1 . PHE A 1 38  ? 119.407 126.902 95.704  1.00 53.71  ? 123 PHE A CD1 1 
ATOM 170  C CD2 . PHE A 1 38  ? 119.820 128.952 96.839  1.00 47.68  ? 123 PHE A CD2 1 
ATOM 171  C CE1 . PHE A 1 38  ? 120.185 126.228 96.623  1.00 55.27  ? 123 PHE A CE1 1 
ATOM 172  C CE2 . PHE A 1 38  ? 120.607 128.283 97.755  1.00 50.86  ? 123 PHE A CE2 1 
ATOM 173  C CZ  . PHE A 1 38  ? 120.788 126.920 97.649  1.00 56.07  ? 123 PHE A CZ  1 
ATOM 174  N N   . PHE A 1 39  ? 115.352 129.592 95.783  1.00 50.10  ? 124 PHE A N   1 
ATOM 175  C CA  . PHE A 1 39  ? 114.294 129.739 96.778  1.00 48.46  ? 124 PHE A CA  1 
ATOM 176  C C   . PHE A 1 39  ? 113.233 128.658 96.619  1.00 54.35  ? 124 PHE A C   1 
ATOM 177  O O   . PHE A 1 39  ? 112.870 127.986 97.589  1.00 60.28  ? 124 PHE A O   1 
ATOM 178  C CB  . PHE A 1 39  ? 113.664 131.130 96.660  1.00 48.28  ? 124 PHE A CB  1 
ATOM 179  C CG  . PHE A 1 39  ? 112.532 131.374 97.623  1.00 49.43  ? 124 PHE A CG  1 
ATOM 180  C CD1 . PHE A 1 39  ? 112.772 131.900 98.881  1.00 49.21  ? 124 PHE A CD1 1 
ATOM 181  C CD2 . PHE A 1 39  ? 111.224 131.089 97.262  1.00 48.95  ? 124 PHE A CD2 1 
ATOM 182  C CE1 . PHE A 1 39  ? 111.730 132.128 99.763  1.00 53.18  ? 124 PHE A CE1 1 
ATOM 183  C CE2 . PHE A 1 39  ? 110.181 131.311 98.139  1.00 51.25  ? 124 PHE A CE2 1 
ATOM 184  C CZ  . PHE A 1 39  ? 110.434 131.832 99.391  1.00 53.96  ? 124 PHE A CZ  1 
ATOM 185  N N   . CYS A 1 40  ? 112.716 128.484 95.400  1.00 51.67  ? 125 CYS A N   1 
ATOM 186  C CA  . CYS A 1 40  ? 111.675 127.485 95.174  1.00 46.74  ? 125 CYS A CA  1 
ATOM 187  C C   . CYS A 1 40  ? 112.198 126.075 95.421  1.00 49.03  ? 125 CYS A C   1 
ATOM 188  O O   . CYS A 1 40  ? 111.491 125.229 95.986  1.00 57.56  ? 125 CYS A O   1 
ATOM 189  C CB  . CYS A 1 40  ? 111.123 127.610 93.753  1.00 50.17  ? 125 CYS A CB  1 
ATOM 190  S SG  . CYS A 1 40  ? 110.416 129.225 93.352  1.00 69.23  ? 125 CYS A SG  1 
ATOM 191  N N   . ILE A 1 41  ? 113.437 125.807 95.005  1.00 48.23  ? 126 ILE A N   1 
ATOM 192  C CA  . ILE A 1 41  ? 114.013 124.476 95.163  1.00 46.27  ? 126 ILE A CA  1 
ATOM 193  C C   . ILE A 1 41  ? 114.134 124.121 96.637  1.00 48.53  ? 126 ILE A C   1 
ATOM 194  O O   . ILE A 1 41  ? 113.759 123.023 97.057  1.00 53.19  ? 126 ILE A O   1 
ATOM 195  C CB  . ILE A 1 41  ? 115.370 124.390 94.442  1.00 45.16  ? 126 ILE A CB  1 
ATOM 196  C CG1 . ILE A 1 41  ? 115.158 124.261 92.933  1.00 47.12  ? 126 ILE A CG1 1 
ATOM 197  C CG2 . ILE A 1 41  ? 116.182 123.220 94.962  1.00 49.83  ? 126 ILE A CG2 1 
ATOM 198  C CD1 . ILE A 1 41  ? 116.422 124.051 92.147  1.00 42.83  ? 126 ILE A CD1 1 
ATOM 199  N N   . LEU A 1 42  ? 114.633 125.051 97.455  1.00 47.87  ? 127 LEU A N   1 
ATOM 200  C CA  . LEU A 1 42  ? 114.748 124.743 98.878  1.00 46.01  ? 127 LEU A CA  1 
ATOM 201  C C   . LEU A 1 42  ? 113.407 124.800 99.601  1.00 49.72  ? 127 LEU A C   1 
ATOM 202  O O   . LEU A 1 42  ? 113.232 124.116 100.614 1.00 55.46  ? 127 LEU A O   1 
ATOM 203  C CB  . LEU A 1 42  ? 115.760 125.669 99.547  1.00 45.49  ? 127 LEU A CB  1 
ATOM 204  C CG  . LEU A 1 42  ? 117.186 125.323 99.123  1.00 48.06  ? 127 LEU A CG  1 
ATOM 205  C CD1 . LEU A 1 42  ? 118.164 126.264 99.762  1.00 50.96  ? 127 LEU A CD1 1 
ATOM 206  C CD2 . LEU A 1 42  ? 117.518 123.883 99.480  1.00 56.18  ? 127 LEU A CD2 1 
ATOM 207  N N   . PHE A 1 43  ? 112.453 125.588 99.102  1.00 47.09  ? 128 PHE A N   1 
ATOM 208  C CA  . PHE A 1 43  ? 111.089 125.525 99.614  1.00 46.05  ? 128 PHE A CA  1 
ATOM 209  C C   . PHE A 1 43  ? 110.531 124.115 99.470  1.00 53.60  ? 128 PHE A C   1 
ATOM 210  O O   . PHE A 1 43  ? 110.059 123.507 100.444 1.00 57.09  ? 128 PHE A O   1 
ATOM 211  C CB  . PHE A 1 43  ? 110.225 126.536 98.855  1.00 44.72  ? 128 PHE A CB  1 
ATOM 212  C CG  . PHE A 1 43  ? 109.014 127.005 99.608  1.00 50.50  ? 128 PHE A CG  1 
ATOM 213  C CD1 . PHE A 1 43  ? 107.832 126.288 99.565  1.00 49.61  ? 128 PHE A CD1 1 
ATOM 214  C CD2 . PHE A 1 43  ? 109.053 128.181 100.338 1.00 51.92  ? 128 PHE A CD2 1 
ATOM 215  C CE1 . PHE A 1 43  ? 106.714 126.728 100.250 1.00 47.85  ? 128 PHE A CE1 1 
ATOM 216  C CE2 . PHE A 1 43  ? 107.939 128.625 101.025 1.00 51.45  ? 128 PHE A CE2 1 
ATOM 217  C CZ  . PHE A 1 43  ? 106.769 127.896 100.980 1.00 48.01  ? 128 PHE A CZ  1 
ATOM 218  N N   . ASN A 1 44  ? 110.615 123.568 98.254  1.00 52.07  ? 129 ASN A N   1 
ATOM 219  C CA  . ASN A 1 44  ? 110.197 122.190 98.024  1.00 45.42  ? 129 ASN A CA  1 
ATOM 220  C C   . ASN A 1 44  ? 111.030 121.216 98.845  1.00 47.83  ? 129 ASN A C   1 
ATOM 221  O O   . ASN A 1 44  ? 110.504 120.226 99.361  1.00 55.80  ? 129 ASN A O   1 
ATOM 222  C CB  . ASN A 1 44  ? 110.292 121.853 96.536  1.00 46.00  ? 129 ASN A CB  1 
ATOM 223  C CG  . ASN A 1 44  ? 109.162 122.455 95.733  1.00 54.69  ? 129 ASN A CG  1 
ATOM 224  O OD1 . ASN A 1 44  ? 108.455 123.341 96.208  1.00 58.05  ? 129 ASN A OD1 1 
ATOM 225  N ND2 . ASN A 1 44  ? 108.987 121.978 94.505  1.00 56.00  ? 129 ASN A ND2 1 
ATOM 226  N N   . TYR A 1 45  ? 112.333 121.476 98.971  1.00 49.45  ? 130 TYR A N   1 
ATOM 227  C CA  . TYR A 1 45  ? 113.199 120.573 99.719  1.00 50.02  ? 130 TYR A CA  1 
ATOM 228  C C   . TYR A 1 45  ? 112.768 120.471 101.175 1.00 50.86  ? 130 TYR A C   1 
ATOM 229  O O   . TYR A 1 45  ? 112.677 119.370 101.720 1.00 56.37  ? 130 TYR A O   1 
ATOM 230  C CB  . TYR A 1 45  ? 114.653 121.035 99.621  1.00 50.82  ? 130 TYR A CB  1 
ATOM 231  C CG  . TYR A 1 45  ? 115.602 120.257 100.506 1.00 53.76  ? 130 TYR A CG  1 
ATOM 232  C CD1 . TYR A 1 45  ? 115.567 118.869 100.546 1.00 56.09  ? 130 TYR A CD1 1 
ATOM 233  C CD2 . TYR A 1 45  ? 116.535 120.911 101.300 1.00 59.75  ? 130 TYR A CD2 1 
ATOM 234  C CE1 . TYR A 1 45  ? 116.430 118.155 101.356 1.00 63.07  ? 130 TYR A CE1 1 
ATOM 235  C CE2 . TYR A 1 45  ? 117.404 120.205 102.111 1.00 64.53  ? 130 TYR A CE2 1 
ATOM 236  C CZ  . TYR A 1 45  ? 117.347 118.828 102.134 1.00 66.72  ? 130 TYR A CZ  1 
ATOM 237  O OH  . TYR A 1 45  ? 118.210 118.120 102.939 1.00 76.63  ? 130 TYR A OH  1 
ATOM 238  N N   . THR A 1 46  ? 112.487 121.605 101.817 1.00 50.88  ? 131 THR A N   1 
ATOM 239  C CA  . THR A 1 46  ? 112.044 121.570 103.208 1.00 48.53  ? 131 THR A CA  1 
ATOM 240  C C   . THR A 1 46  ? 110.666 120.928 103.333 1.00 47.22  ? 131 THR A C   1 
ATOM 241  O O   . THR A 1 46  ? 110.435 120.108 104.239 1.00 57.14  ? 131 THR A O   1 
ATOM 242  C CB  . THR A 1 46  ? 112.037 122.980 103.797 1.00 54.93  ? 131 THR A CB  1 
ATOM 243  O OG1 . THR A 1 46  ? 113.233 123.668 103.410 1.00 57.16  ? 131 THR A OG1 1 
ATOM 244  C CG2 . THR A 1 46  ? 111.957 122.924 105.315 1.00 55.12  ? 131 THR A CG2 1 
ATOM 245  N N   . ILE A 1 47  ? 109.741 121.275 102.429 1.00 49.24  ? 132 ILE A N   1 
ATOM 246  C CA  . ILE A 1 47  ? 108.404 120.686 102.486 1.00 47.91  ? 132 ILE A CA  1 
ATOM 247  C C   . ILE A 1 47  ? 108.491 119.169 102.394 1.00 49.46  ? 132 ILE A C   1 
ATOM 248  O O   . ILE A 1 47  ? 107.885 118.446 103.193 1.00 56.68  ? 132 ILE A O   1 
ATOM 249  C CB  . ILE A 1 47  ? 107.504 121.265 101.379 1.00 50.68  ? 132 ILE A CB  1 
ATOM 250  C CG1 . ILE A 1 47  ? 106.993 122.652 101.768 1.00 50.87  ? 132 ILE A CG1 1 
ATOM 251  C CG2 . ILE A 1 47  ? 106.330 120.339 101.107 1.00 52.05  ? 132 ILE A CG2 1 
ATOM 252  C CD1 . ILE A 1 47  ? 106.168 123.314 100.689 1.00 55.96  ? 132 ILE A CD1 1 
ATOM 253  N N   . LEU A 1 48  ? 109.269 118.664 101.435 1.00 50.90  ? 133 LEU A N   1 
ATOM 254  C CA  . LEU A 1 48  ? 109.401 117.221 101.262 1.00 45.09  ? 133 LEU A CA  1 
ATOM 255  C C   . LEU A 1 48  ? 110.174 116.589 102.411 1.00 47.15  ? 133 LEU A C   1 
ATOM 256  O O   . LEU A 1 48  ? 109.838 115.487 102.854 1.00 56.28  ? 133 LEU A O   1 
ATOM 257  C CB  . LEU A 1 48  ? 110.078 116.917 99.927  1.00 42.85  ? 133 LEU A CB  1 
ATOM 258  C CG  . LEU A 1 48  ? 109.362 117.441 98.683  1.00 44.10  ? 133 LEU A CG  1 
ATOM 259  C CD1 . LEU A 1 48  ? 110.324 117.502 97.512  1.00 43.38  ? 133 LEU A CD1 1 
ATOM 260  C CD2 . LEU A 1 48  ? 108.155 116.580 98.350  1.00 52.02  ? 133 LEU A CD2 1 
ATOM 261  N N   . ARG A 1 49  ? 111.207 117.271 102.911 1.00 44.44  ? 134 ARG A N   1 
ATOM 262  C CA  . ARG A 1 49  ? 112.024 116.725 103.987 1.00 47.70  ? 134 ARG A CA  1 
ATOM 263  C C   . ARG A 1 49  ? 111.216 116.544 105.262 1.00 56.59  ? 134 ARG A C   1 
ATOM 264  O O   . ARG A 1 49  ? 111.518 115.656 106.068 1.00 65.54  ? 134 ARG A O   1 
ATOM 265  C CB  . ARG A 1 49  ? 113.228 117.638 104.229 1.00 48.83  ? 134 ARG A CB  1 
ATOM 266  C CG  . ARG A 1 49  ? 114.306 117.061 105.131 1.00 59.09  ? 134 ARG A CG  1 
ATOM 267  C CD  . ARG A 1 49  ? 115.420 118.075 105.350 1.00 65.41  ? 134 ARG A CD  1 
ATOM 268  N NE  . ARG A 1 49  ? 114.899 119.398 105.675 1.00 69.66  ? 134 ARG A NE  1 
ATOM 269  C CZ  . ARG A 1 49  ? 115.646 120.487 105.811 1.00 78.12  ? 134 ARG A CZ  1 
ATOM 270  N NH1 . ARG A 1 49  ? 116.958 120.449 105.651 1.00 78.33  ? 134 ARG A NH1 1 
ATOM 271  N NH2 . ARG A 1 49  ? 115.059 121.642 106.110 1.00 77.64  ? 134 ARG A NH2 1 
ATOM 272  N N   . ASP A 1 50  ? 110.191 117.370 105.465 1.00 51.86  ? 135 ASP A N   1 
ATOM 273  C CA  . ASP A 1 50  ? 109.302 117.133 106.598 1.00 53.32  ? 135 ASP A CA  1 
ATOM 274  C C   . ASP A 1 50  ? 108.164 116.169 106.260 1.00 58.36  ? 135 ASP A C   1 
ATOM 275  O O   . ASP A 1 50  ? 107.786 115.330 107.090 1.00 63.45  ? 135 ASP A O   1 
ATOM 276  C CB  . ASP A 1 50  ? 108.741 118.463 107.107 1.00 58.80  ? 135 ASP A CB  1 
ATOM 277  C CG  . ASP A 1 50  ? 109.769 119.268 107.883 1.00 69.73  ? 135 ASP A CG  1 
ATOM 278  O OD1 . ASP A 1 50  ? 109.887 119.063 109.110 1.00 72.46  ? 135 ASP A OD1 1 
ATOM 279  O OD2 . ASP A 1 50  ? 110.462 120.102 107.264 1.00 66.96  ? 135 ASP A OD2 1 
ATOM 280  N N   . THR A 1 51  ? 107.616 116.264 105.047 1.00 58.82  ? 136 THR A N   1 
ATOM 281  C CA  . THR A 1 51  ? 106.483 115.425 104.671 1.00 56.57  ? 136 THR A CA  1 
ATOM 282  C C   . THR A 1 51  ? 106.860 113.953 104.651 1.00 61.38  ? 136 THR A C   1 
ATOM 283  O O   . THR A 1 51  ? 106.090 113.100 105.105 1.00 65.51  ? 136 THR A O   1 
ATOM 284  C CB  . THR A 1 51  ? 105.948 115.854 103.305 1.00 61.26  ? 136 THR A CB  1 
ATOM 285  O OG1 . THR A 1 51  ? 105.522 117.221 103.367 1.00 61.85  ? 136 THR A OG1 1 
ATOM 286  C CG2 . THR A 1 51  ? 104.773 114.980 102.896 1.00 64.55  ? 136 THR A CG2 1 
ATOM 287  N N   . LYS A 1 52  ? 108.043 113.635 104.134 1.00 61.33  ? 137 LYS A N   1 
ATOM 288  C CA  . LYS A 1 52  ? 108.438 112.241 103.990 1.00 57.72  ? 137 LYS A CA  1 
ATOM 289  C C   . LYS A 1 52  ? 108.526 111.524 105.338 1.00 64.75  ? 137 LYS A C   1 
ATOM 290  O O   . LYS A 1 52  ? 108.032 110.395 105.475 1.00 71.58  ? 137 LYS A O   1 
ATOM 291  C CB  . LYS A 1 52  ? 109.756 112.169 103.223 1.00 53.45  ? 137 LYS A CB  1 
ATOM 292  C CG  . LYS A 1 52  ? 110.881 112.835 103.965 1.00 52.89  ? 137 LYS A CG  1 
ATOM 293  C CD  . LYS A 1 52  ? 112.205 112.686 103.290 1.00 53.63  ? 137 LYS A CD  1 
ATOM 294  C CE  . LYS A 1 52  ? 113.246 113.376 104.139 1.00 55.50  ? 137 LYS A CE  1 
ATOM 295  N NZ  . LYS A 1 52  ? 113.203 112.907 105.548 1.00 62.10  ? 137 LYS A NZ  1 
ATOM 296  N N   . ASP A 1 53  ? 109.124 112.154 106.353 1.00 66.33  ? 138 ASP A N   1 
ATOM 297  C CA  . ASP A 1 53  ? 109.237 111.443 107.624 1.00 64.85  ? 138 ASP A CA  1 
ATOM 298  C C   . ASP A 1 53  ? 107.958 111.540 108.449 1.00 68.67  ? 138 ASP A C   1 
ATOM 299  O O   . ASP A 1 53  ? 107.693 110.647 109.263 1.00 72.03  ? 138 ASP A O   1 
ATOM 300  C CB  . ASP A 1 53  ? 110.446 111.922 108.443 1.00 67.59  ? 138 ASP A CB  1 
ATOM 301  C CG  . ASP A 1 53  ? 110.361 113.377 108.850 1.00 76.21  ? 138 ASP A CG  1 
ATOM 302  O OD1 . ASP A 1 53  ? 109.395 114.060 108.479 1.00 74.89  ? 138 ASP A OD1 1 
ATOM 303  O OD2 . ASP A 1 53  ? 111.270 113.844 109.564 1.00 79.98  ? 138 ASP A OD2 1 
ATOM 304  N N   . VAL A 1 54  ? 107.136 112.583 108.260 1.00 70.35  ? 139 VAL A N   1 
ATOM 305  C CA  . VAL A 1 54  ? 105.847 112.563 108.952 1.00 66.56  ? 139 VAL A CA  1 
ATOM 306  C C   . VAL A 1 54  ? 104.824 111.696 108.238 1.00 66.22  ? 139 VAL A C   1 
ATOM 307  O O   . VAL A 1 54  ? 103.736 111.464 108.778 1.00 75.45  ? 139 VAL A O   1 
ATOM 308  C CB  . VAL A 1 54  ? 105.232 113.964 109.134 1.00 66.43  ? 139 VAL A CB  1 
ATOM 309  C CG1 . VAL A 1 54  ? 106.139 114.836 109.989 1.00 65.85  ? 139 VAL A CG1 1 
ATOM 310  C CG2 . VAL A 1 54  ? 104.905 114.602 107.796 1.00 66.80  ? 139 VAL A CG2 1 
ATOM 311  N N   . LEU A 1 55  ? 105.146 111.215 107.040 1.00 62.66  ? 140 LEU A N   1 
ATOM 312  C CA  . LEU A 1 55  ? 104.275 110.380 106.225 1.00 65.28  ? 140 LEU A CA  1 
ATOM 313  C C   . LEU A 1 55  ? 104.602 108.897 106.300 1.00 69.84  ? 140 LEU A C   1 
ATOM 314  O O   . LEU A 1 55  ? 103.693 108.076 106.456 1.00 73.10  ? 140 LEU A O   1 
ATOM 315  C CB  . LEU A 1 55  ? 104.363 110.839 104.771 1.00 63.68  ? 140 LEU A CB  1 
ATOM 316  C CG  . LEU A 1 55  ? 103.509 110.184 103.692 1.00 68.28  ? 140 LEU A CG  1 
ATOM 317  C CD1 . LEU A 1 55  ? 102.020 110.359 103.906 1.00 74.13  ? 140 LEU A CD1 1 
ATOM 318  C CD2 . LEU A 1 55  ? 103.939 110.812 102.397 1.00 61.42  ? 140 LEU A CD2 1 
ATOM 319  N N   . VAL A 1 56  ? 105.880 108.532 106.175 1.00 70.28  ? 141 VAL A N   1 
ATOM 320  C CA  . VAL A 1 56  ? 106.244 107.122 106.165 1.00 64.20  ? 141 VAL A CA  1 
ATOM 321  C C   . VAL A 1 56  ? 105.981 106.461 107.516 1.00 70.94  ? 141 VAL A C   1 
ATOM 322  O O   . VAL A 1 56  ? 105.823 105.236 107.582 1.00 79.68  ? 141 VAL A O   1 
ATOM 323  C CB  . VAL A 1 56  ? 107.716 106.976 105.729 1.00 65.70  ? 141 VAL A CB  1 
ATOM 324  C CG1 . VAL A 1 56  ? 108.630 107.609 106.747 1.00 70.34  ? 141 VAL A CG1 1 
ATOM 325  C CG2 . VAL A 1 56  ? 108.081 105.518 105.492 1.00 66.85  ? 141 VAL A CG2 1 
ATOM 326  N N   . VAL A 1 57  ? 105.905 107.237 108.596 1.00 71.40  ? 142 VAL A N   1 
ATOM 327  C CA  . VAL A 1 57  ? 105.623 106.653 109.903 1.00 73.69  ? 142 VAL A CA  1 
ATOM 328  C C   . VAL A 1 57  ? 104.127 106.633 110.212 1.00 75.29  ? 142 VAL A C   1 
ATOM 329  O O   . VAL A 1 57  ? 103.655 105.726 110.905 1.00 81.60  ? 142 VAL A O   1 
ATOM 330  C CB  . VAL A 1 57  ? 106.402 107.388 111.008 1.00 67.86  ? 142 VAL A CB  1 
ATOM 331  C CG1 . VAL A 1 57  ? 107.897 107.253 110.777 1.00 70.31  ? 142 VAL A CG1 1 
ATOM 332  C CG2 . VAL A 1 57  ? 105.984 108.849 111.095 1.00 64.72  ? 142 VAL A CG2 1 
ATOM 333  N N   . THR A 1 58  ? 103.370 107.613 109.723 1.00 71.93  ? 143 THR A N   1 
ATOM 334  C CA  . THR A 1 58  ? 101.921 107.638 109.917 1.00 71.72  ? 143 THR A CA  1 
ATOM 335  C C   . THR A 1 58  ? 101.233 107.047 108.687 1.00 81.54  ? 143 THR A C   1 
ATOM 336  O O   . THR A 1 58  ? 100.486 107.706 107.963 1.00 89.56  ? 143 THR A O   1 
ATOM 337  C CB  . THR A 1 58  ? 101.443 109.059 110.204 1.00 75.90  ? 143 THR A CB  1 
ATOM 338  O OG1 . THR A 1 58  ? 101.401 109.809 108.983 1.00 79.63  ? 143 THR A OG1 1 
ATOM 339  C CG2 . THR A 1 58  ? 102.373 109.747 111.192 1.00 75.76  ? 143 THR A CG2 1 
ATOM 340  N N   . ALA A 1 59  ? 101.511 105.766 108.464 1.00 79.92  ? 144 ALA A N   1 
ATOM 341  C CA  . ALA A 1 59  ? 100.931 105.009 107.367 1.00 83.05  ? 144 ALA A CA  1 
ATOM 342  C C   . ALA A 1 59  ? 100.128 103.843 107.925 1.00 91.60  ? 144 ALA A C   1 
ATOM 343  O O   . ALA A 1 59  ? 100.455 103.294 108.981 1.00 92.97  ? 144 ALA A O   1 
ATOM 344  C CB  . ALA A 1 59  ? 102.013 104.491 106.411 1.00 81.30  ? 144 ALA A CB  1 
ATOM 345  N N   . LYS A 1 60  ? 99.072  103.465 107.205 1.00 97.35  ? 145 LYS A N   1 
ATOM 346  C CA  . LYS A 1 60  ? 98.207  102.366 107.634 1.00 95.57  ? 145 LYS A CA  1 
ATOM 347  C C   . LYS A 1 60  ? 98.963  101.060 107.413 1.00 95.69  ? 145 LYS A C   1 
ATOM 348  O O   . LYS A 1 60  ? 98.835  100.383 106.390 1.00 99.39  ? 145 LYS A O   1 
ATOM 349  C CB  . LYS A 1 60  ? 96.881  102.387 106.883 1.00 98.18  ? 145 LYS A CB  1 
ATOM 350  C CG  . LYS A 1 60  ? 95.915  101.301 107.328 1.00 103.97 ? 145 LYS A CG  1 
ATOM 351  C CD  . LYS A 1 60  ? 94.570  101.426 106.638 1.00 105.58 ? 145 LYS A CD  1 
ATOM 352  C CE  . LYS A 1 60  ? 93.674  100.249 106.982 1.00 101.02 ? 145 LYS A CE  1 
ATOM 353  N NZ  . LYS A 1 60  ? 93.306  100.239 108.425 1.00 96.70  ? 145 LYS A NZ  1 
ATOM 354  N N   . GLY A 1 61  ? 99.782  100.713 108.401 1.00 95.42  ? 146 GLY A N   1 
ATOM 355  C CA  . GLY A 1 61  ? 100.663 99.568  108.311 1.00 96.52  ? 146 GLY A CA  1 
ATOM 356  C C   . GLY A 1 61  ? 102.064 100.013 107.956 1.00 96.20  ? 146 GLY A C   1 
ATOM 357  O O   . GLY A 1 61  ? 102.358 100.261 106.785 1.00 96.82  ? 146 GLY A O   1 
ATOM 358  N N   . SER A 1 62  ? 102.939 100.119 108.953 1.00 93.49  ? 147 SER A N   1 
ATOM 359  C CA  . SER A 1 62  ? 104.282 100.646 108.724 1.00 84.65  ? 147 SER A CA  1 
ATOM 360  C C   . SER A 1 62  ? 105.171 100.225 109.880 1.00 85.66  ? 147 SER A C   1 
ATOM 361  O O   . SER A 1 62  ? 104.873 100.540 111.036 1.00 88.09  ? 147 SER A O   1 
ATOM 362  C CB  . SER A 1 62  ? 104.254 102.170 108.591 1.00 81.64  ? 147 SER A CB  1 
ATOM 363  O OG  . SER A 1 62  ? 105.564 102.710 108.602 1.00 78.84  ? 147 SER A OG  1 
ATOM 364  N N   . SER A 1 63  ? 106.253 99.517  109.573 1.00 85.08  ? 148 SER A N   1 
ATOM 365  C CA  . SER A 1 63  ? 107.221 99.140  110.588 1.00 83.75  ? 148 SER A CA  1 
ATOM 366  C C   . SER A 1 63  ? 108.123 100.323 110.920 1.00 78.03  ? 148 SER A C   1 
ATOM 367  O O   . SER A 1 63  ? 108.410 101.171 110.071 1.00 76.32  ? 148 SER A O   1 
ATOM 368  C CB  . SER A 1 63  ? 108.062 97.955  110.115 1.00 84.80  ? 148 SER A CB  1 
ATOM 369  O OG  . SER A 1 63  ? 108.998 97.567  111.105 1.00 87.77  ? 148 SER A OG  1 
ATOM 370  N N   . ALA A 1 64  ? 108.566 100.379 112.178 1.00 77.02  ? 149 ALA A N   1 
ATOM 371  C CA  . ALA A 1 64  ? 109.442 101.466 112.598 1.00 76.33  ? 149 ALA A CA  1 
ATOM 372  C C   . ALA A 1 64  ? 110.855 101.314 112.057 1.00 78.76  ? 149 ALA A C   1 
ATOM 373  O O   . ALA A 1 64  ? 111.630 102.275 112.104 1.00 81.02  ? 149 ALA A O   1 
ATOM 374  C CB  . ALA A 1 64  ? 109.482 101.561 114.121 1.00 73.17  ? 149 ALA A CB  1 
ATOM 375  N N   . GLU A 1 65  ? 111.211 100.135 111.551 1.00 79.31  ? 150 GLU A N   1 
ATOM 376  C CA  . GLU A 1 65  ? 112.514 99.904  110.931 1.00 77.37  ? 150 GLU A CA  1 
ATOM 377  C C   . GLU A 1 65  ? 112.449 100.071 109.418 1.00 76.67  ? 150 GLU A C   1 
ATOM 378  O O   . GLU A 1 65  ? 113.202 99.436  108.672 1.00 79.25  ? 150 GLU A O   1 
ATOM 379  C CB  . GLU A 1 65  ? 113.043 98.522  111.307 1.00 79.96  ? 150 GLU A CB  1 
ATOM 380  C CG  . GLU A 1 65  ? 112.230 97.352  110.774 1.00 79.99  ? 150 GLU A CG  1 
ATOM 381  C CD  . GLU A 1 65  ? 112.773 96.015  111.239 1.00 90.79  ? 150 GLU A CD  1 
ATOM 382  O OE1 . GLU A 1 65  ? 113.767 96.006  111.993 1.00 87.23  ? 150 GLU A OE1 1 
ATOM 383  O OE2 . GLU A 1 65  ? 112.209 94.973  110.849 1.00 99.11  ? 150 GLU A OE2 1 
ATOM 384  N N   . ILE A 1 66  ? 111.553 100.935 108.943 1.00 76.58  ? 151 ILE A N   1 
ATOM 385  C CA  . ILE A 1 66  ? 111.387 101.174 107.514 1.00 69.76  ? 151 ILE A CA  1 
ATOM 386  C C   . ILE A 1 66  ? 112.211 102.384 107.099 1.00 65.71  ? 151 ILE A C   1 
ATOM 387  O O   . ILE A 1 66  ? 112.652 102.476 105.950 1.00 73.83  ? 151 ILE A O   1 
ATOM 388  C CB  . ILE A 1 66  ? 109.901 101.351 107.143 1.00 69.85  ? 151 ILE A CB  1 
ATOM 389  C CG1 . ILE A 1 66  ? 109.673 100.967 105.682 1.00 72.46  ? 151 ILE A CG1 1 
ATOM 390  C CG2 . ILE A 1 66  ? 109.420 102.771 107.426 1.00 69.76  ? 151 ILE A CG2 1 
ATOM 391  C CD1 . ILE A 1 66  ? 108.245 100.653 105.367 1.00 77.21  ? 151 ILE A CD1 1 
ATOM 392  N N   . ILE A 1 67  ? 112.429 103.318 108.019 1.00 63.30  ? 152 ILE A N   1 
ATOM 393  C CA  . ILE A 1 67  ? 113.241 104.488 107.695 1.00 60.96  ? 152 ILE A CA  1 
ATOM 394  C C   . ILE A 1 67  ? 114.713 104.105 107.822 1.00 66.83  ? 152 ILE A C   1 
ATOM 395  O O   . ILE A 1 67  ? 115.506 104.488 106.950 1.00 71.45  ? 152 ILE A O   1 
ATOM 396  C CB  . ILE A 1 67  ? 112.913 105.695 108.586 1.00 66.07  ? 152 ILE A CB  1 
ATOM 397  C CG1 . ILE A 1 67  ? 111.534 106.254 108.275 1.00 62.43  ? 152 ILE A CG1 1 
ATOM 398  C CG2 . ILE A 1 67  ? 113.876 106.838 108.273 1.00 64.90  ? 152 ILE A CG2 1 
ATOM 399  C CD1 . ILE A 1 67  ? 111.219 107.501 109.090 1.00 68.24  ? 152 ILE A CD1 1 
ATOM 400  N N   . PRO A 1 68  ? 115.144 103.384 108.878 1.00 66.84  ? 153 PRO A N   1 
ATOM 401  C CA  . PRO A 1 68  ? 116.560 102.969 108.914 1.00 64.95  ? 153 PRO A CA  1 
ATOM 402  C C   . PRO A 1 68  ? 116.991 102.176 107.694 1.00 64.98  ? 153 PRO A C   1 
ATOM 403  O O   . PRO A 1 68  ? 118.075 102.427 107.150 1.00 68.70  ? 153 PRO A O   1 
ATOM 404  C CB  . PRO A 1 68  ? 116.641 102.128 110.196 1.00 68.01  ? 153 PRO A CB  1 
ATOM 405  C CG  . PRO A 1 68  ? 115.588 102.693 111.064 1.00 65.84  ? 153 PRO A CG  1 
ATOM 406  C CD  . PRO A 1 68  ? 114.458 103.026 110.138 1.00 66.88  ? 153 PRO A CD  1 
ATOM 407  N N   . PHE A 1 69  ? 116.152 101.251 107.222 1.00 60.29  ? 154 PHE A N   1 
ATOM 408  C CA  . PHE A 1 69  ? 116.512 100.459 106.050 1.00 60.30  ? 154 PHE A CA  1 
ATOM 409  C C   . PHE A 1 69  ? 116.669 101.343 104.820 1.00 65.37  ? 154 PHE A C   1 
ATOM 410  O O   . PHE A 1 69  ? 117.541 101.098 103.979 1.00 73.21  ? 154 PHE A O   1 
ATOM 411  C CB  . PHE A 1 69  ? 115.467 99.369  105.806 1.00 69.21  ? 154 PHE A CB  1 
ATOM 412  C CG  . PHE A 1 69  ? 115.957 98.240  104.940 1.00 77.77  ? 154 PHE A CG  1 
ATOM 413  C CD1 . PHE A 1 69  ? 115.938 98.345  103.559 1.00 75.89  ? 154 PHE A CD1 1 
ATOM 414  C CD2 . PHE A 1 69  ? 116.443 97.074  105.511 1.00 78.01  ? 154 PHE A CD2 1 
ATOM 415  C CE1 . PHE A 1 69  ? 116.391 97.309  102.763 1.00 77.73  ? 154 PHE A CE1 1 
ATOM 416  C CE2 . PHE A 1 69  ? 116.897 96.034  104.719 1.00 77.02  ? 154 PHE A CE2 1 
ATOM 417  C CZ  . PHE A 1 69  ? 116.870 96.152  103.344 1.00 80.44  ? 154 PHE A CZ  1 
ATOM 418  N N   . LEU A 1 70  ? 115.834 102.377 104.697 1.00 66.36  ? 155 LEU A N   1 
ATOM 419  C CA  . LEU A 1 70  ? 115.982 103.337 103.611 1.00 62.15  ? 155 LEU A CA  1 
ATOM 420  C C   . LEU A 1 70  ? 117.155 104.284 103.811 1.00 61.90  ? 155 LEU A C   1 
ATOM 421  O O   . LEU A 1 70  ? 117.604 104.900 102.840 1.00 69.52  ? 155 LEU A O   1 
ATOM 422  C CB  . LEU A 1 70  ? 114.694 104.146 103.428 1.00 59.92  ? 155 LEU A CB  1 
ATOM 423  C CG  . LEU A 1 70  ? 113.669 103.569 102.450 1.00 56.82  ? 155 LEU A CG  1 
ATOM 424  C CD1 . LEU A 1 70  ? 113.179 102.223 102.911 1.00 58.34  ? 155 LEU A CD1 1 
ATOM 425  C CD2 . LEU A 1 70  ? 112.500 104.526 102.273 1.00 63.63  ? 155 LEU A CD2 1 
ATOM 426  N N   . LYS A 1 71  ? 117.665 104.420 105.035 1.00 62.57  ? 156 LYS A N   1 
ATOM 427  C CA  . LYS A 1 71  ? 118.857 105.233 105.240 1.00 64.98  ? 156 LYS A CA  1 
ATOM 428  C C   . LYS A 1 71  ? 120.143 104.447 105.066 1.00 69.53  ? 156 LYS A C   1 
ATOM 429  O O   . LYS A 1 71  ? 121.174 105.030 104.714 1.00 72.88  ? 156 LYS A O   1 
ATOM 430  C CB  . LYS A 1 71  ? 118.854 105.860 106.632 1.00 62.38  ? 156 LYS A CB  1 
ATOM 431  C CG  . LYS A 1 71  ? 118.015 107.102 106.746 1.00 62.95  ? 156 LYS A CG  1 
ATOM 432  C CD  . LYS A 1 71  ? 117.859 107.492 108.194 1.00 68.03  ? 156 LYS A CD  1 
ATOM 433  C CE  . LYS A 1 71  ? 119.169 107.406 108.959 1.00 67.96  ? 156 LYS A CE  1 
ATOM 434  N NZ  . LYS A 1 71  ? 118.953 107.574 110.425 1.00 68.70  ? 156 LYS A NZ  1 
ATOM 435  N N   . THR A 1 72  ? 120.110 103.140 105.313 1.00 67.00  ? 157 THR A N   1 
ATOM 436  C CA  . THR A 1 72  ? 121.317 102.326 105.256 1.00 66.40  ? 157 THR A CA  1 
ATOM 437  C C   . THR A 1 72  ? 121.507 101.693 103.880 1.00 69.60  ? 157 THR A C   1 
ATOM 438  O O   . THR A 1 72  ? 122.545 101.885 103.240 1.00 77.01  ? 157 THR A O   1 
ATOM 439  C CB  . THR A 1 72  ? 121.270 101.242 106.339 1.00 67.09  ? 157 THR A CB  1 
ATOM 440  O OG1 . THR A 1 72  ? 121.054 101.850 107.618 1.00 71.69  ? 157 THR A OG1 1 
ATOM 441  C CG2 . THR A 1 72  ? 122.576 100.467 106.370 1.00 69.22  ? 157 THR A CG2 1 
ATOM 442  N N   . TRP A 1 73  ? 120.507 100.949 103.411 1.00 66.75  ? 158 TRP A N   1 
ATOM 443  C CA  . TRP A 1 73  ? 120.678 100.077 102.259 1.00 69.64  ? 158 TRP A CA  1 
ATOM 444  C C   . TRP A 1 73  ? 120.002 100.590 100.993 1.00 69.95  ? 158 TRP A C   1 
ATOM 445  O O   . TRP A 1 73  ? 120.142 99.957  99.942  1.00 77.25  ? 158 TRP A O   1 
ATOM 446  C CB  . TRP A 1 73  ? 120.140 98.679  102.582 1.00 75.93  ? 158 TRP A CB  1 
ATOM 447  C CG  . TRP A 1 73  ? 120.896 97.995  103.678 1.00 75.02  ? 158 TRP A CG  1 
ATOM 448  C CD1 . TRP A 1 73  ? 120.556 97.951  104.999 1.00 70.46  ? 158 TRP A CD1 1 
ATOM 449  C CD2 . TRP A 1 73  ? 122.132 97.280  103.558 1.00 76.39  ? 158 TRP A CD2 1 
ATOM 450  N NE1 . TRP A 1 73  ? 121.495 97.243  105.707 1.00 68.40  ? 158 TRP A NE1 1 
ATOM 451  C CE2 . TRP A 1 73  ? 122.473 96.821  104.846 1.00 71.10  ? 158 TRP A CE2 1 
ATOM 452  C CE3 . TRP A 1 73  ? 122.979 96.979  102.488 1.00 83.73  ? 158 TRP A CE3 1 
ATOM 453  C CZ2 . TRP A 1 73  ? 123.625 96.077  105.092 1.00 79.34  ? 158 TRP A CZ2 1 
ATOM 454  C CZ3 . TRP A 1 73  ? 124.122 96.240  102.734 1.00 91.00  ? 158 TRP A CZ3 1 
ATOM 455  C CH2 . TRP A 1 73  ? 124.435 95.797  104.026 1.00 89.71  ? 158 TRP A CH2 1 
ATOM 456  N N   . VAL A 1 74  ? 119.273 101.702 101.061 1.00 65.03  ? 159 VAL A N   1 
ATOM 457  C CA  . VAL A 1 74  ? 118.527 102.185 99.903  1.00 60.03  ? 159 VAL A CA  1 
ATOM 458  C C   . VAL A 1 74  ? 119.071 103.533 99.443  1.00 61.54  ? 159 VAL A C   1 
ATOM 459  O O   . VAL A 1 74  ? 119.144 103.803 98.240  1.00 65.96  ? 159 VAL A O   1 
ATOM 460  C CB  . VAL A 1 74  ? 117.021 102.272 100.212 1.00 59.53  ? 159 VAL A CB  1 
ATOM 461  C CG1 . VAL A 1 74  ? 116.247 102.711 98.978  1.00 54.87  ? 159 VAL A CG1 1 
ATOM 462  C CG2 . VAL A 1 74  ? 116.507 100.932 100.716 1.00 62.71  ? 159 VAL A CG2 1 
ATOM 463  N N   . ASN A 1 75  ? 119.455 104.386 100.395 1.00 61.10  ? 160 ASN A N   1 
ATOM 464  C CA  . ASN A 1 75  ? 119.895 105.739 100.059 1.00 55.63  ? 160 ASN A CA  1 
ATOM 465  C C   . ASN A 1 75  ? 121.137 105.718 99.171  1.00 60.15  ? 160 ASN A C   1 
ATOM 466  O O   . ASN A 1 75  ? 121.131 106.254 98.057  1.00 68.93  ? 160 ASN A O   1 
ATOM 467  C CB  . ASN A 1 75  ? 120.161 106.533 101.340 1.00 62.62  ? 160 ASN A CB  1 
ATOM 468  C CG  . ASN A 1 75  ? 118.987 107.408 101.741 1.00 73.96  ? 160 ASN A CG  1 
ATOM 469  O OD1 . ASN A 1 75  ? 117.874 107.242 101.242 1.00 70.04  ? 160 ASN A OD1 1 
ATOM 470  N ND2 . ASN A 1 75  ? 119.232 108.345 102.650 1.00 77.49  ? 160 ASN A ND2 1 
ATOM 471  N N   . LEU A 1 76  ? 122.217 105.106 99.656  1.00 61.27  ? 161 LEU A N   1 
ATOM 472  C CA  . LEU A 1 76  ? 123.495 105.082 98.950  1.00 60.31  ? 161 LEU A CA  1 
ATOM 473  C C   . LEU A 1 76  ? 123.427 104.336 97.617  1.00 60.40  ? 161 LEU A C   1 
ATOM 474  O O   . LEU A 1 76  ? 123.964 104.836 96.617  1.00 64.31  ? 161 LEU A O   1 
ATOM 475  C CB  . LEU A 1 76  ? 124.583 104.483 99.848  1.00 62.59  ? 161 LEU A CB  1 
ATOM 476  C CG  . LEU A 1 76  ? 126.029 104.813 99.477  1.00 69.32  ? 161 LEU A CG  1 
ATOM 477  C CD1 . LEU A 1 76  ? 126.252 106.312 99.469  1.00 61.03  ? 161 LEU A CD1 1 
ATOM 478  C CD2 . LEU A 1 76  ? 126.992 104.136 100.438 1.00 75.59  ? 161 LEU A CD2 1 
ATOM 479  N N   . PRO A 1 77  ? 122.830 103.135 97.549  1.00 58.10  ? 162 PRO A N   1 
ATOM 480  C CA  . PRO A 1 77  ? 122.680 102.497 96.229  1.00 58.94  ? 162 PRO A CA  1 
ATOM 481  C C   . PRO A 1 77  ? 121.873 103.331 95.251  1.00 59.38  ? 162 PRO A C   1 
ATOM 482  O O   . PRO A 1 77  ? 122.206 103.375 94.060  1.00 61.43  ? 162 PRO A O   1 
ATOM 483  C CB  . PRO A 1 77  ? 121.982 101.173 96.564  1.00 61.45  ? 162 PRO A CB  1 
ATOM 484  C CG  . PRO A 1 77  ? 122.422 100.875 97.943  1.00 61.81  ? 162 PRO A CG  1 
ATOM 485  C CD  . PRO A 1 77  ? 122.429 102.212 98.628  1.00 62.21  ? 162 PRO A CD  1 
ATOM 486  N N   . MET A 1 78  ? 120.823 104.005 95.725  1.00 62.77  ? 163 MET A N   1 
ATOM 487  C CA  . MET A 1 78  ? 120.045 104.871 94.845  1.00 63.28  ? 163 MET A CA  1 
ATOM 488  C C   . MET A 1 78  ? 120.885 106.038 94.343  1.00 63.62  ? 163 MET A C   1 
ATOM 489  O O   . MET A 1 78  ? 120.796 106.417 93.171  1.00 67.10  ? 163 MET A O   1 
ATOM 490  C CB  . MET A 1 78  ? 118.798 105.378 95.569  1.00 60.94  ? 163 MET A CB  1 
ATOM 491  C CG  . MET A 1 78  ? 117.860 106.192 94.697  1.00 68.56  ? 163 MET A CG  1 
ATOM 492  S SD  . MET A 1 78  ? 117.153 105.240 93.339  1.00 94.88  ? 163 MET A SD  1 
ATOM 493  C CE  . MET A 1 78  ? 116.000 104.194 94.221  1.00 69.20  ? 163 MET A CE  1 
ATOM 494  N N   . ALA A 1 79  ? 121.711 106.616 95.218  1.00 63.30  ? 164 ALA A N   1 
ATOM 495  C CA  . ALA A 1 79  ? 122.589 107.704 94.798  1.00 58.48  ? 164 ALA A CA  1 
ATOM 496  C C   . ALA A 1 79  ? 123.593 107.236 93.751  1.00 63.58  ? 164 ALA A C   1 
ATOM 497  O O   . ALA A 1 79  ? 123.832 107.929 92.754  1.00 67.64  ? 164 ALA A O   1 
ATOM 498  C CB  . ALA A 1 79  ? 123.308 108.289 96.012  1.00 57.54  ? 164 ALA A CB  1 
ATOM 499  N N   . ILE A 1 80  ? 124.188 106.059 93.956  1.00 62.99  ? 165 ILE A N   1 
ATOM 500  C CA  . ILE A 1 80  ? 125.160 105.537 92.995  1.00 60.38  ? 165 ILE A CA  1 
ATOM 501  C C   . ILE A 1 80  ? 124.486 105.257 91.654  1.00 64.59  ? 165 ILE A C   1 
ATOM 502  O O   . ILE A 1 80  ? 125.026 105.576 90.581  1.00 72.59  ? 165 ILE A O   1 
ATOM 503  C CB  . ILE A 1 80  ? 125.845 104.282 93.567  1.00 57.77  ? 165 ILE A CB  1 
ATOM 504  C CG1 . ILE A 1 80  ? 126.699 104.652 94.783  1.00 57.38  ? 165 ILE A CG1 1 
ATOM 505  C CG2 . ILE A 1 80  ? 126.696 103.603 92.507  1.00 60.34  ? 165 ILE A CG2 1 
ATOM 506  C CD1 . ILE A 1 80  ? 127.510 103.501 95.340  1.00 59.34  ? 165 ILE A CD1 1 
ATOM 507  N N   . GLY A 1 81  ? 123.293 104.659 91.695  1.00 60.87  ? 166 GLY A N   1 
ATOM 508  C CA  . GLY A 1 81  ? 122.557 104.410 90.469  1.00 59.98  ? 166 GLY A CA  1 
ATOM 509  C C   . GLY A 1 81  ? 122.184 105.686 89.742  1.00 65.39  ? 166 GLY A C   1 
ATOM 510  O O   . GLY A 1 81  ? 122.234 105.744 88.511  1.00 75.13  ? 166 GLY A O   1 
ATOM 511  N N   . PHE A 1 82  ? 121.805 106.728 90.489  1.00 63.12  ? 167 PHE A N   1 
ATOM 512  C CA  . PHE A 1 82  ? 121.509 108.000 89.842  1.00 62.34  ? 167 PHE A CA  1 
ATOM 513  C C   . PHE A 1 82  ? 122.758 108.617 89.235  1.00 64.51  ? 167 PHE A C   1 
ATOM 514  O O   . PHE A 1 82  ? 122.676 109.257 88.186  1.00 69.32  ? 167 PHE A O   1 
ATOM 515  C CB  . PHE A 1 82  ? 120.862 108.984 90.815  1.00 62.54  ? 167 PHE A CB  1 
ATOM 516  C CG  . PHE A 1 82  ? 120.406 110.257 90.155  1.00 67.58  ? 167 PHE A CG  1 
ATOM 517  C CD1 . PHE A 1 82  ? 121.257 111.347 90.042  1.00 66.73  ? 167 PHE A CD1 1 
ATOM 518  C CD2 . PHE A 1 82  ? 119.133 110.352 89.619  1.00 67.64  ? 167 PHE A CD2 1 
ATOM 519  C CE1 . PHE A 1 82  ? 120.840 112.506 89.417  1.00 63.52  ? 167 PHE A CE1 1 
ATOM 520  C CE2 . PHE A 1 82  ? 118.710 111.510 88.998  1.00 66.95  ? 167 PHE A CE2 1 
ATOM 521  C CZ  . PHE A 1 82  ? 119.565 112.587 88.896  1.00 66.47  ? 167 PHE A CZ  1 
ATOM 522  N N   . MET A 1 83  ? 123.914 108.455 89.880  1.00 64.13  ? 168 MET A N   1 
ATOM 523  C CA  . MET A 1 83  ? 125.160 108.917 89.274  1.00 64.05  ? 168 MET A CA  1 
ATOM 524  C C   . MET A 1 83  ? 125.398 108.241 87.928  1.00 69.79  ? 168 MET A C   1 
ATOM 525  O O   . MET A 1 83  ? 125.658 108.912 86.917  1.00 74.62  ? 168 MET A O   1 
ATOM 526  C CB  . MET A 1 83  ? 126.326 108.671 90.233  1.00 68.50  ? 168 MET A CB  1 
ATOM 527  C CG  . MET A 1 83  ? 127.706 108.892 89.636  1.00 72.72  ? 168 MET A CG  1 
ATOM 528  S SD  . MET A 1 83  ? 128.989 107.959 90.504  1.00 96.22  ? 168 MET A SD  1 
ATOM 529  C CE  . MET A 1 83  ? 128.427 106.273 90.297  1.00 81.13  ? 168 MET A CE  1 
ATOM 530  N N   . LEU A 1 84  ? 125.288 106.910 87.892  1.00 70.89  ? 169 LEU A N   1 
ATOM 531  C CA  . LEU A 1 84  ? 125.478 106.194 86.628  1.00 67.75  ? 169 LEU A CA  1 
ATOM 532  C C   . LEU A 1 84  ? 124.443 106.593 85.579  1.00 65.97  ? 169 LEU A C   1 
ATOM 533  O O   . LEU A 1 84  ? 124.779 106.732 84.397  1.00 71.92  ? 169 LEU A O   1 
ATOM 534  C CB  . LEU A 1 84  ? 125.465 104.682 86.856  1.00 65.87  ? 169 LEU A CB  1 
ATOM 535  C CG  . LEU A 1 84  ? 126.489 104.175 87.866  1.00 63.52  ? 169 LEU A CG  1 
ATOM 536  C CD1 . LEU A 1 84  ? 126.399 102.676 88.013  1.00 67.76  ? 169 LEU A CD1 1 
ATOM 537  C CD2 . LEU A 1 84  ? 127.858 104.543 87.327  1.00 73.84  ? 169 LEU A CD2 1 
ATOM 538  N N   . LEU A 1 85  ? 123.184 106.777 85.980  1.00 63.54  ? 170 LEU A N   1 
ATOM 539  C CA  . LEU A 1 85  ? 122.159 107.177 85.018  1.00 67.65  ? 170 LEU A CA  1 
ATOM 540  C C   . LEU A 1 85  ? 122.417 108.581 84.479  1.00 72.15  ? 170 LEU A C   1 
ATOM 541  O O   . LEU A 1 85  ? 122.310 108.819 83.268  1.00 78.94  ? 170 LEU A O   1 
ATOM 542  C CB  . LEU A 1 85  ? 120.776 107.095 85.664  1.00 66.96  ? 170 LEU A CB  1 
ATOM 543  C CG  . LEU A 1 85  ? 119.613 107.690 84.869  1.00 64.39  ? 170 LEU A CG  1 
ATOM 544  C CD1 . LEU A 1 85  ? 119.363 106.885 83.603  1.00 58.12  ? 170 LEU A CD1 1 
ATOM 545  C CD2 . LEU A 1 85  ? 118.355 107.762 85.721  1.00 63.18  ? 170 LEU A CD2 1 
ATOM 546  N N   . TYR A 1 86  ? 122.765 109.518 85.365  1.00 67.06  ? 171 TYR A N   1 
ATOM 547  C CA  . TYR A 1 86  ? 122.974 110.904 84.972  1.00 60.57  ? 171 TYR A CA  1 
ATOM 548  C C   . TYR A 1 86  ? 124.181 111.054 84.061  1.00 66.87  ? 171 TYR A C   1 
ATOM 549  O O   . TYR A 1 86  ? 124.165 111.900 83.161  1.00 75.05  ? 171 TYR A O   1 
ATOM 550  C CB  . TYR A 1 86  ? 123.139 111.777 86.216  1.00 59.55  ? 171 TYR A CB  1 
ATOM 551  C CG  . TYR A 1 86  ? 123.184 113.265 85.944  1.00 59.16  ? 171 TYR A CG  1 
ATOM 552  C CD1 . TYR A 1 86  ? 122.017 114.006 85.817  1.00 64.11  ? 171 TYR A CD1 1 
ATOM 553  C CD2 . TYR A 1 86  ? 124.396 113.928 85.809  1.00 60.78  ? 171 TYR A CD2 1 
ATOM 554  C CE1 . TYR A 1 86  ? 122.057 115.367 85.572  1.00 62.64  ? 171 TYR A CE1 1 
ATOM 555  C CE2 . TYR A 1 86  ? 124.447 115.285 85.565  1.00 64.86  ? 171 TYR A CE2 1 
ATOM 556  C CZ  . TYR A 1 86  ? 123.276 116.000 85.447  1.00 64.74  ? 171 TYR A CZ  1 
ATOM 557  O OH  . TYR A 1 86  ? 123.325 117.354 85.200  1.00 65.62  ? 171 TYR A OH  1 
ATOM 558  N N   . THR A 1 87  ? 125.234 110.260 84.276  1.00 68.59  ? 172 THR A N   1 
ATOM 559  C CA  . THR A 1 87  ? 126.386 110.328 83.379  1.00 69.60  ? 172 THR A CA  1 
ATOM 560  C C   . THR A 1 87  ? 125.976 110.059 81.934  1.00 73.34  ? 172 THR A C   1 
ATOM 561  O O   . THR A 1 87  ? 126.252 110.864 81.034  1.00 81.08  ? 172 THR A O   1 
ATOM 562  C CB  . THR A 1 87  ? 127.466 109.340 83.823  1.00 74.24  ? 172 THR A CB  1 
ATOM 563  O OG1 . THR A 1 87  ? 126.894 108.034 83.973  1.00 81.97  ? 172 THR A OG1 1 
ATOM 564  C CG2 . THR A 1 87  ? 128.096 109.781 85.137  1.00 70.92  ? 172 THR A CG2 1 
ATOM 565  N N   . LYS A 1 88  ? 125.279 108.946 81.696  1.00 71.13  ? 173 LYS A N   1 
ATOM 566  C CA  . LYS A 1 88  ? 124.902 108.609 80.328  1.00 73.42  ? 173 LYS A CA  1 
ATOM 567  C C   . LYS A 1 88  ? 123.837 109.561 79.796  1.00 75.23  ? 173 LYS A C   1 
ATOM 568  O O   . LYS A 1 88  ? 123.827 109.879 78.600  1.00 79.05  ? 173 LYS A O   1 
ATOM 569  C CB  . LYS A 1 88  ? 124.422 107.160 80.246  1.00 74.48  ? 173 LYS A CB  1 
ATOM 570  C CG  . LYS A 1 88  ? 124.219 106.676 78.818  1.00 81.06  ? 173 LYS A CG  1 
ATOM 571  C CD  . LYS A 1 88  ? 123.826 105.212 78.760  1.00 91.70  ? 173 LYS A CD  1 
ATOM 572  C CE  . LYS A 1 88  ? 123.754 104.727 77.320  1.00 93.38  ? 173 LYS A CE  1 
ATOM 573  N NZ  . LYS A 1 88  ? 122.656 105.387 76.562  1.00 89.25  ? 173 LYS A NZ  1 
ATOM 574  N N   . LEU A 1 89  ? 122.932 110.029 80.661  1.00 71.06  ? 174 LEU A N   1 
ATOM 575  C CA  . LEU A 1 89  ? 121.931 110.994 80.215  1.00 68.74  ? 174 LEU A CA  1 
ATOM 576  C C   . LEU A 1 89  ? 122.588 112.281 79.732  1.00 71.95  ? 174 LEU A C   1 
ATOM 577  O O   . LEU A 1 89  ? 122.229 112.817 78.678  1.00 76.61  ? 174 LEU A O   1 
ATOM 578  C CB  . LEU A 1 89  ? 120.933 111.282 81.338  1.00 65.67  ? 174 LEU A CB  1 
ATOM 579  C CG  . LEU A 1 89  ? 119.825 110.249 81.543  1.00 63.98  ? 174 LEU A CG  1 
ATOM 580  C CD1 . LEU A 1 89  ? 118.965 110.618 82.741  1.00 65.89  ? 174 LEU A CD1 1 
ATOM 581  C CD2 . LEU A 1 89  ? 118.975 110.119 80.287  1.00 65.53  ? 174 LEU A CD2 1 
ATOM 582  N N   . SER A 1 90  ? 123.567 112.788 80.486  1.00 69.59  ? 175 SER A N   1 
ATOM 583  C CA  . SER A 1 90  ? 124.314 113.958 80.038  1.00 70.00  ? 175 SER A CA  1 
ATOM 584  C C   . SER A 1 90  ? 125.116 113.654 78.781  1.00 76.22  ? 175 SER A C   1 
ATOM 585  O O   . SER A 1 90  ? 125.355 114.549 77.962  1.00 79.65  ? 175 SER A O   1 
ATOM 586  C CB  . SER A 1 90  ? 125.238 114.450 81.152  1.00 71.72  ? 175 SER A CB  1 
ATOM 587  O OG  . SER A 1 90  ? 126.289 113.529 81.387  1.00 74.59  ? 175 SER A OG  1 
ATOM 588  N N   . ASN A 1 91  ? 125.543 112.401 78.614  1.00 77.65  ? 176 ASN A N   1 
ATOM 589  C CA  . ASN A 1 91  ? 126.254 112.018 77.399  1.00 77.80  ? 176 ASN A CA  1 
ATOM 590  C C   . ASN A 1 91  ? 125.345 111.996 76.176  1.00 79.84  ? 176 ASN A C   1 
ATOM 591  O O   . ASN A 1 91  ? 125.817 112.219 75.055  1.00 89.48  ? 176 ASN A O   1 
ATOM 592  C CB  . ASN A 1 91  ? 126.917 110.658 77.601  1.00 83.71  ? 176 ASN A CB  1 
ATOM 593  C CG  . ASN A 1 91  ? 128.163 110.753 78.442  1.00 89.93  ? 176 ASN A CG  1 
ATOM 594  O OD1 . ASN A 1 91  ? 128.715 109.749 78.885  1.00 96.66  ? 176 ASN A OD1 1 
ATOM 595  N ND2 . ASN A 1 91  ? 128.645 111.973 78.624  1.00 89.62  ? 176 ASN A ND2 1 
ATOM 596  N N   . VAL A 1 92  ? 124.050 111.734 76.357  1.00 75.85  ? 177 VAL A N   1 
ATOM 597  C CA  . VAL A 1 92  ? 123.143 111.567 75.230  1.00 72.16  ? 177 VAL A CA  1 
ATOM 598  C C   . VAL A 1 92  ? 122.082 112.661 75.165  1.00 71.88  ? 177 VAL A C   1 
ATOM 599  O O   . VAL A 1 92  ? 121.173 112.584 74.338  1.00 75.62  ? 177 VAL A O   1 
ATOM 600  C CB  . VAL A 1 92  ? 122.483 110.173 75.247  1.00 72.48  ? 177 VAL A CB  1 
ATOM 601  C CG1 . VAL A 1 92  ? 123.542 109.084 75.332  1.00 79.75  ? 177 VAL A CG1 1 
ATOM 602  C CG2 . VAL A 1 92  ? 121.494 110.064 76.398  1.00 73.10  ? 177 VAL A CG2 1 
ATOM 603  N N   . LEU A 1 93  ? 122.177 113.686 76.010  1.00 71.52  ? 178 LEU A N   1 
ATOM 604  C CA  . LEU A 1 93  ? 121.183 114.751 76.023  1.00 69.64  ? 178 LEU A CA  1 
ATOM 605  C C   . LEU A 1 93  ? 121.870 116.103 76.135  1.00 71.99  ? 178 LEU A C   1 
ATOM 606  O O   . LEU A 1 93  ? 122.991 116.211 76.638  1.00 78.28  ? 178 LEU A O   1 
ATOM 607  C CB  . LEU A 1 93  ? 120.183 114.586 77.177  1.00 65.42  ? 178 LEU A CB  1 
ATOM 608  C CG  . LEU A 1 93  ? 119.142 113.473 77.044  1.00 64.76  ? 178 LEU A CG  1 
ATOM 609  C CD1 . LEU A 1 93  ? 118.354 113.325 78.336  1.00 65.09  ? 178 LEU A CD1 1 
ATOM 610  C CD2 . LEU A 1 93  ? 118.212 113.743 75.873  1.00 65.85  ? 178 LEU A CD2 1 
ATOM 611  N N   . SER A 1 94  ? 121.179 117.137 75.658  1.00 65.78  ? 179 SER A N   1 
ATOM 612  C CA  . SER A 1 94  ? 121.662 118.502 75.792  1.00 64.41  ? 179 SER A CA  1 
ATOM 613  C C   . SER A 1 94  ? 121.472 118.984 77.229  1.00 65.18  ? 179 SER A C   1 
ATOM 614  O O   . SER A 1 94  ? 120.961 118.268 78.094  1.00 68.76  ? 179 SER A O   1 
ATOM 615  C CB  . SER A 1 94  ? 120.944 119.418 74.804  1.00 64.75  ? 179 SER A CB  1 
ATOM 616  O OG  . SER A 1 94  ? 119.548 119.178 74.806  1.00 70.15  ? 179 SER A OG  1 
ATOM 617  N N   . LYS A 1 95  ? 121.900 120.221 77.489  1.00 59.76  ? 180 LYS A N   1 
ATOM 618  C CA  . LYS A 1 95  ? 121.808 120.770 78.840  1.00 60.11  ? 180 LYS A CA  1 
ATOM 619  C C   . LYS A 1 95  ? 120.354 120.936 79.273  1.00 63.46  ? 180 LYS A C   1 
ATOM 620  O O   . LYS A 1 95  ? 119.950 120.442 80.334  1.00 63.46  ? 180 LYS A O   1 
ATOM 621  C CB  . LYS A 1 95  ? 122.543 122.109 78.904  1.00 63.48  ? 180 LYS A CB  1 
ATOM 622  C CG  . LYS A 1 95  ? 124.029 122.020 78.596  1.00 64.46  ? 180 LYS A CG  1 
ATOM 623  C CD  . LYS A 1 95  ? 124.786 121.280 79.683  1.00 68.18  ? 180 LYS A CD  1 
ATOM 624  C CE  . LYS A 1 95  ? 126.267 121.195 79.353  1.00 76.34  ? 180 LYS A CE  1 
ATOM 625  N NZ  . LYS A 1 95  ? 126.923 122.531 79.404  1.00 80.70  ? 180 LYS A NZ  1 
ATOM 626  N N   . LYS A 1 96  ? 119.553 121.624 78.455  1.00 61.36  ? 181 LYS A N   1 
ATOM 627  C CA  . LYS A 1 96  ? 118.155 121.863 78.802  1.00 59.07  ? 181 LYS A CA  1 
ATOM 628  C C   . LYS A 1 96  ? 117.367 120.561 78.844  1.00 61.10  ? 181 LYS A C   1 
ATOM 629  O O   . LYS A 1 96  ? 116.545 120.347 79.747  1.00 65.76  ? 181 LYS A O   1 
ATOM 630  C CB  . LYS A 1 96  ? 117.532 122.833 77.799  1.00 58.88  ? 181 LYS A CB  1 
ATOM 631  C CG  . LYS A 1 96  ? 118.369 124.074 77.535  1.00 64.16  ? 181 LYS A CG  1 
ATOM 632  C CD  . LYS A 1 96  ? 118.010 124.711 76.200  1.00 67.41  ? 181 LYS A CD  1 
ATOM 633  C CE  . LYS A 1 96  ? 116.519 124.980 76.093  1.00 70.61  ? 181 LYS A CE  1 
ATOM 634  N NZ  . LYS A 1 96  ? 116.136 125.427 74.725  1.00 74.34  ? 181 LYS A NZ  1 
ATOM 635  N N   . ALA A 1 97  ? 117.599 119.684 77.865  1.00 58.41  ? 182 ALA A N   1 
ATOM 636  C CA  . ALA A 1 97  ? 116.907 118.402 77.839  1.00 54.12  ? 182 ALA A CA  1 
ATOM 637  C C   . ALA A 1 97  ? 117.237 117.580 79.075  1.00 57.09  ? 182 ALA A C   1 
ATOM 638  O O   . ALA A 1 97  ? 116.351 116.956 79.663  1.00 60.33  ? 182 ALA A O   1 
ATOM 639  C CB  . ALA A 1 97  ? 117.267 117.632 76.568  1.00 57.88  ? 182 ALA A CB  1 
ATOM 640  N N   . LEU A 1 98  ? 118.506 117.575 79.489  1.00 58.45  ? 183 LEU A N   1 
ATOM 641  C CA  . LEU A 1 98  ? 118.888 116.847 80.696  1.00 53.06  ? 183 LEU A CA  1 
ATOM 642  C C   . LEU A 1 98  ? 118.248 117.450 81.941  1.00 57.75  ? 183 LEU A C   1 
ATOM 643  O O   . LEU A 1 98  ? 117.744 116.717 82.801  1.00 62.51  ? 183 LEU A O   1 
ATOM 644  C CB  . LEU A 1 98  ? 120.409 116.824 80.829  1.00 54.23  ? 183 LEU A CB  1 
ATOM 645  C CG  . LEU A 1 98  ? 120.986 116.266 82.127  1.00 60.42  ? 183 LEU A CG  1 
ATOM 646  C CD1 . LEU A 1 98  ? 120.707 114.779 82.245  1.00 61.85  ? 183 LEU A CD1 1 
ATOM 647  C CD2 . LEU A 1 98  ? 122.476 116.539 82.176  1.00 62.20  ? 183 LEU A CD2 1 
ATOM 648  N N   . PHE A 1 99  ? 118.256 118.782 82.055  1.00 57.64  ? 184 PHE A N   1 
ATOM 649  C CA  . PHE A 1 99  ? 117.629 119.428 83.205  1.00 51.43  ? 184 PHE A CA  1 
ATOM 650  C C   . PHE A 1 99  ? 116.160 119.044 83.313  1.00 53.53  ? 184 PHE A C   1 
ATOM 651  O O   . PHE A 1 99  ? 115.682 118.663 84.389  1.00 57.57  ? 184 PHE A O   1 
ATOM 652  C CB  . PHE A 1 99  ? 117.786 120.948 83.108  1.00 54.35  ? 184 PHE A CB  1 
ATOM 653  C CG  . PHE A 1 99  ? 117.245 121.698 84.300  1.00 56.01  ? 184 PHE A CG  1 
ATOM 654  C CD1 . PHE A 1 99  ? 115.903 122.044 84.370  1.00 55.92  ? 184 PHE A CD1 1 
ATOM 655  C CD2 . PHE A 1 99  ? 118.076 122.052 85.350  1.00 55.64  ? 184 PHE A CD2 1 
ATOM 656  C CE1 . PHE A 1 99  ? 115.402 122.730 85.461  1.00 53.75  ? 184 PHE A CE1 1 
ATOM 657  C CE2 . PHE A 1 99  ? 117.579 122.739 86.445  1.00 53.94  ? 184 PHE A CE2 1 
ATOM 658  C CZ  . PHE A 1 99  ? 116.241 123.078 86.499  1.00 54.09  ? 184 PHE A CZ  1 
ATOM 659  N N   . TYR A 1 100 ? 115.426 119.140 82.203  1.00 56.16  ? 185 TYR A N   1 
ATOM 660  C CA  . TYR A 1 100 ? 114.008 118.799 82.239  1.00 54.05  ? 185 TYR A CA  1 
ATOM 661  C C   . TYR A 1 100 ? 113.803 117.309 82.492  1.00 54.58  ? 185 TYR A C   1 
ATOM 662  O O   . TYR A 1 100 ? 112.950 116.928 83.300  1.00 60.28  ? 185 TYR A O   1 
ATOM 663  C CB  . TYR A 1 100 ? 113.329 119.245 80.946  1.00 50.39  ? 185 TYR A CB  1 
ATOM 664  C CG  . TYR A 1 100 ? 113.166 120.747 80.862  1.00 50.56  ? 185 TYR A CG  1 
ATOM 665  C CD1 . TYR A 1 100 ? 112.533 121.451 81.878  1.00 54.02  ? 185 TYR A CD1 1 
ATOM 666  C CD2 . TYR A 1 100 ? 113.654 121.462 79.776  1.00 54.04  ? 185 TYR A CD2 1 
ATOM 667  C CE1 . TYR A 1 100 ? 112.385 122.824 81.813  1.00 52.42  ? 185 TYR A CE1 1 
ATOM 668  C CE2 . TYR A 1 100 ? 113.512 122.836 79.702  1.00 55.15  ? 185 TYR A CE2 1 
ATOM 669  C CZ  . TYR A 1 100 ? 112.876 123.511 80.723  1.00 55.63  ? 185 TYR A CZ  1 
ATOM 670  O OH  . TYR A 1 100 ? 112.730 124.877 80.655  1.00 58.48  ? 185 TYR A OH  1 
ATOM 671  N N   . THR A 1 101 ? 114.600 116.456 81.843  1.00 52.99  ? 186 THR A N   1 
ATOM 672  C CA  . THR A 1 101 ? 114.495 115.014 82.036  1.00 52.04  ? 186 THR A CA  1 
ATOM 673  C C   . THR A 1 101 ? 114.719 114.627 83.491  1.00 54.46  ? 186 THR A C   1 
ATOM 674  O O   . THR A 1 101 ? 114.134 113.650 83.972  1.00 62.49  ? 186 THR A O   1 
ATOM 675  C CB  . THR A 1 101 ? 115.502 114.306 81.121  1.00 54.04  ? 186 THR A CB  1 
ATOM 676  O OG1 . THR A 1 101 ? 115.051 114.382 79.762  1.00 63.87  ? 186 THR A OG1 1 
ATOM 677  C CG2 . THR A 1 101 ? 115.674 112.840 81.502  1.00 50.85  ? 186 THR A CG2 1 
ATOM 678  N N   . VAL A 1 102 ? 115.543 115.381 84.211  1.00 52.29  ? 187 VAL A N   1 
ATOM 679  C CA  . VAL A 1 102 ? 115.780 115.072 85.617  1.00 49.91  ? 187 VAL A CA  1 
ATOM 680  C C   . VAL A 1 102 ? 114.703 115.672 86.518  1.00 54.63  ? 187 VAL A C   1 
ATOM 681  O O   . VAL A 1 102 ? 114.245 115.016 87.457  1.00 60.43  ? 187 VAL A O   1 
ATOM 682  C CB  . VAL A 1 102 ? 117.190 115.535 86.033  1.00 52.86  ? 187 VAL A CB  1 
ATOM 683  C CG1 . VAL A 1 102 ? 117.404 115.313 87.521  1.00 55.61  ? 187 VAL A CG1 1 
ATOM 684  C CG2 . VAL A 1 102 ? 118.246 114.786 85.238  1.00 53.41  ? 187 VAL A CG2 1 
ATOM 685  N N   . ILE A 1 103 ? 114.258 116.901 86.260  1.00 54.68  ? 188 ILE A N   1 
ATOM 686  C CA  . ILE A 1 103 ? 113.403 117.579 87.236  1.00 49.54  ? 188 ILE A CA  1 
ATOM 687  C C   . ILE A 1 103 ? 111.921 117.283 87.016  1.00 53.22  ? 188 ILE A C   1 
ATOM 688  O O   . ILE A 1 103 ? 111.169 117.149 87.985  1.00 57.95  ? 188 ILE A O   1 
ATOM 689  C CB  . ILE A 1 103 ? 113.683 119.097 87.245  1.00 49.87  ? 188 ILE A CB  1 
ATOM 690  C CG1 . ILE A 1 103 ? 113.080 119.731 88.501  1.00 49.68  ? 188 ILE A CG1 1 
ATOM 691  C CG2 . ILE A 1 103 ? 113.153 119.778 85.990  1.00 55.01  ? 188 ILE A CG2 1 
ATOM 692  C CD1 . ILE A 1 103 ? 113.579 121.123 88.782  1.00 52.25  ? 188 ILE A CD1 1 
ATOM 693  N N   . VAL A 1 104 ? 111.460 117.187 85.762  1.00 57.05  ? 189 VAL A N   1 
ATOM 694  C CA  . VAL A 1 104 ? 110.031 116.974 85.513  1.00 51.73  ? 189 VAL A CA  1 
ATOM 695  C C   . VAL A 1 104 ? 109.527 115.685 86.144  1.00 57.66  ? 189 VAL A C   1 
ATOM 696  O O   . VAL A 1 104 ? 108.415 115.689 86.695  1.00 60.90  ? 189 VAL A O   1 
ATOM 697  C CB  . VAL A 1 104 ? 109.737 117.070 84.009  1.00 48.74  ? 189 VAL A CB  1 
ATOM 698  C CG1 . VAL A 1 104 ? 108.285 116.721 83.719  1.00 56.61  ? 189 VAL A CG1 1 
ATOM 699  C CG2 . VAL A 1 104 ? 110.064 118.466 83.496  1.00 51.06  ? 189 VAL A CG2 1 
ATOM 700  N N   . PRO A 1 105 ? 110.248 114.555 86.092  1.00 57.30  ? 190 PRO A N   1 
ATOM 701  C CA  . PRO A 1 105 ? 109.770 113.369 86.822  1.00 53.30  ? 190 PRO A CA  1 
ATOM 702  C C   . PRO A 1 105 ? 109.524 113.615 88.300  1.00 58.45  ? 190 PRO A C   1 
ATOM 703  O O   . PRO A 1 105 ? 108.520 113.134 88.834  1.00 65.94  ? 190 PRO A O   1 
ATOM 704  C CB  . PRO A 1 105 ? 110.899 112.359 86.593  1.00 55.66  ? 190 PRO A CB  1 
ATOM 705  C CG  . PRO A 1 105 ? 111.362 112.680 85.229  1.00 56.10  ? 190 PRO A CG  1 
ATOM 706  C CD  . PRO A 1 105 ? 111.323 114.192 85.149  1.00 56.64  ? 190 PRO A CD  1 
ATOM 707  N N   . PHE A 1 106 ? 110.395 114.372 88.974  1.00 59.65  ? 191 PHE A N   1 
ATOM 708  C CA  . PHE A 1 106 ? 110.172 114.678 90.385  1.00 54.90  ? 191 PHE A CA  1 
ATOM 709  C C   . PHE A 1 106 ? 108.872 115.449 90.584  1.00 55.93  ? 191 PHE A C   1 
ATOM 710  O O   . PHE A 1 106 ? 108.062 115.112 91.457  1.00 60.71  ? 191 PHE A O   1 
ATOM 711  C CB  . PHE A 1 106 ? 111.354 115.474 90.942  1.00 54.49  ? 191 PHE A CB  1 
ATOM 712  C CG  . PHE A 1 106 ? 112.532 114.628 91.338  1.00 59.82  ? 191 PHE A CG  1 
ATOM 713  C CD1 . PHE A 1 106 ? 112.591 114.047 92.594  1.00 59.54  ? 191 PHE A CD1 1 
ATOM 714  C CD2 . PHE A 1 106 ? 113.577 114.412 90.457  1.00 59.49  ? 191 PHE A CD2 1 
ATOM 715  C CE1 . PHE A 1 106 ? 113.674 113.273 92.967  1.00 61.44  ? 191 PHE A CE1 1 
ATOM 716  C CE2 . PHE A 1 106 ? 114.661 113.635 90.822  1.00 60.21  ? 191 PHE A CE2 1 
ATOM 717  C CZ  . PHE A 1 106 ? 114.708 113.064 92.078  1.00 62.73  ? 191 PHE A CZ  1 
ATOM 718  N N   . ILE A 1 107 ? 108.654 116.484 89.771  1.00 56.41  ? 192 ILE A N   1 
ATOM 719  C CA  . ILE A 1 107 ? 107.477 117.334 89.935  1.00 53.07  ? 192 ILE A CA  1 
ATOM 720  C C   . ILE A 1 107 ? 106.205 116.537 89.673  1.00 55.69  ? 192 ILE A C   1 
ATOM 721  O O   . ILE A 1 107 ? 105.239 116.596 90.448  1.00 60.01  ? 192 ILE A O   1 
ATOM 722  C CB  . ILE A 1 107 ? 107.576 118.561 89.012  1.00 52.87  ? 192 ILE A CB  1 
ATOM 723  C CG1 . ILE A 1 107 ? 108.720 119.473 89.461  1.00 54.51  ? 192 ILE A CG1 1 
ATOM 724  C CG2 . ILE A 1 107 ? 106.261 119.325 88.992  1.00 56.13  ? 192 ILE A CG2 1 
ATOM 725  C CD1 . ILE A 1 107 ? 109.310 120.306 88.344  1.00 56.95  ? 192 ILE A CD1 1 
ATOM 726  N N   . ILE A 1 108 ? 106.189 115.771 88.578  1.00 55.79  ? 193 ILE A N   1 
ATOM 727  C CA  . ILE A 1 108 ? 104.991 115.007 88.248  1.00 57.17  ? 193 ILE A CA  1 
ATOM 728  C C   . ILE A 1 108 ? 104.752 113.912 89.278  1.00 60.62  ? 193 ILE A C   1 
ATOM 729  O O   . ILE A 1 108 ? 103.600 113.630 89.628  1.00 66.22  ? 193 ILE A O   1 
ATOM 730  C CB  . ILE A 1 108 ? 105.068 114.437 86.817  1.00 57.77  ? 193 ILE A CB  1 
ATOM 731  C CG1 . ILE A 1 108 ? 106.192 113.408 86.684  1.00 63.06  ? 193 ILE A CG1 1 
ATOM 732  C CG2 . ILE A 1 108 ? 105.247 115.560 85.804  1.00 55.42  ? 193 ILE A CG2 1 
ATOM 733  C CD1 . ILE A 1 108 ? 106.172 112.644 85.379  1.00 66.80  ? 193 ILE A CD1 1 
ATOM 734  N N   . TYR A 1 109 ? 105.816 113.288 89.796  1.00 58.05  ? 194 TYR A N   1 
ATOM 735  C CA  . TYR A 1 109 ? 105.635 112.275 90.827  1.00 56.68  ? 194 TYR A CA  1 
ATOM 736  C C   . TYR A 1 109 ? 105.059 112.871 92.100  1.00 62.12  ? 194 TYR A C   1 
ATOM 737  O O   . TYR A 1 109 ? 104.172 112.276 92.716  1.00 68.08  ? 194 TYR A O   1 
ATOM 738  C CB  . TYR A 1 109 ? 106.953 111.568 91.133  1.00 58.04  ? 194 TYR A CB  1 
ATOM 739  C CG  . TYR A 1 109 ? 106.788 110.519 92.206  1.00 59.32  ? 194 TYR A CG  1 
ATOM 740  C CD1 . TYR A 1 109 ? 106.211 109.291 91.919  1.00 66.74  ? 194 TYR A CD1 1 
ATOM 741  C CD2 . TYR A 1 109 ? 107.183 110.768 93.515  1.00 57.87  ? 194 TYR A CD2 1 
ATOM 742  C CE1 . TYR A 1 109 ? 106.042 108.337 92.900  1.00 67.74  ? 194 TYR A CE1 1 
ATOM 743  C CE2 . TYR A 1 109 ? 107.019 109.818 94.503  1.00 63.87  ? 194 TYR A CE2 1 
ATOM 744  C CZ  . TYR A 1 109 ? 106.449 108.604 94.190  1.00 67.38  ? 194 TYR A CZ  1 
ATOM 745  O OH  . TYR A 1 109 ? 106.283 107.653 95.170  1.00 70.35  ? 194 TYR A OH  1 
ATOM 746  N N   . PHE A 1 110 ? 105.556 114.034 92.522  1.00 64.49  ? 195 PHE A N   1 
ATOM 747  C CA  . PHE A 1 110 ? 105.035 114.630 93.747  1.00 56.39  ? 195 PHE A CA  1 
ATOM 748  C C   . PHE A 1 110 ? 103.587 115.075 93.570  1.00 58.67  ? 195 PHE A C   1 
ATOM 749  O O   . PHE A 1 110 ? 102.766 114.901 94.479  1.00 67.33  ? 195 PHE A O   1 
ATOM 750  C CB  . PHE A 1 110 ? 105.934 115.782 94.193  1.00 48.61  ? 195 PHE A CB  1 
ATOM 751  C CG  . PHE A 1 110 ? 107.261 115.325 94.730  1.00 53.54  ? 195 PHE A CG  1 
ATOM 752  C CD1 . PHE A 1 110 ? 107.328 114.261 95.614  1.00 55.41  ? 195 PHE A CD1 1 
ATOM 753  C CD2 . PHE A 1 110 ? 108.438 115.939 94.339  1.00 52.29  ? 195 PHE A CD2 1 
ATOM 754  C CE1 . PHE A 1 110 ? 108.542 113.823 96.107  1.00 52.13  ? 195 PHE A CE1 1 
ATOM 755  C CE2 . PHE A 1 110 ? 109.657 115.503 94.825  1.00 54.07  ? 195 PHE A CE2 1 
ATOM 756  C CZ  . PHE A 1 110 ? 109.708 114.446 95.714  1.00 55.01  ? 195 PHE A CZ  1 
ATOM 757  N N   . GLY A 1 111 ? 103.244 115.615 92.399  1.00 57.85  ? 196 GLY A N   1 
ATOM 758  C CA  . GLY A 1 111 ? 101.852 115.958 92.144  1.00 59.36  ? 196 GLY A CA  1 
ATOM 759  C C   . GLY A 1 111 ? 100.941 114.744 92.144  1.00 64.45  ? 196 GLY A C   1 
ATOM 760  O O   . GLY A 1 111 ? 99.878  114.746 92.774  1.00 72.56  ? 196 GLY A O   1 
ATOM 761  N N   . ALA A 1 112 ? 101.354 113.683 91.445  1.00 61.75  ? 197 ALA A N   1 
ATOM 762  C CA  . ALA A 1 112 ? 100.551 112.466 91.394  1.00 63.19  ? 197 ALA A CA  1 
ATOM 763  C C   . ALA A 1 112 ? 100.421 111.837 92.773  1.00 66.89  ? 197 ALA A C   1 
ATOM 764  O O   . ALA A 1 112 ? 99.363  111.302 93.123  1.00 75.24  ? 197 ALA A O   1 
ATOM 765  C CB  . ALA A 1 112 ? 101.165 111.475 90.406  1.00 64.74  ? 197 ALA A CB  1 
ATOM 766  N N   . PHE A 1 113 ? 101.490 111.883 93.569  1.00 64.63  ? 198 PHE A N   1 
ATOM 767  C CA  . PHE A 1 113 ? 101.424 111.363 94.926  1.00 64.88  ? 198 PHE A CA  1 
ATOM 768  C C   . PHE A 1 113 ? 100.450 112.166 95.774  1.00 65.31  ? 198 PHE A C   1 
ATOM 769  O O   . PHE A 1 113 ? 99.658  111.592 96.530  1.00 71.95  ? 198 PHE A O   1 
ATOM 770  C CB  . PHE A 1 113 ? 102.810 111.377 95.563  1.00 64.76  ? 198 PHE A CB  1 
ATOM 771  C CG  . PHE A 1 113 ? 102.838 110.777 96.927  1.00 66.42  ? 198 PHE A CG  1 
ATOM 772  C CD1 . PHE A 1 113 ? 102.963 109.410 97.089  1.00 69.12  ? 198 PHE A CD1 1 
ATOM 773  C CD2 . PHE A 1 113 ? 102.693 111.572 98.048  1.00 66.11  ? 198 PHE A CD2 1 
ATOM 774  C CE1 . PHE A 1 113 ? 102.973 108.851 98.343  1.00 69.04  ? 198 PHE A CE1 1 
ATOM 775  C CE2 . PHE A 1 113 ? 102.696 111.019 99.300  1.00 69.61  ? 198 PHE A CE2 1 
ATOM 776  C CZ  . PHE A 1 113 ? 102.838 109.655 99.449  1.00 70.97  ? 198 PHE A CZ  1 
ATOM 777  N N   . GLY A 1 114 ? 100.497 113.494 95.666  1.00 66.32  ? 199 GLY A N   1 
ATOM 778  C CA  . GLY A 1 114 ? 99.577  114.315 96.427  1.00 65.04  ? 199 GLY A CA  1 
ATOM 779  C C   . GLY A 1 114 ? 98.131  114.117 96.027  1.00 68.59  ? 199 GLY A C   1 
ATOM 780  O O   . GLY A 1 114 ? 97.234  114.199 96.870  1.00 70.30  ? 199 GLY A O   1 
ATOM 781  N N   . PHE A 1 115 ? 97.878  113.842 94.744  1.00 69.91  ? 200 PHE A N   1 
ATOM 782  C CA  . PHE A 1 115 ? 96.513  113.835 94.242  1.00 69.76  ? 200 PHE A CA  1 
ATOM 783  C C   . PHE A 1 115 ? 95.979  112.462 93.857  1.00 75.03  ? 200 PHE A C   1 
ATOM 784  O O   . PHE A 1 115 ? 94.757  112.292 93.810  1.00 80.80  ? 200 PHE A O   1 
ATOM 785  C CB  . PHE A 1 115 ? 96.397  114.773 93.033  1.00 69.30  ? 200 PHE A CB  1 
ATOM 786  C CG  . PHE A 1 115 ? 96.342  116.225 93.408  1.00 70.76  ? 200 PHE A CG  1 
ATOM 787  C CD1 . PHE A 1 115 ? 97.503  116.917 93.707  1.00 67.70  ? 200 PHE A CD1 1 
ATOM 788  C CD2 . PHE A 1 115 ? 95.132  116.893 93.479  1.00 76.53  ? 200 PHE A CD2 1 
ATOM 789  C CE1 . PHE A 1 115 ? 97.461  118.251 94.060  1.00 68.13  ? 200 PHE A CE1 1 
ATOM 790  C CE2 . PHE A 1 115 ? 95.082  118.228 93.831  1.00 76.41  ? 200 PHE A CE2 1 
ATOM 791  C CZ  . PHE A 1 115 ? 96.249  118.908 94.122  1.00 72.08  ? 200 PHE A CZ  1 
ATOM 792  N N   . VAL A 1 116 ? 96.841  111.485 93.583  1.00 73.26  ? 201 VAL A N   1 
ATOM 793  C CA  . VAL A 1 116 ? 96.367  110.174 93.148  1.00 70.85  ? 201 VAL A CA  1 
ATOM 794  C C   . VAL A 1 116 ? 96.930  109.077 94.042  1.00 73.07  ? 201 VAL A C   1 
ATOM 795  O O   . VAL A 1 116 ? 96.177  108.263 94.591  1.00 78.69  ? 201 VAL A O   1 
ATOM 796  C CB  . VAL A 1 116 ? 96.727  109.917 91.672  1.00 71.21  ? 201 VAL A CB  1 
ATOM 797  C CG1 . VAL A 1 116 ? 96.699  108.425 91.365  1.00 77.02  ? 201 VAL A CG1 1 
ATOM 798  C CG2 . VAL A 1 116 ? 95.779  110.673 90.756  1.00 74.68  ? 201 VAL A CG2 1 
ATOM 799  N N   . MET A 1 117 ? 98.256  109.046 94.196  1.00 70.70  ? 202 MET A N   1 
ATOM 800  C CA  . MET A 1 117 ? 98.891  107.920 94.872  1.00 70.36  ? 202 MET A CA  1 
ATOM 801  C C   . MET A 1 117 ? 98.561  107.882 96.359  1.00 75.09  ? 202 MET A C   1 
ATOM 802  O O   . MET A 1 117 ? 98.432  106.793 96.930  1.00 81.99  ? 202 MET A O   1 
ATOM 803  C CB  . MET A 1 117 ? 100.403 107.961 94.658  1.00 67.57  ? 202 MET A CB  1 
ATOM 804  C CG  . MET A 1 117 ? 100.816 107.729 93.212  1.00 70.31  ? 202 MET A CG  1 
ATOM 805  S SD  . MET A 1 117 ? 102.592 107.859 92.942  1.00 89.32  ? 202 MET A SD  1 
ATOM 806  C CE  . MET A 1 117 ? 103.172 106.380 93.767  1.00 80.01  ? 202 MET A CE  1 
ATOM 807  N N   . TYR A 1 118 ? 98.425  109.039 97.006  1.00 72.13  ? 203 TYR A N   1 
ATOM 808  C CA  . TYR A 1 118 ? 98.040  108.994 98.412  1.00 73.87  ? 203 TYR A CA  1 
ATOM 809  C C   . TYR A 1 118 ? 96.551  108.699 98.579  1.00 77.10  ? 203 TYR A C   1 
ATOM 810  O O   . TYR A 1 118 ? 96.198  107.845 99.402  1.00 84.51  ? 203 TYR A O   1 
ATOM 811  C CB  . TYR A 1 118 ? 98.399  110.285 99.152  1.00 70.40  ? 203 TYR A CB  1 
ATOM 812  C CG  . TYR A 1 118 ? 97.850  110.288 100.561 1.00 74.31  ? 203 TYR A CG  1 
ATOM 813  C CD1 . TYR A 1 118 ? 98.475  109.566 101.569 1.00 73.22  ? 203 TYR A CD1 1 
ATOM 814  C CD2 . TYR A 1 118 ? 96.693  110.989 100.877 1.00 78.47  ? 203 TYR A CD2 1 
ATOM 815  C CE1 . TYR A 1 118 ? 97.969  109.551 102.854 1.00 74.55  ? 203 TYR A CE1 1 
ATOM 816  C CE2 . TYR A 1 118 ? 96.181  110.979 102.158 1.00 79.06  ? 203 TYR A CE2 1 
ATOM 817  C CZ  . TYR A 1 118 ? 96.823  110.260 103.142 1.00 80.35  ? 203 TYR A CZ  1 
ATOM 818  O OH  . TYR A 1 118 ? 96.312  110.249 104.418 1.00 84.65  ? 203 TYR A OH  1 
ATOM 819  N N   . PRO A 1 119 ? 95.640  109.384 97.868  1.00 72.58  ? 204 PRO A N   1 
ATOM 820  C CA  . PRO A 1 119 ? 94.222  109.004 97.997  1.00 76.67  ? 204 PRO A CA  1 
ATOM 821  C C   . PRO A 1 119 ? 93.963  107.552 97.640  1.00 83.26  ? 204 PRO A C   1 
ATOM 822  O O   . PRO A 1 119 ? 93.189  106.875 98.329  1.00 89.34  ? 204 PRO A O   1 
ATOM 823  C CB  . PRO A 1 119 ? 93.514  109.965 97.032  1.00 79.28  ? 204 PRO A CB  1 
ATOM 824  C CG  . PRO A 1 119 ? 94.404  111.145 96.970  1.00 78.36  ? 204 PRO A CG  1 
ATOM 825  C CD  . PRO A 1 119 ? 95.793  110.586 97.024  1.00 74.78  ? 204 PRO A CD  1 
ATOM 826  N N   . LEU A 1 120 ? 94.594  107.053 96.582  1.00 80.05  ? 205 LEU A N   1 
ATOM 827  C CA  . LEU A 1 120 ? 94.502  105.640 96.215  1.00 81.46  ? 205 LEU A CA  1 
ATOM 828  C C   . LEU A 1 120 ? 95.682  104.845 96.769  1.00 85.47  ? 205 LEU A C   1 
ATOM 829  O O   . LEU A 1 120 ? 96.354  104.110 96.047  1.00 91.16  ? 205 LEU A O   1 
ATOM 830  C CB  . LEU A 1 120 ? 94.408  105.499 94.700  1.00 85.03  ? 205 LEU A CB  1 
ATOM 831  C CG  . LEU A 1 120 ? 93.068  105.788 94.012  1.00 89.52  ? 205 LEU A CG  1 
ATOM 832  C CD1 . LEU A 1 120 ? 92.731  107.276 94.010  1.00 80.22  ? 205 LEU A CD1 1 
ATOM 833  C CD2 . LEU A 1 120 ? 93.068  105.238 92.593  1.00 89.28  ? 205 LEU A CD2 1 
ATOM 834  N N   . SER A 1 121 ? 95.940  104.985 98.071  1.00 83.92  ? 206 SER A N   1 
ATOM 835  C CA  . SER A 1 121 ? 97.040  104.252 98.690  1.00 84.01  ? 206 SER A CA  1 
ATOM 836  C C   . SER A 1 121 ? 96.624  102.851 99.111  1.00 91.71  ? 206 SER A C   1 
ATOM 837  O O   . SER A 1 121 ? 97.448  101.929 99.083  1.00 93.47  ? 206 SER A O   1 
ATOM 838  C CB  . SER A 1 121 ? 97.581  105.019 99.896  1.00 80.83  ? 206 SER A CB  1 
ATOM 839  O OG  . SER A 1 121 ? 98.467  106.045 99.487  1.00 81.64  ? 206 SER A OG  1 
ATOM 840  N N   . ASN A 1 122 ? 95.364  102.672 99.510  1.00 94.69  ? 207 ASN A N   1 
ATOM 841  C CA  . ASN A 1 122 ? 94.867  101.344 99.843  1.00 98.46  ? 207 ASN A CA  1 
ATOM 842  C C   . ASN A 1 122 ? 94.784  100.441 98.620  1.00 100.03 ? 207 ASN A C   1 
ATOM 843  O O   . ASN A 1 122 ? 94.714  99.217  98.772  1.00 101.11 ? 207 ASN A O   1 
ATOM 844  C CB  . ASN A 1 122 ? 93.492  101.450 100.504 1.00 98.66  ? 207 ASN A CB  1 
ATOM 845  C CG  . ASN A 1 122 ? 93.557  102.053 101.894 1.00 107.32 ? 207 ASN A CG  1 
ATOM 846  O OD1 . ASN A 1 122 ? 94.449  101.735 102.680 1.00 109.16 ? 207 ASN A OD1 1 
ATOM 847  N ND2 . ASN A 1 122 ? 92.611  102.932 102.202 1.00 109.98 ? 207 ASN A ND2 1 
ATOM 848  N N   . TYR A 1 123 ? 94.797  101.015 97.418  1.00 98.62  ? 208 TYR A N   1 
ATOM 849  C CA  . TYR A 1 123 ? 94.619  100.255 96.187  1.00 100.14 ? 208 TYR A CA  1 
ATOM 850  C C   . TYR A 1 123 ? 95.943  99.804  95.581  1.00 101.31 ? 208 TYR A C   1 
ATOM 851  O O   . TYR A 1 123 ? 96.047  98.673  95.096  1.00 107.64 ? 208 TYR A O   1 
ATOM 852  C CB  . TYR A 1 123 ? 93.843  101.088 95.160  1.00 98.16  ? 208 TYR A CB  1 
ATOM 853  C CG  . TYR A 1 123 ? 92.356  101.213 95.428  1.00 101.25 ? 208 TYR A CG  1 
ATOM 854  C CD1 . TYR A 1 123 ? 91.851  101.190 96.723  1.00 100.83 ? 208 TYR A CD1 1 
ATOM 855  C CD2 . TYR A 1 123 ? 91.456  101.360 94.380  1.00 103.39 ? 208 TYR A CD2 1 
ATOM 856  C CE1 . TYR A 1 123 ? 90.496  101.307 96.965  1.00 101.35 ? 208 TYR A CE1 1 
ATOM 857  C CE2 . TYR A 1 123 ? 90.098  101.477 94.613  1.00 106.57 ? 208 TYR A CE2 1 
ATOM 858  C CZ  . TYR A 1 123 ? 89.624  101.450 95.908  1.00 107.86 ? 208 TYR A CZ  1 
ATOM 859  O OH  . TYR A 1 123 ? 88.274  101.566 96.145  1.00 111.93 ? 208 TYR A OH  1 
ATOM 860  N N   . ILE A 1 124 ? 96.961  100.666 95.599  1.00 96.76  ? 209 ILE A N   1 
ATOM 861  C CA  . ILE A 1 124 ? 98.230  100.346 94.953  1.00 96.92  ? 209 ILE A CA  1 
ATOM 862  C C   . ILE A 1 124 ? 99.201  99.606  95.868  1.00 99.75  ? 209 ILE A C   1 
ATOM 863  O O   . ILE A 1 124 ? 100.186 99.036  95.376  1.00 101.55 ? 209 ILE A O   1 
ATOM 864  C CB  . ILE A 1 124 ? 98.902  101.621 94.414  1.00 92.17  ? 209 ILE A CB  1 
ATOM 865  C CG1 . ILE A 1 124 ? 99.493  102.443 95.562  1.00 90.49  ? 209 ILE A CG1 1 
ATOM 866  C CG2 . ILE A 1 124 ? 97.907  102.450 93.615  1.00 92.38  ? 209 ILE A CG2 1 
ATOM 867  C CD1 . ILE A 1 124 ? 100.021 103.797 95.138  1.00 84.33  ? 209 ILE A CD1 1 
ATOM 868  N N   . HIS A 1 125 ? 98.957  99.597  97.172  1.00 100.13 ? 210 HIS A N   1 
ATOM 869  C CA  . HIS A 1 125 ? 99.866  98.933  98.100  1.00 101.06 ? 210 HIS A CA  1 
ATOM 870  C C   . HIS A 1 125 ? 99.531  97.448  98.186  1.00 105.87 ? 210 HIS A C   1 
ATOM 871  O O   . HIS A 1 125 ? 98.370  97.094  98.415  1.00 109.50 ? 210 HIS A O   1 
ATOM 872  C CB  . HIS A 1 125 ? 99.781  99.574  99.481  1.00 99.50  ? 210 HIS A CB  1 
ATOM 873  C CG  . HIS A 1 125 ? 100.642 100.788 99.634  1.00 90.84  ? 210 HIS A CG  1 
ATOM 874  N ND1 . HIS A 1 125 ? 100.501 101.674 100.681 1.00 86.00  ? 210 HIS A ND1 1 
ATOM 875  C CD2 . HIS A 1 125 ? 101.654 101.265 98.872  1.00 82.03  ? 210 HIS A CD2 1 
ATOM 876  C CE1 . HIS A 1 125 ? 101.388 102.645 100.555 1.00 78.90  ? 210 HIS A CE1 1 
ATOM 877  N NE2 . HIS A 1 125 ? 102.101 102.420 99.467  1.00 76.29  ? 210 HIS A NE2 1 
ATOM 878  N N   . PRO A 1 126 ? 100.508 96.558  98.007  1.00 104.79 ? 211 PRO A N   1 
ATOM 879  C CA  . PRO A 1 126 ? 100.239 95.106  98.062  1.00 109.77 ? 211 PRO A CA  1 
ATOM 880  C C   . PRO A 1 126 ? 100.251 94.562  99.488  1.00 116.33 ? 211 PRO A C   1 
ATOM 881  O O   . PRO A 1 126 ? 101.134 93.795  99.901  1.00 121.37 ? 211 PRO A O   1 
ATOM 882  C CB  . PRO A 1 126 ? 101.369 94.539  97.202  1.00 110.44 ? 211 PRO A CB  1 
ATOM 883  C CG  . PRO A 1 126 ? 102.522 95.461  97.479  1.00 105.90 ? 211 PRO A CG  1 
ATOM 884  C CD  . PRO A 1 126 ? 101.934 96.836  97.758  1.00 103.19 ? 211 PRO A CD  1 
ATOM 885  N N   . GLU A 1 127 ? 99.249  94.967  100.272 1.00 118.20 ? 212 GLU A N   1 
ATOM 886  C CA  . GLU A 1 127 ? 99.124  94.452  101.631 1.00 122.55 ? 212 GLU A CA  1 
ATOM 887  C C   . GLU A 1 127 ? 98.797  92.964  101.629 1.00 126.91 ? 212 GLU A C   1 
ATOM 888  O O   . GLU A 1 127 ? 99.281  92.215  102.485 1.00 126.75 ? 212 GLU A O   1 
ATOM 889  C CB  . GLU A 1 127 ? 98.059  95.235  102.398 1.00 123.80 ? 212 GLU A CB  1 
ATOM 890  C CG  . GLU A 1 127 ? 98.427  96.685  102.666 1.00 125.89 ? 212 GLU A CG  1 
ATOM 891  C CD  . GLU A 1 127 ? 97.317  97.447  103.363 1.00 136.45 ? 212 GLU A CD  1 
ATOM 892  O OE1 . GLU A 1 127 ? 96.197  96.905  103.468 1.00 141.54 ? 212 GLU A OE1 1 
ATOM 893  O OE2 . GLU A 1 127 ? 97.566  98.587  103.807 1.00 130.96 ? 212 GLU A OE2 1 
ATOM 894  N N   . ALA A 1 128 ? 97.973  92.520  100.678 1.00 128.39 ? 213 ALA A N   1 
ATOM 895  C CA  . ALA A 1 128 ? 97.618  91.110  100.577 1.00 125.62 ? 213 ALA A CA  1 
ATOM 896  C C   . ALA A 1 128 ? 98.754  90.250  100.044 1.00 126.20 ? 213 ALA A C   1 
ATOM 897  O O   . ALA A 1 128 ? 98.668  89.020  100.134 1.00 130.65 ? 213 ALA A O   1 
ATOM 898  C CB  . ALA A 1 128 ? 96.384  90.941  99.689  1.00 118.69 ? 213 ALA A CB  1 
ATOM 899  N N   . LEU A 1 129 ? 99.807  90.853  99.496  1.00 124.50 ? 214 LEU A N   1 
ATOM 900  C CA  . LEU A 1 129 ? 100.957 90.100  99.010  1.00 123.36 ? 214 LEU A CA  1 
ATOM 901  C C   . LEU A 1 129 ? 102.112 90.087  100.001 1.00 125.72 ? 214 LEU A C   1 
ATOM 902  O O   . LEU A 1 129 ? 102.739 89.040  100.192 1.00 125.16 ? 214 LEU A O   1 
ATOM 903  C CB  . LEU A 1 129 ? 101.435 90.661  97.664  1.00 120.03 ? 214 LEU A CB  1 
ATOM 904  C CG  . LEU A 1 129 ? 102.459 89.839  96.870  1.00 121.48 ? 214 LEU A CG  1 
ATOM 905  C CD1 . LEU A 1 129 ? 102.230 90.019  95.379  1.00 118.41 ? 214 LEU A CD1 1 
ATOM 906  C CD2 . LEU A 1 129 ? 103.893 90.216  97.224  1.00 121.83 ? 214 LEU A CD2 1 
ATOM 907  N N   . ALA A 1 130 ? 102.417 91.216  100.641 1.00 128.54 ? 215 ALA A N   1 
ATOM 908  C CA  . ALA A 1 130 ? 103.498 91.236  101.624 1.00 128.48 ? 215 ALA A CA  1 
ATOM 909  C C   . ALA A 1 130 ? 103.011 90.891  103.023 1.00 129.94 ? 215 ALA A C   1 
ATOM 910  O O   . ALA A 1 130 ? 103.362 91.550  104.006 1.00 129.68 ? 215 ALA A O   1 
ATOM 911  C CB  . ALA A 1 130 ? 104.183 92.598  101.610 1.00 116.63 ? 215 ALA A CB  1 
ATOM 912  N N   . ASP A 1 131 ? 102.199 89.855  103.123 1.00 132.29 ? 216 ASP A N   1 
ATOM 913  C CA  . ASP A 1 131 ? 101.962 89.017  104.291 1.00 132.08 ? 216 ASP A CA  1 
ATOM 914  C C   . ASP A 1 131 ? 102.038 87.547  103.919 1.00 132.68 ? 216 ASP A C   1 
ATOM 915  O O   . ASP A 1 131 ? 102.534 86.741  104.708 1.00 133.31 ? 216 ASP A O   1 
ATOM 916  C CB  . ASP A 1 131 ? 100.602 89.336  104.935 1.00 131.75 ? 216 ASP A CB  1 
ATOM 917  C CG  . ASP A 1 131 ? 99.456  89.241  103.953 1.00 133.00 ? 216 ASP A CG  1 
ATOM 918  O OD1 . ASP A 1 131 ? 99.692  89.468  102.750 1.00 133.43 ? 216 ASP A OD1 1 
ATOM 919  O OD2 . ASP A 1 131 ? 98.322  88.945  104.384 1.00 131.42 ? 216 ASP A OD2 1 
ATOM 920  N N   . LYS A 1 132 ? 101.554 87.187  102.727 1.00 132.61 ? 217 LYS A N   1 
ATOM 921  C CA  . LYS A 1 132 ? 101.869 85.895  102.127 1.00 132.82 ? 217 LYS A CA  1 
ATOM 922  C C   . LYS A 1 132 ? 103.374 85.683  102.053 1.00 134.32 ? 217 LYS A C   1 
ATOM 923  O O   . LYS A 1 132 ? 103.898 84.657  102.503 1.00 136.09 ? 217 LYS A O   1 
ATOM 924  C CB  . LYS A 1 132 ? 101.244 85.822  100.732 1.00 128.88 ? 217 LYS A CB  1 
ATOM 925  C CG  . LYS A 1 132 ? 101.687 84.643  99.882  1.00 130.45 ? 217 LYS A CG  1 
ATOM 926  C CD  . LYS A 1 132 ? 101.179 83.318  100.404 1.00 130.08 ? 217 LYS A CD  1 
ATOM 927  C CE  . LYS A 1 132 ? 101.446 82.218  99.388  1.00 128.35 ? 217 LYS A CE  1 
ATOM 928  N NZ  . LYS A 1 132 ? 102.905 81.992  99.192  1.00 125.55 ? 217 LYS A NZ  1 
ATOM 929  N N   . LEU A 1 133 ? 104.090 86.659  101.498 1.00 133.05 ? 218 LEU A N   1 
ATOM 930  C CA  . LEU A 1 133 ? 105.538 86.560  101.407 1.00 136.24 ? 218 LEU A CA  1 
ATOM 931  C C   . LEU A 1 133 ? 106.205 86.742  102.765 1.00 135.90 ? 218 LEU A C   1 
ATOM 932  O O   . LEU A 1 133 ? 107.360 86.335  102.936 1.00 136.18 ? 218 LEU A O   1 
ATOM 933  C CB  . LEU A 1 133 ? 106.054 87.582  100.388 1.00 135.77 ? 218 LEU A CB  1 
ATOM 934  C CG  . LEU A 1 133 ? 107.542 87.661  100.052 1.00 137.25 ? 218 LEU A CG  1 
ATOM 935  C CD1 . LEU A 1 133 ? 107.888 86.565  99.065  1.00 137.14 ? 218 LEU A CD1 1 
ATOM 936  C CD2 . LEU A 1 133 ? 107.865 89.011  99.445  1.00 129.39 ? 218 LEU A CD2 1 
ATOM 937  N N   . LEU A 1 134 ? 105.498 87.326  103.738 1.00 134.50 ? 219 LEU A N   1 
ATOM 938  C CA  . LEU A 1 134 ? 106.007 87.388  105.103 1.00 136.13 ? 219 LEU A CA  1 
ATOM 939  C C   . LEU A 1 134 ? 105.861 86.055  105.828 1.00 139.14 ? 219 LEU A C   1 
ATOM 940  O O   . LEU A 1 134 ? 106.685 85.729  106.688 1.00 137.05 ? 219 LEU A O   1 
ATOM 941  C CB  . LEU A 1 134 ? 105.301 88.497  105.885 1.00 134.84 ? 219 LEU A CB  1 
ATOM 942  C CG  . LEU A 1 134 ? 105.835 88.703  107.302 1.00 134.77 ? 219 LEU A CG  1 
ATOM 943  C CD1 . LEU A 1 134 ? 107.294 89.122  107.241 1.00 133.66 ? 219 LEU A CD1 1 
ATOM 944  C CD2 . LEU A 1 134 ? 105.006 89.731  108.052 1.00 130.97 ? 219 LEU A CD2 1 
ATOM 945  N N   . THR A 1 135 ? 104.817 85.282  105.523 1.00 139.49 ? 220 THR A N   1 
ATOM 946  C CA  . THR A 1 135 ? 104.801 83.893  105.966 1.00 136.18 ? 220 THR A CA  1 
ATOM 947  C C   . THR A 1 135 ? 105.764 83.037  105.157 1.00 135.03 ? 220 THR A C   1 
ATOM 948  O O   . THR A 1 135 ? 106.168 81.967  105.624 1.00 133.67 ? 220 THR A O   1 
ATOM 949  C CB  . THR A 1 135 ? 103.388 83.309  105.885 1.00 135.14 ? 220 THR A CB  1 
ATOM 950  O OG1 . THR A 1 135 ? 103.034 83.084  104.514 1.00 135.46 ? 220 THR A OG1 1 
ATOM 951  C CG2 . THR A 1 135 ? 102.375 84.237  106.539 1.00 132.02 ? 220 THR A CG2 1 
ATOM 952  N N   . THR A 1 136 ? 106.138 83.486  103.957 1.00 136.47 ? 221 THR A N   1 
ATOM 953  C CA  . THR A 1 136 ? 107.125 82.759  103.165 1.00 136.45 ? 221 THR A CA  1 
ATOM 954  C C   . THR A 1 136 ? 108.539 83.020  103.675 1.00 137.33 ? 221 THR A C   1 
ATOM 955  O O   . THR A 1 136 ? 109.309 82.080  103.906 1.00 138.46 ? 221 THR A O   1 
ATOM 956  C CB  . THR A 1 136 ? 107.002 83.147  101.691 1.00 136.07 ? 221 THR A CB  1 
ATOM 957  O OG1 . THR A 1 136 ? 105.684 82.836  101.221 1.00 134.75 ? 221 THR A OG1 1 
ATOM 958  C CG2 . THR A 1 136 ? 108.019 82.388  100.854 1.00 133.50 ? 221 THR A CG2 1 
ATOM 959  N N   . LEU A 1 137 ? 108.897 84.289  103.858 1.00 137.84 ? 222 LEU A N   1 
ATOM 960  C CA  . LEU A 1 137 ? 110.224 84.677  104.321 1.00 140.56 ? 222 LEU A CA  1 
ATOM 961  C C   . LEU A 1 137 ? 110.183 85.036  105.801 1.00 139.10 ? 222 LEU A C   1 
ATOM 962  O O   . LEU A 1 137 ? 109.263 85.717  106.260 1.00 138.32 ? 222 LEU A O   1 
ATOM 963  C CB  . LEU A 1 137 ? 110.764 85.860  103.513 1.00 138.25 ? 222 LEU A CB  1 
ATOM 964  C CG  . LEU A 1 137 ? 111.446 85.555  102.176 1.00 135.11 ? 222 LEU A CG  1 
ATOM 965  C CD1 . LEU A 1 137 ? 110.444 85.115  101.124 1.00 132.48 ? 222 LEU A CD1 1 
ATOM 966  C CD2 . LEU A 1 137 ? 112.226 86.767  101.690 1.00 128.50 ? 222 LEU A CD2 1 
ATOM 967  N N   . GLY A 1 138 ? 111.201 84.595  106.538 1.00 138.83 ? 223 GLY A N   1 
ATOM 968  C CA  . GLY A 1 138 ? 111.231 84.729  107.976 1.00 140.36 ? 223 GLY A CA  1 
ATOM 969  C C   . GLY A 1 138 ? 111.186 86.162  108.470 1.00 141.23 ? 223 GLY A C   1 
ATOM 970  O O   . GLY A 1 138 ? 111.319 87.119  107.700 1.00 140.67 ? 223 GLY A O   1 
ATOM 971  N N   . PRO A 1 139 ? 110.991 86.332  109.782 1.00 142.03 ? 224 PRO A N   1 
ATOM 972  C CA  . PRO A 1 139 ? 110.898 87.691  110.345 1.00 139.53 ? 224 PRO A CA  1 
ATOM 973  C C   . PRO A 1 139 ? 112.163 88.513  110.174 1.00 139.11 ? 224 PRO A C   1 
ATOM 974  O O   . PRO A 1 139 ? 112.087 89.746  110.236 1.00 134.62 ? 224 PRO A O   1 
ATOM 975  C CB  . PRO A 1 139 ? 110.597 87.439  111.830 1.00 136.25 ? 224 PRO A CB  1 
ATOM 976  C CG  . PRO A 1 139 ? 110.080 86.033  111.890 1.00 134.83 ? 224 PRO A CG  1 
ATOM 977  C CD  . PRO A 1 139 ? 110.805 85.296  110.810 1.00 138.24 ? 224 PRO A CD  1 
ATOM 978  N N   . ARG A 1 140 ? 113.318 87.876  109.966 1.00 140.86 ? 225 ARG A N   1 
ATOM 979  C CA  . ARG A 1 140 ? 114.543 88.621  109.702 1.00 140.06 ? 225 ARG A CA  1 
ATOM 980  C C   . ARG A 1 140 ? 114.422 89.472  108.445 1.00 140.01 ? 225 ARG A C   1 
ATOM 981  O O   . ARG A 1 140 ? 115.104 90.497  108.331 1.00 139.93 ? 225 ARG A O   1 
ATOM 982  C CB  . ARG A 1 140 ? 115.724 87.653  109.580 1.00 135.70 ? 225 ARG A CB  1 
ATOM 983  C CG  . ARG A 1 140 ? 117.074 88.315  109.346 1.00 132.38 ? 225 ARG A CG  1 
ATOM 984  C CD  . ARG A 1 140 ? 117.427 89.263  110.482 1.00 133.53 ? 225 ARG A CD  1 
ATOM 985  N NE  . ARG A 1 140 ? 118.704 89.931  110.262 1.00 133.71 ? 225 ARG A NE  1 
ATOM 986  C CZ  . ARG A 1 140 ? 119.143 90.959  110.975 1.00 130.36 ? 225 ARG A CZ  1 
ATOM 987  N NH1 . ARG A 1 140 ? 118.430 91.468  111.966 1.00 130.05 ? 225 ARG A NH1 1 
ATOM 988  N NH2 . ARG A 1 140 ? 120.328 91.490  110.687 1.00 122.87 ? 225 ARG A NH2 1 
ATOM 989  N N   . PHE A 1 141 ? 113.556 89.081  107.510 1.00 137.51 ? 226 PHE A N   1 
ATOM 990  C CA  . PHE A 1 141 ? 113.287 89.854  106.309 1.00 134.52 ? 226 PHE A CA  1 
ATOM 991  C C   . PHE A 1 141 ? 112.171 90.873  106.507 1.00 128.52 ? 226 PHE A C   1 
ATOM 992  O O   . PHE A 1 141 ? 111.578 91.325  105.522 1.00 122.79 ? 226 PHE A O   1 
ATOM 993  C CB  . PHE A 1 141 ? 112.943 88.924  105.143 1.00 133.36 ? 226 PHE A CB  1 
ATOM 994  C CG  . PHE A 1 141 ? 114.087 88.059  104.696 1.00 133.09 ? 226 PHE A CG  1 
ATOM 995  C CD1 . PHE A 1 141 ? 114.468 86.949  105.433 1.00 132.95 ? 226 PHE A CD1 1 
ATOM 996  C CD2 . PHE A 1 141 ? 114.788 88.361  103.540 1.00 133.02 ? 226 PHE A CD2 1 
ATOM 997  C CE1 . PHE A 1 141 ? 115.520 86.155  105.023 1.00 135.21 ? 226 PHE A CE1 1 
ATOM 998  C CE2 . PHE A 1 141 ? 115.842 87.570  103.125 1.00 138.10 ? 226 PHE A CE2 1 
ATOM 999  C CZ  . PHE A 1 141 ? 116.208 86.465  103.868 1.00 138.17 ? 226 PHE A CZ  1 
ATOM 1000 N N   . MET A 1 142 ? 111.872 91.241  107.757 1.00 129.81 ? 227 MET A N   1 
ATOM 1001 C CA  . MET A 1 142 ? 110.874 92.273  108.016 1.00 126.99 ? 227 MET A CA  1 
ATOM 1002 C C   . MET A 1 142 ? 111.235 93.594  107.351 1.00 120.18 ? 227 MET A C   1 
ATOM 1003 O O   . MET A 1 142 ? 110.340 94.393  107.057 1.00 116.79 ? 227 MET A O   1 
ATOM 1004 C CB  . MET A 1 142 ? 110.709 92.478  109.525 1.00 126.84 ? 227 MET A CB  1 
ATOM 1005 C CG  . MET A 1 142 ? 109.599 93.446  109.924 1.00 121.44 ? 227 MET A CG  1 
ATOM 1006 S SD  . MET A 1 142 ? 108.005 93.088  109.166 1.00 132.45 ? 227 MET A SD  1 
ATOM 1007 C CE  . MET A 1 142 ? 107.681 91.471  109.860 1.00 122.82 ? 227 MET A CE  1 
ATOM 1008 N N   . GLY A 1 143 ? 112.519 93.833  107.098 1.00 116.98 ? 228 GLY A N   1 
ATOM 1009 C CA  . GLY A 1 143 ? 112.959 95.055  106.473 1.00 106.08 ? 228 GLY A CA  1 
ATOM 1010 C C   . GLY A 1 143 ? 112.371 95.253  105.092 1.00 105.66 ? 228 GLY A C   1 
ATOM 1011 O O   . GLY A 1 143 ? 111.489 96.093  104.898 1.00 104.86 ? 228 GLY A O   1 
ATOM 1012 N N   . PRO A 1 144 ? 112.813 94.455  104.110 1.00 104.25 ? 229 PRO A N   1 
ATOM 1013 C CA  . PRO A 1 144 ? 112.321 94.658  102.736 1.00 100.96 ? 229 PRO A CA  1 
ATOM 1014 C C   . PRO A 1 144 ? 110.814 94.532  102.606 1.00 97.13  ? 229 PRO A C   1 
ATOM 1015 O O   . PRO A 1 144 ? 110.197 95.379  101.943 1.00 94.51  ? 229 PRO A O   1 
ATOM 1016 C CB  . PRO A 1 144 ? 113.051 93.568  101.935 1.00 105.32 ? 229 PRO A CB  1 
ATOM 1017 C CG  . PRO A 1 144 ? 114.208 93.162  102.796 1.00 106.99 ? 229 PRO A CG  1 
ATOM 1018 C CD  . PRO A 1 144 ? 113.742 93.316  104.202 1.00 106.81 ? 229 PRO A CD  1 
ATOM 1019 N N   . ILE A 1 145 ? 110.207 93.531  103.253 1.00 101.21 ? 230 ILE A N   1 
ATOM 1020 C CA  . ILE A 1 145 ? 108.756 93.366  103.215 1.00 101.18 ? 230 ILE A CA  1 
ATOM 1021 C C   . ILE A 1 145 ? 108.065 94.681  103.516 1.00 97.55  ? 230 ILE A C   1 
ATOM 1022 O O   . ILE A 1 145 ? 107.183 95.119  102.763 1.00 101.33 ? 230 ILE A O   1 
ATOM 1023 C CB  . ILE A 1 145 ? 108.313 92.275  104.214 1.00 106.48 ? 230 ILE A CB  1 
ATOM 1024 C CG1 . ILE A 1 145 ? 108.974 90.935  103.893 1.00 112.86 ? 230 ILE A CG1 1 
ATOM 1025 C CG2 . ILE A 1 145 ? 106.798 92.140  104.223 1.00 111.51 ? 230 ILE A CG2 1 
ATOM 1026 C CD1 . ILE A 1 145 ? 108.627 90.402  102.543 1.00 113.09 ? 230 ILE A CD1 1 
ATOM 1027 N N   . ALA A 1 146 ? 108.493 95.356  104.587 1.00 94.95  ? 231 ALA A N   1 
ATOM 1028 C CA  . ALA A 1 146 ? 107.875 96.613  104.986 1.00 91.68  ? 231 ALA A CA  1 
ATOM 1029 C C   . ALA A 1 146 ? 107.801 97.591  103.823 1.00 89.07  ? 231 ALA A C   1 
ATOM 1030 O O   . ALA A 1 146 ? 106.726 98.135  103.535 1.00 88.81  ? 231 ALA A O   1 
ATOM 1031 C CB  . ALA A 1 146 ? 108.647 97.221  106.158 1.00 93.18  ? 231 ALA A CB  1 
ATOM 1032 N N   . ILE A 1 147 ? 108.915 97.789  103.106 1.00 88.09  ? 232 ILE A N   1 
ATOM 1033 C CA  . ILE A 1 147 ? 108.896 98.734  101.993 1.00 78.59  ? 232 ILE A CA  1 
ATOM 1034 C C   . ILE A 1 147 ? 107.831 98.343  100.984 1.00 82.18  ? 232 ILE A C   1 
ATOM 1035 O O   . ILE A 1 147 ? 107.017 99.178  100.577 1.00 86.28  ? 232 ILE A O   1 
ATOM 1036 C CB  . ILE A 1 147 ? 110.278 98.865  101.326 1.00 77.76  ? 232 ILE A CB  1 
ATOM 1037 C CG1 . ILE A 1 147 ? 111.320 99.419  102.296 1.00 76.11  ? 232 ILE A CG1 1 
ATOM 1038 C CG2 . ILE A 1 147 ? 110.189 99.741  100.082 1.00 76.17  ? 232 ILE A CG2 1 
ATOM 1039 C CD1 . ILE A 1 147 ? 112.044 98.409  103.112 1.00 77.43  ? 232 ILE A CD1 1 
ATOM 1040 N N   . LEU A 1 148 ? 107.784 97.063  100.607 1.00 86.13  ? 233 LEU A N   1 
ATOM 1041 C CA  . LEU A 1 148 ? 106.778 96.611  99.655  1.00 87.28  ? 233 LEU A CA  1 
ATOM 1042 C C   . LEU A 1 148 ? 105.413 97.068  100.140 1.00 86.60  ? 233 LEU A C   1 
ATOM 1043 O O   . LEU A 1 148 ? 104.674 97.733  99.406  1.00 87.09  ? 233 LEU A O   1 
ATOM 1044 C CB  . LEU A 1 148 ? 106.813 95.088  99.498  1.00 91.17  ? 233 LEU A CB  1 
ATOM 1045 C CG  . LEU A 1 148 ? 107.884 94.501  98.574  1.00 94.91  ? 233 LEU A CG  1 
ATOM 1046 C CD1 . LEU A 1 148 ? 107.957 92.991  98.737  1.00 98.92  ? 233 LEU A CD1 1 
ATOM 1047 C CD2 . LEU A 1 148 ? 107.603 94.874  97.128  1.00 91.37  ? 233 LEU A CD2 1 
ATOM 1048 N N   . ARG A 1 149 ? 105.135 96.806  101.417 1.00 88.20  ? 234 ARG A N   1 
ATOM 1049 C CA  . ARG A 1 149 ? 103.824 97.072  101.987 1.00 88.91  ? 234 ARG A CA  1 
ATOM 1050 C C   . ARG A 1 149 ? 103.411 98.529  101.829 1.00 88.47  ? 234 ARG A C   1 
ATOM 1051 O O   . ARG A 1 149 ? 102.214 98.811  101.709 1.00 93.98  ? 234 ARG A O   1 
ATOM 1052 C CB  . ARG A 1 149 ? 103.830 96.664  103.463 1.00 91.26  ? 234 ARG A CB  1 
ATOM 1053 C CG  . ARG A 1 149 ? 102.477 96.642  104.136 1.00 97.12  ? 234 ARG A CG  1 
ATOM 1054 C CD  . ARG A 1 149 ? 102.631 96.243  105.593 1.00 102.62 ? 234 ARG A CD  1 
ATOM 1055 N NE  . ARG A 1 149 ? 102.821 94.802  105.720 1.00 111.84 ? 234 ARG A NE  1 
ATOM 1056 C CZ  . ARG A 1 149 ? 101.857 93.938  106.005 1.00 118.23 ? 234 ARG A CZ  1 
ATOM 1057 N NH1 . ARG A 1 149 ? 100.612 94.335  106.209 1.00 114.66 ? 234 ARG A NH1 1 
ATOM 1058 N NH2 . ARG A 1 149 ? 102.148 92.642  106.085 1.00 122.98 ? 234 ARG A NH2 1 
ATOM 1059 N N   . ILE A 1 150 ? 104.368 99.458  101.828 1.00 83.81  ? 235 ILE A N   1 
ATOM 1060 C CA  . ILE A 1 150 ? 104.068 100.867 101.597 1.00 80.27  ? 235 ILE A CA  1 
ATOM 1061 C C   . ILE A 1 150 ? 104.962 101.458 100.510 1.00 77.46  ? 235 ILE A C   1 
ATOM 1062 O O   . ILE A 1 150 ? 105.300 102.648 100.562 1.00 74.96  ? 235 ILE A O   1 
ATOM 1063 C CB  . ILE A 1 150 ? 104.143 101.678 102.908 1.00 75.47  ? 235 ILE A CB  1 
ATOM 1064 C CG1 . ILE A 1 150 ? 105.583 101.880 103.385 1.00 74.15  ? 235 ILE A CG1 1 
ATOM 1065 C CG2 . ILE A 1 150 ? 103.286 101.052 103.985 1.00 83.99  ? 235 ILE A CG2 1 
ATOM 1066 C CD1 . ILE A 1 150 ? 105.773 103.147 104.180 1.00 72.48  ? 235 ILE A CD1 1 
ATOM 1067 N N   . TRP A 1 151 ? 105.337 100.642 99.515  1.00 80.65  ? 236 TRP A N   1 
ATOM 1068 C CA  . TRP A 1 151 ? 106.246 101.062 98.444  1.00 71.45  ? 236 TRP A CA  1 
ATOM 1069 C C   . TRP A 1 151 ? 106.058 102.516 98.018  1.00 70.20  ? 236 TRP A C   1 
ATOM 1070 O O   . TRP A 1 151 ? 107.026 103.287 98.030  1.00 71.09  ? 236 TRP A O   1 
ATOM 1071 C CB  . TRP A 1 151 ? 106.107 100.110 97.245  1.00 72.41  ? 236 TRP A CB  1 
ATOM 1072 C CG  . TRP A 1 151 ? 104.866 100.288 96.413  1.00 76.38  ? 236 TRP A CG  1 
ATOM 1073 C CD1 . TRP A 1 151 ? 103.679 99.633  96.573  1.00 83.08  ? 236 TRP A CD1 1 
ATOM 1074 C CD2 . TRP A 1 151 ? 104.693 101.161 95.289  1.00 75.34  ? 236 TRP A CD2 1 
ATOM 1075 N NE1 . TRP A 1 151 ? 102.776 100.050 95.628  1.00 86.77  ? 236 TRP A NE1 1 
ATOM 1076 C CE2 . TRP A 1 151 ? 103.372 100.988 94.827  1.00 82.22  ? 236 TRP A CE2 1 
ATOM 1077 C CE3 . TRP A 1 151 ? 105.521 102.078 94.634  1.00 73.65  ? 236 TRP A CE3 1 
ATOM 1078 C CZ2 . TRP A 1 151 ? 102.862 101.695 93.739  1.00 84.65  ? 236 TRP A CZ2 1 
ATOM 1079 C CZ3 . TRP A 1 151 ? 105.012 102.779 93.555  1.00 76.52  ? 236 TRP A CZ3 1 
ATOM 1080 C CH2 . TRP A 1 151 ? 103.696 102.583 93.118  1.00 81.08  ? 236 TRP A CH2 1 
ATOM 1081 N N   . SER A 1 152 ? 104.817 102.915 97.718  1.00 76.96  ? 237 SER A N   1 
ATOM 1082 C CA  . SER A 1 152 ? 104.548 104.288 97.295  1.00 72.76  ? 237 SER A CA  1 
ATOM 1083 C C   . SER A 1 152 ? 105.191 105.292 98.240  1.00 68.43  ? 237 SER A C   1 
ATOM 1084 O O   . SER A 1 152 ? 106.105 106.030 97.850  1.00 71.40  ? 237 SER A O   1 
ATOM 1085 C CB  . SER A 1 152 ? 103.037 104.521 97.213  1.00 72.22  ? 237 SER A CB  1 
ATOM 1086 O OG  . SER A 1 152 ? 102.744 105.860 96.858  1.00 73.96  ? 237 SER A OG  1 
ATOM 1087 N N   . PHE A 1 153 ? 104.764 105.289 99.506  1.00 67.22  ? 238 PHE A N   1 
ATOM 1088 C CA  . PHE A 1 153 ? 105.343 106.201 100.485 1.00 60.84  ? 238 PHE A CA  1 
ATOM 1089 C C   . PHE A 1 153 ? 106.857 106.066 100.539 1.00 67.31  ? 238 PHE A C   1 
ATOM 1090 O O   . PHE A 1 153 ? 107.564 107.082 100.513 1.00 71.75  ? 238 PHE A O   1 
ATOM 1091 C CB  . PHE A 1 153 ? 104.740 105.963 101.875 1.00 60.98  ? 238 PHE A CB  1 
ATOM 1092 C CG  . PHE A 1 153 ? 103.238 106.132 101.942 1.00 65.12  ? 238 PHE A CG  1 
ATOM 1093 C CD1 . PHE A 1 153 ? 102.519 106.618 100.863 1.00 69.51  ? 238 PHE A CD1 1 
ATOM 1094 C CD2 . PHE A 1 153 ? 102.550 105.811 103.101 1.00 72.35  ? 238 PHE A CD2 1 
ATOM 1095 C CE1 . PHE A 1 153 ? 101.149 106.773 100.932 1.00 70.90  ? 238 PHE A CE1 1 
ATOM 1096 C CE2 . PHE A 1 153 ? 101.178 105.964 103.177 1.00 78.57  ? 238 PHE A CE2 1 
ATOM 1097 C CZ  . PHE A 1 153 ? 100.478 106.446 102.091 1.00 72.11  ? 238 PHE A CZ  1 
ATOM 1098 N N   . CYS A 1 154 ? 107.373 104.832 100.558 1.00 70.53  ? 239 CYS A N   1 
ATOM 1099 C CA  . CYS A 1 154 ? 108.820 104.662 100.593 1.00 65.24  ? 239 CYS A CA  1 
ATOM 1100 C C   . CYS A 1 154 ? 109.468 105.321 99.388  1.00 63.71  ? 239 CYS A C   1 
ATOM 1101 O O   . CYS A 1 154 ? 110.443 106.069 99.535  1.00 65.61  ? 239 CYS A O   1 
ATOM 1102 C CB  . CYS A 1 154 ? 109.188 103.180 100.657 1.00 67.99  ? 239 CYS A CB  1 
ATOM 1103 S SG  . CYS A 1 154 ? 108.806 102.385 102.228 1.00 86.13  ? 239 CYS A SG  1 
ATOM 1104 N N   . LEU A 1 155 ? 108.902 105.104 98.197  1.00 62.54  ? 240 LEU A N   1 
ATOM 1105 C CA  . LEU A 1 155 ? 109.428 105.779 97.020  1.00 59.56  ? 240 LEU A CA  1 
ATOM 1106 C C   . LEU A 1 155 ? 109.418 107.284 97.230  1.00 60.06  ? 240 LEU A C   1 
ATOM 1107 O O   . LEU A 1 155 ? 110.438 107.951 97.008  1.00 62.00  ? 240 LEU A O   1 
ATOM 1108 C CB  . LEU A 1 155 ? 108.618 105.387 95.782  1.00 63.03  ? 240 LEU A CB  1 
ATOM 1109 C CG  . LEU A 1 155 ? 108.990 106.061 94.461  1.00 66.09  ? 240 LEU A CG  1 
ATOM 1110 C CD1 . LEU A 1 155 ? 110.445 105.797 94.117  1.00 64.76  ? 240 LEU A CD1 1 
ATOM 1111 C CD2 . LEU A 1 155 ? 108.085 105.561 93.348  1.00 67.42  ? 240 LEU A CD2 1 
ATOM 1112 N N   . PHE A 1 156 ? 108.303 107.817 97.744  1.00 60.42  ? 241 PHE A N   1 
ATOM 1113 C CA  . PHE A 1 156 ? 108.249 109.230 98.097  1.00 58.58  ? 241 PHE A CA  1 
ATOM 1114 C C   . PHE A 1 156 ? 109.449 109.608 98.947  1.00 58.51  ? 241 PHE A C   1 
ATOM 1115 O O   . PHE A 1 156 ? 110.231 110.494 98.574  1.00 66.33  ? 241 PHE A O   1 
ATOM 1116 C CB  . PHE A 1 156 ? 106.939 109.532 98.833  1.00 59.91  ? 241 PHE A CB  1 
ATOM 1117 C CG  . PHE A 1 156 ? 106.760 110.982 99.201  1.00 62.44  ? 241 PHE A CG  1 
ATOM 1118 C CD1 . PHE A 1 156 ? 107.259 111.479 100.395 1.00 59.02  ? 241 PHE A CD1 1 
ATOM 1119 C CD2 . PHE A 1 156 ? 106.089 111.846 98.352  1.00 63.76  ? 241 PHE A CD2 1 
ATOM 1120 C CE1 . PHE A 1 156 ? 107.093 112.809 100.734 1.00 55.09  ? 241 PHE A CE1 1 
ATOM 1121 C CE2 . PHE A 1 156 ? 105.920 113.178 98.686  1.00 62.09  ? 241 PHE A CE2 1 
ATOM 1122 C CZ  . PHE A 1 156 ? 106.423 113.659 99.878  1.00 57.27  ? 241 PHE A CZ  1 
ATOM 1123 N N   . TYR A 1 157 ? 109.657 108.880 100.051 1.00 55.02  ? 242 TYR A N   1 
ATOM 1124 C CA  . TYR A 1 157 ? 110.821 109.124 100.894 1.00 53.90  ? 242 TYR A CA  1 
ATOM 1125 C C   . TYR A 1 157 ? 112.080 109.198 100.048 1.00 58.73  ? 242 TYR A C   1 
ATOM 1126 O O   . TYR A 1 157 ? 112.746 110.242 99.997  1.00 63.85  ? 242 TYR A O   1 
ATOM 1127 C CB  . TYR A 1 157 ? 110.940 108.024 101.953 1.00 54.16  ? 242 TYR A CB  1 
ATOM 1128 C CG  . TYR A 1 157 ? 111.942 108.314 103.052 1.00 55.71  ? 242 TYR A CG  1 
ATOM 1129 C CD1 . TYR A 1 157 ? 113.294 108.043 102.879 1.00 56.25  ? 242 TYR A CD1 1 
ATOM 1130 C CD2 . TYR A 1 157 ? 111.534 108.851 104.266 1.00 58.99  ? 242 TYR A CD2 1 
ATOM 1131 C CE1 . TYR A 1 157 ? 114.211 108.304 103.881 1.00 55.33  ? 242 TYR A CE1 1 
ATOM 1132 C CE2 . TYR A 1 157 ? 112.443 109.115 105.274 1.00 56.68  ? 242 TYR A CE2 1 
ATOM 1133 C CZ  . TYR A 1 157 ? 113.779 108.840 105.076 1.00 58.41  ? 242 TYR A CZ  1 
ATOM 1134 O OH  . TYR A 1 157 ? 114.688 109.102 106.076 1.00 74.70  ? 242 TYR A OH  1 
ATOM 1135 N N   . VAL A 1 158 ? 112.358 108.131 99.292  1.00 62.23  ? 243 VAL A N   1 
ATOM 1136 C CA  . VAL A 1 158 ? 113.570 108.103 98.484  1.00 60.09  ? 243 VAL A CA  1 
ATOM 1137 C C   . VAL A 1 158 ? 113.606 109.313 97.569  1.00 58.98  ? 243 VAL A C   1 
ATOM 1138 O O   . VAL A 1 158 ? 114.572 110.089 97.580  1.00 60.98  ? 243 VAL A O   1 
ATOM 1139 C CB  . VAL A 1 158 ? 113.652 106.786 97.688  1.00 58.80  ? 243 VAL A CB  1 
ATOM 1140 C CG1 . VAL A 1 158 ? 114.632 106.920 96.531  1.00 59.49  ? 243 VAL A CG1 1 
ATOM 1141 C CG2 . VAL A 1 158 ? 114.045 105.636 98.601  1.00 57.82  ? 243 VAL A CG2 1 
ATOM 1142 N N   . MET A 1 159 ? 112.505 109.559 96.854  1.00 58.57  ? 244 MET A N   1 
ATOM 1143 C CA  . MET A 1 159 ? 112.501 110.658 95.903  1.00 58.43  ? 244 MET A CA  1 
ATOM 1144 C C   . MET A 1 159 ? 112.770 111.973 96.612  1.00 58.59  ? 244 MET A C   1 
ATOM 1145 O O   . MET A 1 159 ? 113.592 112.771 96.142  1.00 61.19  ? 244 MET A O   1 
ATOM 1146 C CB  . MET A 1 159 ? 111.170 110.695 95.148  1.00 62.00  ? 244 MET A CB  1 
ATOM 1147 C CG  . MET A 1 159 ? 110.940 109.477 94.251  1.00 62.13  ? 244 MET A CG  1 
ATOM 1148 S SD  . MET A 1 159 ? 112.157 109.244 92.937  1.00 92.53  ? 244 MET A SD  1 
ATOM 1149 C CE  . MET A 1 159 ? 111.783 110.624 91.862  1.00 58.55  ? 244 MET A CE  1 
ATOM 1150 N N   . ALA A 1 160 ? 112.149 112.173 97.781  1.00 54.64  ? 245 ALA A N   1 
ATOM 1151 C CA  . ALA A 1 160 ? 112.416 113.385 98.544  1.00 47.85  ? 245 ALA A CA  1 
ATOM 1152 C C   . ALA A 1 160 ? 113.901 113.516 98.844  1.00 58.83  ? 245 ALA A C   1 
ATOM 1153 O O   . ALA A 1 160 ? 114.512 114.540 98.508  1.00 64.78  ? 245 ALA A O   1 
ATOM 1154 C CB  . ALA A 1 160 ? 111.585 113.399 99.828  1.00 47.77  ? 245 ALA A CB  1 
ATOM 1155 N N   . GLU A 1 161 ? 114.513 112.459 99.400  1.00 60.52  ? 246 GLU A N   1 
ATOM 1156 C CA  . GLU A 1 161 ? 115.964 112.466 99.564  1.00 56.57  ? 246 GLU A CA  1 
ATOM 1157 C C   . GLU A 1 161 ? 116.658 112.830 98.266  1.00 58.21  ? 246 GLU A C   1 
ATOM 1158 O O   . GLU A 1 161 ? 117.461 113.772 98.229  1.00 59.15  ? 246 GLU A O   1 
ATOM 1159 C CB  . GLU A 1 161 ? 116.473 111.105 100.047 1.00 58.96  ? 246 GLU A CB  1 
ATOM 1160 C CG  . GLU A 1 161 ? 116.007 110.621 101.406 1.00 67.80  ? 246 GLU A CG  1 
ATOM 1161 C CD  . GLU A 1 161 ? 116.457 111.526 102.512 1.00 80.09  ? 246 GLU A CD  1 
ATOM 1162 O OE1 . GLU A 1 161 ? 117.680 111.673 102.695 1.00 89.66  ? 246 GLU A OE1 1 
ATOM 1163 O OE2 . GLU A 1 161 ? 115.605 112.097 103.228 1.00 76.07  ? 246 GLU A OE2 1 
ATOM 1164 N N   . LEU A 1 162 ? 116.304 112.146 97.174  1.00 58.60  ? 247 LEU A N   1 
ATOM 1165 C CA  . LEU A 1 162 ? 116.988 112.408 95.921  1.00 56.86  ? 247 LEU A CA  1 
ATOM 1166 C C   . LEU A 1 162 ? 116.825 113.857 95.512  1.00 55.69  ? 247 LEU A C   1 
ATOM 1167 O O   . LEU A 1 162 ? 117.787 114.467 95.034  1.00 62.24  ? 247 LEU A O   1 
ATOM 1168 C CB  . LEU A 1 162 ? 116.482 111.470 94.830  1.00 57.80  ? 247 LEU A CB  1 
ATOM 1169 C CG  . LEU A 1 162 ? 117.211 110.128 94.751  1.00 57.69  ? 247 LEU A CG  1 
ATOM 1170 C CD1 . LEU A 1 162 ? 116.843 109.403 93.468  1.00 65.78  ? 247 LEU A CD1 1 
ATOM 1171 C CD2 . LEU A 1 162 ? 118.719 110.325 94.850  1.00 61.46  ? 247 LEU A CD2 1 
ATOM 1172 N N   . TRP A 1 163 ? 115.643 114.437 95.740  1.00 54.05  ? 248 TRP A N   1 
ATOM 1173 C CA  . TRP A 1 163 ? 115.463 115.846 95.422  1.00 53.05  ? 248 TRP A CA  1 
ATOM 1174 C C   . TRP A 1 163 ? 116.523 116.677 96.128  1.00 51.79  ? 248 TRP A C   1 
ATOM 1175 O O   . TRP A 1 163 ? 117.317 117.373 95.481  1.00 54.48  ? 248 TRP A O   1 
ATOM 1176 C CB  . TRP A 1 163 ? 114.054 116.294 95.816  1.00 53.12  ? 248 TRP A CB  1 
ATOM 1177 C CG  . TRP A 1 163 ? 113.799 117.766 95.649  1.00 50.66  ? 248 TRP A CG  1 
ATOM 1178 C CD1 . TRP A 1 163 ? 114.198 118.771 96.482  1.00 51.33  ? 248 TRP A CD1 1 
ATOM 1179 C CD2 . TRP A 1 163 ? 113.078 118.394 94.581  1.00 48.82  ? 248 TRP A CD2 1 
ATOM 1180 N NE1 . TRP A 1 163 ? 113.776 119.985 95.996  1.00 47.48  ? 248 TRP A NE1 1 
ATOM 1181 C CE2 . TRP A 1 163 ? 113.085 119.780 94.831  1.00 46.12  ? 248 TRP A CE2 1 
ATOM 1182 C CE3 . TRP A 1 163 ? 112.429 117.918 93.438  1.00 51.15  ? 248 TRP A CE3 1 
ATOM 1183 C CZ2 . TRP A 1 163 ? 112.470 120.695 93.979  1.00 46.96  ? 248 TRP A CZ2 1 
ATOM 1184 C CZ3 . TRP A 1 163 ? 111.819 118.827 92.593  1.00 53.83  ? 248 TRP A CZ3 1 
ATOM 1185 C CH2 . TRP A 1 163 ? 111.843 120.200 92.869  1.00 51.69  ? 248 TRP A CH2 1 
ATOM 1186 N N   . GLY A 1 164 ? 116.631 116.514 97.450  1.00 56.35  ? 249 GLY A N   1 
ATOM 1187 C CA  . GLY A 1 164 ? 117.607 117.280 98.200  1.00 56.91  ? 249 GLY A CA  1 
ATOM 1188 C C   . GLY A 1 164 ? 119.028 116.991 97.773  1.00 58.22  ? 249 GLY A C   1 
ATOM 1189 O O   . GLY A 1 164 ? 119.914 117.834 97.932  1.00 57.39  ? 249 GLY A O   1 
ATOM 1190 N N   . SER A 1 165 ? 119.265 115.805 97.212  1.00 60.88  ? 250 SER A N   1 
ATOM 1191 C CA  . SER A 1 165 ? 120.608 115.468 96.764  1.00 56.38  ? 250 SER A CA  1 
ATOM 1192 C C   . SER A 1 165 ? 120.860 115.912 95.331  1.00 54.13  ? 250 SER A C   1 
ATOM 1193 O O   . SER A 1 165 ? 122.014 116.159 94.962  1.00 57.39  ? 250 SER A O   1 
ATOM 1194 C CB  . SER A 1 165 ? 120.845 113.963 96.895  1.00 57.55  ? 250 SER A CB  1 
ATOM 1195 O OG  . SER A 1 165 ? 122.132 113.609 96.421  1.00 67.33  ? 250 SER A OG  1 
ATOM 1196 N N   . VAL A 1 166 ? 119.814 116.030 94.514  1.00 57.21  ? 251 VAL A N   1 
ATOM 1197 C CA  . VAL A 1 166 ? 119.966 116.177 93.067  1.00 49.32  ? 251 VAL A CA  1 
ATOM 1198 C C   . VAL A 1 166 ? 119.495 117.546 92.591  1.00 49.15  ? 251 VAL A C   1 
ATOM 1199 O O   . VAL A 1 166 ? 120.269 118.312 92.016  1.00 54.10  ? 251 VAL A O   1 
ATOM 1200 C CB  . VAL A 1 166 ? 119.240 115.042 92.314  1.00 49.93  ? 251 VAL A CB  1 
ATOM 1201 C CG1 . VAL A 1 166 ? 119.121 115.379 90.838  1.00 50.83  ? 251 VAL A CG1 1 
ATOM 1202 C CG2 . VAL A 1 166 ? 119.961 113.721 92.526  1.00 54.75  ? 251 VAL A CG2 1 
ATOM 1203 N N   . VAL A 1 167 ? 118.219 117.866 92.812  1.00 49.52  ? 252 VAL A N   1 
ATOM 1204 C CA  . VAL A 1 167 ? 117.680 119.133 92.327  1.00 46.53  ? 252 VAL A CA  1 
ATOM 1205 C C   . VAL A 1 167 ? 118.362 120.302 93.024  1.00 49.87  ? 252 VAL A C   1 
ATOM 1206 O O   . VAL A 1 167 ? 118.637 121.339 92.407  1.00 57.50  ? 252 VAL A O   1 
ATOM 1207 C CB  . VAL A 1 167 ? 116.152 119.163 92.512  1.00 48.28  ? 252 VAL A CB  1 
ATOM 1208 C CG1 . VAL A 1 167 ? 115.576 120.472 91.998  1.00 49.22  ? 252 VAL A CG1 1 
ATOM 1209 C CG2 . VAL A 1 167 ? 115.516 117.978 91.803  1.00 46.69  ? 252 VAL A CG2 1 
ATOM 1210 N N   . VAL A 1 168 ? 118.654 120.152 94.318  1.00 50.90  ? 253 VAL A N   1 
ATOM 1211 C CA  . VAL A 1 168 ? 119.328 121.215 95.055  1.00 47.75  ? 253 VAL A CA  1 
ATOM 1212 C C   . VAL A 1 168 ? 120.764 121.376 94.569  1.00 52.35  ? 253 VAL A C   1 
ATOM 1213 O O   . VAL A 1 168 ? 121.212 122.488 94.264  1.00 60.12  ? 253 VAL A O   1 
ATOM 1214 C CB  . VAL A 1 168 ? 119.280 120.932 96.567  1.00 48.98  ? 253 VAL A CB  1 
ATOM 1215 C CG1 . VAL A 1 168 ? 120.032 122.013 97.332  1.00 53.41  ? 253 VAL A CG1 1 
ATOM 1216 C CG2 . VAL A 1 168 ? 117.843 120.823 97.048  1.00 53.45  ? 253 VAL A CG2 1 
ATOM 1217 N N   . SER A 1 169 ? 121.504 120.270 94.480  1.00 50.33  ? 254 SER A N   1 
ATOM 1218 C CA  . SER A 1 169 ? 122.950 120.338 94.232  1.00 48.93  ? 254 SER A CA  1 
ATOM 1219 C C   . SER A 1 169 ? 123.286 120.190 92.751  1.00 49.70  ? 254 SER A C   1 
ATOM 1220 O O   . SER A 1 169 ? 123.844 121.104 92.140  1.00 55.15  ? 254 SER A O   1 
ATOM 1221 C CB  . SER A 1 169 ? 123.670 119.277 95.068  1.00 56.52  ? 254 SER A CB  1 
ATOM 1222 O OG  . SER A 1 169 ? 123.668 119.623 96.442  1.00 64.90  ? 254 SER A OG  1 
ATOM 1223 N N   . VAL A 1 170 ? 122.945 119.045 92.158  1.00 50.47  ? 255 VAL A N   1 
ATOM 1224 C CA  . VAL A 1 170 ? 123.372 118.777 90.786  1.00 43.66  ? 255 VAL A CA  1 
ATOM 1225 C C   . VAL A 1 170 ? 122.639 119.688 89.811  1.00 45.88  ? 255 VAL A C   1 
ATOM 1226 O O   . VAL A 1 170 ? 123.259 120.442 89.054  1.00 53.81  ? 255 VAL A O   1 
ATOM 1227 C CB  . VAL A 1 170 ? 123.170 117.294 90.434  1.00 42.83  ? 255 VAL A CB  1 
ATOM 1228 C CG1 . VAL A 1 170 ? 123.389 117.071 88.947  1.00 49.43  ? 255 VAL A CG1 1 
ATOM 1229 C CG2 . VAL A 1 170 ? 124.136 116.450 91.229  1.00 51.76  ? 255 VAL A CG2 1 
ATOM 1230 N N   . LEU A 1 171 ? 121.307 119.652 89.836  1.00 44.42  ? 256 LEU A N   1 
ATOM 1231 C CA  . LEU A 1 171 ? 120.521 120.403 88.863  1.00 44.56  ? 256 LEU A CA  1 
ATOM 1232 C C   . LEU A 1 171 ? 120.769 121.903 88.986  1.00 48.14  ? 256 LEU A C   1 
ATOM 1233 O O   . LEU A 1 171 ? 121.301 122.538 88.065  1.00 58.12  ? 256 LEU A O   1 
ATOM 1234 C CB  . LEU A 1 171 ? 119.038 120.084 89.044  1.00 42.24  ? 256 LEU A CB  1 
ATOM 1235 C CG  . LEU A 1 171 ? 118.519 118.845 88.318  1.00 44.18  ? 256 LEU A CG  1 
ATOM 1236 C CD1 . LEU A 1 171 ? 117.010 118.826 88.363  1.00 46.09  ? 256 LEU A CD1 1 
ATOM 1237 C CD2 . LEU A 1 171 ? 119.014 118.813 86.880  1.00 50.00  ? 256 LEU A CD2 1 
ATOM 1238 N N   . PHE A 1 172 ? 120.397 122.487 90.129  1.00 43.56  ? 257 PHE A N   1 
ATOM 1239 C CA  . PHE A 1 172 ? 120.469 123.937 90.271  1.00 42.63  ? 257 PHE A CA  1 
ATOM 1240 C C   . PHE A 1 172 ? 121.898 124.444 90.167  1.00 49.45  ? 257 PHE A C   1 
ATOM 1241 O O   . PHE A 1 172 ? 122.180 125.382 89.415  1.00 57.42  ? 257 PHE A O   1 
ATOM 1242 C CB  . PHE A 1 172 ? 119.879 124.396 91.599  1.00 42.88  ? 257 PHE A CB  1 
ATOM 1243 C CG  . PHE A 1 172 ? 120.056 125.866 91.829  1.00 43.68  ? 257 PHE A CG  1 
ATOM 1244 C CD1 . PHE A 1 172 ? 119.408 126.785 91.022  1.00 47.42  ? 257 PHE A CD1 1 
ATOM 1245 C CD2 . PHE A 1 172 ? 120.941 126.330 92.786  1.00 47.58  ? 257 PHE A CD2 1 
ATOM 1246 C CE1 . PHE A 1 172 ? 119.590 128.140 91.206  1.00 46.03  ? 257 PHE A CE1 1 
ATOM 1247 C CE2 . PHE A 1 172 ? 121.132 127.686 92.972  1.00 47.76  ? 257 PHE A CE2 1 
ATOM 1248 C CZ  . PHE A 1 172 ? 120.456 128.591 92.179  1.00 45.10  ? 257 PHE A CZ  1 
ATOM 1249 N N   . TRP A 1 173 ? 122.809 123.870 90.953  1.00 45.91  ? 258 TRP A N   1 
ATOM 1250 C CA  . TRP A 1 173 ? 124.156 124.418 90.982  1.00 43.38  ? 258 TRP A CA  1 
ATOM 1251 C C   . TRP A 1 173 ? 124.918 124.099 89.705  1.00 47.26  ? 258 TRP A C   1 
ATOM 1252 O O   . TRP A 1 173 ? 125.793 124.875 89.317  1.00 58.21  ? 258 TRP A O   1 
ATOM 1253 C CB  . TRP A 1 173 ? 124.918 123.911 92.206  1.00 47.73  ? 258 TRP A CB  1 
ATOM 1254 C CG  . TRP A 1 173 ? 124.499 124.583 93.478  1.00 47.57  ? 258 TRP A CG  1 
ATOM 1255 C CD1 . TRP A 1 173 ? 123.855 124.004 94.533  1.00 47.40  ? 258 TRP A CD1 1 
ATOM 1256 C CD2 . TRP A 1 173 ? 124.651 125.968 93.813  1.00 45.99  ? 258 TRP A CD2 1 
ATOM 1257 N NE1 . TRP A 1 173 ? 123.620 124.936 95.514  1.00 47.28  ? 258 TRP A NE1 1 
ATOM 1258 C CE2 . TRP A 1 173 ? 124.097 126.150 95.096  1.00 47.21  ? 258 TRP A CE2 1 
ATOM 1259 C CE3 . TRP A 1 173 ? 125.213 127.068 93.158  1.00 48.79  ? 258 TRP A CE3 1 
ATOM 1260 C CZ2 . TRP A 1 173 ? 124.087 127.387 95.736  1.00 50.81  ? 258 TRP A CZ2 1 
ATOM 1261 C CZ3 . TRP A 1 173 ? 125.202 128.295 93.796  1.00 51.84  ? 258 TRP A CZ3 1 
ATOM 1262 C CH2 . TRP A 1 173 ? 124.643 128.445 95.071  1.00 48.41  ? 258 TRP A CH2 1 
ATOM 1263 N N   . GLY A 1 174 ? 124.589 122.996 89.029  1.00 45.96  ? 259 GLY A N   1 
ATOM 1264 C CA  . GLY A 1 174 ? 125.125 122.777 87.698  1.00 45.79  ? 259 GLY A CA  1 
ATOM 1265 C C   . GLY A 1 174 ? 124.664 123.836 86.718  1.00 50.07  ? 259 GLY A C   1 
ATOM 1266 O O   . GLY A 1 174 ? 125.464 124.361 85.942  1.00 58.11  ? 259 GLY A O   1 
ATOM 1267 N N   . PHE A 1 175 ? 123.375 124.188 86.761  1.00 49.92  ? 260 PHE A N   1 
ATOM 1268 C CA  . PHE A 1 175 ? 122.879 125.286 85.934  1.00 49.69  ? 260 PHE A CA  1 
ATOM 1269 C C   . PHE A 1 175 ? 123.604 126.587 86.257  1.00 51.18  ? 260 PHE A C   1 
ATOM 1270 O O   . PHE A 1 175 ? 124.021 127.323 85.353  1.00 61.97  ? 260 PHE A O   1 
ATOM 1271 C CB  . PHE A 1 175 ? 121.372 125.445 86.137  1.00 49.92  ? 260 PHE A CB  1 
ATOM 1272 C CG  . PHE A 1 175 ? 120.750 126.506 85.276  1.00 54.20  ? 260 PHE A CG  1 
ATOM 1273 C CD1 . PHE A 1 175 ? 121.090 126.625 83.939  1.00 53.79  ? 260 PHE A CD1 1 
ATOM 1274 C CD2 . PHE A 1 175 ? 119.822 127.386 85.807  1.00 57.52  ? 260 PHE A CD2 1 
ATOM 1275 C CE1 . PHE A 1 175 ? 120.512 127.600 83.150  1.00 55.02  ? 260 PHE A CE1 1 
ATOM 1276 C CE2 . PHE A 1 175 ? 119.244 128.365 85.024  1.00 57.24  ? 260 PHE A CE2 1 
ATOM 1277 C CZ  . PHE A 1 175 ? 119.591 128.472 83.694  1.00 57.05  ? 260 PHE A CZ  1 
ATOM 1278 N N   . ALA A 1 176 ? 123.770 126.877 87.548  1.00 47.07  ? 261 ALA A N   1 
ATOM 1279 C CA  . ALA A 1 176 ? 124.419 128.117 87.962  1.00 46.03  ? 261 ALA A CA  1 
ATOM 1280 C C   . ALA A 1 176 ? 125.860 128.173 87.471  1.00 52.96  ? 261 ALA A C   1 
ATOM 1281 O O   . ALA A 1 176 ? 126.267 129.140 86.820  1.00 58.99  ? 261 ALA A O   1 
ATOM 1282 C CB  . ALA A 1 176 ? 124.358 128.257 89.483  1.00 42.81  ? 261 ALA A CB  1 
ATOM 1283 N N   . ASN A 1 177 ? 126.641 127.128 87.753  1.00 53.08  ? 262 ASN A N   1 
ATOM 1284 C CA  . ASN A 1 177 ? 128.020 127.072 87.285  1.00 47.09  ? 262 ASN A CA  1 
ATOM 1285 C C   . ASN A 1 177 ? 128.108 127.063 85.766  1.00 54.38  ? 262 ASN A C   1 
ATOM 1286 O O   . ASN A 1 177 ? 129.130 127.482 85.212  1.00 57.08  ? 262 ASN A O   1 
ATOM 1287 C CB  . ASN A 1 177 ? 128.717 125.835 87.856  1.00 46.58  ? 262 ASN A CB  1 
ATOM 1288 C CG  . ASN A 1 177 ? 128.661 125.781 89.371  1.00 47.70  ? 262 ASN A CG  1 
ATOM 1289 O OD1 . ASN A 1 177 ? 128.436 126.794 90.032  1.00 52.03  ? 262 ASN A OD1 1 
ATOM 1290 N ND2 . ASN A 1 177 ? 128.858 124.591 89.928  1.00 49.21  ? 262 ASN A ND2 1 
ATOM 1291 N N   . GLN A 1 178 ? 127.062 126.597 85.082  1.00 53.06  ? 263 GLN A N   1 
ATOM 1292 C CA  . GLN A 1 178 ? 127.041 126.635 83.626  1.00 58.62  ? 263 GLN A CA  1 
ATOM 1293 C C   . GLN A 1 178 ? 126.819 128.049 83.107  1.00 60.35  ? 263 GLN A C   1 
ATOM 1294 O O   . GLN A 1 178 ? 127.386 128.430 82.077  1.00 69.86  ? 263 GLN A O   1 
ATOM 1295 C CB  . GLN A 1 178 ? 125.957 125.690 83.103  1.00 56.19  ? 263 GLN A CB  1 
ATOM 1296 C CG  . GLN A 1 178 ? 125.682 125.791 81.613  1.00 63.95  ? 263 GLN A CG  1 
ATOM 1297 C CD  . GLN A 1 178 ? 124.229 125.520 81.274  1.00 64.52  ? 263 GLN A CD  1 
ATOM 1298 O OE1 . GLN A 1 178 ? 123.598 124.638 81.856  1.00 62.21  ? 263 GLN A OE1 1 
ATOM 1299 N NE2 . GLN A 1 178 ? 123.690 126.280 80.328  1.00 66.57  ? 263 GLN A NE2 1 
ATOM 1300 N N   . ILE A 1 179 ? 126.008 128.845 83.805  1.00 55.51  ? 264 ILE A N   1 
ATOM 1301 C CA  . ILE A 1 179 ? 125.665 130.171 83.303  1.00 56.19  ? 264 ILE A CA  1 
ATOM 1302 C C   . ILE A 1 179 ? 126.417 131.295 84.010  1.00 61.54  ? 264 ILE A C   1 
ATOM 1303 O O   . ILE A 1 179 ? 126.527 132.395 83.448  1.00 70.21  ? 264 ILE A O   1 
ATOM 1304 C CB  . ILE A 1 179 ? 124.146 130.415 83.395  1.00 58.79  ? 264 ILE A CB  1 
ATOM 1305 C CG1 . ILE A 1 179 ? 123.670 130.370 84.844  1.00 55.38  ? 264 ILE A CG1 1 
ATOM 1306 C CG2 . ILE A 1 179 ? 123.412 129.346 82.620  1.00 67.21  ? 264 ILE A CG2 1 
ATOM 1307 C CD1 . ILE A 1 179 ? 122.240 130.832 85.011  1.00 54.46  ? 264 ILE A CD1 1 
ATOM 1308 N N   . THR A 1 180 ? 126.941 131.056 85.208  1.00 60.14  ? 265 THR A N   1 
ATOM 1309 C CA  . THR A 1 180 ? 127.613 132.086 85.989  1.00 58.09  ? 265 THR A CA  1 
ATOM 1310 C C   . THR A 1 180 ? 129.122 131.972 85.821  1.00 61.44  ? 265 THR A C   1 
ATOM 1311 O O   . THR A 1 180 ? 129.671 130.867 85.772  1.00 63.18  ? 265 THR A O   1 
ATOM 1312 C CB  . THR A 1 180 ? 127.244 131.972 87.472  1.00 55.71  ? 265 THR A CB  1 
ATOM 1313 O OG1 . THR A 1 180 ? 125.818 131.939 87.611  1.00 64.78  ? 265 THR A OG1 1 
ATOM 1314 C CG2 . THR A 1 180 ? 127.788 133.149 88.260  1.00 60.72  ? 265 THR A CG2 1 
ATOM 1315 N N   . THR A 1 181 ? 129.787 133.120 85.720  1.00 64.41  ? 266 THR A N   1 
ATOM 1316 C CA  . THR A 1 181 ? 131.238 133.171 85.715  1.00 60.82  ? 266 THR A CA  1 
ATOM 1317 C C   . THR A 1 181 ? 131.755 133.094 87.150  1.00 62.77  ? 266 THR A C   1 
ATOM 1318 O O   . THR A 1 181 ? 130.988 133.073 88.113  1.00 67.18  ? 266 THR A O   1 
ATOM 1319 C CB  . THR A 1 181 ? 131.732 134.442 85.023  1.00 64.13  ? 266 THR A CB  1 
ATOM 1320 O OG1 . THR A 1 181 ? 131.129 135.587 85.638  1.00 66.98  ? 266 THR A OG1 1 
ATOM 1321 C CG2 . THR A 1 181 ? 131.371 134.419 83.546  1.00 71.45  ? 266 THR A CG2 1 
ATOM 1322 N N   . VAL A 1 182 ? 133.079 133.045 87.298  1.00 63.53  ? 267 VAL A N   1 
ATOM 1323 C CA  . VAL A 1 182 ? 133.661 133.001 88.635  1.00 61.94  ? 267 VAL A CA  1 
ATOM 1324 C C   . VAL A 1 182 ? 133.468 134.327 89.367  1.00 63.43  ? 267 VAL A C   1 
ATOM 1325 O O   . VAL A 1 182 ? 133.218 134.341 90.577  1.00 67.69  ? 267 VAL A O   1 
ATOM 1326 C CB  . VAL A 1 182 ? 135.147 132.614 88.553  1.00 64.93  ? 267 VAL A CB  1 
ATOM 1327 C CG1 . VAL A 1 182 ? 135.686 132.283 89.934  1.00 59.86  ? 267 VAL A CG1 1 
ATOM 1328 C CG2 . VAL A 1 182 ? 135.328 131.435 87.610  1.00 63.93  ? 267 VAL A CG2 1 
ATOM 1329 N N   . ASP A 1 183 ? 133.578 135.453 88.659  1.00 62.11  ? 268 ASP A N   1 
ATOM 1330 C CA  . ASP A 1 183 ? 133.413 136.756 89.298  1.00 60.73  ? 268 ASP A CA  1 
ATOM 1331 C C   . ASP A 1 183 ? 131.986 136.944 89.801  1.00 63.76  ? 268 ASP A C   1 
ATOM 1332 O O   . ASP A 1 183 ? 131.764 137.302 90.967  1.00 69.58  ? 268 ASP A O   1 
ATOM 1333 C CB  . ASP A 1 183 ? 133.788 137.865 88.313  1.00 71.11  ? 268 ASP A CB  1 
ATOM 1334 C CG  . ASP A 1 183 ? 135.243 137.804 87.893  1.00 83.50  ? 268 ASP A CG  1 
ATOM 1335 O OD1 . ASP A 1 183 ? 136.076 137.326 88.691  1.00 84.05  ? 268 ASP A OD1 1 
ATOM 1336 O OD2 . ASP A 1 183 ? 135.554 138.231 86.760  1.00 89.85  ? 268 ASP A OD2 1 
ATOM 1337 N N   . GLU A 1 184 ? 131.001 136.699 88.933  1.00 64.70  ? 269 GLU A N   1 
ATOM 1338 C CA  . GLU A 1 184 ? 129.608 136.798 89.349  1.00 64.87  ? 269 GLU A CA  1 
ATOM 1339 C C   . GLU A 1 184 ? 129.283 135.788 90.440  1.00 58.28  ? 269 GLU A C   1 
ATOM 1340 O O   . GLU A 1 184 ? 128.400 136.032 91.269  1.00 63.43  ? 269 GLU A O   1 
ATOM 1341 C CB  . GLU A 1 184 ? 128.683 136.597 88.148  1.00 65.45  ? 269 GLU A CB  1 
ATOM 1342 C CG  . GLU A 1 184 ? 128.915 137.568 87.002  1.00 72.44  ? 269 GLU A CG  1 
ATOM 1343 C CD  . GLU A 1 184 ? 127.915 137.384 85.876  1.00 88.33  ? 269 GLU A CD  1 
ATOM 1344 O OE1 . GLU A 1 184 ? 127.498 136.232 85.634  1.00 86.60  ? 269 GLU A OE1 1 
ATOM 1345 O OE2 . GLU A 1 184 ? 127.545 138.390 85.234  1.00 95.22  ? 269 GLU A OE2 1 
ATOM 1346 N N   . ALA A 1 185 ? 129.985 134.653 90.459  1.00 56.98  ? 270 ALA A N   1 
ATOM 1347 C CA  . ALA A 1 185 ? 129.757 133.659 91.502  1.00 55.08  ? 270 ALA A CA  1 
ATOM 1348 C C   . ALA A 1 185 ? 130.277 134.145 92.850  1.00 57.41  ? 270 ALA A C   1 
ATOM 1349 O O   . ALA A 1 185 ? 129.609 133.981 93.878  1.00 59.30  ? 270 ALA A O   1 
ATOM 1350 C CB  . ALA A 1 185 ? 130.402 132.333 91.111  1.00 55.58  ? 270 ALA A CB  1 
ATOM 1351 N N   . LYS A 1 186 ? 131.477 134.739 92.871  1.00 60.90  ? 271 LYS A N   1 
ATOM 1352 C CA  . LYS A 1 186 ? 131.937 135.404 94.088  1.00 57.65  ? 271 LYS A CA  1 
ATOM 1353 C C   . LYS A 1 186 ? 130.954 136.470 94.535  1.00 62.07  ? 271 LYS A C   1 
ATOM 1354 O O   . LYS A 1 186 ? 130.710 136.630 95.737  1.00 66.54  ? 271 LYS A O   1 
ATOM 1355 C CB  . LYS A 1 186 ? 133.318 136.045 93.890  1.00 54.71  ? 271 LYS A CB  1 
ATOM 1356 C CG  . LYS A 1 186 ? 134.474 135.072 93.856  1.00 51.26  ? 271 LYS A CG  1 
ATOM 1357 C CD  . LYS A 1 186 ? 135.828 135.735 93.702  1.00 56.61  ? 271 LYS A CD  1 
ATOM 1358 C CE  . LYS A 1 186 ? 136.927 134.680 93.692  1.00 73.22  ? 271 LYS A CE  1 
ATOM 1359 N NZ  . LYS A 1 186 ? 138.285 135.258 93.508  1.00 80.18  ? 271 LYS A NZ  1 
ATOM 1360 N N   . LYS A 1 187 ? 130.381 137.207 93.586  1.00 62.43  ? 272 LYS A N   1 
ATOM 1361 C CA  . LYS A 1 187 ? 129.538 138.337 93.952  1.00 59.65  ? 272 LYS A CA  1 
ATOM 1362 C C   . LYS A 1 187 ? 128.149 137.911 94.426  1.00 64.80  ? 272 LYS A C   1 
ATOM 1363 O O   . LYS A 1 187 ? 127.545 138.609 95.248  1.00 76.40  ? 272 LYS A O   1 
ATOM 1364 C CB  . LYS A 1 187 ? 129.433 139.302 92.770  1.00 63.10  ? 272 LYS A CB  1 
ATOM 1365 C CG  . LYS A 1 187 ? 128.623 140.554 93.049  1.00 68.88  ? 272 LYS A CG  1 
ATOM 1366 C CD  . LYS A 1 187 ? 128.662 141.507 91.867  1.00 79.43  ? 272 LYS A CD  1 
ATOM 1367 C CE  . LYS A 1 187 ? 127.734 142.687 92.086  1.00 87.47  ? 272 LYS A CE  1 
ATOM 1368 N NZ  . LYS A 1 187 ? 128.193 143.541 93.215  1.00 86.40  ? 272 LYS A NZ  1 
ATOM 1369 N N   . PHE A 1 188 ? 127.628 136.773 93.951  1.00 61.93  ? 273 PHE A N   1 
ATOM 1370 C CA  . PHE A 1 188 ? 126.214 136.465 94.133  1.00 55.12  ? 273 PHE A CA  1 
ATOM 1371 C C   . PHE A 1 188 ? 125.900 135.115 94.769  1.00 55.12  ? 273 PHE A C   1 
ATOM 1372 O O   . PHE A 1 188 ? 124.720 134.829 94.994  1.00 65.63  ? 273 PHE A O   1 
ATOM 1373 C CB  . PHE A 1 188 ? 125.485 136.544 92.784  1.00 57.62  ? 273 PHE A CB  1 
ATOM 1374 C CG  . PHE A 1 188 ? 125.363 137.937 92.248  1.00 64.27  ? 273 PHE A CG  1 
ATOM 1375 C CD1 . PHE A 1 188 ? 124.561 138.869 92.884  1.00 66.09  ? 273 PHE A CD1 1 
ATOM 1376 C CD2 . PHE A 1 188 ? 126.059 138.319 91.115  1.00 64.35  ? 273 PHE A CD2 1 
ATOM 1377 C CE1 . PHE A 1 188 ? 124.448 140.154 92.394  1.00 70.28  ? 273 PHE A CE1 1 
ATOM 1378 C CE2 . PHE A 1 188 ? 125.952 139.602 90.624  1.00 69.94  ? 273 PHE A CE2 1 
ATOM 1379 C CZ  . PHE A 1 188 ? 125.144 140.520 91.262  1.00 76.26  ? 273 PHE A CZ  1 
ATOM 1380 N N   . TYR A 1 189 ? 126.892 134.280 95.061  1.00 55.08  ? 274 TYR A N   1 
ATOM 1381 C CA  . TYR A 1 189 ? 126.564 132.983 95.647  1.00 52.36  ? 274 TYR A CA  1 
ATOM 1382 C C   . TYR A 1 189 ? 126.176 133.091 97.122  1.00 59.38  ? 274 TYR A C   1 
ATOM 1383 O O   . TYR A 1 189 ? 125.234 132.408 97.547  1.00 63.01  ? 274 TYR A O   1 
ATOM 1384 C CB  . TYR A 1 189 ? 127.714 131.989 95.458  1.00 52.58  ? 274 TYR A CB  1 
ATOM 1385 C CG  . TYR A 1 189 ? 127.697 131.301 94.109  1.00 55.23  ? 274 TYR A CG  1 
ATOM 1386 C CD1 . TYR A 1 189 ? 126.963 131.823 93.050  1.00 55.84  ? 274 TYR A CD1 1 
ATOM 1387 C CD2 . TYR A 1 189 ? 128.401 130.122 93.897  1.00 54.69  ? 274 TYR A CD2 1 
ATOM 1388 C CE1 . TYR A 1 189 ? 126.939 131.198 91.818  1.00 49.51  ? 274 TYR A CE1 1 
ATOM 1389 C CE2 . TYR A 1 189 ? 128.382 129.489 92.667  1.00 50.89  ? 274 TYR A CE2 1 
ATOM 1390 C CZ  . TYR A 1 189 ? 127.649 130.031 91.632  1.00 47.93  ? 274 TYR A CZ  1 
ATOM 1391 O OH  . TYR A 1 189 ? 127.626 129.406 90.407  1.00 52.01  ? 274 TYR A OH  1 
ATOM 1392 N N   . PRO A 1 190 ? 126.859 133.899 97.945  1.00 57.10  ? 275 PRO A N   1 
ATOM 1393 C CA  . PRO A 1 190 ? 126.336 134.135 99.302  1.00 60.97  ? 275 PRO A CA  1 
ATOM 1394 C C   . PRO A 1 190 ? 124.944 134.746 99.314  1.00 68.35  ? 275 PRO A C   1 
ATOM 1395 O O   . PRO A 1 190 ? 124.137 134.417 100.193 1.00 74.02  ? 275 PRO A O   1 
ATOM 1396 C CB  . PRO A 1 190 ? 127.378 135.078 99.916  1.00 65.60  ? 275 PRO A CB  1 
ATOM 1397 C CG  . PRO A 1 190 ? 128.632 134.737 99.205  1.00 59.44  ? 275 PRO A CG  1 
ATOM 1398 C CD  . PRO A 1 190 ? 128.211 134.472 97.789  1.00 53.58  ? 275 PRO A CD  1 
ATOM 1399 N N   . LEU A 1 191 ? 124.632 135.622 98.357  1.00 62.72  ? 276 LEU A N   1 
ATOM 1400 C CA  . LEU A 1 191 ? 123.281 136.154 98.233  1.00 62.00  ? 276 LEU A CA  1 
ATOM 1401 C C   . LEU A 1 191 ? 122.289 135.122 97.718  1.00 63.76  ? 276 LEU A C   1 
ATOM 1402 O O   . LEU A 1 191 ? 121.089 135.408 97.684  1.00 68.32  ? 276 LEU A O   1 
ATOM 1403 C CB  . LEU A 1 191 ? 123.257 137.388 97.324  1.00 65.73  ? 276 LEU A CB  1 
ATOM 1404 C CG  . LEU A 1 191 ? 123.625 138.743 97.938  1.00 75.14  ? 276 LEU A CG  1 
ATOM 1405 C CD1 . LEU A 1 191 ? 122.612 139.132 99.008  1.00 75.24  ? 276 LEU A CD1 1 
ATOM 1406 C CD2 . LEU A 1 191 ? 125.032 138.760 98.505  1.00 74.55  ? 276 LEU A CD2 1 
ATOM 1407 N N   . PHE A 1 192 ? 122.757 133.953 97.282  1.00 63.35  ? 277 PHE A N   1 
ATOM 1408 C CA  . PHE A 1 192 ? 121.844 132.835 97.078  1.00 57.29  ? 277 PHE A CA  1 
ATOM 1409 C C   . PHE A 1 192 ? 121.545 132.132 98.396  1.00 59.68  ? 277 PHE A C   1 
ATOM 1410 O O   . PHE A 1 192 ? 120.400 131.741 98.647  1.00 68.04  ? 277 PHE A O   1 
ATOM 1411 C CB  . PHE A 1 192 ? 122.421 131.855 96.054  1.00 57.82  ? 277 PHE A CB  1 
ATOM 1412 C CG  . PHE A 1 192 ? 122.404 132.371 94.639  1.00 55.55  ? 277 PHE A CG  1 
ATOM 1413 C CD1 . PHE A 1 192 ? 121.836 133.598 94.337  1.00 56.96  ? 277 PHE A CD1 1 
ATOM 1414 C CD2 . PHE A 1 192 ? 122.956 131.625 93.610  1.00 55.72  ? 277 PHE A CD2 1 
ATOM 1415 C CE1 . PHE A 1 192 ? 121.820 134.072 93.039  1.00 57.28  ? 277 PHE A CE1 1 
ATOM 1416 C CE2 . PHE A 1 192 ? 122.943 132.094 92.309  1.00 56.85  ? 277 PHE A CE2 1 
ATOM 1417 C CZ  . PHE A 1 192 ? 122.375 133.319 92.024  1.00 58.74  ? 277 PHE A CZ  1 
ATOM 1418 N N   . GLY A 1 193 ? 122.557 131.982 99.256  1.00 61.09  ? 278 GLY A N   1 
ATOM 1419 C CA  . GLY A 1 193 ? 122.316 131.434 100.584 1.00 64.00  ? 278 GLY A CA  1 
ATOM 1420 C C   . GLY A 1 193 ? 121.411 132.319 101.420 1.00 66.97  ? 278 GLY A C   1 
ATOM 1421 O O   . GLY A 1 193 ? 120.626 131.830 102.239 1.00 67.79  ? 278 GLY A O   1 
ATOM 1422 N N   . LEU A 1 194 ? 121.519 133.633 101.237 1.00 69.39  ? 279 LEU A N   1 
ATOM 1423 C CA  . LEU A 1 194 ? 120.537 134.558 101.790 1.00 66.71  ? 279 LEU A CA  1 
ATOM 1424 C C   . LEU A 1 194 ? 119.358 134.591 100.825 1.00 65.39  ? 279 LEU A C   1 
ATOM 1425 O O   . LEU A 1 194 ? 119.443 135.179 99.743  1.00 77.34  ? 279 LEU A O   1 
ATOM 1426 C CB  . LEU A 1 194 ? 121.145 135.943 101.996 1.00 71.72  ? 279 LEU A CB  1 
ATOM 1427 C CG  . LEU A 1 194 ? 120.210 137.069 102.449 1.00 73.86  ? 279 LEU A CG  1 
ATOM 1428 C CD1 . LEU A 1 194 ? 120.905 137.926 103.494 1.00 79.58  ? 279 LEU A CD1 1 
ATOM 1429 C CD2 . LEU A 1 194 ? 119.766 137.935 101.278 1.00 69.74  ? 279 LEU A CD2 1 
ATOM 1430 N N   . GLY A 1 195 ? 118.257 133.967 101.219 1.00 59.98  ? 280 GLY A N   1 
ATOM 1431 C CA  . GLY A 1 195 ? 117.218 133.611 100.279 1.00 60.42  ? 280 GLY A CA  1 
ATOM 1432 C C   . GLY A 1 195 ? 117.019 132.115 100.336 1.00 56.53  ? 280 GLY A C   1 
ATOM 1433 O O   . GLY A 1 195 ? 115.888 131.639 100.392 1.00 60.06  ? 280 GLY A O   1 
ATOM 1434 N N   . ALA A 1 196 ? 118.121 131.362 100.382 1.00 55.11  ? 281 ALA A N   1 
ATOM 1435 C CA  . ALA A 1 196 ? 118.035 129.964 100.787 1.00 50.52  ? 281 ALA A CA  1 
ATOM 1436 C C   . ALA A 1 196 ? 117.513 129.845 102.210 1.00 57.09  ? 281 ALA A C   1 
ATOM 1437 O O   . ALA A 1 196 ? 116.601 129.057 102.492 1.00 59.04  ? 281 ALA A O   1 
ATOM 1438 C CB  . ALA A 1 196 ? 119.409 129.311 100.680 1.00 57.21  ? 281 ALA A CB  1 
ATOM 1439 N N   . ASN A 1 197 ? 118.086 130.630 103.122 1.00 58.23  ? 282 ASN A N   1 
ATOM 1440 C CA  . ASN A 1 197 ? 117.612 130.627 104.502 1.00 53.13  ? 282 ASN A CA  1 
ATOM 1441 C C   . ASN A 1 197 ? 116.184 131.149 104.596 1.00 54.07  ? 282 ASN A C   1 
ATOM 1442 O O   . ASN A 1 197 ? 115.392 130.659 105.409 1.00 59.75  ? 282 ASN A O   1 
ATOM 1443 C CB  . ASN A 1 197 ? 118.555 131.445 105.382 1.00 54.00  ? 282 ASN A CB  1 
ATOM 1444 C CG  . ASN A 1 197 ? 119.616 130.590 106.039 1.00 59.18  ? 282 ASN A CG  1 
ATOM 1445 O OD1 . ASN A 1 197 ? 119.431 130.095 107.151 1.00 60.40  ? 282 ASN A OD1 1 
ATOM 1446 N ND2 . ASN A 1 197 ? 120.724 130.384 105.341 1.00 56.58  ? 282 ASN A ND2 1 
ATOM 1447 N N   . VAL A 1 198 ? 115.832 132.134 103.767 1.00 51.51  ? 283 VAL A N   1 
ATOM 1448 C CA  . VAL A 1 198 ? 114.458 132.626 103.747 1.00 49.16  ? 283 VAL A CA  1 
ATOM 1449 C C   . VAL A 1 198 ? 113.509 131.546 103.240 1.00 51.20  ? 283 VAL A C   1 
ATOM 1450 O O   . VAL A 1 198 ? 112.379 131.419 103.724 1.00 53.47  ? 283 VAL A O   1 
ATOM 1451 C CB  . VAL A 1 198 ? 114.362 133.910 102.904 1.00 48.61  ? 283 VAL A CB  1 
ATOM 1452 C CG1 . VAL A 1 198 ? 112.986 134.542 103.056 1.00 53.12  ? 283 VAL A CG1 1 
ATOM 1453 C CG2 . VAL A 1 198 ? 115.450 134.890 103.309 1.00 50.15  ? 283 VAL A CG2 1 
ATOM 1454 N N   . ALA A 1 199 ? 113.947 130.760 102.254 1.00 54.59  ? 284 ALA A N   1 
ATOM 1455 C CA  . ALA A 1 199 ? 113.146 129.639 101.781 1.00 47.24  ? 284 ALA A CA  1 
ATOM 1456 C C   . ALA A 1 199 ? 112.942 128.613 102.883 1.00 48.01  ? 284 ALA A C   1 
ATOM 1457 O O   . ALA A 1 199 ? 111.833 128.101 103.063 1.00 51.58  ? 284 ALA A O   1 
ATOM 1458 C CB  . ALA A 1 199 ? 113.808 128.993 100.564 1.00 49.70  ? 284 ALA A CB  1 
ATOM 1459 N N   . LEU A 1 200 ? 114.000 128.304 103.635 1.00 50.23  ? 285 LEU A N   1 
ATOM 1460 C CA  . LEU A 1 200 ? 113.850 127.382 104.758 1.00 49.71  ? 285 LEU A CA  1 
ATOM 1461 C C   . LEU A 1 200 ? 112.876 127.931 105.795 1.00 47.79  ? 285 LEU A C   1 
ATOM 1462 O O   . LEU A 1 200 ? 112.014 127.199 106.293 1.00 53.07  ? 285 LEU A O   1 
ATOM 1463 C CB  . LEU A 1 200 ? 115.207 127.085 105.397 1.00 47.99  ? 285 LEU A CB  1 
ATOM 1464 C CG  . LEU A 1 200 ? 116.334 126.637 104.465 1.00 43.30  ? 285 LEU A CG  1 
ATOM 1465 C CD1 . LEU A 1 200 ? 117.655 126.554 105.214 1.00 55.49  ? 285 LEU A CD1 1 
ATOM 1466 C CD2 . LEU A 1 200 ? 115.997 125.303 103.820 1.00 47.84  ? 285 LEU A CD2 1 
ATOM 1467 N N   . ILE A 1 201 ? 112.980 129.225 106.112 1.00 45.06  ? 286 ILE A N   1 
ATOM 1468 C CA  . ILE A 1 201 ? 112.094 129.829 107.106 1.00 44.06  ? 286 ILE A CA  1 
ATOM 1469 C C   . ILE A 1 201 ? 110.643 129.762 106.642 1.00 48.62  ? 286 ILE A C   1 
ATOM 1470 O O   . ILE A 1 201 ? 109.756 129.305 107.375 1.00 55.65  ? 286 ILE A O   1 
ATOM 1471 C CB  . ILE A 1 201 ? 112.520 131.281 107.392 1.00 43.43  ? 286 ILE A CB  1 
ATOM 1472 C CG1 . ILE A 1 201 ? 113.865 131.320 108.120 1.00 46.07  ? 286 ILE A CG1 1 
ATOM 1473 C CG2 . ILE A 1 201 ? 111.450 132.005 108.197 1.00 46.93  ? 286 ILE A CG2 1 
ATOM 1474 C CD1 . ILE A 1 201 ? 114.462 132.710 108.214 1.00 46.18  ? 286 ILE A CD1 1 
ATOM 1475 N N   . PHE A 1 202 ? 110.383 130.210 105.411 1.00 51.37  ? 287 PHE A N   1 
ATOM 1476 C CA  . PHE A 1 202 ? 109.014 130.252 104.910 1.00 46.79  ? 287 PHE A CA  1 
ATOM 1477 C C   . PHE A 1 202 ? 108.438 128.858 104.713 1.00 48.16  ? 287 PHE A C   1 
ATOM 1478 O O   . PHE A 1 202 ? 107.248 128.647 104.960 1.00 49.56  ? 287 PHE A O   1 
ATOM 1479 C CB  . PHE A 1 202 ? 108.948 131.047 103.605 1.00 47.21  ? 287 PHE A CB  1 
ATOM 1480 C CG  . PHE A 1 202 ? 109.011 132.538 103.798 1.00 56.25  ? 287 PHE A CG  1 
ATOM 1481 C CD1 . PHE A 1 202 ? 109.140 133.084 105.065 1.00 56.86  ? 287 PHE A CD1 1 
ATOM 1482 C CD2 . PHE A 1 202 ? 108.931 133.393 102.712 1.00 61.46  ? 287 PHE A CD2 1 
ATOM 1483 C CE1 . PHE A 1 202 ? 109.194 134.453 105.245 1.00 61.38  ? 287 PHE A CE1 1 
ATOM 1484 C CE2 . PHE A 1 202 ? 108.985 134.764 102.885 1.00 66.22  ? 287 PHE A CE2 1 
ATOM 1485 C CZ  . PHE A 1 202 ? 109.116 135.294 104.153 1.00 69.18  ? 287 PHE A CZ  1 
ATOM 1486 N N   . SER A 1 203 ? 109.253 127.892 104.287 1.00 48.38  ? 288 SER A N   1 
ATOM 1487 C CA  . SER A 1 203 ? 108.752 126.532 104.145 1.00 43.40  ? 288 SER A CA  1 
ATOM 1488 C C   . SER A 1 203 ? 108.492 125.891 105.500 1.00 46.64  ? 288 SER A C   1 
ATOM 1489 O O   . SER A 1 203 ? 107.544 125.113 105.637 1.00 53.40  ? 288 SER A O   1 
ATOM 1490 C CB  . SER A 1 203 ? 109.731 125.692 103.329 1.00 49.24  ? 288 SER A CB  1 
ATOM 1491 O OG  . SER A 1 203 ? 109.269 124.359 103.212 1.00 57.91  ? 288 SER A OG  1 
ATOM 1492 N N   . GLY A 1 204 ? 109.307 126.201 106.511 1.00 48.77  ? 289 GLY A N   1 
ATOM 1493 C CA  . GLY A 1 204 ? 108.997 125.743 107.854 1.00 46.31  ? 289 GLY A CA  1 
ATOM 1494 C C   . GLY A 1 204 ? 107.695 126.321 108.369 1.00 49.44  ? 289 GLY A C   1 
ATOM 1495 O O   . GLY A 1 204 ? 106.887 125.614 108.977 1.00 54.82  ? 289 GLY A O   1 
ATOM 1496 N N   . ARG A 1 205 ? 107.466 127.614 108.122 1.00 48.13  ? 290 ARG A N   1 
ATOM 1497 C CA  . ARG A 1 205 ? 106.188 128.214 108.497 1.00 43.73  ? 290 ARG A CA  1 
ATOM 1498 C C   . ARG A 1 205 ? 105.031 127.595 107.724 1.00 46.75  ? 290 ARG A C   1 
ATOM 1499 O O   . ARG A 1 205 ? 103.942 127.426 108.276 1.00 55.88  ? 290 ARG A O   1 
ATOM 1500 C CB  . ARG A 1 205 ? 106.216 129.730 108.288 1.00 46.56  ? 290 ARG A CB  1 
ATOM 1501 C CG  . ARG A 1 205 ? 107.380 130.448 108.955 1.00 48.22  ? 290 ARG A CG  1 
ATOM 1502 C CD  . ARG A 1 205 ? 107.615 129.946 110.372 1.00 50.02  ? 290 ARG A CD  1 
ATOM 1503 N NE  . ARG A 1 205 ? 106.514 130.284 111.267 1.00 60.69  ? 290 ARG A NE  1 
ATOM 1504 C CZ  . ARG A 1 205 ? 106.411 129.858 112.519 1.00 63.28  ? 290 ARG A CZ  1 
ATOM 1505 N NH1 . ARG A 1 205 ? 107.328 129.073 113.060 1.00 58.76  ? 290 ARG A NH1 1 
ATOM 1506 N NH2 . ARG A 1 205 ? 105.361 130.229 113.246 1.00 68.57  ? 290 ARG A NH2 1 
ATOM 1507 N N   . THR A 1 206 ? 105.243 127.257 106.451 1.00 46.44  ? 291 THR A N   1 
ATOM 1508 C CA  . THR A 1 206 ? 104.204 126.600 105.661 1.00 44.70  ? 291 THR A CA  1 
ATOM 1509 C C   . THR A 1 206 ? 103.876 125.216 106.212 1.00 48.43  ? 291 THR A C   1 
ATOM 1510 O O   . THR A 1 206 ? 102.699 124.844 106.324 1.00 57.49  ? 291 THR A O   1 
ATOM 1511 C CB  . THR A 1 206 ? 104.654 126.506 104.201 1.00 45.35  ? 291 THR A CB  1 
ATOM 1512 O OG1 . THR A 1 206 ? 104.882 127.824 103.683 1.00 49.71  ? 291 THR A OG1 1 
ATOM 1513 C CG2 . THR A 1 206 ? 103.607 125.812 103.356 1.00 46.16  ? 291 THR A CG2 1 
ATOM 1514 N N   . VAL A 1 207 ? 104.906 124.441 106.560 1.00 47.40  ? 292 VAL A N   1 
ATOM 1515 C CA  . VAL A 1 207 ? 104.692 123.122 107.147 1.00 48.21  ? 292 VAL A CA  1 
ATOM 1516 C C   . VAL A 1 207 ? 103.969 123.243 108.481 1.00 55.52  ? 292 VAL A C   1 
ATOM 1517 O O   . VAL A 1 207 ? 103.070 122.454 108.786 1.00 61.88  ? 292 VAL A O   1 
ATOM 1518 C CB  . VAL A 1 207 ? 106.032 122.372 107.285 1.00 52.56  ? 292 VAL A CB  1 
ATOM 1519 C CG1 . VAL A 1 207 ? 105.823 121.027 107.945 1.00 55.27  ? 292 VAL A CG1 1 
ATOM 1520 C CG2 . VAL A 1 207 ? 106.663 122.169 105.919 1.00 51.50  ? 292 VAL A CG2 1 
ATOM 1521 N N   . LYS A 1 208 ? 104.344 124.234 109.295 1.00 57.39  ? 293 LYS A N   1 
ATOM 1522 C CA  . LYS A 1 208 ? 103.640 124.462 110.555 1.00 52.22  ? 293 LYS A CA  1 
ATOM 1523 C C   . LYS A 1 208 ? 102.184 124.850 110.319 1.00 55.78  ? 293 LYS A C   1 
ATOM 1524 O O   . LYS A 1 208 ? 101.285 124.366 111.019 1.00 68.68  ? 293 LYS A O   1 
ATOM 1525 C CB  . LYS A 1 208 ? 104.355 125.541 111.367 1.00 50.61  ? 293 LYS A CB  1 
ATOM 1526 C CG  . LYS A 1 208 ? 103.686 125.853 112.694 1.00 63.68  ? 293 LYS A CG  1 
ATOM 1527 C CD  . LYS A 1 208 ? 104.664 126.465 113.681 1.00 71.13  ? 293 LYS A CD  1 
ATOM 1528 C CE  . LYS A 1 208 ? 104.076 126.495 115.081 1.00 67.85  ? 293 LYS A CE  1 
ATOM 1529 N NZ  . LYS A 1 208 ? 105.115 126.758 116.114 1.00 67.50  ? 293 LYS A NZ  1 
ATOM 1530 N N   . TYR A 1 209 ? 101.935 125.723 109.339 1.00 49.65  ? 294 TYR A N   1 
ATOM 1531 C CA  . TYR A 1 209 ? 100.570 126.132 109.032 1.00 50.52  ? 294 TYR A CA  1 
ATOM 1532 C C   . TYR A 1 209 ? 99.720  124.945 108.616 1.00 56.72  ? 294 TYR A C   1 
ATOM 1533 O O   . TYR A 1 209 ? 98.575  124.813 109.055 1.00 66.00  ? 294 TYR A O   1 
ATOM 1534 C CB  . TYR A 1 209 ? 100.564 127.194 107.931 1.00 49.84  ? 294 TYR A CB  1 
ATOM 1535 C CG  . TYR A 1 209 ? 99.170  127.606 107.503 1.00 51.83  ? 294 TYR A CG  1 
ATOM 1536 C CD1 . TYR A 1 209 ? 98.439  128.532 108.235 1.00 56.32  ? 294 TYR A CD1 1 
ATOM 1537 C CD2 . TYR A 1 209 ? 98.584  127.061 106.365 1.00 56.86  ? 294 TYR A CD2 1 
ATOM 1538 C CE1 . TYR A 1 209 ? 97.164  128.904 107.846 1.00 56.40  ? 294 TYR A CE1 1 
ATOM 1539 C CE2 . TYR A 1 209 ? 97.312  127.427 105.970 1.00 60.31  ? 294 TYR A CE2 1 
ATOM 1540 C CZ  . TYR A 1 209 ? 96.606  128.349 106.713 1.00 62.79  ? 294 TYR A CZ  1 
ATOM 1541 O OH  . TYR A 1 209 ? 95.339  128.716 106.320 1.00 76.05  ? 294 TYR A OH  1 
ATOM 1542 N N   . PHE A 1 210 ? 100.259 124.066 107.774 1.00 56.31  ? 295 PHE A N   1 
ATOM 1543 C CA  . PHE A 1 210 ? 99.456  122.930 107.337 1.00 53.47  ? 295 PHE A CA  1 
ATOM 1544 C C   . PHE A 1 210 ? 99.343  121.856 108.412 1.00 60.42  ? 295 PHE A C   1 
ATOM 1545 O O   . PHE A 1 210 ? 98.321  121.166 108.479 1.00 69.87  ? 295 PHE A O   1 
ATOM 1546 C CB  . PHE A 1 210 ? 100.011 122.361 106.033 1.00 52.80  ? 295 PHE A CB  1 
ATOM 1547 C CG  . PHE A 1 210 ? 99.710  123.222 104.845 1.00 53.32  ? 295 PHE A CG  1 
ATOM 1548 C CD1 . PHE A 1 210 ? 98.398  123.496 104.498 1.00 54.56  ? 295 PHE A CD1 1 
ATOM 1549 C CD2 . PHE A 1 210 ? 100.726 123.772 104.085 1.00 51.10  ? 295 PHE A CD2 1 
ATOM 1550 C CE1 . PHE A 1 210 ? 98.104  124.298 103.417 1.00 51.98  ? 295 PHE A CE1 1 
ATOM 1551 C CE2 . PHE A 1 210 ? 100.435 124.571 102.998 1.00 52.63  ? 295 PHE A CE2 1 
ATOM 1552 C CZ  . PHE A 1 210 ? 99.124  124.833 102.663 1.00 54.85  ? 295 PHE A CZ  1 
ATOM 1553 N N   . SER A 1 211 ? 100.345 121.726 109.284 1.00 58.10  ? 296 SER A N   1 
ATOM 1554 C CA  . SER A 1 211 ? 100.207 120.851 110.443 1.00 54.68  ? 296 SER A CA  1 
ATOM 1555 C C   . SER A 1 211 ? 99.067  121.319 111.338 1.00 64.47  ? 296 SER A C   1 
ATOM 1556 O O   . SER A 1 211 ? 98.255  120.512 111.804 1.00 73.88  ? 296 SER A O   1 
ATOM 1557 C CB  . SER A 1 211 ? 101.520 120.804 111.223 1.00 54.15  ? 296 SER A CB  1 
ATOM 1558 O OG  . SER A 1 211 ? 101.386 120.029 112.402 1.00 64.70  ? 296 SER A OG  1 
ATOM 1559 N N   . ASN A 1 212 ? 98.992  122.627 111.588 1.00 63.62  ? 297 ASN A N   1 
ATOM 1560 C CA  . ASN A 1 212 ? 97.888  123.161 112.379 1.00 64.03  ? 297 ASN A CA  1 
ATOM 1561 C C   . ASN A 1 212 ? 96.558  123.016 111.646 1.00 72.45  ? 297 ASN A C   1 
ATOM 1562 O O   . ASN A 1 212 ? 95.549  122.643 112.252 1.00 85.49  ? 297 ASN A O   1 
ATOM 1563 C CB  . ASN A 1 212 ? 98.158  124.621 112.738 1.00 62.63  ? 297 ASN A CB  1 
ATOM 1564 C CG  . ASN A 1 212 ? 99.472  124.805 113.477 1.00 65.85  ? 297 ASN A CG  1 
ATOM 1565 O OD1 . ASN A 1 212 ? 99.927  123.909 114.188 1.00 60.71  ? 297 ASN A OD1 1 
ATOM 1566 N ND2 . ASN A 1 212 ? 100.088 125.970 113.311 1.00 68.89  ? 297 ASN A ND2 1 
ATOM 1567 N N   . LEU A 1 213 ? 96.545  123.286 110.336 1.00 67.30  ? 298 LEU A N   1 
ATOM 1568 C CA  . LEU A 1 213 ? 95.321  123.179 109.548 1.00 70.36  ? 298 LEU A CA  1 
ATOM 1569 C C   . LEU A 1 213 ? 94.784  121.756 109.530 1.00 76.13  ? 298 LEU A C   1 
ATOM 1570 O O   . LEU A 1 213 ? 93.566  121.553 109.465 1.00 81.35  ? 298 LEU A O   1 
ATOM 1571 C CB  . LEU A 1 213 ? 95.578  123.665 108.121 1.00 67.15  ? 298 LEU A CB  1 
ATOM 1572 C CG  . LEU A 1 213 ? 94.390  123.688 107.158 1.00 73.65  ? 298 LEU A CG  1 
ATOM 1573 C CD1 . LEU A 1 213 ? 93.317  124.649 107.644 1.00 80.42  ? 298 LEU A CD1 1 
ATOM 1574 C CD2 . LEU A 1 213 ? 94.845  124.047 105.750 1.00 69.90  ? 298 LEU A CD2 1 
ATOM 1575 N N   . ARG A 1 214 ? 95.675  120.763 109.581 1.00 76.82  ? 299 ARG A N   1 
ATOM 1576 C CA  . ARG A 1 214 ? 95.243  119.372 109.656 1.00 77.67  ? 299 ARG A CA  1 
ATOM 1577 C C   . ARG A 1 214 ? 94.351  119.128 110.868 1.00 82.84  ? 299 ARG A C   1 
ATOM 1578 O O   . ARG A 1 214 ? 93.501  118.231 110.844 1.00 86.20  ? 299 ARG A O   1 
ATOM 1579 C CB  . ARG A 1 214 ? 96.472  118.460 109.693 1.00 73.39  ? 299 ARG A CB  1 
ATOM 1580 C CG  . ARG A 1 214 ? 96.182  116.970 109.767 1.00 76.96  ? 299 ARG A CG  1 
ATOM 1581 C CD  . ARG A 1 214 ? 96.345  116.451 111.186 1.00 83.86  ? 299 ARG A CD  1 
ATOM 1582 N NE  . ARG A 1 214 ? 97.454  117.102 111.871 1.00 81.50  ? 299 ARG A NE  1 
ATOM 1583 C CZ  . ARG A 1 214 ? 98.722  116.730 111.770 1.00 76.24  ? 299 ARG A CZ  1 
ATOM 1584 N NH1 . ARG A 1 214 ? 99.083  115.703 111.020 1.00 76.99  ? 299 ARG A NH1 1 
ATOM 1585 N NH2 . ARG A 1 214 ? 99.651  117.407 112.440 1.00 74.95  ? 299 ARG A NH2 1 
ATOM 1586 N N   . LYS A 1 215 ? 94.520  119.920 111.925 1.00 85.41  ? 300 LYS A N   1 
ATOM 1587 C CA  . LYS A 1 215 ? 93.745  119.781 113.152 1.00 88.97  ? 300 LYS A CA  1 
ATOM 1588 C C   . LYS A 1 215 ? 92.601  120.782 113.259 1.00 90.10  ? 300 LYS A C   1 
ATOM 1589 O O   . LYS A 1 215 ? 91.547  120.447 113.808 1.00 93.98  ? 300 LYS A O   1 
ATOM 1590 C CB  . LYS A 1 215 ? 94.663  119.929 114.369 1.00 84.37  ? 300 LYS A CB  1 
ATOM 1591 C CG  . LYS A 1 215 ? 95.721  118.843 114.484 1.00 80.79  ? 300 LYS A CG  1 
ATOM 1592 C CD  . LYS A 1 215 ? 96.551  119.010 115.746 1.00 85.99  ? 300 LYS A CD  1 
ATOM 1593 C CE  . LYS A 1 215 ? 97.460  120.225 115.652 1.00 81.74  ? 300 LYS A CE  1 
ATOM 1594 N NZ  . LYS A 1 215 ? 98.502  120.060 114.601 1.00 78.90  ? 300 LYS A NZ  1 
ATOM 1595 N N   . ASN A 1 216 ? 92.781  122.005 112.750 1.00 90.02  ? 301 ASN A N   1 
ATOM 1596 C CA  . ASN A 1 216 ? 91.758  123.034 112.920 1.00 94.19  ? 301 ASN A CA  1 
ATOM 1597 C C   . ASN A 1 216 ? 90.491  122.728 112.131 1.00 98.95  ? 301 ASN A C   1 
ATOM 1598 O O   . ASN A 1 216 ? 89.393  123.077 112.577 1.00 105.86 ? 301 ASN A O   1 
ATOM 1599 C CB  . ASN A 1 216 ? 92.301  124.410 112.526 1.00 92.27  ? 301 ASN A CB  1 
ATOM 1600 C CG  . ASN A 1 216 ? 93.443  124.868 113.413 1.00 93.31  ? 301 ASN A CG  1 
ATOM 1601 O OD1 . ASN A 1 216 ? 94.577  125.015 112.962 1.00 92.46  ? 301 ASN A OD1 1 
ATOM 1602 N ND2 . ASN A 1 216 ? 93.144  125.096 114.687 1.00 97.24  ? 301 ASN A ND2 1 
ATOM 1603 N N   . LEU A 1 217 ? 90.613  122.094 110.967 1.00 94.73  ? 302 LEU A N   1 
ATOM 1604 C CA  . LEU A 1 217 ? 89.430  121.777 110.180 1.00 101.01 ? 302 LEU A CA  1 
ATOM 1605 C C   . LEU A 1 217 ? 88.566  120.749 110.906 1.00 110.08 ? 302 LEU A C   1 
ATOM 1606 O O   . LEU A 1 217 ? 89.062  119.895 111.646 1.00 109.40 ? 302 LEU A O   1 
ATOM 1607 C CB  . LEU A 1 217 ? 89.823  121.278 108.786 1.00 101.20 ? 302 LEU A CB  1 
ATOM 1608 C CG  . LEU A 1 217 ? 90.759  120.081 108.600 1.00 101.40 ? 302 LEU A CG  1 
ATOM 1609 C CD1 . LEU A 1 217 ? 90.006  118.759 108.649 1.00 101.28 ? 302 LEU A CD1 1 
ATOM 1610 C CD2 . LEU A 1 217 ? 91.520  120.215 107.288 1.00 89.22  ? 302 LEU A CD2 1 
ATOM 1611 N N   . GLY A 1 218 ? 87.257  120.842 110.683 1.00 117.64 ? 303 GLY A N   1 
ATOM 1612 C CA  . GLY A 1 218 ? 86.287  120.103 111.457 1.00 123.41 ? 303 GLY A CA  1 
ATOM 1613 C C   . GLY A 1 218 ? 86.320  118.605 111.235 1.00 130.18 ? 303 GLY A C   1 
ATOM 1614 O O   . GLY A 1 218 ? 87.094  118.083 110.425 1.00 126.36 ? 303 GLY A O   1 
ATOM 1615 N N   . PRO A 1 219 ? 85.471  117.883 111.962 1.00 134.72 ? 304 PRO A N   1 
ATOM 1616 C CA  . PRO A 1 219 ? 85.465  116.419 111.868 1.00 132.26 ? 304 PRO A CA  1 
ATOM 1617 C C   . PRO A 1 219 ? 84.867  115.945 110.553 1.00 128.76 ? 304 PRO A C   1 
ATOM 1618 O O   . PRO A 1 219 ? 84.243  116.697 109.802 1.00 126.24 ? 304 PRO A O   1 
ATOM 1619 C CB  . PRO A 1 219 ? 84.605  115.993 113.060 1.00 132.27 ? 304 PRO A CB  1 
ATOM 1620 C CG  . PRO A 1 219 ? 83.677  117.144 113.266 1.00 132.30 ? 304 PRO A CG  1 
ATOM 1621 C CD  . PRO A 1 219 ? 84.467  118.380 112.919 1.00 133.00 ? 304 PRO A CD  1 
ATOM 1622 N N   . GLY A 1 220 ? 85.076  114.659 110.278 1.00 126.53 ? 305 GLY A N   1 
ATOM 1623 C CA  . GLY A 1 220 ? 84.593  114.048 109.060 1.00 122.46 ? 305 GLY A CA  1 
ATOM 1624 C C   . GLY A 1 220 ? 85.439  114.314 107.837 1.00 122.03 ? 305 GLY A C   1 
ATOM 1625 O O   . GLY A 1 220 ? 85.099  113.826 106.751 1.00 124.26 ? 305 GLY A O   1 
ATOM 1626 N N   . VAL A 1 221 ? 86.528  115.065 107.975 1.00 118.75 ? 306 VAL A N   1 
ATOM 1627 C CA  . VAL A 1 221 ? 87.407  115.415 106.867 1.00 111.92 ? 306 VAL A CA  1 
ATOM 1628 C C   . VAL A 1 221 ? 88.793  114.869 107.170 1.00 108.75 ? 306 VAL A C   1 
ATOM 1629 O O   . VAL A 1 221 ? 89.300  115.035 108.286 1.00 108.86 ? 306 VAL A O   1 
ATOM 1630 C CB  . VAL A 1 221 ? 87.458  116.937 106.640 1.00 106.75 ? 306 VAL A CB  1 
ATOM 1631 C CG1 . VAL A 1 221 ? 88.238  117.262 105.375 1.00 98.04  ? 306 VAL A CG1 1 
ATOM 1632 C CG2 . VAL A 1 221 ? 86.052  117.514 106.572 1.00 108.36 ? 306 VAL A CG2 1 
ATOM 1633 N N   . ASP A 1 222 ? 89.402  114.218 106.182 1.00 104.36 ? 307 ASP A N   1 
ATOM 1634 C CA  . ASP A 1 222 ? 90.761  113.720 106.338 1.00 95.24  ? 307 ASP A CA  1 
ATOM 1635 C C   . ASP A 1 222 ? 91.730  114.895 106.296 1.00 89.23  ? 307 ASP A C   1 
ATOM 1636 O O   . ASP A 1 222 ? 92.216  115.270 105.224 1.00 85.47  ? 307 ASP A O   1 
ATOM 1637 C CB  . ASP A 1 222 ? 91.091  112.697 105.249 1.00 93.13  ? 307 ASP A CB  1 
ATOM 1638 C CG  . ASP A 1 222 ? 92.266  111.811 105.615 1.00 94.92  ? 307 ASP A CG  1 
ATOM 1639 O OD1 . ASP A 1 222 ? 92.949  112.105 106.618 1.00 92.24  ? 307 ASP A OD1 1 
ATOM 1640 O OD2 . ASP A 1 222 ? 92.507  110.817 104.897 1.00 93.89  ? 307 ASP A OD2 1 
ATOM 1641 N N   . GLY A 1 223 ? 92.002  115.485 107.463 1.00 87.97  ? 308 GLY A N   1 
ATOM 1642 C CA  . GLY A 1 223 ? 92.828  116.681 107.506 1.00 80.20  ? 308 GLY A CA  1 
ATOM 1643 C C   . GLY A 1 223 ? 94.230  116.452 106.977 1.00 74.03  ? 308 GLY A C   1 
ATOM 1644 O O   . GLY A 1 223 ? 94.808  117.326 106.327 1.00 75.04  ? 308 GLY A O   1 
ATOM 1645 N N   . TRP A 1 224 ? 94.799  115.277 107.255 1.00 75.18  ? 309 TRP A N   1 
ATOM 1646 C CA  . TRP A 1 224 ? 96.116  114.953 106.719 1.00 72.09  ? 309 TRP A CA  1 
ATOM 1647 C C   . TRP A 1 224 ? 96.088  114.872 105.199 1.00 71.68  ? 309 TRP A C   1 
ATOM 1648 O O   . TRP A 1 224 ? 97.033  115.309 104.534 1.00 67.26  ? 309 TRP A O   1 
ATOM 1649 C CB  . TRP A 1 224 ? 96.626  113.651 107.340 1.00 74.41  ? 309 TRP A CB  1 
ATOM 1650 C CG  . TRP A 1 224 ? 97.867  113.091 106.702 1.00 79.43  ? 309 TRP A CG  1 
ATOM 1651 C CD1 . TRP A 1 224 ? 97.996  111.871 106.110 1.00 84.52  ? 309 TRP A CD1 1 
ATOM 1652 C CD2 . TRP A 1 224 ? 99.141  113.736 106.566 1.00 80.00  ? 309 TRP A CD2 1 
ATOM 1653 N NE1 . TRP A 1 224 ? 99.272  111.706 105.630 1.00 84.32  ? 309 TRP A NE1 1 
ATOM 1654 C CE2 . TRP A 1 224 ? 99.994  112.839 105.895 1.00 78.14  ? 309 TRP A CE2 1 
ATOM 1655 C CE3 . TRP A 1 224 ? 99.645  114.981 106.951 1.00 80.60  ? 309 TRP A CE3 1 
ATOM 1656 C CZ2 . TRP A 1 224 ? 101.319 113.147 105.602 1.00 72.81  ? 309 TRP A CZ2 1 
ATOM 1657 C CZ3 . TRP A 1 224 ? 100.963 115.281 106.653 1.00 75.88  ? 309 TRP A CZ3 1 
ATOM 1658 C CH2 . TRP A 1 224 ? 101.783 114.370 105.990 1.00 70.44  ? 309 TRP A CH2 1 
ATOM 1659 N N   . ALA A 1 225 ? 95.005  114.337 104.628 1.00 78.63  ? 310 ALA A N   1 
ATOM 1660 C CA  . ALA A 1 225 ? 94.887  114.291 103.174 1.00 73.40  ? 310 ALA A CA  1 
ATOM 1661 C C   . ALA A 1 225 ? 94.828  115.692 102.574 1.00 67.67  ? 310 ALA A C   1 
ATOM 1662 O O   . ALA A 1 225 ? 95.488  115.966 101.566 1.00 68.23  ? 310 ALA A O   1 
ATOM 1663 C CB  . ALA A 1 225 ? 93.655  113.483 102.770 1.00 76.98  ? 310 ALA A CB  1 
ATOM 1664 N N   . VAL A 1 226 ? 94.049  116.591 103.180 1.00 72.87  ? 311 VAL A N   1 
ATOM 1665 C CA  . VAL A 1 226 ? 93.952  117.956 102.670 1.00 65.52  ? 311 VAL A CA  1 
ATOM 1666 C C   . VAL A 1 226 ? 95.288  118.676 102.803 1.00 65.92  ? 311 VAL A C   1 
ATOM 1667 O O   . VAL A 1 226 ? 95.724  119.382 101.885 1.00 66.14  ? 311 VAL A O   1 
ATOM 1668 C CB  . VAL A 1 226 ? 92.823  118.716 103.392 1.00 63.85  ? 311 VAL A CB  1 
ATOM 1669 C CG1 . VAL A 1 226 ? 92.800  120.176 102.961 1.00 65.10  ? 311 VAL A CG1 1 
ATOM 1670 C CG2 . VAL A 1 226 ? 91.481  118.055 103.121 1.00 70.85  ? 311 VAL A CG2 1 
ATOM 1671 N N   . SER A 1 227 ? 95.958  118.511 103.947 1.00 66.64  ? 312 SER A N   1 
ATOM 1672 C CA  . SER A 1 227 ? 97.256  119.147 104.145 1.00 57.48  ? 312 SER A CA  1 
ATOM 1673 C C   . SER A 1 227 ? 98.281  118.629 103.146 1.00 61.92  ? 312 SER A C   1 
ATOM 1674 O O   . SER A 1 227 ? 99.070  119.406 102.597 1.00 66.82  ? 312 SER A O   1 
ATOM 1675 C CB  . SER A 1 227 ? 97.739  118.920 105.578 1.00 66.60  ? 312 SER A CB  1 
ATOM 1676 O OG  . SER A 1 227 ? 96.856  119.513 106.515 1.00 74.80  ? 312 SER A OG  1 
ATOM 1677 N N   . LEU A 1 228 ? 98.284  117.317 102.895 1.00 64.03  ? 313 LEU A N   1 
ATOM 1678 C CA  . LEU A 1 228 ? 99.212  116.750 101.923 1.00 59.52  ? 313 LEU A CA  1 
ATOM 1679 C C   . LEU A 1 228 ? 98.901  117.231 100.513 1.00 59.81  ? 313 LEU A C   1 
ATOM 1680 O O   . LEU A 1 228 ? 99.819  117.533 99.742  1.00 61.74  ? 313 LEU A O   1 
ATOM 1681 C CB  . LEU A 1 228 ? 99.177  115.225 101.993 1.00 61.03  ? 313 LEU A CB  1 
ATOM 1682 C CG  . LEU A 1 228 ? 100.103 114.503 101.016 1.00 63.50  ? 313 LEU A CG  1 
ATOM 1683 C CD1 . LEU A 1 228 ? 101.551 114.810 101.336 1.00 65.47  ? 313 LEU A CD1 1 
ATOM 1684 C CD2 . LEU A 1 228 ? 99.857  113.009 101.063 1.00 68.94  ? 313 LEU A CD2 1 
ATOM 1685 N N   . LYS A 1 229 ? 97.617  117.308 100.153 1.00 60.12  ? 314 LYS A N   1 
ATOM 1686 C CA  . LYS A 1 229 ? 97.255  117.822 98.837  1.00 54.67  ? 314 LYS A CA  1 
ATOM 1687 C C   . LYS A 1 229 ? 97.713  119.262 98.666  1.00 58.45  ? 314 LYS A C   1 
ATOM 1688 O O   . LYS A 1 229 ? 98.259  119.624 97.620  1.00 62.24  ? 314 LYS A O   1 
ATOM 1689 C CB  . LYS A 1 229 ? 95.745  117.714 98.615  1.00 60.29  ? 314 LYS A CB  1 
ATOM 1690 C CG  . LYS A 1 229 ? 95.270  116.332 98.206  1.00 63.58  ? 314 LYS A CG  1 
ATOM 1691 C CD  . LYS A 1 229 ? 93.918  116.402 97.513  1.00 70.23  ? 314 LYS A CD  1 
ATOM 1692 C CE  . LYS A 1 229 ? 93.551  115.070 96.880  1.00 77.44  ? 314 LYS A CE  1 
ATOM 1693 N NZ  . LYS A 1 229 ? 92.340  115.179 96.020  1.00 84.06  ? 314 LYS A NZ  1 
ATOM 1694 N N   . ALA A 1 230 ? 97.516  120.095 99.690  1.00 61.50  ? 315 ALA A N   1 
ATOM 1695 C CA  . ALA A 1 230 ? 97.940  121.488 99.595  1.00 56.35  ? 315 ALA A CA  1 
ATOM 1696 C C   . ALA A 1 230 ? 99.460  121.610 99.530  1.00 52.97  ? 315 ALA A C   1 
ATOM 1697 O O   . ALA A 1 230 ? 99.991  122.408 98.747  1.00 57.68  ? 315 ALA A O   1 
ATOM 1698 C CB  . ALA A 1 230 ? 97.384  122.283 100.773 1.00 57.66  ? 315 ALA A CB  1 
ATOM 1699 N N   . MET A 1 231 ? 100.178 120.831 100.343 1.00 52.19  ? 316 MET A N   1 
ATOM 1700 C CA  . MET A 1 231 ? 101.635 120.894 100.327 1.00 51.67  ? 316 MET A CA  1 
ATOM 1701 C C   . MET A 1 231 ? 102.197 120.418 98.993  1.00 57.75  ? 316 MET A C   1 
ATOM 1702 O O   . MET A 1 231 ? 103.136 121.018 98.461  1.00 60.98  ? 316 MET A O   1 
ATOM 1703 C CB  . MET A 1 231 ? 102.213 120.078 101.484 1.00 55.59  ? 316 MET A CB  1 
ATOM 1704 C CG  . MET A 1 231 ? 102.285 120.848 102.795 1.00 59.93  ? 316 MET A CG  1 
ATOM 1705 S SD  . MET A 1 231 ? 103.202 119.990 104.088 1.00 77.34  ? 316 MET A SD  1 
ATOM 1706 C CE  . MET A 1 231 ? 102.291 118.453 104.190 1.00 64.41  ? 316 MET A CE  1 
ATOM 1707 N N   . MET A 1 232 ? 101.629 119.352 98.424  1.00 57.98  ? 317 MET A N   1 
ATOM 1708 C CA  . MET A 1 232 ? 102.086 118.897 97.116  1.00 53.38  ? 317 MET A CA  1 
ATOM 1709 C C   . MET A 1 232 ? 101.669 119.857 96.010  1.00 56.79  ? 317 MET A C   1 
ATOM 1710 O O   . MET A 1 232 ? 102.372 119.977 95.003  1.00 61.46  ? 317 MET A O   1 
ATOM 1711 C CB  . MET A 1 232 ? 101.567 117.487 96.838  1.00 52.21  ? 317 MET A CB  1 
ATOM 1712 C CG  . MET A 1 232 ? 102.153 116.415 97.752  1.00 56.98  ? 317 MET A CG  1 
ATOM 1713 S SD  . MET A 1 232 ? 103.951 116.273 97.652  1.00 79.34  ? 317 MET A SD  1 
ATOM 1714 C CE  . MET A 1 232 ? 104.461 117.146 99.133  1.00 64.17  ? 317 MET A CE  1 
ATOM 1715 N N   . SER A 1 233 ? 100.542 120.553 96.176  1.00 56.88  ? 318 SER A N   1 
ATOM 1716 C CA  . SER A 1 233 ? 100.184 121.606 95.233  1.00 54.05  ? 318 SER A CA  1 
ATOM 1717 C C   . SER A 1 233 ? 101.210 122.728 95.261  1.00 53.59  ? 318 SER A C   1 
ATOM 1718 O O   . SER A 1 233 ? 101.598 123.250 94.212  1.00 57.14  ? 318 SER A O   1 
ATOM 1719 C CB  . SER A 1 233 ? 98.788  122.144 95.549  1.00 57.99  ? 318 SER A CB  1 
ATOM 1720 O OG  . SER A 1 233 ? 97.877  121.087 95.797  1.00 66.70  ? 318 SER A OG  1 
ATOM 1721 N N   . ILE A 1 234 ? 101.669 123.105 96.455  1.00 54.14  ? 319 ILE A N   1 
ATOM 1722 C CA  . ILE A 1 234 ? 102.739 124.093 96.557  1.00 51.11  ? 319 ILE A CA  1 
ATOM 1723 C C   . ILE A 1 234 ? 104.026 123.553 95.942  1.00 52.31  ? 319 ILE A C   1 
ATOM 1724 O O   . ILE A 1 234 ? 104.775 124.290 95.288  1.00 60.96  ? 319 ILE A O   1 
ATOM 1725 C CB  . ILE A 1 234 ? 102.943 124.518 98.023  1.00 49.42  ? 319 ILE A CB  1 
ATOM 1726 C CG1 . ILE A 1 234 ? 101.663 125.141 98.579  1.00 49.96  ? 319 ILE A CG1 1 
ATOM 1727 C CG2 . ILE A 1 234 ? 104.105 125.492 98.145  1.00 49.13  ? 319 ILE A CG2 1 
ATOM 1728 C CD1 . ILE A 1 234 ? 101.794 125.618 100.003 1.00 47.97  ? 319 ILE A CD1 1 
ATOM 1729 N N   . VAL A 1 235 ? 104.302 122.262 96.141  1.00 52.52  ? 320 VAL A N   1 
ATOM 1730 C CA  . VAL A 1 235 ? 105.503 121.653 95.571  1.00 52.44  ? 320 VAL A CA  1 
ATOM 1731 C C   . VAL A 1 235 ? 105.477 121.747 94.051  1.00 54.86  ? 320 VAL A C   1 
ATOM 1732 O O   . VAL A 1 235 ? 106.456 122.160 93.421  1.00 57.26  ? 320 VAL A O   1 
ATOM 1733 C CB  . VAL A 1 235 ? 105.641 120.194 96.041  1.00 53.64  ? 320 VAL A CB  1 
ATOM 1734 C CG1 . VAL A 1 235 ? 106.641 119.446 95.171  1.00 53.57  ? 320 VAL A CG1 1 
ATOM 1735 C CG2 . VAL A 1 235 ? 106.071 120.145 97.495  1.00 57.68  ? 320 VAL A CG2 1 
ATOM 1736 N N   . VAL A 1 236 ? 104.351 121.377 93.438  1.00 55.45  ? 321 VAL A N   1 
ATOM 1737 C CA  . VAL A 1 236 ? 104.266 121.421 91.980  1.00 51.61  ? 321 VAL A CA  1 
ATOM 1738 C C   . VAL A 1 236 ? 104.198 122.856 91.473  1.00 55.01  ? 321 VAL A C   1 
ATOM 1739 O O   . VAL A 1 236 ? 104.681 123.148 90.376  1.00 61.57  ? 321 VAL A O   1 
ATOM 1740 C CB  . VAL A 1 236 ? 103.086 120.574 91.464  1.00 51.52  ? 321 VAL A CB  1 
ATOM 1741 C CG1 . VAL A 1 236 ? 103.124 119.198 92.086  1.00 53.42  ? 321 VAL A CG1 1 
ATOM 1742 C CG2 . VAL A 1 236 ? 101.754 121.251 91.750  1.00 53.69  ? 321 VAL A CG2 1 
ATOM 1743 N N   . GLY A 1 237 ? 103.619 123.777 92.247  1.00 55.19  ? 322 GLY A N   1 
ATOM 1744 C CA  . GLY A 1 237 ? 103.643 125.173 91.844  1.00 52.83  ? 322 GLY A CA  1 
ATOM 1745 C C   . GLY A 1 237 ? 105.053 125.728 91.807  1.00 55.88  ? 322 GLY A C   1 
ATOM 1746 O O   . GLY A 1 237 ? 105.453 126.386 90.842  1.00 64.62  ? 322 GLY A O   1 
ATOM 1747 N N   . MET A 1 238 ? 105.837 125.443 92.847  1.00 52.41  ? 323 MET A N   1 
ATOM 1748 C CA  . MET A 1 238 ? 107.232 125.865 92.851  1.00 50.70  ? 323 MET A CA  1 
ATOM 1749 C C   . MET A 1 238 ? 108.040 125.132 91.787  1.00 55.97  ? 323 MET A C   1 
ATOM 1750 O O   . MET A 1 238 ? 108.975 125.706 91.225  1.00 60.98  ? 323 MET A O   1 
ATOM 1751 C CB  . MET A 1 238 ? 107.847 125.652 94.233  1.00 49.35  ? 323 MET A CB  1 
ATOM 1752 C CG  . MET A 1 238 ? 107.234 126.515 95.327  1.00 50.85  ? 323 MET A CG  1 
ATOM 1753 S SD  . MET A 1 238 ? 107.496 128.279 95.061  1.00 72.97  ? 323 MET A SD  1 
ATOM 1754 C CE  . MET A 1 238 ? 106.473 128.977 96.355  1.00 60.62  ? 323 MET A CE  1 
ATOM 1755 N N   . GLY A 1 239 ? 107.697 123.878 91.488  1.00 55.04  ? 324 GLY A N   1 
ATOM 1756 C CA  . GLY A 1 239 ? 108.383 123.169 90.418  1.00 50.64  ? 324 GLY A CA  1 
ATOM 1757 C C   . GLY A 1 239 ? 108.111 123.763 89.049  1.00 53.39  ? 324 GLY A C   1 
ATOM 1758 O O   . GLY A 1 239 ? 109.024 123.902 88.229  1.00 60.77  ? 324 GLY A O   1 
ATOM 1759 N N   . LEU A 1 240 ? 106.851 124.109 88.775  1.00 50.76  ? 325 LEU A N   1 
ATOM 1760 C CA  . LEU A 1 240 ? 106.531 124.816 87.541  1.00 49.66  ? 325 LEU A CA  1 
ATOM 1761 C C   . LEU A 1 240 ? 107.200 126.181 87.502  1.00 54.02  ? 325 LEU A C   1 
ATOM 1762 O O   . LEU A 1 240 ? 107.624 126.630 86.433  1.00 62.66  ? 325 LEU A O   1 
ATOM 1763 C CB  . LEU A 1 240 ? 105.017 124.961 87.381  1.00 53.78  ? 325 LEU A CB  1 
ATOM 1764 C CG  . LEU A 1 240 ? 104.194 123.674 87.291  1.00 62.22  ? 325 LEU A CG  1 
ATOM 1765 C CD1 . LEU A 1 240 ? 102.706 123.986 87.311  1.00 63.16  ? 325 LEU A CD1 1 
ATOM 1766 C CD2 . LEU A 1 240 ? 104.563 122.886 86.044  1.00 62.71  ? 325 LEU A CD2 1 
ATOM 1767 N N   . ALA A 1 241 ? 107.311 126.850 88.652  1.00 51.03  ? 326 ALA A N   1 
ATOM 1768 C CA  . ALA A 1 241 ? 108.062 128.099 88.706  1.00 48.94  ? 326 ALA A CA  1 
ATOM 1769 C C   . ALA A 1 241 ? 109.528 127.872 88.356  1.00 52.02  ? 326 ALA A C   1 
ATOM 1770 O O   . ALA A 1 241 ? 110.132 128.672 87.635  1.00 60.28  ? 326 ALA A O   1 
ATOM 1771 C CB  . ALA A 1 241 ? 107.931 128.731 90.092  1.00 48.34  ? 326 ALA A CB  1 
ATOM 1772 N N   . ILE A 1 242 ? 110.113 126.782 88.858  1.00 54.42  ? 327 ILE A N   1 
ATOM 1773 C CA  . ILE A 1 242 ? 111.503 126.460 88.550  1.00 51.08  ? 327 ILE A CA  1 
ATOM 1774 C C   . ILE A 1 242 ? 111.673 126.216 87.058  1.00 53.46  ? 327 ILE A C   1 
ATOM 1775 O O   . ILE A 1 242 ? 112.619 126.713 86.436  1.00 61.24  ? 327 ILE A O   1 
ATOM 1776 C CB  . ILE A 1 242 ? 111.963 125.239 89.370  1.00 52.46  ? 327 ILE A CB  1 
ATOM 1777 C CG1 . ILE A 1 242 ? 112.113 125.598 90.848  1.00 51.02  ? 327 ILE A CG1 1 
ATOM 1778 C CG2 . ILE A 1 242 ? 113.279 124.702 88.830  1.00 56.75  ? 327 ILE A CG2 1 
ATOM 1779 C CD1 . ILE A 1 242 ? 111.834 124.436 91.780  1.00 50.17  ? 327 ILE A CD1 1 
ATOM 1780 N N   . CYS A 1 243 ? 110.762 125.443 86.463  1.00 49.96  ? 328 CYS A N   1 
ATOM 1781 C CA  . CYS A 1 243 ? 110.841 125.170 85.029  1.00 49.21  ? 328 CYS A CA  1 
ATOM 1782 C C   . CYS A 1 243 ? 110.677 126.446 84.210  1.00 53.17  ? 328 CYS A C   1 
ATOM 1783 O O   . CYS A 1 243 ? 111.406 126.662 83.233  1.00 61.98  ? 328 CYS A O   1 
ATOM 1784 C CB  . CYS A 1 243 ? 109.790 124.135 84.630  1.00 51.61  ? 328 CYS A CB  1 
ATOM 1785 S SG  . CYS A 1 243 ? 109.917 122.558 85.505  1.00 70.53  ? 328 CYS A SG  1 
ATOM 1786 N N   . LEU A 1 244 ? 109.727 127.303 84.593  1.00 51.43  ? 329 LEU A N   1 
ATOM 1787 C CA  . LEU A 1 244 ? 109.516 128.554 83.873  1.00 50.38  ? 329 LEU A CA  1 
ATOM 1788 C C   . LEU A 1 244 ? 110.729 129.467 83.984  1.00 55.73  ? 329 LEU A C   1 
ATOM 1789 O O   . LEU A 1 244 ? 111.125 130.100 83.001  1.00 62.59  ? 329 LEU A O   1 
ATOM 1790 C CB  . LEU A 1 244 ? 108.264 129.257 84.399  1.00 51.65  ? 329 LEU A CB  1 
ATOM 1791 C CG  . LEU A 1 244 ? 106.922 128.671 83.956  1.00 63.15  ? 329 LEU A CG  1 
ATOM 1792 C CD1 . LEU A 1 244 ? 105.767 129.406 84.619  1.00 66.56  ? 329 LEU A CD1 1 
ATOM 1793 C CD2 . LEU A 1 244 ? 106.791 128.714 82.442  1.00 65.87  ? 329 LEU A CD2 1 
ATOM 1794 N N   . LEU A 1 245 ? 111.334 129.549 85.171  1.00 50.83  ? 330 LEU A N   1 
ATOM 1795 C CA  . LEU A 1 245 ? 112.523 130.376 85.340  1.00 47.96  ? 330 LEU A CA  1 
ATOM 1796 C C   . LEU A 1 245 ? 113.706 129.811 84.563  1.00 55.61  ? 330 LEU A C   1 
ATOM 1797 O O   . LEU A 1 245 ? 114.497 130.570 83.994  1.00 64.68  ? 330 LEU A O   1 
ATOM 1798 C CB  . LEU A 1 245 ? 112.861 130.509 86.823  1.00 48.43  ? 330 LEU A CB  1 
ATOM 1799 C CG  . LEU A 1 245 ? 111.897 131.332 87.680  1.00 47.57  ? 330 LEU A CG  1 
ATOM 1800 C CD1 . LEU A 1 245 ? 112.011 130.934 89.143  1.00 47.01  ? 330 LEU A CD1 1 
ATOM 1801 C CD2 . LEU A 1 245 ? 112.155 132.819 87.505  1.00 55.81  ? 330 LEU A CD2 1 
ATOM 1802 N N   . TYR A 1 246 ? 113.845 128.483 84.529  1.00 54.67  ? 331 TYR A N   1 
ATOM 1803 C CA  . TYR A 1 246 ? 114.890 127.863 83.720  1.00 52.17  ? 331 TYR A CA  1 
ATOM 1804 C C   . TYR A 1 246 ? 114.713 128.207 82.248  1.00 56.26  ? 331 TYR A C   1 
ATOM 1805 O O   . TYR A 1 246 ? 115.672 128.584 81.563  1.00 62.14  ? 331 TYR A O   1 
ATOM 1806 C CB  . TYR A 1 246 ? 114.872 126.347 83.922  1.00 48.02  ? 331 TYR A CB  1 
ATOM 1807 C CG  . TYR A 1 246 ? 116.050 125.628 83.307  1.00 53.91  ? 331 TYR A CG  1 
ATOM 1808 C CD1 . TYR A 1 246 ? 117.261 125.536 83.977  1.00 59.01  ? 331 TYR A CD1 1 
ATOM 1809 C CD2 . TYR A 1 246 ? 115.950 125.044 82.051  1.00 54.80  ? 331 TYR A CD2 1 
ATOM 1810 C CE1 . TYR A 1 246 ? 118.337 124.878 83.415  1.00 57.72  ? 331 TYR A CE1 1 
ATOM 1811 C CE2 . TYR A 1 246 ? 117.022 124.387 81.480  1.00 54.53  ? 331 TYR A CE2 1 
ATOM 1812 C CZ  . TYR A 1 246 ? 118.214 124.308 82.167  1.00 57.38  ? 331 TYR A CZ  1 
ATOM 1813 O OH  . TYR A 1 246 ? 119.286 123.654 81.605  1.00 64.83  ? 331 TYR A OH  1 
ATOM 1814 N N   . TRP A 1 247 ? 113.481 128.088 81.748  1.00 54.54  ? 332 TRP A N   1 
ATOM 1815 C CA  . TRP A 1 247 ? 113.200 128.445 80.362  1.00 54.78  ? 332 TRP A CA  1 
ATOM 1816 C C   . TRP A 1 247 ? 113.487 129.920 80.104  1.00 60.74  ? 332 TRP A C   1 
ATOM 1817 O O   . TRP A 1 247 ? 114.058 130.278 79.066  1.00 72.03  ? 332 TRP A O   1 
ATOM 1818 C CB  . TRP A 1 247 ? 111.746 128.102 80.031  1.00 57.65  ? 332 TRP A CB  1 
ATOM 1819 C CG  . TRP A 1 247 ? 111.226 128.741 78.785  1.00 67.08  ? 332 TRP A CG  1 
ATOM 1820 C CD1 . TRP A 1 247 ? 111.357 128.278 77.509  1.00 71.63  ? 332 TRP A CD1 1 
ATOM 1821 C CD2 . TRP A 1 247 ? 110.472 129.955 78.698  1.00 66.20  ? 332 TRP A CD2 1 
ATOM 1822 N NE1 . TRP A 1 247 ? 110.739 129.134 76.630  1.00 70.59  ? 332 TRP A NE1 1 
ATOM 1823 C CE2 . TRP A 1 247 ? 110.187 130.172 77.335  1.00 68.12  ? 332 TRP A CE2 1 
ATOM 1824 C CE3 . TRP A 1 247 ? 110.015 130.883 79.639  1.00 66.97  ? 332 TRP A CE3 1 
ATOM 1825 C CZ2 . TRP A 1 247 ? 109.466 131.277 76.891  1.00 72.36  ? 332 TRP A CZ2 1 
ATOM 1826 C CZ3 . TRP A 1 247 ? 109.299 131.979 79.196  1.00 70.53  ? 332 TRP A CZ3 1 
ATOM 1827 C CH2 . TRP A 1 247 ? 109.031 132.167 77.834  1.00 73.51  ? 332 TRP A CH2 1 
ATOM 1828 N N   . TRP A 1 248 ? 113.112 130.788 81.046  1.00 57.45  ? 333 TRP A N   1 
ATOM 1829 C CA  . TRP A 1 248 ? 113.345 132.218 80.883  1.00 61.14  ? 333 TRP A CA  1 
ATOM 1830 C C   . TRP A 1 248 ? 114.835 132.533 80.818  1.00 65.10  ? 333 TRP A C   1 
ATOM 1831 O O   . TRP A 1 248 ? 115.276 133.322 79.976  1.00 73.95  ? 333 TRP A O   1 
ATOM 1832 C CB  . TRP A 1 248 ? 112.680 132.990 82.023  1.00 62.56  ? 333 TRP A CB  1 
ATOM 1833 C CG  . TRP A 1 248 ? 113.173 134.398 82.147  1.00 69.54  ? 333 TRP A CG  1 
ATOM 1834 C CD1 . TRP A 1 248 ? 114.217 134.840 82.907  1.00 71.41  ? 333 TRP A CD1 1 
ATOM 1835 C CD2 . TRP A 1 248 ? 112.652 135.548 81.472  1.00 70.72  ? 333 TRP A CD2 1 
ATOM 1836 N NE1 . TRP A 1 248 ? 114.373 136.196 82.753  1.00 70.51  ? 333 TRP A NE1 1 
ATOM 1837 C CE2 . TRP A 1 248 ? 113.424 136.655 81.877  1.00 72.56  ? 333 TRP A CE2 1 
ATOM 1838 C CE3 . TRP A 1 248 ? 111.605 135.750 80.569  1.00 75.22  ? 333 TRP A CE3 1 
ATOM 1839 C CZ2 . TRP A 1 248 ? 113.182 137.944 81.409  1.00 80.80  ? 333 TRP A CZ2 1 
ATOM 1840 C CZ3 . TRP A 1 248 ? 111.366 137.030 80.105  1.00 82.64  ? 333 TRP A CZ3 1 
ATOM 1841 C CH2 . TRP A 1 248 ? 112.151 138.111 80.526  1.00 85.85  ? 333 TRP A CH2 1 
ATOM 1842 N N   . VAL A 1 249 ? 115.627 131.933 81.708  1.00 63.31  ? 334 VAL A N   1 
ATOM 1843 C CA  . VAL A 1 249 ? 117.065 132.192 81.702  1.00 61.58  ? 334 VAL A CA  1 
ATOM 1844 C C   . VAL A 1 249 ? 117.699 131.642 80.432  1.00 66.18  ? 334 VAL A C   1 
ATOM 1845 O O   . VAL A 1 249 ? 118.590 132.267 79.844  1.00 77.20  ? 334 VAL A O   1 
ATOM 1846 C CB  . VAL A 1 249 ? 117.732 131.611 82.963  1.00 61.68  ? 334 VAL A CB  1 
ATOM 1847 C CG1 . VAL A 1 249 ? 119.225 131.895 82.947  1.00 66.79  ? 334 VAL A CG1 1 
ATOM 1848 C CG2 . VAL A 1 249 ? 117.115 132.207 84.204  1.00 59.43  ? 334 VAL A CG2 1 
ATOM 1849 N N   . ASN A 1 250 ? 117.251 130.470 79.982  1.00 64.62  ? 335 ASN A N   1 
ATOM 1850 C CA  . ASN A 1 250 ? 117.844 129.872 78.795  1.00 66.03  ? 335 ASN A CA  1 
ATOM 1851 C C   . ASN A 1 250 ? 117.423 130.568 77.507  1.00 68.85  ? 335 ASN A C   1 
ATOM 1852 O O   . ASN A 1 250 ? 118.120 130.435 76.495  1.00 75.85  ? 335 ASN A O   1 
ATOM 1853 C CB  . ASN A 1 250 ? 117.489 128.386 78.724  1.00 63.15  ? 335 ASN A CB  1 
ATOM 1854 C CG  . ASN A 1 250 ? 118.335 127.543 79.659  1.00 64.14  ? 335 ASN A CG  1 
ATOM 1855 O OD1 . ASN A 1 250 ? 119.183 126.768 79.221  1.00 67.89  ? 335 ASN A OD1 1 
ATOM 1856 N ND2 . ASN A 1 250 ? 118.104 127.692 80.958  1.00 61.84  ? 335 ASN A ND2 1 
ATOM 1857 N N   . ARG A 1 251 ? 116.311 131.304 77.513  1.00 69.37  ? 336 ARG A N   1 
ATOM 1858 C CA  . ARG A 1 251 ? 115.852 131.983 76.306  1.00 73.63  ? 336 ARG A CA  1 
ATOM 1859 C C   . ARG A 1 251 ? 116.221 133.463 76.263  1.00 78.74  ? 336 ARG A C   1 
ATOM 1860 O O   . ARG A 1 251 ? 116.796 133.925 75.273  1.00 79.37  ? 336 ARG A O   1 
ATOM 1861 C CB  . ARG A 1 251 ? 114.334 131.825 76.158  1.00 72.38  ? 336 ARG A CB  1 
ATOM 1862 C CG  . ARG A 1 251 ? 113.781 132.441 74.882  1.00 83.16  ? 336 ARG A CG  1 
ATOM 1863 C CD  . ARG A 1 251 ? 112.307 132.127 74.696  1.00 88.99  ? 336 ARG A CD  1 
ATOM 1864 N NE  . ARG A 1 251 ? 111.829 132.546 73.383  1.00 95.00  ? 336 ARG A NE  1 
ATOM 1865 C CZ  . ARG A 1 251 ? 111.916 131.810 72.284  1.00 105.35 ? 336 ARG A CZ  1 
ATOM 1866 N NH1 . ARG A 1 251 ? 112.456 130.602 72.302  1.00 107.08 ? 336 ARG A NH1 1 
ATOM 1867 N NH2 . ARG A 1 251 ? 111.451 132.298 71.138  1.00 108.20 ? 336 ARG A NH2 1 
ATOM 1868 N N   . TYR A 1 252 ? 115.905 134.221 77.315  1.00 75.02  ? 337 TYR A N   1 
ATOM 1869 C CA  . TYR A 1 252 ? 116.019 135.675 77.296  1.00 73.34  ? 337 TYR A CA  1 
ATOM 1870 C C   . TYR A 1 252 ? 117.201 136.195 78.109  1.00 78.64  ? 337 TYR A C   1 
ATOM 1871 O O   . TYR A 1 252 ? 117.175 137.344 78.561  1.00 85.80  ? 337 TYR A O   1 
ATOM 1872 C CB  . TYR A 1 252 ? 114.723 136.312 77.799  1.00 76.75  ? 337 TYR A CB  1 
ATOM 1873 C CG  . TYR A 1 252 ? 113.534 136.093 76.894  1.00 83.79  ? 337 TYR A CG  1 
ATOM 1874 C CD1 . TYR A 1 252 ? 113.462 136.708 75.651  1.00 87.68  ? 337 TYR A CD1 1 
ATOM 1875 C CD2 . TYR A 1 252 ? 112.482 135.276 77.282  1.00 83.92  ? 337 TYR A CD2 1 
ATOM 1876 C CE1 . TYR A 1 252 ? 112.376 136.514 74.820  1.00 91.11  ? 337 TYR A CE1 1 
ATOM 1877 C CE2 . TYR A 1 252 ? 111.391 135.076 76.459  1.00 90.09  ? 337 TYR A CE2 1 
ATOM 1878 C CZ  . TYR A 1 252 ? 111.344 135.697 75.229  1.00 94.10  ? 337 TYR A CZ  1 
ATOM 1879 O OH  . TYR A 1 252 ? 110.260 135.500 74.404  1.00 95.44  ? 337 TYR A OH  1 
ATOM 1880 N N   . VAL A 1 253 ? 118.236 135.380 78.308  1.00 76.60  ? 338 VAL A N   1 
ATOM 1881 C CA  . VAL A 1 253 ? 119.444 135.801 79.004  1.00 77.66  ? 338 VAL A CA  1 
ATOM 1882 C C   . VAL A 1 253 ? 120.648 135.376 78.172  1.00 82.61  ? 338 VAL A C   1 
ATOM 1883 O O   . VAL A 1 253 ? 120.874 134.177 77.984  1.00 82.15  ? 338 VAL A O   1 
ATOM 1884 C CB  . VAL A 1 253 ? 119.543 135.220 80.424  1.00 76.75  ? 338 VAL A CB  1 
ATOM 1885 C CG1 . VAL A 1 253 ? 120.897 135.546 81.036  1.00 78.50  ? 338 VAL A CG1 1 
ATOM 1886 C CG2 . VAL A 1 253 ? 118.419 135.753 81.300  1.00 75.40  ? 338 VAL A CG2 1 
ATOM 1887 N N   . PRO A 1 254 ? 121.442 136.309 77.644  1.00 87.34  ? 339 PRO A N   1 
ATOM 1888 C CA  . PRO A 1 254 ? 122.650 135.926 76.896  1.00 89.60  ? 339 PRO A CA  1 
ATOM 1889 C C   . PRO A 1 254 ? 123.663 135.269 77.821  1.00 91.80  ? 339 PRO A C   1 
ATOM 1890 O O   . PRO A 1 254 ? 124.118 135.871 78.796  1.00 93.31  ? 339 PRO A O   1 
ATOM 1891 C CB  . PRO A 1 254 ? 123.164 137.261 76.342  1.00 87.76  ? 339 PRO A CB  1 
ATOM 1892 C CG  . PRO A 1 254 ? 122.577 138.297 77.245  1.00 89.19  ? 339 PRO A CG  1 
ATOM 1893 C CD  . PRO A 1 254 ? 121.238 137.767 77.661  1.00 84.03  ? 339 PRO A CD  1 
ATOM 1894 N N   . LEU A 1 255 ? 124.014 134.033 77.509  1.00 91.10  ? 340 LEU A N   1 
ATOM 1895 C CA  . LEU A 1 255 ? 124.841 133.276 78.429  1.00 94.51  ? 340 LEU A CA  1 
ATOM 1896 C C   . LEU A 1 255 ? 126.259 133.151 77.886  1.00 101.74 ? 340 LEU A C   1 
ATOM 1897 O O   . LEU A 1 255 ? 126.461 133.138 76.668  1.00 102.44 ? 340 LEU A O   1 
ATOM 1898 C CB  . LEU A 1 255 ? 124.252 131.878 78.640  1.00 92.91  ? 340 LEU A CB  1 
ATOM 1899 C CG  . LEU A 1 255 ? 122.804 131.903 79.141  1.00 91.74  ? 340 LEU A CG  1 
ATOM 1900 C CD1 . LEU A 1 255 ? 122.038 130.647 78.706  1.00 78.72  ? 340 LEU A CD1 1 
ATOM 1901 C CD2 . LEU A 1 255 ? 122.694 132.156 80.641  1.00 82.90  ? 340 LEU A CD2 1 
ATOM 1902 N N   . PRO A 1 256 ? 127.267 133.068 78.753  1.00 104.45 ? 341 PRO A N   1 
ATOM 1903 C CA  . PRO A 1 256 ? 128.635 132.856 78.262  1.00 104.55 ? 341 PRO A CA  1 
ATOM 1904 C C   . PRO A 1 256 ? 128.734 131.519 77.544  1.00 112.83 ? 341 PRO A C   1 
ATOM 1905 O O   . PRO A 1 256 ? 128.342 130.480 78.080  1.00 115.19 ? 341 PRO A O   1 
ATOM 1906 C CB  . PRO A 1 256 ? 129.486 132.884 79.539  1.00 99.15  ? 341 PRO A CB  1 
ATOM 1907 C CG  . PRO A 1 256 ? 128.602 133.468 80.603  1.00 96.00  ? 341 PRO A CG  1 
ATOM 1908 C CD  . PRO A 1 256 ? 127.204 133.115 80.223  1.00 96.75  ? 341 PRO A CD  1 
ATOM 1909 N N   . THR A 1 257 ? 129.260 131.546 76.319  1.00 117.01 ? 342 THR A N   1 
ATOM 1910 C CA  . THR A 1 257 ? 129.164 130.351 75.491  1.00 124.77 ? 342 THR A CA  1 
ATOM 1911 C C   . THR A 1 257 ? 130.131 129.261 75.950  1.00 129.91 ? 342 THR A C   1 
ATOM 1912 O O   . THR A 1 257 ? 129.670 128.226 76.430  1.00 125.96 ? 342 THR A O   1 
ATOM 1913 C CB  . THR A 1 257 ? 129.364 130.722 74.011  1.00 127.07 ? 342 THR A CB  1 
ATOM 1914 O OG1 . THR A 1 257 ? 129.371 129.540 73.199  1.00 130.24 ? 342 THR A OG1 1 
ATOM 1915 C CG2 . THR A 1 257 ? 130.625 131.569 73.775  1.00 123.62 ? 342 THR A CG2 1 
ATOM 1916 N N   . ARG A 1 258 ? 131.445 129.466 75.765  1.00 132.62 ? 343 ARG A N   1 
ATOM 1917 C CA  . ARG A 1 258 ? 132.587 128.906 76.497  1.00 130.31 ? 343 ARG A CA  1 
ATOM 1918 C C   . ARG A 1 258 ? 133.870 129.400 75.840  1.00 131.80 ? 343 ARG A C   1 
ATOM 1919 O O   . ARG A 1 258 ? 133.822 130.146 74.856  1.00 129.40 ? 343 ARG A O   1 
ATOM 1920 C CB  . ARG A 1 258 ? 132.632 127.370 76.570  1.00 129.43 ? 343 ARG A CB  1 
ATOM 1921 C CG  . ARG A 1 258 ? 131.698 126.699 77.568  1.00 121.61 ? 343 ARG A CG  1 
ATOM 1922 C CD  . ARG A 1 258 ? 131.920 127.210 78.983  1.00 118.55 ? 343 ARG A CD  1 
ATOM 1923 N NE  . ARG A 1 258 ? 133.218 126.834 79.529  1.00 113.64 ? 343 ARG A NE  1 
ATOM 1924 C CZ  . ARG A 1 258 ? 133.774 127.407 80.588  1.00 107.64 ? 343 ARG A CZ  1 
ATOM 1925 N NH1 . ARG A 1 258 ? 133.171 128.389 81.238  1.00 109.27 ? 343 ARG A NH1 1 
ATOM 1926 N NH2 . ARG A 1 258 ? 134.962 126.982 81.006  1.00 100.99 ? 343 ARG A NH2 1 
ATOM 1927 N N   . SER A 1 259 ? 135.018 128.994 76.374  1.00 135.64 ? 344 SER A N   1 
ATOM 1928 C CA  . SER A 1 259 ? 136.241 128.992 75.587  1.00 139.09 ? 344 SER A CA  1 
ATOM 1929 C C   . SER A 1 259 ? 136.201 127.825 74.607  1.00 141.64 ? 344 SER A C   1 
ATOM 1930 O O   . SER A 1 259 ? 135.579 126.792 74.870  1.00 143.21 ? 344 SER A O   1 
ATOM 1931 C CB  . SER A 1 259 ? 137.471 128.889 76.490  1.00 139.78 ? 344 SER A CB  1 
ATOM 1932 O OG  . SER A 1 259 ? 137.531 127.625 77.129  1.00 139.79 ? 344 SER A OG  1 
ATOM 1933 N N   . LYS A 1 260 ? 136.874 127.988 73.467  1.00 142.34 ? 345 LYS A N   1 
ATOM 1934 C CA  . LYS A 1 260 ? 136.725 127.027 72.378  1.00 142.21 ? 345 LYS A CA  1 
ATOM 1935 C C   . LYS A 1 260 ? 137.481 125.718 72.631  1.00 142.20 ? 345 LYS A C   1 
ATOM 1936 O O   . LYS A 1 260 ? 137.579 124.880 71.728  1.00 142.66 ? 345 LYS A O   1 
ATOM 1937 C CB  . LYS A 1 260 ? 137.163 127.661 71.051  1.00 141.78 ? 345 LYS A CB  1 
ATOM 1938 C CG  . LYS A 1 260 ? 136.618 126.949 69.811  1.00 140.74 ? 345 LYS A CG  1 
ATOM 1939 C CD  . LYS A 1 260 ? 136.934 127.697 68.528  1.00 136.47 ? 345 LYS A CD  1 
ATOM 1940 C CE  . LYS A 1 260 ? 138.389 127.527 68.135  1.00 134.85 ? 345 LYS A CE  1 
ATOM 1941 N NZ  . LYS A 1 260 ? 138.675 126.129 67.706  1.00 134.08 ? 345 LYS A NZ  1 
ATOM 1942 N N   . ASN A 1 261 ? 138.005 125.514 73.842  1.00 141.83 ? 346 ASN A N   1 
ATOM 1943 C CA  . ASN A 1 261 ? 138.467 124.196 74.263  1.00 144.57 ? 346 ASN A CA  1 
ATOM 1944 C C   . ASN A 1 261 ? 137.294 123.256 74.538  1.00 148.66 ? 346 ASN A C   1 
ATOM 1945 O O   . ASN A 1 261 ? 137.501 122.069 74.813  1.00 146.99 ? 346 ASN A O   1 
ATOM 1946 C CB  . ASN A 1 261 ? 139.379 124.358 75.491  1.00 140.39 ? 346 ASN A CB  1 
ATOM 1947 C CG  . ASN A 1 261 ? 139.885 123.035 76.050  1.00 137.67 ? 346 ASN A CG  1 
ATOM 1948 O OD1 . ASN A 1 261 ? 139.180 122.340 76.784  1.00 134.33 ? 346 ASN A OD1 1 
ATOM 1949 N ND2 . ASN A 1 261 ? 141.115 122.680 75.698  1.00 135.89 ? 346 ASN A ND2 1 
ATOM 1950 N N   . LYS A 1 262 ? 136.068 123.766 74.390  1.00 149.43 ? 347 LYS A N   1 
ATOM 1951 C CA  . LYS A 1 262 ? 134.844 123.030 74.687  1.00 147.83 ? 347 LYS A CA  1 
ATOM 1952 C C   . LYS A 1 262 ? 134.764 121.689 73.968  1.00 150.43 ? 347 LYS A C   1 
ATOM 1953 O O   . LYS A 1 262 ? 134.097 120.772 74.461  1.00 149.17 ? 347 LYS A O   1 
ATOM 1954 C CB  . LYS A 1 262 ? 133.644 123.893 74.291  1.00 143.63 ? 347 LYS A CB  1 
ATOM 1955 C CG  . LYS A 1 262 ? 133.753 124.429 72.865  1.00 142.71 ? 347 LYS A CG  1 
ATOM 1956 C CD  . LYS A 1 262 ? 132.612 125.361 72.491  1.00 139.70 ? 347 LYS A CD  1 
ATOM 1957 C CE  . LYS A 1 262 ? 132.795 126.732 73.117  1.00 135.52 ? 347 LYS A CE  1 
ATOM 1958 N NZ  . LYS A 1 262 ? 131.963 127.773 72.454  1.00 129.19 ? 347 LYS A NZ  1 
ATOM 1959 N N   . LYS A 1 263 ? 135.413 121.554 72.815  1.00 150.86 ? 348 LYS A N   1 
ATOM 1960 C CA  . LYS A 1 263 ? 135.328 120.331 72.027  1.00 149.13 ? 348 LYS A CA  1 
ATOM 1961 C C   . LYS A 1 263 ? 136.188 119.244 72.660  1.00 147.43 ? 348 LYS A C   1 
ATOM 1962 O O   . LYS A 1 263 ? 137.380 119.451 72.910  1.00 145.38 ? 348 LYS A O   1 
ATOM 1963 C CB  . LYS A 1 263 ? 135.771 120.592 70.590  1.00 146.20 ? 348 LYS A CB  1 
ATOM 1964 C CG  . LYS A 1 263 ? 134.906 121.590 69.843  1.00 144.14 ? 348 LYS A CG  1 
ATOM 1965 C CD  . LYS A 1 263 ? 135.324 121.685 68.386  1.00 140.51 ? 348 LYS A CD  1 
ATOM 1966 C CE  . LYS A 1 263 ? 136.685 122.348 68.246  1.00 135.87 ? 348 LYS A CE  1 
ATOM 1967 N NZ  . LYS A 1 263 ? 136.657 123.777 68.659  1.00 137.23 ? 348 LYS A NZ  1 
ATOM 1968 N N   . GLU A 1 264 ? 135.583 118.086 72.912  1.00 146.49 ? 349 GLU A N   1 
ATOM 1969 C CA  . GLU A 1 264 ? 136.306 116.930 73.421  1.00 144.92 ? 349 GLU A CA  1 
ATOM 1970 C C   . GLU A 1 264 ? 135.501 115.680 73.104  1.00 143.37 ? 349 GLU A C   1 
ATOM 1971 O O   . GLU A 1 264 ? 134.268 115.719 73.094  1.00 142.36 ? 349 GLU A O   1 
ATOM 1972 C CB  . GLU A 1 264 ? 136.563 117.042 74.931  1.00 141.94 ? 349 GLU A CB  1 
ATOM 1973 C CG  . GLU A 1 264 ? 137.359 115.883 75.519  1.00 139.42 ? 349 GLU A CG  1 
ATOM 1974 C CD  . GLU A 1 264 ? 138.763 115.781 74.949  1.00 140.57 ? 349 GLU A CD  1 
ATOM 1975 O OE1 . GLU A 1 264 ? 139.319 116.820 74.533  1.00 138.73 ? 349 GLU A OE1 1 
ATOM 1976 O OE2 . GLU A 1 264 ? 139.310 114.659 74.914  1.00 141.00 ? 349 GLU A OE2 1 
ATOM 1977 N N   . LYS A 1 265 ? 136.208 114.586 72.835  1.00 143.73 ? 350 LYS A N   1 
ATOM 1978 C CA  . LYS A 1 265 ? 135.593 113.306 72.526  1.00 143.66 ? 350 LYS A CA  1 
ATOM 1979 C C   . LYS A 1 265 ? 134.606 112.913 73.624  1.00 144.23 ? 350 LYS A C   1 
ATOM 1980 O O   . LYS A 1 265 ? 135.016 112.736 74.782  1.00 143.84 ? 350 LYS A O   1 
ATOM 1981 C CB  . LYS A 1 265 ? 136.677 112.239 72.370  1.00 142.06 ? 350 LYS A CB  1 
ATOM 1982 C CG  . LYS A 1 265 ? 136.178 110.824 72.095  1.00 138.12 ? 350 LYS A CG  1 
ATOM 1983 C CD  . LYS A 1 265 ? 136.102 109.996 73.374  1.00 137.34 ? 350 LYS A CD  1 
ATOM 1984 C CE  . LYS A 1 265 ? 137.490 109.719 73.933  1.00 134.97 ? 350 LYS A CE  1 
ATOM 1985 N NZ  . LYS A 1 265 ? 137.441 108.932 75.196  1.00 129.46 ? 350 LYS A NZ  1 
ATOM 1986 N N   . PRO A 1 266 ? 133.313 112.782 73.313  1.00 144.43 ? 351 PRO A N   1 
ATOM 1987 C CA  . PRO A 1 266 ? 132.355 112.323 74.327  1.00 141.83 ? 351 PRO A CA  1 
ATOM 1988 C C   . PRO A 1 266 ? 132.676 110.911 74.783  1.00 138.75 ? 351 PRO A C   1 
ATOM 1989 O O   . PRO A 1 266 ? 132.645 109.972 73.982  1.00 137.38 ? 351 PRO A O   1 
ATOM 1990 C CB  . PRO A 1 266 ? 131.006 112.393 73.600  1.00 137.38 ? 351 PRO A CB  1 
ATOM 1991 C CG  . PRO A 1 266 ? 131.235 113.317 72.443  1.00 137.61 ? 351 PRO A CG  1 
ATOM 1992 C CD  . PRO A 1 266 ? 132.656 113.101 72.035  1.00 141.71 ? 351 PRO A CD  1 
ATOM 1993 N N   . LYS A 1 267 ? 132.995 110.757 76.069  1.00 135.10 ? 352 LYS A N   1 
ATOM 1994 C CA  . LYS A 1 267 ? 133.421 109.461 76.582  1.00 132.93 ? 352 LYS A CA  1 
ATOM 1995 C C   . LYS A 1 267 ? 132.328 108.414 76.400  1.00 133.88 ? 352 LYS A C   1 
ATOM 1996 O O   . LYS A 1 267 ? 132.534 107.391 75.736  1.00 134.76 ? 352 LYS A O   1 
ATOM 1997 C CB  . LYS A 1 267 ? 133.815 109.590 78.055  1.00 124.49 ? 352 LYS A CB  1 
ATOM 1998 C CG  . LYS A 1 267 ? 135.046 110.455 78.293  1.00 120.99 ? 352 LYS A CG  1 
ATOM 1999 C CD  . LYS A 1 267 ? 135.413 110.512 79.767  1.00 115.54 ? 352 LYS A CD  1 
ATOM 2000 C CE  . LYS A 1 267 ? 136.591 111.442 80.010  1.00 110.26 ? 352 LYS A CE  1 
ATOM 2001 N NZ  . LYS A 1 267 ? 137.854 110.909 79.427  1.00 112.22 ? 352 LYS A NZ  1 
ATOM 2002 N N   . MET A 1 268 ? 131.159 108.650 77.002  1.00 133.30 ? 353 MET A N   1 
ATOM 2003 C CA  . MET A 1 268 ? 130.017 107.738 76.944  1.00 131.17 ? 353 MET A CA  1 
ATOM 2004 C C   . MET A 1 268 ? 130.347 106.378 77.546  1.00 132.03 ? 353 MET A C   1 
ATOM 2005 O O   . MET A 1 268 ? 129.529 105.454 77.495  1.00 130.56 ? 353 MET A O   1 
ATOM 2006 C CB  . MET A 1 268 ? 129.501 107.584 75.510  1.00 131.62 ? 353 MET A CB  1 
ATOM 2007 C CG  . MET A 1 268 ? 129.325 108.898 74.769  1.00 131.83 ? 353 MET A CG  1 
ATOM 2008 S SD  . MET A 1 268 ? 128.242 108.721 73.339  1.00 146.22 ? 353 MET A SD  1 
ATOM 2009 C CE  . MET A 1 268 ? 128.072 110.427 72.824  1.00 127.06 ? 353 MET A CE  1 
ATOM 2010 N N   . GLY A 1 269 ? 131.538 106.248 78.118  1.00 129.20 ? 354 GLY A N   1 
ATOM 2011 C CA  . GLY A 1 269 ? 131.898 105.055 78.848  1.00 123.37 ? 354 GLY A CA  1 
ATOM 2012 C C   . GLY A 1 269 ? 131.689 105.257 80.331  1.00 120.57 ? 354 GLY A C   1 
ATOM 2013 O O   . GLY A 1 269 ? 132.487 105.932 80.989  1.00 120.88 ? 354 GLY A O   1 
ATOM 2014 N N   . THR A 1 270 ? 130.613 104.681 80.872  1.00 119.49 ? 355 THR A N   1 
ATOM 2015 C CA  . THR A 1 270 ? 130.361 104.780 82.303  1.00 120.27 ? 355 THR A CA  1 
ATOM 2016 C C   . THR A 1 270 ? 131.457 104.113 83.121  1.00 118.02 ? 355 THR A C   1 
ATOM 2017 O O   . THR A 1 270 ? 131.528 104.335 84.334  1.00 119.05 ? 355 THR A O   1 
ATOM 2018 C CB  . THR A 1 270 ? 128.997 104.175 82.642  1.00 120.44 ? 355 THR A CB  1 
ATOM 2019 O OG1 . THR A 1 270 ? 129.093 102.746 82.665  1.00 126.34 ? 355 THR A OG1 1 
ATOM 2020 C CG2 . THR A 1 270 ? 127.957 104.598 81.612  1.00 111.50 ? 355 THR A CG2 1 
ATOM 2021 N N   . MET A 1 271 ? 132.293 103.290 82.492  1.00 115.91 ? 356 MET A N   1 
ATOM 2022 C CA  . MET A 1 271 ? 133.558 102.868 83.076  1.00 117.34 ? 356 MET A CA  1 
ATOM 2023 C C   . MET A 1 271 ? 134.673 103.861 82.770  1.00 117.32 ? 356 MET A C   1 
ATOM 2024 O O   . MET A 1 271 ? 135.484 104.170 83.649  1.00 115.45 ? 356 MET A O   1 
ATOM 2025 C CB  . MET A 1 271 ? 133.924 101.469 82.565  1.00 122.49 ? 356 MET A CB  1 
ATOM 2026 C CG  . MET A 1 271 ? 135.201 100.863 83.144  1.00 125.99 ? 356 MET A CG  1 
ATOM 2027 S SD  . MET A 1 271 ? 136.727 101.424 82.358  1.00 131.25 ? 356 MET A SD  1 
ATOM 2028 C CE  . MET A 1 271 ? 136.626 100.579 80.781  1.00 115.09 ? 356 MET A CE  1 
ATOM 2029 N N   . GLU A 1 272 ? 134.724 104.370 81.536  1.00 118.30 ? 357 GLU A N   1 
ATOM 2030 C CA  . GLU A 1 272 ? 135.775 105.308 81.152  1.00 112.99 ? 357 GLU A CA  1 
ATOM 2031 C C   . GLU A 1 272 ? 135.629 106.637 81.885  1.00 109.51 ? 357 GLU A C   1 
ATOM 2032 O O   . GLU A 1 272 ? 136.613 107.189 82.393  1.00 108.34 ? 357 GLU A O   1 
ATOM 2033 C CB  . GLU A 1 272 ? 135.754 105.525 79.638  1.00 113.78 ? 357 GLU A CB  1 
ATOM 2034 C CG  . GLU A 1 272 ? 136.833 106.467 79.126  1.00 119.40 ? 357 GLU A CG  1 
ATOM 2035 C CD  . GLU A 1 272 ? 136.806 106.619 77.617  1.00 122.87 ? 357 GLU A CD  1 
ATOM 2036 O OE1 . GLU A 1 272 ? 135.940 105.993 76.970  1.00 122.85 ? 357 GLU A OE1 1 
ATOM 2037 O OE2 . GLU A 1 272 ? 137.649 107.366 77.078  1.00 123.97 ? 357 GLU A OE2 1 
ATOM 2038 N N   . SER A 1 273 ? 134.406 107.171 81.943  1.00 112.45 ? 358 SER A N   1 
ATOM 2039 C CA  . SER A 1 273 ? 134.188 108.445 82.620  1.00 105.77 ? 358 SER A CA  1 
ATOM 2040 C C   . SER A 1 273 ? 134.519 108.344 84.103  1.00 99.06  ? 358 SER A C   1 
ATOM 2041 O O   . SER A 1 273 ? 135.198 109.216 84.657  1.00 97.60  ? 358 SER A O   1 
ATOM 2042 C CB  . SER A 1 273 ? 132.744 108.906 82.423  1.00 104.40 ? 358 SER A CB  1 
ATOM 2043 O OG  . SER A 1 273 ? 132.409 108.968 81.048  1.00 111.21 ? 358 SER A OG  1 
ATOM 2044 N N   . LEU A 1 274 ? 134.061 107.277 84.760  1.00 98.13  ? 359 LEU A N   1 
ATOM 2045 C CA  . LEU A 1 274 ? 134.377 107.095 86.172  1.00 96.28  ? 359 LEU A CA  1 
ATOM 2046 C C   . LEU A 1 274 ? 135.869 106.872 86.384  1.00 99.58  ? 359 LEU A C   1 
ATOM 2047 O O   . LEU A 1 274 ? 136.433 107.345 87.377  1.00 104.73 ? 359 LEU A O   1 
ATOM 2048 C CB  . LEU A 1 274 ? 133.561 105.940 86.752  1.00 97.68  ? 359 LEU A CB  1 
ATOM 2049 C CG  . LEU A 1 274 ? 132.197 106.326 87.338  1.00 96.83  ? 359 LEU A CG  1 
ATOM 2050 C CD1 . LEU A 1 274 ? 131.210 106.762 86.264  1.00 97.12  ? 359 LEU A CD1 1 
ATOM 2051 C CD2 . LEU A 1 274 ? 131.627 105.174 88.152  1.00 98.04  ? 359 LEU A CD2 1 
ATOM 2052 N N   . LYS A 1 275 ? 136.529 106.161 85.466  1.00 98.91  ? 360 LYS A N   1 
ATOM 2053 C CA  . LYS A 1 275 ? 137.973 105.982 85.586  1.00 97.79  ? 360 LYS A CA  1 
ATOM 2054 C C   . LYS A 1 275 ? 138.700 107.318 85.486  1.00 96.79  ? 360 LYS A C   1 
ATOM 2055 O O   . LYS A 1 275 ? 139.679 107.556 86.204  1.00 94.57  ? 360 LYS A O   1 
ATOM 2056 C CB  . LYS A 1 275 ? 138.482 105.010 84.520  1.00 99.77  ? 360 LYS A CB  1 
ATOM 2057 C CG  . LYS A 1 275 ? 139.974 104.726 84.616  1.00 101.44 ? 360 LYS A CG  1 
ATOM 2058 C CD  . LYS A 1 275 ? 140.414 103.673 83.612  1.00 102.10 ? 360 LYS A CD  1 
ATOM 2059 C CE  . LYS A 1 275 ? 141.926 103.509 83.617  1.00 104.94 ? 360 LYS A CE  1 
ATOM 2060 N NZ  . LYS A 1 275 ? 142.421 102.956 84.909  1.00 99.24  ? 360 LYS A NZ  1 
ATOM 2061 N N   . PHE A 1 276 ? 138.240 108.201 84.596  1.00 99.03  ? 361 PHE A N   1 
ATOM 2062 C CA  . PHE A 1 276 ? 138.818 109.539 84.521  1.00 95.28  ? 361 PHE A CA  1 
ATOM 2063 C C   . PHE A 1 276 ? 138.562 110.330 85.799  1.00 88.90  ? 361 PHE A C   1 
ATOM 2064 O O   . PHE A 1 276 ? 139.454 111.031 86.292  1.00 90.37  ? 361 PHE A O   1 
ATOM 2065 C CB  . PHE A 1 276 ? 138.261 110.288 83.310  1.00 98.04  ? 361 PHE A CB  1 
ATOM 2066 C CG  . PHE A 1 276 ? 138.836 111.665 83.134  1.00 98.37  ? 361 PHE A CG  1 
ATOM 2067 C CD1 . PHE A 1 276 ? 140.114 111.839 82.631  1.00 102.55 ? 361 PHE A CD1 1 
ATOM 2068 C CD2 . PHE A 1 276 ? 138.097 112.787 83.474  1.00 95.42  ? 361 PHE A CD2 1 
ATOM 2069 C CE1 . PHE A 1 276 ? 140.645 113.106 82.469  1.00 103.16 ? 361 PHE A CE1 1 
ATOM 2070 C CE2 . PHE A 1 276 ? 138.621 114.055 83.315  1.00 94.21  ? 361 PHE A CE2 1 
ATOM 2071 C CZ  . PHE A 1 276 ? 139.897 114.215 82.812  1.00 99.17  ? 361 PHE A CZ  1 
ATOM 2072 N N   . LEU A 1 277 ? 137.346 110.237 86.345  1.00 89.36  ? 362 LEU A N   1 
ATOM 2073 C CA  . LEU A 1 277 ? 137.015 110.991 87.552  1.00 85.99  ? 362 LEU A CA  1 
ATOM 2074 C C   . LEU A 1 277 ? 137.831 110.527 88.755  1.00 85.91  ? 362 LEU A C   1 
ATOM 2075 O O   . LEU A 1 277 ? 138.279 111.354 89.559  1.00 87.11  ? 362 LEU A O   1 
ATOM 2076 C CB  . LEU A 1 277 ? 135.516 110.898 87.841  1.00 84.39  ? 362 LEU A CB  1 
ATOM 2077 C CG  . LEU A 1 277 ? 134.643 112.019 87.262  1.00 81.37  ? 362 LEU A CG  1 
ATOM 2078 C CD1 . LEU A 1 277 ? 134.601 112.009 85.745  1.00 84.58  ? 362 LEU A CD1 1 
ATOM 2079 C CD2 . LEU A 1 277 ? 133.237 111.923 87.824  1.00 71.87  ? 362 LEU A CD2 1 
ATOM 2080 N N   . VAL A 1 278 ? 138.032 109.216 88.905  1.00 89.33  ? 363 VAL A N   1 
ATOM 2081 C CA  . VAL A 1 278 ? 138.858 108.728 90.008  1.00 86.47  ? 363 VAL A CA  1 
ATOM 2082 C C   . VAL A 1 278 ? 140.316 109.130 89.812  1.00 87.88  ? 363 VAL A C   1 
ATOM 2083 O O   . VAL A 1 278 ? 141.039 109.364 90.788  1.00 90.10  ? 363 VAL A O   1 
ATOM 2084 C CB  . VAL A 1 278 ? 138.705 107.202 90.169  1.00 84.54  ? 363 VAL A CB  1 
ATOM 2085 C CG1 . VAL A 1 278 ? 139.459 106.719 91.398  1.00 86.66  ? 363 VAL A CG1 1 
ATOM 2086 C CG2 . VAL A 1 278 ? 137.239 106.831 90.299  1.00 88.00  ? 363 VAL A CG2 1 
ATOM 2087 N N   . SER A 1 279 ? 140.770 109.229 88.565  1.00 87.19  ? 364 SER A N   1 
ATOM 2088 C CA  . SER A 1 279 ? 142.146 109.603 88.268  1.00 87.67  ? 364 SER A CA  1 
ATOM 2089 C C   . SER A 1 279 ? 142.350 111.110 88.169  1.00 86.28  ? 364 SER A C   1 
ATOM 2090 O O   . SER A 1 279 ? 143.476 111.552 87.920  1.00 83.27  ? 364 SER A O   1 
ATOM 2091 C CB  . SER A 1 279 ? 142.604 108.939 86.965  1.00 92.89  ? 364 SER A CB  1 
ATOM 2092 O OG  . SER A 1 279 ? 143.928 109.320 86.636  1.00 100.79 ? 364 SER A OG  1 
ATOM 2093 N N   . SER A 1 280 ? 141.297 111.908 88.355  1.00 88.96  ? 365 SER A N   1 
ATOM 2094 C CA  . SER A 1 280 ? 141.425 113.360 88.262  1.00 81.48  ? 365 SER A CA  1 
ATOM 2095 C C   . SER A 1 280 ? 141.843 113.937 89.609  1.00 75.67  ? 365 SER A C   1 
ATOM 2096 O O   . SER A 1 280 ? 141.160 113.704 90.613  1.00 75.73  ? 365 SER A O   1 
ATOM 2097 C CB  . SER A 1 280 ? 140.114 113.992 87.816  1.00 83.01  ? 365 SER A CB  1 
ATOM 2098 O OG  . SER A 1 280 ? 140.221 115.404 87.758  1.00 80.88  ? 365 SER A OG  1 
ATOM 2099 N N   . PRO A 1 281 ? 142.947 114.688 89.673  1.00 73.64  ? 366 PRO A N   1 
ATOM 2100 C CA  . PRO A 1 281 ? 143.370 115.274 90.955  1.00 69.38  ? 366 PRO A CA  1 
ATOM 2101 C C   . PRO A 1 281 ? 142.438 116.358 91.474  1.00 69.70  ? 366 PRO A C   1 
ATOM 2102 O O   . PRO A 1 281 ? 142.505 116.683 92.666  1.00 72.30  ? 366 PRO A O   1 
ATOM 2103 C CB  . PRO A 1 281 ? 144.757 115.840 90.633  1.00 65.59  ? 366 PRO A CB  1 
ATOM 2104 C CG  . PRO A 1 281 ? 144.667 116.201 89.187  1.00 70.72  ? 366 PRO A CG  1 
ATOM 2105 C CD  . PRO A 1 281 ? 143.795 115.139 88.555  1.00 75.03  ? 366 PRO A CD  1 
ATOM 2106 N N   . TYR A 1 282 ? 141.581 116.922 90.626  1.00 70.01  ? 367 TYR A N   1 
ATOM 2107 C CA  . TYR A 1 282 ? 140.648 117.972 91.019  1.00 66.49  ? 367 TYR A CA  1 
ATOM 2108 C C   . TYR A 1 282 ? 139.424 117.404 91.728  1.00 65.03  ? 367 TYR A C   1 
ATOM 2109 O O   . TYR A 1 282 ? 139.051 117.875 92.816  1.00 66.88  ? 367 TYR A O   1 
ATOM 2110 C CB  . TYR A 1 282 ? 140.232 118.761 89.774  1.00 64.55  ? 367 TYR A CB  1 
ATOM 2111 C CG  . TYR A 1 282 ? 139.779 120.178 90.029  1.00 64.04  ? 367 TYR A CG  1 
ATOM 2112 C CD1 . TYR A 1 282 ? 140.691 121.224 90.030  1.00 62.08  ? 367 TYR A CD1 1 
ATOM 2113 C CD2 . TYR A 1 282 ? 138.439 120.477 90.226  1.00 66.93  ? 367 TYR A CD2 1 
ATOM 2114 C CE1 . TYR A 1 282 ? 140.286 122.524 90.253  1.00 62.02  ? 367 TYR A CE1 1 
ATOM 2115 C CE2 . TYR A 1 282 ? 138.023 121.775 90.444  1.00 61.83  ? 367 TYR A CE2 1 
ATOM 2116 C CZ  . TYR A 1 282 ? 138.951 122.795 90.454  1.00 60.89  ? 367 TYR A CZ  1 
ATOM 2117 O OH  . TYR A 1 282 ? 138.545 124.091 90.671  1.00 64.31  ? 367 TYR A OH  1 
ATOM 2118 N N   . ILE A 1 283 ? 138.805 116.385 91.129  1.00 64.53  ? 368 ILE A N   1 
ATOM 2119 C CA  . ILE A 1 283 ? 137.681 115.709 91.760  1.00 60.30  ? 368 ILE A CA  1 
ATOM 2120 C C   . ILE A 1 283 ? 138.107 115.055 93.066  1.00 64.24  ? 368 ILE A C   1 
ATOM 2121 O O   . ILE A 1 283 ? 137.316 114.993 94.011  1.00 69.75  ? 368 ILE A O   1 
ATOM 2122 C CB  . ILE A 1 283 ? 137.064 114.683 90.792  1.00 63.35  ? 368 ILE A CB  1 
ATOM 2123 C CG1 . ILE A 1 283 ? 136.849 115.312 89.414  1.00 66.75  ? 368 ILE A CG1 1 
ATOM 2124 C CG2 . ILE A 1 283 ? 135.753 114.143 91.342  1.00 61.12  ? 368 ILE A CG2 1 
ATOM 2125 C CD1 . ILE A 1 283 ? 135.898 116.491 89.423  1.00 62.17  ? 368 ILE A CD1 1 
ATOM 2126 N N   . ARG A 1 284 ? 139.348 114.570 93.153  1.00 64.44  ? 369 ARG A N   1 
ATOM 2127 C CA  . ARG A 1 284 ? 139.821 113.975 94.399  1.00 62.98  ? 369 ARG A CA  1 
ATOM 2128 C C   . ARG A 1 284 ? 139.782 114.984 95.540  1.00 62.97  ? 369 ARG A C   1 
ATOM 2129 O O   . ARG A 1 284 ? 139.221 114.709 96.607  1.00 63.88  ? 369 ARG A O   1 
ATOM 2130 C CB  . ARG A 1 284 ? 141.237 113.423 94.219  1.00 64.62  ? 369 ARG A CB  1 
ATOM 2131 C CG  . ARG A 1 284 ? 141.291 111.939 93.897  1.00 76.71  ? 369 ARG A CG  1 
ATOM 2132 C CD  . ARG A 1 284 ? 142.709 111.400 94.014  1.00 80.78  ? 369 ARG A CD  1 
ATOM 2133 N NE  . ARG A 1 284 ? 143.487 111.614 92.800  1.00 90.02  ? 369 ARG A NE  1 
ATOM 2134 C CZ  . ARG A 1 284 ? 144.587 110.942 92.489  1.00 98.44  ? 369 ARG A CZ  1 
ATOM 2135 N NH1 . ARG A 1 284 ? 145.071 110.002 93.284  1.00 104.66 ? 369 ARG A NH1 1 
ATOM 2136 N NH2 . ARG A 1 284 ? 145.218 111.220 91.351  1.00 95.43  ? 369 ARG A NH2 1 
ATOM 2137 N N   . ASP A 1 285 ? 140.361 116.169 95.328  1.00 61.53  ? 370 ASP A N   1 
ATOM 2138 C CA  . ASP A 1 285 ? 140.362 117.185 96.377  1.00 53.45  ? 370 ASP A CA  1 
ATOM 2139 C C   . ASP A 1 285 ? 138.951 117.669 96.691  1.00 56.83  ? 370 ASP A C   1 
ATOM 2140 O O   . ASP A 1 285 ? 138.609 117.878 97.860  1.00 62.03  ? 370 ASP A O   1 
ATOM 2141 C CB  . ASP A 1 285 ? 141.257 118.360 95.981  1.00 57.44  ? 370 ASP A CB  1 
ATOM 2142 C CG  . ASP A 1 285 ? 142.608 117.915 95.455  1.00 70.81  ? 370 ASP A CG  1 
ATOM 2143 O OD1 . ASP A 1 285 ? 143.109 116.866 95.911  1.00 73.21  ? 370 ASP A OD1 1 
ATOM 2144 O OD2 . ASP A 1 285 ? 143.174 118.621 94.594  1.00 74.54  ? 370 ASP A OD2 1 
ATOM 2145 N N   . LEU A 1 286 ? 138.118 117.863 95.665  1.00 56.25  ? 371 LEU A N   1 
ATOM 2146 C CA  . LEU A 1 286 ? 136.762 118.347 95.915  1.00 53.37  ? 371 LEU A CA  1 
ATOM 2147 C C   . LEU A 1 286 ? 135.941 117.329 96.708  1.00 54.38  ? 371 LEU A C   1 
ATOM 2148 O O   . LEU A 1 286 ? 135.233 117.689 97.665  1.00 61.75  ? 371 LEU A O   1 
ATOM 2149 C CB  . LEU A 1 286 ? 136.101 118.688 94.581  1.00 54.45  ? 371 LEU A CB  1 
ATOM 2150 C CG  . LEU A 1 286 ? 134.873 119.591 94.541  1.00 57.37  ? 371 LEU A CG  1 
ATOM 2151 C CD1 . LEU A 1 286 ? 135.108 120.868 95.316  1.00 58.01  ? 371 LEU A CD1 1 
ATOM 2152 C CD2 . LEU A 1 286 ? 134.610 119.922 93.093  1.00 56.93  ? 371 LEU A CD2 1 
ATOM 2153 N N   . ALA A 1 287 ? 136.042 116.049 96.341  1.00 53.66  ? 372 ALA A N   1 
ATOM 2154 C CA  . ALA A 1 287 ? 135.391 114.996 97.106  1.00 52.61  ? 372 ALA A CA  1 
ATOM 2155 C C   . ALA A 1 287 ? 135.951 114.908 98.516  1.00 55.35  ? 372 ALA A C   1 
ATOM 2156 O O   . ALA A 1 287 ? 135.210 114.604 99.456  1.00 58.58  ? 372 ALA A O   1 
ATOM 2157 C CB  . ALA A 1 287 ? 135.547 113.656 96.388  1.00 57.41  ? 372 ALA A CB  1 
ATOM 2158 N N   . THR A 1 288 ? 137.252 115.159 98.684  1.00 55.96  ? 373 THR A N   1 
ATOM 2159 C CA  . THR A 1 288 ? 137.825 115.184 100.024 1.00 48.24  ? 373 THR A CA  1 
ATOM 2160 C C   . THR A 1 288 ? 137.202 116.290 100.864 1.00 50.94  ? 373 THR A C   1 
ATOM 2161 O O   . THR A 1 288 ? 136.863 116.073 102.031 1.00 58.77  ? 373 THR A O   1 
ATOM 2162 C CB  . THR A 1 288 ? 139.342 115.355 99.951  1.00 46.78  ? 373 THR A CB  1 
ATOM 2163 O OG1 . THR A 1 288 ? 139.896 114.362 99.080  1.00 58.62  ? 373 THR A OG1 1 
ATOM 2164 C CG2 . THR A 1 288 ? 139.960 115.209 101.335 1.00 53.03  ? 373 THR A CG2 1 
ATOM 2165 N N   . LEU A 1 289 ? 137.032 117.481 100.282 1.00 54.50  ? 374 LEU A N   1 
ATOM 2166 C CA  . LEU A 1 289 ? 136.346 118.558 100.995 1.00 51.30  ? 374 LEU A CA  1 
ATOM 2167 C C   . LEU A 1 289 ? 134.951 118.129 101.433 1.00 54.62  ? 374 LEU A C   1 
ATOM 2168 O O   . LEU A 1 289 ? 134.585 118.274 102.606 1.00 61.58  ? 374 LEU A O   1 
ATOM 2169 C CB  . LEU A 1 289 ? 136.264 119.822 100.133 1.00 48.60  ? 374 LEU A CB  1 
ATOM 2170 C CG  . LEU A 1 289 ? 137.374 120.878 100.202 1.00 49.92  ? 374 LEU A CG  1 
ATOM 2171 C CD1 . LEU A 1 289 ? 138.665 120.423 99.558  1.00 55.15  ? 374 LEU A CD1 1 
ATOM 2172 C CD2 . LEU A 1 289 ? 136.895 122.182 99.575  1.00 54.28  ? 374 LEU A CD2 1 
ATOM 2173 N N   . VAL A 1 290 ? 134.162 117.585 100.503 1.00 54.28  ? 375 VAL A N   1 
ATOM 2174 C CA  . VAL A 1 290 ? 132.778 117.228 100.830 1.00 52.31  ? 375 VAL A CA  1 
ATOM 2175 C C   . VAL A 1 290 ? 132.739 116.155 101.918 1.00 55.78  ? 375 VAL A C   1 
ATOM 2176 O O   . VAL A 1 290 ? 132.012 116.274 102.920 1.00 62.70  ? 375 VAL A O   1 
ATOM 2177 C CB  . VAL A 1 290 ? 132.030 116.776 99.563  1.00 51.21  ? 375 VAL A CB  1 
ATOM 2178 C CG1 . VAL A 1 290 ? 130.601 116.378 99.901  1.00 58.12  ? 375 VAL A CG1 1 
ATOM 2179 C CG2 . VAL A 1 290 ? 132.046 117.880 98.518  1.00 50.10  ? 375 VAL A CG2 1 
ATOM 2180 N N   . VAL A 1 291 ? 133.533 115.095 101.740 1.00 52.03  ? 376 VAL A N   1 
ATOM 2181 C CA  . VAL A 1 291 ? 133.524 113.968 102.669 1.00 49.94  ? 376 VAL A CA  1 
ATOM 2182 C C   . VAL A 1 291 ? 133.990 114.412 104.050 1.00 54.85  ? 376 VAL A C   1 
ATOM 2183 O O   . VAL A 1 291 ? 133.385 114.062 105.072 1.00 61.02  ? 376 VAL A O   1 
ATOM 2184 C CB  . VAL A 1 291 ? 134.397 112.824 102.119 1.00 48.10  ? 376 VAL A CB  1 
ATOM 2185 C CG1 . VAL A 1 291 ? 134.833 111.889 103.236 1.00 55.26  ? 376 VAL A CG1 1 
ATOM 2186 C CG2 . VAL A 1 291 ? 133.657 112.063 101.029 1.00 56.95  ? 376 VAL A CG2 1 
ATOM 2187 N N   . ALA A 1 292 ? 135.080 115.185 104.099 1.00 50.51  ? 377 ALA A N   1 
ATOM 2188 C CA  . ALA A 1 292 ? 135.605 115.652 105.374 1.00 46.87  ? 377 ALA A CA  1 
ATOM 2189 C C   . ALA A 1 292 ? 134.608 116.553 106.082 1.00 49.65  ? 377 ALA A C   1 
ATOM 2190 O O   . ALA A 1 292 ? 134.446 116.459 107.303 1.00 55.02  ? 377 ALA A O   1 
ATOM 2191 C CB  . ALA A 1 292 ? 136.931 116.380 105.158 1.00 48.17  ? 377 ALA A CB  1 
ATOM 2192 N N   . TYR A 1 293 ? 133.925 117.427 105.337 1.00 49.47  ? 378 TYR A N   1 
ATOM 2193 C CA  . TYR A 1 293 ? 132.907 118.271 105.950 1.00 50.94  ? 378 TYR A CA  1 
ATOM 2194 C C   . TYR A 1 293 ? 131.843 117.407 106.617 1.00 54.95  ? 378 TYR A C   1 
ATOM 2195 O O   . TYR A 1 293 ? 131.570 117.541 107.821 1.00 60.78  ? 378 TYR A O   1 
ATOM 2196 C CB  . TYR A 1 293 ? 132.282 119.173 104.879 1.00 49.06  ? 378 TYR A CB  1 
ATOM 2197 C CG  . TYR A 1 293 ? 131.219 120.140 105.363 1.00 54.26  ? 378 TYR A CG  1 
ATOM 2198 C CD1 . TYR A 1 293 ? 131.566 121.265 106.101 1.00 56.48  ? 378 TYR A CD1 1 
ATOM 2199 C CD2 . TYR A 1 293 ? 129.873 119.919 105.103 1.00 55.91  ? 378 TYR A CD2 1 
ATOM 2200 C CE1 . TYR A 1 293 ? 130.605 122.158 106.545 1.00 51.99  ? 378 TYR A CE1 1 
ATOM 2201 C CE2 . TYR A 1 293 ? 128.903 120.802 105.552 1.00 55.53  ? 378 TYR A CE2 1 
ATOM 2202 C CZ  . TYR A 1 293 ? 129.276 121.917 106.275 1.00 53.48  ? 378 TYR A CZ  1 
ATOM 2203 O OH  . TYR A 1 293 ? 128.319 122.799 106.724 1.00 58.72  ? 378 TYR A OH  1 
ATOM 2204 N N   . GLY A 1 294 ? 131.271 116.468 105.858 1.00 56.92  ? 379 GLY A N   1 
ATOM 2205 C CA  . GLY A 1 294 ? 130.213 115.639 106.419 1.00 56.00  ? 379 GLY A CA  1 
ATOM 2206 C C   . GLY A 1 294 ? 130.663 114.879 107.653 1.00 60.77  ? 379 GLY A C   1 
ATOM 2207 O O   . GLY A 1 294 ? 129.999 114.907 108.699 1.00 66.16  ? 379 GLY A O   1 
ATOM 2208 N N   . ILE A 1 295 ? 131.825 114.225 107.559 1.00 60.12  ? 380 ILE A N   1 
ATOM 2209 C CA  . ILE A 1 295 ? 132.325 113.420 108.671 1.00 58.21  ? 380 ILE A CA  1 
ATOM 2210 C C   . ILE A 1 295 ? 132.565 114.294 109.895 1.00 59.68  ? 380 ILE A C   1 
ATOM 2211 O O   . ILE A 1 295 ? 132.188 113.938 111.020 1.00 66.59  ? 380 ILE A O   1 
ATOM 2212 C CB  . ILE A 1 295 ? 133.606 112.671 108.262 1.00 56.17  ? 380 ILE A CB  1 
ATOM 2213 C CG1 . ILE A 1 295 ? 133.323 111.679 107.134 1.00 57.16  ? 380 ILE A CG1 1 
ATOM 2214 C CG2 . ILE A 1 295 ? 134.194 111.942 109.457 1.00 59.16  ? 380 ILE A CG2 1 
ATOM 2215 C CD1 . ILE A 1 295 ? 134.526 110.850 106.735 1.00 56.41  ? 380 ILE A CD1 1 
ATOM 2216 N N   . SER A 1 296 ? 133.201 115.453 109.695 1.00 55.86  ? 381 SER A N   1 
ATOM 2217 C CA  . SER A 1 296 ? 133.576 116.300 110.819 1.00 56.42  ? 381 SER A CA  1 
ATOM 2218 C C   . SER A 1 296 ? 132.349 116.774 111.583 1.00 59.55  ? 381 SER A C   1 
ATOM 2219 O O   . SER A 1 296 ? 132.270 116.606 112.810 1.00 64.57  ? 381 SER A O   1 
ATOM 2220 C CB  . SER A 1 296 ? 134.402 117.488 110.325 1.00 59.75  ? 381 SER A CB  1 
ATOM 2221 O OG  . SER A 1 296 ? 135.613 117.053 109.731 1.00 62.65  ? 381 SER A OG  1 
ATOM 2222 N N   . ILE A 1 297 ? 131.371 117.360 110.878 1.00 59.34  ? 382 ILE A N   1 
ATOM 2223 C CA  . ILE A 1 297 ? 130.171 117.797 111.594 1.00 61.29  ? 382 ILE A CA  1 
ATOM 2224 C C   . ILE A 1 297 ? 129.461 116.629 112.264 1.00 61.67  ? 382 ILE A C   1 
ATOM 2225 O O   . ILE A 1 297 ? 129.064 116.738 113.428 1.00 66.87  ? 382 ILE A O   1 
ATOM 2226 C CB  . ILE A 1 297 ? 129.211 118.627 110.714 1.00 60.62  ? 382 ILE A CB  1 
ATOM 2227 C CG1 . ILE A 1 297 ? 129.867 119.927 110.243 1.00 60.31  ? 382 ILE A CG1 1 
ATOM 2228 C CG2 . ILE A 1 297 ? 127.915 118.925 111.456 1.00 67.17  ? 382 ILE A CG2 1 
ATOM 2229 C CD1 . ILE A 1 297 ? 130.613 119.889 109.013 1.00 60.22  ? 382 ILE A CD1 1 
ATOM 2230 N N   . ASN A 1 298 ? 129.303 115.493 111.579 1.00 65.41  ? 383 ASN A N   1 
ATOM 2231 C CA  . ASN A 1 298 ? 128.561 114.404 112.216 1.00 64.21  ? 383 ASN A CA  1 
ATOM 2232 C C   . ASN A 1 298 ? 129.237 113.941 113.509 1.00 63.86  ? 383 ASN A C   1 
ATOM 2233 O O   . ASN A 1 298 ? 128.591 113.864 114.569 1.00 66.86  ? 383 ASN A O   1 
ATOM 2234 C CB  . ASN A 1 298 ? 128.382 113.245 111.236 1.00 68.36  ? 383 ASN A CB  1 
ATOM 2235 C CG  . ASN A 1 298 ? 127.452 113.598 110.089 1.00 75.88  ? 383 ASN A CG  1 
ATOM 2236 O OD1 . ASN A 1 298 ? 127.667 113.188 108.949 1.00 77.88  ? 383 ASN A OD1 1 
ATOM 2237 N ND2 . ASN A 1 298 ? 126.412 114.369 110.390 1.00 75.47  ? 383 ASN A ND2 1 
ATOM 2238 N N   . LEU A 1 299 ? 130.545 113.671 113.456 1.00 61.59  ? 384 LEU A N   1 
ATOM 2239 C CA  . LEU A 1 299 ? 131.237 113.149 114.633 1.00 58.74  ? 384 LEU A CA  1 
ATOM 2240 C C   . LEU A 1 299 ? 131.239 114.164 115.773 1.00 62.50  ? 384 LEU A C   1 
ATOM 2241 O O   . LEU A 1 299 ? 130.896 113.833 116.921 1.00 66.44  ? 384 LEU A O   1 
ATOM 2242 C CB  . LEU A 1 299 ? 132.671 112.748 114.277 1.00 54.94  ? 384 LEU A CB  1 
ATOM 2243 C CG  . LEU A 1 299 ? 132.937 111.799 113.104 1.00 58.37  ? 384 LEU A CG  1 
ATOM 2244 C CD1 . LEU A 1 299 ? 134.336 111.206 113.199 1.00 61.86  ? 384 LEU A CD1 1 
ATOM 2245 C CD2 . LEU A 1 299 ? 131.890 110.703 113.014 1.00 61.15  ? 384 LEU A CD2 1 
ATOM 2246 N N   . VAL A 1 300 ? 131.628 115.411 115.479 1.00 60.46  ? 385 VAL A N   1 
ATOM 2247 C CA  . VAL A 1 300 ? 131.738 116.379 116.563 1.00 56.72  ? 385 VAL A CA  1 
ATOM 2248 C C   . VAL A 1 300 ? 130.360 116.719 117.113 1.00 60.34  ? 385 VAL A C   1 
ATOM 2249 O O   . VAL A 1 300 ? 130.218 117.003 118.306 1.00 65.71  ? 385 VAL A O   1 
ATOM 2250 C CB  . VAL A 1 300 ? 132.501 117.638 116.108 1.00 64.23  ? 385 VAL A CB  1 
ATOM 2251 C CG1 . VAL A 1 300 ? 131.655 118.497 115.175 1.00 68.41  ? 385 VAL A CG1 1 
ATOM 2252 C CG2 . VAL A 1 300 ? 132.961 118.429 117.317 1.00 64.49  ? 385 VAL A CG2 1 
ATOM 2253 N N   . GLU A 1 301 ? 129.323 116.671 116.272 1.00 62.72  ? 386 GLU A N   1 
ATOM 2254 C CA  . GLU A 1 301 ? 127.965 116.912 116.736 1.00 62.27  ? 386 GLU A CA  1 
ATOM 2255 C C   . GLU A 1 301 ? 127.528 115.839 117.722 1.00 58.12  ? 386 GLU A C   1 
ATOM 2256 O O   . GLU A 1 301 ? 126.954 116.154 118.772 1.00 65.17  ? 386 GLU A O   1 
ATOM 2257 C CB  . GLU A 1 301 ? 127.030 116.974 115.525 1.00 66.10  ? 386 GLU A CB  1 
ATOM 2258 C CG  . GLU A 1 301 ? 125.611 117.443 115.794 1.00 65.55  ? 386 GLU A CG  1 
ATOM 2259 C CD  . GLU A 1 301 ? 124.706 116.337 116.286 1.00 74.64  ? 386 GLU A CD  1 
ATOM 2260 O OE1 . GLU A 1 301 ? 124.947 115.164 115.932 1.00 78.85  ? 386 GLU A OE1 1 
ATOM 2261 O OE2 . GLU A 1 301 ? 123.738 116.645 117.007 1.00 78.85  ? 386 GLU A OE2 1 
ATOM 2262 N N   . VAL A 1 302 ? 127.812 114.569 117.416 1.00 59.70  ? 387 VAL A N   1 
ATOM 2263 C CA  . VAL A 1 302 ? 127.457 113.499 118.350 1.00 54.72  ? 387 VAL A CA  1 
ATOM 2264 C C   . VAL A 1 302 ? 128.185 113.685 119.679 1.00 54.80  ? 387 VAL A C   1 
ATOM 2265 O O   . VAL A 1 302 ? 127.578 113.611 120.761 1.00 58.03  ? 387 VAL A O   1 
ATOM 2266 C CB  . VAL A 1 302 ? 127.757 112.122 117.731 1.00 58.42  ? 387 VAL A CB  1 
ATOM 2267 C CG1 . VAL A 1 302 ? 127.486 111.020 118.743 1.00 55.71  ? 387 VAL A CG1 1 
ATOM 2268 C CG2 . VAL A 1 302 ? 126.918 111.910 116.482 1.00 63.31  ? 387 VAL A CG2 1 
ATOM 2269 N N   . THR A 1 303 ? 129.496 113.941 119.619 1.00 61.25  ? 388 THR A N   1 
ATOM 2270 C CA  . THR A 1 303 ? 130.271 114.077 120.854 1.00 57.32  ? 388 THR A CA  1 
ATOM 2271 C C   . THR A 1 303 ? 129.780 115.259 121.688 1.00 58.40  ? 388 THR A C   1 
ATOM 2272 O O   . THR A 1 303 ? 129.605 115.151 122.914 1.00 60.25  ? 388 THR A O   1 
ATOM 2273 C CB  . THR A 1 303 ? 131.757 114.229 120.527 1.00 57.48  ? 388 THR A CB  1 
ATOM 2274 O OG1 . THR A 1 303 ? 132.202 113.093 119.775 1.00 65.29  ? 388 THR A OG1 1 
ATOM 2275 C CG2 . THR A 1 303 ? 132.577 114.333 121.806 1.00 61.12  ? 388 THR A CG2 1 
ATOM 2276 N N   . TRP A 1 304 ? 129.536 116.396 121.033 1.00 59.06  ? 389 TRP A N   1 
ATOM 2277 C CA  . TRP A 1 304 ? 129.096 117.584 121.749 1.00 56.15  ? 389 TRP A CA  1 
ATOM 2278 C C   . TRP A 1 304 ? 127.708 117.396 122.339 1.00 58.58  ? 389 TRP A C   1 
ATOM 2279 O O   . TRP A 1 304 ? 127.429 117.901 123.428 1.00 61.76  ? 389 TRP A O   1 
ATOM 2280 C CB  . TRP A 1 304 ? 129.124 118.802 120.830 1.00 58.15  ? 389 TRP A CB  1 
ATOM 2281 C CG  . TRP A 1 304 ? 128.394 119.968 121.409 1.00 56.53  ? 389 TRP A CG  1 
ATOM 2282 C CD1 . TRP A 1 304 ? 128.778 120.731 122.473 1.00 54.86  ? 389 TRP A CD1 1 
ATOM 2283 C CD2 . TRP A 1 304 ? 127.142 120.499 120.966 1.00 54.27  ? 389 TRP A CD2 1 
ATOM 2284 N NE1 . TRP A 1 304 ? 127.845 121.709 122.716 1.00 56.63  ? 389 TRP A NE1 1 
ATOM 2285 C CE2 . TRP A 1 304 ? 126.830 121.587 121.804 1.00 55.09  ? 389 TRP A CE2 1 
ATOM 2286 C CE3 . TRP A 1 304 ? 126.256 120.162 119.939 1.00 52.10  ? 389 TRP A CE3 1 
ATOM 2287 C CZ2 . TRP A 1 304 ? 125.669 122.339 121.647 1.00 58.13  ? 389 TRP A CZ2 1 
ATOM 2288 C CZ3 . TRP A 1 304 ? 125.105 120.909 119.785 1.00 53.22  ? 389 TRP A CZ3 1 
ATOM 2289 C CH2 . TRP A 1 304 ? 124.823 121.986 120.632 1.00 57.93  ? 389 TRP A CH2 1 
ATOM 2290 N N   . LYS A 1 305 ? 126.819 116.682 121.643 1.00 58.25  ? 390 LYS A N   1 
ATOM 2291 C CA  . LYS A 1 305 ? 125.499 116.446 122.217 1.00 53.93  ? 390 LYS A CA  1 
ATOM 2292 C C   . LYS A 1 305 ? 125.571 115.523 123.427 1.00 56.72  ? 390 LYS A C   1 
ATOM 2293 O O   . LYS A 1 305 ? 124.810 115.704 124.386 1.00 62.80  ? 390 LYS A O   1 
ATOM 2294 C CB  . LYS A 1 305 ? 124.549 115.880 121.163 1.00 59.15  ? 390 LYS A CB  1 
ATOM 2295 C CG  . LYS A 1 305 ? 123.724 116.950 120.469 1.00 60.70  ? 390 LYS A CG  1 
ATOM 2296 C CD  . LYS A 1 305 ? 122.499 116.369 119.790 1.00 71.92  ? 390 LYS A CD  1 
ATOM 2297 C CE  . LYS A 1 305 ? 121.493 117.460 119.461 1.00 70.11  ? 390 LYS A CE  1 
ATOM 2298 N NZ  . LYS A 1 305 ? 120.290 116.921 118.771 1.00 77.84  ? 390 LYS A NZ  1 
ATOM 2299 N N   . SER A 1 306 ? 126.474 114.538 123.410 1.00 58.34  ? 391 SER A N   1 
ATOM 2300 C CA  . SER A 1 306 ? 126.666 113.715 124.603 1.00 58.21  ? 391 SER A CA  1 
ATOM 2301 C C   . SER A 1 306 ? 127.135 114.563 125.784 1.00 58.27  ? 391 SER A C   1 
ATOM 2302 O O   . SER A 1 306 ? 126.582 114.478 126.894 1.00 59.14  ? 391 SER A O   1 
ATOM 2303 C CB  . SER A 1 306 ? 127.662 112.593 124.312 1.00 59.41  ? 391 SER A CB  1 
ATOM 2304 O OG  . SER A 1 306 ? 128.955 113.113 124.055 1.00 65.24  ? 391 SER A OG  1 
ATOM 2305 N N   . LYS A 1 307 ? 128.152 115.402 125.558 1.00 61.47  ? 392 LYS A N   1 
ATOM 2306 C CA  . LYS A 1 307 ? 128.618 116.286 126.625 1.00 57.34  ? 392 LYS A CA  1 
ATOM 2307 C C   . LYS A 1 307 ? 127.517 117.235 127.087 1.00 53.14  ? 392 LYS A C   1 
ATOM 2308 O O   . LYS A 1 307 ? 127.394 117.517 128.285 1.00 58.12  ? 392 LYS A O   1 
ATOM 2309 C CB  . LYS A 1 307 ? 129.839 117.078 126.160 1.00 55.35  ? 392 LYS A CB  1 
ATOM 2310 C CG  . LYS A 1 307 ? 131.037 116.205 125.862 1.00 53.86  ? 392 LYS A CG  1 
ATOM 2311 C CD  . LYS A 1 307 ? 131.540 115.551 127.135 1.00 53.89  ? 392 LYS A CD  1 
ATOM 2312 C CE  . LYS A 1 307 ? 132.460 114.391 126.829 1.00 54.32  ? 392 LYS A CE  1 
ATOM 2313 N NZ  . LYS A 1 307 ? 133.256 113.991 128.023 1.00 56.92  ? 392 LYS A NZ  1 
ATOM 2314 N N   . LEU A 1 308 ? 126.715 117.729 126.147 1.00 54.82  ? 393 LEU A N   1 
ATOM 2315 C CA  . LEU A 1 308 ? 125.584 118.593 126.456 1.00 55.42  ? 393 LEU A CA  1 
ATOM 2316 C C   . LEU A 1 308 ? 124.599 117.916 127.393 1.00 54.60  ? 393 LEU A C   1 
ATOM 2317 O O   . LEU A 1 308 ? 124.168 118.512 128.388 1.00 56.55  ? 393 LEU A O   1 
ATOM 2318 C CB  . LEU A 1 308 ? 124.889 118.969 125.155 1.00 53.92  ? 393 LEU A CB  1 
ATOM 2319 C CG  . LEU A 1 308 ? 123.722 119.936 125.224 1.00 58.20  ? 393 LEU A CG  1 
ATOM 2320 C CD1 . LEU A 1 308 ? 124.208 121.361 125.357 1.00 61.12  ? 393 LEU A CD1 1 
ATOM 2321 C CD2 . LEU A 1 308 ? 122.893 119.729 123.983 1.00 59.41  ? 393 LEU A CD2 1 
ATOM 2322 N N   . LYS A 1 309 ? 124.211 116.681 127.076 1.00 57.65  ? 394 LYS A N   1 
ATOM 2323 C CA  . LYS A 1 309 ? 123.332 115.930 127.961 1.00 49.21  ? 394 LYS A CA  1 
ATOM 2324 C C   . LYS A 1 309 ? 123.945 115.782 129.341 1.00 53.08  ? 394 LYS A C   1 
ATOM 2325 O O   . LYS A 1 309 ? 123.243 115.919 130.350 1.00 49.56  ? 394 LYS A O   1 
ATOM 2326 C CB  . LYS A 1 309 ? 123.057 114.550 127.379 1.00 50.48  ? 394 LYS A CB  1 
ATOM 2327 C CG  . LYS A 1 309 ? 121.822 114.465 126.535 1.00 52.77  ? 394 LYS A CG  1 
ATOM 2328 C CD  . LYS A 1 309 ? 121.766 113.096 125.928 1.00 52.46  ? 394 LYS A CD  1 
ATOM 2329 C CE  . LYS A 1 309 ? 122.684 113.035 124.733 1.00 57.92  ? 394 LYS A CE  1 
ATOM 2330 N NZ  . LYS A 1 309 ? 122.494 114.209 123.841 1.00 60.79  ? 394 LYS A NZ  1 
ATOM 2331 N N   . ALA A 1 310 ? 125.247 115.496 129.403 1.00 59.98  ? 395 ALA A N   1 
ATOM 2332 C CA  . ALA A 1 310 ? 125.917 115.436 130.698 1.00 55.20  ? 395 ALA A CA  1 
ATOM 2333 C C   . ALA A 1 310 ? 125.830 116.766 131.441 1.00 54.44  ? 395 ALA A C   1 
ATOM 2334 O O   . ALA A 1 310 ? 125.770 116.782 132.676 1.00 58.96  ? 395 ALA A O   1 
ATOM 2335 C CB  . ALA A 1 310 ? 127.377 115.022 130.517 1.00 55.88  ? 395 ALA A CB  1 
ATOM 2336 N N   . GLN A 1 311 ? 125.813 117.886 130.714 1.00 56.01  ? 396 GLN A N   1 
ATOM 2337 C CA  . GLN A 1 311 ? 125.871 119.195 131.359 1.00 53.15  ? 396 GLN A CA  1 
ATOM 2338 C C   . GLN A 1 311 ? 124.528 119.602 131.960 1.00 57.50  ? 396 GLN A C   1 
ATOM 2339 O O   . GLN A 1 311 ? 124.466 120.021 133.121 1.00 63.07  ? 396 GLN A O   1 
ATOM 2340 C CB  . GLN A 1 311 ? 126.348 120.250 130.360 1.00 56.71  ? 396 GLN A CB  1 
ATOM 2341 C CG  . GLN A 1 311 ? 126.097 121.691 130.789 1.00 58.21  ? 396 GLN A CG  1 
ATOM 2342 C CD  . GLN A 1 311 ? 126.672 122.008 132.158 1.00 59.06  ? 396 GLN A CD  1 
ATOM 2343 O OE1 . GLN A 1 311 ? 125.951 122.414 133.069 1.00 61.59  ? 396 GLN A OE1 1 
ATOM 2344 N NE2 . GLN A 1 311 ? 127.978 121.818 132.310 1.00 64.80  ? 396 GLN A NE2 1 
ATOM 2345 N N   . PHE A 1 312 ? 123.444 119.501 131.186 1.00 58.07  ? 397 PHE A N   1 
ATOM 2346 C CA  . PHE A 1 312 ? 122.122 119.949 131.621 1.00 51.88  ? 397 PHE A CA  1 
ATOM 2347 C C   . PHE A 1 312 ? 121.264 118.745 131.986 1.00 56.60  ? 397 PHE A C   1 
ATOM 2348 O O   . PHE A 1 312 ? 120.600 118.160 131.116 1.00 62.58  ? 397 PHE A O   1 
ATOM 2349 C CB  . PHE A 1 312 ? 121.444 120.786 130.532 1.00 52.34  ? 397 PHE A CB  1 
ATOM 2350 C CG  . PHE A 1 312 ? 122.227 122.002 130.121 1.00 60.96  ? 397 PHE A CG  1 
ATOM 2351 C CD1 . PHE A 1 312 ? 122.196 123.155 130.889 1.00 61.13  ? 397 PHE A CD1 1 
ATOM 2352 C CD2 . PHE A 1 312 ? 122.987 121.995 128.963 1.00 58.37  ? 397 PHE A CD2 1 
ATOM 2353 C CE1 . PHE A 1 312 ? 122.913 124.275 130.513 1.00 56.52  ? 397 PHE A CE1 1 
ATOM 2354 C CE2 . PHE A 1 312 ? 123.705 123.113 128.581 1.00 57.43  ? 397 PHE A CE2 1 
ATOM 2355 C CZ  . PHE A 1 312 ? 123.668 124.254 129.358 1.00 56.43  ? 397 PHE A CZ  1 
ATOM 2356 N N   . PRO A 1 313 ? 121.230 118.337 133.259 1.00 56.68  ? 398 PRO A N   1 
ATOM 2357 C CA  . PRO A 1 313 ? 120.419 117.170 133.632 1.00 52.43  ? 398 PRO A CA  1 
ATOM 2358 C C   . PRO A 1 313 ? 118.932 117.455 133.682 1.00 57.05  ? 398 PRO A C   1 
ATOM 2359 O O   . PRO A 1 313 ? 118.135 116.512 133.594 1.00 59.86  ? 398 PRO A O   1 
ATOM 2360 C CB  . PRO A 1 313 ? 120.949 116.798 135.030 1.00 50.88  ? 398 PRO A CB  1 
ATOM 2361 C CG  . PRO A 1 313 ? 122.111 117.741 135.301 1.00 57.70  ? 398 PRO A CG  1 
ATOM 2362 C CD  . PRO A 1 313 ? 121.895 118.929 134.429 1.00 57.57  ? 398 PRO A CD  1 
ATOM 2363 N N   . SER A 1 314 ? 118.536 118.707 133.823 1.00 57.86  ? 399 SER A N   1 
ATOM 2364 C CA  . SER A 1 314 ? 117.112 118.965 133.916 1.00 54.19  ? 399 SER A CA  1 
ATOM 2365 C C   . SER A 1 314 ? 116.535 119.298 132.547 1.00 53.72  ? 399 SER A C   1 
ATOM 2366 O O   . SER A 1 314 ? 117.227 119.854 131.688 1.00 60.07  ? 399 SER A O   1 
ATOM 2367 C CB  . SER A 1 314 ? 116.831 120.119 134.883 1.00 60.27  ? 399 SER A CB  1 
ATOM 2368 O OG  . SER A 1 314 ? 117.373 121.329 134.394 1.00 62.23  ? 399 SER A OG  1 
ATOM 2369 N N   . PRO A 1 315 ? 115.266 118.951 132.326 1.00 52.34  ? 400 PRO A N   1 
ATOM 2370 C CA  . PRO A 1 315 ? 114.645 119.237 131.023 1.00 52.85  ? 400 PRO A CA  1 
ATOM 2371 C C   . PRO A 1 315 ? 114.536 120.719 130.727 1.00 59.40  ? 400 PRO A C   1 
ATOM 2372 O O   . PRO A 1 315 ? 114.802 121.154 129.597 1.00 62.87  ? 400 PRO A O   1 
ATOM 2373 C CB  . PRO A 1 315 ? 113.255 118.601 131.155 1.00 47.42  ? 400 PRO A CB  1 
ATOM 2374 C CG  . PRO A 1 315 ? 113.358 117.658 132.318 1.00 52.40  ? 400 PRO A CG  1 
ATOM 2375 C CD  . PRO A 1 315 ? 114.348 118.258 133.240 1.00 55.70  ? 400 PRO A CD  1 
ATOM 2376 N N   . ASN A 1 316 ? 114.132 121.506 131.725 1.00 60.14  ? 401 ASN A N   1 
ATOM 2377 C CA  . ASN A 1 316 ? 113.887 122.925 131.512 1.00 56.14  ? 401 ASN A CA  1 
ATOM 2378 C C   . ASN A 1 316 ? 115.168 123.654 131.135 1.00 61.70  ? 401 ASN A C   1 
ATOM 2379 O O   . ASN A 1 316 ? 115.170 124.492 130.229 1.00 64.73  ? 401 ASN A O   1 
ATOM 2380 C CB  . ASN A 1 316 ? 113.258 123.534 132.765 1.00 60.60  ? 401 ASN A CB  1 
ATOM 2381 C CG  . ASN A 1 316 ? 111.974 122.835 133.166 1.00 71.16  ? 401 ASN A CG  1 
ATOM 2382 O OD1 . ASN A 1 316 ? 110.931 123.022 132.539 1.00 79.69  ? 401 ASN A OD1 1 
ATOM 2383 N ND2 . ASN A 1 316 ? 112.046 122.017 134.209 1.00 72.88  ? 401 ASN A ND2 1 
ATOM 2384 N N   . GLU A 1 317 ? 116.274 123.343 131.815 1.00 61.23  ? 402 GLU A N   1 
ATOM 2385 C CA  . GLU A 1 317 ? 117.543 123.977 131.473 1.00 59.38  ? 402 GLU A CA  1 
ATOM 2386 C C   . GLU A 1 317 ? 118.022 123.546 130.091 1.00 58.43  ? 402 GLU A C   1 
ATOM 2387 O O   . GLU A 1 317 ? 118.576 124.357 129.342 1.00 65.89  ? 402 GLU A O   1 
ATOM 2388 C CB  . GLU A 1 317 ? 118.596 123.661 132.535 1.00 65.82  ? 402 GLU A CB  1 
ATOM 2389 C CG  . GLU A 1 317 ? 118.295 124.266 133.899 1.00 79.52  ? 402 GLU A CG  1 
ATOM 2390 C CD  . GLU A 1 317 ? 118.358 125.780 133.895 1.00 89.40  ? 402 GLU A CD  1 
ATOM 2391 O OE1 . GLU A 1 317 ? 119.159 126.343 133.119 1.00 90.61  ? 402 GLU A OE1 1 
ATOM 2392 O OE2 . GLU A 1 317 ? 117.603 126.409 134.666 1.00 93.44  ? 402 GLU A OE2 1 
ATOM 2393 N N   . TYR A 1 318 ? 117.809 122.278 129.732 1.00 56.98  ? 403 TYR A N   1 
ATOM 2394 C CA  . TYR A 1 318 ? 118.212 121.801 128.412 1.00 54.47  ? 403 TYR A CA  1 
ATOM 2395 C C   . TYR A 1 318 ? 117.449 122.534 127.313 1.00 56.44  ? 403 TYR A C   1 
ATOM 2396 O O   . TYR A 1 318 ? 118.039 122.990 126.325 1.00 60.92  ? 403 TYR A O   1 
ATOM 2397 C CB  . TYR A 1 318 ? 117.989 120.289 128.321 1.00 54.47  ? 403 TYR A CB  1 
ATOM 2398 C CG  . TYR A 1 318 ? 118.570 119.635 127.087 1.00 55.34  ? 403 TYR A CG  1 
ATOM 2399 C CD1 . TYR A 1 318 ? 117.850 119.570 125.901 1.00 49.98  ? 403 TYR A CD1 1 
ATOM 2400 C CD2 . TYR A 1 318 ? 119.836 119.065 127.115 1.00 56.43  ? 403 TYR A CD2 1 
ATOM 2401 C CE1 . TYR A 1 318 ? 118.381 118.967 124.775 1.00 49.87  ? 403 TYR A CE1 1 
ATOM 2402 C CE2 . TYR A 1 318 ? 120.372 118.458 125.997 1.00 52.31  ? 403 TYR A CE2 1 
ATOM 2403 C CZ  . TYR A 1 318 ? 119.642 118.413 124.829 1.00 53.41  ? 403 TYR A CZ  1 
ATOM 2404 O OH  . TYR A 1 318 ? 120.173 117.811 123.712 1.00 61.12  ? 403 TYR A OH  1 
ATOM 2405 N N   . SER A 1 319 ? 116.131 122.679 127.480 1.00 55.66  ? 404 SER A N   1 
ATOM 2406 C CA  . SER A 1 319 ? 115.334 123.390 126.484 1.00 51.47  ? 404 SER A CA  1 
ATOM 2407 C C   . SER A 1 319 ? 115.632 124.887 126.480 1.00 57.21  ? 404 SER A C   1 
ATOM 2408 O O   . SER A 1 319 ? 115.612 125.523 125.419 1.00 63.24  ? 404 SER A O   1 
ATOM 2409 C CB  . SER A 1 319 ? 113.846 123.142 126.729 1.00 57.91  ? 404 SER A CB  1 
ATOM 2410 O OG  . SER A 1 319 ? 113.413 123.763 127.926 1.00 67.78  ? 404 SER A OG  1 
ATOM 2411 N N   . ALA A 1 320 ? 115.915 125.469 127.646 1.00 55.45  ? 405 ALA A N   1 
ATOM 2412 C CA  . ALA A 1 320 ? 116.306 126.872 127.686 1.00 54.58  ? 405 ALA A CA  1 
ATOM 2413 C C   . ALA A 1 320 ? 117.622 127.090 126.956 1.00 57.83  ? 405 ALA A C   1 
ATOM 2414 O O   . ALA A 1 320 ? 117.806 128.116 126.290 1.00 64.79  ? 405 ALA A O   1 
ATOM 2415 C CB  . ALA A 1 320 ? 116.403 127.350 129.135 1.00 56.71  ? 405 ALA A CB  1 
ATOM 2416 N N   . PHE A 1 321 ? 118.550 126.137 127.069 1.00 57.48  ? 406 PHE A N   1 
ATOM 2417 C CA  . PHE A 1 321 ? 119.805 126.255 126.337 1.00 56.22  ? 406 PHE A CA  1 
ATOM 2418 C C   . PHE A 1 321 ? 119.592 126.046 124.843 1.00 61.40  ? 406 PHE A C   1 
ATOM 2419 O O   . PHE A 1 321 ? 120.272 126.671 124.027 1.00 65.57  ? 406 PHE A O   1 
ATOM 2420 C CB  . PHE A 1 321 ? 120.838 125.265 126.873 1.00 55.84  ? 406 PHE A CB  1 
ATOM 2421 C CG  . PHE A 1 321 ? 122.162 125.342 126.164 1.00 58.78  ? 406 PHE A CG  1 
ATOM 2422 C CD1 . PHE A 1 321 ? 123.120 126.258 126.566 1.00 63.54  ? 406 PHE A CD1 1 
ATOM 2423 C CD2 . PHE A 1 321 ? 122.444 124.515 125.091 1.00 58.25  ? 406 PHE A CD2 1 
ATOM 2424 C CE1 . PHE A 1 321 ? 124.333 126.341 125.915 1.00 62.73  ? 406 PHE A CE1 1 
ATOM 2425 C CE2 . PHE A 1 321 ? 123.657 124.598 124.434 1.00 53.38  ? 406 PHE A CE2 1 
ATOM 2426 C CZ  . PHE A 1 321 ? 124.604 125.510 124.850 1.00 57.57  ? 406 PHE A CZ  1 
ATOM 2427 N N   . MET A 1 322 ? 118.670 125.161 124.463 1.00 61.04  ? 407 MET A N   1 
ATOM 2428 C CA  . MET A 1 322 ? 118.331 124.969 123.048 1.00 58.33  ? 407 MET A CA  1 
ATOM 2429 C C   . MET A 1 322 ? 117.252 125.912 122.543 1.00 62.89  ? 407 MET A C   1 
ATOM 2430 O O   . MET A 1 322 ? 116.646 125.681 121.491 1.00 67.61  ? 407 MET A O   1 
ATOM 2431 C CB  . MET A 1 322 ? 117.946 123.522 122.793 1.00 60.11  ? 407 MET A CB  1 
ATOM 2432 C CG  . MET A 1 322 ? 119.112 122.603 123.019 1.00 56.66  ? 407 MET A CG  1 
ATOM 2433 S SD  . MET A 1 322 ? 120.252 123.163 121.728 1.00 81.66  ? 407 MET A SD  1 
ATOM 2434 C CE  . MET A 1 322 ? 121.731 122.263 122.109 1.00 63.35  ? 407 MET A CE  1 
ATOM 2435 N N   . GLY A 1 323 ? 116.983 126.976 123.284 1.00 61.81  ? 408 GLY A N   1 
ATOM 2436 C CA  . GLY A 1 323 ? 116.380 128.155 122.691 1.00 58.38  ? 408 GLY A CA  1 
ATOM 2437 C C   . GLY A 1 323 ? 117.459 129.170 122.356 1.00 60.71  ? 408 GLY A C   1 
ATOM 2438 O O   . GLY A 1 323 ? 117.466 129.776 121.276 1.00 66.25  ? 408 GLY A O   1 
ATOM 2439 N N   . ASP A 1 324 ? 118.401 129.336 123.289 1.00 59.85  ? 409 ASP A N   1 
ATOM 2440 C CA  . ASP A 1 324 ? 119.502 130.273 123.095 1.00 58.88  ? 409 ASP A CA  1 
ATOM 2441 C C   . ASP A 1 324 ? 120.440 129.806 121.989 1.00 59.52  ? 409 ASP A C   1 
ATOM 2442 O O   . ASP A 1 324 ? 120.975 130.623 121.231 1.00 64.74  ? 409 ASP A O   1 
ATOM 2443 C CB  . ASP A 1 324 ? 120.264 130.448 124.408 1.00 63.91  ? 409 ASP A CB  1 
ATOM 2444 C CG  . ASP A 1 324 ? 119.351 130.802 125.566 1.00 71.95  ? 409 ASP A CG  1 
ATOM 2445 O OD1 . ASP A 1 324 ? 118.287 131.407 125.321 1.00 75.86  ? 409 ASP A OD1 1 
ATOM 2446 O OD2 . ASP A 1 324 ? 119.692 130.465 126.719 1.00 75.05  ? 409 ASP A OD2 1 
ATOM 2447 N N   . PHE A 1 325 ? 120.657 128.492 121.893 1.00 58.14  ? 410 PHE A N   1 
ATOM 2448 C CA  . PHE A 1 325 ? 121.466 127.932 120.818 1.00 55.06  ? 410 PHE A CA  1 
ATOM 2449 C C   . PHE A 1 325 ? 120.862 128.257 119.461 1.00 58.74  ? 410 PHE A C   1 
ATOM 2450 O O   . PHE A 1 325 ? 121.580 128.621 118.526 1.00 61.51  ? 410 PHE A O   1 
ATOM 2451 C CB  . PHE A 1 325 ? 121.591 126.419 121.012 1.00 54.18  ? 410 PHE A CB  1 
ATOM 2452 C CG  . PHE A 1 325 ? 122.419 125.726 119.965 1.00 59.57  ? 410 PHE A CG  1 
ATOM 2453 C CD1 . PHE A 1 325 ? 123.790 125.912 119.905 1.00 65.05  ? 410 PHE A CD1 1 
ATOM 2454 C CD2 . PHE A 1 325 ? 121.823 124.877 119.046 1.00 62.02  ? 410 PHE A CD2 1 
ATOM 2455 C CE1 . PHE A 1 325 ? 124.550 125.265 118.946 1.00 62.60  ? 410 PHE A CE1 1 
ATOM 2456 C CE2 . PHE A 1 325 ? 122.577 124.231 118.084 1.00 65.03  ? 410 PHE A CE2 1 
ATOM 2457 C CZ  . PHE A 1 325 ? 123.942 124.427 118.034 1.00 62.13  ? 410 PHE A CZ  1 
ATOM 2458 N N   . SER A 1 326 ? 119.536 128.159 119.343 1.00 58.14  ? 411 SER A N   1 
ATOM 2459 C CA  . SER A 1 326 ? 118.878 128.472 118.078 1.00 52.90  ? 411 SER A CA  1 
ATOM 2460 C C   . SER A 1 326 ? 118.928 129.966 117.775 1.00 58.19  ? 411 SER A C   1 
ATOM 2461 O O   . SER A 1 326 ? 119.114 130.363 116.617 1.00 67.16  ? 411 SER A O   1 
ATOM 2462 C CB  . SER A 1 326 ? 117.433 127.977 118.109 1.00 53.12  ? 411 SER A CB  1 
ATOM 2463 O OG  . SER A 1 326 ? 117.383 126.561 118.106 1.00 58.98  ? 411 SER A OG  1 
ATOM 2464 N N   . THR A 1 327 ? 118.750 130.812 118.795 1.00 56.83  ? 412 THR A N   1 
ATOM 2465 C CA  . THR A 1 327 ? 118.862 132.252 118.568 1.00 56.13  ? 412 THR A CA  1 
ATOM 2466 C C   . THR A 1 327 ? 120.262 132.626 118.091 1.00 61.88  ? 412 THR A C   1 
ATOM 2467 O O   . THR A 1 327 ? 120.420 133.395 117.130 1.00 66.75  ? 412 THR A O   1 
ATOM 2468 C CB  . THR A 1 327 ? 118.508 133.021 119.841 1.00 53.33  ? 412 THR A CB  1 
ATOM 2469 O OG1 . THR A 1 327 ? 117.205 132.631 120.291 1.00 59.10  ? 412 THR A OG1 1 
ATOM 2470 C CG2 . THR A 1 327 ? 118.520 134.521 119.578 1.00 56.39  ? 412 THR A CG2 1 
ATOM 2471 N N   . CYS A 1 328 ? 121.292 132.080 118.745 1.00 58.57  ? 413 CYS A N   1 
ATOM 2472 C CA  . CYS A 1 328 ? 122.661 132.313 118.304 1.00 55.71  ? 413 CYS A CA  1 
ATOM 2473 C C   . CYS A 1 328 ? 122.905 131.732 116.920 1.00 58.58  ? 413 CYS A C   1 
ATOM 2474 O O   . CYS A 1 328 ? 123.660 132.309 116.134 1.00 63.06  ? 413 CYS A O   1 
ATOM 2475 C CB  . CYS A 1 328 ? 123.649 131.725 119.312 1.00 60.90  ? 413 CYS A CB  1 
ATOM 2476 S SG  . CYS A 1 328 ? 123.636 132.529 120.931 1.00 93.87  ? 413 CYS A SG  1 
ATOM 2477 N N   . THR A 1 329 ? 122.277 130.598 116.603 1.00 59.79  ? 414 THR A N   1 
ATOM 2478 C CA  . THR A 1 329 ? 122.420 130.007 115.277 1.00 55.68  ? 414 THR A CA  1 
ATOM 2479 C C   . THR A 1 329 ? 121.870 130.936 114.203 1.00 59.62  ? 414 THR A C   1 
ATOM 2480 O O   . THR A 1 329 ? 122.495 131.129 113.157 1.00 67.89  ? 414 THR A O   1 
ATOM 2481 C CB  . THR A 1 329 ? 121.712 128.651 115.231 1.00 52.28  ? 414 THR A CB  1 
ATOM 2482 O OG1 . THR A 1 329 ? 122.349 127.746 116.143 1.00 60.34  ? 414 THR A OG1 1 
ATOM 2483 C CG2 . THR A 1 329 ? 121.762 128.065 113.828 1.00 53.84  ? 414 THR A CG2 1 
ATOM 2484 N N   . GLY A 1 330 ? 120.702 131.529 114.450 1.00 56.07  ? 415 GLY A N   1 
ATOM 2485 C CA  . GLY A 1 330 ? 120.146 132.469 113.485 1.00 52.95  ? 415 GLY A CA  1 
ATOM 2486 C C   . GLY A 1 330 ? 120.981 133.730 113.343 1.00 57.32  ? 415 GLY A C   1 
ATOM 2487 O O   . GLY A 1 330 ? 121.239 134.200 112.224 1.00 65.91  ? 415 GLY A O   1 
ATOM 2488 N N   . VAL A 1 331 ? 121.419 134.293 114.474 1.00 57.62  ? 416 VAL A N   1 
ATOM 2489 C CA  . VAL A 1 331 ? 122.263 135.485 114.429 1.00 58.03  ? 416 VAL A CA  1 
ATOM 2490 C C   . VAL A 1 331 ? 123.544 135.196 113.658 1.00 61.29  ? 416 VAL A C   1 
ATOM 2491 O O   . VAL A 1 331 ? 123.964 135.982 112.797 1.00 67.00  ? 416 VAL A O   1 
ATOM 2492 C CB  . VAL A 1 331 ? 122.563 135.981 115.856 1.00 56.94  ? 416 VAL A CB  1 
ATOM 2493 C CG1 . VAL A 1 331 ? 123.660 137.036 115.836 1.00 61.18  ? 416 VAL A CG1 1 
ATOM 2494 C CG2 . VAL A 1 331 ? 121.303 136.527 116.506 1.00 54.20  ? 416 VAL A CG2 1 
ATOM 2495 N N   . ALA A 1 332 ? 124.175 134.056 113.946 1.00 60.20  ? 417 ALA A N   1 
ATOM 2496 C CA  . ALA A 1 332 ? 125.386 133.672 113.241 1.00 58.07  ? 417 ALA A CA  1 
ATOM 2497 C C   . ALA A 1 332 ? 125.119 133.406 111.770 1.00 60.24  ? 417 ALA A C   1 
ATOM 2498 O O   . ALA A 1 332 ? 125.962 133.721 110.939 1.00 69.21  ? 417 ALA A O   1 
ATOM 2499 C CB  . ALA A 1 332 ? 126.012 132.446 113.898 1.00 62.12  ? 417 ALA A CB  1 
ATOM 2500 N N   . THR A 1 333 ? 123.969 132.829 111.423 1.00 61.14  ? 418 THR A N   1 
ATOM 2501 C CA  . THR A 1 333 ? 123.649 132.631 110.013 1.00 60.09  ? 418 THR A CA  1 
ATOM 2502 C C   . THR A 1 333 ? 123.629 133.964 109.277 1.00 67.35  ? 418 THR A C   1 
ATOM 2503 O O   . THR A 1 333 ? 124.247 134.113 108.215 1.00 76.12  ? 418 THR A O   1 
ATOM 2504 C CB  . THR A 1 333 ? 122.304 131.914 109.875 1.00 55.94  ? 418 THR A CB  1 
ATOM 2505 O OG1 . THR A 1 333 ? 122.453 130.535 110.235 1.00 54.18  ? 418 THR A OG1 1 
ATOM 2506 C CG2 . THR A 1 333 ? 121.793 132.006 108.445 1.00 58.13  ? 418 THR A CG2 1 
ATOM 2507 N N   . PHE A 1 334 ? 122.956 134.959 109.855 1.00 63.36  ? 419 PHE A N   1 
ATOM 2508 C CA  . PHE A 1 334 ? 122.898 136.280 109.228 1.00 65.89  ? 419 PHE A CA  1 
ATOM 2509 C C   . PHE A 1 334 ? 124.292 136.896 109.096 1.00 71.94  ? 419 PHE A C   1 
ATOM 2510 O O   . PHE A 1 334 ? 124.709 137.322 108.002 1.00 78.27  ? 419 PHE A O   1 
ATOM 2511 C CB  . PHE A 1 334 ? 121.977 137.187 110.046 1.00 65.69  ? 419 PHE A CB  1 
ATOM 2512 C CG  . PHE A 1 334 ? 121.600 138.463 109.354 1.00 69.64  ? 419 PHE A CG  1 
ATOM 2513 C CD1 . PHE A 1 334 ? 120.625 138.472 108.370 1.00 74.45  ? 419 PHE A CD1 1 
ATOM 2514 C CD2 . PHE A 1 334 ? 122.209 139.657 109.698 1.00 71.38  ? 419 PHE A CD2 1 
ATOM 2515 C CE1 . PHE A 1 334 ? 120.273 139.648 107.736 1.00 82.52  ? 419 PHE A CE1 1 
ATOM 2516 C CE2 . PHE A 1 334 ? 121.861 140.836 109.068 1.00 78.51  ? 419 PHE A CE2 1 
ATOM 2517 C CZ  . PHE A 1 334 ? 120.892 140.831 108.086 1.00 85.21  ? 419 PHE A CZ  1 
ATOM 2518 N N   . THR A 1 335 ? 125.036 136.941 110.207 1.00 66.16  ? 420 THR A N   1 
ATOM 2519 C CA  . THR A 1 335 ? 126.351 137.569 110.183 1.00 65.63  ? 420 THR A CA  1 
ATOM 2520 C C   . THR A 1 335 ? 127.344 136.816 109.307 1.00 68.68  ? 420 THR A C   1 
ATOM 2521 O O   . THR A 1 335 ? 128.196 137.452 108.687 1.00 76.55  ? 420 THR A O   1 
ATOM 2522 C CB  . THR A 1 335 ? 126.907 137.718 111.602 1.00 68.36  ? 420 THR A CB  1 
ATOM 2523 O OG1 . THR A 1 335 ? 127.266 136.432 112.123 1.00 75.17  ? 420 THR A OG1 1 
ATOM 2524 C CG2 . THR A 1 335 ? 125.890 138.393 112.514 1.00 71.11  ? 420 THR A CG2 1 
ATOM 2525 N N   . MET A 1 336 ? 127.253 135.487 109.234 1.00 66.84  ? 421 MET A N   1 
ATOM 2526 C CA  . MET A 1 336 ? 128.071 134.720 108.303 1.00 66.28  ? 421 MET A CA  1 
ATOM 2527 C C   . MET A 1 336 ? 127.696 134.976 106.856 1.00 70.95  ? 421 MET A C   1 
ATOM 2528 O O   . MET A 1 336 ? 128.573 134.976 105.994 1.00 73.19  ? 421 MET A O   1 
ATOM 2529 C CB  . MET A 1 336 ? 127.993 133.222 108.602 1.00 66.24  ? 421 MET A CB  1 
ATOM 2530 C CG  . MET A 1 336 ? 128.583 132.808 109.926 1.00 71.00  ? 421 MET A CG  1 
ATOM 2531 S SD  . MET A 1 336 ? 130.320 133.257 109.883 1.00 97.95  ? 421 MET A SD  1 
ATOM 2532 C CE  . MET A 1 336 ? 130.888 132.073 108.667 1.00 75.94  ? 421 MET A CE  1 
ATOM 2533 N N   . MET A 1 337 ? 126.416 135.184 106.550 1.00 71.81  ? 422 MET A N   1 
ATOM 2534 C CA  . MET A 1 337 ? 126.074 135.565 105.183 1.00 69.71  ? 422 MET A CA  1 
ATOM 2535 C C   . MET A 1 337 ? 126.771 136.867 104.802 1.00 73.57  ? 422 MET A C   1 
ATOM 2536 O O   . MET A 1 337 ? 127.411 136.967 103.744 1.00 77.28  ? 422 MET A O   1 
ATOM 2537 C CB  . MET A 1 337 ? 124.560 135.697 105.034 1.00 71.47  ? 422 MET A CB  1 
ATOM 2538 C CG  . MET A 1 337 ? 123.819 134.393 105.219 1.00 76.59  ? 422 MET A CG  1 
ATOM 2539 S SD  . MET A 1 337 ? 124.274 133.217 103.936 1.00 90.49  ? 422 MET A SD  1 
ATOM 2540 C CE  . MET A 1 337 ? 123.456 131.747 104.536 1.00 72.47  ? 422 MET A CE  1 
ATOM 2541 N N   . LEU A 1 338 ? 126.690 137.867 105.685 1.00 73.36  ? 423 LEU A N   1 
ATOM 2542 C CA  . LEU A 1 338 ? 127.335 139.146 105.385 1.00 72.44  ? 423 LEU A CA  1 
ATOM 2543 C C   . LEU A 1 338 ? 128.855 138.999 105.306 1.00 70.62  ? 423 LEU A C   1 
ATOM 2544 O O   . LEU A 1 338 ? 129.492 139.484 104.358 1.00 70.71  ? 423 LEU A O   1 
ATOM 2545 C CB  . LEU A 1 338 ? 126.936 140.196 106.423 1.00 72.26  ? 423 LEU A CB  1 
ATOM 2546 C CG  . LEU A 1 338 ? 125.599 140.924 106.225 1.00 76.30  ? 423 LEU A CG  1 
ATOM 2547 C CD1 . LEU A 1 338 ? 125.631 141.749 104.945 1.00 71.84  ? 423 LEU A CD1 1 
ATOM 2548 C CD2 . LEU A 1 338 ? 124.401 139.984 106.233 1.00 76.37  ? 423 LEU A CD2 1 
ATOM 2549 N N   . LEU A 1 339 ? 129.451 138.318 106.288 1.00 71.74  ? 424 LEU A N   1 
ATOM 2550 C CA  . LEU A 1 339 ? 130.898 138.143 106.321 1.00 72.94  ? 424 LEU A CA  1 
ATOM 2551 C C   . LEU A 1 339 ? 131.389 137.317 105.142 1.00 74.99  ? 424 LEU A C   1 
ATOM 2552 O O   . LEU A 1 339 ? 132.507 137.527 104.664 1.00 77.74  ? 424 LEU A O   1 
ATOM 2553 C CB  . LEU A 1 339 ? 131.306 137.495 107.647 1.00 74.88  ? 424 LEU A CB  1 
ATOM 2554 C CG  . LEU A 1 339 ? 132.786 137.328 108.003 1.00 83.34  ? 424 LEU A CG  1 
ATOM 2555 C CD1 . LEU A 1 339 ? 132.971 137.450 109.506 1.00 85.82  ? 424 LEU A CD1 1 
ATOM 2556 C CD2 . LEU A 1 339 ? 133.324 135.989 107.521 1.00 77.81  ? 424 LEU A CD2 1 
ATOM 2557 N N   . SER A 1 340 ? 130.572 136.383 104.656 1.00 75.30  ? 425 SER A N   1 
ATOM 2558 C CA  . SER A 1 340 ? 130.949 135.583 103.501 1.00 72.44  ? 425 SER A CA  1 
ATOM 2559 C C   . SER A 1 340 ? 130.930 136.418 102.233 1.00 70.90  ? 425 SER A C   1 
ATOM 2560 O O   . SER A 1 340 ? 131.856 136.335 101.416 1.00 71.62  ? 425 SER A O   1 
ATOM 2561 C CB  . SER A 1 340 ? 130.012 134.385 103.369 1.00 71.91  ? 425 SER A CB  1 
ATOM 2562 O OG  . SER A 1 340 ? 128.691 134.803 103.070 1.00 74.04  ? 425 SER A OG  1 
ATOM 2563 N N   . GLN A 1 341 ? 129.885 137.230 102.047 1.00 73.27  ? 426 GLN A N   1 
ATOM 2564 C CA  . GLN A 1 341 ? 129.893 138.129 100.898 1.00 71.15  ? 426 GLN A CA  1 
ATOM 2565 C C   . GLN A 1 341 ? 131.053 139.112 100.963 1.00 72.56  ? 426 GLN A C   1 
ATOM 2566 O O   . GLN A 1 341 ? 131.524 139.571 99.917  1.00 75.26  ? 426 GLN A O   1 
ATOM 2567 C CB  . GLN A 1 341 ? 128.573 138.891 100.788 1.00 76.51  ? 426 GLN A CB  1 
ATOM 2568 C CG  . GLN A 1 341 ? 128.342 139.475 99.400  1.00 83.77  ? 426 GLN A CG  1 
ATOM 2569 C CD  . GLN A 1 341 ? 128.548 140.975 99.343  1.00 91.03  ? 426 GLN A CD  1 
ATOM 2570 O OE1 . GLN A 1 341 ? 128.685 141.636 100.372 1.00 91.12  ? 426 GLN A OE1 1 
ATOM 2571 N NE2 . GLN A 1 341 ? 128.575 141.522 98.133  1.00 86.33  ? 426 GLN A NE2 1 
ATOM 2572 N N   . TYR A 1 342 ? 131.526 139.444 102.167 1.00 77.03  ? 427 TYR A N   1 
ATOM 2573 C CA  . TYR A 1 342 ? 132.701 140.305 102.283 1.00 74.98  ? 427 TYR A CA  1 
ATOM 2574 C C   . TYR A 1 342 ? 133.989 139.561 101.929 1.00 74.51  ? 427 TYR A C   1 
ATOM 2575 O O   . TYR A 1 342 ? 134.793 140.045 101.121 1.00 77.21  ? 427 TYR A O   1 
ATOM 2576 C CB  . TYR A 1 342 ? 132.775 140.892 103.697 1.00 76.27  ? 427 TYR A CB  1 
ATOM 2577 C CG  . TYR A 1 342 ? 134.138 141.413 104.105 1.00 80.13  ? 427 TYR A CG  1 
ATOM 2578 C CD1 . TYR A 1 342 ? 135.069 140.584 104.724 1.00 84.22  ? 427 TYR A CD1 1 
ATOM 2579 C CD2 . TYR A 1 342 ? 134.497 142.733 103.866 1.00 80.21  ? 427 TYR A CD2 1 
ATOM 2580 C CE1 . TYR A 1 342 ? 136.312 141.057 105.096 1.00 85.20  ? 427 TYR A CE1 1 
ATOM 2581 C CE2 . TYR A 1 342 ? 135.739 143.214 104.234 1.00 83.34  ? 427 TYR A CE2 1 
ATOM 2582 C CZ  . TYR A 1 342 ? 136.642 142.372 104.848 1.00 86.89  ? 427 TYR A CZ  1 
ATOM 2583 O OH  . TYR A 1 342 ? 137.880 142.846 105.217 1.00 89.45  ? 427 TYR A OH  1 
ATOM 2584 N N   . VAL A 1 343 ? 134.203 138.385 102.527 1.00 74.73  ? 428 VAL A N   1 
ATOM 2585 C CA  . VAL A 1 343 ? 135.463 137.668 102.347 1.00 75.57  ? 428 VAL A CA  1 
ATOM 2586 C C   . VAL A 1 343 ? 135.611 137.185 100.911 1.00 77.10  ? 428 VAL A C   1 
ATOM 2587 O O   . VAL A 1 343 ? 136.726 137.146 100.376 1.00 82.15  ? 428 VAL A O   1 
ATOM 2588 C CB  . VAL A 1 343 ? 135.582 136.504 103.355 1.00 74.14  ? 428 VAL A CB  1 
ATOM 2589 C CG1 . VAL A 1 343 ? 134.454 135.507 103.179 1.00 72.70  ? 428 VAL A CG1 1 
ATOM 2590 C CG2 . VAL A 1 343 ? 136.931 135.809 103.227 1.00 73.23  ? 428 VAL A CG2 1 
ATOM 2591 N N   . PHE A 1 344 ? 134.506 136.811 100.259 1.00 75.88  ? 429 PHE A N   1 
ATOM 2592 C CA  . PHE A 1 344 ? 134.585 136.411 98.859  1.00 71.15  ? 429 PHE A CA  1 
ATOM 2593 C C   . PHE A 1 344 ? 135.011 137.579 97.980  1.00 75.88  ? 429 PHE A C   1 
ATOM 2594 O O   . PHE A 1 344 ? 135.799 137.405 97.043  1.00 79.70  ? 429 PHE A O   1 
ATOM 2595 C CB  . PHE A 1 344 ? 133.241 135.851 98.401  1.00 60.52  ? 429 PHE A CB  1 
ATOM 2596 C CG  . PHE A 1 344 ? 133.102 134.374 98.611  1.00 55.53  ? 429 PHE A CG  1 
ATOM 2597 C CD1 . PHE A 1 344 ? 133.914 133.485 97.928  1.00 55.17  ? 429 PHE A CD1 1 
ATOM 2598 C CD2 . PHE A 1 344 ? 132.169 133.874 99.502  1.00 61.10  ? 429 PHE A CD2 1 
ATOM 2599 C CE1 . PHE A 1 344 ? 133.790 132.125 98.124  1.00 59.94  ? 429 PHE A CE1 1 
ATOM 2600 C CE2 . PHE A 1 344 ? 132.041 132.516 99.703  1.00 61.64  ? 429 PHE A CE2 1 
ATOM 2601 C CZ  . PHE A 1 344 ? 132.852 131.642 99.013  1.00 60.82  ? 429 PHE A CZ  1 
ATOM 2602 N N   . ASN A 1 345 ? 134.495 138.775 98.265  1.00 76.03  ? 430 ASN A N   1 
ATOM 2603 C CA  . ASN A 1 345 ? 134.898 139.958 97.513  1.00 78.87  ? 430 ASN A CA  1 
ATOM 2604 C C   . ASN A 1 345 ? 136.368 140.287 97.746  1.00 83.38  ? 430 ASN A C   1 
ATOM 2605 O O   . ASN A 1 345 ? 137.096 140.601 96.797  1.00 87.82  ? 430 ASN A O   1 
ATOM 2606 C CB  . ASN A 1 345 ? 134.014 141.146 97.901  1.00 82.21  ? 430 ASN A CB  1 
ATOM 2607 C CG  . ASN A 1 345 ? 134.233 142.363 97.015  1.00 92.85  ? 430 ASN A CG  1 
ATOM 2608 O OD1 . ASN A 1 345 ? 135.069 142.353 96.111  1.00 94.71  ? 430 ASN A OD1 1 
ATOM 2609 N ND2 . ASN A 1 345 ? 133.481 143.424 97.279  1.00 97.01  ? 430 ASN A ND2 1 
ATOM 2610 N N   . LYS A 1 346 ? 136.828 140.208 98.995  1.00 81.56  ? 431 LYS A N   1 
ATOM 2611 C CA  . LYS A 1 346 ? 138.155 140.719 99.329  1.00 78.88  ? 431 LYS A CA  1 
ATOM 2612 C C   . LYS A 1 346 ? 139.257 139.675 99.152  1.00 78.49  ? 431 LYS A C   1 
ATOM 2613 O O   . LYS A 1 346 ? 140.187 139.874 98.364  1.00 81.41  ? 431 LYS A O   1 
ATOM 2614 C CB  . LYS A 1 346 ? 138.161 141.257 100.764 1.00 80.95  ? 431 LYS A CB  1 
ATOM 2615 C CG  . LYS A 1 346 ? 139.491 141.858 101.187 1.00 83.99  ? 431 LYS A CG  1 
ATOM 2616 C CD  . LYS A 1 346 ? 139.316 142.827 102.343 1.00 87.75  ? 431 LYS A CD  1 
ATOM 2617 C CE  . LYS A 1 346 ? 140.656 143.333 102.850 1.00 92.53  ? 431 LYS A CE  1 
ATOM 2618 N NZ  . LYS A 1 346 ? 140.491 144.328 103.945 1.00 95.42  ? 431 LYS A NZ  1 
ATOM 2619 N N   . TYR A 1 347 ? 139.167 138.560 99.876  1.00 79.22  ? 432 TYR A N   1 
ATOM 2620 C CA  . TYR A 1 347 ? 140.295 137.642 99.981  1.00 78.41  ? 432 TYR A CA  1 
ATOM 2621 C C   . TYR A 1 347 ? 140.320 136.573 98.894  1.00 80.04  ? 432 TYR A C   1 
ATOM 2622 O O   . TYR A 1 347 ? 141.405 136.112 98.522  1.00 81.35  ? 432 TYR A O   1 
ATOM 2623 C CB  . TYR A 1 347 ? 140.298 136.984 101.362 1.00 76.09  ? 432 TYR A CB  1 
ATOM 2624 C CG  . TYR A 1 347 ? 140.415 137.978 102.496 1.00 79.48  ? 432 TYR A CG  1 
ATOM 2625 C CD1 . TYR A 1 347 ? 141.635 138.563 102.808 1.00 85.00  ? 432 TYR A CD1 1 
ATOM 2626 C CD2 . TYR A 1 347 ? 139.304 138.345 103.243 1.00 80.04  ? 432 TYR A CD2 1 
ATOM 2627 C CE1 . TYR A 1 347 ? 141.747 139.476 103.839 1.00 90.08  ? 432 TYR A CE1 1 
ATOM 2628 C CE2 . TYR A 1 347 ? 139.406 139.257 104.276 1.00 86.97  ? 432 TYR A CE2 1 
ATOM 2629 C CZ  . TYR A 1 347 ? 140.629 139.819 104.570 1.00 93.58  ? 432 TYR A CZ  1 
ATOM 2630 O OH  . TYR A 1 347 ? 140.735 140.728 105.597 1.00 100.53 ? 432 TYR A OH  1 
ATOM 2631 N N   . GLY A 1 348 ? 139.170 136.165 98.379  1.00 76.73  ? 433 GLY A N   1 
ATOM 2632 C CA  . GLY A 1 348 ? 139.118 135.246 97.261  1.00 72.77  ? 433 GLY A CA  1 
ATOM 2633 C C   . GLY A 1 348 ? 138.634 133.864 97.662  1.00 68.70  ? 433 GLY A C   1 
ATOM 2634 O O   . GLY A 1 348 ? 138.111 133.639 98.758  1.00 71.45  ? 433 GLY A O   1 
ATOM 2635 N N   . TRP A 1 349 ? 138.823 132.921 96.735  1.00 67.68  ? 434 TRP A N   1 
ATOM 2636 C CA  . TRP A 1 349 ? 138.302 131.571 96.924  1.00 62.59  ? 434 TRP A CA  1 
ATOM 2637 C C   . TRP A 1 349 ? 139.120 130.787 97.943  1.00 65.12  ? 434 TRP A C   1 
ATOM 2638 O O   . TRP A 1 349 ? 138.561 130.008 98.722  1.00 68.10  ? 434 TRP A O   1 
ATOM 2639 C CB  . TRP A 1 349 ? 138.267 130.832 95.584  1.00 61.47  ? 434 TRP A CB  1 
ATOM 2640 C CG  . TRP A 1 349 ? 137.564 129.504 95.632  1.00 60.92  ? 434 TRP A CG  1 
ATOM 2641 C CD1 . TRP A 1 349 ? 136.264 129.254 95.299  1.00 60.60  ? 434 TRP A CD1 1 
ATOM 2642 C CD2 . TRP A 1 349 ? 138.128 128.242 96.016  1.00 61.61  ? 434 TRP A CD2 1 
ATOM 2643 N NE1 . TRP A 1 349 ? 135.981 127.920 95.461  1.00 59.09  ? 434 TRP A NE1 1 
ATOM 2644 C CE2 . TRP A 1 349 ? 137.108 127.276 95.900  1.00 59.45  ? 434 TRP A CE2 1 
ATOM 2645 C CE3 . TRP A 1 349 ? 139.394 127.835 96.450  1.00 62.27  ? 434 TRP A CE3 1 
ATOM 2646 C CZ2 . TRP A 1 349 ? 137.314 125.932 96.202  1.00 54.82  ? 434 TRP A CZ2 1 
ATOM 2647 C CZ3 . TRP A 1 349 ? 139.595 126.500 96.751  1.00 61.60  ? 434 TRP A CZ3 1 
ATOM 2648 C CH2 . TRP A 1 349 ? 138.561 125.565 96.625  1.00 57.19  ? 434 TRP A CH2 1 
ATOM 2649 N N   . GLY A 1 350 ? 140.442 130.964 97.943  1.00 62.95  ? 435 GLY A N   1 
ATOM 2650 C CA  . GLY A 1 350 ? 141.283 130.161 98.818  1.00 61.12  ? 435 GLY A CA  1 
ATOM 2651 C C   . GLY A 1 350 ? 141.050 130.437 100.291 1.00 65.04  ? 435 GLY A C   1 
ATOM 2652 O O   . GLY A 1 350 ? 140.927 129.510 101.099 1.00 70.10  ? 435 GLY A O   1 
ATOM 2653 N N   . VAL A 1 351 ? 140.990 131.717 100.660 1.00 62.84  ? 436 VAL A N   1 
ATOM 2654 C CA  . VAL A 1 351 ? 140.798 132.073 102.063 1.00 59.98  ? 436 VAL A CA  1 
ATOM 2655 C C   . VAL A 1 351 ? 139.449 131.565 102.554 1.00 59.45  ? 436 VAL A C   1 
ATOM 2656 O O   . VAL A 1 351 ? 139.349 130.955 103.623 1.00 65.44  ? 436 VAL A O   1 
ATOM 2657 C CB  . VAL A 1 351 ? 140.936 133.594 102.254 1.00 64.43  ? 436 VAL A CB  1 
ATOM 2658 C CG1 . VAL A 1 351 ? 140.348 134.021 103.591 1.00 63.46  ? 436 VAL A CG1 1 
ATOM 2659 C CG2 . VAL A 1 351 ? 142.395 134.011 102.147 1.00 71.89  ? 436 VAL A CG2 1 
ATOM 2660 N N   . ALA A 1 352 ? 138.394 131.795 101.768 1.00 57.47  ? 437 ALA A N   1 
ATOM 2661 C CA  . ALA A 1 352 ? 137.064 131.342 102.161 1.00 57.40  ? 437 ALA A CA  1 
ATOM 2662 C C   . ALA A 1 352 ? 136.976 129.822 102.205 1.00 58.96  ? 437 ALA A C   1 
ATOM 2663 O O   . ALA A 1 352 ? 136.255 129.269 103.043 1.00 60.38  ? 437 ALA A O   1 
ATOM 2664 C CB  . ALA A 1 352 ? 136.013 131.911 101.208 1.00 58.71  ? 437 ALA A CB  1 
ATOM 2665 N N   . ALA A 1 353 ? 137.693 129.133 101.316 1.00 59.17  ? 438 ALA A N   1 
ATOM 2666 C CA  . ALA A 1 353 ? 137.689 127.675 101.331 1.00 59.94  ? 438 ALA A CA  1 
ATOM 2667 C C   . ALA A 1 353 ? 138.433 127.126 102.539 1.00 59.19  ? 438 ALA A C   1 
ATOM 2668 O O   . ALA A 1 353 ? 138.077 126.058 103.049 1.00 64.26  ? 438 ALA A O   1 
ATOM 2669 C CB  . ALA A 1 353 ? 138.299 127.132 100.040 1.00 56.93  ? 438 ALA A CB  1 
ATOM 2670 N N   . LYS A 1 354 ? 139.465 127.828 103.005 1.00 58.02  ? 439 LYS A N   1 
ATOM 2671 C CA  . LYS A 1 354 ? 140.211 127.367 104.169 1.00 55.38  ? 439 LYS A CA  1 
ATOM 2672 C C   . LYS A 1 354 ? 139.618 127.820 105.497 1.00 55.32  ? 439 LYS A C   1 
ATOM 2673 O O   . LYS A 1 354 ? 139.965 127.243 106.531 1.00 57.66  ? 439 LYS A O   1 
ATOM 2674 C CB  . LYS A 1 354 ? 141.670 127.829 104.092 1.00 55.80  ? 439 LYS A CB  1 
ATOM 2675 C CG  . LYS A 1 354 ? 142.460 127.224 102.944 1.00 56.01  ? 439 LYS A CG  1 
ATOM 2676 C CD  . LYS A 1 354 ? 143.666 128.079 102.593 1.00 53.67  ? 439 LYS A CD  1 
ATOM 2677 C CE  . LYS A 1 354 ? 144.129 127.826 101.169 1.00 57.89  ? 439 LYS A CE  1 
ATOM 2678 N NZ  . LYS A 1 354 ? 145.160 128.810 100.740 1.00 62.24  ? 439 LYS A NZ  1 
ATOM 2679 N N   . ILE A 1 355 ? 138.738 128.826 105.504 1.00 59.82  ? 440 ILE A N   1 
ATOM 2680 C CA  . ILE A 1 355 ? 138.214 129.327 106.776 1.00 56.49  ? 440 ILE A CA  1 
ATOM 2681 C C   . ILE A 1 355 ? 137.470 128.229 107.527 1.00 56.57  ? 440 ILE A C   1 
ATOM 2682 O O   . ILE A 1 355 ? 137.648 128.060 108.740 1.00 61.52  ? 440 ILE A O   1 
ATOM 2683 C CB  . ILE A 1 355 ? 137.320 130.562 106.556 1.00 53.55  ? 440 ILE A CB  1 
ATOM 2684 C CG1 . ILE A 1 355 ? 138.160 131.792 106.217 1.00 50.66  ? 440 ILE A CG1 1 
ATOM 2685 C CG2 . ILE A 1 355 ? 136.518 130.861 107.810 1.00 54.44  ? 440 ILE A CG2 1 
ATOM 2686 C CD1 . ILE A 1 355 ? 137.352 133.064 106.069 1.00 51.37  ? 440 ILE A CD1 1 
ATOM 2687 N N   . THR A 1 356 ? 136.625 127.464 106.825 1.00 57.92  ? 441 THR A N   1 
ATOM 2688 C CA  . THR A 1 356 ? 135.842 126.435 107.510 1.00 58.33  ? 441 THR A CA  1 
ATOM 2689 C C   . THR A 1 356 ? 136.718 125.362 108.149 1.00 56.53  ? 441 THR A C   1 
ATOM 2690 O O   . THR A 1 356 ? 136.559 125.109 109.358 1.00 61.68  ? 441 THR A O   1 
ATOM 2691 C CB  . THR A 1 356 ? 134.812 125.833 106.545 1.00 57.62  ? 441 THR A CB  1 
ATOM 2692 O OG1 . THR A 1 356 ? 134.156 126.882 105.822 1.00 64.13  ? 441 THR A OG1 1 
ATOM 2693 C CG2 . THR A 1 356 ? 133.777 125.018 107.306 1.00 52.44  ? 441 THR A CG2 1 
ATOM 2694 N N   . PRO A 1 357 ? 137.643 124.702 107.435 1.00 52.46  ? 442 PRO A N   1 
ATOM 2695 C CA  . PRO A 1 357 ? 138.461 123.678 108.105 1.00 48.89  ? 442 PRO A CA  1 
ATOM 2696 C C   . PRO A 1 357 ? 139.329 124.222 109.227 1.00 54.77  ? 442 PRO A C   1 
ATOM 2697 O O   . PRO A 1 357 ? 139.484 123.539 110.242 1.00 61.83  ? 442 PRO A O   1 
ATOM 2698 C CB  . PRO A 1 357 ? 139.309 123.096 106.964 1.00 48.70  ? 442 PRO A CB  1 
ATOM 2699 C CG  . PRO A 1 357 ? 139.300 124.129 105.910 1.00 53.25  ? 442 PRO A CG  1 
ATOM 2700 C CD  . PRO A 1 357 ? 137.960 124.779 105.997 1.00 56.09  ? 442 PRO A CD  1 
ATOM 2701 N N   . THR A 1 358 ? 139.884 125.431 109.093 1.00 52.20  ? 443 THR A N   1 
ATOM 2702 C CA  . THR A 1 358 ? 140.718 125.971 110.166 1.00 46.96  ? 443 THR A CA  1 
ATOM 2703 C C   . THR A 1 358 ? 139.905 126.262 111.422 1.00 55.12  ? 443 THR A C   1 
ATOM 2704 O O   . THR A 1 358 ? 140.344 125.948 112.534 1.00 65.05  ? 443 THR A O   1 
ATOM 2705 C CB  . THR A 1 358 ? 141.445 127.238 109.707 1.00 51.68  ? 443 THR A CB  1 
ATOM 2706 O OG1 . THR A 1 358 ? 140.494 128.281 109.456 1.00 61.08  ? 443 THR A OG1 1 
ATOM 2707 C CG2 . THR A 1 358 ? 142.291 126.974 108.474 1.00 51.45  ? 443 THR A CG2 1 
ATOM 2708 N N   . VAL A 1 359 ? 138.732 126.879 111.272 1.00 55.14  ? 444 VAL A N   1 
ATOM 2709 C CA  . VAL A 1 359 ? 137.914 127.173 112.445 1.00 53.81  ? 444 VAL A CA  1 
ATOM 2710 C C   . VAL A 1 359 ? 137.432 125.881 113.090 1.00 58.78  ? 444 VAL A C   1 
ATOM 2711 O O   . VAL A 1 359 ? 137.447 125.743 114.321 1.00 65.16  ? 444 VAL A O   1 
ATOM 2712 C CB  . VAL A 1 359 ? 136.739 128.094 112.074 1.00 55.39  ? 444 VAL A CB  1 
ATOM 2713 C CG1 . VAL A 1 359 ? 135.761 128.191 113.236 1.00 57.25  ? 444 VAL A CG1 1 
ATOM 2714 C CG2 . VAL A 1 359 ? 137.245 129.472 111.680 1.00 56.41  ? 444 VAL A CG2 1 
ATOM 2715 N N   . LEU A 1 360 ? 137.001 124.913 112.274 1.00 64.23  ? 445 LEU A N   1 
ATOM 2716 C CA  . LEU A 1 360 ? 136.594 123.627 112.831 1.00 61.43  ? 445 LEU A CA  1 
ATOM 2717 C C   . LEU A 1 360 ? 137.755 122.947 113.545 1.00 58.60  ? 445 LEU A C   1 
ATOM 2718 O O   . LEU A 1 360 ? 137.570 122.365 114.615 1.00 61.53  ? 445 LEU A O   1 
ATOM 2719 C CB  . LEU A 1 360 ? 136.022 122.724 111.738 1.00 56.67  ? 445 LEU A CB  1 
ATOM 2720 C CG  . LEU A 1 360 ? 134.660 123.145 111.182 1.00 59.83  ? 445 LEU A CG  1 
ATOM 2721 C CD1 . LEU A 1 360 ? 134.042 122.025 110.361 1.00 62.58  ? 445 LEU A CD1 1 
ATOM 2722 C CD2 . LEU A 1 360 ? 133.726 123.563 112.309 1.00 64.23  ? 445 LEU A CD2 1 
ATOM 2723 N N   . LEU A 1 361 ? 138.963 123.037 112.984 1.00 59.00  ? 446 LEU A N   1 
ATOM 2724 C CA  . LEU A 1 361 ? 140.137 122.453 113.624 1.00 59.29  ? 446 LEU A CA  1 
ATOM 2725 C C   . LEU A 1 361 ? 140.422 123.105 114.970 1.00 64.29  ? 446 LEU A C   1 
ATOM 2726 O O   . LEU A 1 361 ? 140.633 122.414 115.971 1.00 68.89  ? 446 LEU A O   1 
ATOM 2727 C CB  . LEU A 1 361 ? 141.347 122.582 112.699 1.00 55.78  ? 446 LEU A CB  1 
ATOM 2728 C CG  . LEU A 1 361 ? 142.693 122.142 113.276 1.00 59.19  ? 446 LEU A CG  1 
ATOM 2729 C CD1 . LEU A 1 361 ? 142.655 120.687 113.684 1.00 61.81  ? 446 LEU A CD1 1 
ATOM 2730 C CD2 . LEU A 1 361 ? 143.805 122.387 112.268 1.00 63.19  ? 446 LEU A CD2 1 
ATOM 2731 N N   . LEU A 1 362 ? 140.442 124.438 115.013 1.00 61.64  ? 447 LEU A N   1 
ATOM 2732 C CA  . LEU A 1 362 ? 140.752 125.132 116.261 1.00 58.85  ? 447 LEU A CA  1 
ATOM 2733 C C   . LEU A 1 362 ? 139.708 124.826 117.328 1.00 62.47  ? 447 LEU A C   1 
ATOM 2734 O O   . LEU A 1 362 ? 140.045 124.471 118.469 1.00 70.64  ? 447 LEU A O   1 
ATOM 2735 C CB  . LEU A 1 362 ? 140.842 126.638 116.012 1.00 60.09  ? 447 LEU A CB  1 
ATOM 2736 C CG  . LEU A 1 362 ? 141.961 127.144 115.098 1.00 65.96  ? 447 LEU A CG  1 
ATOM 2737 C CD1 . LEU A 1 362 ? 142.191 128.635 115.302 1.00 66.85  ? 447 LEU A CD1 1 
ATOM 2738 C CD2 . LEU A 1 362 ? 143.247 126.364 115.327 1.00 65.14  ? 447 LEU A CD2 1 
ATOM 2739 N N   . THR A 1 363 ? 138.428 124.949 116.968 1.00 60.02  ? 448 THR A N   1 
ATOM 2740 C CA  . THR A 1 363 ? 137.364 124.682 117.926 1.00 61.16  ? 448 THR A CA  1 
ATOM 2741 C C   . THR A 1 363 ? 137.354 123.223 118.360 1.00 63.97  ? 448 THR A C   1 
ATOM 2742 O O   . THR A 1 363 ? 137.102 122.935 119.532 1.00 67.29  ? 448 THR A O   1 
ATOM 2743 C CB  . THR A 1 363 ? 136.012 125.076 117.332 1.00 63.42  ? 448 THR A CB  1 
ATOM 2744 O OG1 . THR A 1 363 ? 135.875 124.499 116.028 1.00 68.39  ? 448 THR A OG1 1 
ATOM 2745 C CG2 . THR A 1 363 ? 135.897 126.590 117.229 1.00 60.26  ? 448 THR A CG2 1 
ATOM 2746 N N   . GLY A 1 364 ? 137.635 122.292 117.446 1.00 62.75  ? 449 GLY A N   1 
ATOM 2747 C CA  . GLY A 1 364 ? 137.680 120.890 117.819 1.00 60.34  ? 449 GLY A CA  1 
ATOM 2748 C C   . GLY A 1 364 ? 138.845 120.558 118.729 1.00 63.34  ? 449 GLY A C   1 
ATOM 2749 O O   . GLY A 1 364 ? 138.709 119.746 119.644 1.00 68.40  ? 449 GLY A O   1 
ATOM 2750 N N   . VAL A 1 365 ? 140.009 121.166 118.487 1.00 60.68  ? 450 VAL A N   1 
ATOM 2751 C CA  . VAL A 1 365 ? 141.141 120.956 119.383 1.00 59.71  ? 450 VAL A CA  1 
ATOM 2752 C C   . VAL A 1 365 ? 140.817 121.477 120.775 1.00 64.39  ? 450 VAL A C   1 
ATOM 2753 O O   . VAL A 1 365 ? 141.055 120.793 121.776 1.00 68.72  ? 450 VAL A O   1 
ATOM 2754 C CB  . VAL A 1 365 ? 142.418 121.603 118.815 1.00 59.19  ? 450 VAL A CB  1 
ATOM 2755 C CG1 . VAL A 1 365 ? 143.547 121.507 119.826 1.00 62.81  ? 450 VAL A CG1 1 
ATOM 2756 C CG2 . VAL A 1 365 ? 142.831 120.908 117.531 1.00 56.34  ? 450 VAL A CG2 1 
ATOM 2757 N N   . ALA A 1 366 ? 140.238 122.679 120.862 1.00 64.21  ? 451 ALA A N   1 
ATOM 2758 C CA  . ALA A 1 366 ? 139.847 123.202 122.171 1.00 62.57  ? 451 ALA A CA  1 
ATOM 2759 C C   . ALA A 1 366 ? 138.802 122.310 122.835 1.00 67.03  ? 451 ALA A C   1 
ATOM 2760 O O   . ALA A 1 366 ? 138.889 122.014 124.035 1.00 75.88  ? 451 ALA A O   1 
ATOM 2761 C CB  . ALA A 1 366 ? 139.324 124.631 122.032 1.00 60.49  ? 451 ALA A CB  1 
ATOM 2762 N N   . PHE A 1 367 ? 137.817 121.858 122.057 1.00 65.27  ? 452 PHE A N   1 
ATOM 2763 C CA  . PHE A 1 367 ? 136.740 121.025 122.580 1.00 60.77  ? 452 PHE A CA  1 
ATOM 2764 C C   . PHE A 1 367 ? 137.278 119.708 123.126 1.00 62.81  ? 452 PHE A C   1 
ATOM 2765 O O   . PHE A 1 367 ? 137.047 119.364 124.292 1.00 70.48  ? 452 PHE A O   1 
ATOM 2766 C CB  . PHE A 1 367 ? 135.718 120.810 121.457 1.00 59.91  ? 452 PHE A CB  1 
ATOM 2767 C CG  . PHE A 1 367 ? 134.569 119.915 121.813 1.00 59.05  ? 452 PHE A CG  1 
ATOM 2768 C CD1 . PHE A 1 367 ? 133.645 120.292 122.770 1.00 59.39  ? 452 PHE A CD1 1 
ATOM 2769 C CD2 . PHE A 1 367 ? 134.364 118.733 121.121 1.00 57.64  ? 452 PHE A CD2 1 
ATOM 2770 C CE1 . PHE A 1 367 ? 132.572 119.476 123.074 1.00 53.97  ? 452 PHE A CE1 1 
ATOM 2771 C CE2 . PHE A 1 367 ? 133.287 117.919 121.413 1.00 53.58  ? 452 PHE A CE2 1 
ATOM 2772 C CZ  . PHE A 1 367 ? 132.393 118.291 122.394 1.00 52.87  ? 452 PHE A CZ  1 
ATOM 2773 N N   . PHE A 1 368 ? 138.052 118.985 122.313 1.00 60.32  ? 453 PHE A N   1 
ATOM 2774 C CA  . PHE A 1 368 ? 138.590 117.700 122.735 1.00 62.95  ? 453 PHE A CA  1 
ATOM 2775 C C   . PHE A 1 368 ? 139.669 117.843 123.800 1.00 72.23  ? 453 PHE A C   1 
ATOM 2776 O O   . PHE A 1 368 ? 139.922 116.883 124.533 1.00 82.92  ? 453 PHE A O   1 
ATOM 2777 C CB  . PHE A 1 368 ? 139.132 116.936 121.527 1.00 63.34  ? 453 PHE A CB  1 
ATOM 2778 C CG  . PHE A 1 368 ? 138.061 116.286 120.693 1.00 66.56  ? 453 PHE A CG  1 
ATOM 2779 C CD1 . PHE A 1 368 ? 137.264 117.045 119.851 1.00 63.40  ? 453 PHE A CD1 1 
ATOM 2780 C CD2 . PHE A 1 368 ? 137.847 114.920 120.754 1.00 70.89  ? 453 PHE A CD2 1 
ATOM 2781 C CE1 . PHE A 1 368 ? 136.277 116.454 119.085 1.00 64.64  ? 453 PHE A CE1 1 
ATOM 2782 C CE2 . PHE A 1 368 ? 136.861 114.322 119.989 1.00 70.68  ? 453 PHE A CE2 1 
ATOM 2783 C CZ  . PHE A 1 368 ? 136.076 115.091 119.154 1.00 68.39  ? 453 PHE A CZ  1 
ATOM 2784 N N   . SER A 1 369 ? 140.304 119.012 123.916 1.00 68.62  ? 454 SER A N   1 
ATOM 2785 C CA  . SER A 1 369 ? 141.222 119.238 125.026 1.00 68.13  ? 454 SER A CA  1 
ATOM 2786 C C   . SER A 1 369 ? 140.460 119.412 126.332 1.00 72.32  ? 454 SER A C   1 
ATOM 2787 O O   . SER A 1 369 ? 140.840 118.847 127.365 1.00 80.92  ? 454 SER A O   1 
ATOM 2788 C CB  . SER A 1 369 ? 142.099 120.457 124.744 1.00 70.81  ? 454 SER A CB  1 
ATOM 2789 O OG  . SER A 1 369 ? 141.314 121.628 124.606 1.00 75.23  ? 454 SER A OG  1 
ATOM 2790 N N   . LEU A 1 370 ? 139.378 120.197 126.307 1.00 70.79  ? 455 LEU A N   1 
ATOM 2791 C CA  . LEU A 1 370 ? 138.560 120.350 127.507 1.00 70.24  ? 455 LEU A CA  1 
ATOM 2792 C C   . LEU A 1 370 ? 137.877 119.043 127.890 1.00 75.71  ? 455 LEU A C   1 
ATOM 2793 O O   . LEU A 1 370 ? 137.587 118.817 129.071 1.00 81.07  ? 455 LEU A O   1 
ATOM 2794 C CB  . LEU A 1 370 ? 137.524 121.458 127.307 1.00 65.90  ? 455 LEU A CB  1 
ATOM 2795 C CG  . LEU A 1 370 ? 138.083 122.879 127.210 1.00 65.94  ? 455 LEU A CG  1 
ATOM 2796 C CD1 . LEU A 1 370 ? 137.164 123.766 126.388 1.00 66.39  ? 455 LEU A CD1 1 
ATOM 2797 C CD2 . LEU A 1 370 ? 138.299 123.461 128.599 1.00 69.84  ? 455 LEU A CD2 1 
ATOM 2798 N N   . ILE A 1 371 ? 137.610 118.175 126.914 1.00 73.54  ? 456 ILE A N   1 
ATOM 2799 C CA  . ILE A 1 371 ? 137.074 116.848 127.221 1.00 69.44  ? 456 ILE A CA  1 
ATOM 2800 C C   . ILE A 1 371 ? 138.150 115.945 127.809 1.00 75.85  ? 456 ILE A C   1 
ATOM 2801 O O   . ILE A 1 371 ? 138.032 115.469 128.944 1.00 78.15  ? 456 ILE A O   1 
ATOM 2802 C CB  . ILE A 1 371 ? 136.443 116.206 125.973 1.00 63.82  ? 456 ILE A CB  1 
ATOM 2803 C CG1 . ILE A 1 371 ? 135.412 117.132 125.332 1.00 63.30  ? 456 ILE A CG1 1 
ATOM 2804 C CG2 . ILE A 1 371 ? 135.888 114.821 126.295 1.00 67.17  ? 456 ILE A CG2 1 
ATOM 2805 C CD1 . ILE A 1 371 ? 134.811 116.548 124.092 1.00 62.38  ? 456 ILE A CD1 1 
ATOM 2806 N N   . LEU A 1 372 ? 139.204 115.676 127.034 1.00 75.54  ? 457 LEU A N   1 
ATOM 2807 C CA  . LEU A 1 372 ? 140.197 114.685 127.439 1.00 76.76  ? 457 LEU A CA  1 
ATOM 2808 C C   . LEU A 1 372 ? 140.932 115.111 128.702 1.00 81.91  ? 457 LEU A C   1 
ATOM 2809 O O   . LEU A 1 372 ? 141.132 114.300 129.615 1.00 89.16  ? 457 LEU A O   1 
ATOM 2810 C CB  . LEU A 1 372 ? 141.182 114.445 126.296 1.00 76.42  ? 457 LEU A CB  1 
ATOM 2811 C CG  . LEU A 1 372 ? 140.654 113.591 125.143 1.00 71.64  ? 457 LEU A CG  1 
ATOM 2812 C CD1 . LEU A 1 372 ? 141.505 113.783 123.898 1.00 72.05  ? 457 LEU A CD1 1 
ATOM 2813 C CD2 . LEU A 1 372 ? 140.608 112.126 125.543 1.00 73.68  ? 457 LEU A CD2 1 
ATOM 2814 N N   . PHE A 1 373 ? 141.338 116.375 128.779 1.00 82.04  ? 458 PHE A N   1 
ATOM 2815 C CA  . PHE A 1 373 ? 142.043 116.907 129.940 1.00 87.51  ? 458 PHE A CA  1 
ATOM 2816 C C   . PHE A 1 373 ? 141.151 117.964 130.584 1.00 91.29  ? 458 PHE A C   1 
ATOM 2817 O O   . PHE A 1 373 ? 141.276 119.161 130.324 1.00 93.69  ? 458 PHE A O   1 
ATOM 2818 C CB  . PHE A 1 373 ? 143.408 117.480 129.538 1.00 88.55  ? 458 PHE A CB  1 
ATOM 2819 C CG  . PHE A 1 373 ? 144.138 116.652 128.519 1.00 88.69  ? 458 PHE A CG  1 
ATOM 2820 C CD1 . PHE A 1 373 ? 144.739 115.456 128.878 1.00 87.83  ? 458 PHE A CD1 1 
ATOM 2821 C CD2 . PHE A 1 373 ? 144.227 117.071 127.202 1.00 86.62  ? 458 PHE A CD2 1 
ATOM 2822 C CE1 . PHE A 1 373 ? 145.412 114.693 127.941 1.00 89.92  ? 458 PHE A CE1 1 
ATOM 2823 C CE2 . PHE A 1 373 ? 144.899 116.314 126.261 1.00 89.14  ? 458 PHE A CE2 1 
ATOM 2824 C CZ  . PHE A 1 373 ? 145.492 115.123 126.632 1.00 89.96  ? 458 PHE A CZ  1 
ATOM 2825 N N   . GLY A 1 374 ? 140.242 117.506 131.442 1.00 91.63  ? 459 GLY A N   1 
ATOM 2826 C CA  . GLY A 1 374 ? 139.389 118.408 132.187 1.00 95.11  ? 459 GLY A CA  1 
ATOM 2827 C C   . GLY A 1 374 ? 140.008 118.776 133.518 1.00 105.21 ? 459 GLY A C   1 
ATOM 2828 O O   . GLY A 1 374 ? 139.802 119.881 134.029 1.00 107.04 ? 459 GLY A O   1 
ATOM 2829 N N   . GLY A 1 375 ? 140.780 117.851 134.081 1.00 106.29 ? 460 GLY A N   1 
ATOM 2830 C CA  . GLY A 1 375 ? 141.471 118.075 135.328 1.00 107.53 ? 460 GLY A CA  1 
ATOM 2831 C C   . GLY A 1 375 ? 142.450 119.230 135.259 1.00 109.48 ? 460 GLY A C   1 
ATOM 2832 O O   . GLY A 1 375 ? 142.332 120.213 135.998 1.00 110.85 ? 460 GLY A O   1 
ATOM 2833 N N   . PRO A 1 376 ? 143.449 119.129 134.376 1.00 105.52 ? 461 PRO A N   1 
ATOM 2834 C CA  . PRO A 1 376 ? 144.393 120.247 134.219 1.00 105.55 ? 461 PRO A CA  1 
ATOM 2835 C C   . PRO A 1 376 ? 143.727 121.558 133.838 1.00 104.16 ? 461 PRO A C   1 
ATOM 2836 O O   . PRO A 1 376 ? 144.169 122.619 134.294 1.00 103.94 ? 461 PRO A O   1 
ATOM 2837 C CB  . PRO A 1 376 ? 145.332 119.753 133.111 1.00 103.01 ? 461 PRO A CB  1 
ATOM 2838 C CG  . PRO A 1 376 ? 145.306 118.274 133.242 1.00 102.88 ? 461 PRO A CG  1 
ATOM 2839 C CD  . PRO A 1 376 ? 143.903 117.921 133.663 1.00 101.25 ? 461 PRO A CD  1 
ATOM 2840 N N   . PHE A 1 377 ? 142.673 121.519 133.022 1.00 104.85 ? 462 PHE A N   1 
ATOM 2841 C CA  . PHE A 1 377 ? 142.020 122.737 132.561 1.00 104.89 ? 462 PHE A CA  1 
ATOM 2842 C C   . PHE A 1 377 ? 141.017 123.305 133.556 1.00 108.09 ? 462 PHE A C   1 
ATOM 2843 O O   . PHE A 1 377 ? 140.529 124.419 133.337 1.00 109.29 ? 462 PHE A O   1 
ATOM 2844 C CB  . PHE A 1 377 ? 141.316 122.487 131.225 1.00 98.91  ? 462 PHE A CB  1 
ATOM 2845 C CG  . PHE A 1 377 ? 142.201 122.680 130.028 1.00 97.02  ? 462 PHE A CG  1 
ATOM 2846 C CD1 . PHE A 1 377 ? 143.036 121.664 129.594 1.00 93.11  ? 462 PHE A CD1 1 
ATOM 2847 C CD2 . PHE A 1 377 ? 142.198 123.880 129.337 1.00 100.51 ? 462 PHE A CD2 1 
ATOM 2848 C CE1 . PHE A 1 377 ? 143.851 121.842 128.492 1.00 91.69  ? 462 PHE A CE1 1 
ATOM 2849 C CE2 . PHE A 1 377 ? 143.010 124.064 128.235 1.00 99.52  ? 462 PHE A CE2 1 
ATOM 2850 C CZ  . PHE A 1 377 ? 143.838 123.044 127.812 1.00 98.66  ? 462 PHE A CZ  1 
ATOM 2851 N N   . ALA A 1 378 ? 140.695 122.577 134.627 1.00 108.05 ? 463 ALA A N   1 
ATOM 2852 C CA  . ALA A 1 378 ? 139.729 123.085 135.599 1.00 107.08 ? 463 ALA A CA  1 
ATOM 2853 C C   . ALA A 1 378 ? 140.130 124.434 136.188 1.00 111.45 ? 463 ALA A C   1 
ATOM 2854 O O   . ALA A 1 378 ? 139.276 125.337 136.231 1.00 108.24 ? 463 ALA A O   1 
ATOM 2855 C CB  . ALA A 1 378 ? 139.495 122.036 136.692 1.00 104.44 ? 463 ALA A CB  1 
ATOM 2856 N N   . PRO A 1 379 ? 141.366 124.650 136.660 1.00 113.28 ? 464 PRO A N   1 
ATOM 2857 C CA  . PRO A 1 379 ? 141.724 126.007 137.111 1.00 110.73 ? 464 PRO A CA  1 
ATOM 2858 C C   . PRO A 1 379 ? 141.679 127.045 136.002 1.00 111.11 ? 464 PRO A C   1 
ATOM 2859 O O   . PRO A 1 379 ? 141.277 128.190 136.248 1.00 110.40 ? 464 PRO A O   1 
ATOM 2860 C CB  . PRO A 1 379 ? 143.145 125.831 137.668 1.00 109.38 ? 464 PRO A CB  1 
ATOM 2861 C CG  . PRO A 1 379 ? 143.270 124.376 137.954 1.00 106.28 ? 464 PRO A CG  1 
ATOM 2862 C CD  . PRO A 1 379 ? 142.473 123.703 136.888 1.00 109.59 ? 464 PRO A CD  1 
ATOM 2863 N N   . LEU A 1 380 ? 142.081 126.678 134.781 1.00 110.13 ? 465 LEU A N   1 
ATOM 2864 C CA  . LEU A 1 380 ? 142.086 127.641 133.684 1.00 108.34 ? 465 LEU A CA  1 
ATOM 2865 C C   . LEU A 1 380 ? 140.673 128.087 133.328 1.00 110.39 ? 465 LEU A C   1 
ATOM 2866 O O   . LEU A 1 380 ? 140.437 129.270 133.059 1.00 114.96 ? 465 LEU A O   1 
ATOM 2867 C CB  . LEU A 1 380 ? 142.788 127.050 132.460 1.00 108.90 ? 465 LEU A CB  1 
ATOM 2868 C CG  . LEU A 1 380 ? 144.305 126.870 132.551 1.00 112.56 ? 465 LEU A CG  1 
ATOM 2869 C CD1 . LEU A 1 380 ? 144.665 125.464 132.993 1.00 108.09 ? 465 LEU A CD1 1 
ATOM 2870 C CD2 . LEU A 1 380 ? 144.964 127.199 131.219 1.00 108.09 ? 465 LEU A CD2 1 
ATOM 2871 N N   . VAL A 1 381 ? 139.720 127.154 133.314 1.00 109.83 ? 466 VAL A N   1 
ATOM 2872 C CA  . VAL A 1 381 ? 138.342 127.519 133.005 1.00 110.27 ? 466 VAL A CA  1 
ATOM 2873 C C   . VAL A 1 381 ? 137.643 128.152 134.203 1.00 111.24 ? 466 VAL A C   1 
ATOM 2874 O O   . VAL A 1 381 ? 136.692 128.922 134.021 1.00 109.09 ? 466 VAL A O   1 
ATOM 2875 C CB  . VAL A 1 381 ? 137.558 126.294 132.499 1.00 104.61 ? 466 VAL A CB  1 
ATOM 2876 C CG1 . VAL A 1 381 ? 137.478 125.223 133.571 1.00 101.34 ? 466 VAL A CG1 1 
ATOM 2877 C CG2 . VAL A 1 381 ? 136.173 126.697 132.027 1.00 96.98  ? 466 VAL A CG2 1 
ATOM 2878 N N   . ALA A 1 382 ? 138.103 127.867 135.426 1.00 113.39 ? 467 ALA A N   1 
ATOM 2879 C CA  . ALA A 1 382 ? 137.497 128.476 136.606 1.00 111.44 ? 467 ALA A CA  1 
ATOM 2880 C C   . ALA A 1 382 ? 137.597 129.995 136.569 1.00 111.16 ? 467 ALA A C   1 
ATOM 2881 O O   . ALA A 1 382 ? 136.761 130.686 137.161 1.00 110.89 ? 467 ALA A O   1 
ATOM 2882 C CB  . ALA A 1 382 ? 138.152 127.930 137.874 1.00 114.33 ? 467 ALA A CB  1 
ATOM 2883 N N   . LYS A 1 383 ? 138.611 130.532 135.883 1.00 110.65 ? 468 LYS A N   1 
ATOM 2884 C CA  . LYS A 1 383 ? 138.700 131.977 135.702 1.00 110.04 ? 468 LYS A CA  1 
ATOM 2885 C C   . LYS A 1 383 ? 137.518 132.511 134.904 1.00 110.55 ? 468 LYS A C   1 
ATOM 2886 O O   . LYS A 1 383 ? 137.136 133.676 135.061 1.00 111.72 ? 468 LYS A O   1 
ATOM 2887 C CB  . LYS A 1 383 ? 140.013 132.343 135.007 1.00 111.36 ? 468 LYS A CB  1 
ATOM 2888 C CG  . LYS A 1 383 ? 141.201 131.479 135.402 1.00 111.54 ? 468 LYS A CG  1 
ATOM 2889 C CD  . LYS A 1 383 ? 141.491 131.575 136.891 1.00 110.97 ? 468 LYS A CD  1 
ATOM 2890 C CE  . LYS A 1 383 ? 142.258 132.846 137.218 1.00 110.34 ? 468 LYS A CE  1 
ATOM 2891 N NZ  . LYS A 1 383 ? 142.201 133.170 138.669 1.00 109.53 ? 468 LYS A NZ  1 
ATOM 2892 N N   . LEU A 1 384 ? 136.932 131.679 134.048 1.00 109.32 ? 469 LEU A N   1 
ATOM 2893 C CA  . LEU A 1 384 ? 135.770 132.050 133.255 1.00 104.31 ? 469 LEU A CA  1 
ATOM 2894 C C   . LEU A 1 384 ? 134.456 131.730 133.954 1.00 101.96 ? 469 LEU A C   1 
ATOM 2895 O O   . LEU A 1 384 ? 133.389 131.984 133.384 1.00 100.62 ? 469 LEU A O   1 
ATOM 2896 C CB  . LEU A 1 384 ? 135.821 131.342 131.898 1.00 103.15 ? 469 LEU A CB  1 
ATOM 2897 C CG  . LEU A 1 384 ? 136.958 131.752 130.960 1.00 108.15 ? 469 LEU A CG  1 
ATOM 2898 C CD1 . LEU A 1 384 ? 136.997 130.861 129.728 1.00 108.21 ? 469 LEU A CD1 1 
ATOM 2899 C CD2 . LEU A 1 384 ? 136.818 133.212 130.561 1.00 108.06 ? 469 LEU A CD2 1 
ATOM 2900 N N   . GLY A 1 385 ? 134.507 131.187 135.166 1.00 101.89 ? 470 GLY A N   1 
ATOM 2901 C CA  . GLY A 1 385 ? 133.301 130.816 135.885 1.00 98.73  ? 470 GLY A CA  1 
ATOM 2902 C C   . GLY A 1 385 ? 132.529 129.682 135.249 1.00 94.90  ? 470 GLY A C   1 
ATOM 2903 O O   . GLY A 1 385 ? 131.291 129.710 135.234 1.00 90.27  ? 470 GLY A O   1 
ATOM 2904 N N   . MET A 1 386 ? 133.227 128.680 134.719 1.00 95.24  ? 471 MET A N   1 
ATOM 2905 C CA  . MET A 1 386 ? 132.579 127.554 134.065 1.00 88.08  ? 471 MET A CA  1 
ATOM 2906 C C   . MET A 1 386 ? 133.217 126.252 134.518 1.00 87.67  ? 471 MET A C   1 
ATOM 2907 O O   . MET A 1 386 ? 134.434 126.178 134.708 1.00 92.29  ? 471 MET A O   1 
ATOM 2908 C CB  . MET A 1 386 ? 132.674 127.651 132.537 1.00 84.32  ? 471 MET A CB  1 
ATOM 2909 C CG  . MET A 1 386 ? 131.909 128.803 131.922 1.00 85.71  ? 471 MET A CG  1 
ATOM 2910 S SD  . MET A 1 386 ? 132.034 128.786 130.126 1.00 87.53  ? 471 MET A SD  1 
ATOM 2911 C CE  . MET A 1 386 ? 133.711 129.348 129.874 1.00 91.98  ? 471 MET A CE  1 
ATOM 2912 N N   . THR A 1 387 ? 132.386 125.233 134.696 1.00 82.30  ? 472 THR A N   1 
ATOM 2913 C CA  . THR A 1 387 ? 132.895 123.876 134.795 1.00 78.30  ? 472 THR A CA  1 
ATOM 2914 C C   . THR A 1 387 ? 133.550 123.501 133.467 1.00 82.79  ? 472 THR A C   1 
ATOM 2915 O O   . THR A 1 387 ? 133.073 123.921 132.406 1.00 86.92  ? 472 THR A O   1 
ATOM 2916 C CB  . THR A 1 387 ? 131.752 122.909 135.126 1.00 80.10  ? 472 THR A CB  1 
ATOM 2917 O OG1 . THR A 1 387 ? 131.122 123.316 136.348 1.00 95.96  ? 472 THR A OG1 1 
ATOM 2918 C CG2 . THR A 1 387 ? 132.250 121.477 135.278 1.00 81.39  ? 472 THR A CG2 1 
ATOM 2919 N N   . PRO A 1 388 ? 134.652 122.744 133.480 1.00 81.58  ? 473 PRO A N   1 
ATOM 2920 C CA  . PRO A 1 388 ? 135.251 122.318 132.202 1.00 75.32  ? 473 PRO A CA  1 
ATOM 2921 C C   . PRO A 1 388 ? 134.269 121.595 131.300 1.00 71.96  ? 473 PRO A C   1 
ATOM 2922 O O   . PRO A 1 388 ? 134.376 121.691 130.069 1.00 71.20  ? 473 PRO A O   1 
ATOM 2923 C CB  . PRO A 1 388 ? 136.408 121.404 132.638 1.00 77.00  ? 473 PRO A CB  1 
ATOM 2924 C CG  . PRO A 1 388 ? 136.242 121.199 134.124 1.00 84.61  ? 473 PRO A CG  1 
ATOM 2925 C CD  . PRO A 1 388 ? 135.505 122.392 134.626 1.00 84.55  ? 473 PRO A CD  1 
ATOM 2926 N N   . LEU A 1 389 ? 133.302 120.880 131.879 1.00 74.24  ? 474 LEU A N   1 
ATOM 2927 C CA  . LEU A 1 389 ? 132.215 120.321 131.084 1.00 69.68  ? 474 LEU A CA  1 
ATOM 2928 C C   . LEU A 1 389 ? 131.414 121.421 130.396 1.00 68.69  ? 474 LEU A C   1 
ATOM 2929 O O   . LEU A 1 389 ? 131.080 121.308 129.212 1.00 72.36  ? 474 LEU A O   1 
ATOM 2930 C CB  . LEU A 1 389 ? 131.311 119.467 131.973 1.00 66.44  ? 474 LEU A CB  1 
ATOM 2931 C CG  . LEU A 1 389 ? 130.009 118.936 131.372 1.00 59.43  ? 474 LEU A CG  1 
ATOM 2932 C CD1 . LEU A 1 389 ? 130.290 118.076 130.151 1.00 57.79  ? 474 LEU A CD1 1 
ATOM 2933 C CD2 . LEU A 1 389 ? 129.231 118.153 132.417 1.00 60.88  ? 474 LEU A CD2 1 
ATOM 2934 N N   . LEU A 1 390 ? 131.110 122.503 131.119 1.00 68.21  ? 475 LEU A N   1 
ATOM 2935 C CA  . LEU A 1 390 ? 130.373 123.611 130.517 1.00 64.44  ? 475 LEU A CA  1 
ATOM 2936 C C   . LEU A 1 390 ? 131.210 124.323 129.459 1.00 64.48  ? 475 LEU A C   1 
ATOM 2937 O O   . LEU A 1 390 ? 130.678 124.773 128.436 1.00 69.37  ? 475 LEU A O   1 
ATOM 2938 C CB  . LEU A 1 390 ? 129.919 124.590 131.601 1.00 68.60  ? 475 LEU A CB  1 
ATOM 2939 C CG  . LEU A 1 390 ? 129.041 125.756 131.144 1.00 66.03  ? 475 LEU A CG  1 
ATOM 2940 C CD1 . LEU A 1 390 ? 127.657 125.260 130.762 1.00 65.84  ? 475 LEU A CD1 1 
ATOM 2941 C CD2 . LEU A 1 390 ? 128.943 126.809 132.235 1.00 68.79  ? 475 LEU A CD2 1 
ATOM 2942 N N   . ALA A 1 391 ? 132.520 124.442 129.690 1.00 68.24  ? 476 ALA A N   1 
ATOM 2943 C CA  . ALA A 1 391 ? 133.400 125.017 128.679 1.00 66.07  ? 476 ALA A CA  1 
ATOM 2944 C C   . ALA A 1 391 ? 133.391 124.179 127.410 1.00 62.86  ? 476 ALA A C   1 
ATOM 2945 O O   . ALA A 1 391 ? 133.325 124.714 126.297 1.00 64.85  ? 476 ALA A O   1 
ATOM 2946 C CB  . ALA A 1 391 ? 134.821 125.142 129.224 1.00 70.00  ? 476 ALA A CB  1 
ATOM 2947 N N   . ALA A 1 392 ? 133.463 122.854 127.560 1.00 66.21  ? 477 ALA A N   1 
ATOM 2948 C CA  . ALA A 1 392 ? 133.377 121.976 126.399 1.00 56.97  ? 477 ALA A CA  1 
ATOM 2949 C C   . ALA A 1 392 ? 132.033 122.127 125.702 1.00 57.30  ? 477 ALA A C   1 
ATOM 2950 O O   . ALA A 1 392 ? 131.963 122.137 124.469 1.00 62.71  ? 477 ALA A O   1 
ATOM 2951 C CB  . ALA A 1 392 ? 133.610 120.525 126.817 1.00 63.25  ? 477 ALA A CB  1 
ATOM 2952 N N   . VAL A 1 393 ? 130.956 122.256 126.479 1.00 57.73  ? 478 VAL A N   1 
ATOM 2953 C CA  . VAL A 1 393 ? 129.630 122.439 125.893 1.00 55.74  ? 478 VAL A CA  1 
ATOM 2954 C C   . VAL A 1 393 ? 129.594 123.700 125.039 1.00 58.95  ? 478 VAL A C   1 
ATOM 2955 O O   . VAL A 1 393 ? 129.111 123.686 123.903 1.00 60.87  ? 478 VAL A O   1 
ATOM 2956 C CB  . VAL A 1 393 ? 128.558 122.472 126.997 1.00 53.56  ? 478 VAL A CB  1 
ATOM 2957 C CG1 . VAL A 1 393 ? 127.255 123.037 126.456 1.00 57.16  ? 478 VAL A CG1 1 
ATOM 2958 C CG2 . VAL A 1 393 ? 128.339 121.078 127.550 1.00 56.75  ? 478 VAL A CG2 1 
ATOM 2959 N N   . TYR A 1 394 ? 130.119 124.807 125.569 1.00 61.19  ? 479 TYR A N   1 
ATOM 2960 C CA  . TYR A 1 394 ? 130.085 126.062 124.821 1.00 55.42  ? 479 TYR A CA  1 
ATOM 2961 C C   . TYR A 1 394 ? 130.988 126.016 123.593 1.00 56.68  ? 479 TYR A C   1 
ATOM 2962 O O   . TYR A 1 394 ? 130.624 126.537 122.531 1.00 62.22  ? 479 TYR A O   1 
ATOM 2963 C CB  . TYR A 1 394 ? 130.465 127.232 125.728 1.00 57.60  ? 479 TYR A CB  1 
ATOM 2964 C CG  . TYR A 1 394 ? 129.378 127.622 126.703 1.00 59.18  ? 479 TYR A CG  1 
ATOM 2965 C CD1 . TYR A 1 394 ? 129.678 128.322 127.860 1.00 64.79  ? 479 TYR A CD1 1 
ATOM 2966 C CD2 . TYR A 1 394 ? 128.053 127.291 126.465 1.00 60.80  ? 479 TYR A CD2 1 
ATOM 2967 C CE1 . TYR A 1 394 ? 128.691 128.683 128.757 1.00 72.51  ? 479 TYR A CE1 1 
ATOM 2968 C CE2 . TYR A 1 394 ? 127.057 127.647 127.355 1.00 66.22  ? 479 TYR A CE2 1 
ATOM 2969 C CZ  . TYR A 1 394 ? 127.381 128.342 128.499 1.00 75.19  ? 479 TYR A CZ  1 
ATOM 2970 O OH  . TYR A 1 394 ? 126.393 128.698 129.387 1.00 81.01  ? 479 TYR A OH  1 
ATOM 2971 N N   . VAL A 1 395 ? 132.171 125.407 123.715 1.00 56.62  ? 480 VAL A N   1 
ATOM 2972 C CA  . VAL A 1 395 ? 133.073 125.309 122.567 1.00 53.36  ? 480 VAL A CA  1 
ATOM 2973 C C   . VAL A 1 395 ? 132.439 124.469 121.465 1.00 57.36  ? 480 VAL A C   1 
ATOM 2974 O O   . VAL A 1 395 ? 132.459 124.840 120.284 1.00 65.43  ? 480 VAL A O   1 
ATOM 2975 C CB  . VAL A 1 395 ? 134.437 124.743 123.000 1.00 55.24  ? 480 VAL A CB  1 
ATOM 2976 C CG1 . VAL A 1 395 ? 135.307 124.476 121.783 1.00 54.91  ? 480 VAL A CG1 1 
ATOM 2977 C CG2 . VAL A 1 395 ? 135.137 125.712 123.936 1.00 57.82  ? 480 VAL A CG2 1 
ATOM 2978 N N   . GLY A 1 396 ? 131.861 123.324 121.836 1.00 55.21  ? 481 GLY A N   1 
ATOM 2979 C CA  . GLY A 1 396 ? 131.172 122.502 120.860 1.00 54.76  ? 481 GLY A CA  1 
ATOM 2980 C C   . GLY A 1 396 ? 129.967 123.189 120.256 1.00 59.58  ? 481 GLY A C   1 
ATOM 2981 O O   . GLY A 1 396 ? 129.680 123.007 119.072 1.00 64.31  ? 481 GLY A O   1 
ATOM 2982 N N   . ALA A 1 397 ? 129.250 123.988 121.051 1.00 61.27  ? 482 ALA A N   1 
ATOM 2983 C CA  . ALA A 1 397 ? 128.122 124.744 120.519 1.00 56.87  ? 482 ALA A CA  1 
ATOM 2984 C C   . ALA A 1 397 ? 128.579 125.766 119.487 1.00 57.03  ? 482 ALA A C   1 
ATOM 2985 O O   . ALA A 1 397 ? 127.962 125.898 118.425 1.00 63.31  ? 482 ALA A O   1 
ATOM 2986 C CB  . ALA A 1 397 ? 127.368 125.432 121.656 1.00 56.23  ? 482 ALA A CB  1 
ATOM 2987 N N   . LEU A 1 398 ? 129.660 126.494 119.777 1.00 58.37  ? 483 LEU A N   1 
ATOM 2988 C CA  . LEU A 1 398 ? 130.169 127.465 118.814 1.00 59.12  ? 483 LEU A CA  1 
ATOM 2989 C C   . LEU A 1 398 ? 130.664 126.778 117.546 1.00 59.75  ? 483 LEU A C   1 
ATOM 2990 O O   . LEU A 1 398 ? 130.452 127.282 116.436 1.00 63.47  ? 483 LEU A O   1 
ATOM 2991 C CB  . LEU A 1 398 ? 131.284 128.301 119.443 1.00 60.10  ? 483 LEU A CB  1 
ATOM 2992 C CG  . LEU A 1 398 ? 131.858 129.406 118.554 1.00 68.03  ? 483 LEU A CG  1 
ATOM 2993 C CD1 . LEU A 1 398 ? 130.783 130.422 118.200 1.00 65.90  ? 483 LEU A CD1 1 
ATOM 2994 C CD2 . LEU A 1 398 ? 133.038 130.085 119.230 1.00 73.08  ? 483 LEU A CD2 1 
ATOM 2995 N N   . GLN A 1 399 ? 131.328 125.630 117.693 1.00 59.83  ? 484 GLN A N   1 
ATOM 2996 C CA  . GLN A 1 399 ? 131.789 124.883 116.527 1.00 57.39  ? 484 GLN A CA  1 
ATOM 2997 C C   . GLN A 1 399 ? 130.626 124.365 115.687 1.00 59.33  ? 484 GLN A C   1 
ATOM 2998 O O   . GLN A 1 399 ? 130.652 124.478 114.455 1.00 67.86  ? 484 GLN A O   1 
ATOM 2999 C CB  . GLN A 1 399 ? 132.696 123.745 116.992 1.00 58.27  ? 484 GLN A CB  1 
ATOM 3000 C CG  . GLN A 1 399 ? 133.182 122.799 115.917 1.00 59.76  ? 484 GLN A CG  1 
ATOM 3001 C CD  . GLN A 1 399 ? 133.970 121.651 116.510 1.00 65.99  ? 484 GLN A CD  1 
ATOM 3002 O OE1 . GLN A 1 399 ? 133.860 121.364 117.702 1.00 64.09  ? 484 GLN A OE1 1 
ATOM 3003 N NE2 . GLN A 1 399 ? 134.771 120.988 115.684 1.00 69.34  ? 484 GLN A NE2 1 
ATOM 3004 N N   . ASN A 1 400 ? 129.595 123.818 116.331 1.00 58.76  ? 485 ASN A N   1 
ATOM 3005 C CA  . ASN A 1 400 ? 128.384 123.359 115.666 1.00 57.22  ? 485 ASN A CA  1 
ATOM 3006 C C   . ASN A 1 400 ? 127.615 124.501 115.014 1.00 57.63  ? 485 ASN A C   1 
ATOM 3007 O O   . ASN A 1 400 ? 126.947 124.280 113.999 1.00 63.40  ? 485 ASN A O   1 
ATOM 3008 C CB  . ASN A 1 400 ? 127.503 122.623 116.689 1.00 56.58  ? 485 ASN A CB  1 
ATOM 3009 C CG  . ASN A 1 400 ? 126.328 121.897 116.058 1.00 64.30  ? 485 ASN A CG  1 
ATOM 3010 O OD1 . ASN A 1 400 ? 125.479 122.500 115.403 1.00 68.52  ? 485 ASN A OD1 1 
ATOM 3011 N ND2 . ASN A 1 400 ? 126.276 120.587 116.259 1.00 65.51  ? 485 ASN A ND2 1 
ATOM 3012 N N   . ILE A 1 401 ? 127.699 125.706 115.567 1.00 59.01  ? 486 ILE A N   1 
ATOM 3013 C CA  . ILE A 1 401 ? 127.103 126.883 114.944 1.00 55.65  ? 486 ILE A CA  1 
ATOM 3014 C C   . ILE A 1 401 ? 127.883 127.316 113.709 1.00 59.57  ? 486 ILE A C   1 
ATOM 3015 O O   . ILE A 1 401 ? 127.291 127.582 112.660 1.00 67.27  ? 486 ILE A O   1 
ATOM 3016 C CB  . ILE A 1 401 ? 127.004 128.024 115.975 1.00 53.72  ? 486 ILE A CB  1 
ATOM 3017 C CG1 . ILE A 1 401 ? 125.870 127.757 116.965 1.00 53.06  ? 486 ILE A CG1 1 
ATOM 3018 C CG2 . ILE A 1 401 ? 126.805 129.352 115.283 1.00 55.25  ? 486 ILE A CG2 1 
ATOM 3019 C CD1 . ILE A 1 401 ? 125.695 128.844 118.000 1.00 56.32  ? 486 ILE A CD1 1 
ATOM 3020 N N   . PHE A 1 402 ? 129.213 127.391 113.811 1.00 57.33  ? 487 PHE A N   1 
ATOM 3021 C CA  . PHE A 1 402 ? 130.008 127.824 112.667 1.00 54.76  ? 487 PHE A CA  1 
ATOM 3022 C C   . PHE A 1 402 ? 129.923 126.827 111.522 1.00 57.78  ? 487 PHE A C   1 
ATOM 3023 O O   . PHE A 1 402 ? 129.937 127.223 110.354 1.00 63.71  ? 487 PHE A O   1 
ATOM 3024 C CB  . PHE A 1 402 ? 131.475 128.009 113.055 1.00 57.06  ? 487 PHE A CB  1 
ATOM 3025 C CG  . PHE A 1 402 ? 132.316 128.606 111.959 1.00 63.15  ? 487 PHE A CG  1 
ATOM 3026 C CD1 . PHE A 1 402 ? 132.244 129.958 111.675 1.00 67.74  ? 487 PHE A CD1 1 
ATOM 3027 C CD2 . PHE A 1 402 ? 133.119 127.803 111.164 1.00 64.19  ? 487 PHE A CD2 1 
ATOM 3028 C CE1 . PHE A 1 402 ? 133.009 130.512 110.667 1.00 68.22  ? 487 PHE A CE1 1 
ATOM 3029 C CE2 . PHE A 1 402 ? 133.876 128.351 110.142 1.00 68.01  ? 487 PHE A CE2 1 
ATOM 3030 C CZ  . PHE A 1 402 ? 133.817 129.706 109.893 1.00 68.81  ? 487 PHE A CZ  1 
ATOM 3031 N N   . SER A 1 403 ? 129.844 125.534 111.836 1.00 58.67  ? 488 SER A N   1 
ATOM 3032 C CA  . SER A 1 403 ? 129.814 124.512 110.799 1.00 55.03  ? 488 SER A CA  1 
ATOM 3033 C C   . SER A 1 403 ? 128.482 124.451 110.062 1.00 57.27  ? 488 SER A C   1 
ATOM 3034 O O   . SER A 1 403 ? 128.461 124.071 108.887 1.00 63.63  ? 488 SER A O   1 
ATOM 3035 C CB  . SER A 1 403 ? 130.133 123.147 111.408 1.00 55.82  ? 488 SER A CB  1 
ATOM 3036 O OG  . SER A 1 403 ? 129.104 122.727 112.285 1.00 59.42  ? 488 SER A OG  1 
ATOM 3037 N N   . LYS A 1 404 ? 127.378 124.812 110.716 1.00 56.48  ? 489 LYS A N   1 
ATOM 3038 C CA  . LYS A 1 404 ? 126.072 124.803 110.069 1.00 57.16  ? 489 LYS A CA  1 
ATOM 3039 C C   . LYS A 1 404 ? 125.670 126.154 109.493 1.00 59.85  ? 489 LYS A C   1 
ATOM 3040 O O   . LYS A 1 404 ? 124.807 126.196 108.610 1.00 61.56  ? 489 LYS A O   1 
ATOM 3041 C CB  . LYS A 1 404 ? 124.990 124.333 111.050 1.00 56.61  ? 489 LYS A CB  1 
ATOM 3042 C CG  . LYS A 1 404 ? 125.253 122.963 111.653 1.00 59.48  ? 489 LYS A CG  1 
ATOM 3043 C CD  . LYS A 1 404 ? 123.958 122.287 112.068 1.00 63.61  ? 489 LYS A CD  1 
ATOM 3044 C CE  . LYS A 1 404 ? 123.162 121.830 110.855 1.00 71.14  ? 489 LYS A CE  1 
ATOM 3045 N NZ  . LYS A 1 404 ? 123.848 120.732 110.119 1.00 71.48  ? 489 LYS A NZ  1 
ATOM 3046 N N   . SER A 1 405 ? 126.262 127.249 109.965 1.00 59.50  ? 490 SER A N   1 
ATOM 3047 C CA  . SER A 1 405 ? 125.999 128.561 109.392 1.00 59.67  ? 490 SER A CA  1 
ATOM 3048 C C   . SER A 1 405 ? 126.917 128.891 108.223 1.00 65.59  ? 490 SER A C   1 
ATOM 3049 O O   . SER A 1 405 ? 126.640 129.845 107.489 1.00 73.02  ? 490 SER A O   1 
ATOM 3050 C CB  . SER A 1 405 ? 126.131 129.647 110.466 1.00 61.38  ? 490 SER A CB  1 
ATOM 3051 O OG  . SER A 1 405 ? 127.469 129.758 110.918 1.00 70.49  ? 490 SER A OG  1 
ATOM 3052 N N   . ALA A 1 406 ? 127.993 128.131 108.033 1.00 61.97  ? 491 ALA A N   1 
ATOM 3053 C CA  . ALA A 1 406 ? 128.901 128.333 106.913 1.00 59.12  ? 491 ALA A CA  1 
ATOM 3054 C C   . ALA A 1 406 ? 128.565 127.458 105.713 1.00 61.46  ? 491 ALA A C   1 
ATOM 3055 O O   . ALA A 1 406 ? 129.280 127.515 104.708 1.00 63.93  ? 491 ALA A O   1 
ATOM 3056 C CB  . ALA A 1 406 ? 130.347 128.073 107.346 1.00 57.44  ? 491 ALA A CB  1 
ATOM 3057 N N   . LYS A 1 407 ? 127.512 126.646 105.797 1.00 60.63  ? 492 LYS A N   1 
ATOM 3058 C CA  . LYS A 1 407 ? 127.106 125.824 104.664 1.00 56.74  ? 492 LYS A CA  1 
ATOM 3059 C C   . LYS A 1 407 ? 126.687 126.699 103.490 1.00 60.09  ? 492 LYS A C   1 
ATOM 3060 O O   . LYS A 1 407 ? 127.353 126.713 102.452 1.00 64.69  ? 492 LYS A O   1 
ATOM 3061 C CB  . LYS A 1 407 ? 125.962 124.885 105.051 1.00 55.91  ? 492 LYS A CB  1 
ATOM 3062 C CG  . LYS A 1 407 ? 125.336 124.169 103.863 1.00 61.12  ? 492 LYS A CG  1 
ATOM 3063 C CD  . LYS A 1 407 ? 124.112 123.363 104.266 1.00 66.91  ? 492 LYS A CD  1 
ATOM 3064 C CE  . LYS A 1 407 ? 123.487 122.683 103.057 1.00 68.34  ? 492 LYS A CE  1 
ATOM 3065 N NZ  . LYS A 1 407 ? 122.349 121.801 103.437 1.00 68.13  ? 492 LYS A NZ  1 
ATOM 3066 N N   . TYR A 1 408 ? 125.604 127.458 103.659 1.00 60.36  ? 493 TYR A N   1 
ATOM 3067 C CA  . TYR A 1 408 ? 125.062 128.265 102.574 1.00 59.77  ? 493 TYR A CA  1 
ATOM 3068 C C   . TYR A 1 408 ? 125.810 129.575 102.370 1.00 63.03  ? 493 TYR A C   1 
ATOM 3069 O O   . TYR A 1 408 ? 125.571 130.254 101.366 1.00 71.02  ? 493 TYR A O   1 
ATOM 3070 C CB  . TYR A 1 408 ? 123.581 128.558 102.828 1.00 59.19  ? 493 TYR A CB  1 
ATOM 3071 C CG  . TYR A 1 408 ? 122.674 127.376 102.584 1.00 59.08  ? 493 TYR A CG  1 
ATOM 3072 C CD1 . TYR A 1 408 ? 122.736 126.664 101.394 1.00 61.61  ? 493 TYR A CD1 1 
ATOM 3073 C CD2 . TYR A 1 408 ? 121.757 126.970 103.544 1.00 61.23  ? 493 TYR A CD2 1 
ATOM 3074 C CE1 . TYR A 1 408 ? 121.909 125.582 101.165 1.00 66.36  ? 493 TYR A CE1 1 
ATOM 3075 C CE2 . TYR A 1 408 ? 120.925 125.889 103.324 1.00 65.86  ? 493 TYR A CE2 1 
ATOM 3076 C CZ  . TYR A 1 408 ? 121.006 125.198 102.134 1.00 71.60  ? 493 TYR A CZ  1 
ATOM 3077 O OH  . TYR A 1 408 ? 120.180 124.121 101.910 1.00 72.77  ? 493 TYR A OH  1 
ATOM 3078 N N   . SER A 1 409 ? 126.699 129.945 103.288 1.00 62.72  ? 494 SER A N   1 
ATOM 3079 C CA  . SER A 1 409 ? 127.449 131.190 103.186 1.00 62.09  ? 494 SER A CA  1 
ATOM 3080 C C   . SER A 1 409 ? 128.886 130.986 102.732 1.00 63.73  ? 494 SER A C   1 
ATOM 3081 O O   . SER A 1 409 ? 129.376 131.736 101.884 1.00 71.45  ? 494 SER A O   1 
ATOM 3082 C CB  . SER A 1 409 ? 127.450 131.919 104.533 1.00 66.80  ? 494 SER A CB  1 
ATOM 3083 O OG  . SER A 1 409 ? 128.237 131.227 105.487 1.00 66.39  ? 494 SER A OG  1 
ATOM 3084 N N   . LEU A 1 410 ? 129.561 129.983 103.259 1.00 61.22  ? 495 LEU A N   1 
ATOM 3085 C CA  . LEU A 1 410 ? 131.006 129.885 103.104 1.00 52.65  ? 495 LEU A CA  1 
ATOM 3086 C C   . LEU A 1 410 ? 131.465 128.592 102.447 1.00 53.64  ? 495 LEU A C   1 
ATOM 3087 O O   . LEU A 1 410 ? 132.426 128.614 101.674 1.00 61.49  ? 495 LEU A O   1 
ATOM 3088 C CB  . LEU A 1 410 ? 131.657 130.036 104.483 1.00 58.19  ? 495 LEU A CB  1 
ATOM 3089 C CG  . LEU A 1 410 ? 133.139 130.386 104.561 1.00 59.56  ? 495 LEU A CG  1 
ATOM 3090 C CD1 . LEU A 1 410 ? 133.390 131.787 104.031 1.00 56.22  ? 495 LEU A CD1 1 
ATOM 3091 C CD2 . LEU A 1 410 ? 133.586 130.268 105.998 1.00 60.87  ? 495 LEU A CD2 1 
ATOM 3092 N N   . PHE A 1 411 ? 130.809 127.468 102.733 1.00 52.22  ? 496 PHE A N   1 
ATOM 3093 C CA  . PHE A 1 411 ? 131.248 126.188 102.190 1.00 51.66  ? 496 PHE A CA  1 
ATOM 3094 C C   . PHE A 1 411 ? 130.636 125.894 100.825 1.00 53.78  ? 496 PHE A C   1 
ATOM 3095 O O   . PHE A 1 411 ? 131.361 125.587 99.874  1.00 58.17  ? 496 PHE A O   1 
ATOM 3096 C CB  . PHE A 1 411 ? 130.918 125.055 103.166 1.00 52.41  ? 496 PHE A CB  1 
ATOM 3097 C CG  . PHE A 1 411 ? 131.369 123.704 102.692 1.00 57.77  ? 496 PHE A CG  1 
ATOM 3098 C CD1 . PHE A 1 411 ? 132.714 123.378 102.664 1.00 57.54  ? 496 PHE A CD1 1 
ATOM 3099 C CD2 . PHE A 1 411 ? 130.448 122.762 102.265 1.00 57.98  ? 496 PHE A CD2 1 
ATOM 3100 C CE1 . PHE A 1 411 ? 133.133 122.137 102.224 1.00 53.43  ? 496 PHE A CE1 1 
ATOM 3101 C CE2 . PHE A 1 411 ? 130.860 121.519 101.825 1.00 55.07  ? 496 PHE A CE2 1 
ATOM 3102 C CZ  . PHE A 1 411 ? 132.204 121.206 101.804 1.00 53.89  ? 496 PHE A CZ  1 
ATOM 3103 N N   . ASP A 1 412 ? 129.309 125.962 100.717 1.00 53.40  ? 497 ASP A N   1 
ATOM 3104 C CA  . ASP A 1 412 ? 128.668 125.711 99.429  1.00 54.27  ? 497 ASP A CA  1 
ATOM 3105 C C   . ASP A 1 412 ? 129.106 126.687 98.343  1.00 55.62  ? 497 ASP A C   1 
ATOM 3106 O O   . ASP A 1 412 ? 129.336 126.230 97.209  1.00 61.28  ? 497 ASP A O   1 
ATOM 3107 C CB  . ASP A 1 412 ? 127.140 125.715 99.582  1.00 58.37  ? 497 ASP A CB  1 
ATOM 3108 C CG  . ASP A 1 412 ? 126.613 124.441 100.212 1.00 67.97  ? 497 ASP A CG  1 
ATOM 3109 O OD1 . ASP A 1 412 ? 127.417 123.518 100.456 1.00 71.55  ? 497 ASP A OD1 1 
ATOM 3110 O OD2 . ASP A 1 412 ? 125.391 124.363 100.464 1.00 69.41  ? 497 ASP A OD2 1 
ATOM 3111 N N   . PRO A 1 413 ? 129.201 128.003 98.578  1.00 51.02  ? 498 PRO A N   1 
ATOM 3112 C CA  . PRO A 1 413 ? 129.721 128.879 97.513  1.00 48.63  ? 498 PRO A CA  1 
ATOM 3113 C C   . PRO A 1 413 ? 131.091 128.459 97.003  1.00 56.29  ? 498 PRO A C   1 
ATOM 3114 O O   . PRO A 1 413 ? 131.300 128.393 95.785  1.00 60.58  ? 498 PRO A O   1 
ATOM 3115 C CB  . PRO A 1 413 ? 129.752 130.252 98.191  1.00 49.10  ? 498 PRO A CB  1 
ATOM 3116 C CG  . PRO A 1 413 ? 128.641 130.201 99.162  1.00 50.79  ? 498 PRO A CG  1 
ATOM 3117 C CD  . PRO A 1 413 ? 128.608 128.788 99.680  1.00 53.65  ? 498 PRO A CD  1 
ATOM 3118 N N   . CYS A 1 414 ? 132.025 128.141 97.905  1.00 53.73  ? 499 CYS A N   1 
ATOM 3119 C CA  . CYS A 1 414 ? 133.343 127.683 97.477  1.00 48.13  ? 499 CYS A CA  1 
ATOM 3120 C C   . CYS A 1 414 ? 133.245 126.386 96.688  1.00 48.83  ? 499 CYS A C   1 
ATOM 3121 O O   . CYS A 1 414 ? 133.886 126.235 95.638  1.00 52.38  ? 499 CYS A O   1 
ATOM 3122 C CB  . CYS A 1 414 ? 134.255 127.493 98.691  1.00 54.74  ? 499 CYS A CB  1 
ATOM 3123 S SG  . CYS A 1 414 ? 134.946 129.008 99.378  1.00 71.43  ? 499 CYS A SG  1 
ATOM 3124 N N   . LYS A 1 415 ? 132.440 125.440 97.178  1.00 48.12  ? 500 LYS A N   1 
ATOM 3125 C CA  . LYS A 1 415 ? 132.320 124.147 96.516  1.00 47.91  ? 500 LYS A CA  1 
ATOM 3126 C C   . LYS A 1 415 ? 131.788 124.299 95.099  1.00 50.65  ? 500 LYS A C   1 
ATOM 3127 O O   . LYS A 1 415 ? 132.332 123.708 94.160  1.00 55.07  ? 500 LYS A O   1 
ATOM 3128 C CB  . LYS A 1 415 ? 131.411 123.226 97.331  1.00 51.22  ? 500 LYS A CB  1 
ATOM 3129 C CG  . LYS A 1 415 ? 131.164 121.872 96.690  1.00 55.44  ? 500 LYS A CG  1 
ATOM 3130 C CD  . LYS A 1 415 ? 130.303 120.993 97.580  1.00 58.60  ? 500 LYS A CD  1 
ATOM 3131 C CE  . LYS A 1 415 ? 128.870 121.499 97.629  1.00 56.90  ? 500 LYS A CE  1 
ATOM 3132 N NZ  . LYS A 1 415 ? 127.935 120.478 98.176  1.00 66.29  ? 500 LYS A NZ  1 
ATOM 3133 N N   . GLU A 1 416 ? 130.736 125.100 94.919  1.00 52.83  ? 501 GLU A N   1 
ATOM 3134 C CA  . GLU A 1 416 ? 130.167 125.266 93.586  1.00 49.22  ? 501 GLU A CA  1 
ATOM 3135 C C   . GLU A 1 416 ? 131.080 126.075 92.676  1.00 47.95  ? 501 GLU A C   1 
ATOM 3136 O O   . GLU A 1 416 ? 131.173 125.787 91.478  1.00 55.10  ? 501 GLU A O   1 
ATOM 3137 C CB  . GLU A 1 416 ? 128.782 125.915 93.659  1.00 52.34  ? 501 GLU A CB  1 
ATOM 3138 C CG  . GLU A 1 416 ? 127.866 125.425 94.781  1.00 52.91  ? 501 GLU A CG  1 
ATOM 3139 C CD  . GLU A 1 416 ? 127.659 123.914 94.829  1.00 59.24  ? 501 GLU A CD  1 
ATOM 3140 O OE1 . GLU A 1 416 ? 128.135 123.184 93.935  1.00 60.75  ? 501 GLU A OE1 1 
ATOM 3141 O OE2 . GLU A 1 416 ? 127.008 123.450 95.788  1.00 63.83  ? 501 GLU A OE2 1 
ATOM 3142 N N   . MET A 1 417 ? 131.762 127.088 93.213  1.00 46.63  ? 502 MET A N   1 
ATOM 3143 C CA  . MET A 1 417 ? 132.649 127.874 92.369  1.00 47.13  ? 502 MET A CA  1 
ATOM 3144 C C   . MET A 1 417 ? 133.888 127.102 91.953  1.00 51.75  ? 502 MET A C   1 
ATOM 3145 O O   . MET A 1 417 ? 134.503 127.446 90.939  1.00 55.87  ? 502 MET A O   1 
ATOM 3146 C CB  . MET A 1 417 ? 133.063 129.153 93.076  1.00 45.75  ? 502 MET A CB  1 
ATOM 3147 C CG  . MET A 1 417 ? 131.934 130.112 93.298  1.00 53.10  ? 502 MET A CG  1 
ATOM 3148 S SD  . MET A 1 417 ? 132.617 131.482 94.204  1.00 69.67  ? 502 MET A SD  1 
ATOM 3149 C CE  . MET A 1 417 ? 133.577 132.106 92.841  1.00 64.57  ? 502 MET A CE  1 
ATOM 3150 N N   . ALA A 1 418 ? 134.272 126.076 92.713  1.00 53.42  ? 503 ALA A N   1 
ATOM 3151 C CA  . ALA A 1 418 ? 135.361 125.216 92.269  1.00 50.71  ? 503 ALA A CA  1 
ATOM 3152 C C   . ALA A 1 418 ? 135.025 124.485 90.973  1.00 55.10  ? 503 ALA A C   1 
ATOM 3153 O O   . ALA A 1 418 ? 135.940 124.053 90.267  1.00 62.57  ? 503 ALA A O   1 
ATOM 3154 C CB  . ALA A 1 418 ? 135.719 124.209 93.363  1.00 52.50  ? 503 ALA A CB  1 
ATOM 3155 N N   . TYR A 1 419 ? 133.737 124.343 90.642  1.00 52.28  ? 504 TYR A N   1 
ATOM 3156 C CA  . TYR A 1 419 ? 133.337 123.657 89.418  1.00 47.75  ? 504 TYR A CA  1 
ATOM 3157 C C   . TYR A 1 419 ? 133.396 124.547 88.184  1.00 53.83  ? 504 TYR A C   1 
ATOM 3158 O O   . TYR A 1 419 ? 133.476 124.023 87.068  1.00 65.75  ? 504 TYR A O   1 
ATOM 3159 C CB  . TYR A 1 419 ? 131.911 123.112 89.547  1.00 45.08  ? 504 TYR A CB  1 
ATOM 3160 C CG  . TYR A 1 419 ? 131.744 121.968 90.521  1.00 47.85  ? 504 TYR A CG  1 
ATOM 3161 C CD1 . TYR A 1 419 ? 132.017 120.662 90.143  1.00 49.71  ? 504 TYR A CD1 1 
ATOM 3162 C CD2 . TYR A 1 419 ? 131.273 122.193 91.806  1.00 49.40  ? 504 TYR A CD2 1 
ATOM 3163 C CE1 . TYR A 1 419 ? 131.853 119.614 91.028  1.00 51.53  ? 504 TYR A CE1 1 
ATOM 3164 C CE2 . TYR A 1 419 ? 131.106 121.153 92.699  1.00 50.71  ? 504 TYR A CE2 1 
ATOM 3165 C CZ  . TYR A 1 419 ? 131.393 119.865 92.304  1.00 56.40  ? 504 TYR A CZ  1 
ATOM 3166 O OH  . TYR A 1 419 ? 131.228 118.827 93.191  1.00 64.13  ? 504 TYR A OH  1 
ATOM 3167 N N   . ILE A 1 420 ? 133.348 125.871 88.355  1.00 52.46  ? 505 ILE A N   1 
ATOM 3168 C CA  . ILE A 1 420 ? 133.149 126.765 87.210  1.00 53.10  ? 505 ILE A CA  1 
ATOM 3169 C C   . ILE A 1 420 ? 134.275 126.685 86.183  1.00 58.11  ? 505 ILE A C   1 
ATOM 3170 O O   . ILE A 1 420 ? 133.980 126.513 84.990  1.00 67.26  ? 505 ILE A O   1 
ATOM 3171 C CB  . ILE A 1 420 ? 132.902 128.202 87.699  1.00 45.87  ? 505 ILE A CB  1 
ATOM 3172 C CG1 . ILE A 1 420 ? 131.687 128.243 88.628  1.00 45.34  ? 505 ILE A CG1 1 
ATOM 3173 C CG2 . ILE A 1 420 ? 132.702 129.137 86.516  1.00 54.74  ? 505 ILE A CG2 1 
ATOM 3174 C CD1 . ILE A 1 420 ? 131.132 129.630 88.851  1.00 48.63  ? 505 ILE A CD1 1 
ATOM 3175 N N   . PRO A 1 421 ? 135.559 126.799 86.553  1.00 53.82  ? 506 PRO A N   1 
ATOM 3176 C CA  . PRO A 1 421 ? 136.606 126.839 85.516  1.00 55.83  ? 506 PRO A CA  1 
ATOM 3177 C C   . PRO A 1 421 ? 136.841 125.510 84.814  1.00 59.75  ? 506 PRO A C   1 
ATOM 3178 O O   . PRO A 1 421 ? 137.606 125.478 83.842  1.00 68.80  ? 506 PRO A O   1 
ATOM 3179 C CB  . PRO A 1 421 ? 137.848 127.282 86.295  1.00 63.64  ? 506 PRO A CB  1 
ATOM 3180 C CG  . PRO A 1 421 ? 137.625 126.735 87.649  1.00 60.42  ? 506 PRO A CG  1 
ATOM 3181 C CD  . PRO A 1 421 ? 136.148 126.896 87.902  1.00 57.32  ? 506 PRO A CD  1 
ATOM 3182 N N   . LEU A 1 422 ? 136.219 124.425 85.266  1.00 60.93  ? 507 LEU A N   1 
ATOM 3183 C CA  . LEU A 1 422 ? 136.401 123.131 84.630  1.00 63.09  ? 507 LEU A CA  1 
ATOM 3184 C C   . LEU A 1 422 ? 135.740 123.112 83.252  1.00 72.55  ? 507 LEU A C   1 
ATOM 3185 O O   . LEU A 1 422 ? 134.892 123.946 82.922  1.00 75.46  ? 507 LEU A O   1 
ATOM 3186 C CB  . LEU A 1 422 ? 135.817 122.022 85.505  1.00 58.02  ? 507 LEU A CB  1 
ATOM 3187 C CG  . LEU A 1 422 ? 136.669 121.517 86.669  1.00 58.83  ? 507 LEU A CG  1 
ATOM 3188 C CD1 . LEU A 1 422 ? 135.820 120.703 87.634  1.00 59.48  ? 507 LEU A CD1 1 
ATOM 3189 C CD2 . LEU A 1 422 ? 137.844 120.697 86.163  1.00 61.68  ? 507 LEU A CD2 1 
ATOM 3190 N N   . ASP A 1 423 ? 136.147 122.144 82.436  1.00 76.09  ? 508 ASP A N   1 
ATOM 3191 C CA  . ASP A 1 423 ? 135.468 121.895 81.174  1.00 79.65  ? 508 ASP A CA  1 
ATOM 3192 C C   . ASP A 1 423 ? 134.150 121.171 81.424  1.00 79.56  ? 508 ASP A C   1 
ATOM 3193 O O   . ASP A 1 423 ? 133.994 120.443 82.408  1.00 79.76  ? 508 ASP A O   1 
ATOM 3194 C CB  . ASP A 1 423 ? 136.360 121.090 80.225  1.00 78.83  ? 508 ASP A CB  1 
ATOM 3195 C CG  . ASP A 1 423 ? 136.901 119.826 80.859  1.00 80.45  ? 508 ASP A CG  1 
ATOM 3196 O OD1 . ASP A 1 423 ? 136.706 119.641 82.076  1.00 79.02  ? 508 ASP A OD1 1 
ATOM 3197 O OD2 . ASP A 1 423 ? 137.524 119.017 80.139  1.00 83.63  ? 508 ASP A OD2 1 
ATOM 3198 N N   . GLU A 1 424 ? 133.197 121.377 80.508  1.00 80.91  ? 509 GLU A N   1 
ATOM 3199 C CA  . GLU A 1 424 ? 131.814 120.972 80.752  1.00 79.60  ? 509 GLU A CA  1 
ATOM 3200 C C   . GLU A 1 424 ? 131.685 119.478 81.015  1.00 80.24  ? 509 GLU A C   1 
ATOM 3201 O O   . GLU A 1 424 ? 130.875 119.069 81.856  1.00 83.22  ? 509 GLU A O   1 
ATOM 3202 C CB  . GLU A 1 424 ? 130.937 121.387 79.572  1.00 81.45  ? 509 GLU A CB  1 
ATOM 3203 C CG  . GLU A 1 424 ? 131.278 122.763 79.041  1.00 90.82  ? 509 GLU A CG  1 
ATOM 3204 C CD  . GLU A 1 424 ? 131.059 123.843 80.081  1.00 99.68  ? 509 GLU A CD  1 
ATOM 3205 O OE1 . GLU A 1 424 ? 129.902 124.031 80.512  1.00 96.48  ? 509 GLU A OE1 1 
ATOM 3206 O OE2 . GLU A 1 424 ? 132.050 124.485 80.487  1.00 101.40 ? 509 GLU A OE2 1 
ATOM 3207 N N   . ASP A 1 425 ? 132.469 118.652 80.320  1.00 79.32  ? 510 ASP A N   1 
ATOM 3208 C CA  . ASP A 1 425 ? 132.459 117.218 80.586  1.00 80.58  ? 510 ASP A CA  1 
ATOM 3209 C C   . ASP A 1 425 ? 132.773 116.934 82.050  1.00 78.79  ? 510 ASP A C   1 
ATOM 3210 O O   . ASP A 1 425 ? 131.930 116.414 82.795  1.00 76.85  ? 510 ASP A O   1 
ATOM 3211 C CB  . ASP A 1 425 ? 133.464 116.515 79.669  1.00 87.56  ? 510 ASP A CB  1 
ATOM 3212 C CG  . ASP A 1 425 ? 133.491 115.012 79.873  1.00 99.58  ? 510 ASP A CG  1 
ATOM 3213 O OD1 . ASP A 1 425 ? 134.199 114.547 80.792  1.00 101.00 ? 510 ASP A OD1 1 
ATOM 3214 O OD2 . ASP A 1 425 ? 132.808 114.294 79.113  1.00 105.46 ? 510 ASP A OD2 1 
ATOM 3215 N N   . THR A 1 426 ? 133.986 117.290 82.482  1.00 80.55  ? 511 THR A N   1 
ATOM 3216 C CA  . THR A 1 426 ? 134.382 117.048 83.864  1.00 72.55  ? 511 THR A CA  1 
ATOM 3217 C C   . THR A 1 426 ? 133.501 117.825 84.829  1.00 68.02  ? 511 THR A C   1 
ATOM 3218 O O   . THR A 1 426 ? 133.136 117.309 85.887  1.00 69.04  ? 511 THR A O   1 
ATOM 3219 C CB  . THR A 1 426 ? 135.853 117.412 84.070  1.00 74.13  ? 511 THR A CB  1 
ATOM 3220 O OG1 . THR A 1 426 ? 136.671 116.611 83.207  1.00 85.58  ? 511 THR A OG1 1 
ATOM 3221 C CG2 . THR A 1 426 ? 136.270 117.173 85.515  1.00 74.04  ? 511 THR A CG2 1 
ATOM 3222 N N   . LYS A 1 427 ? 133.137 119.060 84.479  1.00 71.17  ? 512 LYS A N   1 
ATOM 3223 C CA  . LYS A 1 427 ? 132.262 119.850 85.341  1.00 66.59  ? 512 LYS A CA  1 
ATOM 3224 C C   . LYS A 1 427 ? 130.993 119.078 85.687  1.00 67.45  ? 512 LYS A C   1 
ATOM 3225 O O   . LYS A 1 427 ? 130.729 118.782 86.859  1.00 67.13  ? 512 LYS A O   1 
ATOM 3226 C CB  . LYS A 1 427 ? 131.919 121.179 84.662  1.00 61.98  ? 512 LYS A CB  1 
ATOM 3227 C CG  . LYS A 1 427 ? 131.150 122.150 85.544  1.00 59.68  ? 512 LYS A CG  1 
ATOM 3228 C CD  . LYS A 1 427 ? 130.579 123.302 84.731  1.00 60.40  ? 512 LYS A CD  1 
ATOM 3229 C CE  . LYS A 1 427 ? 131.647 124.336 84.416  1.00 58.34  ? 512 LYS A CE  1 
ATOM 3230 N NZ  . LYS A 1 427 ? 131.068 125.683 84.160  1.00 63.48  ? 512 LYS A NZ  1 
ATOM 3231 N N   . VAL A 1 428 ? 130.217 118.707 84.666  1.00 67.23  ? 513 VAL A N   1 
ATOM 3232 C CA  . VAL A 1 428 ? 128.936 118.042 84.898  1.00 62.51  ? 513 VAL A CA  1 
ATOM 3233 C C   . VAL A 1 428 ? 129.142 116.692 85.580  1.00 66.11  ? 513 VAL A C   1 
ATOM 3234 O O   . VAL A 1 428 ? 128.455 116.359 86.558  1.00 68.24  ? 513 VAL A O   1 
ATOM 3235 C CB  . VAL A 1 428 ? 128.165 117.894 83.573  1.00 61.91  ? 513 VAL A CB  1 
ATOM 3236 C CG1 . VAL A 1 428 ? 126.887 117.101 83.783  1.00 62.88  ? 513 VAL A CG1 1 
ATOM 3237 C CG2 . VAL A 1 428 ? 127.853 119.263 82.984  1.00 66.96  ? 513 VAL A CG2 1 
ATOM 3238 N N   . LYS A 1 429 ? 130.094 115.894 85.082  1.00 64.61  ? 514 LYS A N   1 
ATOM 3239 C CA  . LYS A 1 429 ? 130.238 114.537 85.604  1.00 60.18  ? 514 LYS A CA  1 
ATOM 3240 C C   . LYS A 1 429 ? 130.734 114.532 87.044  1.00 63.16  ? 514 LYS A C   1 
ATOM 3241 O O   . LYS A 1 429 ? 130.211 113.785 87.877  1.00 65.73  ? 514 LYS A O   1 
ATOM 3242 C CB  . LYS A 1 429 ? 131.168 113.720 84.711  1.00 65.27  ? 514 LYS A CB  1 
ATOM 3243 C CG  . LYS A 1 429 ? 130.699 113.646 83.280  1.00 68.48  ? 514 LYS A CG  1 
ATOM 3244 C CD  . LYS A 1 429 ? 129.789 112.458 83.075  1.00 72.89  ? 514 LYS A CD  1 
ATOM 3245 C CE  . LYS A 1 429 ? 129.353 112.385 81.637  1.00 79.64  ? 514 LYS A CE  1 
ATOM 3246 N NZ  . LYS A 1 429 ? 130.537 112.415 80.735  1.00 86.15  ? 514 LYS A NZ  1 
ATOM 3247 N N   . GLY A 1 430 ? 131.747 115.342 87.357  1.00 63.48  ? 515 GLY A N   1 
ATOM 3248 C CA  . GLY A 1 430 ? 132.206 115.438 88.728  1.00 60.36  ? 515 GLY A CA  1 
ATOM 3249 C C   . GLY A 1 430 ? 131.162 116.037 89.647  1.00 60.19  ? 515 GLY A C   1 
ATOM 3250 O O   . GLY A 1 430 ? 131.041 115.627 90.802  1.00 63.17  ? 515 GLY A O   1 
ATOM 3251 N N   . LYS A 1 431 ? 130.385 117.002 89.149  1.00 60.55  ? 516 LYS A N   1 
ATOM 3252 C CA  . LYS A 1 431 ? 129.288 117.546 89.939  1.00 56.50  ? 516 LYS A CA  1 
ATOM 3253 C C   . LYS A 1 431 ? 128.325 116.442 90.351  1.00 54.17  ? 516 LYS A C   1 
ATOM 3254 O O   . LYS A 1 431 ? 127.973 116.309 91.530  1.00 57.92  ? 516 LYS A O   1 
ATOM 3255 C CB  . LYS A 1 431 ? 128.565 118.627 89.136  1.00 62.22  ? 516 LYS A CB  1 
ATOM 3256 C CG  . LYS A 1 431 ? 127.465 119.332 89.893  1.00 54.35  ? 516 LYS A CG  1 
ATOM 3257 C CD  . LYS A 1 431 ? 128.044 120.389 90.808  1.00 49.86  ? 516 LYS A CD  1 
ATOM 3258 C CE  . LYS A 1 431 ? 126.955 121.056 91.615  1.00 52.01  ? 516 LYS A CE  1 
ATOM 3259 N NZ  . LYS A 1 431 ? 127.385 121.306 93.014  1.00 58.86  ? 516 LYS A NZ  1 
ATOM 3260 N N   . ALA A 1 432 ? 127.913 115.619 89.385  1.00 59.58  ? 517 ALA A N   1 
ATOM 3261 C CA  . ALA A 1 432 ? 127.011 114.513 89.686  1.00 59.72  ? 517 ALA A CA  1 
ATOM 3262 C C   . ALA A 1 432 ? 127.658 113.517 90.642  1.00 61.55  ? 517 ALA A C   1 
ATOM 3263 O O   . ALA A 1 432 ? 127.062 113.124 91.650  1.00 64.63  ? 517 ALA A O   1 
ATOM 3264 C CB  . ALA A 1 432 ? 126.587 113.820 88.394  1.00 57.65  ? 517 ALA A CB  1 
ATOM 3265 N N   . ALA A 1 433 ? 128.892 113.103 90.344  1.00 62.63  ? 518 ALA A N   1 
ATOM 3266 C CA  . ALA A 1 433 ? 129.539 112.053 91.124  1.00 58.50  ? 518 ALA A CA  1 
ATOM 3267 C C   . ALA A 1 433 ? 129.900 112.501 92.533  1.00 59.93  ? 518 ALA A C   1 
ATOM 3268 O O   . ALA A 1 433 ? 130.082 111.649 93.409  1.00 66.55  ? 518 ALA A O   1 
ATOM 3269 C CB  . ALA A 1 433 ? 130.792 111.559 90.402  1.00 60.73  ? 518 ALA A CB  1 
ATOM 3270 N N   . ILE A 1 434 ? 130.011 113.805 92.775  1.00 59.24  ? 519 ILE A N   1 
ATOM 3271 C CA  . ILE A 1 434 ? 130.375 114.307 94.092  1.00 56.06  ? 519 ILE A CA  1 
ATOM 3272 C C   . ILE A 1 434 ? 129.116 114.610 94.892  1.00 64.04  ? 519 ILE A C   1 
ATOM 3273 O O   . ILE A 1 434 ? 128.926 114.079 95.992  1.00 71.30  ? 519 ILE A O   1 
ATOM 3274 C CB  . ILE A 1 434 ? 131.268 115.556 93.981  1.00 52.75  ? 519 ILE A CB  1 
ATOM 3275 C CG1 . ILE A 1 434 ? 132.664 115.176 93.485  1.00 52.56  ? 519 ILE A CG1 1 
ATOM 3276 C CG2 . ILE A 1 434 ? 131.357 116.268 95.320  1.00 57.08  ? 519 ILE A CG2 1 
ATOM 3277 C CD1 . ILE A 1 434 ? 133.569 116.364 93.262  1.00 54.98  ? 519 ILE A CD1 1 
ATOM 3278 N N   . ASP A 1 435 ? 128.244 115.458 94.345  1.00 64.64  ? 520 ASP A N   1 
ATOM 3279 C CA  . ASP A 1 435 ? 127.102 115.926 95.123  1.00 64.37  ? 520 ASP A CA  1 
ATOM 3280 C C   . ASP A 1 435 ? 125.994 114.888 95.260  1.00 65.80  ? 520 ASP A C   1 
ATOM 3281 O O   . ASP A 1 435 ? 125.041 115.135 96.007  1.00 71.52  ? 520 ASP A O   1 
ATOM 3282 C CB  . ASP A 1 435 ? 126.550 117.212 94.510  1.00 65.21  ? 520 ASP A CB  1 
ATOM 3283 C CG  . ASP A 1 435 ? 127.571 118.333 94.498  1.00 69.07  ? 520 ASP A CG  1 
ATOM 3284 O OD1 . ASP A 1 435 ? 128.451 118.332 93.612  1.00 68.96  ? 520 ASP A OD1 1 
ATOM 3285 O OD2 . ASP A 1 435 ? 127.500 119.212 95.384  1.00 67.93  ? 520 ASP A OD2 1 
ATOM 3286 N N   . VAL A 1 436 ? 126.082 113.751 94.576  1.00 62.21  ? 521 VAL A N   1 
ATOM 3287 C CA  . VAL A 1 436 ? 125.120 112.671 94.729  1.00 62.00  ? 521 VAL A CA  1 
ATOM 3288 C C   . VAL A 1 436 ? 125.695 111.513 95.535  1.00 67.03  ? 521 VAL A C   1 
ATOM 3289 O O   . VAL A 1 436 ? 125.001 110.934 96.372  1.00 71.51  ? 521 VAL A O   1 
ATOM 3290 C CB  . VAL A 1 436 ? 124.610 112.182 93.354  1.00 62.00  ? 521 VAL A CB  1 
ATOM 3291 C CG1 . VAL A 1 436 ? 123.690 110.990 93.519  1.00 64.52  ? 521 VAL A CG1 1 
ATOM 3292 C CG2 . VAL A 1 436 ? 123.886 113.292 92.635  1.00 62.94  ? 521 VAL A CG2 1 
ATOM 3293 N N   . VAL A 1 437 ? 126.961 111.174 95.312  1.00 65.48  ? 522 VAL A N   1 
ATOM 3294 C CA  . VAL A 1 437 ? 127.565 109.966 95.859  1.00 61.27  ? 522 VAL A CA  1 
ATOM 3295 C C   . VAL A 1 437 ? 128.500 110.282 97.024  1.00 65.43  ? 522 VAL A C   1 
ATOM 3296 O O   . VAL A 1 437 ? 128.427 109.648 98.078  1.00 73.03  ? 522 VAL A O   1 
ATOM 3297 C CB  . VAL A 1 437 ? 128.301 109.174 94.754  1.00 59.56  ? 522 VAL A CB  1 
ATOM 3298 C CG1 . VAL A 1 437 ? 129.006 107.968 95.336  1.00 57.11  ? 522 VAL A CG1 1 
ATOM 3299 C CG2 . VAL A 1 437 ? 127.324 108.748 93.675  1.00 64.33  ? 522 VAL A CG2 1 
ATOM 3300 N N   . CYS A 1 438 ? 129.386 111.265 96.851  1.00 64.62  ? 523 CYS A N   1 
ATOM 3301 C CA  . CYS A 1 438 ? 130.446 111.498 97.828  1.00 64.74  ? 523 CYS A CA  1 
ATOM 3302 C C   . CYS A 1 438 ? 129.931 112.046 99.155  1.00 68.46  ? 523 CYS A C   1 
ATOM 3303 O O   . CYS A 1 438 ? 130.537 111.774 100.194 1.00 72.57  ? 523 CYS A O   1 
ATOM 3304 C CB  . CYS A 1 438 ? 131.495 112.443 97.242  1.00 67.31  ? 523 CYS A CB  1 
ATOM 3305 S SG  . CYS A 1 438 ? 132.677 111.624 96.147  1.00 78.16  ? 523 CYS A SG  1 
ATOM 3306 N N   . ASN A 1 439 ? 128.838 112.806 99.152  1.00 69.87  ? 524 ASN A N   1 
ATOM 3307 C CA  . ASN A 1 439 ? 128.283 113.373 100.380 1.00 69.60  ? 524 ASN A CA  1 
ATOM 3308 C C   . ASN A 1 439 ? 127.609 112.289 101.228 1.00 69.28  ? 524 ASN A C   1 
ATOM 3309 O O   . ASN A 1 439 ? 127.854 112.208 102.448 1.00 74.54  ? 524 ASN A O   1 
ATOM 3310 C CB  . ASN A 1 439 ? 127.317 114.513 100.030 1.00 72.99  ? 524 ASN A CB  1 
ATOM 3311 C CG  . ASN A 1 439 ? 126.968 115.377 101.221 1.00 81.77  ? 524 ASN A CG  1 
ATOM 3312 O OD1 . ASN A 1 439 ? 126.321 114.925 102.165 1.00 85.70  ? 524 ASN A OD1 1 
ATOM 3313 N ND2 . ASN A 1 439 ? 127.382 116.638 101.175 1.00 80.71  ? 524 ASN A ND2 1 
ATOM 3314 N N   . PRO A 1 440 ? 126.748 111.442 100.643 1.00 67.91  ? 525 PRO A N   1 
ATOM 3315 C CA  . PRO A 1 440 ? 126.277 110.279 101.405 1.00 66.44  ? 525 PRO A CA  1 
ATOM 3316 C C   . PRO A 1 440 ? 127.406 109.366 101.841 1.00 68.20  ? 525 PRO A C   1 
ATOM 3317 O O   . PRO A 1 440 ? 127.310 108.764 102.917 1.00 71.80  ? 525 PRO A O   1 
ATOM 3318 C CB  . PRO A 1 440 ? 125.325 109.579 100.428 1.00 66.92  ? 525 PRO A CB  1 
ATOM 3319 C CG  . PRO A 1 440 ? 124.838 110.664 99.558  1.00 69.00  ? 525 PRO A CG  1 
ATOM 3320 C CD  . PRO A 1 440 ? 126.028 111.552 99.357  1.00 69.42  ? 525 PRO A CD  1 
ATOM 3321 N N   . LEU A 1 441 ? 128.476 109.246 101.049 1.00 68.34  ? 526 LEU A N   1 
ATOM 3322 C CA  . LEU A 1 441 ? 129.637 108.496 101.514 1.00 65.85  ? 526 LEU A CA  1 
ATOM 3323 C C   . LEU A 1 441 ? 130.296 109.165 102.708 1.00 70.12  ? 526 LEU A C   1 
ATOM 3324 O O   . LEU A 1 441 ? 130.812 108.475 103.585 1.00 73.79  ? 526 LEU A O   1 
ATOM 3325 C CB  . LEU A 1 441 ? 130.667 108.305 100.401 1.00 63.40  ? 526 LEU A CB  1 
ATOM 3326 C CG  . LEU A 1 441 ? 130.458 107.125 99.455  1.00 67.12  ? 526 LEU A CG  1 
ATOM 3327 C CD1 . LEU A 1 441 ? 131.062 107.427 98.101  1.00 69.04  ? 526 LEU A CD1 1 
ATOM 3328 C CD2 . LEU A 1 441 ? 131.056 105.856 100.046 1.00 71.11  ? 526 LEU A CD2 1 
ATOM 3329 N N   . GLY A 1 442 ? 130.306 110.497 102.759 1.00 65.53  ? 527 GLY A N   1 
ATOM 3330 C CA  . GLY A 1 442 ? 130.826 111.166 103.941 1.00 64.11  ? 527 GLY A CA  1 
ATOM 3331 C C   . GLY A 1 442 ? 130.022 110.829 105.183 1.00 69.37  ? 527 GLY A C   1 
ATOM 3332 O O   . GLY A 1 442 ? 130.581 110.486 106.231 1.00 71.08  ? 527 GLY A O   1 
ATOM 3333 N N   . LYS A 1 443 ? 128.692 110.898 105.073 1.00 71.40  ? 528 LYS A N   1 
ATOM 3334 C CA  . LYS A 1 443 ? 127.858 110.536 106.220 1.00 64.30  ? 528 LYS A CA  1 
ATOM 3335 C C   . LYS A 1 443 ? 128.053 109.073 106.613 1.00 65.69  ? 528 LYS A C   1 
ATOM 3336 O O   . LYS A 1 443 ? 128.190 108.749 107.804 1.00 71.00  ? 528 LYS A O   1 
ATOM 3337 C CB  . LYS A 1 443 ? 126.383 110.817 105.928 1.00 68.66  ? 528 LYS A CB  1 
ATOM 3338 C CG  . LYS A 1 443 ? 125.984 112.277 106.060 1.00 75.60  ? 528 LYS A CG  1 
ATOM 3339 C CD  . LYS A 1 443 ? 124.495 112.459 105.812 1.00 84.29  ? 528 LYS A CD  1 
ATOM 3340 C CE  . LYS A 1 443 ? 123.737 112.578 107.128 1.00 82.86  ? 528 LYS A CE  1 
ATOM 3341 N NZ  . LYS A 1 443 ? 122.265 112.689 106.927 1.00 85.63  ? 528 LYS A NZ  1 
ATOM 3342 N N   . SER A 1 444 ? 128.078 108.176 105.624 1.00 63.88  ? 529 SER A N   1 
ATOM 3343 C CA  . SER A 1 444 ? 128.243 106.754 105.903 1.00 62.88  ? 529 SER A CA  1 
ATOM 3344 C C   . SER A 1 444 ? 129.606 106.466 106.515 1.00 65.48  ? 529 SER A C   1 
ATOM 3345 O O   . SER A 1 444 ? 129.728 105.614 107.400 1.00 71.61  ? 529 SER A O   1 
ATOM 3346 C CB  . SER A 1 444 ? 128.047 105.943 104.622 1.00 69.67  ? 529 SER A CB  1 
ATOM 3347 O OG  . SER A 1 444 ? 126.706 106.016 104.172 1.00 73.79  ? 529 SER A OG  1 
ATOM 3348 N N   . GLY A 1 445 ? 130.646 107.159 106.049 1.00 67.43  ? 530 GLY A N   1 
ATOM 3349 C CA  . GLY A 1 445 ? 131.966 106.978 106.620 1.00 67.58  ? 530 GLY A CA  1 
ATOM 3350 C C   . GLY A 1 445 ? 132.047 107.462 108.051 1.00 68.98  ? 530 GLY A C   1 
ATOM 3351 O O   . GLY A 1 445 ? 132.696 106.834 108.886 1.00 70.74  ? 530 GLY A O   1 
ATOM 3352 N N   . GLY A 1 446 ? 131.388 108.581 108.359 1.00 68.01  ? 531 GLY A N   1 
ATOM 3353 C CA  . GLY A 1 446 ? 131.324 109.016 109.747 1.00 63.33  ? 531 GLY A CA  1 
ATOM 3354 C C   . GLY A 1 446 ? 130.636 107.996 110.636 1.00 67.38  ? 531 GLY A C   1 
ATOM 3355 O O   . GLY A 1 446 ? 131.118 107.669 111.729 1.00 71.26  ? 531 GLY A O   1 
ATOM 3356 N N   . ALA A 1 447 ? 129.501 107.466 110.168 1.00 72.36  ? 532 ALA A N   1 
ATOM 3357 C CA  . ALA A 1 447 ? 128.790 106.452 110.943 1.00 66.10  ? 532 ALA A CA  1 
ATOM 3358 C C   . ALA A 1 447 ? 129.636 105.195 111.124 1.00 67.43  ? 532 ALA A C   1 
ATOM 3359 O O   . ALA A 1 447 ? 129.688 104.625 112.221 1.00 71.02  ? 532 ALA A O   1 
ATOM 3360 C CB  . ALA A 1 447 ? 127.461 106.113 110.268 1.00 65.81  ? 532 ALA A CB  1 
ATOM 3361 N N   . LEU A 1 448 ? 130.308 104.753 110.058 1.00 70.65  ? 533 LEU A N   1 
ATOM 3362 C CA  . LEU A 1 448 ? 131.159 103.570 110.137 1.00 65.04  ? 533 LEU A CA  1 
ATOM 3363 C C   . LEU A 1 448 ? 132.334 103.800 111.076 1.00 65.07  ? 533 LEU A C   1 
ATOM 3364 O O   . LEU A 1 448 ? 132.738 102.892 111.808 1.00 73.81  ? 533 LEU A O   1 
ATOM 3365 C CB  . LEU A 1 448 ? 131.655 103.194 108.741 1.00 64.79  ? 533 LEU A CB  1 
ATOM 3366 C CG  . LEU A 1 448 ? 131.967 101.719 108.481 1.00 72.96  ? 533 LEU A CG  1 
ATOM 3367 C CD1 . LEU A 1 448 ? 130.709 100.874 108.595 1.00 73.69  ? 533 LEU A CD1 1 
ATOM 3368 C CD2 . LEU A 1 448 ? 132.615 101.544 107.116 1.00 74.34  ? 533 LEU A CD2 1 
ATOM 3369 N N   . ILE A 1 449 ? 132.901 105.005 111.057 1.00 63.72  ? 534 ILE A N   1 
ATOM 3370 C CA  . ILE A 1 449 ? 133.993 105.350 111.962 1.00 61.33  ? 534 ILE A CA  1 
ATOM 3371 C C   . ILE A 1 449 ? 133.541 105.241 113.412 1.00 65.28  ? 534 ILE A C   1 
ATOM 3372 O O   . ILE A 1 449 ? 134.221 104.634 114.252 1.00 72.32  ? 534 ILE A O   1 
ATOM 3373 C CB  . ILE A 1 449 ? 134.513 106.762 111.637 1.00 62.68  ? 534 ILE A CB  1 
ATOM 3374 C CG1 . ILE A 1 449 ? 135.444 106.737 110.419 1.00 64.39  ? 534 ILE A CG1 1 
ATOM 3375 C CG2 . ILE A 1 449 ? 135.145 107.390 112.847 1.00 60.65  ? 534 ILE A CG2 1 
ATOM 3376 C CD1 . ILE A 1 449 ? 135.816 108.113 109.909 1.00 61.29  ? 534 ILE A CD1 1 
ATOM 3377 N N   . GLN A 1 450 ? 132.387 105.832 113.729 1.00 64.75  ? 535 GLN A N   1 
ATOM 3378 C CA  . GLN A 1 450 ? 131.903 105.769 115.106 1.00 59.43  ? 535 GLN A CA  1 
ATOM 3379 C C   . GLN A 1 450 ? 131.580 104.337 115.515 1.00 64.40  ? 535 GLN A C   1 
ATOM 3380 O O   . GLN A 1 450 ? 131.871 103.925 116.646 1.00 70.28  ? 535 GLN A O   1 
ATOM 3381 C CB  . GLN A 1 450 ? 130.687 106.675 115.283 1.00 58.18  ? 535 GLN A CB  1 
ATOM 3382 C CG  . GLN A 1 450 ? 131.022 108.152 115.314 1.00 57.78  ? 535 GLN A CG  1 
ATOM 3383 C CD  . GLN A 1 450 ? 129.788 109.030 115.327 1.00 61.87  ? 535 GLN A CD  1 
ATOM 3384 O OE1 . GLN A 1 450 ? 129.700 109.985 116.098 1.00 66.08  ? 535 GLN A OE1 1 
ATOM 3385 N NE2 . GLN A 1 450 ? 128.826 108.710 114.469 1.00 59.46  ? 535 GLN A NE2 1 
ATOM 3386 N N   . GLN A 1 451 ? 130.988 103.556 114.607 1.00 67.75  ? 536 GLN A N   1 
ATOM 3387 C CA  . GLN A 1 451 ? 130.684 102.165 114.926 1.00 64.25  ? 536 GLN A CA  1 
ATOM 3388 C C   . GLN A 1 451 ? 131.956 101.353 115.143 1.00 67.09  ? 536 GLN A C   1 
ATOM 3389 O O   . GLN A 1 451 ? 132.001 100.484 116.021 1.00 73.13  ? 536 GLN A O   1 
ATOM 3390 C CB  . GLN A 1 451 ? 129.829 101.545 113.821 1.00 61.28  ? 536 GLN A CB  1 
ATOM 3391 C CG  . GLN A 1 451 ? 129.103 100.281 114.246 1.00 70.58  ? 536 GLN A CG  1 
ATOM 3392 C CD  . GLN A 1 451 ? 127.911 100.569 115.138 1.00 76.61  ? 536 GLN A CD  1 
ATOM 3393 O OE1 . GLN A 1 451 ? 127.882 100.173 116.303 1.00 79.45  ? 536 GLN A OE1 1 
ATOM 3394 N NE2 . GLN A 1 451 ? 126.919 101.263 114.593 1.00 75.96  ? 536 GLN A NE2 1 
ATOM 3395 N N   . PHE A 1 452 ? 132.994 101.609 114.343 1.00 69.49  ? 537 PHE A N   1 
ATOM 3396 C CA  . PHE A 1 452 ? 134.270 100.930 114.539 1.00 71.84  ? 537 PHE A CA  1 
ATOM 3397 C C   . PHE A 1 452 ? 134.883 101.286 115.885 1.00 75.52  ? 537 PHE A C   1 
ATOM 3398 O O   . PHE A 1 452 ? 135.415 100.412 116.578 1.00 80.19  ? 537 PHE A O   1 
ATOM 3399 C CB  . PHE A 1 452 ? 135.233 101.279 113.404 1.00 73.08  ? 537 PHE A CB  1 
ATOM 3400 C CG  . PHE A 1 452 ? 136.518 100.500 113.442 1.00 82.24  ? 537 PHE A CG  1 
ATOM 3401 C CD1 . PHE A 1 452 ? 136.506 99.116  113.460 1.00 85.92  ? 537 PHE A CD1 1 
ATOM 3402 C CD2 . PHE A 1 452 ? 137.738 101.155 113.462 1.00 82.56  ? 537 PHE A CD2 1 
ATOM 3403 C CE1 . PHE A 1 452 ? 137.687 98.398  113.496 1.00 86.23  ? 537 PHE A CE1 1 
ATOM 3404 C CE2 . PHE A 1 452 ? 138.923 100.444 113.497 1.00 81.02  ? 537 PHE A CE2 1 
ATOM 3405 C CZ  . PHE A 1 452 ? 138.897 99.063  113.514 1.00 84.78  ? 537 PHE A CZ  1 
ATOM 3406 N N   . MET A 1 453 ? 134.816 102.561 116.273 1.00 73.48  ? 538 MET A N   1 
ATOM 3407 C CA  . MET A 1 453 ? 135.298 102.943 117.598 1.00 70.93  ? 538 MET A CA  1 
ATOM 3408 C C   . MET A 1 453 ? 134.507 102.244 118.698 1.00 72.81  ? 538 MET A C   1 
ATOM 3409 O O   . MET A 1 453 ? 135.079 101.824 119.713 1.00 79.76  ? 538 MET A O   1 
ATOM 3410 C CB  . MET A 1 453 ? 135.252 104.461 117.761 1.00 65.15  ? 538 MET A CB  1 
ATOM 3411 C CG  . MET A 1 453 ? 136.200 105.180 116.822 1.00 68.88  ? 538 MET A CG  1 
ATOM 3412 S SD  . MET A 1 453 ? 137.895 104.714 117.235 1.00 102.70 ? 538 MET A SD  1 
ATOM 3413 C CE  . MET A 1 453 ? 138.818 105.458 115.898 1.00 80.11  ? 538 MET A CE  1 
ATOM 3414 N N   . ILE A 1 454 ? 133.193 102.097 118.511 1.00 70.94  ? 539 ILE A N   1 
ATOM 3415 C CA  . ILE A 1 454 ? 132.378 101.391 119.499 1.00 66.00  ? 539 ILE A CA  1 
ATOM 3416 C C   . ILE A 1 454 ? 132.823 99.938  119.619 1.00 71.52  ? 539 ILE A C   1 
ATOM 3417 O O   . ILE A 1 454 ? 133.135 99.454  120.712 1.00 75.16  ? 539 ILE A O   1 
ATOM 3418 C CB  . ILE A 1 454 ? 130.885 101.484 119.139 1.00 62.66  ? 539 ILE A CB  1 
ATOM 3419 C CG1 . ILE A 1 454 ? 130.380 102.916 119.304 1.00 62.44  ? 539 ILE A CG1 1 
ATOM 3420 C CG2 . ILE A 1 454 ? 130.071 100.522 119.992 1.00 65.11  ? 539 ILE A CG2 1 
ATOM 3421 C CD1 . ILE A 1 454 ? 128.918 103.067 118.988 1.00 64.60  ? 539 ILE A CD1 1 
ATOM 3422 N N   . LEU A 1 455 ? 132.874 99.224  118.491 1.00 74.64  ? 540 LEU A N   1 
ATOM 3423 C CA  . LEU A 1 455 ? 133.246 97.811  118.538 1.00 72.96  ? 540 LEU A CA  1 
ATOM 3424 C C   . LEU A 1 455 ? 134.681 97.604  118.995 1.00 71.20  ? 540 LEU A C   1 
ATOM 3425 O O   . LEU A 1 455 ? 135.008 96.526  119.503 1.00 77.63  ? 540 LEU A O   1 
ATOM 3426 C CB  . LEU A 1 455 ? 133.038 97.140  117.178 1.00 70.91  ? 540 LEU A CB  1 
ATOM 3427 C CG  . LEU A 1 455 ? 131.747 97.424  116.413 1.00 73.53  ? 540 LEU A CG  1 
ATOM 3428 C CD1 . LEU A 1 455 ? 131.801 96.797  115.030 1.00 75.24  ? 540 LEU A CD1 1 
ATOM 3429 C CD2 . LEU A 1 455 ? 130.549 96.905  117.192 1.00 74.77  ? 540 LEU A CD2 1 
ATOM 3430 N N   . SER A 1 456 ? 135.545 98.602  118.823 1.00 70.50  ? 541 SER A N   1 
ATOM 3431 C CA  . SER A 1 456 ? 136.901 98.483  119.339 1.00 78.52  ? 541 SER A CA  1 
ATOM 3432 C C   . SER A 1 456 ? 136.943 98.677  120.850 1.00 80.29  ? 541 SER A C   1 
ATOM 3433 O O   . SER A 1 456 ? 137.588 97.897  121.560 1.00 81.38  ? 541 SER A O   1 
ATOM 3434 C CB  . SER A 1 456 ? 137.815 99.496  118.647 1.00 79.81  ? 541 SER A CB  1 
ATOM 3435 O OG  . SER A 1 456 ? 137.587 99.512  117.248 1.00 80.73  ? 541 SER A OG  1 
ATOM 3436 N N   . PHE A 1 457 ? 136.376 99.791  121.318 1.00 77.21  ? 542 PHE A N   1 
ATOM 3437 C CA  . PHE A 1 457 ? 136.361 100.182 122.704 1.00 73.12  ? 542 PHE A CA  1 
ATOM 3438 C C   . PHE A 1 457 ? 135.037 100.261 123.416 1.00 74.20  ? 542 PHE A C   1 
ATOM 3439 O O   . PHE A 1 457 ? 134.859 101.059 124.240 1.00 80.08  ? 542 PHE A O   1 
ATOM 3440 C CB  . PHE A 1 457 ? 136.934 101.541 122.743 1.00 74.83  ? 542 PHE A CB  1 
ATOM 3441 C CG  . PHE A 1 457 ? 138.038 101.782 121.795 1.00 80.31  ? 542 PHE A CG  1 
ATOM 3442 C CD1 . PHE A 1 457 ? 139.324 101.536 122.155 1.00 88.78  ? 542 PHE A CD1 1 
ATOM 3443 C CD2 . PHE A 1 457 ? 137.790 102.336 120.584 1.00 77.30  ? 542 PHE A CD2 1 
ATOM 3444 C CE1 . PHE A 1 457 ? 140.352 101.791 121.289 1.00 92.13  ? 542 PHE A CE1 1 
ATOM 3445 C CE2 . PHE A 1 457 ? 138.798 102.595 119.708 1.00 81.70  ? 542 PHE A CE2 1 
ATOM 3446 C CZ  . PHE A 1 457 ? 140.086 102.325 120.060 1.00 88.95  ? 542 PHE A CZ  1 
ATOM 3447 N N   . GLY A 1 458 ? 134.073 99.520  123.040 1.00 74.14  ? 543 GLY A N   1 
ATOM 3448 C CA  . GLY A 1 458 ? 132.845 99.355  123.788 1.00 75.33  ? 543 GLY A CA  1 
ATOM 3449 C C   . GLY A 1 458 ? 131.957 100.576 123.872 1.00 75.55  ? 543 GLY A C   1 
ATOM 3450 O O   . GLY A 1 458 ? 130.743 100.427 124.060 1.00 78.28  ? 543 GLY A O   1 
ATOM 3451 N N   . SER A 1 459 ? 132.510 101.779 123.739 1.00 71.28  ? 544 SER A N   1 
ATOM 3452 C CA  . SER A 1 459 ? 131.729 102.994 123.904 1.00 70.52  ? 544 SER A CA  1 
ATOM 3453 C C   . SER A 1 459 ? 132.366 104.123 123.110 1.00 72.90  ? 544 SER A C   1 
ATOM 3454 O O   . SER A 1 459 ? 133.562 104.091 122.806 1.00 76.48  ? 544 SER A O   1 
ATOM 3455 C CB  . SER A 1 459 ? 131.621 103.388 125.383 1.00 74.80  ? 544 SER A CB  1 
ATOM 3456 O OG  . SER A 1 459 ? 130.888 104.589 125.543 1.00 81.50  ? 544 SER A OG  1 
ATOM 3457 N N   . LEU A 1 460 ? 131.551 105.124 122.775 1.00 69.97  ? 545 LEU A N   1 
ATOM 3458 C CA  . LEU A 1 460 ? 132.080 106.359 122.213 1.00 67.42  ? 545 LEU A CA  1 
ATOM 3459 C C   . LEU A 1 460 ? 132.701 107.257 123.272 1.00 72.62  ? 545 LEU A C   1 
ATOM 3460 O O   . LEU A 1 460 ? 133.425 108.195 122.920 1.00 78.01  ? 545 LEU A O   1 
ATOM 3461 C CB  . LEU A 1 460 ? 130.984 107.124 121.468 1.00 63.92  ? 545 LEU A CB  1 
ATOM 3462 C CG  . LEU A 1 460 ? 130.595 106.568 120.098 1.00 56.24  ? 545 LEU A CG  1 
ATOM 3463 C CD1 . LEU A 1 460 ? 129.605 107.496 119.435 1.00 57.81  ? 545 LEU A CD1 1 
ATOM 3464 C CD2 . LEU A 1 460 ? 131.823 106.378 119.220 1.00 58.71  ? 545 LEU A CD2 1 
ATOM 3465 N N   . ALA A 1 461 ? 132.426 107.001 124.551 1.00 68.94  ? 546 ALA A N   1 
ATOM 3466 C CA  . ALA A 1 461 ? 133.135 107.663 125.637 1.00 73.61  ? 546 ALA A CA  1 
ATOM 3467 C C   . ALA A 1 461 ? 134.527 107.087 125.850 1.00 74.95  ? 546 ALA A C   1 
ATOM 3468 O O   . ALA A 1 461 ? 135.443 107.823 126.233 1.00 75.70  ? 546 ALA A O   1 
ATOM 3469 C CB  . ALA A 1 461 ? 132.331 107.559 126.935 1.00 78.30  ? 546 ALA A CB  1 
ATOM 3470 N N   . ASN A 1 462 ? 134.705 105.789 125.605 1.00 74.53  ? 547 ASN A N   1 
ATOM 3471 C CA  . ASN A 1 462 ? 136.007 105.144 125.717 1.00 70.23  ? 547 ASN A CA  1 
ATOM 3472 C C   . ASN A 1 462 ? 136.846 105.289 124.455 1.00 74.40  ? 547 ASN A C   1 
ATOM 3473 O O   . ASN A 1 462 ? 137.961 104.759 124.408 1.00 77.09  ? 547 ASN A O   1 
ATOM 3474 C CB  . ASN A 1 462 ? 135.836 103.659 126.052 1.00 68.41  ? 547 ASN A CB  1 
ATOM 3475 C CG  . ASN A 1 462 ? 134.946 103.431 127.259 1.00 80.70  ? 547 ASN A CG  1 
ATOM 3476 O OD1 . ASN A 1 462 ? 134.818 104.298 128.123 1.00 90.03  ? 547 ASN A OD1 1 
ATOM 3477 N ND2 . ASN A 1 462 ? 134.328 102.257 127.325 1.00 82.53  ? 547 ASN A ND2 1 
ATOM 3478 N N   . SER A 1 463 ? 136.337 105.982 123.434 1.00 75.74  ? 548 SER A N   1 
ATOM 3479 C CA  . SER A 1 463 ? 137.068 106.206 122.192 1.00 75.33  ? 548 SER A CA  1 
ATOM 3480 C C   . SER A 1 463 ? 137.275 107.690 121.911 1.00 73.69  ? 548 SER A C   1 
ATOM 3481 O O   . SER A 1 463 ? 137.517 108.071 120.762 1.00 75.47  ? 548 SER A O   1 
ATOM 3482 C CB  . SER A 1 463 ? 136.346 105.540 121.019 1.00 76.83  ? 548 SER A CB  1 
ATOM 3483 O OG  . SER A 1 463 ? 135.023 106.030 120.891 1.00 77.21  ? 548 SER A OG  1 
ATOM 3484 N N   . THR A 1 464 ? 137.174 108.536 122.938 1.00 71.93  ? 549 THR A N   1 
ATOM 3485 C CA  . THR A 1 464 ? 137.347 109.975 122.740 1.00 68.48  ? 549 THR A CA  1 
ATOM 3486 C C   . THR A 1 464 ? 138.724 110.352 122.202 1.00 69.16  ? 549 THR A C   1 
ATOM 3487 O O   . THR A 1 464 ? 138.785 111.149 121.250 1.00 74.71  ? 549 THR A O   1 
ATOM 3488 C CB  . THR A 1 464 ? 137.040 110.714 124.048 1.00 69.12  ? 549 THR A CB  1 
ATOM 3489 O OG1 . THR A 1 464 ? 135.672 110.494 124.413 1.00 73.70  ? 549 THR A OG1 1 
ATOM 3490 C CG2 . THR A 1 464 ? 137.278 112.209 123.886 1.00 63.29  ? 549 THR A CG2 1 
ATOM 3491 N N   . PRO A 1 465 ? 139.848 109.857 122.743 1.00 70.95  ? 550 PRO A N   1 
ATOM 3492 C CA  . PRO A 1 465 ? 141.147 110.258 122.168 1.00 69.76  ? 550 PRO A CA  1 
ATOM 3493 C C   . PRO A 1 465 ? 141.321 109.825 120.724 1.00 73.00  ? 550 PRO A C   1 
ATOM 3494 O O   . PRO A 1 465 ? 141.836 110.588 119.899 1.00 77.93  ? 550 PRO A O   1 
ATOM 3495 C CB  . PRO A 1 465 ? 142.163 109.577 123.094 1.00 69.86  ? 550 PRO A CB  1 
ATOM 3496 C CG  . PRO A 1 465 ? 141.426 108.427 123.679 1.00 73.69  ? 550 PRO A CG  1 
ATOM 3497 C CD  . PRO A 1 465 ? 140.026 108.916 123.865 1.00 73.04  ? 550 PRO A CD  1 
ATOM 3498 N N   . TYR A 1 466 ? 140.892 108.608 120.399 1.00 73.45  ? 551 TYR A N   1 
ATOM 3499 C CA  . TYR A 1 466 ? 140.970 108.107 119.030 1.00 72.01  ? 551 TYR A CA  1 
ATOM 3500 C C   . TYR A 1 466 ? 140.015 108.843 118.100 1.00 72.69  ? 551 TYR A C   1 
ATOM 3501 O O   . TYR A 1 466 ? 140.363 109.126 116.948 1.00 76.53  ? 551 TYR A O   1 
ATOM 3502 C CB  . TYR A 1 466 ? 140.712 106.606 119.056 1.00 75.09  ? 551 TYR A CB  1 
ATOM 3503 C CG  . TYR A 1 466 ? 141.624 105.935 120.052 1.00 80.30  ? 551 TYR A CG  1 
ATOM 3504 C CD1 . TYR A 1 466 ? 142.956 105.708 119.744 1.00 84.77  ? 551 TYR A CD1 1 
ATOM 3505 C CD2 . TYR A 1 466 ? 141.204 105.682 121.350 1.00 80.84  ? 551 TYR A CD2 1 
ATOM 3506 C CE1 . TYR A 1 466 ? 143.813 105.128 120.654 1.00 87.49  ? 551 TYR A CE1 1 
ATOM 3507 C CE2 . TYR A 1 466 ? 142.061 105.115 122.278 1.00 84.26  ? 551 TYR A CE2 1 
ATOM 3508 C CZ  . TYR A 1 466 ? 143.363 104.837 121.921 1.00 89.19  ? 551 TYR A CZ  1 
ATOM 3509 O OH  . TYR A 1 466 ? 144.221 104.273 122.836 1.00 92.01  ? 551 TYR A OH  1 
ATOM 3510 N N   . LEU A 1 467 ? 138.812 109.170 118.582 1.00 73.04  ? 552 LEU A N   1 
ATOM 3511 C CA  . LEU A 1 467 ? 137.905 109.992 117.787 1.00 70.72  ? 552 LEU A CA  1 
ATOM 3512 C C   . LEU A 1 467 ? 138.521 111.354 117.498 1.00 70.99  ? 552 LEU A C   1 
ATOM 3513 O O   . LEU A 1 467 ? 138.445 111.853 116.369 1.00 73.89  ? 552 LEU A O   1 
ATOM 3514 C CB  . LEU A 1 467 ? 136.564 110.147 118.507 1.00 67.41  ? 552 LEU A CB  1 
ATOM 3515 C CG  . LEU A 1 467 ? 135.405 109.275 118.015 1.00 69.93  ? 552 LEU A CG  1 
ATOM 3516 C CD1 . LEU A 1 467 ? 134.143 109.557 118.816 1.00 75.75  ? 552 LEU A CD1 1 
ATOM 3517 C CD2 . LEU A 1 467 ? 135.158 109.494 116.531 1.00 71.08  ? 552 LEU A CD2 1 
ATOM 3518 N N   . GLY A 1 468 ? 139.154 111.962 118.502 1.00 69.90  ? 553 GLY A N   1 
ATOM 3519 C CA  . GLY A 1 468 ? 139.823 113.233 118.279 1.00 65.61  ? 553 GLY A CA  1 
ATOM 3520 C C   . GLY A 1 468 ? 140.985 113.123 117.312 1.00 74.80  ? 553 GLY A C   1 
ATOM 3521 O O   . GLY A 1 468 ? 141.184 113.997 116.468 1.00 80.62  ? 553 GLY A O   1 
ATOM 3522 N N   . MET A 1 469 ? 141.768 112.046 117.420 1.00 75.26  ? 554 MET A N   1 
ATOM 3523 C CA  . MET A 1 469 ? 142.904 111.856 116.522 1.00 71.65  ? 554 MET A CA  1 
ATOM 3524 C C   . MET A 1 469 ? 142.450 111.687 115.077 1.00 74.10  ? 554 MET A C   1 
ATOM 3525 O O   . MET A 1 469 ? 143.024 112.288 114.160 1.00 79.67  ? 554 MET A O   1 
ATOM 3526 C CB  . MET A 1 469 ? 143.724 110.646 116.970 1.00 71.67  ? 554 MET A CB  1 
ATOM 3527 C CG  . MET A 1 469 ? 145.070 110.513 116.278 1.00 80.95  ? 554 MET A CG  1 
ATOM 3528 S SD  . MET A 1 469 ? 145.598 108.796 116.119 1.00 119.55 ? 554 MET A SD  1 
ATOM 3529 C CE  . MET A 1 469 ? 145.119 108.448 114.428 1.00 82.47  ? 554 MET A CE  1 
ATOM 3530 N N   . ILE A 1 470 ? 141.417 110.872 114.850 1.00 71.52  ? 555 ILE A N   1 
ATOM 3531 C CA  . ILE A 1 470 ? 140.950 110.667 113.484 1.00 68.43  ? 555 ILE A CA  1 
ATOM 3532 C C   . ILE A 1 470 ? 140.259 111.917 112.954 1.00 68.52  ? 555 ILE A C   1 
ATOM 3533 O O   . ILE A 1 470 ? 140.331 112.204 111.756 1.00 72.68  ? 555 ILE A O   1 
ATOM 3534 C CB  . ILE A 1 470 ? 140.036 109.435 113.404 1.00 70.16  ? 555 ILE A CB  1 
ATOM 3535 C CG1 . ILE A 1 470 ? 138.843 109.615 114.329 1.00 73.55  ? 555 ILE A CG1 1 
ATOM 3536 C CG2 . ILE A 1 470 ? 140.810 108.172 113.754 1.00 77.66  ? 555 ILE A CG2 1 
ATOM 3537 C CD1 . ILE A 1 470 ? 137.934 108.461 114.355 1.00 75.11  ? 555 ILE A CD1 1 
ATOM 3538 N N   . LEU A 1 471 ? 139.581 112.681 113.817 1.00 68.43  ? 556 LEU A N   1 
ATOM 3539 C CA  . LEU A 1 471 ? 139.032 113.961 113.381 1.00 61.90  ? 556 LEU A CA  1 
ATOM 3540 C C   . LEU A 1 471 ? 140.145 114.928 113.000 1.00 61.78  ? 556 LEU A C   1 
ATOM 3541 O O   . LEU A 1 471 ? 140.018 115.681 112.027 1.00 66.71  ? 556 LEU A O   1 
ATOM 3542 C CB  . LEU A 1 471 ? 138.150 114.555 114.479 1.00 63.95  ? 556 LEU A CB  1 
ATOM 3543 C CG  . LEU A 1 471 ? 136.650 114.272 114.372 1.00 68.23  ? 556 LEU A CG  1 
ATOM 3544 C CD1 . LEU A 1 471 ? 135.884 115.004 115.464 1.00 64.35  ? 556 LEU A CD1 1 
ATOM 3545 C CD2 . LEU A 1 471 ? 136.126 114.651 112.996 1.00 66.21  ? 556 LEU A CD2 1 
ATOM 3546 N N   . LEU A 1 472 ? 141.241 114.919 113.761 1.00 66.74  ? 557 LEU A N   1 
ATOM 3547 C CA  . LEU A 1 472 ? 142.417 115.707 113.410 1.00 70.42  ? 557 LEU A CA  1 
ATOM 3548 C C   . LEU A 1 472 ? 142.942 115.317 112.037 1.00 67.22  ? 557 LEU A C   1 
ATOM 3549 O O   . LEU A 1 472 ? 143.226 116.179 111.200 1.00 68.78  ? 557 LEU A O   1 
ATOM 3550 C CB  . LEU A 1 472 ? 143.500 115.513 114.473 1.00 71.14  ? 557 LEU A CB  1 
ATOM 3551 C CG  . LEU A 1 472 ? 144.807 116.297 114.342 1.00 75.74  ? 557 LEU A CG  1 
ATOM 3552 C CD1 . LEU A 1 472 ? 144.559 117.789 114.424 1.00 76.13  ? 557 LEU A CD1 1 
ATOM 3553 C CD2 . LEU A 1 472 ? 145.804 115.857 115.404 1.00 79.18  ? 557 LEU A CD2 1 
ATOM 3554 N N   . VAL A 1 473 ? 143.066 114.012 111.786 1.00 66.00  ? 558 VAL A N   1 
ATOM 3555 C CA  . VAL A 1 473 ? 143.555 113.544 110.490 1.00 61.66  ? 558 VAL A CA  1 
ATOM 3556 C C   . VAL A 1 473 ? 142.598 113.953 109.375 1.00 62.97  ? 558 VAL A C   1 
ATOM 3557 O O   . VAL A 1 473 ? 143.025 114.367 108.289 1.00 67.00  ? 558 VAL A O   1 
ATOM 3558 C CB  . VAL A 1 473 ? 143.774 112.019 110.520 1.00 59.78  ? 558 VAL A CB  1 
ATOM 3559 C CG1 . VAL A 1 473 ? 144.168 111.509 109.142 1.00 61.51  ? 558 VAL A CG1 1 
ATOM 3560 C CG2 . VAL A 1 473 ? 144.836 111.657 111.545 1.00 62.76  ? 558 VAL A CG2 1 
ATOM 3561 N N   . ILE A 1 474 ? 141.293 113.846 109.625 1.00 63.37  ? 559 ILE A N   1 
ATOM 3562 C CA  . ILE A 1 474 ? 140.300 114.145 108.598 1.00 60.52  ? 559 ILE A CA  1 
ATOM 3563 C C   . ILE A 1 474 ? 140.325 115.627 108.242 1.00 60.76  ? 559 ILE A C   1 
ATOM 3564 O O   . ILE A 1 474 ? 140.340 115.996 107.063 1.00 61.47  ? 559 ILE A O   1 
ATOM 3565 C CB  . ILE A 1 474 ? 138.904 113.691 109.063 1.00 58.91  ? 559 ILE A CB  1 
ATOM 3566 C CG1 . ILE A 1 474 ? 138.728 112.194 108.805 1.00 61.39  ? 559 ILE A CG1 1 
ATOM 3567 C CG2 . ILE A 1 474 ? 137.813 114.485 108.357 1.00 53.87  ? 559 ILE A CG2 1 
ATOM 3568 C CD1 . ILE A 1 474 ? 137.748 111.523 109.736 1.00 66.53  ? 559 ILE A CD1 1 
ATOM 3569 N N   . VAL A 1 475 ? 140.346 116.502 109.251 1.00 60.92  ? 560 VAL A N   1 
ATOM 3570 C CA  . VAL A 1 475 ? 140.402 117.931 108.965 1.00 53.68  ? 560 VAL A CA  1 
ATOM 3571 C C   . VAL A 1 475 ? 141.764 118.347 108.418 1.00 58.17  ? 560 VAL A C   1 
ATOM 3572 O O   . VAL A 1 475 ? 141.852 119.328 107.671 1.00 63.41  ? 560 VAL A O   1 
ATOM 3573 C CB  . VAL A 1 475 ? 140.023 118.755 110.211 1.00 54.73  ? 560 VAL A CB  1 
ATOM 3574 C CG1 . VAL A 1 475 ? 138.665 118.318 110.741 1.00 55.91  ? 560 VAL A CG1 1 
ATOM 3575 C CG2 . VAL A 1 475 ? 141.081 118.615 111.284 1.00 63.40  ? 560 VAL A CG2 1 
ATOM 3576 N N   . THR A 1 476 ? 142.833 117.615 108.743 1.00 57.87  ? 561 THR A N   1 
ATOM 3577 C CA  . THR A 1 476 ? 144.130 117.888 108.132 1.00 55.19  ? 561 THR A CA  1 
ATOM 3578 C C   . THR A 1 476 ? 144.108 117.562 106.644 1.00 59.46  ? 561 THR A C   1 
ATOM 3579 O O   . THR A 1 476 ? 144.606 118.336 105.816 1.00 64.39  ? 561 THR A O   1 
ATOM 3580 C CB  . THR A 1 476 ? 145.219 117.084 108.845 1.00 58.64  ? 561 THR A CB  1 
ATOM 3581 O OG1 . THR A 1 476 ? 145.263 117.457 110.228 1.00 69.06  ? 561 THR A OG1 1 
ATOM 3582 C CG2 . THR A 1 476 ? 146.577 117.343 108.212 1.00 58.41  ? 561 THR A CG2 1 
ATOM 3583 N N   . ALA A 1 477 ? 143.534 116.410 106.287 1.00 57.24  ? 562 ALA A N   1 
ATOM 3584 C CA  . ALA A 1 477 ? 143.341 116.087 104.879 1.00 52.99  ? 562 ALA A CA  1 
ATOM 3585 C C   . ALA A 1 477 ? 142.416 117.091 104.209 1.00 55.85  ? 562 ALA A C   1 
ATOM 3586 O O   . ALA A 1 477 ? 142.594 117.409 103.031 1.00 61.08  ? 562 ALA A O   1 
ATOM 3587 C CB  . ALA A 1 477 ? 142.788 114.670 104.732 1.00 59.54  ? 562 ALA A CB  1 
ATOM 3588 N N   . TRP A 1 478 ? 141.432 117.604 104.949 1.00 58.44  ? 563 TRP A N   1 
ATOM 3589 C CA  . TRP A 1 478 ? 140.550 118.641 104.425 1.00 51.93  ? 563 TRP A CA  1 
ATOM 3590 C C   . TRP A 1 478 ? 141.330 119.908 104.091 1.00 53.53  ? 563 TRP A C   1 
ATOM 3591 O O   . TRP A 1 478 ? 141.139 120.501 103.024 1.00 59.71  ? 563 TRP A O   1 
ATOM 3592 C CB  . TRP A 1 478 ? 139.452 118.924 105.452 1.00 50.13  ? 563 TRP A CB  1 
ATOM 3593 C CG  . TRP A 1 478 ? 138.337 119.817 105.001 1.00 50.35  ? 563 TRP A CG  1 
ATOM 3594 C CD1 . TRP A 1 478 ? 138.168 120.374 103.767 1.00 57.01  ? 563 TRP A CD1 1 
ATOM 3595 C CD2 . TRP A 1 478 ? 137.218 120.237 105.789 1.00 48.53  ? 563 TRP A CD2 1 
ATOM 3596 N NE1 . TRP A 1 478 ? 137.017 121.126 103.743 1.00 59.90  ? 563 TRP A NE1 1 
ATOM 3597 C CE2 . TRP A 1 478 ? 136.415 121.056 104.972 1.00 50.41  ? 563 TRP A CE2 1 
ATOM 3598 C CE3 . TRP A 1 478 ? 136.820 120.003 107.108 1.00 45.81  ? 563 TRP A CE3 1 
ATOM 3599 C CZ2 . TRP A 1 478 ? 135.238 121.642 105.431 1.00 49.73  ? 563 TRP A CZ2 1 
ATOM 3600 C CZ3 . TRP A 1 478 ? 135.653 120.585 107.562 1.00 50.03  ? 563 TRP A CZ3 1 
ATOM 3601 C CH2 . TRP A 1 478 ? 134.876 121.395 106.727 1.00 52.60  ? 563 TRP A CH2 1 
ATOM 3602 N N   . LEU A 1 479 ? 142.223 120.330 104.989 1.00 55.16  ? 564 LEU A N   1 
ATOM 3603 C CA  . LEU A 1 479 ? 143.054 121.504 104.729 1.00 54.33  ? 564 LEU A CA  1 
ATOM 3604 C C   . LEU A 1 479 ? 143.985 121.279 103.543 1.00 56.97  ? 564 LEU A C   1 
ATOM 3605 O O   . LEU A 1 479 ? 144.149 122.165 102.693 1.00 63.17  ? 564 LEU A O   1 
ATOM 3606 C CB  . LEU A 1 479 ? 143.860 121.862 105.976 1.00 55.95  ? 564 LEU A CB  1 
ATOM 3607 C CG  . LEU A 1 479 ? 143.135 122.687 107.036 1.00 55.93  ? 564 LEU A CG  1 
ATOM 3608 C CD1 . LEU A 1 479 ? 143.943 122.746 108.322 1.00 55.45  ? 564 LEU A CD1 1 
ATOM 3609 C CD2 . LEU A 1 479 ? 142.880 124.079 106.498 1.00 56.04  ? 564 LEU A CD2 1 
ATOM 3610 N N   . ALA A 1 480 ? 144.617 120.104 103.477 1.00 52.12  ? 565 ALA A N   1 
ATOM 3611 C CA  . ALA A 1 480 ? 145.514 119.813 102.362 1.00 55.24  ? 565 ALA A CA  1 
ATOM 3612 C C   . ALA A 1 480 ? 144.759 119.793 101.039 1.00 61.48  ? 565 ALA A C   1 
ATOM 3613 O O   . ALA A 1 480 ? 145.244 120.313 100.024 1.00 69.14  ? 565 ALA A O   1 
ATOM 3614 C CB  . ALA A 1 480 ? 146.227 118.481 102.595 1.00 54.86  ? 565 ALA A CB  1 
ATOM 3615 N N   . ALA A 1 481 ? 143.564 119.198 101.034 1.00 57.38  ? 566 ALA A N   1 
ATOM 3616 C CA  . ALA A 1 481 ? 142.741 119.178 99.834  1.00 59.43  ? 566 ALA A CA  1 
ATOM 3617 C C   . ALA A 1 481 ? 142.310 120.583 99.444  1.00 62.06  ? 566 ALA A C   1 
ATOM 3618 O O   . ALA A 1 481 ? 142.271 120.914 98.258  1.00 66.87  ? 566 ALA A O   1 
ATOM 3619 C CB  . ALA A 1 481 ? 141.525 118.280 100.048 1.00 57.06  ? 566 ALA A CB  1 
ATOM 3620 N N   . ALA A 1 482 ? 141.981 121.424 100.428 1.00 59.05  ? 567 ALA A N   1 
ATOM 3621 C CA  . ALA A 1 482 ? 141.621 122.805 100.124 1.00 55.98  ? 567 ALA A CA  1 
ATOM 3622 C C   . ALA A 1 482 ? 142.787 123.549 99.487  1.00 60.80  ? 567 ALA A C   1 
ATOM 3623 O O   . ALA A 1 482 ? 142.602 124.283 98.510  1.00 68.36  ? 567 ALA A O   1 
ATOM 3624 C CB  . ALA A 1 482 ? 141.155 123.519 101.393 1.00 55.95  ? 567 ALA A CB  1 
ATOM 3625 N N   . LYS A 1 483 ? 143.998 123.360 100.016 1.00 60.18  ? 568 LYS A N   1 
ATOM 3626 C CA  . LYS A 1 483 ? 145.170 124.020 99.445  1.00 60.00  ? 568 LYS A CA  1 
ATOM 3627 C C   . LYS A 1 483 ? 145.425 123.557 98.012  1.00 63.89  ? 568 LYS A C   1 
ATOM 3628 O O   . LYS A 1 483 ? 145.603 124.380 97.100  1.00 67.87  ? 568 LYS A O   1 
ATOM 3629 C CB  . LYS A 1 483 ? 146.395 123.756 100.322 1.00 61.79  ? 568 LYS A CB  1 
ATOM 3630 C CG  . LYS A 1 483 ? 147.654 124.471 99.862  1.00 74.85  ? 568 LYS A CG  1 
ATOM 3631 C CD  . LYS A 1 483 ? 148.815 124.207 100.808 1.00 77.41  ? 568 LYS A CD  1 
ATOM 3632 C CE  . LYS A 1 483 ? 150.048 124.996 100.401 1.00 80.50  ? 568 LYS A CE  1 
ATOM 3633 N NZ  . LYS A 1 483 ? 150.606 124.515 99.107  1.00 77.05  ? 568 LYS A NZ  1 
ATOM 3634 N N   . SER A 1 484 ? 145.447 122.238 97.797  1.00 62.60  ? 569 SER A N   1 
ATOM 3635 C CA  . SER A 1 484 ? 145.693 121.712 96.457  1.00 63.61  ? 569 SER A CA  1 
ATOM 3636 C C   . SER A 1 484 ? 144.598 122.140 95.488  1.00 65.50  ? 569 SER A C   1 
ATOM 3637 O O   . SER A 1 484 ? 144.876 122.487 94.332  1.00 70.67  ? 569 SER A O   1 
ATOM 3638 C CB  . SER A 1 484 ? 145.802 120.188 96.503  1.00 67.52  ? 569 SER A CB  1 
ATOM 3639 O OG  . SER A 1 484 ? 146.925 119.779 97.265  1.00 79.46  ? 569 SER A OG  1 
ATOM 3640 N N   . LEU A 1 485 ? 143.345 122.126 95.945  1.00 65.02  ? 570 LEU A N   1 
ATOM 3641 C CA  . LEU A 1 485 ? 142.224 122.515 95.104  1.00 65.04  ? 570 LEU A CA  1 
ATOM 3642 C C   . LEU A 1 485 ? 142.289 123.990 94.745  1.00 65.27  ? 570 LEU A C   1 
ATOM 3643 O O   . LEU A 1 485 ? 141.962 124.368 93.621  1.00 69.43  ? 570 LEU A O   1 
ATOM 3644 C CB  . LEU A 1 485 ? 140.911 122.193 95.815  1.00 55.97  ? 570 LEU A CB  1 
ATOM 3645 C CG  . LEU A 1 485 ? 139.624 122.483 95.048  1.00 53.57  ? 570 LEU A CG  1 
ATOM 3646 C CD1 . LEU A 1 485 ? 139.656 121.806 93.690  1.00 53.08  ? 570 LEU A CD1 1 
ATOM 3647 C CD2 . LEU A 1 485 ? 138.427 122.026 95.855  1.00 57.42  ? 570 LEU A CD2 1 
ATOM 3648 N N   . GLU A 1 486 ? 142.701 124.841 95.687  1.00 63.99  ? 571 GLU A N   1 
ATOM 3649 C CA  . GLU A 1 486 ? 142.845 126.261 95.387  1.00 62.46  ? 571 GLU A CA  1 
ATOM 3650 C C   . GLU A 1 486 ? 143.956 126.494 94.371  1.00 66.93  ? 571 GLU A C   1 
ATOM 3651 O O   . GLU A 1 486 ? 143.806 127.313 93.452  1.00 75.75  ? 571 GLU A O   1 
ATOM 3652 C CB  . GLU A 1 486 ? 143.096 127.030 96.687  1.00 64.32  ? 571 GLU A CB  1 
ATOM 3653 C CG  . GLU A 1 486 ? 143.202 128.545 96.571  1.00 65.59  ? 571 GLU A CG  1 
ATOM 3654 C CD  . GLU A 1 486 ? 144.551 129.035 96.097  1.00 78.72  ? 571 GLU A CD  1 
ATOM 3655 O OE1 . GLU A 1 486 ? 145.552 128.316 96.289  1.00 83.81  ? 571 GLU A OE1 1 
ATOM 3656 O OE2 . GLU A 1 486 ? 144.612 130.158 95.557  1.00 84.75  ? 571 GLU A OE2 1 
ATOM 3657 N N   . GLY A 1 487 ? 145.071 125.774 94.509  1.00 63.46  ? 572 GLY A N   1 
ATOM 3658 C CA  . GLY A 1 487 ? 146.127 125.885 93.512  1.00 66.89  ? 572 GLY A CA  1 
ATOM 3659 C C   . GLY A 1 487 ? 145.660 125.474 92.128  1.00 67.56  ? 572 GLY A C   1 
ATOM 3660 O O   . GLY A 1 487 ? 145.854 126.201 91.146  1.00 72.71  ? 572 GLY A O   1 
ATOM 3661 N N   . GLN A 1 488 ? 145.006 124.311 92.035  1.00 65.68  ? 573 GLN A N   1 
ATOM 3662 C CA  . GLN A 1 488 ? 144.499 123.849 90.745  1.00 63.26  ? 573 GLN A CA  1 
ATOM 3663 C C   . GLN A 1 488 ? 143.412 124.771 90.206  1.00 65.64  ? 573 GLN A C   1 
ATOM 3664 O O   . GLN A 1 488 ? 143.296 124.949 88.989  1.00 73.16  ? 573 GLN A O   1 
ATOM 3665 C CB  . GLN A 1 488 ? 143.967 122.420 90.866  1.00 63.34  ? 573 GLN A CB  1 
ATOM 3666 C CG  . GLN A 1 488 ? 145.000 121.400 91.316  1.00 67.10  ? 573 GLN A CG  1 
ATOM 3667 C CD  . GLN A 1 488 ? 144.367 120.122 91.830  1.00 66.93  ? 573 GLN A CD  1 
ATOM 3668 O OE1 . GLN A 1 488 ? 143.155 119.933 91.728  1.00 68.41  ? 573 GLN A OE1 1 
ATOM 3669 N NE2 . GLN A 1 488 ? 145.186 119.237 92.385  1.00 72.94  ? 573 GLN A NE2 1 
ATOM 3670 N N   . PHE A 1 489 ? 142.616 125.366 91.093  1.00 65.73  ? 574 PHE A N   1 
ATOM 3671 C CA  . PHE A 1 489 ? 141.542 126.262 90.685  1.00 61.85  ? 574 PHE A CA  1 
ATOM 3672 C C   . PHE A 1 489 ? 142.102 127.533 90.062  1.00 63.69  ? 574 PHE A C   1 
ATOM 3673 O O   . PHE A 1 489 ? 141.646 127.969 88.997  1.00 69.01  ? 574 PHE A O   1 
ATOM 3674 C CB  . PHE A 1 489 ? 140.667 126.567 91.904  1.00 57.45  ? 574 PHE A CB  1 
ATOM 3675 C CG  . PHE A 1 489 ? 139.658 127.655 91.691  1.00 56.30  ? 574 PHE A CG  1 
ATOM 3676 C CD1 . PHE A 1 489 ? 138.448 127.384 91.076  1.00 59.39  ? 574 PHE A CD1 1 
ATOM 3677 C CD2 . PHE A 1 489 ? 139.900 128.941 92.147  1.00 59.31  ? 574 PHE A CD2 1 
ATOM 3678 C CE1 . PHE A 1 489 ? 137.511 128.381 90.894  1.00 57.66  ? 574 PHE A CE1 1 
ATOM 3679 C CE2 . PHE A 1 489 ? 138.966 129.941 91.967  1.00 61.09  ? 574 PHE A CE2 1 
ATOM 3680 C CZ  . PHE A 1 489 ? 137.769 129.660 91.341  1.00 57.45  ? 574 PHE A CZ  1 
ATOM 3681 N N   . ASN A 1 490 ? 143.112 128.132 90.702  1.00 65.89  ? 575 ASN A N   1 
ATOM 3682 C CA  . ASN A 1 490 ? 143.771 129.284 90.095  1.00 68.60  ? 575 ASN A CA  1 
ATOM 3683 C C   . ASN A 1 490 ? 144.446 128.906 88.786  1.00 73.75  ? 575 ASN A C   1 
ATOM 3684 O O   . ASN A 1 490 ? 144.419 129.681 87.821  1.00 78.17  ? 575 ASN A O   1 
ATOM 3685 C CB  . ASN A 1 490 ? 144.790 129.898 91.053  1.00 73.32  ? 575 ASN A CB  1 
ATOM 3686 C CG  . ASN A 1 490 ? 144.141 130.609 92.215  1.00 75.30  ? 575 ASN A CG  1 
ATOM 3687 O OD1 . ASN A 1 490 ? 142.986 131.026 92.139  1.00 73.03  ? 575 ASN A OD1 1 
ATOM 3688 N ND2 . ASN A 1 490 ? 144.891 130.779 93.289  1.00 74.34  ? 575 ASN A ND2 1 
ATOM 3689 N N   . SER A 1 491 ? 145.065 127.722 88.731  1.00 72.49  ? 576 SER A N   1 
ATOM 3690 C CA  . SER A 1 491 ? 145.704 127.291 87.492  1.00 74.59  ? 576 SER A CA  1 
ATOM 3691 C C   . SER A 1 491 ? 144.690 127.193 86.359  1.00 79.38  ? 576 SER A C   1 
ATOM 3692 O O   . SER A 1 491 ? 144.928 127.692 85.252  1.00 88.03  ? 576 SER A O   1 
ATOM 3693 C CB  . SER A 1 491 ? 146.412 125.952 87.705  1.00 77.41  ? 576 SER A CB  1 
ATOM 3694 O OG  . SER A 1 491 ? 147.013 125.499 86.505  1.00 84.85  ? 576 SER A OG  1 
ATOM 3695 N N   . LEU A 1 492 ? 143.539 126.566 86.624  1.00 75.75  ? 577 LEU A N   1 
ATOM 3696 C CA  . LEU A 1 492 ? 142.506 126.441 85.600  1.00 73.19  ? 577 LEU A CA  1 
ATOM 3697 C C   . LEU A 1 492 ? 141.978 127.805 85.179  1.00 83.21  ? 577 LEU A C   1 
ATOM 3698 O O   . LEU A 1 492 ? 141.800 128.067 83.984  1.00 92.88  ? 577 LEU A O   1 
ATOM 3699 C CB  . LEU A 1 492 ? 141.356 125.563 86.095  1.00 65.60  ? 577 LEU A CB  1 
ATOM 3700 C CG  . LEU A 1 492 ? 141.608 124.082 86.370  1.00 68.49  ? 577 LEU A CG  1 
ATOM 3701 C CD1 . LEU A 1 492 ? 140.366 123.462 86.979  1.00 67.65  ? 577 LEU A CD1 1 
ATOM 3702 C CD2 . LEU A 1 492 ? 141.998 123.357 85.095  1.00 70.97  ? 577 LEU A CD2 1 
ATOM 3703 N N   . ARG A 1 493 ? 141.708 128.685 86.148  1.00 80.18  ? 578 ARG A N   1 
ATOM 3704 C CA  . ARG A 1 493 ? 141.172 130.000 85.810  1.00 79.21  ? 578 ARG A CA  1 
ATOM 3705 C C   . ARG A 1 493 ? 142.144 130.777 84.933  1.00 90.00  ? 578 ARG A C   1 
ATOM 3706 O O   . ARG A 1 493 ? 141.756 131.330 83.896  1.00 102.41 ? 578 ARG A O   1 
ATOM 3707 C CB  . ARG A 1 493 ? 140.848 130.786 87.080  1.00 73.70  ? 578 ARG A CB  1 
ATOM 3708 C CG  . ARG A 1 493 ? 139.720 130.199 87.905  1.00 68.99  ? 578 ARG A CG  1 
ATOM 3709 C CD  . ARG A 1 493 ? 138.810 131.288 88.441  1.00 71.26  ? 578 ARG A CD  1 
ATOM 3710 N NE  . ARG A 1 493 ? 139.510 132.229 89.305  1.00 71.16  ? 578 ARG A NE  1 
ATOM 3711 C CZ  . ARG A 1 493 ? 139.384 133.547 89.232  1.00 75.56  ? 578 ARG A CZ  1 
ATOM 3712 N NH1 . ARG A 1 493 ? 138.590 134.117 88.341  1.00 71.90  ? 578 ARG A NH1 1 
ATOM 3713 N NH2 . ARG A 1 493 ? 140.071 134.312 90.076  1.00 83.62  ? 578 ARG A NH2 1 
ATOM 3714 N N   . SER A 1 494 ? 143.421 130.813 85.326  1.00 88.55  ? 579 SER A N   1 
ATOM 3715 C CA  . SER A 1 494 ? 144.416 131.537 84.543  1.00 97.91  ? 579 SER A CA  1 
ATOM 3716 C C   . SER A 1 494 ? 144.571 130.933 83.154  1.00 102.89 ? 579 SER A C   1 
ATOM 3717 O O   . SER A 1 494 ? 144.622 131.661 82.152  1.00 108.85 ? 579 SER A O   1 
ATOM 3718 C CB  . SER A 1 494 ? 145.755 131.547 85.279  1.00 96.07  ? 579 SER A CB  1 
ATOM 3719 O OG  . SER A 1 494 ? 146.304 130.243 85.359  1.00 93.41  ? 579 SER A OG  1 
ATOM 3720 N N   . GLU A 1 495 ? 144.626 129.601 83.068  1.00 101.90 ? 580 GLU A N   1 
ATOM 3721 C CA  . GLU A 1 495 ? 144.809 128.954 81.776  1.00 108.44 ? 580 GLU A CA  1 
ATOM 3722 C C   . GLU A 1 495 ? 143.640 129.252 80.846  1.00 110.59 ? 580 GLU A C   1 
ATOM 3723 O O   . GLU A 1 495 ? 143.837 129.594 79.674  1.00 117.17 ? 580 GLU A O   1 
ATOM 3724 C CB  . GLU A 1 495 ? 144.982 127.447 81.966  1.00 105.52 ? 580 GLU A CB  1 
ATOM 3725 C CG  . GLU A 1 495 ? 145.232 126.683 80.677  1.00 117.82 ? 580 GLU A CG  1 
ATOM 3726 C CD  . GLU A 1 495 ? 146.559 127.043 80.035  1.00 124.97 ? 580 GLU A CD  1 
ATOM 3727 O OE1 . GLU A 1 495 ? 147.481 127.466 80.766  1.00 126.19 ? 580 GLU A OE1 1 
ATOM 3728 O OE2 . GLU A 1 495 ? 146.681 126.905 78.800  1.00 126.99 ? 580 GLU A OE2 1 
ATOM 3729 N N   . GLU A 1 496 ? 142.410 129.157 81.358  1.00 105.44 ? 581 GLU A N   1 
ATOM 3730 C CA  . GLU A 1 496 ? 141.255 129.352 80.489  1.00 109.78 ? 581 GLU A CA  1 
ATOM 3731 C C   . GLU A 1 496 ? 141.100 130.817 80.093  1.00 116.38 ? 581 GLU A C   1 
ATOM 3732 O O   . GLU A 1 496 ? 140.730 131.113 78.951  1.00 125.05 ? 581 GLU A O   1 
ATOM 3733 C CB  . GLU A 1 496 ? 139.982 128.816 81.152  1.00 110.92 ? 581 GLU A CB  1 
ATOM 3734 C CG  . GLU A 1 496 ? 139.526 129.537 82.409  1.00 109.67 ? 581 GLU A CG  1 
ATOM 3735 C CD  . GLU A 1 496 ? 138.579 130.682 82.109  1.00 113.22 ? 581 GLU A CD  1 
ATOM 3736 O OE1 . GLU A 1 496 ? 137.990 130.692 81.008  1.00 112.88 ? 581 GLU A OE1 1 
ATOM 3737 O OE2 . GLU A 1 496 ? 138.420 131.568 82.974  1.00 111.24 ? 581 GLU A OE2 1 
ATOM 3738 N N   . GLU A 1 497 ? 141.394 131.754 81.005  1.00 115.64 ? 582 GLU A N   1 
ATOM 3739 C CA  . GLU A 1 497 ? 141.300 133.162 80.631  1.00 118.17 ? 582 GLU A CA  1 
ATOM 3740 C C   . GLU A 1 497 ? 142.342 133.518 79.576  1.00 124.73 ? 582 GLU A C   1 
ATOM 3741 O O   . GLU A 1 497 ? 142.035 134.218 78.601  1.00 129.27 ? 582 GLU A O   1 
ATOM 3742 C CB  . GLU A 1 497 ? 141.419 134.069 81.864  1.00 113.81 ? 582 GLU A CB  1 
ATOM 3743 C CG  . GLU A 1 497 ? 142.718 133.989 82.652  1.00 113.77 ? 582 GLU A CG  1 
ATOM 3744 C CD  . GLU A 1 497 ? 143.813 134.888 82.106  1.00 120.29 ? 582 GLU A CD  1 
ATOM 3745 O OE1 . GLU A 1 497 ? 143.492 135.841 81.367  1.00 123.68 ? 582 GLU A OE1 1 
ATOM 3746 O OE2 . GLU A 1 497 ? 144.997 134.634 82.414  1.00 119.71 ? 582 GLU A OE2 1 
ATOM 3747 N N   . LEU A 1 498 ? 143.576 133.021 79.729  1.00 123.55 ? 583 LEU A N   1 
ATOM 3748 C CA  . LEU A 1 498 ? 144.592 133.334 78.730  1.00 124.19 ? 583 LEU A CA  1 
ATOM 3749 C C   . LEU A 1 498 ? 144.278 132.660 77.400  1.00 129.30 ? 583 LEU A C   1 
ATOM 3750 O O   . LEU A 1 498 ? 144.525 133.238 76.335  1.00 133.10 ? 583 LEU A O   1 
ATOM 3751 C CB  . LEU A 1 498 ? 145.988 132.948 79.234  1.00 119.56 ? 583 LEU A CB  1 
ATOM 3752 C CG  . LEU A 1 498 ? 146.411 131.499 79.494  1.00 118.40 ? 583 LEU A CG  1 
ATOM 3753 C CD1 . LEU A 1 498 ? 146.936 130.828 78.231  1.00 119.30 ? 583 LEU A CD1 1 
ATOM 3754 C CD2 . LEU A 1 498 ? 147.460 131.452 80.595  1.00 114.30 ? 583 LEU A CD2 1 
ATOM 3755 N N   . GLU A 1 499 ? 143.711 131.450 77.436  1.00 129.47 ? 584 GLU A N   1 
ATOM 3756 C CA  . GLU A 1 499 ? 143.343 130.776 76.195  1.00 133.12 ? 584 GLU A CA  1 
ATOM 3757 C C   . GLU A 1 499 ? 142.225 131.522 75.473  1.00 137.29 ? 584 GLU A C   1 
ATOM 3758 O O   . GLU A 1 499 ? 142.270 131.689 74.247  1.00 142.38 ? 584 GLU A O   1 
ATOM 3759 C CB  . GLU A 1 499 ? 142.940 129.329 76.489  1.00 132.48 ? 584 GLU A CB  1 
ATOM 3760 C CG  . GLU A 1 499 ? 142.781 128.439 75.260  1.00 138.80 ? 584 GLU A CG  1 
ATOM 3761 C CD  . GLU A 1 499 ? 141.445 128.610 74.564  1.00 141.28 ? 584 GLU A CD  1 
ATOM 3762 O OE1 . GLU A 1 499 ? 140.488 129.080 75.213  1.00 140.59 ? 584 GLU A OE1 1 
ATOM 3763 O OE2 . GLU A 1 499 ? 141.353 128.276 73.364  1.00 139.98 ? 584 GLU A OE2 1 
ATOM 3764 N N   . LYS A 1 500 ? 141.214 131.981 76.213  1.00 133.82 ? 585 LYS A N   1 
ATOM 3765 C CA  . LYS A 1 500 ? 140.139 132.741 75.582  1.00 135.63 ? 585 LYS A CA  1 
ATOM 3766 C C   . LYS A 1 500 ? 140.657 134.055 75.013  1.00 140.53 ? 585 LYS A C   1 
ATOM 3767 O O   . LYS A 1 500 ? 140.271 134.452 73.905  1.00 145.74 ? 585 LYS A O   1 
ATOM 3768 C CB  . LYS A 1 500 ? 139.003 132.987 76.576  1.00 131.68 ? 585 LYS A CB  1 
ATOM 3769 C CG  . LYS A 1 500 ? 137.917 133.919 76.051  1.00 134.69 ? 585 LYS A CG  1 
ATOM 3770 C CD  . LYS A 1 500 ? 136.918 134.290 77.134  1.00 131.78 ? 585 LYS A CD  1 
ATOM 3771 C CE  . LYS A 1 500 ? 135.890 133.186 77.329  1.00 128.89 ? 585 LYS A CE  1 
ATOM 3772 N NZ  . LYS A 1 500 ? 135.526 132.537 76.037  1.00 130.22 ? 585 LYS A NZ  1 
ATOM 3773 N N   . GLU A 1 501 ? 141.546 134.738 75.741  1.00 138.37 ? 586 GLU A N   1 
ATOM 3774 C CA  . GLU A 1 501 ? 142.062 136.005 75.236  1.00 141.47 ? 586 GLU A CA  1 
ATOM 3775 C C   . GLU A 1 501 ? 142.985 135.801 74.038  1.00 142.78 ? 586 GLU A C   1 
ATOM 3776 O O   . GLU A 1 501 ? 143.052 136.668 73.158  1.00 143.36 ? 586 GLU A O   1 
ATOM 3777 C CB  . GLU A 1 501 ? 142.769 136.773 76.355  1.00 141.77 ? 586 GLU A CB  1 
ATOM 3778 C CG  . GLU A 1 501 ? 143.452 138.055 75.900  1.00 144.79 ? 586 GLU A CG  1 
ATOM 3779 C CD  . GLU A 1 501 ? 143.520 139.106 76.992  1.00 146.16 ? 586 GLU A CD  1 
ATOM 3780 O OE1 . GLU A 1 501 ? 143.574 138.732 78.182  1.00 144.54 ? 586 GLU A OE1 1 
ATOM 3781 O OE2 . GLU A 1 501 ? 143.516 140.310 76.657  1.00 145.39 ? 586 GLU A OE2 1 
ATOM 3782 N N   . MET A 1 502 ? 143.691 134.668 73.970  1.00 142.17 ? 587 MET A N   1 
ATOM 3783 C CA  . MET A 1 502 ? 144.534 134.411 72.805  1.00 144.03 ? 587 MET A CA  1 
ATOM 3784 C C   . MET A 1 502 ? 143.695 134.041 71.586  1.00 146.74 ? 587 MET A C   1 
ATOM 3785 O O   . MET A 1 502 ? 143.984 134.484 70.469  1.00 146.37 ? 587 MET A O   1 
ATOM 3786 C CB  . MET A 1 502 ? 145.579 133.327 73.114  1.00 142.31 ? 587 MET A CB  1 
ATOM 3787 C CG  . MET A 1 502 ? 145.103 131.873 73.053  1.00 143.57 ? 587 MET A CG  1 
ATOM 3788 S SD  . MET A 1 502 ? 145.109 131.115 71.410  1.00 147.89 ? 587 MET A SD  1 
ATOM 3789 C CE  . MET A 1 502 ? 146.848 131.160 70.992  1.00 137.64 ? 587 MET A CE  1 
ATOM 3790 N N   . GLU A 1 503 ? 142.644 133.235 71.775  1.00 147.04 ? 588 GLU A N   1 
ATOM 3791 C CA  . GLU A 1 503 ? 141.834 132.854 70.623  1.00 146.89 ? 588 GLU A CA  1 
ATOM 3792 C C   . GLU A 1 503 ? 140.980 134.019 70.142  1.00 150.08 ? 588 GLU A C   1 
ATOM 3793 O O   . GLU A 1 503 ? 140.645 134.093 68.955  1.00 150.40 ? 588 GLU A O   1 
ATOM 3794 C CB  . GLU A 1 503 ? 140.954 131.644 70.950  1.00 145.42 ? 588 GLU A CB  1 
ATOM 3795 C CG  . GLU A 1 503 ? 139.910 131.869 72.030  1.00 146.69 ? 588 GLU A CG  1 
ATOM 3796 C CD  . GLU A 1 503 ? 138.599 132.393 71.469  1.00 149.62 ? 588 GLU A CD  1 
ATOM 3797 O OE1 . GLU A 1 503 ? 138.367 132.232 70.251  1.00 149.66 ? 588 GLU A OE1 1 
ATOM 3798 O OE2 . GLU A 1 503 ? 137.804 132.967 72.241  1.00 148.53 ? 588 GLU A OE2 1 
ATOM 3799 N N   . ARG A 1 504 ? 140.624 134.937 71.044  1.00 149.33 ? 589 ARG A N   1 
ATOM 3800 C CA  . ARG A 1 504 ? 139.819 136.092 70.672  1.00 147.20 ? 589 ARG A CA  1 
ATOM 3801 C C   . ARG A 1 504 ? 140.653 137.218 70.072  1.00 147.42 ? 589 ARG A C   1 
ATOM 3802 O O   . ARG A 1 504 ? 140.114 138.032 69.313  1.00 146.64 ? 589 ARG A O   1 
ATOM 3803 C CB  . ARG A 1 504 ? 139.042 136.586 71.898  1.00 143.97 ? 589 ARG A CB  1 
ATOM 3804 C CG  . ARG A 1 504 ? 137.939 137.601 71.617  1.00 145.47 ? 589 ARG A CG  1 
ATOM 3805 C CD  . ARG A 1 504 ? 138.425 139.033 71.775  1.00 144.37 ? 589 ARG A CD  1 
ATOM 3806 N NE  . ARG A 1 504 ? 138.923 139.287 73.121  1.00 142.63 ? 589 ARG A NE  1 
ATOM 3807 C CZ  . ARG A 1 504 ? 139.675 140.325 73.460  1.00 138.45 ? 589 ARG A CZ  1 
ATOM 3808 N NH1 . ARG A 1 504 ? 140.036 141.236 72.571  1.00 135.42 ? 589 ARG A NH1 1 
ATOM 3809 N NH2 . ARG A 1 504 ? 140.073 140.454 74.722  1.00 135.03 ? 589 ARG A NH2 1 
ATOM 3810 N N   . ALA A 1 505 ? 141.947 137.274 70.376  1.00 147.75 ? 590 ALA A N   1 
ATOM 3811 C CA  . ALA A 1 505 ? 142.816 138.333 69.867  1.00 147.01 ? 590 ALA A CA  1 
ATOM 3812 C C   . ALA A 1 505 ? 142.912 138.298 68.345  1.00 148.39 ? 590 ALA A C   1 
ATOM 3813 O O   . ALA A 1 505 ? 142.682 139.306 67.676  1.00 145.73 ? 590 ALA A O   1 
ATOM 3814 C CB  . ALA A 1 505 ? 144.202 138.222 70.485  1.00 141.18 ? 590 ALA A CB  1 
ATOM 3815 N N   . GLU B 2 1   ? 98.753  113.164 117.023 1.00 80.84  ? 1   GLU B N   1 
ATOM 3816 C CA  . GLU B 2 1   ? 99.715  113.822 117.898 1.00 78.64  ? 1   GLU B CA  1 
ATOM 3817 C C   . GLU B 2 1   ? 100.785 112.843 118.372 1.00 77.64  ? 1   GLU B C   1 
ATOM 3818 O O   . GLU B 2 1   ? 100.773 111.668 118.006 1.00 78.42  ? 1   GLU B O   1 
ATOM 3819 C CB  . GLU B 2 1   ? 99.007  114.448 119.101 1.00 80.98  ? 1   GLU B CB  1 
ATOM 3820 C CG  . GLU B 2 1   ? 98.373  113.436 120.042 1.00 87.06  ? 1   GLU B CG  1 
ATOM 3821 C CD  . GLU B 2 1   ? 97.637  114.092 121.194 1.00 98.21  ? 1   GLU B CD  1 
ATOM 3822 O OE1 . GLU B 2 1   ? 97.591  115.339 121.240 1.00 101.05 ? 1   GLU B OE1 1 
ATOM 3823 O OE2 . GLU B 2 1   ? 97.104  113.359 122.054 1.00 100.69 ? 1   GLU B OE2 1 
ATOM 3824 N N   . VAL B 2 2   ? 101.708 113.337 119.189 1.00 71.03  ? 2   VAL B N   1 
ATOM 3825 C CA  . VAL B 2 2   ? 102.796 112.527 119.724 1.00 64.45  ? 2   VAL B CA  1 
ATOM 3826 C C   . VAL B 2 2   ? 102.322 111.856 121.005 1.00 70.31  ? 2   VAL B C   1 
ATOM 3827 O O   . VAL B 2 2   ? 101.755 112.512 121.888 1.00 78.03  ? 2   VAL B O   1 
ATOM 3828 C CB  . VAL B 2 2   ? 104.045 113.385 119.980 1.00 54.44  ? 2   VAL B CB  1 
ATOM 3829 C CG1 . VAL B 2 2   ? 105.100 112.580 120.718 1.00 53.93  ? 2   VAL B CG1 1 
ATOM 3830 C CG2 . VAL B 2 2   ? 104.592 113.918 118.671 1.00 49.25  ? 2   VAL B CG2 1 
ATOM 3831 N N   . GLN B 2 3   ? 102.548 110.548 121.109 1.00 65.33  ? 3   GLN B N   1 
ATOM 3832 C CA  . GLN B 2 3   ? 102.126 109.774 122.270 1.00 61.66  ? 3   GLN B CA  1 
ATOM 3833 C C   . GLN B 2 3   ? 103.302 108.958 122.783 1.00 63.74  ? 3   GLN B C   1 
ATOM 3834 O O   . GLN B 2 3   ? 103.922 108.210 122.021 1.00 68.87  ? 3   GLN B O   1 
ATOM 3835 C CB  . GLN B 2 3   ? 100.948 108.860 121.922 1.00 68.38  ? 3   GLN B CB  1 
ATOM 3836 C CG  . GLN B 2 3   ? 100.378 108.108 123.111 1.00 78.87  ? 3   GLN B CG  1 
ATOM 3837 C CD  . GLN B 2 3   ? 99.795  109.037 124.157 1.00 80.75  ? 3   GLN B CD  1 
ATOM 3838 O OE1 . GLN B 2 3   ? 100.389 109.251 125.214 1.00 79.90  ? 3   GLN B OE1 1 
ATOM 3839 N NE2 . GLN B 2 3   ? 98.627  109.598 123.865 1.00 84.70  ? 3   GLN B NE2 1 
ATOM 3840 N N   . LEU B 2 4   ? 103.608 109.104 124.070 1.00 63.91  ? 4   LEU B N   1 
ATOM 3841 C CA  . LEU B 2 4   ? 104.642 108.320 124.735 1.00 61.97  ? 4   LEU B CA  1 
ATOM 3842 C C   . LEU B 2 4   ? 104.026 107.684 125.970 1.00 64.53  ? 4   LEU B C   1 
ATOM 3843 O O   . LEU B 2 4   ? 103.445 108.387 126.803 1.00 69.70  ? 4   LEU B O   1 
ATOM 3844 C CB  . LEU B 2 4   ? 105.840 109.193 125.122 1.00 53.45  ? 4   LEU B CB  1 
ATOM 3845 C CG  . LEU B 2 4   ? 106.650 109.827 123.990 1.00 51.50  ? 4   LEU B CG  1 
ATOM 3846 C CD1 . LEU B 2 4   ? 107.279 111.120 124.460 1.00 50.53  ? 4   LEU B CD1 1 
ATOM 3847 C CD2 . LEU B 2 4   ? 107.719 108.876 123.503 1.00 54.33  ? 4   LEU B CD2 1 
ATOM 3848 N N   . VAL B 2 5   ? 104.139 106.363 126.089 1.00 56.74  ? 5   VAL B N   1 
ATOM 3849 C CA  . VAL B 2 5   ? 103.573 105.637 127.221 1.00 56.82  ? 5   VAL B CA  1 
ATOM 3850 C C   . VAL B 2 5   ? 104.658 104.768 127.840 1.00 65.53  ? 5   VAL B C   1 
ATOM 3851 O O   . VAL B 2 5   ? 105.298 103.974 127.141 1.00 68.15  ? 5   VAL B O   1 
ATOM 3852 C CB  . VAL B 2 5   ? 102.360 104.783 126.805 1.00 55.76  ? 5   VAL B CB  1 
ATOM 3853 C CG1 . VAL B 2 5   ? 101.995 103.803 127.910 1.00 63.41  ? 5   VAL B CG1 1 
ATOM 3854 C CG2 . VAL B 2 5   ? 101.175 105.676 126.470 1.00 62.68  ? 5   VAL B CG2 1 
ATOM 3855 N N   . GLU B 2 6   ? 104.855 104.909 129.148 1.00 65.53  ? 6   GLU B N   1 
ATOM 3856 C CA  . GLU B 2 6   ? 105.855 104.147 129.879 1.00 60.60  ? 6   GLU B CA  1 
ATOM 3857 C C   . GLU B 2 6   ? 105.208 102.951 130.569 1.00 66.63  ? 6   GLU B C   1 
ATOM 3858 O O   . GLU B 2 6   ? 104.030 102.980 130.932 1.00 68.95  ? 6   GLU B O   1 
ATOM 3859 C CB  . GLU B 2 6   ? 106.555 105.014 130.928 1.00 60.08  ? 6   GLU B CB  1 
ATOM 3860 C CG  . GLU B 2 6   ? 107.493 106.071 130.374 1.00 56.31  ? 6   GLU B CG  1 
ATOM 3861 C CD  . GLU B 2 6   ? 106.779 107.375 130.085 1.00 62.15  ? 6   GLU B CD  1 
ATOM 3862 O OE1 . GLU B 2 6   ? 107.450 108.354 129.701 1.00 63.56  ? 6   GLU B OE1 1 
ATOM 3863 O OE2 . GLU B 2 6   ? 105.541 107.417 130.239 1.00 69.82  ? 6   GLU B OE2 1 
ATOM 3864 N N   . SER B 2 7   ? 105.997 101.894 130.744 1.00 64.33  ? 7   SER B N   1 
ATOM 3865 C CA  . SER B 2 7   ? 105.549 100.710 131.462 1.00 65.22  ? 7   SER B CA  1 
ATOM 3866 C C   . SER B 2 7   ? 106.761 100.012 132.061 1.00 61.60  ? 7   SER B C   1 
ATOM 3867 O O   . SER B 2 7   ? 107.906 100.298 131.705 1.00 62.65  ? 7   SER B O   1 
ATOM 3868 C CB  . SER B 2 7   ? 104.766 99.761  130.549 1.00 66.36  ? 7   SER B CB  1 
ATOM 3869 O OG  . SER B 2 7   ? 103.518 100.321 130.179 1.00 75.29  ? 7   SER B OG  1 
ATOM 3870 N N   . GLY B 2 8   ? 106.496 99.088  132.982 1.00 59.98  ? 8   GLY B N   1 
ATOM 3871 C CA  . GLY B 2 8   ? 107.536 98.302  133.611 1.00 62.11  ? 8   GLY B CA  1 
ATOM 3872 C C   . GLY B 2 8   ? 107.958 98.774  134.986 1.00 63.66  ? 8   GLY B C   1 
ATOM 3873 O O   . GLY B 2 8   ? 108.660 98.032  135.686 1.00 62.91  ? 8   GLY B O   1 
ATOM 3874 N N   . GLY B 2 9   ? 107.562 99.976  135.393 1.00 59.01  ? 9   GLY B N   1 
ATOM 3875 C CA  . GLY B 2 9   ? 107.910 100.451 136.720 1.00 55.00  ? 9   GLY B CA  1 
ATOM 3876 C C   . GLY B 2 9   ? 107.101 99.743  137.794 1.00 62.73  ? 9   GLY B C   1 
ATOM 3877 O O   . GLY B 2 9   ? 105.911 99.468  137.628 1.00 69.14  ? 9   GLY B O   1 
ATOM 3878 N N   . GLY B 2 10  ? 107.756 99.453  138.907 1.00 57.81  ? 10  GLY B N   1 
ATOM 3879 C CA  . GLY B 2 10  ? 107.105 98.759  139.993 1.00 52.52  ? 10  GLY B CA  1 
ATOM 3880 C C   . GLY B 2 10  ? 107.945 98.734  141.250 1.00 54.68  ? 10  GLY B C   1 
ATOM 3881 O O   . GLY B 2 10  ? 108.900 99.498  141.398 1.00 61.07  ? 10  GLY B O   1 
ATOM 3882 N N   . LEU B 2 11  ? 107.567 97.840  142.162 1.00 51.92  ? 11  LEU B N   1 
ATOM 3883 C CA  . LEU B 2 11  ? 108.240 97.666  143.445 1.00 49.10  ? 11  LEU B CA  1 
ATOM 3884 C C   . LEU B 2 11  ? 109.232 96.514  143.351 1.00 56.35  ? 11  LEU B C   1 
ATOM 3885 O O   . LEU B 2 11  ? 108.846 95.377  143.055 1.00 60.21  ? 11  LEU B O   1 
ATOM 3886 C CB  . LEU B 2 11  ? 107.224 97.415  144.559 1.00 49.02  ? 11  LEU B CB  1 
ATOM 3887 C CG  . LEU B 2 11  ? 107.688 97.588  146.008 1.00 49.77  ? 11  LEU B CG  1 
ATOM 3888 C CD1 . LEU B 2 11  ? 108.494 98.851  146.181 1.00 51.48  ? 11  LEU B CD1 1 
ATOM 3889 C CD2 . LEU B 2 11  ? 106.486 97.606  146.939 1.00 51.65  ? 11  LEU B CD2 1 
ATOM 3890 N N   . VAL B 2 12  ? 110.505 96.809  143.609 1.00 56.10  ? 12  VAL B N   1 
ATOM 3891 C CA  . VAL B 2 12  ? 111.573 95.821  143.571 1.00 55.52  ? 12  VAL B CA  1 
ATOM 3892 C C   . VAL B 2 12  ? 112.471 96.036  144.782 1.00 53.16  ? 12  VAL B C   1 
ATOM 3893 O O   . VAL B 2 12  ? 112.607 97.154  145.287 1.00 56.90  ? 12  VAL B O   1 
ATOM 3894 C CB  . VAL B 2 12  ? 112.378 95.912  142.251 1.00 55.16  ? 12  VAL B CB  1 
ATOM 3895 C CG1 . VAL B 2 12  ? 112.985 97.297  142.091 1.00 49.11  ? 12  VAL B CG1 1 
ATOM 3896 C CG2 . VAL B 2 12  ? 113.441 94.822  142.166 1.00 60.56  ? 12  VAL B CG2 1 
ATOM 3897 N N   . GLN B 2 13  ? 113.073 94.951  145.261 1.00 54.96  ? 13  GLN B N   1 
ATOM 3898 C CA  . GLN B 2 13  ? 113.996 95.033  146.382 1.00 53.39  ? 13  GLN B CA  1 
ATOM 3899 C C   . GLN B 2 13  ? 115.298 95.709  145.955 1.00 57.90  ? 13  GLN B C   1 
ATOM 3900 O O   . GLN B 2 13  ? 115.641 95.768  144.771 1.00 63.46  ? 13  GLN B O   1 
ATOM 3901 C CB  . GLN B 2 13  ? 114.280 93.635  146.938 1.00 57.15  ? 13  GLN B CB  1 
ATOM 3902 C CG  . GLN B 2 13  ? 114.882 93.618  148.332 1.00 59.82  ? 13  GLN B CG  1 
ATOM 3903 C CD  . GLN B 2 13  ? 113.963 94.228  149.370 1.00 60.90  ? 13  GLN B CD  1 
ATOM 3904 O OE1 . GLN B 2 13  ? 114.407 94.959  150.253 1.00 63.21  ? 13  GLN B OE1 1 
ATOM 3905 N NE2 . GLN B 2 13  ? 112.673 93.927  149.269 1.00 63.77  ? 13  GLN B NE2 1 
ATOM 3906 N N   . ALA B 2 14  ? 116.019 96.238  146.943 1.00 59.19  ? 14  ALA B N   1 
ATOM 3907 C CA  . ALA B 2 14  ? 117.326 96.828  146.682 1.00 60.09  ? 14  ALA B CA  1 
ATOM 3908 C C   . ALA B 2 14  ? 118.272 95.779  146.115 1.00 67.64  ? 14  ALA B C   1 
ATOM 3909 O O   . ALA B 2 14  ? 118.370 94.665  146.638 1.00 71.14  ? 14  ALA B O   1 
ATOM 3910 C CB  . ALA B 2 14  ? 117.901 97.431  147.963 1.00 59.01  ? 14  ALA B CB  1 
ATOM 3911 N N   . GLY B 2 15  ? 118.972 96.138  145.044 1.00 63.70  ? 15  GLY B N   1 
ATOM 3912 C CA  . GLY B 2 15  ? 119.788 95.190  144.317 1.00 62.10  ? 15  GLY B CA  1 
ATOM 3913 C C   . GLY B 2 15  ? 119.056 94.403  143.255 1.00 65.02  ? 15  GLY B C   1 
ATOM 3914 O O   . GLY B 2 15  ? 119.604 93.414  142.754 1.00 71.20  ? 15  GLY B O   1 
ATOM 3915 N N   . GLY B 2 16  ? 117.836 94.806  142.894 1.00 63.09  ? 16  GLY B N   1 
ATOM 3916 C CA  . GLY B 2 16  ? 117.040 94.090  141.924 1.00 60.32  ? 16  GLY B CA  1 
ATOM 3917 C C   . GLY B 2 16  ? 117.126 94.688  140.525 1.00 60.35  ? 16  GLY B C   1 
ATOM 3918 O O   . GLY B 2 16  ? 117.831 95.659  140.263 1.00 62.81  ? 16  GLY B O   1 
ATOM 3919 N N   . SER B 2 17  ? 116.373 94.074  139.616 1.00 58.13  ? 17  SER B N   1 
ATOM 3920 C CA  . SER B 2 17  ? 116.343 94.462  138.214 1.00 57.54  ? 17  SER B CA  1 
ATOM 3921 C C   . SER B 2 17  ? 114.941 94.918  137.831 1.00 59.53  ? 17  SER B C   1 
ATOM 3922 O O   . SER B 2 17  ? 113.946 94.465  138.403 1.00 63.82  ? 17  SER B O   1 
ATOM 3923 C CB  . SER B 2 17  ? 116.778 93.303  137.310 1.00 66.26  ? 17  SER B CB  1 
ATOM 3924 O OG  . SER B 2 17  ? 118.109 92.906  137.592 1.00 75.03  ? 17  SER B OG  1 
ATOM 3925 N N   . LEU B 2 18  ? 114.872 95.822  136.854 1.00 55.83  ? 18  LEU B N   1 
ATOM 3926 C CA  . LEU B 2 18  ? 113.592 96.352  136.397 1.00 50.32  ? 18  LEU B CA  1 
ATOM 3927 C C   . LEU B 2 18  ? 113.774 96.944  135.008 1.00 54.46  ? 18  LEU B C   1 
ATOM 3928 O O   . LEU B 2 18  ? 114.692 97.736  134.789 1.00 60.66  ? 18  LEU B O   1 
ATOM 3929 C CB  . LEU B 2 18  ? 113.061 97.410  137.370 1.00 47.68  ? 18  LEU B CB  1 
ATOM 3930 C CG  . LEU B 2 18  ? 111.550 97.640  137.396 1.00 52.36  ? 18  LEU B CG  1 
ATOM 3931 C CD1 . LEU B 2 18  ? 110.819 96.352  137.735 1.00 57.08  ? 18  LEU B CD1 1 
ATOM 3932 C CD2 . LEU B 2 18  ? 111.201 98.732  138.392 1.00 55.93  ? 18  LEU B CD2 1 
ATOM 3933 N N   . ARG B 2 19  ? 112.907 96.564  134.075 1.00 52.18  ? 19  ARG B N   1 
ATOM 3934 C CA  . ARG B 2 19  ? 113.032 96.981  132.682 1.00 51.90  ? 19  ARG B CA  1 
ATOM 3935 C C   . ARG B 2 19  ? 111.878 97.913  132.332 1.00 54.87  ? 19  ARG B C   1 
ATOM 3936 O O   . ARG B 2 19  ? 110.730 97.472  132.216 1.00 61.24  ? 19  ARG B O   1 
ATOM 3937 C CB  . ARG B 2 19  ? 113.061 95.768  131.755 1.00 57.92  ? 19  ARG B CB  1 
ATOM 3938 C CG  . ARG B 2 19  ? 113.450 96.090  130.321 1.00 56.26  ? 19  ARG B CG  1 
ATOM 3939 C CD  . ARG B 2 19  ? 113.457 94.837  129.460 1.00 60.20  ? 19  ARG B CD  1 
ATOM 3940 N NE  . ARG B 2 19  ? 114.389 94.946  128.343 1.00 68.55  ? 19  ARG B NE  1 
ATOM 3941 C CZ  . ARG B 2 19  ? 114.140 94.514  127.115 1.00 76.10  ? 19  ARG B CZ  1 
ATOM 3942 N NH1 . ARG B 2 19  ? 112.991 93.937  126.805 1.00 73.06  ? 19  ARG B NH1 1 
ATOM 3943 N NH2 . ARG B 2 19  ? 115.068 94.664  126.174 1.00 75.05  ? 19  ARG B NH2 1 
ATOM 3944 N N   . LEU B 2 20  ? 112.185 99.197  132.166 1.00 51.02  ? 20  LEU B N   1 
ATOM 3945 C CA  . LEU B 2 20  ? 111.202 100.152 131.680 1.00 50.90  ? 20  LEU B CA  1 
ATOM 3946 C C   . LEU B 2 20  ? 111.117 100.101 130.162 1.00 52.77  ? 20  LEU B C   1 
ATOM 3947 O O   . LEU B 2 20  ? 112.109 99.868  129.469 1.00 62.59  ? 20  LEU B O   1 
ATOM 3948 C CB  . LEU B 2 20  ? 111.552 101.572 132.123 1.00 48.22  ? 20  LEU B CB  1 
ATOM 3949 C CG  . LEU B 2 20  ? 111.835 101.784 133.607 1.00 44.30  ? 20  LEU B CG  1 
ATOM 3950 C CD1 . LEU B 2 20  ? 112.209 103.229 133.878 1.00 44.02  ? 20  LEU B CD1 1 
ATOM 3951 C CD2 . LEU B 2 20  ? 110.634 101.372 134.440 1.00 49.97  ? 20  LEU B CD2 1 
ATOM 3952 N N   . SER B 2 21  ? 109.913 100.335 129.648 1.00 50.68  ? 21  SER B N   1 
ATOM 3953 C CA  . SER B 2 21  ? 109.661 100.331 128.213 1.00 52.64  ? 21  SER B CA  1 
ATOM 3954 C C   . SER B 2 21  ? 108.816 101.545 127.869 1.00 59.33  ? 21  SER B C   1 
ATOM 3955 O O   . SER B 2 21  ? 107.728 101.722 128.423 1.00 67.73  ? 21  SER B O   1 
ATOM 3956 C CB  . SER B 2 21  ? 108.955 99.044  127.778 1.00 59.75  ? 21  SER B CB  1 
ATOM 3957 O OG  . SER B 2 21  ? 107.646 98.977  128.314 1.00 69.01  ? 21  SER B OG  1 
ATOM 3958 N N   . CYS B 2 22  ? 109.318 102.377 126.963 1.00 55.07  ? 22  CYS B N   1 
ATOM 3959 C CA  . CYS B 2 22  ? 108.597 103.538 126.458 1.00 55.53  ? 22  CYS B CA  1 
ATOM 3960 C C   . CYS B 2 22  ? 108.142 103.228 125.039 1.00 62.23  ? 22  CYS B C   1 
ATOM 3961 O O   . CYS B 2 22  ? 108.969 103.108 124.127 1.00 67.96  ? 22  CYS B O   1 
ATOM 3962 C CB  . CYS B 2 22  ? 109.468 104.791 126.489 1.00 56.48  ? 22  CYS B CB  1 
ATOM 3963 S SG  . CYS B 2 22  ? 108.759 106.188 125.595 1.00 83.89  ? 22  CYS B SG  1 
ATOM 3964 N N   . ALA B 2 23  ? 106.832 103.079 124.866 1.00 62.54  ? 23  ALA B N   1 
ATOM 3965 C CA  . ALA B 2 23  ? 106.228 102.915 123.552 1.00 58.38  ? 23  ALA B CA  1 
ATOM 3966 C C   . ALA B 2 23  ? 105.884 104.293 123.004 1.00 65.33  ? 23  ALA B C   1 
ATOM 3967 O O   . ALA B 2 23  ? 105.207 105.084 123.675 1.00 71.30  ? 23  ALA B O   1 
ATOM 3968 C CB  . ALA B 2 23  ? 104.985 102.030 123.628 1.00 54.84  ? 23  ALA B CB  1 
ATOM 3969 N N   . ALA B 2 24  ? 106.352 104.577 121.794 1.00 64.11  ? 24  ALA B N   1 
ATOM 3970 C CA  . ALA B 2 24  ? 106.213 105.887 121.182 1.00 62.17  ? 24  ALA B CA  1 
ATOM 3971 C C   . ALA B 2 24  ? 105.408 105.791 119.893 1.00 67.69  ? 24  ALA B C   1 
ATOM 3972 O O   . ALA B 2 24  ? 105.433 104.773 119.196 1.00 73.91  ? 24  ALA B O   1 
ATOM 3973 C CB  . ALA B 2 24  ? 107.584 106.499 120.896 1.00 58.72  ? 24  ALA B CB  1 
ATOM 3974 N N   . SER B 2 25  ? 104.689 106.868 119.587 1.00 62.51  ? 25  SER B N   1 
ATOM 3975 C CA  . SER B 2 25  ? 103.845 106.915 118.403 1.00 61.03  ? 25  SER B CA  1 
ATOM 3976 C C   . SER B 2 25  ? 103.690 108.363 117.963 1.00 63.74  ? 25  SER B C   1 
ATOM 3977 O O   . SER B 2 25  ? 103.753 109.285 118.781 1.00 68.87  ? 25  SER B O   1 
ATOM 3978 C CB  . SER B 2 25  ? 102.472 106.287 118.670 1.00 65.04  ? 25  SER B CB  1 
ATOM 3979 O OG  . SER B 2 25  ? 101.512 106.739 117.732 1.00 80.08  ? 25  SER B OG  1 
ATOM 3980 N N   . GLY B 2 26  ? 103.484 108.548 116.662 1.00 57.17  ? 26  GLY B N   1 
ATOM 3981 C CA  . GLY B 2 26  ? 103.267 109.862 116.097 1.00 54.20  ? 26  GLY B CA  1 
ATOM 3982 C C   . GLY B 2 26  ? 104.496 110.551 115.548 1.00 56.26  ? 26  GLY B C   1 
ATOM 3983 O O   . GLY B 2 26  ? 104.413 111.733 115.197 1.00 60.73  ? 26  GLY B O   1 
ATOM 3984 N N   . PHE B 2 27  ? 105.624 109.860 115.462 1.00 55.42  ? 27  PHE B N   1 
ATOM 3985 C CA  . PHE B 2 27  ? 106.864 110.447 114.971 1.00 53.66  ? 27  PHE B CA  1 
ATOM 3986 C C   . PHE B 2 27  ? 107.856 109.321 114.700 1.00 57.92  ? 27  PHE B C   1 
ATOM 3987 O O   . PHE B 2 27  ? 107.700 108.216 115.227 1.00 60.53  ? 27  PHE B O   1 
ATOM 3988 C CB  . PHE B 2 27  ? 107.452 111.440 115.991 1.00 47.14  ? 27  PHE B CB  1 
ATOM 3989 C CG  . PHE B 2 27  ? 107.810 110.823 117.312 1.00 51.46  ? 27  PHE B CG  1 
ATOM 3990 C CD1 . PHE B 2 27  ? 106.832 110.574 118.263 1.00 52.96  ? 27  PHE B CD1 1 
ATOM 3991 C CD2 . PHE B 2 27  ? 109.120 110.487 117.608 1.00 53.18  ? 27  PHE B CD2 1 
ATOM 3992 C CE1 . PHE B 2 27  ? 107.157 110.007 119.479 1.00 48.98  ? 27  PHE B CE1 1 
ATOM 3993 C CE2 . PHE B 2 27  ? 109.451 109.921 118.823 1.00 48.83  ? 27  PHE B CE2 1 
ATOM 3994 C CZ  . PHE B 2 27  ? 108.468 109.681 119.760 1.00 48.51  ? 27  PHE B CZ  1 
ATOM 3995 N N   . PRO B 2 28  ? 108.881 109.579 113.872 1.00 61.99  ? 28  PRO B N   1 
ATOM 3996 C CA  . PRO B 2 28  ? 109.939 108.583 113.696 1.00 61.50  ? 28  PRO B CA  1 
ATOM 3997 C C   . PRO B 2 28  ? 110.771 108.433 114.957 1.00 62.59  ? 28  PRO B C   1 
ATOM 3998 O O   . PRO B 2 28  ? 111.602 109.295 115.273 1.00 65.44  ? 28  PRO B O   1 
ATOM 3999 C CB  . PRO B 2 28  ? 110.763 109.166 112.554 1.00 62.00  ? 28  PRO B CB  1 
ATOM 4000 C CG  . PRO B 2 28  ? 109.810 110.044 111.815 1.00 67.78  ? 28  PRO B CG  1 
ATOM 4001 C CD  . PRO B 2 28  ? 108.923 110.643 112.849 1.00 63.73  ? 28  PRO B CD  1 
ATOM 4002 N N   . VAL B 2 29  ? 110.565 107.332 115.687 1.00 61.02  ? 29  VAL B N   1 
ATOM 4003 C CA  . VAL B 2 29  ? 111.246 107.145 116.961 1.00 61.52  ? 29  VAL B CA  1 
ATOM 4004 C C   . VAL B 2 29  ? 112.696 106.734 116.763 1.00 62.43  ? 29  VAL B C   1 
ATOM 4005 O O   . VAL B 2 29  ? 113.513 106.877 117.681 1.00 68.47  ? 29  VAL B O   1 
ATOM 4006 C CB  . VAL B 2 29  ? 110.473 106.113 117.798 1.00 62.74  ? 29  VAL B CB  1 
ATOM 4007 C CG1 . VAL B 2 29  ? 110.931 106.134 119.253 1.00 60.00  ? 29  VAL B CG1 1 
ATOM 4008 C CG2 . VAL B 2 29  ? 108.982 106.378 117.691 1.00 59.00  ? 29  VAL B CG2 1 
ATOM 4009 N N   . THR B 2 30  ? 113.039 106.238 115.580 1.00 61.96  ? 30  THR B N   1 
ATOM 4010 C CA  . THR B 2 30  ? 114.383 105.775 115.276 1.00 58.20  ? 30  THR B CA  1 
ATOM 4011 C C   . THR B 2 30  ? 115.248 106.870 114.678 1.00 58.40  ? 30  THR B C   1 
ATOM 4012 O O   . THR B 2 30  ? 116.434 106.641 114.421 1.00 62.37  ? 30  THR B O   1 
ATOM 4013 C CB  . THR B 2 30  ? 114.309 104.595 114.313 1.00 65.66  ? 30  THR B CB  1 
ATOM 4014 O OG1 . THR B 2 30  ? 113.690 105.017 113.091 1.00 70.03  ? 30  THR B OG1 1 
ATOM 4015 C CG2 . THR B 2 30  ? 113.436 103.523 114.919 1.00 67.28  ? 30  THR B CG2 1 
ATOM 4016 N N   . GLU B 2 31  ? 114.676 108.044 114.442 1.00 60.34  ? 31  GLU B N   1 
ATOM 4017 C CA  . GLU B 2 31  ? 115.369 109.145 113.795 1.00 57.45  ? 31  GLU B CA  1 
ATOM 4018 C C   . GLU B 2 31  ? 115.628 110.302 114.736 1.00 62.18  ? 31  GLU B C   1 
ATOM 4019 O O   . GLU B 2 31  ? 116.278 111.277 114.335 1.00 62.87  ? 31  GLU B O   1 
ATOM 4020 C CB  . GLU B 2 31  ? 114.564 109.638 112.589 1.00 62.29  ? 31  GLU B CB  1 
ATOM 4021 C CG  . GLU B 2 31  ? 114.137 108.526 111.672 1.00 72.60  ? 31  GLU B CG  1 
ATOM 4022 C CD  . GLU B 2 31  ? 115.319 107.869 111.055 1.00 75.60  ? 31  GLU B CD  1 
ATOM 4023 O OE1 . GLU B 2 31  ? 115.835 106.873 111.613 1.00 73.33  ? 31  GLU B OE1 1 
ATOM 4024 O OE2 . GLU B 2 31  ? 115.806 108.410 110.052 1.00 74.68  ? 31  GLU B OE2 1 
ATOM 4025 N N   . HIS B 2 32  ? 115.156 110.214 115.969 1.00 60.03  ? 32  HIS B N   1 
ATOM 4026 C CA  . HIS B 2 32  ? 115.290 111.267 116.953 1.00 50.87  ? 32  HIS B CA  1 
ATOM 4027 C C   . HIS B 2 32  ? 115.855 110.662 118.225 1.00 49.25  ? 32  HIS B C   1 
ATOM 4028 O O   . HIS B 2 32  ? 115.729 109.459 118.471 1.00 53.78  ? 32  HIS B O   1 
ATOM 4029 C CB  . HIS B 2 32  ? 113.942 111.934 117.229 1.00 56.62  ? 32  HIS B CB  1 
ATOM 4030 C CG  . HIS B 2 32  ? 113.444 112.769 116.091 1.00 54.86  ? 32  HIS B CG  1 
ATOM 4031 N ND1 . HIS B 2 32  ? 112.408 112.370 115.274 1.00 55.47  ? 32  HIS B ND1 1 
ATOM 4032 C CD2 . HIS B 2 32  ? 113.838 113.982 115.634 1.00 57.00  ? 32  HIS B CD2 1 
ATOM 4033 C CE1 . HIS B 2 32  ? 112.188 113.297 114.361 1.00 57.07  ? 32  HIS B CE1 1 
ATOM 4034 N NE2 . HIS B 2 32  ? 113.041 114.287 114.558 1.00 58.74  ? 32  HIS B NE2 1 
ATOM 4035 N N   . GLU B 2 33  ? 116.485 111.505 119.032 1.00 50.82  ? 33  GLU B N   1 
ATOM 4036 C CA  . GLU B 2 33  ? 117.123 111.034 120.249 1.00 50.95  ? 33  GLU B CA  1 
ATOM 4037 C C   . GLU B 2 33  ? 116.086 110.923 121.358 1.00 51.68  ? 33  GLU B C   1 
ATOM 4038 O O   . GLU B 2 33  ? 115.380 111.890 121.660 1.00 56.73  ? 33  GLU B O   1 
ATOM 4039 C CB  . GLU B 2 33  ? 118.251 111.982 120.647 1.00 54.69  ? 33  GLU B CB  1 
ATOM 4040 C CG  . GLU B 2 33  ? 119.044 111.527 121.845 1.00 52.17  ? 33  GLU B CG  1 
ATOM 4041 C CD  . GLU B 2 33  ? 120.302 112.340 122.030 1.00 63.62  ? 33  GLU B CD  1 
ATOM 4042 O OE1 . GLU B 2 33  ? 121.339 111.741 122.380 1.00 73.59  ? 33  GLU B OE1 1 
ATOM 4043 O OE2 . GLU B 2 33  ? 120.257 113.573 121.831 1.00 65.64  ? 33  GLU B OE2 1 
ATOM 4044 N N   . MET B 2 34  ? 115.992 109.741 121.958 1.00 46.12  ? 34  MET B N   1 
ATOM 4045 C CA  . MET B 2 34  ? 114.990 109.450 122.976 1.00 45.94  ? 34  MET B CA  1 
ATOM 4046 C C   . MET B 2 34  ? 115.650 109.511 124.345 1.00 47.03  ? 34  MET B C   1 
ATOM 4047 O O   . MET B 2 34  ? 116.666 108.844 124.577 1.00 47.30  ? 34  MET B O   1 
ATOM 4048 C CB  . MET B 2 34  ? 114.353 108.080 122.740 1.00 46.85  ? 34  MET B CB  1 
ATOM 4049 C CG  . MET B 2 34  ? 113.460 108.024 121.512 1.00 49.02  ? 34  MET B CG  1 
ATOM 4050 S SD  . MET B 2 34  ? 111.880 108.853 121.768 1.00 61.94  ? 34  MET B SD  1 
ATOM 4051 C CE  . MET B 2 34  ? 111.215 107.902 123.130 1.00 54.27  ? 34  MET B CE  1 
ATOM 4052 N N   . TYR B 2 35  ? 115.073 110.303 125.244 1.00 43.08  ? 35  TYR B N   1 
ATOM 4053 C CA  . TYR B 2 35  ? 115.634 110.542 126.563 1.00 39.70  ? 35  TYR B CA  1 
ATOM 4054 C C   . TYR B 2 35  ? 114.823 109.819 127.629 1.00 43.49  ? 35  TYR B C   1 
ATOM 4055 O O   . TYR B 2 35  ? 113.634 109.545 127.459 1.00 47.22  ? 35  TYR B O   1 
ATOM 4056 C CB  . TYR B 2 35  ? 115.672 112.041 126.888 1.00 42.22  ? 35  TYR B CB  1 
ATOM 4057 C CG  . TYR B 2 35  ? 116.500 112.890 125.948 1.00 41.85  ? 35  TYR B CG  1 
ATOM 4058 C CD1 . TYR B 2 35  ? 116.089 113.129 124.643 1.00 43.97  ? 35  TYR B CD1 1 
ATOM 4059 C CD2 . TYR B 2 35  ? 117.688 113.468 126.375 1.00 44.89  ? 35  TYR B CD2 1 
ATOM 4060 C CE1 . TYR B 2 35  ? 116.843 113.909 123.787 1.00 48.84  ? 35  TYR B CE1 1 
ATOM 4061 C CE2 . TYR B 2 35  ? 118.446 114.250 125.528 1.00 47.58  ? 35  TYR B CE2 1 
ATOM 4062 C CZ  . TYR B 2 35  ? 118.020 114.467 124.235 1.00 51.14  ? 35  TYR B CZ  1 
ATOM 4063 O OH  . TYR B 2 35  ? 118.776 115.245 123.389 1.00 60.08  ? 35  TYR B OH  1 
ATOM 4064 N N   . TRP B 2 36  ? 115.485 109.543 128.748 1.00 44.00  ? 36  TRP B N   1 
ATOM 4065 C CA  . TRP B 2 36  ? 114.869 108.973 129.939 1.00 38.74  ? 36  TRP B CA  1 
ATOM 4066 C C   . TRP B 2 36  ? 115.250 109.861 131.111 1.00 43.90  ? 36  TRP B C   1 
ATOM 4067 O O   . TRP B 2 36  ? 116.433 109.938 131.468 1.00 46.48  ? 36  TRP B O   1 
ATOM 4068 C CB  . TRP B 2 36  ? 115.338 107.538 130.180 1.00 35.84  ? 36  TRP B CB  1 
ATOM 4069 C CG  . TRP B 2 36  ? 114.493 106.493 129.536 1.00 42.53  ? 36  TRP B CG  1 
ATOM 4070 C CD1 . TRP B 2 36  ? 114.803 105.748 128.438 1.00 46.75  ? 36  TRP B CD1 1 
ATOM 4071 C CD2 . TRP B 2 36  ? 113.204 106.050 129.972 1.00 42.29  ? 36  TRP B CD2 1 
ATOM 4072 N NE1 . TRP B 2 36  ? 113.779 104.878 128.153 1.00 47.59  ? 36  TRP B NE1 1 
ATOM 4073 C CE2 . TRP B 2 36  ? 112.785 105.043 129.082 1.00 39.43  ? 36  TRP B CE2 1 
ATOM 4074 C CE3 . TRP B 2 36  ? 112.360 106.413 131.026 1.00 46.94  ? 36  TRP B CE3 1 
ATOM 4075 C CZ2 . TRP B 2 36  ? 111.561 104.394 129.212 1.00 42.34  ? 36  TRP B CZ2 1 
ATOM 4076 C CZ3 . TRP B 2 36  ? 111.144 105.768 131.154 1.00 47.25  ? 36  TRP B CZ3 1 
ATOM 4077 C CH2 . TRP B 2 36  ? 110.756 104.771 130.252 1.00 47.51  ? 36  TRP B CH2 1 
ATOM 4078 N N   . TYR B 2 37  ? 114.252 110.530 131.683 1.00 43.51  ? 37  TYR B N   1 
ATOM 4079 C CA  . TYR B 2 37  ? 114.378 111.349 132.877 1.00 38.37  ? 37  TYR B CA  1 
ATOM 4080 C C   . TYR B 2 37  ? 113.699 110.651 134.047 1.00 43.56  ? 37  TYR B C   1 
ATOM 4081 O O   . TYR B 2 37  ? 112.893 109.735 133.867 1.00 51.45  ? 37  TYR B O   1 
ATOM 4082 C CB  . TYR B 2 37  ? 113.736 112.729 132.680 1.00 41.01  ? 37  TYR B CB  1 
ATOM 4083 C CG  . TYR B 2 37  ? 114.420 113.627 131.676 1.00 40.65  ? 37  TYR B CG  1 
ATOM 4084 C CD1 . TYR B 2 37  ? 114.210 113.467 130.313 1.00 39.65  ? 37  TYR B CD1 1 
ATOM 4085 C CD2 . TYR B 2 37  ? 115.255 114.653 132.094 1.00 45.42  ? 37  TYR B CD2 1 
ATOM 4086 C CE1 . TYR B 2 37  ? 114.828 114.295 129.395 1.00 40.96  ? 37  TYR B CE1 1 
ATOM 4087 C CE2 . TYR B 2 37  ? 115.878 115.482 131.185 1.00 48.35  ? 37  TYR B CE2 1 
ATOM 4088 C CZ  . TYR B 2 37  ? 115.660 115.300 129.838 1.00 45.62  ? 37  TYR B CZ  1 
ATOM 4089 O OH  . TYR B 2 37  ? 116.280 116.129 128.933 1.00 51.23  ? 37  TYR B OH  1 
ATOM 4090 N N   . ARG B 2 38  ? 114.012 111.110 135.256 1.00 43.63  ? 38  ARG B N   1 
ATOM 4091 C CA  . ARG B 2 38  ? 113.305 110.659 136.444 1.00 44.64  ? 38  ARG B CA  1 
ATOM 4092 C C   . ARG B 2 38  ? 113.133 111.828 137.401 1.00 53.47  ? 38  ARG B C   1 
ATOM 4093 O O   . ARG B 2 38  ? 113.959 112.744 137.448 1.00 60.40  ? 38  ARG B O   1 
ATOM 4094 C CB  . ARG B 2 38  ? 114.027 109.495 137.139 1.00 46.08  ? 38  ARG B CB  1 
ATOM 4095 C CG  . ARG B 2 38  ? 115.261 109.881 137.932 1.00 49.21  ? 38  ARG B CG  1 
ATOM 4096 C CD  . ARG B 2 38  ? 115.931 108.644 138.506 1.00 50.47  ? 38  ARG B CD  1 
ATOM 4097 N NE  . ARG B 2 38  ? 117.222 108.943 139.113 1.00 56.66  ? 38  ARG B NE  1 
ATOM 4098 C CZ  . ARG B 2 38  ? 118.133 108.029 139.417 1.00 58.27  ? 38  ARG B CZ  1 
ATOM 4099 N NH1 . ARG B 2 38  ? 117.928 106.744 139.179 1.00 54.65  ? 38  ARG B NH1 1 
ATOM 4100 N NH2 . ARG B 2 38  ? 119.278 108.414 139.971 1.00 65.96  ? 38  ARG B NH2 1 
ATOM 4101 N N   . GLN B 2 39  ? 112.038 111.792 138.155 1.00 50.74  ? 39  GLN B N   1 
ATOM 4102 C CA  . GLN B 2 39  ? 111.689 112.850 139.095 1.00 53.74  ? 39  GLN B CA  1 
ATOM 4103 C C   . GLN B 2 39  ? 111.271 112.218 140.412 1.00 59.05  ? 39  GLN B C   1 
ATOM 4104 O O   . GLN B 2 39  ? 110.397 111.346 140.434 1.00 62.54  ? 39  GLN B O   1 
ATOM 4105 C CB  . GLN B 2 39  ? 110.563 113.728 138.541 1.00 54.84  ? 39  GLN B CB  1 
ATOM 4106 C CG  . GLN B 2 39  ? 110.337 115.015 139.315 1.00 58.77  ? 39  GLN B CG  1 
ATOM 4107 C CD  . GLN B 2 39  ? 109.426 115.979 138.583 1.00 62.54  ? 39  GLN B CD  1 
ATOM 4108 O OE1 . GLN B 2 39  ? 108.453 115.571 137.949 1.00 66.31  ? 39  GLN B OE1 1 
ATOM 4109 N NE2 . GLN B 2 39  ? 109.736 117.268 138.668 1.00 67.01  ? 39  GLN B NE2 1 
ATOM 4110 N N   . ALA B 2 40  ? 111.888 112.644 141.487 1.00 58.68  ? 40  ALA B N   1 
ATOM 4111 C CA  . ALA B 2 40  ? 111.440 112.179 142.786 1.00 59.23  ? 40  ALA B CA  1 
ATOM 4112 C C   . ALA B 2 40  ? 110.631 113.266 143.482 1.00 72.31  ? 40  ALA B C   1 
ATOM 4113 O O   . ALA B 2 40  ? 110.864 114.458 143.257 1.00 78.34  ? 40  ALA B O   1 
ATOM 4114 C CB  . ALA B 2 40  ? 112.631 111.785 143.665 1.00 65.00  ? 40  ALA B CB  1 
ATOM 4115 N N   . PRO B 2 41  ? 109.659 112.892 144.314 1.00 76.19  ? 41  PRO B N   1 
ATOM 4116 C CA  . PRO B 2 41  ? 108.883 113.907 145.038 1.00 74.99  ? 41  PRO B CA  1 
ATOM 4117 C C   . PRO B 2 41  ? 109.789 114.775 145.901 1.00 80.46  ? 41  PRO B C   1 
ATOM 4118 O O   . PRO B 2 41  ? 110.603 114.274 146.679 1.00 80.13  ? 41  PRO B O   1 
ATOM 4119 C CB  . PRO B 2 41  ? 107.915 113.074 145.886 1.00 74.81  ? 41  PRO B CB  1 
ATOM 4120 C CG  . PRO B 2 41  ? 107.793 111.780 145.151 1.00 79.79  ? 41  PRO B CG  1 
ATOM 4121 C CD  . PRO B 2 41  ? 109.145 111.531 144.547 1.00 79.91  ? 41  PRO B CD  1 
ATOM 4122 N N   . GLY B 2 42  ? 109.640 116.089 145.753 1.00 81.23  ? 42  GLY B N   1 
ATOM 4123 C CA  . GLY B 2 42  ? 110.488 117.039 146.438 1.00 80.71  ? 42  GLY B CA  1 
ATOM 4124 C C   . GLY B 2 42  ? 111.762 117.405 145.708 1.00 84.09  ? 42  GLY B C   1 
ATOM 4125 O O   . GLY B 2 42  ? 112.499 118.277 146.187 1.00 85.35  ? 42  GLY B O   1 
ATOM 4126 N N   . LYS B 2 43  ? 112.045 116.774 144.572 1.00 83.16  ? 43  LYS B N   1 
ATOM 4127 C CA  . LYS B 2 43  ? 113.234 117.058 143.783 1.00 78.60  ? 43  LYS B CA  1 
ATOM 4128 C C   . LYS B 2 43  ? 112.838 117.405 142.354 1.00 78.11  ? 43  LYS B C   1 
ATOM 4129 O O   . LYS B 2 43  ? 111.723 117.123 141.907 1.00 75.71  ? 43  LYS B O   1 
ATOM 4130 C CB  . LYS B 2 43  ? 114.204 115.868 143.778 1.00 74.84  ? 43  LYS B CB  1 
ATOM 4131 C CG  . LYS B 2 43  ? 114.388 115.197 145.130 1.00 76.14  ? 43  LYS B CG  1 
ATOM 4132 C CD  . LYS B 2 43  ? 115.332 114.006 145.034 1.00 79.88  ? 43  LYS B CD  1 
ATOM 4133 C CE  . LYS B 2 43  ? 116.534 114.313 144.153 1.00 84.34  ? 43  LYS B CE  1 
ATOM 4134 N NZ  . LYS B 2 43  ? 117.523 113.200 144.151 1.00 86.12  ? 43  LYS B NZ  1 
ATOM 4135 N N   . GLU B 2 44  ? 113.771 118.027 141.640 1.00 77.55  ? 44  GLU B N   1 
ATOM 4136 C CA  . GLU B 2 44  ? 113.539 118.398 140.254 1.00 74.55  ? 44  GLU B CA  1 
ATOM 4137 C C   . GLU B 2 44  ? 113.738 117.194 139.337 1.00 72.00  ? 44  GLU B C   1 
ATOM 4138 O O   . GLU B 2 44  ? 114.391 116.208 139.690 1.00 72.80  ? 44  GLU B O   1 
ATOM 4139 C CB  . GLU B 2 44  ? 114.472 119.537 139.839 1.00 75.29  ? 44  GLU B CB  1 
ATOM 4140 C CG  . GLU B 2 44  ? 113.874 120.488 138.814 1.00 80.93  ? 44  GLU B CG  1 
ATOM 4141 C CD  . GLU B 2 44  ? 112.875 121.452 139.425 1.00 89.24  ? 44  GLU B CD  1 
ATOM 4142 O OE1 . GLU B 2 44  ? 112.797 121.524 140.670 1.00 85.47  ? 44  GLU B OE1 1 
ATOM 4143 O OE2 . GLU B 2 44  ? 112.165 122.138 138.660 1.00 92.45  ? 44  GLU B OE2 1 
ATOM 4144 N N   . ARG B 2 45  ? 113.159 117.286 138.143 1.00 70.24  ? 45  ARG B N   1 
ATOM 4145 C CA  . ARG B 2 45  ? 113.285 116.221 137.156 1.00 62.44  ? 45  ARG B CA  1 
ATOM 4146 C C   . ARG B 2 45  ? 114.723 116.156 136.653 1.00 61.59  ? 45  ARG B C   1 
ATOM 4147 O O   . ARG B 2 45  ? 115.270 117.162 136.189 1.00 63.86  ? 45  ARG B O   1 
ATOM 4148 C CB  . ARG B 2 45  ? 112.315 116.458 136.001 1.00 59.99  ? 45  ARG B CB  1 
ATOM 4149 C CG  . ARG B 2 45  ? 112.022 115.226 135.160 1.00 55.21  ? 45  ARG B CG  1 
ATOM 4150 C CD  . ARG B 2 45  ? 110.866 115.478 134.202 1.00 52.97  ? 45  ARG B CD  1 
ATOM 4151 N NE  . ARG B 2 45  ? 109.610 115.708 134.907 1.00 52.60  ? 45  ARG B NE  1 
ATOM 4152 C CZ  . ARG B 2 45  ? 108.477 116.069 134.320 1.00 54.83  ? 45  ARG B CZ  1 
ATOM 4153 N NH1 . ARG B 2 45  ? 108.403 116.250 133.012 1.00 53.18  ? 45  ARG B NH1 1 
ATOM 4154 N NH2 . ARG B 2 45  ? 107.390 116.251 135.065 1.00 58.96  ? 45  ARG B NH2 1 
ATOM 4155 N N   . GLU B 2 46  ? 115.333 114.977 136.745 1.00 58.96  ? 46  GLU B N   1 
ATOM 4156 C CA  . GLU B 2 46  ? 116.724 114.781 136.367 1.00 55.24  ? 46  GLU B CA  1 
ATOM 4157 C C   . GLU B 2 46  ? 116.822 113.760 135.243 1.00 51.71  ? 46  GLU B C   1 
ATOM 4158 O O   . GLU B 2 46  ? 115.982 112.864 135.119 1.00 54.10  ? 46  GLU B O   1 
ATOM 4159 C CB  . GLU B 2 46  ? 117.569 114.320 137.562 1.00 59.38  ? 46  GLU B CB  1 
ATOM 4160 C CG  . GLU B 2 46  ? 117.195 112.947 138.095 1.00 59.34  ? 46  GLU B CG  1 
ATOM 4161 C CD  . GLU B 2 46  ? 118.006 112.553 139.313 1.00 70.73  ? 46  GLU B CD  1 
ATOM 4162 O OE1 . GLU B 2 46  ? 118.846 113.363 139.757 1.00 79.01  ? 46  GLU B OE1 1 
ATOM 4163 O OE2 . GLU B 2 46  ? 117.803 111.432 139.825 1.00 73.80  ? 46  GLU B OE2 1 
ATOM 4164 N N   . TRP B 2 47  ? 117.861 113.904 134.425 1.00 48.00  ? 47  TRP B N   1 
ATOM 4165 C CA  . TRP B 2 47  ? 118.078 113.038 133.275 1.00 41.24  ? 47  TRP B CA  1 
ATOM 4166 C C   . TRP B 2 47  ? 118.765 111.746 133.699 1.00 46.37  ? 47  TRP B C   1 
ATOM 4167 O O   . TRP B 2 47  ? 119.663 111.754 134.546 1.00 55.45  ? 47  TRP B O   1 
ATOM 4168 C CB  . TRP B 2 47  ? 118.914 113.762 132.218 1.00 42.16  ? 47  TRP B CB  1 
ATOM 4169 C CG  . TRP B 2 47  ? 119.340 112.904 131.073 1.00 44.66  ? 47  TRP B CG  1 
ATOM 4170 C CD1 . TRP B 2 47  ? 118.543 112.391 130.093 1.00 45.75  ? 47  TRP B CD1 1 
ATOM 4171 C CD2 . TRP B 2 47  ? 120.672 112.471 130.776 1.00 45.26  ? 47  TRP B CD2 1 
ATOM 4172 N NE1 . TRP B 2 47  ? 119.295 111.657 129.208 1.00 44.68  ? 47  TRP B NE1 1 
ATOM 4173 C CE2 . TRP B 2 47  ? 120.606 111.692 129.605 1.00 45.30  ? 47  TRP B CE2 1 
ATOM 4174 C CE3 . TRP B 2 47  ? 121.914 112.664 131.389 1.00 44.80  ? 47  TRP B CE3 1 
ATOM 4175 C CZ2 . TRP B 2 47  ? 121.733 111.105 129.035 1.00 45.17  ? 47  TRP B CZ2 1 
ATOM 4176 C CZ3 . TRP B 2 47  ? 123.031 112.082 130.822 1.00 44.38  ? 47  TRP B CZ3 1 
ATOM 4177 C CH2 . TRP B 2 47  ? 122.934 111.312 129.656 1.00 44.94  ? 47  TRP B CH2 1 
ATOM 4178 N N   . VAL B 2 48  ? 118.337 110.635 133.101 1.00 42.46  ? 48  VAL B N   1 
ATOM 4179 C CA  . VAL B 2 48  ? 118.871 109.310 133.413 1.00 36.20  ? 48  VAL B CA  1 
ATOM 4180 C C   . VAL B 2 48  ? 119.699 108.760 132.258 1.00 42.25  ? 48  VAL B C   1 
ATOM 4181 O O   . VAL B 2 48  ? 120.890 108.483 132.414 1.00 48.89  ? 48  VAL B O   1 
ATOM 4182 C CB  . VAL B 2 48  ? 117.742 108.331 133.806 1.00 33.84  ? 48  VAL B CB  1 
ATOM 4183 C CG1 . VAL B 2 48  ? 118.282 106.912 133.913 1.00 40.71  ? 48  VAL B CG1 1 
ATOM 4184 C CG2 . VAL B 2 48  ? 117.101 108.761 135.105 1.00 42.98  ? 48  VAL B CG2 1 
ATOM 4185 N N   . ALA B 2 49  ? 119.087 108.591 131.088 1.00 42.58  ? 49  ALA B N   1 
ATOM 4186 C CA  . ALA B 2 49  ? 119.811 107.945 129.997 1.00 37.98  ? 49  ALA B CA  1 
ATOM 4187 C C   . ALA B 2 49  ? 119.143 108.234 128.663 1.00 40.83  ? 49  ALA B C   1 
ATOM 4188 O O   . ALA B 2 49  ? 117.923 108.146 128.545 1.00 50.74  ? 49  ALA B O   1 
ATOM 4189 C CB  . ALA B 2 49  ? 119.898 106.429 130.214 1.00 41.24  ? 49  ALA B CB  1 
ATOM 4190 N N   . ALA B 2 50  ? 119.950 108.542 127.654 1.00 40.21  ? 50  ALA B N   1 
ATOM 4191 C CA  . ALA B 2 50  ? 119.437 108.833 126.326 1.00 38.32  ? 50  ALA B CA  1 
ATOM 4192 C C   . ALA B 2 50  ? 120.033 107.876 125.304 1.00 45.72  ? 50  ALA B C   1 
ATOM 4193 O O   . ALA B 2 50  ? 121.071 107.249 125.533 1.00 50.65  ? 50  ALA B O   1 
ATOM 4194 C CB  . ALA B 2 50  ? 119.733 110.278 125.917 1.00 43.68  ? 50  ALA B CB  1 
ATOM 4195 N N   . ILE B 2 51  ? 119.348 107.763 124.170 1.00 50.21  ? 51  ILE B N   1 
ATOM 4196 C CA  . ILE B 2 51  ? 119.836 106.989 123.034 1.00 42.33  ? 51  ILE B CA  1 
ATOM 4197 C C   . ILE B 2 51  ? 119.601 107.802 121.767 1.00 50.80  ? 51  ILE B C   1 
ATOM 4198 O O   . ILE B 2 51  ? 118.517 108.363 121.571 1.00 60.67  ? 51  ILE B O   1 
ATOM 4199 C CB  . ILE B 2 51  ? 119.172 105.597 122.953 1.00 41.18  ? 51  ILE B CB  1 
ATOM 4200 C CG1 . ILE B 2 51  ? 119.834 104.749 121.867 1.00 44.89  ? 51  ILE B CG1 1 
ATOM 4201 C CG2 . ILE B 2 51  ? 117.663 105.702 122.746 1.00 45.07  ? 51  ILE B CG2 1 
ATOM 4202 C CD1 . ILE B 2 51  ? 119.362 103.315 121.838 1.00 46.71  ? 51  ILE B CD1 1 
ATOM 4203 N N   . ASP B 2 52  ? 120.625 107.890 120.922 1.00 50.62  ? 52  ASP B N   1 
ATOM 4204 C CA  . ASP B 2 52  ? 120.588 108.752 119.752 1.00 49.76  ? 52  ASP B CA  1 
ATOM 4205 C C   . ASP B 2 52  ? 119.911 108.027 118.587 1.00 52.16  ? 52  ASP B C   1 
ATOM 4206 O O   . ASP B 2 52  ? 119.473 106.880 118.702 1.00 57.01  ? 52  ASP B O   1 
ATOM 4207 C CB  . ASP B 2 52  ? 122.005 109.200 119.391 1.00 57.19  ? 52  ASP B CB  1 
ATOM 4208 C CG  . ASP B 2 52  ? 122.027 110.396 118.455 1.00 73.98  ? 52  ASP B CG  1 
ATOM 4209 O OD1 . ASP B 2 52  ? 120.941 110.854 118.042 1.00 73.93  ? 52  ASP B OD1 1 
ATOM 4210 O OD2 . ASP B 2 52  ? 123.133 110.878 118.131 1.00 78.65  ? 52  ASP B OD2 1 
ATOM 4211 N N   . SER B 2 53  ? 119.816 108.714 117.445 1.00 57.05  ? 53  SER B N   1 
ATOM 4212 C CA  . SER B 2 53  ? 119.280 108.091 116.242 1.00 57.69  ? 53  SER B CA  1 
ATOM 4213 C C   . SER B 2 53  ? 120.176 106.972 115.728 1.00 63.21  ? 53  SER B C   1 
ATOM 4214 O O   . SER B 2 53  ? 119.691 106.077 115.029 1.00 65.58  ? 53  SER B O   1 
ATOM 4215 C CB  . SER B 2 53  ? 119.078 109.142 115.149 1.00 59.63  ? 53  SER B CB  1 
ATOM 4216 O OG  . SER B 2 53  ? 120.308 109.744 114.784 1.00 63.32  ? 53  SER B OG  1 
ATOM 4217 N N   . TYR B 2 54  ? 121.411 106.935 116.114 1.00 66.68  ? 54  TYR B N   1 
ATOM 4218 C CA  . TYR B 2 54  ? 122.328 105.957 115.727 1.00 56.51  ? 54  TYR B CA  1 
ATOM 4219 C C   . TYR B 2 54  ? 122.356 104.880 116.743 1.00 58.01  ? 54  TYR B C   1 
ATOM 4220 O O   . TYR B 2 54  ? 122.887 103.869 116.448 1.00 60.22  ? 54  TYR B O   1 
ATOM 4221 C CB  . TYR B 2 54  ? 123.636 106.629 115.768 1.00 56.76  ? 54  TYR B CB  1 
ATOM 4222 C CG  . TYR B 2 54  ? 123.901 107.724 114.845 1.00 67.03  ? 54  TYR B CG  1 
ATOM 4223 C CD1 . TYR B 2 54  ? 124.388 107.475 113.595 1.00 76.57  ? 54  TYR B CD1 1 
ATOM 4224 C CD2 . TYR B 2 54  ? 123.775 109.006 115.248 1.00 73.34  ? 54  TYR B CD2 1 
ATOM 4225 C CE1 . TYR B 2 54  ? 124.683 108.491 112.740 1.00 82.59  ? 54  TYR B CE1 1 
ATOM 4226 C CE2 . TYR B 2 54  ? 124.062 110.033 114.405 1.00 79.12  ? 54  TYR B CE2 1 
ATOM 4227 C CZ  . TYR B 2 54  ? 124.519 109.765 113.153 1.00 88.16  ? 54  TYR B CZ  1 
ATOM 4228 O OH  . TYR B 2 54  ? 124.811 110.799 112.311 1.00 96.76  ? 54  TYR B OH  1 
ATOM 4229 N N   . GLY B 2 55  ? 121.806 105.061 117.955 1.00 57.09  ? 55  GLY B N   1 
ATOM 4230 C CA  . GLY B 2 55  ? 121.814 104.086 119.026 1.00 53.50  ? 55  GLY B CA  1 
ATOM 4231 C C   . GLY B 2 55  ? 123.121 104.086 119.791 1.00 57.00  ? 55  GLY B C   1 
ATOM 4232 O O   . GLY B 2 55  ? 123.776 103.046 119.913 1.00 67.16  ? 55  GLY B O   1 
ATOM 4233 N N   . TYR B 2 56  ? 123.509 105.247 120.321 1.00 51.00  ? 56  TYR B N   1 
ATOM 4234 C CA  . TYR B 2 56  ? 124.841 105.423 120.881 1.00 53.37  ? 56  TYR B CA  1 
ATOM 4235 C C   . TYR B 2 56  ? 124.862 105.397 122.406 1.00 62.93  ? 56  TYR B C   1 
ATOM 4236 O O   . TYR B 2 56  ? 125.943 105.270 122.990 1.00 75.47  ? 56  TYR B O   1 
ATOM 4237 C CB  . TYR B 2 56  ? 125.448 106.729 120.360 1.00 55.41  ? 56  TYR B CB  1 
ATOM 4238 C CG  . TYR B 2 56  ? 126.065 106.550 118.991 1.00 59.97  ? 56  TYR B CG  1 
ATOM 4239 C CD1 . TYR B 2 56  ? 126.223 105.282 118.449 1.00 58.66  ? 56  TYR B CD1 1 
ATOM 4240 C CD2 . TYR B 2 56  ? 126.450 107.641 118.226 1.00 58.99  ? 56  TYR B CD2 1 
ATOM 4241 C CE1 . TYR B 2 56  ? 126.768 105.101 117.196 1.00 55.25  ? 56  TYR B CE1 1 
ATOM 4242 C CE2 . TYR B 2 56  ? 127.005 107.468 116.971 1.00 61.13  ? 56  TYR B CE2 1 
ATOM 4243 C CZ  . TYR B 2 56  ? 127.158 106.194 116.461 1.00 58.92  ? 56  TYR B CZ  1 
ATOM 4244 O OH  . TYR B 2 56  ? 127.699 106.005 115.212 1.00 61.52  ? 56  TYR B OH  1 
ATOM 4245 N N   . THR B 2 57  ? 123.700 105.512 123.054 1.00 52.49  ? 57  THR B N   1 
ATOM 4246 C CA  . THR B 2 57  ? 123.501 105.149 124.460 1.00 46.52  ? 57  THR B CA  1 
ATOM 4247 C C   . THR B 2 57  ? 124.436 105.928 125.393 1.00 50.59  ? 57  THR B C   1 
ATOM 4248 O O   . THR B 2 57  ? 125.363 105.388 125.994 1.00 57.89  ? 57  THR B O   1 
ATOM 4249 C CB  . THR B 2 57  ? 123.664 103.636 124.666 1.00 51.52  ? 57  THR B CB  1 
ATOM 4250 O OG1 . THR B 2 57  ? 124.991 103.232 124.307 1.00 60.93  ? 57  THR B OG1 1 
ATOM 4251 C CG2 . THR B 2 57  ? 122.664 102.875 123.810 1.00 55.71  ? 57  THR B CG2 1 
ATOM 4252 N N   . GLU B 2 58  ? 124.182 107.232 125.473 1.00 49.60  ? 58  GLU B N   1 
ATOM 4253 C CA  . GLU B 2 58  ? 124.785 108.044 126.522 1.00 48.06  ? 58  GLU B CA  1 
ATOM 4254 C C   . GLU B 2 58  ? 123.997 107.890 127.819 1.00 48.30  ? 58  GLU B C   1 
ATOM 4255 O O   . GLU B 2 58  ? 122.763 107.855 127.811 1.00 46.55  ? 58  GLU B O   1 
ATOM 4256 C CB  . GLU B 2 58  ? 124.835 109.515 126.107 1.00 48.75  ? 58  GLU B CB  1 
ATOM 4257 C CG  . GLU B 2 58  ? 125.547 110.418 127.107 1.00 60.71  ? 58  GLU B CG  1 
ATOM 4258 C CD  . GLU B 2 58  ? 127.025 110.102 127.238 1.00 73.48  ? 58  GLU B CD  1 
ATOM 4259 O OE1 . GLU B 2 58  ? 127.619 109.597 126.262 1.00 80.21  ? 58  GLU B OE1 1 
ATOM 4260 O OE2 . GLU B 2 58  ? 127.594 110.356 128.321 1.00 76.29  ? 58  GLU B OE2 1 
ATOM 4261 N N   . TYR B 2 59  ? 124.716 107.796 128.937 1.00 51.44  ? 59  TYR B N   1 
ATOM 4262 C CA  . TYR B 2 59  ? 124.101 107.590 130.241 1.00 46.71  ? 59  TYR B CA  1 
ATOM 4263 C C   . TYR B 2 59  ? 124.531 108.687 131.205 1.00 55.56  ? 59  TYR B C   1 
ATOM 4264 O O   . TYR B 2 59  ? 125.534 109.375 130.994 1.00 63.90  ? 59  TYR B O   1 
ATOM 4265 C CB  . TYR B 2 59  ? 124.470 106.228 130.849 1.00 47.15  ? 59  TYR B CB  1 
ATOM 4266 C CG  . TYR B 2 59  ? 124.178 105.036 129.969 1.00 50.38  ? 59  TYR B CG  1 
ATOM 4267 C CD1 . TYR B 2 59  ? 122.981 104.343 130.081 1.00 45.22  ? 59  TYR B CD1 1 
ATOM 4268 C CD2 . TYR B 2 59  ? 125.115 104.579 129.053 1.00 52.95  ? 59  TYR B CD2 1 
ATOM 4269 C CE1 . TYR B 2 59  ? 122.714 103.248 129.286 1.00 44.39  ? 59  TYR B CE1 1 
ATOM 4270 C CE2 . TYR B 2 59  ? 124.859 103.480 128.257 1.00 53.19  ? 59  TYR B CE2 1 
ATOM 4271 C CZ  . TYR B 2 59  ? 123.657 102.820 128.376 1.00 52.81  ? 59  TYR B CZ  1 
ATOM 4272 O OH  . TYR B 2 59  ? 123.398 101.726 127.583 1.00 61.49  ? 59  TYR B OH  1 
ATOM 4273 N N   . ALA B 2 60  ? 123.752 108.842 132.272 1.00 53.60  ? 60  ALA B N   1 
ATOM 4274 C CA  . ALA B 2 60  ? 124.140 109.705 133.376 1.00 53.15  ? 60  ALA B CA  1 
ATOM 4275 C C   . ALA B 2 60  ? 125.072 108.957 134.321 1.00 63.00  ? 60  ALA B C   1 
ATOM 4276 O O   . ALA B 2 60  ? 124.969 107.740 134.497 1.00 71.64  ? 60  ALA B O   1 
ATOM 4277 C CB  . ALA B 2 60  ? 122.912 110.204 134.137 1.00 46.48  ? 60  ALA B CB  1 
ATOM 4278 N N   . ASP B 2 61  ? 125.993 109.704 134.934 1.00 64.17  ? 61  ASP B N   1 
ATOM 4279 C CA  . ASP B 2 61  ? 126.996 109.095 135.801 1.00 64.67  ? 61  ASP B CA  1 
ATOM 4280 C C   . ASP B 2 61  ? 126.385 108.427 137.027 1.00 65.24  ? 61  ASP B C   1 
ATOM 4281 O O   . ASP B 2 61  ? 127.004 107.521 137.596 1.00 72.03  ? 61  ASP B O   1 
ATOM 4282 C CB  . ASP B 2 61  ? 128.020 110.145 136.235 1.00 70.68  ? 61  ASP B CB  1 
ATOM 4283 C CG  . ASP B 2 61  ? 127.373 111.416 136.752 1.00 81.74  ? 61  ASP B CG  1 
ATOM 4284 O OD1 . ASP B 2 61  ? 126.134 111.435 136.915 1.00 82.04  ? 61  ASP B OD1 1 
ATOM 4285 O OD2 . ASP B 2 61  ? 128.104 112.398 136.995 1.00 86.30  ? 61  ASP B OD2 1 
ATOM 4286 N N   . SER B 2 62  ? 125.190 108.850 137.446 1.00 61.80  ? 62  SER B N   1 
ATOM 4287 C CA  . SER B 2 62  ? 124.557 108.234 138.607 1.00 61.04  ? 62  SER B CA  1 
ATOM 4288 C C   . SER B 2 62  ? 124.130 106.800 138.323 1.00 62.84  ? 62  SER B C   1 
ATOM 4289 O O   . SER B 2 62  ? 124.088 105.974 139.241 1.00 65.42  ? 62  SER B O   1 
ATOM 4290 C CB  . SER B 2 62  ? 123.353 109.065 139.052 1.00 60.65  ? 62  SER B CB  1 
ATOM 4291 O OG  . SER B 2 62  ? 123.754 110.351 139.490 1.00 74.01  ? 62  SER B OG  1 
ATOM 4292 N N   . VAL B 2 63  ? 123.810 106.487 137.068 1.00 62.89  ? 63  VAL B N   1 
ATOM 4293 C CA  . VAL B 2 63  ? 123.334 105.166 136.682 1.00 55.68  ? 63  VAL B CA  1 
ATOM 4294 C C   . VAL B 2 63  ? 124.287 104.452 135.738 1.00 59.42  ? 63  VAL B C   1 
ATOM 4295 O O   . VAL B 2 63  ? 124.002 103.321 135.331 1.00 58.43  ? 63  VAL B O   1 
ATOM 4296 C CB  . VAL B 2 63  ? 121.928 105.243 136.054 1.00 53.01  ? 63  VAL B CB  1 
ATOM 4297 C CG1 . VAL B 2 63  ? 120.994 106.051 136.941 1.00 53.80  ? 63  VAL B CG1 1 
ATOM 4298 C CG2 . VAL B 2 63  ? 122.001 105.843 134.657 1.00 49.65  ? 63  VAL B CG2 1 
ATOM 4299 N N   . LYS B 2 64  ? 125.406 105.074 135.375 1.00 65.99  ? 64  LYS B N   1 
ATOM 4300 C CA  . LYS B 2 64  ? 126.324 104.478 134.413 1.00 60.93  ? 64  LYS B CA  1 
ATOM 4301 C C   . LYS B 2 64  ? 126.920 103.193 134.976 1.00 61.44  ? 64  LYS B C   1 
ATOM 4302 O O   . LYS B 2 64  ? 127.393 103.161 136.117 1.00 63.99  ? 64  LYS B O   1 
ATOM 4303 C CB  . LYS B 2 64  ? 127.426 105.474 134.052 1.00 60.28  ? 64  LYS B CB  1 
ATOM 4304 C CG  . LYS B 2 64  ? 128.271 105.087 132.845 1.00 68.41  ? 64  LYS B CG  1 
ATOM 4305 C CD  . LYS B 2 64  ? 129.542 104.356 133.248 1.00 76.57  ? 64  LYS B CD  1 
ATOM 4306 C CE  . LYS B 2 64  ? 130.403 104.045 132.034 1.00 78.91  ? 64  LYS B CE  1 
ATOM 4307 N NZ  . LYS B 2 64  ? 131.636 103.298 132.404 1.00 84.02  ? 64  LYS B NZ  1 
ATOM 4308 N N   . GLY B 2 65  ? 126.898 102.133 134.169 1.00 61.97  ? 65  GLY B N   1 
ATOM 4309 C CA  . GLY B 2 65  ? 127.357 100.827 134.575 1.00 59.73  ? 65  GLY B CA  1 
ATOM 4310 C C   . GLY B 2 65  ? 126.264 99.910  135.086 1.00 62.52  ? 65  GLY B C   1 
ATOM 4311 O O   . GLY B 2 65  ? 126.463 98.690  135.120 1.00 65.86  ? 65  GLY B O   1 
ATOM 4312 N N   . ARG B 2 66  ? 125.119 100.463 135.477 1.00 61.50  ? 66  ARG B N   1 
ATOM 4313 C CA  . ARG B 2 66  ? 123.986 99.683  135.960 1.00 53.17  ? 66  ARG B CA  1 
ATOM 4314 C C   . ARG B 2 66  ? 122.800 99.697  135.013 1.00 55.51  ? 66  ARG B C   1 
ATOM 4315 O O   . ARG B 2 66  ? 122.145 98.667  134.839 1.00 59.74  ? 66  ARG B O   1 
ATOM 4316 C CB  . ARG B 2 66  ? 123.534 100.196 137.332 1.00 50.20  ? 66  ARG B CB  1 
ATOM 4317 C CG  . ARG B 2 66  ? 124.609 100.162 138.403 1.00 57.53  ? 66  ARG B CG  1 
ATOM 4318 C CD  . ARG B 2 66  ? 124.060 100.655 139.730 1.00 56.10  ? 66  ARG B CD  1 
ATOM 4319 N NE  . ARG B 2 66  ? 123.559 102.021 139.631 1.00 55.39  ? 66  ARG B NE  1 
ATOM 4320 C CZ  . ARG B 2 66  ? 122.329 102.393 139.958 1.00 57.09  ? 66  ARG B CZ  1 
ATOM 4321 N NH1 . ARG B 2 66  ? 121.443 101.524 140.415 1.00 54.72  ? 66  ARG B NH1 1 
ATOM 4322 N NH2 . ARG B 2 66  ? 121.985 103.671 139.836 1.00 58.49  ? 66  ARG B NH2 1 
ATOM 4323 N N   . PHE B 2 67  ? 122.505 100.836 134.395 1.00 53.72  ? 67  PHE B N   1 
ATOM 4324 C CA  . PHE B 2 67  ? 121.379 100.950 133.481 1.00 46.56  ? 67  PHE B CA  1 
ATOM 4325 C C   . PHE B 2 67  ? 121.854 100.788 132.042 1.00 53.35  ? 67  PHE B C   1 
ATOM 4326 O O   . PHE B 2 67  ? 123.015 101.037 131.709 1.00 57.18  ? 67  PHE B O   1 
ATOM 4327 C CB  . PHE B 2 67  ? 120.655 102.293 133.642 1.00 46.53  ? 67  PHE B CB  1 
ATOM 4328 C CG  . PHE B 2 67  ? 119.942 102.464 134.965 1.00 47.49  ? 67  PHE B CG  1 
ATOM 4329 C CD1 . PHE B 2 67  ? 120.117 101.560 136.001 1.00 49.11  ? 67  PHE B CD1 1 
ATOM 4330 C CD2 . PHE B 2 67  ? 119.076 103.528 135.157 1.00 43.87  ? 67  PHE B CD2 1 
ATOM 4331 C CE1 . PHE B 2 67  ? 119.464 101.727 137.208 1.00 46.22  ? 67  PHE B CE1 1 
ATOM 4332 C CE2 . PHE B 2 67  ? 118.416 103.698 136.360 1.00 44.46  ? 67  PHE B CE2 1 
ATOM 4333 C CZ  . PHE B 2 67  ? 118.611 102.797 137.386 1.00 48.66  ? 67  PHE B CZ  1 
ATOM 4334 N N   . THR B 2 68  ? 120.929 100.362 131.187 1.00 55.53  ? 68  THR B N   1 
ATOM 4335 C CA  . THR B 2 68  ? 121.236 100.114 129.781 1.00 52.87  ? 68  THR B CA  1 
ATOM 4336 C C   . THR B 2 68  ? 120.025 100.520 128.952 1.00 49.08  ? 68  THR B C   1 
ATOM 4337 O O   . THR B 2 68  ? 118.971 99.886  129.046 1.00 51.48  ? 68  THR B O   1 
ATOM 4338 C CB  . THR B 2 68  ? 121.594 98.649  129.544 1.00 56.24  ? 68  THR B CB  1 
ATOM 4339 O OG1 . THR B 2 68  ? 122.779 98.320  130.281 1.00 58.81  ? 68  THR B OG1 1 
ATOM 4340 C CG2 . THR B 2 68  ? 121.837 98.392  128.064 1.00 58.11  ? 68  THR B CG2 1 
ATOM 4341 N N   . ILE B 2 69  ? 120.170 101.574 128.162 1.00 48.84  ? 69  ILE B N   1 
ATOM 4342 C CA  . ILE B 2 69  ? 119.110 102.019 127.266 1.00 46.35  ? 69  ILE B CA  1 
ATOM 4343 C C   . ILE B 2 69  ? 119.300 101.336 125.919 1.00 55.02  ? 69  ILE B C   1 
ATOM 4344 O O   . ILE B 2 69  ? 120.425 101.112 125.459 1.00 61.84  ? 69  ILE B O   1 
ATOM 4345 C CB  . ILE B 2 69  ? 119.089 103.558 127.141 1.00 43.55  ? 69  ILE B CB  1 
ATOM 4346 C CG1 . ILE B 2 69  ? 117.826 104.021 126.409 1.00 40.75  ? 69  ILE B CG1 1 
ATOM 4347 C CG2 . ILE B 2 69  ? 120.341 104.070 126.444 1.00 41.86  ? 69  ILE B CG2 1 
ATOM 4348 C CD1 . ILE B 2 69  ? 117.626 105.519 126.427 1.00 43.78  ? 69  ILE B CD1 1 
ATOM 4349 N N   . SER B 2 70  ? 118.185 100.978 125.289 1.00 51.67  ? 70  SER B N   1 
ATOM 4350 C CA  . SER B 2 70  ? 118.232 100.212 124.044 1.00 47.00  ? 70  SER B CA  1 
ATOM 4351 C C   . SER B 2 70  ? 116.937 100.423 123.280 1.00 52.18  ? 70  SER B C   1 
ATOM 4352 O O   . SER B 2 70  ? 115.863 100.087 123.783 1.00 58.37  ? 70  SER B O   1 
ATOM 4353 C CB  . SER B 2 70  ? 118.453 98.726  124.330 1.00 50.47  ? 70  SER B CB  1 
ATOM 4354 O OG  . SER B 2 70  ? 118.117 97.934  123.204 1.00 66.77  ? 70  SER B OG  1 
ATOM 4355 N N   . ARG B 2 71  ? 117.029 100.972 122.076 1.00 54.15  ? 71  ARG B N   1 
ATOM 4356 C CA  . ARG B 2 71  ? 115.857 101.160 121.234 1.00 54.33  ? 71  ARG B CA  1 
ATOM 4357 C C   . ARG B 2 71  ? 115.681 99.943  120.338 1.00 57.60  ? 71  ARG B C   1 
ATOM 4358 O O   . ARG B 2 71  ? 116.624 99.523  119.661 1.00 65.63  ? 71  ARG B O   1 
ATOM 4359 C CB  . ARG B 2 71  ? 115.993 102.424 120.386 1.00 57.20  ? 71  ARG B CB  1 
ATOM 4360 C CG  . ARG B 2 71  ? 114.837 102.654 119.425 1.00 56.92  ? 71  ARG B CG  1 
ATOM 4361 C CD  . ARG B 2 71  ? 115.165 103.757 118.434 1.00 59.09  ? 71  ARG B CD  1 
ATOM 4362 N NE  . ARG B 2 71  ? 116.531 103.637 117.939 1.00 57.58  ? 71  ARG B NE  1 
ATOM 4363 C CZ  . ARG B 2 71  ? 117.470 104.559 118.096 1.00 57.72  ? 71  ARG B CZ  1 
ATOM 4364 N NH1 . ARG B 2 71  ? 117.225 105.692 118.732 1.00 56.94  ? 71  ARG B NH1 1 
ATOM 4365 N NH2 . ARG B 2 71  ? 118.686 104.336 117.606 1.00 54.55  ? 71  ARG B NH2 1 
ATOM 4366 N N   . ASP B 2 72  ? 114.479 99.375  120.341 1.00 59.30  ? 72  ASP B N   1 
ATOM 4367 C CA  . ASP B 2 72  ? 114.125 98.267  119.463 1.00 67.04  ? 72  ASP B CA  1 
ATOM 4368 C C   . ASP B 2 72  ? 113.268 98.858  118.350 1.00 74.25  ? 72  ASP B C   1 
ATOM 4369 O O   . ASP B 2 72  ? 112.140 99.312  118.587 1.00 77.89  ? 72  ASP B O   1 
ATOM 4370 C CB  . ASP B 2 72  ? 113.398 97.161  120.222 1.00 72.29  ? 72  ASP B CB  1 
ATOM 4371 C CG  . ASP B 2 72  ? 113.341 95.859  119.443 1.00 83.86  ? 72  ASP B CG  1 
ATOM 4372 O OD1 . ASP B 2 72  ? 113.497 95.891  118.204 1.00 84.42  ? 72  ASP B OD1 1 
ATOM 4373 O OD2 . ASP B 2 72  ? 113.147 94.799  120.073 1.00 90.40  ? 72  ASP B OD2 1 
ATOM 4374 N N   . ASN B 2 73  ? 113.834 98.871  117.140 1.00 73.77  ? 73  ASN B N   1 
ATOM 4375 C CA  . ASN B 2 73  ? 113.138 99.417  115.984 1.00 72.24  ? 73  ASN B CA  1 
ATOM 4376 C C   . ASN B 2 73  ? 112.057 98.464  115.497 1.00 74.67  ? 73  ASN B C   1 
ATOM 4377 O O   . ASN B 2 73  ? 111.055 98.903  114.922 1.00 75.46  ? 73  ASN B O   1 
ATOM 4378 C CB  . ASN B 2 73  ? 114.135 99.695  114.859 1.00 71.12  ? 73  ASN B CB  1 
ATOM 4379 C CG  . ASN B 2 73  ? 115.188 100.712 115.253 1.00 69.97  ? 73  ASN B CG  1 
ATOM 4380 O OD1 . ASN B 2 73  ? 115.091 101.347 116.302 1.00 68.71  ? 73  ASN B OD1 1 
ATOM 4381 N ND2 . ASN B 2 73  ? 116.193 100.883 114.403 1.00 71.04  ? 73  ASN B ND2 1 
ATOM 4382 N N   . SER B 2 74  ? 112.252 97.160  115.708 1.00 74.57  ? 74  SER B N   1 
ATOM 4383 C CA  . SER B 2 74  ? 111.253 96.179  115.303 1.00 75.99  ? 74  SER B CA  1 
ATOM 4384 C C   . SER B 2 74  ? 109.944 96.381  116.054 1.00 79.40  ? 74  SER B C   1 
ATOM 4385 O O   . SER B 2 74  ? 108.862 96.320  115.459 1.00 84.08  ? 74  SER B O   1 
ATOM 4386 C CB  . SER B 2 74  ? 111.792 94.766  115.531 1.00 77.54  ? 74  SER B CB  1 
ATOM 4387 O OG  . SER B 2 74  ? 111.975 94.510  116.913 1.00 83.29  ? 74  SER B OG  1 
ATOM 4388 N N   . LYS B 2 75  ? 110.021 96.627  117.360 1.00 80.20  ? 75  LYS B N   1 
ATOM 4389 C CA  . LYS B 2 75  ? 108.842 96.886  118.174 1.00 74.35  ? 75  LYS B CA  1 
ATOM 4390 C C   . LYS B 2 75  ? 108.611 98.369  118.427 1.00 71.56  ? 75  LYS B C   1 
ATOM 4391 O O   . LYS B 2 75  ? 107.634 98.721  119.096 1.00 79.42  ? 75  LYS B O   1 
ATOM 4392 C CB  . LYS B 2 75  ? 108.942 96.138  119.506 1.00 79.90  ? 75  LYS B CB  1 
ATOM 4393 C CG  . LYS B 2 75  ? 109.347 94.683  119.353 1.00 87.71  ? 75  LYS B CG  1 
ATOM 4394 C CD  . LYS B 2 75  ? 109.093 93.899  120.627 1.00 97.16  ? 75  LYS B CD  1 
ATOM 4395 C CE  . LYS B 2 75  ? 108.780 92.444  120.317 1.00 99.33  ? 75  LYS B CE  1 
ATOM 4396 N NZ  . LYS B 2 75  ? 110.003 91.596  120.347 1.00 94.89  ? 75  LYS B NZ  1 
ATOM 4397 N N   . ASN B 2 76  ? 109.487 99.237  117.916 1.00 70.49  ? 76  ASN B N   1 
ATOM 4398 C CA  . ASN B 2 76  ? 109.278 100.683 117.906 1.00 70.40  ? 76  ASN B CA  1 
ATOM 4399 C C   . ASN B 2 76  ? 109.290 101.260 119.327 1.00 65.99  ? 76  ASN B C   1 
ATOM 4400 O O   . ASN B 2 76  ? 108.628 102.257 119.618 1.00 63.89  ? 76  ASN B O   1 
ATOM 4401 C CB  . ASN B 2 76  ? 107.971 101.022 117.163 1.00 74.45  ? 76  ASN B CB  1 
ATOM 4402 C CG  . ASN B 2 76  ? 107.646 102.506 117.149 1.00 77.14  ? 76  ASN B CG  1 
ATOM 4403 O OD1 . ASN B 2 76  ? 108.542 103.349 117.139 1.00 73.35  ? 76  ASN B OD1 1 
ATOM 4404 N ND2 . ASN B 2 76  ? 106.359 102.830 117.153 1.00 81.42  ? 76  ASN B ND2 1 
ATOM 4405 N N   . THR B 2 77  ? 110.038 100.648 120.243 1.00 66.22  ? 77  THR B N   1 
ATOM 4406 C CA  . THR B 2 77  ? 110.002 101.085 121.636 1.00 59.80  ? 77  THR B CA  1 
ATOM 4407 C C   . THR B 2 77  ? 111.405 101.226 122.204 1.00 60.76  ? 77  THR B C   1 
ATOM 4408 O O   . THR B 2 77  ? 112.315 100.469 121.863 1.00 66.76  ? 77  THR B O   1 
ATOM 4409 C CB  . THR B 2 77  ? 109.200 100.121 122.532 1.00 63.23  ? 77  THR B CB  1 
ATOM 4410 O OG1 . THR B 2 77  ? 109.883 98.865  122.626 1.00 69.33  ? 77  THR B OG1 1 
ATOM 4411 C CG2 . THR B 2 77  ? 107.789 99.908  122.001 1.00 67.95  ? 77  THR B CG2 1 
ATOM 4412 N N   . VAL B 2 78  ? 111.562 102.191 123.097 1.00 54.85  ? 78  VAL B N   1 
ATOM 4413 C CA  . VAL B 2 78  ? 112.816 102.371 123.818 1.00 51.60  ? 78  VAL B CA  1 
ATOM 4414 C C   . VAL B 2 78  ? 112.744 101.566 125.108 1.00 54.20  ? 78  VAL B C   1 
ATOM 4415 O O   . VAL B 2 78  ? 111.668 101.366 125.676 1.00 61.58  ? 78  VAL B O   1 
ATOM 4416 C CB  . VAL B 2 78  ? 113.090 103.866 124.084 1.00 50.91  ? 78  VAL B CB  1 
ATOM 4417 C CG1 . VAL B 2 78  ? 114.523 104.079 124.551 1.00 53.67  ? 78  VAL B CG1 1 
ATOM 4418 C CG2 . VAL B 2 78  ? 112.815 104.676 122.831 1.00 52.51  ? 78  VAL B CG2 1 
ATOM 4419 N N   . TYR B 2 79  ? 113.893 101.087 125.575 1.00 49.17  ? 79  TYR B N   1 
ATOM 4420 C CA  . TYR B 2 79  ? 113.970 100.264 126.768 1.00 48.76  ? 79  TYR B CA  1 
ATOM 4421 C C   . TYR B 2 79  ? 115.056 100.801 127.684 1.00 49.13  ? 79  TYR B C   1 
ATOM 4422 O O   . TYR B 2 79  ? 116.061 101.354 127.231 1.00 55.75  ? 79  TYR B O   1 
ATOM 4423 C CB  . TYR B 2 79  ? 114.281 98.800  126.428 1.00 53.11  ? 79  TYR B CB  1 
ATOM 4424 C CG  . TYR B 2 79  ? 113.193 98.081  125.669 1.00 54.65  ? 79  TYR B CG  1 
ATOM 4425 C CD1 . TYR B 2 79  ? 111.958 97.835  126.251 1.00 57.63  ? 79  TYR B CD1 1 
ATOM 4426 C CD2 . TYR B 2 79  ? 113.406 97.638  124.371 1.00 54.56  ? 79  TYR B CD2 1 
ATOM 4427 C CE1 . TYR B 2 79  ? 110.963 97.173  125.559 1.00 60.68  ? 79  TYR B CE1 1 
ATOM 4428 C CE2 . TYR B 2 79  ? 112.418 96.976  123.671 1.00 61.70  ? 79  TYR B CE2 1 
ATOM 4429 C CZ  . TYR B 2 79  ? 111.199 96.745  124.271 1.00 67.38  ? 79  TYR B CZ  1 
ATOM 4430 O OH  . TYR B 2 79  ? 110.211 96.087  123.576 1.00 78.58  ? 79  TYR B OH  1 
ATOM 4431 N N   . LEU B 2 80  ? 114.850 100.601 128.982 1.00 46.69  ? 80  LEU B N   1 
ATOM 4432 C CA  . LEU B 2 80  ? 115.820 100.978 130.008 1.00 46.22  ? 80  LEU B CA  1 
ATOM 4433 C C   . LEU B 2 80  ? 115.894 99.824  131.002 1.00 49.97  ? 80  LEU B C   1 
ATOM 4434 O O   . LEU B 2 80  ? 115.026 99.688  131.869 1.00 54.93  ? 80  LEU B O   1 
ATOM 4435 C CB  . LEU B 2 80  ? 115.427 102.282 130.693 1.00 43.95  ? 80  LEU B CB  1 
ATOM 4436 C CG  . LEU B 2 80  ? 116.438 102.863 131.682 1.00 40.37  ? 80  LEU B CG  1 
ATOM 4437 C CD1 . LEU B 2 80  ? 117.468 103.714 130.957 1.00 43.82  ? 80  LEU B CD1 1 
ATOM 4438 C CD2 . LEU B 2 80  ? 115.730 103.674 132.755 1.00 43.20  ? 80  LEU B CD2 1 
ATOM 4439 N N   . GLN B 2 81  ? 116.906 98.977  130.846 1.00 51.26  ? 81  GLN B N   1 
ATOM 4440 C CA  . GLN B 2 81  ? 117.171 97.913  131.803 1.00 49.76  ? 81  GLN B CA  1 
ATOM 4441 C C   . GLN B 2 81  ? 117.895 98.495  133.009 1.00 53.62  ? 81  GLN B C   1 
ATOM 4442 O O   . GLN B 2 81  ? 118.829 99.286  132.854 1.00 57.22  ? 81  GLN B O   1 
ATOM 4443 C CB  . GLN B 2 81  ? 118.009 96.814  131.148 1.00 45.14  ? 81  GLN B CB  1 
ATOM 4444 C CG  . GLN B 2 81  ? 118.465 95.724  132.094 1.00 50.04  ? 81  GLN B CG  1 
ATOM 4445 C CD  . GLN B 2 81  ? 117.314 94.907  132.642 1.00 56.53  ? 81  GLN B CD  1 
ATOM 4446 O OE1 . GLN B 2 81  ? 116.501 94.373  131.888 1.00 62.42  ? 81  GLN B OE1 1 
ATOM 4447 N NE2 . GLN B 2 81  ? 117.237 94.806  133.964 1.00 56.52  ? 81  GLN B NE2 1 
ATOM 4448 N N   . MET B 2 82  ? 117.468 98.106  134.210 1.00 53.16  ? 82  MET B N   1 
ATOM 4449 C CA  . MET B 2 82  ? 118.007 98.649  135.454 1.00 50.90  ? 82  MET B CA  1 
ATOM 4450 C C   . MET B 2 82  ? 118.446 97.474  136.320 1.00 57.69  ? 82  MET B C   1 
ATOM 4451 O O   . MET B 2 82  ? 117.614 96.824  136.960 1.00 61.97  ? 82  MET B O   1 
ATOM 4452 C CB  . MET B 2 82  ? 116.969 99.500  136.178 1.00 53.70  ? 82  MET B CB  1 
ATOM 4453 C CG  . MET B 2 82  ? 116.573 100.777 135.460 1.00 53.37  ? 82  MET B CG  1 
ATOM 4454 S SD  . MET B 2 82  ? 115.395 101.724 136.441 1.00 55.45  ? 82  MET B SD  1 
ATOM 4455 C CE  . MET B 2 82  ? 113.914 100.746 136.223 1.00 50.87  ? 82  MET B CE  1 
ATOM 4456 N N   . ASN B 2 83  ? 119.745 97.205  136.338 1.00 57.12  ? 83  ASN B N   1 
ATOM 4457 C CA  . ASN B 2 83  ? 120.318 96.156  137.166 1.00 58.88  ? 83  ASN B CA  1 
ATOM 4458 C C   . ASN B 2 83  ? 120.969 96.758  138.403 1.00 59.01  ? 83  ASN B C   1 
ATOM 4459 O O   . ASN B 2 83  ? 121.409 97.911  138.394 1.00 62.55  ? 83  ASN B O   1 
ATOM 4460 C CB  . ASN B 2 83  ? 121.346 95.340  136.378 1.00 60.32  ? 83  ASN B CB  1 
ATOM 4461 C CG  . ASN B 2 83  ? 120.804 94.848  135.054 1.00 64.35  ? 83  ASN B CG  1 
ATOM 4462 O OD1 . ASN B 2 83  ? 119.594 94.844  134.835 1.00 65.46  ? 83  ASN B OD1 1 
ATOM 4463 N ND2 . ASN B 2 83  ? 121.697 94.433  134.162 1.00 67.97  ? 83  ASN B ND2 1 
ATOM 4464 N N   . SER B 2 84  ? 121.031 95.957  139.465 1.00 61.23  ? 84  SER B N   1 
ATOM 4465 C CA  . SER B 2 84  ? 121.627 96.353  140.739 1.00 64.01  ? 84  SER B CA  1 
ATOM 4466 C C   . SER B 2 84  ? 121.005 97.662  141.230 1.00 63.28  ? 84  SER B C   1 
ATOM 4467 O O   . SER B 2 84  ? 121.684 98.633  141.569 1.00 64.14  ? 84  SER B O   1 
ATOM 4468 C CB  . SER B 2 84  ? 123.149 96.474  140.633 1.00 69.16  ? 84  SER B CB  1 
ATOM 4469 O OG  . SER B 2 84  ? 123.744 95.191  140.602 1.00 85.86  ? 84  SER B OG  1 
ATOM 4470 N N   . LEU B 2 85  ? 119.675 97.671  141.255 1.00 60.13  ? 85  LEU B N   1 
ATOM 4471 C CA  . LEU B 2 85  ? 118.948 98.854  141.690 1.00 52.77  ? 85  LEU B CA  1 
ATOM 4472 C C   . LEU B 2 85  ? 119.212 99.150  143.160 1.00 56.71  ? 85  LEU B C   1 
ATOM 4473 O O   . LEU B 2 85  ? 119.509 98.273  143.953 1.00 61.79  ? 85  LEU B O   1 
ATOM 4474 C CB  . LEU B 2 85  ? 117.445 98.694  141.455 1.00 50.95  ? 85  LEU B CB  1 
ATOM 4475 C CG  . LEU B 2 85  ? 116.968 98.977  140.027 1.00 49.87  ? 85  LEU B CG  1 
ATOM 4476 C CD1 . LEU B 2 85  ? 115.537 98.528  139.844 1.00 52.43  ? 85  LEU B CD1 1 
ATOM 4477 C CD2 . LEU B 2 85  ? 117.110 100.458 139.699 1.00 43.75  ? 85  LEU B CD2 1 
ATOM 4478 N N   . LYS B 2 86  ? 119.091 100.405 143.512 1.00 54.61  ? 86  LYS B N   1 
ATOM 4479 C CA  . LYS B 2 86  ? 119.415 100.944 144.813 1.00 51.45  ? 86  LYS B CA  1 
ATOM 4480 C C   . LYS B 2 86  ? 118.348 101.948 145.264 1.00 51.96  ? 86  LYS B C   1 
ATOM 4481 O O   . LYS B 2 86  ? 117.734 102.630 144.431 1.00 55.20  ? 86  LYS B O   1 
ATOM 4482 C CB  . LYS B 2 86  ? 120.802 101.601 144.731 1.00 55.63  ? 86  LYS B CB  1 
ATOM 4483 C CG  . LYS B 2 86  ? 120.915 102.811 143.823 1.00 57.97  ? 86  LYS B CG  1 
ATOM 4484 C CD  . LYS B 2 86  ? 122.325 103.393 143.834 1.00 61.90  ? 86  LYS B CD  1 
ATOM 4485 C CE  . LYS B 2 86  ? 123.345 102.578 143.105 1.00 64.66  ? 86  LYS B CE  1 
ATOM 4486 N NZ  . LYS B 2 86  ? 124.601 103.367 143.112 1.00 65.10  ? 86  LYS B NZ  1 
ATOM 4487 N N   . PRO B 2 87  ? 118.081 102.047 146.569 1.00 49.47  ? 87  PRO B N   1 
ATOM 4488 C CA  . PRO B 2 87  ? 116.839 102.677 147.045 1.00 45.63  ? 87  PRO B CA  1 
ATOM 4489 C C   . PRO B 2 87  ? 116.678 104.131 146.646 1.00 50.06  ? 87  PRO B C   1 
ATOM 4490 O O   . PRO B 2 87  ? 115.569 104.661 146.812 1.00 58.81  ? 87  PRO B O   1 
ATOM 4491 C CB  . PRO B 2 87  ? 116.932 102.520 148.576 1.00 44.68  ? 87  PRO B CB  1 
ATOM 4492 C CG  . PRO B 2 87  ? 118.326 102.080 148.866 1.00 51.48  ? 87  PRO B CG  1 
ATOM 4493 C CD  . PRO B 2 87  ? 118.774 101.342 147.649 1.00 50.04  ? 87  PRO B CD  1 
ATOM 4494 N N   . GLU B 2 88  ? 117.707 104.807 146.153 1.00 50.56  ? 88  GLU B N   1 
ATOM 4495 C CA  . GLU B 2 88  ? 117.509 106.172 145.683 1.00 47.49  ? 88  GLU B CA  1 
ATOM 4496 C C   . GLU B 2 88  ? 117.217 106.237 144.193 1.00 53.53  ? 88  GLU B C   1 
ATOM 4497 O O   . GLU B 2 88  ? 117.223 107.333 143.625 1.00 57.21  ? 88  GLU B O   1 
ATOM 4498 C CB  . GLU B 2 88  ? 118.709 107.059 146.052 1.00 48.54  ? 88  GLU B CB  1 
ATOM 4499 C CG  . GLU B 2 88  ? 120.038 106.787 145.332 1.00 58.04  ? 88  GLU B CG  1 
ATOM 4500 C CD  . GLU B 2 88  ? 120.838 105.690 145.997 1.00 69.29  ? 88  GLU B CD  1 
ATOM 4501 O OE1 . GLU B 2 88  ? 120.253 104.952 146.806 1.00 69.10  ? 88  GLU B OE1 1 
ATOM 4502 O OE2 . GLU B 2 88  ? 122.058 105.609 145.770 1.00 72.13  ? 88  GLU B OE2 1 
ATOM 4503 N N   . ASP B 2 89  ? 116.985 105.099 143.554 1.00 56.57  ? 89  ASP B N   1 
ATOM 4504 C CA  . ASP B 2 89  ? 116.437 105.069 142.208 1.00 54.10  ? 89  ASP B CA  1 
ATOM 4505 C C   . ASP B 2 89  ? 114.915 105.153 142.209 1.00 53.57  ? 89  ASP B C   1 
ATOM 4506 O O   . ASP B 2 89  ? 114.299 105.114 141.139 1.00 56.74  ? 89  ASP B O   1 
ATOM 4507 C CB  . ASP B 2 89  ? 116.895 103.799 141.489 1.00 52.96  ? 89  ASP B CB  1 
ATOM 4508 C CG  . ASP B 2 89  ? 118.402 103.699 141.394 1.00 59.94  ? 89  ASP B CG  1 
ATOM 4509 O OD1 . ASP B 2 89  ? 119.073 104.754 141.373 1.00 63.08  ? 89  ASP B OD1 1 
ATOM 4510 O OD2 . ASP B 2 89  ? 118.926 102.566 141.327 1.00 61.45  ? 89  ASP B OD2 1 
ATOM 4511 N N   . THR B 2 90  ? 114.299 105.248 143.387 1.00 50.26  ? 90  THR B N   1 
ATOM 4512 C CA  . THR B 2 90  ? 112.852 105.388 143.493 1.00 44.91  ? 90  THR B CA  1 
ATOM 4513 C C   . THR B 2 90  ? 112.420 106.760 142.990 1.00 56.18  ? 90  THR B C   1 
ATOM 4514 O O   . THR B 2 90  ? 112.751 107.783 143.600 1.00 66.14  ? 90  THR B O   1 
ATOM 4515 C CB  . THR B 2 90  ? 112.409 105.191 144.942 1.00 43.32  ? 90  THR B CB  1 
ATOM 4516 O OG1 . THR B 2 90  ? 112.735 103.863 145.370 1.00 56.82  ? 90  THR B OG1 1 
ATOM 4517 C CG2 . THR B 2 90  ? 110.912 105.427 145.087 1.00 46.92  ? 90  THR B CG2 1 
ATOM 4518 N N   . ALA B 2 91  ? 111.675 106.782 141.889 1.00 52.77  ? 91  ALA B N   1 
ATOM 4519 C CA  . ALA B 2 91  ? 111.208 108.022 141.278 1.00 47.36  ? 91  ALA B CA  1 
ATOM 4520 C C   . ALA B 2 91  ? 110.192 107.668 140.198 1.00 51.00  ? 91  ALA B C   1 
ATOM 4521 O O   . ALA B 2 91  ? 109.961 106.494 139.893 1.00 60.44  ? 91  ALA B O   1 
ATOM 4522 C CB  . ALA B 2 91  ? 112.370 108.834 140.699 1.00 49.80  ? 91  ALA B CB  1 
ATOM 4523 N N   . VAL B 2 92  ? 109.585 108.699 139.619 1.00 49.65  ? 92  VAL B N   1 
ATOM 4524 C CA  . VAL B 2 92  ? 108.716 108.553 138.459 1.00 48.99  ? 92  VAL B CA  1 
ATOM 4525 C C   . VAL B 2 92  ? 109.569 108.787 137.222 1.00 51.59  ? 92  VAL B C   1 
ATOM 4526 O O   . VAL B 2 92  ? 110.180 109.852 137.072 1.00 54.90  ? 92  VAL B O   1 
ATOM 4527 C CB  . VAL B 2 92  ? 107.534 109.534 138.511 1.00 50.38  ? 92  VAL B CB  1 
ATOM 4528 C CG1 . VAL B 2 92  ? 106.707 109.430 137.240 1.00 53.36  ? 92  VAL B CG1 1 
ATOM 4529 C CG2 . VAL B 2 92  ? 106.677 109.270 139.736 1.00 54.84  ? 92  VAL B CG2 1 
ATOM 4530 N N   . TYR B 2 93  ? 109.623 107.792 136.345 1.00 48.78  ? 93  TYR B N   1 
ATOM 4531 C CA  . TYR B 2 93  ? 110.463 107.828 135.159 1.00 43.46  ? 93  TYR B CA  1 
ATOM 4532 C C   . TYR B 2 93  ? 109.629 108.228 133.951 1.00 51.24  ? 93  TYR B C   1 
ATOM 4533 O O   . TYR B 2 93  ? 108.538 107.688 133.734 1.00 54.96  ? 93  TYR B O   1 
ATOM 4534 C CB  . TYR B 2 93  ? 111.125 106.470 134.923 1.00 43.22  ? 93  TYR B CB  1 
ATOM 4535 C CG  . TYR B 2 93  ? 112.243 106.161 135.894 1.00 44.50  ? 93  TYR B CG  1 
ATOM 4536 C CD1 . TYR B 2 93  ? 111.968 105.734 137.186 1.00 44.12  ? 93  TYR B CD1 1 
ATOM 4537 C CD2 . TYR B 2 93  ? 113.573 106.292 135.517 1.00 41.10  ? 93  TYR B CD2 1 
ATOM 4538 C CE1 . TYR B 2 93  ? 112.985 105.451 138.077 1.00 44.98  ? 93  TYR B CE1 1 
ATOM 4539 C CE2 . TYR B 2 93  ? 114.597 106.009 136.402 1.00 44.04  ? 93  TYR B CE2 1 
ATOM 4540 C CZ  . TYR B 2 93  ? 114.297 105.589 137.680 1.00 42.64  ? 93  TYR B CZ  1 
ATOM 4541 O OH  . TYR B 2 93  ? 115.311 105.306 138.566 1.00 48.61  ? 93  TYR B OH  1 
ATOM 4542 N N   . TYR B 2 94  ? 110.146 109.176 133.176 1.00 51.20  ? 94  TYR B N   1 
ATOM 4543 C CA  . TYR B 2 94  ? 109.502 109.671 131.971 1.00 49.40  ? 94  TYR B CA  1 
ATOM 4544 C C   . TYR B 2 94  ? 110.418 109.424 130.782 1.00 50.71  ? 94  TYR B C   1 
ATOM 4545 O O   . TYR B 2 94  ? 111.644 109.519 130.904 1.00 52.57  ? 94  TYR B O   1 
ATOM 4546 C CB  . TYR B 2 94  ? 109.204 111.174 132.072 1.00 50.94  ? 94  TYR B CB  1 
ATOM 4547 C CG  . TYR B 2 94  ? 108.435 111.597 133.304 1.00 54.56  ? 94  TYR B CG  1 
ATOM 4548 C CD1 . TYR B 2 94  ? 107.047 111.620 133.308 1.00 55.69  ? 94  TYR B CD1 1 
ATOM 4549 C CD2 . TYR B 2 94  ? 109.100 111.989 134.459 1.00 51.94  ? 94  TYR B CD2 1 
ATOM 4550 C CE1 . TYR B 2 94  ? 106.343 112.013 134.432 1.00 57.50  ? 94  TYR B CE1 1 
ATOM 4551 C CE2 . TYR B 2 94  ? 108.405 112.383 135.586 1.00 54.37  ? 94  TYR B CE2 1 
ATOM 4552 C CZ  . TYR B 2 94  ? 107.027 112.395 135.566 1.00 57.10  ? 94  TYR B CZ  1 
ATOM 4553 O OH  . TYR B 2 94  ? 106.331 112.785 136.688 1.00 62.61  ? 94  TYR B OH  1 
ATOM 4554 N N   . CYS B 2 95  ? 109.831 109.100 129.636 1.00 53.36  ? 95  CYS B N   1 
ATOM 4555 C CA  . CYS B 2 95  ? 110.573 109.135 128.387 1.00 47.13  ? 95  CYS B CA  1 
ATOM 4556 C C   . CYS B 2 95  ? 110.200 110.402 127.633 1.00 54.03  ? 95  CYS B C   1 
ATOM 4557 O O   . CYS B 2 95  ? 109.041 110.824 127.622 1.00 59.90  ? 95  CYS B O   1 
ATOM 4558 C CB  . CYS B 2 95  ? 110.307 107.905 127.515 1.00 50.30  ? 95  CYS B CB  1 
ATOM 4559 S SG  . CYS B 2 95  ? 108.601 107.638 127.006 1.00 79.16  ? 95  CYS B SG  1 
ATOM 4560 N N   . ASN B 2 96  ? 111.200 111.012 127.010 1.00 49.94  ? 96  ASN B N   1 
ATOM 4561 C CA  . ASN B 2 96  ? 111.049 112.332 126.424 1.00 42.59  ? 96  ASN B CA  1 
ATOM 4562 C C   . ASN B 2 96  ? 111.572 112.332 124.998 1.00 48.32  ? 96  ASN B C   1 
ATOM 4563 O O   . ASN B 2 96  ? 112.526 111.622 124.665 1.00 53.95  ? 96  ASN B O   1 
ATOM 4564 C CB  . ASN B 2 96  ? 111.787 113.394 127.249 1.00 43.46  ? 96  ASN B CB  1 
ATOM 4565 C CG  . ASN B 2 96  ? 111.596 114.793 126.704 1.00 48.95  ? 96  ASN B CG  1 
ATOM 4566 O OD1 . ASN B 2 96  ? 112.561 115.526 126.496 1.00 52.17  ? 96  ASN B OD1 1 
ATOM 4567 N ND2 . ASN B 2 96  ? 110.346 115.170 126.461 1.00 54.65  ? 96  ASN B ND2 1 
ATOM 4568 N N   . VAL B 2 97  ? 110.927 113.136 124.158 1.00 51.56  ? 97  VAL B N   1 
ATOM 4569 C CA  . VAL B 2 97  ? 111.429 113.406 122.814 1.00 46.28  ? 97  VAL B CA  1 
ATOM 4570 C C   . VAL B 2 97  ? 111.381 114.911 122.571 1.00 52.80  ? 97  VAL B C   1 
ATOM 4571 O O   . VAL B 2 97  ? 110.412 115.582 122.948 1.00 61.85  ? 97  VAL B O   1 
ATOM 4572 C CB  . VAL B 2 97  ? 110.654 112.625 121.731 1.00 42.43  ? 97  VAL B CB  1 
ATOM 4573 C CG1 . VAL B 2 97  ? 109.239 113.149 121.565 1.00 44.65  ? 97  VAL B CG1 1 
ATOM 4574 C CG2 . VAL B 2 97  ? 111.410 112.662 120.406 1.00 45.30  ? 97  VAL B CG2 1 
ATOM 4575 N N   . LYS B 2 98  ? 112.447 115.443 121.975 1.00 48.48  ? 98  LYS B N   1 
ATOM 4576 C CA  . LYS B 2 98  ? 112.608 116.872 121.758 1.00 46.39  ? 98  LYS B CA  1 
ATOM 4577 C C   . LYS B 2 98  ? 112.908 117.160 120.294 1.00 56.84  ? 98  LYS B C   1 
ATOM 4578 O O   . LYS B 2 98  ? 113.411 116.305 119.560 1.00 65.33  ? 98  LYS B O   1 
ATOM 4579 C CB  . LYS B 2 98  ? 113.745 117.457 122.608 1.00 45.40  ? 98  LYS B CB  1 
ATOM 4580 C CG  . LYS B 2 98  ? 113.939 116.826 123.968 1.00 47.71  ? 98  LYS B CG  1 
ATOM 4581 C CD  . LYS B 2 98  ? 115.301 117.206 124.525 1.00 47.32  ? 98  LYS B CD  1 
ATOM 4582 C CE  . LYS B 2 98  ? 115.526 116.624 125.905 1.00 43.90  ? 98  LYS B CE  1 
ATOM 4583 N NZ  . LYS B 2 98  ? 114.892 117.452 126.967 1.00 47.08  ? 98  LYS B NZ  1 
ATOM 4584 N N   . ASP B 2 99  ? 112.601 118.395 119.888 1.00 53.53  ? 99  ASP B N   1 
ATOM 4585 C CA  . ASP B 2 99  ? 112.973 118.931 118.578 1.00 52.78  ? 99  ASP B CA  1 
ATOM 4586 C C   . ASP B 2 99  ? 112.535 117.994 117.452 1.00 56.79  ? 99  ASP B C   1 
ATOM 4587 O O   . ASP B 2 99  ? 113.335 117.529 116.638 1.00 61.29  ? 99  ASP B O   1 
ATOM 4588 C CB  . ASP B 2 99  ? 114.480 119.206 118.515 1.00 56.52  ? 99  ASP B CB  1 
ATOM 4589 C CG  . ASP B 2 99  ? 114.817 120.394 117.637 1.00 73.34  ? 99  ASP B CG  1 
ATOM 4590 O OD1 . ASP B 2 99  ? 113.881 121.089 117.189 1.00 76.13  ? 99  ASP B OD1 1 
ATOM 4591 O OD2 . ASP B 2 99  ? 116.019 120.632 117.394 1.00 83.37  ? 99  ASP B OD2 1 
ATOM 4592 N N   . LEU B 2 100 ? 111.233 117.723 117.422 1.00 54.64  ? 100 LEU B N   1 
ATOM 4593 C CA  . LEU B 2 100 ? 110.680 116.760 116.481 1.00 50.03  ? 100 LEU B CA  1 
ATOM 4594 C C   . LEU B 2 100 ? 110.472 117.336 115.086 1.00 52.29  ? 100 LEU B C   1 
ATOM 4595 O O   . LEU B 2 100 ? 110.090 116.588 114.179 1.00 56.45  ? 100 LEU B O   1 
ATOM 4596 C CB  . LEU B 2 100 ? 109.359 116.207 117.015 1.00 45.08  ? 100 LEU B CB  1 
ATOM 4597 C CG  . LEU B 2 100 ? 109.474 114.951 117.876 1.00 37.47  ? 100 LEU B CG  1 
ATOM 4598 C CD1 . LEU B 2 100 ? 108.131 114.610 118.489 1.00 40.93  ? 100 LEU B CD1 1 
ATOM 4599 C CD2 . LEU B 2 100 ? 110.008 113.797 117.053 1.00 42.34  ? 100 LEU B CD2 1 
ATOM 4600 N N   . GLY B 2 101 ? 110.702 118.625 114.891 1.00 51.00  ? 101 GLY B N   1 
ATOM 4601 C CA  . GLY B 2 101 ? 110.597 119.243 113.588 1.00 52.47  ? 101 GLY B CA  1 
ATOM 4602 C C   . GLY B 2 101 ? 109.547 120.335 113.540 1.00 53.64  ? 101 GLY B C   1 
ATOM 4603 O O   . GLY B 2 101 ? 109.047 120.814 114.562 1.00 61.60  ? 101 GLY B O   1 
ATOM 4604 N N   . ALA B 2 102 ? 109.214 120.739 112.313 1.00 53.59  ? 102 ALA B N   1 
ATOM 4605 C CA  . ALA B 2 102 ? 108.218 121.777 112.090 1.00 50.97  ? 102 ALA B CA  1 
ATOM 4606 C C   . ALA B 2 102 ? 106.789 121.253 112.122 1.00 53.58  ? 102 ALA B C   1 
ATOM 4607 O O   . ALA B 2 102 ? 105.856 122.049 112.270 1.00 60.76  ? 102 ALA B O   1 
ATOM 4608 C CB  . ALA B 2 102 ? 108.469 122.472 110.749 1.00 49.63  ? 102 ALA B CB  1 
ATOM 4609 N N   . TRP B 2 103 ? 106.597 119.939 111.991 1.00 52.30  ? 103 TRP B N   1 
ATOM 4610 C CA  . TRP B 2 103 ? 105.263 119.356 112.059 1.00 49.92  ? 103 TRP B CA  1 
ATOM 4611 C C   . TRP B 2 103 ? 104.683 119.356 113.466 1.00 52.98  ? 103 TRP B C   1 
ATOM 4612 O O   . TRP B 2 103 ? 103.500 119.040 113.630 1.00 57.69  ? 103 TRP B O   1 
ATOM 4613 C CB  . TRP B 2 103 ? 105.285 117.928 111.511 1.00 45.79  ? 103 TRP B CB  1 
ATOM 4614 C CG  . TRP B 2 103 ? 103.936 117.451 111.097 1.00 51.40  ? 103 TRP B CG  1 
ATOM 4615 C CD1 . TRP B 2 103 ? 103.165 116.526 111.736 1.00 52.15  ? 103 TRP B CD1 1 
ATOM 4616 C CD2 . TRP B 2 103 ? 103.169 117.914 109.982 1.00 59.51  ? 103 TRP B CD2 1 
ATOM 4617 N NE1 . TRP B 2 103 ? 101.976 116.363 111.070 1.00 58.22  ? 103 TRP B NE1 1 
ATOM 4618 C CE2 . TRP B 2 103 ? 101.952 117.208 109.992 1.00 59.71  ? 103 TRP B CE2 1 
ATOM 4619 C CE3 . TRP B 2 103 ? 103.398 118.849 108.969 1.00 54.75  ? 103 TRP B CE3 1 
ATOM 4620 C CZ2 . TRP B 2 103 ? 100.965 117.412 109.034 1.00 61.00  ? 103 TRP B CZ2 1 
ATOM 4621 C CZ3 . TRP B 2 103 ? 102.420 119.046 108.015 1.00 54.88  ? 103 TRP B CZ3 1 
ATOM 4622 C CH2 . TRP B 2 103 ? 101.219 118.330 108.052 1.00 60.35  ? 103 TRP B CH2 1 
ATOM 4623 N N   . TYR B 2 104 ? 105.474 119.705 114.473 1.00 51.10  ? 104 TYR B N   1 
ATOM 4624 C CA  . TYR B 2 104 ? 105.074 119.595 115.865 1.00 46.17  ? 104 TYR B CA  1 
ATOM 4625 C C   . TYR B 2 104 ? 105.199 120.956 116.539 1.00 55.90  ? 104 TYR B C   1 
ATOM 4626 O O   . TYR B 2 104 ? 105.980 121.809 116.109 1.00 60.36  ? 104 TYR B O   1 
ATOM 4627 C CB  . TYR B 2 104 ? 105.922 118.538 116.575 1.00 46.71  ? 104 TYR B CB  1 
ATOM 4628 C CG  . TYR B 2 104 ? 105.960 117.227 115.814 1.00 44.07  ? 104 TYR B CG  1 
ATOM 4629 C CD1 . TYR B 2 104 ? 105.012 116.240 116.041 1.00 42.79  ? 104 TYR B CD1 1 
ATOM 4630 C CD2 . TYR B 2 104 ? 106.925 116.994 114.841 1.00 45.02  ? 104 TYR B CD2 1 
ATOM 4631 C CE1 . TYR B 2 104 ? 105.039 115.047 115.340 1.00 42.99  ? 104 TYR B CE1 1 
ATOM 4632 C CE2 . TYR B 2 104 ? 106.960 115.806 114.137 1.00 43.50  ? 104 TYR B CE2 1 
ATOM 4633 C CZ  . TYR B 2 104 ? 106.015 114.836 114.389 1.00 44.06  ? 104 TYR B CZ  1 
ATOM 4634 O OH  . TYR B 2 104 ? 106.047 113.653 113.688 1.00 49.60  ? 104 TYR B OH  1 
ATOM 4635 N N   . ASN B 2 105 ? 104.416 121.154 117.601 1.00 55.14  ? 105 ASN B N   1 
ATOM 4636 C CA  . ASN B 2 105 ? 104.186 122.483 118.149 1.00 53.76  ? 105 ASN B CA  1 
ATOM 4637 C C   . ASN B 2 105 ? 104.817 122.724 119.515 1.00 57.80  ? 105 ASN B C   1 
ATOM 4638 O O   . ASN B 2 105 ? 104.817 123.870 119.975 1.00 65.87  ? 105 ASN B O   1 
ATOM 4639 C CB  . ASN B 2 105 ? 102.676 122.748 118.257 1.00 52.29  ? 105 ASN B CB  1 
ATOM 4640 C CG  . ASN B 2 105 ? 101.970 122.669 116.918 1.00 60.99  ? 105 ASN B CG  1 
ATOM 4641 O OD1 . ASN B 2 105 ? 102.368 123.319 115.952 1.00 65.04  ? 105 ASN B OD1 1 
ATOM 4642 N ND2 . ASN B 2 105 ? 100.912 121.868 116.854 1.00 62.60  ? 105 ASN B ND2 1 
ATOM 4643 N N   . ASP B 2 106 ? 105.355 121.697 120.172 1.00 54.48  ? 106 ASP B N   1 
ATOM 4644 C CA  . ASP B 2 106 ? 105.711 121.807 121.581 1.00 60.62  ? 106 ASP B CA  1 
ATOM 4645 C C   . ASP B 2 106 ? 107.205 121.755 121.868 1.00 56.83  ? 106 ASP B C   1 
ATOM 4646 O O   . ASP B 2 106 ? 107.636 122.307 122.881 1.00 67.26  ? 106 ASP B O   1 
ATOM 4647 C CB  . ASP B 2 106 ? 105.021 120.698 122.385 1.00 62.17  ? 106 ASP B CB  1 
ATOM 4648 C CG  . ASP B 2 106 ? 103.519 120.885 122.463 1.00 65.37  ? 106 ASP B CG  1 
ATOM 4649 O OD1 . ASP B 2 106 ? 103.060 122.046 122.419 1.00 69.05  ? 106 ASP B OD1 1 
ATOM 4650 O OD2 . ASP B 2 106 ? 102.796 119.872 122.566 1.00 66.44  ? 106 ASP B OD2 1 
ATOM 4651 N N   . TYR B 2 107 ? 107.987 121.074 121.023 1.00 48.95  ? 107 TYR B N   1 
ATOM 4652 C CA  . TYR B 2 107 ? 109.425 120.858 121.194 1.00 55.22  ? 107 TYR B CA  1 
ATOM 4653 C C   . TYR B 2 107 ? 109.752 119.866 122.308 1.00 64.59  ? 107 TYR B C   1 
ATOM 4654 O O   . TYR B 2 107 ? 110.873 119.354 122.367 1.00 69.15  ? 107 TYR B O   1 
ATOM 4655 C CB  . TYR B 2 107 ? 110.159 122.186 121.443 1.00 53.02  ? 107 TYR B CB  1 
ATOM 4656 C CG  . TYR B 2 107 ? 111.620 122.012 121.799 1.00 53.88  ? 107 TYR B CG  1 
ATOM 4657 C CD1 . TYR B 2 107 ? 112.583 121.812 120.821 1.00 61.78  ? 107 TYR B CD1 1 
ATOM 4658 C CD2 . TYR B 2 107 ? 112.031 122.039 123.127 1.00 53.15  ? 107 TYR B CD2 1 
ATOM 4659 C CE1 . TYR B 2 107 ? 113.914 121.638 121.158 1.00 59.92  ? 107 TYR B CE1 1 
ATOM 4660 C CE2 . TYR B 2 107 ? 113.352 121.865 123.472 1.00 57.97  ? 107 TYR B CE2 1 
ATOM 4661 C CZ  . TYR B 2 107 ? 114.290 121.668 122.486 1.00 58.34  ? 107 TYR B CZ  1 
ATOM 4662 O OH  . TYR B 2 107 ? 115.608 121.499 122.834 1.00 62.45  ? 107 TYR B OH  1 
ATOM 4663 N N   . ASP B 2 108 ? 108.771 119.514 123.132 1.00 63.89  ? 108 ASP B N   1 
ATOM 4664 C CA  . ASP B 2 108 ? 108.981 118.572 124.225 1.00 54.08  ? 108 ASP B CA  1 
ATOM 4665 C C   . ASP B 2 108 ? 107.743 117.707 124.369 1.00 57.53  ? 108 ASP B C   1 
ATOM 4666 O O   . ASP B 2 108 ? 106.640 118.230 124.556 1.00 59.84  ? 108 ASP B O   1 
ATOM 4667 C CB  . ASP B 2 108 ? 109.275 119.284 125.554 1.00 58.61  ? 108 ASP B CB  1 
ATOM 4668 C CG  . ASP B 2 108 ? 110.624 119.982 125.572 1.00 67.05  ? 108 ASP B CG  1 
ATOM 4669 O OD1 . ASP B 2 108 ? 111.551 119.522 124.875 1.00 64.82  ? 108 ASP B OD1 1 
ATOM 4670 O OD2 . ASP B 2 108 ? 110.760 120.993 126.292 1.00 75.11  ? 108 ASP B OD2 1 
ATOM 4671 N N   . TYR B 2 109 ? 107.924 116.393 124.284 1.00 51.81  ? 109 TYR B N   1 
ATOM 4672 C CA  . TYR B 2 109 ? 106.835 115.459 124.525 1.00 49.75  ? 109 TYR B CA  1 
ATOM 4673 C C   . TYR B 2 109 ? 107.260 114.443 125.571 1.00 49.67  ? 109 TYR B C   1 
ATOM 4674 O O   . TYR B 2 109 ? 108.364 113.887 125.497 1.00 54.70  ? 109 TYR B O   1 
ATOM 4675 C CB  . TYR B 2 109 ? 106.391 114.771 123.234 1.00 50.20  ? 109 TYR B CB  1 
ATOM 4676 C CG  . TYR B 2 109 ? 105.838 115.747 122.223 1.00 51.07  ? 109 TYR B CG  1 
ATOM 4677 C CD1 . TYR B 2 109 ? 104.506 116.139 122.271 1.00 51.50  ? 109 TYR B CD1 1 
ATOM 4678 C CD2 . TYR B 2 109 ? 106.645 116.290 121.234 1.00 48.96  ? 109 TYR B CD2 1 
ATOM 4679 C CE1 . TYR B 2 109 ? 103.991 117.035 121.357 1.00 48.63  ? 109 TYR B CE1 1 
ATOM 4680 C CE2 . TYR B 2 109 ? 106.139 117.188 120.314 1.00 48.39  ? 109 TYR B CE2 1 
ATOM 4681 C CZ  . TYR B 2 109 ? 104.811 117.557 120.381 1.00 47.74  ? 109 TYR B CZ  1 
ATOM 4682 O OH  . TYR B 2 109 ? 104.301 118.451 119.468 1.00 53.80  ? 109 TYR B OH  1 
ATOM 4683 N N   . TRP B 2 110 ? 106.372 114.222 126.540 1.00 49.04  ? 110 TRP B N   1 
ATOM 4684 C CA  . TRP B 2 110 ? 106.596 113.361 127.688 1.00 49.86  ? 110 TRP B CA  1 
ATOM 4685 C C   . TRP B 2 110 ? 105.517 112.295 127.780 1.00 55.71  ? 110 TRP B C   1 
ATOM 4686 O O   . TRP B 2 110 ? 104.401 112.458 127.279 1.00 63.86  ? 110 TRP B O   1 
ATOM 4687 C CB  . TRP B 2 110 ? 106.599 114.150 129.001 1.00 53.51  ? 110 TRP B CB  1 
ATOM 4688 C CG  . TRP B 2 110 ? 107.506 115.304 128.994 1.00 49.82  ? 110 TRP B CG  1 
ATOM 4689 C CD1 . TRP B 2 110 ? 107.290 116.528 128.434 1.00 48.61  ? 110 TRP B CD1 1 
ATOM 4690 C CD2 . TRP B 2 110 ? 108.827 115.324 129.517 1.00 47.10  ? 110 TRP B CD2 1 
ATOM 4691 N NE1 . TRP B 2 110 ? 108.392 117.327 128.616 1.00 51.93  ? 110 TRP B NE1 1 
ATOM 4692 C CE2 . TRP B 2 110 ? 109.352 116.605 129.275 1.00 48.55  ? 110 TRP B CE2 1 
ATOM 4693 C CE3 . TRP B 2 110 ? 109.616 114.383 130.183 1.00 46.34  ? 110 TRP B CE3 1 
ATOM 4694 C CZ2 . TRP B 2 110 ? 110.627 116.966 129.675 1.00 49.75  ? 110 TRP B CZ2 1 
ATOM 4695 C CZ3 . TRP B 2 110 ? 110.875 114.743 130.577 1.00 49.31  ? 110 TRP B CZ3 1 
ATOM 4696 C CH2 . TRP B 2 110 ? 111.372 116.017 130.319 1.00 51.64  ? 110 TRP B CH2 1 
ATOM 4697 N N   . GLY B 2 111 ? 105.869 111.200 128.441 1.00 51.41  ? 111 GLY B N   1 
ATOM 4698 C CA  . GLY B 2 111 ? 104.875 110.253 128.883 1.00 55.60  ? 111 GLY B CA  1 
ATOM 4699 C C   . GLY B 2 111 ? 104.289 110.649 130.223 1.00 61.32  ? 111 GLY B C   1 
ATOM 4700 O O   . GLY B 2 111 ? 104.703 111.618 130.858 1.00 67.97  ? 111 GLY B O   1 
ATOM 4701 N N   . GLN B 2 112 ? 103.302 109.872 130.660 1.00 60.97  ? 112 GLN B N   1 
ATOM 4702 C CA  . GLN B 2 112 ? 102.687 110.102 131.959 1.00 63.55  ? 112 GLN B CA  1 
ATOM 4703 C C   . GLN B 2 112 ? 103.550 109.605 133.110 1.00 68.04  ? 112 GLN B C   1 
ATOM 4704 O O   . GLN B 2 112 ? 103.188 109.816 134.272 1.00 71.73  ? 112 GLN B O   1 
ATOM 4705 C CB  . GLN B 2 112 ? 101.308 109.439 132.011 1.00 71.43  ? 112 GLN B CB  1 
ATOM 4706 C CG  . GLN B 2 112 ? 100.316 110.028 131.021 1.00 75.50  ? 112 GLN B CG  1 
ATOM 4707 C CD  . GLN B 2 112 ? 100.211 111.537 131.131 1.00 75.61  ? 112 GLN B CD  1 
ATOM 4708 O OE1 . GLN B 2 112 ? 100.047 112.082 132.224 1.00 77.49  ? 112 GLN B OE1 1 
ATOM 4709 N NE2 . GLN B 2 112 ? 100.312 112.222 129.998 1.00 70.85  ? 112 GLN B NE2 1 
ATOM 4710 N N   . GLY B 2 113 ? 104.666 108.952 132.816 1.00 67.95  ? 113 GLY B N   1 
ATOM 4711 C CA  . GLY B 2 113 ? 105.578 108.485 133.834 1.00 57.42  ? 113 GLY B CA  1 
ATOM 4712 C C   . GLY B 2 113 ? 105.188 107.127 134.389 1.00 60.67  ? 113 GLY B C   1 
ATOM 4713 O O   . GLY B 2 113 ? 104.036 106.699 134.335 1.00 69.26  ? 113 GLY B O   1 
ATOM 4714 N N   . THR B 2 114 ? 106.188 106.435 134.929 1.00 58.14  ? 114 THR B N   1 
ATOM 4715 C CA  . THR B 2 114 ? 105.971 105.159 135.594 1.00 56.33  ? 114 THR B CA  1 
ATOM 4716 C C   . THR B 2 114 ? 106.732 105.162 136.912 1.00 56.72  ? 114 THR B C   1 
ATOM 4717 O O   . THR B 2 114 ? 107.878 105.613 136.969 1.00 61.07  ? 114 THR B O   1 
ATOM 4718 C CB  . THR B 2 114 ? 106.397 103.980 134.700 1.00 54.85  ? 114 THR B CB  1 
ATOM 4719 O OG1 . THR B 2 114 ? 106.015 102.743 135.314 1.00 67.08  ? 114 THR B OG1 1 
ATOM 4720 C CG2 . THR B 2 114 ? 107.899 103.987 134.427 1.00 48.87  ? 114 THR B CG2 1 
ATOM 4721 N N   . GLN B 2 115 ? 106.084 104.696 137.973 1.00 53.72  ? 115 GLN B N   1 
ATOM 4722 C CA  . GLN B 2 115 ? 106.684 104.746 139.299 1.00 52.03  ? 115 GLN B CA  1 
ATOM 4723 C C   . GLN B 2 115 ? 107.603 103.550 139.509 1.00 56.95  ? 115 GLN B C   1 
ATOM 4724 O O   . GLN B 2 115 ? 107.204 102.403 139.286 1.00 59.92  ? 115 GLN B O   1 
ATOM 4725 C CB  . GLN B 2 115 ? 105.600 104.772 140.376 1.00 58.69  ? 115 GLN B CB  1 
ATOM 4726 C CG  . GLN B 2 115 ? 106.143 104.877 141.793 1.00 60.02  ? 115 GLN B CG  1 
ATOM 4727 C CD  . GLN B 2 115 ? 106.509 106.298 142.175 1.00 63.60  ? 115 GLN B CD  1 
ATOM 4728 O OE1 . GLN B 2 115 ? 107.628 106.568 142.612 1.00 65.53  ? 115 GLN B OE1 1 
ATOM 4729 N NE2 . GLN B 2 115 ? 105.560 107.213 142.023 1.00 58.70  ? 115 GLN B NE2 1 
ATOM 4730 N N   . VAL B 2 116 ? 108.833 103.819 139.939 1.00 58.51  ? 116 VAL B N   1 
ATOM 4731 C CA  . VAL B 2 116 ? 109.791 102.784 140.307 1.00 54.00  ? 116 VAL B CA  1 
ATOM 4732 C C   . VAL B 2 116 ? 110.156 103.007 141.764 1.00 54.81  ? 116 VAL B C   1 
ATOM 4733 O O   . VAL B 2 116 ? 110.696 104.063 142.119 1.00 59.88  ? 116 VAL B O   1 
ATOM 4734 C CB  . VAL B 2 116 ? 111.044 102.819 139.418 1.00 50.50  ? 116 VAL B CB  1 
ATOM 4735 C CG1 . VAL B 2 116 ? 112.117 101.898 139.980 1.00 51.67  ? 116 VAL B CG1 1 
ATOM 4736 C CG2 . VAL B 2 116 ? 110.695 102.436 137.991 1.00 54.18  ? 116 VAL B CG2 1 
ATOM 4737 N N   . THR B 2 117 ? 109.861 102.024 142.607 1.00 50.80  ? 117 THR B N   1 
ATOM 4738 C CA  . THR B 2 117 ? 110.145 102.107 144.031 1.00 47.01  ? 117 THR B CA  1 
ATOM 4739 C C   . THR B 2 117 ? 111.058 100.954 144.416 1.00 49.58  ? 117 THR B C   1 
ATOM 4740 O O   . THR B 2 117 ? 110.796 99.802  144.055 1.00 56.58  ? 117 THR B O   1 
ATOM 4741 C CB  . THR B 2 117 ? 108.855 102.078 144.855 1.00 49.07  ? 117 THR B CB  1 
ATOM 4742 O OG1 . THR B 2 117 ? 107.966 103.099 144.387 1.00 59.20  ? 117 THR B OG1 1 
ATOM 4743 C CG2 . THR B 2 117 ? 109.162 102.336 146.323 1.00 50.85  ? 117 THR B CG2 1 
ATOM 4744 N N   . VAL B 2 118 ? 112.132 101.268 145.133 1.00 47.24  ? 118 VAL B N   1 
ATOM 4745 C CA  . VAL B 2 118 ? 113.138 100.290 145.526 1.00 46.74  ? 118 VAL B CA  1 
ATOM 4746 C C   . VAL B 2 118 ? 113.141 100.211 147.047 1.00 50.28  ? 118 VAL B C   1 
ATOM 4747 O O   . VAL B 2 118 ? 113.382 101.218 147.726 1.00 54.62  ? 118 VAL B O   1 
ATOM 4748 C CB  . VAL B 2 118 ? 114.528 100.656 144.984 1.00 44.92  ? 118 VAL B CB  1 
ATOM 4749 C CG1 . VAL B 2 118 ? 115.569 99.682  145.494 1.00 53.97  ? 118 VAL B CG1 1 
ATOM 4750 C CG2 . VAL B 2 118 ? 114.512 100.680 143.461 1.00 46.15  ? 118 VAL B CG2 1 
ATOM 4751 N N   . SER B 2 119 ? 112.884 99.018  147.577 1.00 45.04  ? 119 SER B N   1 
ATOM 4752 C CA  . SER B 2 119 ? 112.673 98.831  149.006 1.00 45.71  ? 119 SER B CA  1 
ATOM 4753 C C   . SER B 2 119 ? 113.970 98.454  149.711 1.00 54.19  ? 119 SER B C   1 
ATOM 4754 O O   . SER B 2 119 ? 114.733 97.612  149.231 1.00 63.95  ? 119 SER B O   1 
ATOM 4755 C CB  . SER B 2 119 ? 111.618 97.752  149.252 1.00 50.75  ? 119 SER B CB  1 
ATOM 4756 O OG  . SER B 2 119 ? 110.346 98.166  148.786 1.00 68.92  ? 119 SER B OG  1 
ATOM 4757 N N   . SER B 2 120 ? 114.214 99.091  150.851 1.00 54.07  ? 120 SER B N   1 
ATOM 4758 C CA  . SER B 2 120 ? 115.369 98.793  151.701 1.00 50.29  ? 120 SER B CA  1 
ATOM 4759 C C   . SER B 2 120 ? 115.010 97.804  152.804 1.00 56.32  ? 120 SER B C   1 
ATOM 4760 O O   . SER B 2 120 ? 115.253 98.056  153.984 1.00 65.15  ? 120 SER B O   1 
ATOM 4761 C CB  . SER B 2 120 ? 115.931 100.081 152.290 1.00 53.42  ? 120 SER B CB  1 
ATOM 4762 O OG  . SER B 2 120 ? 116.213 101.028 151.277 1.00 58.72  ? 120 SER B OG  1 
ATOM 4763 N N   . LEU B 2 121 ? 114.431 96.666  152.441 1.00 55.24  ? 121 LEU B N   1 
ATOM 4764 C CA  . LEU B 2 121 ? 114.057 95.658  153.421 1.00 55.38  ? 121 LEU B CA  1 
ATOM 4765 C C   . LEU B 2 121 ? 115.165 94.621  153.578 1.00 59.92  ? 121 LEU B C   1 
ATOM 4766 O O   . LEU B 2 121 ? 115.990 94.412  152.686 1.00 66.76  ? 121 LEU B O   1 
ATOM 4767 C CB  . LEU B 2 121 ? 112.744 94.972  153.034 1.00 55.42  ? 121 LEU B CB  1 
ATOM 4768 C CG  . LEU B 2 121 ? 111.421 95.659  153.396 1.00 42.36  ? 121 LEU B CG  1 
ATOM 4769 C CD1 . LEU B 2 121 ? 111.271 95.757  154.908 1.00 52.16  ? 121 LEU B CD1 1 
ATOM 4770 C CD2 . LEU B 2 121 ? 111.278 97.031  152.754 1.00 48.24  ? 121 LEU B CD2 1 
ATOM 4771 N N   . GLU B 2 122 ? 115.170 93.968  154.736 1.00 59.46  ? 122 GLU B N   1 
ATOM 4772 C CA  . GLU B 2 122 ? 116.188 92.976  155.056 1.00 61.34  ? 122 GLU B CA  1 
ATOM 4773 C C   . GLU B 2 122 ? 115.562 91.612  155.326 1.00 65.01  ? 122 GLU B C   1 
ATOM 4774 O O   . GLU B 2 122 ? 116.152 90.576  155.021 1.00 61.17  ? 122 GLU B O   1 
ATOM 4775 C CB  . GLU B 2 122 ? 117.010 93.429  156.264 1.00 66.53  ? 122 GLU B CB  1 
ATOM 4776 C CG  . GLU B 2 122 ? 117.867 94.657  156.003 1.00 77.57  ? 122 GLU B CG  1 
ATOM 4777 C CD  . GLU B 2 122 ? 118.653 95.090  157.225 1.00 88.72  ? 122 GLU B CD  1 
ATOM 4778 O OE1 . GLU B 2 122 ? 118.436 94.510  158.310 1.00 91.31  ? 122 GLU B OE1 1 
ATOM 4779 O OE2 . GLU B 2 122 ? 119.487 96.011  157.100 1.00 88.25  ? 122 GLU B OE2 1 
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