data_9J3M
# 
_entry.id   9J3M 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9J3M         pdb_00009j3m 10.2210/pdb9j3m/pdb 
WWPDB D_1300049907 ?            ?                   
EMDB  EMD-61119    ?            ?                   
# 
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 ? 
# 
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' 
# 
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        
# 
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'             
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  ? 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9J3M 
_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        'ADP/Pi bound Arabidopsis ATP/ADP translocator AtNTT1' 
_pdbx_database_related.db_id          EMD-61119 
_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            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_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-D7'                           13474.857 1 ? ? ? ? 
3 non-polymer syn "ADENOSINE-5'-DIPHOSPHATE"                 427.201   1 ? ? ? ? 
4 non-polymer syn 'PHOSPHATE ION'                            94.971    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 
;EVQLVESGGGLVQAGGSLRLSCAASGFPVDEAYMTWYRQAPGKEREWVAAIYSSGYTRYADSVKGRFTISRDNSKNTVYL
QMNSLKPEDTAVYYCNVKDYVYNTYLYDYWGQGTQVTVSS
;
;EVQLVESGGGLVQAGGSLRLSCAASGFPVDEAYMTWYRQAPGKEREWVAAIYSSGYTRYADSVKGRFTISRDNSKNTVYL
QMNSLKPEDTAVYYCNVKDYVYNTYLYDYWGQGTQVTVSS
;
B ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3 "ADENOSINE-5'-DIPHOSPHATE" ADP 
4 'PHOSPHATE ION'            PO4 
# 
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  ASP n 
2 31  GLU n 
2 32  ALA n 
2 33  TYR n 
2 34  MET n 
2 35  THR 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  TYR n 
2 53  SER n 
2 54  SER n 
2 55  GLY n 
2 56  TYR n 
2 57  THR n 
2 58  ARG 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 TYR n 
2 101 VAL n 
2 102 TYR n 
2 103 ASN n 
2 104 THR n 
2 105 TYR n 
2 106 LEU 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 
# 
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' 1 120 ?                 ? ?                          ? ? ? ? ? ? '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 
ADP non-polymer         n "ADENOSINE-5'-DIPHOSPHATE" ? 'C10 H15 N5 O10 P2' 427.201 
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 
PO4 non-polymer         . 'PHOSPHATE ION'            ? 'O4 P -3'           94.971  
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 ?   ?   ?   A . n 
A 1 496 GLU 496 581 ?   ?   ?   A . n 
A 1 497 GLU 497 582 ?   ?   ?   A . n 
A 1 498 LEU 498 583 ?   ?   ?   A . n 
A 1 499 GLU 499 584 ?   ?   ?   A . n 
A 1 500 LYS 500 585 ?   ?   ?   A . n 
A 1 501 GLU 501 586 ?   ?   ?   A . n 
A 1 502 MET 502 587 ?   ?   ?   A . n 
A 1 503 GLU 503 588 ?   ?   ?   A . n 
A 1 504 ARG 504 589 ?   ?   ?   A . n 
A 1 505 ALA 505 590 ?   ?   ?   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  ASP 30  30  30  ASP ASP B . n 
B 2 31  GLU 31  31  31  GLU GLU B . n 
B 2 32  ALA 32  32  32  ALA ALA B . n 
B 2 33  TYR 33  33  33  TYR TYR B . n 
B 2 34  MET 34  34  34  MET MET B . n 
B 2 35  THR 35  35  35  THR THR 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  TYR 52  52  52  TYR TYR B . n 
B 2 53  SER 53  53  53  SER SER B . n 
B 2 54  SER 54  54  54  SER SER 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  ARG 58  58  58  ARG ARG 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 TYR 100 100 100 TYR TYR B . n 
B 2 101 VAL 101 101 101 VAL VAL B . n 
B 2 102 TYR 102 102 102 TYR TYR B . n 
B 2 103 ASN 103 103 103 ASN ASN B . n 
B 2 104 THR 104 104 104 THR THR B . n 
B 2 105 TYR 105 105 105 TYR TYR B . n 
B 2 106 LEU 106 106 106 LEU LEU 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 
# 
loop_
_pdbx_entity_instance_feature.ordinal 
_pdbx_entity_instance_feature.comp_id 
_pdbx_entity_instance_feature.asym_id 
_pdbx_entity_instance_feature.seq_num 
_pdbx_entity_instance_feature.auth_comp_id 
_pdbx_entity_instance_feature.auth_asym_id 
_pdbx_entity_instance_feature.auth_seq_num 
_pdbx_entity_instance_feature.feature_type 
_pdbx_entity_instance_feature.details 
1 ADP ? ? ADP ? ? 'SUBJECT OF INVESTIGATION' ? 
2 PO4 ? ? PO4 ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 3 ADP 1 701 701 ADP ADP A . 
D 4 PO4 1 702 801 PO4 PO4 A . 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9J3M 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     1.00 
_cell.length_a_esd                 ? 
_cell.length_b                     1.00 
_cell.length_b_esd                 ? 
_cell.length_c                     1.00 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        ? 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9J3M 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                1 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9J3M 
_exptl.crystals_number            ? 
_exptl.details                    ? 
_exptl.method                     'ELECTRON MICROSCOPY' 
_exptl.method_details             ? 
# 
_refine.pdbx_refine_id                           'ELECTRON MICROSCOPY' 
_refine.entry_id                                 9J3M 
_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 ? 4824 ? f_bond_d           ? ? 
'ELECTRON MICROSCOPY' ? 0.665 ? 6561 ? f_angle_d          ? ? 
'ELECTRON MICROSCOPY' ? 5.939 ? 647  ? f_dihedral_angle_d ? ? 
'ELECTRON MICROSCOPY' ? 0.041 ? 747  ? f_chiral_restr     ? ? 
'ELECTRON MICROSCOPY' ? 0.006 ? 795  ? f_plane_restr      ? ? 
# 
_struct.entry_id                     9J3M 
_struct.title                        'ADP/Pi bound 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        9J3M 
_struct_keywords.text            '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 ? 
C N N 3 ? 
D N N 4 ? 
# 
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 9J3M       9J3M   ? 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 9J3M A 3 ? 539 ? Q39002 88 ? 624 ? 88 624 
2 2 9J3M B 1 ? 120 ? 9J3M   1  ? 120 ? 1  120 
# 
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 9J3M MET A 1   ? UNP Q39002 ? ? 'initiating methionine' 86  1  
1 9J3M ALA A 2   ? UNP Q39002 ? ? 'expression tag'        87  2  
1 9J3M VAL A 540 ? UNP Q39002 ? ? 'expression tag'        625 3  
1 9J3M ASP A 541 ? UNP Q39002 ? ? 'expression tag'        626 4  
1 9J3M GLU A 542 ? UNP Q39002 ? ? 'expression tag'        627 5  
1 9J3M LEU A 543 ? UNP Q39002 ? ? 'expression tag'        628 6  
1 9J3M THR A 544 ? UNP Q39002 ? ? 'expression tag'        629 7  
1 9J3M SER A 545 ? UNP Q39002 ? ? 'expression tag'        630 8  
1 9J3M ARG A 546 ? UNP Q39002 ? ? 'expression tag'        631 9  
1 9J3M GLY A 547 ? UNP Q39002 ? ? 'expression tag'        632 10 
1 9J3M ARG A 548 ? UNP Q39002 ? ? 'expression tag'        633 11 
1 9J3M GLY A 549 ? UNP Q39002 ? ? 'expression tag'        634 12 
1 9J3M SER A 550 ? UNP Q39002 ? ? 'expression tag'        635 13 
1 9J3M GLY A 551 ? UNP Q39002 ? ? 'expression tag'        636 14 
1 9J3M GLY A 552 ? UNP Q39002 ? ? 'expression tag'        637 15 
1 9J3M LEU A 553 ? UNP Q39002 ? ? 'expression tag'        638 16 
1 9J3M ASN A 554 ? UNP Q39002 ? ? 'expression tag'        639 17 
1 9J3M ASP A 555 ? UNP Q39002 ? ? 'expression tag'        640 18 
1 9J3M ILE A 556 ? UNP Q39002 ? ? 'expression tag'        641 19 
1 9J3M PHE A 557 ? UNP Q39002 ? ? 'expression tag'        642 20 
1 9J3M GLU A 558 ? UNP Q39002 ? ? 'expression tag'        643 21 
1 9J3M ALA A 559 ? UNP Q39002 ? ? 'expression tag'        644 22 
1 9J3M GLN A 560 ? UNP Q39002 ? ? 'expression tag'        645 23 
1 9J3M LYS A 561 ? UNP Q39002 ? ? 'expression tag'        646 24 
1 9J3M ILE A 562 ? UNP Q39002 ? ? 'expression tag'        647 25 
1 9J3M GLU A 563 ? UNP Q39002 ? ? 'expression tag'        648 26 
1 9J3M TRP A 564 ? UNP Q39002 ? ? 'expression tag'        649 27 
1 9J3M HIS A 565 ? UNP Q39002 ? ? 'expression tag'        650 28 
1 9J3M GLU A 566 ? UNP Q39002 ? ? 'expression tag'        651 29 
1 9J3M GLY A 567 ? UNP Q39002 ? ? 'expression tag'        652 30 
1 9J3M SER A 568 ? UNP Q39002 ? ? 'expression tag'        653 31 
1 9J3M GLY A 569 ? UNP Q39002 ? ? 'expression tag'        654 32 
1 9J3M LEU A 570 ? UNP Q39002 ? ? 'expression tag'        655 33 
1 9J3M GLU A 571 ? UNP Q39002 ? ? 'expression tag'        656 34 
1 9J3M VAL A 572 ? UNP Q39002 ? ? 'expression tag'        657 35 
1 9J3M LEU A 573 ? UNP Q39002 ? ? 'expression tag'        658 36 
1 9J3M PHE A 574 ? UNP Q39002 ? ? 'expression tag'        659 37 
1 9J3M GLN A 575 ? UNP Q39002 ? ? 'expression tag'        660 38 
1 9J3M GLY A 576 ? UNP Q39002 ? ? 'expression tag'        661 39 
1 9J3M PRO A 577 ? UNP Q39002 ? ? 'expression tag'        662 40 
1 9J3M ASP A 578 ? UNP Q39002 ? ? 'expression tag'        663 41 
1 9J3M TYR A 579 ? UNP Q39002 ? ? 'expression tag'        664 42 
1 9J3M LYS A 580 ? UNP Q39002 ? ? 'expression tag'        665 43 
1 9J3M ASP A 581 ? UNP Q39002 ? ? 'expression tag'        666 44 
1 9J3M ASP A 582 ? UNP Q39002 ? ? 'expression tag'        667 45 
1 9J3M ASP A 583 ? UNP Q39002 ? ? 'expression tag'        668 46 
1 9J3M ASP A 584 ? UNP Q39002 ? ? 'expression tag'        669 47 
1 9J3M LYS A 585 ? UNP Q39002 ? ? 'expression tag'        670 48 
1 9J3M TRP A 586 ? UNP Q39002 ? ? 'expression tag'        671 49 
1 9J3M SER A 587 ? UNP Q39002 ? ? 'expression tag'        672 50 
1 9J3M HIS A 588 ? UNP Q39002 ? ? 'expression tag'        673 51 
1 9J3M PRO A 589 ? UNP Q39002 ? ? 'expression tag'        674 52 
1 9J3M GLN A 590 ? UNP Q39002 ? ? 'expression tag'        675 53 
1 9J3M PHE A 591 ? UNP Q39002 ? ? 'expression tag'        676 54 
1 9J3M GLU A 592 ? UNP Q39002 ? ? 'expression tag'        677 55 
1 9J3M LYS A 593 ? UNP Q39002 ? ? 'expression tag'        678 56 
1 9J3M GLY A 594 ? UNP Q39002 ? ? 'expression tag'        679 57 
1 9J3M GLY A 595 ? UNP Q39002 ? ? 'expression tag'        680 58 
1 9J3M GLY A 596 ? UNP Q39002 ? ? 'expression tag'        681 59 
1 9J3M GLY A 597 ? UNP Q39002 ? ? 'expression tag'        682 60 
1 9J3M SER A 598 ? UNP Q39002 ? ? 'expression tag'        683 61 
1 9J3M GLY A 599 ? UNP Q39002 ? ? 'expression tag'        684 62 
1 9J3M GLY A 600 ? UNP Q39002 ? ? 'expression tag'        685 63 
1 9J3M SER A 601 ? UNP Q39002 ? ? 'expression tag'        686 64 
1 9J3M ALA A 602 ? UNP Q39002 ? ? 'expression tag'        687 65 
1 9J3M TRP A 603 ? UNP Q39002 ? ? 'expression tag'        688 66 
1 9J3M SER A 604 ? UNP Q39002 ? ? 'expression tag'        689 67 
1 9J3M HIS A 605 ? UNP Q39002 ? ? 'expression tag'        690 68 
1 9J3M PRO A 606 ? UNP Q39002 ? ? 'expression tag'        691 69 
1 9J3M GLN A 607 ? UNP Q39002 ? ? 'expression tag'        692 70 
1 9J3M PHE A 608 ? UNP Q39002 ? ? 'expression tag'        693 71 
1 9J3M GLU A 609 ? UNP Q39002 ? ? 'expression tag'        694 72 
1 9J3M 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,C,D 
# 
_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 LYS A 19  ? VAL A 23  ? LYS A 104 VAL A 108 5 ? 5  
HELX_P HELX_P2  AA2 GLU A 24  ? THR A 58  ? GLU A 109 THR A 143 1 ? 35 
HELX_P HELX_P3  AA3 GLU A 65  ? VAL A 74  ? GLU A 150 VAL A 159 1 ? 10 
HELX_P HELX_P4  AA4 VAL A 74  ? ASN A 91  ? VAL A 159 ASN A 176 1 ? 18 
HELX_P HELX_P5  AA5 SER A 94  ? VAL A 116 ? SER A 179 VAL A 201 1 ? 23 
HELX_P HELX_P6  AA6 LEU A 120 ? HIS A 125 ? LEU A 205 HIS A 210 1 ? 6  
HELX_P HELX_P7  AA7 PRO A 126 ? GLY A 138 ? PRO A 211 GLY A 223 1 ? 13 
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 VAL A 170 ? THR A 180 ? VAL A 255 THR A 265 1 ? 11 
HELX_P HELX_P11 AB2 THR A 181 ? PHE A 188 ? THR A 266 PHE A 273 1 ? 8  
HELX_P HELX_P12 AB3 PHE A 188 ? ASN A 212 ? PHE A 273 ASN A 297 1 ? 25 
HELX_P HELX_P13 AB4 ASP A 222 ? VAL A 253 ? ASP A 307 VAL A 338 1 ? 32 
HELX_P HELX_P14 AB5 MET A 271 ? SER A 280 ? MET A 356 SER A 365 1 ? 10 
HELX_P HELX_P15 AB6 TYR A 282 ? PHE A 312 ? TYR A 367 PHE A 397 1 ? 31 
HELX_P HELX_P16 AB7 SER A 314 ? GLY A 348 ? SER A 399 GLY A 433 1 ? 35 
HELX_P HELX_P17 AB8 GLY A 348 ? LEU A 372 ? GLY A 433 LEU A 457 1 ? 25 
HELX_P HELX_P18 AB9 PHE A 377 ? LEU A 384 ? PHE A 462 LEU A 469 1 ? 8  
HELX_P HELX_P19 AC1 THR A 387 ? MET A 417 ? THR A 472 MET A 502 1 ? 31 
HELX_P HELX_P20 AC2 ASP A 425 ? VAL A 437 ? ASP A 510 VAL A 522 1 ? 13 
HELX_P HELX_P21 AC3 CYS A 438 ? GLY A 458 ? CYS A 523 GLY A 543 1 ? 21 
HELX_P HELX_P22 AC4 LEU A 460 ? ASN A 462 ? LEU A 545 ASN A 547 5 ? 3  
HELX_P HELX_P23 AC5 SER A 463 ? ASN A 490 ? SER A 548 ASN A 575 1 ? 28 
HELX_P HELX_P24 AC6 PRO B 28  ? ALA B 32  ? PRO B 28  ALA B 32  5 ? 5  
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               2.028 
_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 ? 4 ? 
AA2 ? 6 ? 
AA3 ? 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 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA3 1 2 ? parallel      
AA3 2 3 ? anti-parallel 
AA3 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 GLN B 3   ? SER B 7   ? GLN B 3   SER B 7   
AA1 2 SER B 17  ? SER B 25  ? SER B 17  SER B 25  
AA1 3 THR B 77  ? ASN B 83  ? THR B 77  ASN B 83  
AA1 4 PHE B 67  ? ASP B 72  ? PHE B 67  ASP B 72  
AA2 1 LEU B 11  ? VAL B 12  ? LEU B 11  VAL B 12  
AA2 2 THR B 114 ? VAL B 118 ? THR B 114 VAL B 118 
AA2 3 ALA B 91  ? TYR B 100 ? ALA B 91  TYR B 100 
AA2 4 TYR B 33  ? GLN B 39  ? TYR B 33  GLN B 39  
AA2 5 GLU B 46  ? ILE B 51  ? GLU B 46  ILE B 51  
AA2 6 THR B 57  ? TYR B 59  ? THR B 57  TYR B 59  
AA3 1 LEU B 11  ? VAL B 12  ? LEU B 11  VAL B 12  
AA3 2 THR B 114 ? VAL B 118 ? THR B 114 VAL B 118 
AA3 3 ALA B 91  ? TYR B 100 ? ALA B 91  TYR B 100 
AA3 4 TYR B 105 ? TRP B 110 ? TYR B 105 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 SER B 7   ? N SER B 7   O SER B 21  ? O SER B 21  
AA1 2 3 N LEU B 18  ? N LEU B 18  O MET B 82  ? O MET B 82  
AA1 3 4 O THR B 77  ? O THR B 77  N ASP B 72  ? N ASP B 72  
AA2 1 2 N VAL B 12  ? N VAL B 12  O THR B 117 ? O THR B 117 
AA2 2 3 O THR B 114 ? O THR B 114 N TYR B 93  ? N TYR B 93  
AA2 3 4 O TYR B 94  ? O TYR B 94  N TYR B 37  ? N TYR B 37  
AA2 4 5 N ARG B 38  ? N ARG B 38  O GLU B 46  ? O GLU B 46  
AA2 5 6 N ALA B 50  ? N ALA B 50  O ARG B 58  ? O ARG B 58  
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 N VAL B 97  ? N VAL B 97  O TYR B 109 ? O TYR B 109 
# 
_pdbx_entry_details.entry_id                   9J3M 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 VAL A 201 ? ? -121.39 -56.80 
2 1 LYS A 300 ? ? 66.93   -7.26  
3 1 GLN A 426 ? ? -65.21  0.80   
4 1 PHE A 462 ? ? -91.64  46.76  
5 1 PRO A 506 ? ? -92.37  52.51  
6 1 VAL B 48  ? ? -107.64 -60.32 
7 1 TYR B 102 ? ? -124.68 -53.28 
# 
_em_3d_fitting.id                1 
_em_3d_fitting.entry_id          9J3M 
_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                    9J3M 
_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                  2.77 
_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               649675 
_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                 'ADP/Pi bound 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                        9J3M 
_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              9J3M 
_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                9J3M 
_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 GLU 580 ? A GLU 495 
17  1 Y 1 A GLU 581 ? A GLU 496 
18  1 Y 1 A GLU 582 ? A GLU 497 
19  1 Y 1 A LEU 583 ? A LEU 498 
20  1 Y 1 A GLU 584 ? A GLU 499 
21  1 Y 1 A LYS 585 ? A LYS 500 
22  1 Y 1 A GLU 586 ? A GLU 501 
23  1 Y 1 A MET 587 ? A MET 502 
24  1 Y 1 A GLU 588 ? A GLU 503 
25  1 Y 1 A ARG 589 ? A ARG 504 
26  1 Y 1 A ALA 590 ? A ALA 505 
27  1 Y 1 A SER 591 ? A SER 506 
28  1 Y 1 A SER 592 ? A SER 507 
29  1 Y 1 A VAL 593 ? A VAL 508 
30  1 Y 1 A LYS 594 ? A LYS 509 
31  1 Y 1 A ILE 595 ? A ILE 510 
32  1 Y 1 A PRO 596 ? A PRO 511 
33  1 Y 1 A VAL 597 ? A VAL 512 
34  1 Y 1 A VAL 598 ? A VAL 513 
35  1 Y 1 A SER 599 ? A SER 514 
36  1 Y 1 A GLN 600 ? A GLN 515 
37  1 Y 1 A ASP 601 ? A ASP 516 
38  1 Y 1 A GLU 602 ? A GLU 517 
39  1 Y 1 A SER 603 ? A SER 518 
40  1 Y 1 A GLY 604 ? A GLY 519 
41  1 Y 1 A ASN 605 ? A ASN 520 
42  1 Y 1 A GLY 606 ? A GLY 521 
43  1 Y 1 A SER 607 ? A SER 522 
44  1 Y 1 A LEU 608 ? A LEU 523 
45  1 Y 1 A GLY 609 ? A GLY 524 
46  1 Y 1 A GLU 610 ? A GLU 525 
47  1 Y 1 A SER 611 ? A SER 526 
48  1 Y 1 A PRO 612 ? A PRO 527 
49  1 Y 1 A SER 613 ? A SER 528 
50  1 Y 1 A SER 614 ? A SER 529 
51  1 Y 1 A SER 615 ? A SER 530 
52  1 Y 1 A PRO 616 ? A PRO 531 
53  1 Y 1 A GLU 617 ? A GLU 532 
54  1 Y 1 A LYS 618 ? A LYS 533 
55  1 Y 1 A SER 619 ? A SER 534 
56  1 Y 1 A ALA 620 ? A ALA 535 
57  1 Y 1 A PRO 621 ? A PRO 536 
58  1 Y 1 A THR 622 ? A THR 537 
59  1 Y 1 A ASN 623 ? A ASN 538 
60  1 Y 1 A LEU 624 ? A LEU 539 
61  1 Y 1 A VAL 625 ? A VAL 540 
62  1 Y 1 A ASP 626 ? A ASP 541 
63  1 Y 1 A GLU 627 ? A GLU 542 
64  1 Y 1 A LEU 628 ? A LEU 543 
65  1 Y 1 A THR 629 ? A THR 544 
66  1 Y 1 A SER 630 ? A SER 545 
67  1 Y 1 A ARG 631 ? A ARG 546 
68  1 Y 1 A GLY 632 ? A GLY 547 
69  1 Y 1 A ARG 633 ? A ARG 548 
70  1 Y 1 A GLY 634 ? A GLY 549 
71  1 Y 1 A SER 635 ? A SER 550 
72  1 Y 1 A GLY 636 ? A GLY 551 
73  1 Y 1 A GLY 637 ? A GLY 552 
74  1 Y 1 A LEU 638 ? A LEU 553 
75  1 Y 1 A ASN 639 ? A ASN 554 
76  1 Y 1 A ASP 640 ? A ASP 555 
77  1 Y 1 A ILE 641 ? A ILE 556 
78  1 Y 1 A PHE 642 ? A PHE 557 
79  1 Y 1 A GLU 643 ? A GLU 558 
80  1 Y 1 A ALA 644 ? A ALA 559 
81  1 Y 1 A GLN 645 ? A GLN 560 
82  1 Y 1 A LYS 646 ? A LYS 561 
83  1 Y 1 A ILE 647 ? A ILE 562 
84  1 Y 1 A GLU 648 ? A GLU 563 
85  1 Y 1 A TRP 649 ? A TRP 564 
86  1 Y 1 A HIS 650 ? A HIS 565 
87  1 Y 1 A GLU 651 ? A GLU 566 
88  1 Y 1 A GLY 652 ? A GLY 567 
89  1 Y 1 A SER 653 ? A SER 568 
90  1 Y 1 A GLY 654 ? A GLY 569 
91  1 Y 1 A LEU 655 ? A LEU 570 
92  1 Y 1 A GLU 656 ? A GLU 571 
93  1 Y 1 A VAL 657 ? A VAL 572 
94  1 Y 1 A LEU 658 ? A LEU 573 
95  1 Y 1 A PHE 659 ? A PHE 574 
96  1 Y 1 A GLN 660 ? A GLN 575 
97  1 Y 1 A GLY 661 ? A GLY 576 
98  1 Y 1 A PRO 662 ? A PRO 577 
99  1 Y 1 A ASP 663 ? A ASP 578 
100 1 Y 1 A TYR 664 ? A TYR 579 
101 1 Y 1 A LYS 665 ? A LYS 580 
102 1 Y 1 A ASP 666 ? A ASP 581 
103 1 Y 1 A ASP 667 ? A ASP 582 
104 1 Y 1 A ASP 668 ? A ASP 583 
105 1 Y 1 A ASP 669 ? A ASP 584 
106 1 Y 1 A LYS 670 ? A LYS 585 
107 1 Y 1 A TRP 671 ? A TRP 586 
108 1 Y 1 A SER 672 ? A SER 587 
109 1 Y 1 A HIS 673 ? A HIS 588 
110 1 Y 1 A PRO 674 ? A PRO 589 
111 1 Y 1 A GLN 675 ? A GLN 590 
112 1 Y 1 A PHE 676 ? A PHE 591 
113 1 Y 1 A GLU 677 ? A GLU 592 
114 1 Y 1 A LYS 678 ? A LYS 593 
115 1 Y 1 A GLY 679 ? A GLY 594 
116 1 Y 1 A GLY 680 ? A GLY 595 
117 1 Y 1 A GLY 681 ? A GLY 596 
118 1 Y 1 A GLY 682 ? A GLY 597 
119 1 Y 1 A SER 683 ? A SER 598 
120 1 Y 1 A GLY 684 ? A GLY 599 
121 1 Y 1 A GLY 685 ? A GLY 600 
122 1 Y 1 A SER 686 ? A SER 601 
123 1 Y 1 A ALA 687 ? A ALA 602 
124 1 Y 1 A TRP 688 ? A TRP 603 
125 1 Y 1 A SER 689 ? A SER 604 
126 1 Y 1 A HIS 690 ? A HIS 605 
127 1 Y 1 A PRO 691 ? A PRO 606 
128 1 Y 1 A GLN 692 ? A GLN 607 
129 1 Y 1 A PHE 693 ? A PHE 608 
130 1 Y 1 A GLU 694 ? A GLU 609 
131 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 
ADP PB     P N N 1   
ADP O1B    O N N 2   
ADP O2B    O N N 3   
ADP O3B    O N N 4   
ADP PA     P N S 5   
ADP O1A    O N N 6   
ADP O2A    O N N 7   
ADP O3A    O N N 8   
ADP "O5'"  O N N 9   
ADP "C5'"  C N N 10  
ADP "C4'"  C N R 11  
ADP "O4'"  O N N 12  
ADP "C3'"  C N S 13  
ADP "O3'"  O N N 14  
ADP "C2'"  C N R 15  
ADP "O2'"  O N N 16  
ADP "C1'"  C N R 17  
ADP N9     N Y N 18  
ADP C8     C Y N 19  
ADP N7     N Y N 20  
ADP C5     C Y N 21  
ADP C6     C Y N 22  
ADP N6     N N N 23  
ADP N1     N Y N 24  
ADP C2     C Y N 25  
ADP N3     N Y N 26  
ADP C4     C Y N 27  
ADP HOB2   H N N 28  
ADP HOB3   H N N 29  
ADP HOA2   H N N 30  
ADP "H5'1" H N N 31  
ADP "H5'2" H N N 32  
ADP "H4'"  H N N 33  
ADP "H3'"  H N N 34  
ADP "HO3'" H N N 35  
ADP "H2'"  H N N 36  
ADP "HO2'" H N N 37  
ADP "H1'"  H N N 38  
ADP H8     H N N 39  
ADP HN61   H N N 40  
ADP HN62   H N N 41  
ADP H2     H N N 42  
ALA N      N N N 43  
ALA CA     C N S 44  
ALA C      C N N 45  
ALA O      O N N 46  
ALA CB     C N N 47  
ALA OXT    O N N 48  
ALA H      H N N 49  
ALA H2     H N N 50  
ALA HA     H N N 51  
ALA HB1    H N N 52  
ALA HB2    H N N 53  
ALA HB3    H N N 54  
ALA HXT    H N N 55  
ARG N      N N N 56  
ARG CA     C N S 57  
ARG C      C N N 58  
ARG O      O N N 59  
ARG CB     C N N 60  
ARG CG     C N N 61  
ARG CD     C N N 62  
ARG NE     N N N 63  
ARG CZ     C N N 64  
ARG NH1    N N N 65  
ARG NH2    N N N 66  
ARG OXT    O N N 67  
ARG H      H N N 68  
ARG H2     H N N 69  
ARG HA     H N N 70  
ARG HB2    H N N 71  
ARG HB3    H N N 72  
ARG HG2    H N N 73  
ARG HG3    H N N 74  
ARG HD2    H N N 75  
ARG HD3    H N N 76  
ARG HE     H N N 77  
ARG HH11   H N N 78  
ARG HH12   H N N 79  
ARG HH21   H N N 80  
ARG HH22   H N N 81  
ARG HXT    H N N 82  
ASN N      N N N 83  
ASN CA     C N S 84  
ASN C      C N N 85  
ASN O      O N N 86  
ASN CB     C N N 87  
ASN CG     C N N 88  
ASN OD1    O N N 89  
ASN ND2    N N N 90  
ASN OXT    O N N 91  
ASN H      H N N 92  
ASN H2     H N N 93  
ASN HA     H N N 94  
ASN HB2    H N N 95  
ASN HB3    H N N 96  
ASN HD21   H N N 97  
ASN HD22   H N N 98  
ASN HXT    H N N 99  
ASP N      N N N 100 
ASP CA     C N S 101 
ASP C      C N N 102 
ASP O      O N N 103 
ASP CB     C N N 104 
ASP CG     C N N 105 
ASP OD1    O N N 106 
ASP OD2    O N N 107 
ASP OXT    O N N 108 
ASP H      H N N 109 
ASP H2     H N N 110 
ASP HA     H N N 111 
ASP HB2    H N N 112 
ASP HB3    H N N 113 
ASP HD2    H N N 114 
ASP HXT    H N N 115 
CYS N      N N N 116 
CYS CA     C N R 117 
CYS C      C N N 118 
CYS O      O N N 119 
CYS CB     C N N 120 
CYS SG     S N N 121 
CYS OXT    O N N 122 
CYS H      H N N 123 
CYS H2     H N N 124 
CYS HA     H N N 125 
CYS HB2    H N N 126 
CYS HB3    H N N 127 
CYS HG     H N N 128 
CYS HXT    H N N 129 
GLN N      N N N 130 
GLN CA     C N S 131 
GLN C      C N N 132 
GLN O      O N N 133 
GLN CB     C N N 134 
GLN CG     C N N 135 
GLN CD     C N N 136 
GLN OE1    O N N 137 
GLN NE2    N N N 138 
GLN OXT    O N N 139 
GLN H      H N N 140 
GLN H2     H N N 141 
GLN HA     H N N 142 
GLN HB2    H N N 143 
GLN HB3    H N N 144 
GLN HG2    H N N 145 
GLN HG3    H N N 146 
GLN HE21   H N N 147 
GLN HE22   H N N 148 
GLN HXT    H N N 149 
GLU N      N N N 150 
GLU CA     C N S 151 
GLU C      C N N 152 
GLU O      O N N 153 
GLU CB     C N N 154 
GLU CG     C N N 155 
GLU CD     C N N 156 
GLU OE1    O N N 157 
GLU OE2    O N N 158 
GLU OXT    O N N 159 
GLU H      H N N 160 
GLU H2     H N N 161 
GLU HA     H N N 162 
GLU HB2    H N N 163 
GLU HB3    H N N 164 
GLU HG2    H N N 165 
GLU HG3    H N N 166 
GLU HE2    H N N 167 
GLU HXT    H N N 168 
GLY N      N N N 169 
GLY CA     C N N 170 
GLY C      C N N 171 
GLY O      O N N 172 
GLY OXT    O N N 173 
GLY H      H N N 174 
GLY H2     H N N 175 
GLY HA2    H N N 176 
GLY HA3    H N N 177 
GLY HXT    H N N 178 
HIS N      N N N 179 
HIS CA     C N S 180 
HIS C      C N N 181 
HIS O      O N N 182 
HIS CB     C N N 183 
HIS CG     C Y N 184 
HIS ND1    N Y N 185 
HIS CD2    C Y N 186 
HIS CE1    C Y N 187 
HIS NE2    N Y N 188 
HIS OXT    O N N 189 
HIS H      H N N 190 
HIS H2     H N N 191 
HIS HA     H N N 192 
HIS HB2    H N N 193 
HIS HB3    H N N 194 
HIS HD1    H N N 195 
HIS HD2    H N N 196 
HIS HE1    H N N 197 
HIS HE2    H N N 198 
HIS HXT    H N N 199 
ILE N      N N N 200 
ILE CA     C N S 201 
ILE C      C N N 202 
ILE O      O N N 203 
ILE CB     C N S 204 
ILE CG1    C N N 205 
ILE CG2    C N N 206 
ILE CD1    C N N 207 
ILE OXT    O N N 208 
ILE H      H N N 209 
ILE H2     H N N 210 
ILE HA     H N N 211 
ILE HB     H N N 212 
ILE HG12   H N N 213 
ILE HG13   H N N 214 
ILE HG21   H N N 215 
ILE HG22   H N N 216 
ILE HG23   H N N 217 
ILE HD11   H N N 218 
ILE HD12   H N N 219 
ILE HD13   H N N 220 
ILE HXT    H N N 221 
LEU N      N N N 222 
LEU CA     C N S 223 
LEU C      C N N 224 
LEU O      O N N 225 
LEU CB     C N N 226 
LEU CG     C N N 227 
LEU CD1    C N N 228 
LEU CD2    C N N 229 
LEU OXT    O N N 230 
LEU H      H N N 231 
LEU H2     H N N 232 
LEU HA     H N N 233 
LEU HB2    H N N 234 
LEU HB3    H N N 235 
LEU HG     H N N 236 
LEU HD11   H N N 237 
LEU HD12   H N N 238 
LEU HD13   H N N 239 
LEU HD21   H N N 240 
LEU HD22   H N N 241 
LEU HD23   H N N 242 
LEU HXT    H N N 243 
LYS N      N N N 244 
LYS CA     C N S 245 
LYS C      C N N 246 
LYS O      O N N 247 
LYS CB     C N N 248 
LYS CG     C N N 249 
LYS CD     C N N 250 
LYS CE     C N N 251 
LYS NZ     N N N 252 
LYS OXT    O N N 253 
LYS H      H N N 254 
LYS H2     H N N 255 
LYS HA     H N N 256 
LYS HB2    H N N 257 
LYS HB3    H N N 258 
LYS HG2    H N N 259 
LYS HG3    H N N 260 
LYS HD2    H N N 261 
LYS HD3    H N N 262 
LYS HE2    H N N 263 
LYS HE3    H N N 264 
LYS HZ1    H N N 265 
LYS HZ2    H N N 266 
LYS HZ3    H N N 267 
LYS HXT    H N N 268 
MET N      N N N 269 
MET CA     C N S 270 
MET C      C N N 271 
MET O      O N N 272 
MET CB     C N N 273 
MET CG     C N N 274 
MET SD     S N N 275 
MET CE     C N N 276 
MET OXT    O N N 277 
MET H      H N N 278 
MET H2     H N N 279 
MET HA     H N N 280 
MET HB2    H N N 281 
MET HB3    H N N 282 
MET HG2    H N N 283 
MET HG3    H N N 284 
MET HE1    H N N 285 
MET HE2    H N N 286 
MET HE3    H N N 287 
MET HXT    H N N 288 
PHE N      N N N 289 
PHE CA     C N S 290 
PHE C      C N N 291 
PHE O      O N N 292 
PHE CB     C N N 293 
PHE CG     C Y N 294 
PHE CD1    C Y N 295 
PHE CD2    C Y N 296 
PHE CE1    C Y N 297 
PHE CE2    C Y N 298 
PHE CZ     C Y N 299 
PHE OXT    O N N 300 
PHE H      H N N 301 
PHE H2     H N N 302 
PHE HA     H N N 303 
PHE HB2    H N N 304 
PHE HB3    H N N 305 
PHE HD1    H N N 306 
PHE HD2    H N N 307 
PHE HE1    H N N 308 
PHE HE2    H N N 309 
PHE HZ     H N N 310 
PHE HXT    H N N 311 
PO4 P      P N N 312 
PO4 O1     O N N 313 
PO4 O2     O N N 314 
PO4 O3     O N N 315 
PO4 O4     O N N 316 
PRO N      N N N 317 
PRO CA     C N S 318 
PRO C      C N N 319 
PRO O      O N N 320 
PRO CB     C N N 321 
PRO CG     C N N 322 
PRO CD     C N N 323 
PRO OXT    O N N 324 
PRO H      H N N 325 
PRO HA     H N N 326 
PRO HB2    H N N 327 
PRO HB3    H N N 328 
PRO HG2    H N N 329 
PRO HG3    H N N 330 
PRO HD2    H N N 331 
PRO HD3    H N N 332 
PRO HXT    H N N 333 
SER N      N N N 334 
SER CA     C N S 335 
SER C      C N N 336 
SER O      O N N 337 
SER CB     C N N 338 
SER OG     O N N 339 
SER OXT    O N N 340 
SER H      H N N 341 
SER H2     H N N 342 
SER HA     H N N 343 
SER HB2    H N N 344 
SER HB3    H N N 345 
SER HG     H N N 346 
SER HXT    H N N 347 
THR N      N N N 348 
THR CA     C N S 349 
THR C      C N N 350 
THR O      O N N 351 
THR CB     C N R 352 
THR OG1    O N N 353 
THR CG2    C N N 354 
THR OXT    O N N 355 
THR H      H N N 356 
THR H2     H N N 357 
THR HA     H N N 358 
THR HB     H N N 359 
THR HG1    H N N 360 
THR HG21   H N N 361 
THR HG22   H N N 362 
THR HG23   H N N 363 
THR HXT    H N N 364 
TRP N      N N N 365 
TRP CA     C N S 366 
TRP C      C N N 367 
TRP O      O N N 368 
TRP CB     C N N 369 
TRP CG     C Y N 370 
TRP CD1    C Y N 371 
TRP CD2    C Y N 372 
TRP NE1    N Y N 373 
TRP CE2    C Y N 374 
TRP CE3    C Y N 375 
TRP CZ2    C Y N 376 
TRP CZ3    C Y N 377 
TRP CH2    C Y N 378 
TRP OXT    O N N 379 
TRP H      H N N 380 
TRP H2     H N N 381 
TRP HA     H N N 382 
TRP HB2    H N N 383 
TRP HB3    H N N 384 
TRP HD1    H N N 385 
TRP HE1    H N N 386 
TRP HE3    H N N 387 
TRP HZ2    H N N 388 
TRP HZ3    H N N 389 
TRP HH2    H N N 390 
TRP HXT    H N N 391 
TYR N      N N N 392 
TYR CA     C N S 393 
TYR C      C N N 394 
TYR O      O N N 395 
TYR CB     C N N 396 
TYR CG     C Y N 397 
TYR CD1    C Y N 398 
TYR CD2    C Y N 399 
TYR CE1    C Y N 400 
TYR CE2    C Y N 401 
TYR CZ     C Y N 402 
TYR OH     O N N 403 
TYR OXT    O N N 404 
TYR H      H N N 405 
TYR H2     H N N 406 
TYR HA     H N N 407 
TYR HB2    H N N 408 
TYR HB3    H N N 409 
TYR HD1    H N N 410 
TYR HD2    H N N 411 
TYR HE1    H N N 412 
TYR HE2    H N N 413 
TYR HH     H N N 414 
TYR HXT    H N N 415 
VAL N      N N N 416 
VAL CA     C N S 417 
VAL C      C N N 418 
VAL O      O N N 419 
VAL CB     C N N 420 
VAL CG1    C N N 421 
VAL CG2    C N N 422 
VAL OXT    O N N 423 
VAL H      H N N 424 
VAL H2     H N N 425 
VAL HA     H N N 426 
VAL HB     H N N 427 
VAL HG11   H N N 428 
VAL HG12   H N N 429 
VAL HG13   H N N 430 
VAL HG21   H N N 431 
VAL HG22   H N N 432 
VAL HG23   H N N 433 
VAL HXT    H N N 434 
# 
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 
ADP PB    O1B    doub N N 1   
ADP PB    O2B    sing N N 2   
ADP PB    O3B    sing N N 3   
ADP PB    O3A    sing N N 4   
ADP O2B   HOB2   sing N N 5   
ADP O3B   HOB3   sing N N 6   
ADP PA    O1A    doub N N 7   
ADP PA    O2A    sing N N 8   
ADP PA    O3A    sing N N 9   
ADP PA    "O5'"  sing N N 10  
ADP O2A   HOA2   sing N N 11  
ADP "O5'" "C5'"  sing N N 12  
ADP "C5'" "C4'"  sing N N 13  
ADP "C5'" "H5'1" sing N N 14  
ADP "C5'" "H5'2" sing N N 15  
ADP "C4'" "O4'"  sing N N 16  
ADP "C4'" "C3'"  sing N N 17  
ADP "C4'" "H4'"  sing N N 18  
ADP "O4'" "C1'"  sing N N 19  
ADP "C3'" "O3'"  sing N N 20  
ADP "C3'" "C2'"  sing N N 21  
ADP "C3'" "H3'"  sing N N 22  
ADP "O3'" "HO3'" sing N N 23  
ADP "C2'" "O2'"  sing N N 24  
ADP "C2'" "C1'"  sing N N 25  
ADP "C2'" "H2'"  sing N N 26  
ADP "O2'" "HO2'" sing N N 27  
ADP "C1'" N9     sing N N 28  
ADP "C1'" "H1'"  sing N N 29  
ADP N9    C8     sing Y N 30  
ADP N9    C4     sing Y N 31  
ADP C8    N7     doub Y N 32  
ADP C8    H8     sing N N 33  
ADP N7    C5     sing Y N 34  
ADP C5    C6     sing Y N 35  
ADP C5    C4     doub Y N 36  
ADP C6    N6     sing N N 37  
ADP C6    N1     doub Y N 38  
ADP N6    HN61   sing N N 39  
ADP N6    HN62   sing N N 40  
ADP N1    C2     sing Y N 41  
ADP C2    N3     doub Y N 42  
ADP C2    H2     sing N N 43  
ADP N3    C4     sing Y N 44  
ALA N     CA     sing N N 45  
ALA N     H      sing N N 46  
ALA N     H2     sing N N 47  
ALA CA    C      sing N N 48  
ALA CA    CB     sing N N 49  
ALA CA    HA     sing N N 50  
ALA C     O      doub N N 51  
ALA C     OXT    sing N N 52  
ALA CB    HB1    sing N N 53  
ALA CB    HB2    sing N N 54  
ALA CB    HB3    sing N N 55  
ALA OXT   HXT    sing N N 56  
ARG N     CA     sing N N 57  
ARG N     H      sing N N 58  
ARG N     H2     sing N N 59  
ARG CA    C      sing N N 60  
ARG CA    CB     sing N N 61  
ARG CA    HA     sing N N 62  
ARG C     O      doub N N 63  
ARG C     OXT    sing N N 64  
ARG CB    CG     sing N N 65  
ARG CB    HB2    sing N N 66  
ARG CB    HB3    sing N N 67  
ARG CG    CD     sing N N 68  
ARG CG    HG2    sing N N 69  
ARG CG    HG3    sing N N 70  
ARG CD    NE     sing N N 71  
ARG CD    HD2    sing N N 72  
ARG CD    HD3    sing N N 73  
ARG NE    CZ     sing N N 74  
ARG NE    HE     sing N N 75  
ARG CZ    NH1    sing N N 76  
ARG CZ    NH2    doub N N 77  
ARG NH1   HH11   sing N N 78  
ARG NH1   HH12   sing N N 79  
ARG NH2   HH21   sing N N 80  
ARG NH2   HH22   sing N N 81  
ARG OXT   HXT    sing N N 82  
ASN N     CA     sing N N 83  
ASN N     H      sing N N 84  
ASN N     H2     sing N N 85  
ASN CA    C      sing N N 86  
ASN CA    CB     sing N N 87  
ASN CA    HA     sing N N 88  
ASN C     O      doub N N 89  
ASN C     OXT    sing N N 90  
ASN CB    CG     sing N N 91  
ASN CB    HB2    sing N N 92  
ASN CB    HB3    sing N N 93  
ASN CG    OD1    doub N N 94  
ASN CG    ND2    sing N N 95  
ASN ND2   HD21   sing N N 96  
ASN ND2   HD22   sing N N 97  
ASN OXT   HXT    sing N N 98  
ASP N     CA     sing N N 99  
ASP N     H      sing N N 100 
ASP N     H2     sing N N 101 
ASP CA    C      sing N N 102 
ASP CA    CB     sing N N 103 
ASP CA    HA     sing N N 104 
ASP C     O      doub N N 105 
ASP C     OXT    sing N N 106 
ASP CB    CG     sing N N 107 
ASP CB    HB2    sing N N 108 
ASP CB    HB3    sing N N 109 
ASP CG    OD1    doub N N 110 
ASP CG    OD2    sing N N 111 
ASP OD2   HD2    sing N N 112 
ASP OXT   HXT    sing N N 113 
CYS N     CA     sing N N 114 
CYS N     H      sing N N 115 
CYS N     H2     sing N N 116 
CYS CA    C      sing N N 117 
CYS CA    CB     sing N N 118 
CYS CA    HA     sing N N 119 
CYS C     O      doub N N 120 
CYS C     OXT    sing N N 121 
CYS CB    SG     sing N N 122 
CYS CB    HB2    sing N N 123 
CYS CB    HB3    sing N N 124 
CYS SG    HG     sing N N 125 
CYS OXT   HXT    sing N N 126 
GLN N     CA     sing N N 127 
GLN N     H      sing N N 128 
GLN N     H2     sing N N 129 
GLN CA    C      sing N N 130 
GLN CA    CB     sing N N 131 
GLN CA    HA     sing N N 132 
GLN C     O      doub N N 133 
GLN C     OXT    sing N N 134 
GLN CB    CG     sing N N 135 
GLN CB    HB2    sing N N 136 
GLN CB    HB3    sing N N 137 
GLN CG    CD     sing N N 138 
GLN CG    HG2    sing N N 139 
GLN CG    HG3    sing N N 140 
GLN CD    OE1    doub N N 141 
GLN CD    NE2    sing N N 142 
GLN NE2   HE21   sing N N 143 
GLN NE2   HE22   sing N N 144 
GLN OXT   HXT    sing N N 145 
GLU N     CA     sing N N 146 
GLU N     H      sing N N 147 
GLU N     H2     sing N N 148 
GLU CA    C      sing N N 149 
GLU CA    CB     sing N N 150 
GLU CA    HA     sing N N 151 
GLU C     O      doub N N 152 
GLU C     OXT    sing N N 153 
GLU CB    CG     sing N N 154 
GLU CB    HB2    sing N N 155 
GLU CB    HB3    sing N N 156 
GLU CG    CD     sing N N 157 
GLU CG    HG2    sing N N 158 
GLU CG    HG3    sing N N 159 
GLU CD    OE1    doub N N 160 
GLU CD    OE2    sing N N 161 
GLU OE2   HE2    sing N N 162 
GLU OXT   HXT    sing N N 163 
GLY N     CA     sing N N 164 
GLY N     H      sing N N 165 
GLY N     H2     sing N N 166 
GLY CA    C      sing N N 167 
GLY CA    HA2    sing N N 168 
GLY CA    HA3    sing N N 169 
GLY C     O      doub N N 170 
GLY C     OXT    sing N N 171 
GLY OXT   HXT    sing N N 172 
HIS N     CA     sing N N 173 
HIS N     H      sing N N 174 
HIS N     H2     sing N N 175 
HIS CA    C      sing N N 176 
HIS CA    CB     sing N N 177 
HIS CA    HA     sing N N 178 
HIS C     O      doub N N 179 
HIS C     OXT    sing N N 180 
HIS CB    CG     sing N N 181 
HIS CB    HB2    sing N N 182 
HIS CB    HB3    sing N N 183 
HIS CG    ND1    sing Y N 184 
HIS CG    CD2    doub Y N 185 
HIS ND1   CE1    doub Y N 186 
HIS ND1   HD1    sing N N 187 
HIS CD2   NE2    sing Y N 188 
HIS CD2   HD2    sing N N 189 
HIS CE1   NE2    sing Y N 190 
HIS CE1   HE1    sing N N 191 
HIS NE2   HE2    sing N N 192 
HIS OXT   HXT    sing N N 193 
ILE N     CA     sing N N 194 
ILE N     H      sing N N 195 
ILE N     H2     sing N N 196 
ILE CA    C      sing N N 197 
ILE CA    CB     sing N N 198 
ILE CA    HA     sing N N 199 
ILE C     O      doub N N 200 
ILE C     OXT    sing N N 201 
ILE CB    CG1    sing N N 202 
ILE CB    CG2    sing N N 203 
ILE CB    HB     sing N N 204 
ILE CG1   CD1    sing N N 205 
ILE CG1   HG12   sing N N 206 
ILE CG1   HG13   sing N N 207 
ILE CG2   HG21   sing N N 208 
ILE CG2   HG22   sing N N 209 
ILE CG2   HG23   sing N N 210 
ILE CD1   HD11   sing N N 211 
ILE CD1   HD12   sing N N 212 
ILE CD1   HD13   sing N N 213 
ILE OXT   HXT    sing N N 214 
LEU N     CA     sing N N 215 
LEU N     H      sing N N 216 
LEU N     H2     sing N N 217 
LEU CA    C      sing N N 218 
LEU CA    CB     sing N N 219 
LEU CA    HA     sing N N 220 
LEU C     O      doub N N 221 
LEU C     OXT    sing N N 222 
LEU CB    CG     sing N N 223 
LEU CB    HB2    sing N N 224 
LEU CB    HB3    sing N N 225 
LEU CG    CD1    sing N N 226 
LEU CG    CD2    sing N N 227 
LEU CG    HG     sing N N 228 
LEU CD1   HD11   sing N N 229 
LEU CD1   HD12   sing N N 230 
LEU CD1   HD13   sing N N 231 
LEU CD2   HD21   sing N N 232 
LEU CD2   HD22   sing N N 233 
LEU CD2   HD23   sing N N 234 
LEU OXT   HXT    sing N N 235 
LYS N     CA     sing N N 236 
LYS N     H      sing N N 237 
LYS N     H2     sing N N 238 
LYS CA    C      sing N N 239 
LYS CA    CB     sing N N 240 
LYS CA    HA     sing N N 241 
LYS C     O      doub N N 242 
LYS C     OXT    sing N N 243 
LYS CB    CG     sing N N 244 
LYS CB    HB2    sing N N 245 
LYS CB    HB3    sing N N 246 
LYS CG    CD     sing N N 247 
LYS CG    HG2    sing N N 248 
LYS CG    HG3    sing N N 249 
LYS CD    CE     sing N N 250 
LYS CD    HD2    sing N N 251 
LYS CD    HD3    sing N N 252 
LYS CE    NZ     sing N N 253 
LYS CE    HE2    sing N N 254 
LYS CE    HE3    sing N N 255 
LYS NZ    HZ1    sing N N 256 
LYS NZ    HZ2    sing N N 257 
LYS NZ    HZ3    sing N N 258 
LYS OXT   HXT    sing N N 259 
MET N     CA     sing N N 260 
MET N     H      sing N N 261 
MET N     H2     sing N N 262 
MET CA    C      sing N N 263 
MET CA    CB     sing N N 264 
MET CA    HA     sing N N 265 
MET C     O      doub N N 266 
MET C     OXT    sing N N 267 
MET CB    CG     sing N N 268 
MET CB    HB2    sing N N 269 
MET CB    HB3    sing N N 270 
MET CG    SD     sing N N 271 
MET CG    HG2    sing N N 272 
MET CG    HG3    sing N N 273 
MET SD    CE     sing N N 274 
MET CE    HE1    sing N N 275 
MET CE    HE2    sing N N 276 
MET CE    HE3    sing N N 277 
MET OXT   HXT    sing N N 278 
PHE N     CA     sing N N 279 
PHE N     H      sing N N 280 
PHE N     H2     sing N N 281 
PHE CA    C      sing N N 282 
PHE CA    CB     sing N N 283 
PHE CA    HA     sing N N 284 
PHE C     O      doub N N 285 
PHE C     OXT    sing N N 286 
PHE CB    CG     sing N N 287 
PHE CB    HB2    sing N N 288 
PHE CB    HB3    sing N N 289 
PHE CG    CD1    doub Y N 290 
PHE CG    CD2    sing Y N 291 
PHE CD1   CE1    sing Y N 292 
PHE CD1   HD1    sing N N 293 
PHE CD2   CE2    doub Y N 294 
PHE CD2   HD2    sing N N 295 
PHE CE1   CZ     doub Y N 296 
PHE CE1   HE1    sing N N 297 
PHE CE2   CZ     sing Y N 298 
PHE CE2   HE2    sing N N 299 
PHE CZ    HZ     sing N N 300 
PHE OXT   HXT    sing N N 301 
PO4 P     O1     doub N N 302 
PO4 P     O2     sing N N 303 
PO4 P     O3     sing N N 304 
PO4 P     O4     sing N N 305 
PRO N     CA     sing N N 306 
PRO N     CD     sing N N 307 
PRO N     H      sing N N 308 
PRO CA    C      sing N N 309 
PRO CA    CB     sing N N 310 
PRO CA    HA     sing N N 311 
PRO C     O      doub N N 312 
PRO C     OXT    sing N N 313 
PRO CB    CG     sing N N 314 
PRO CB    HB2    sing N N 315 
PRO CB    HB3    sing N N 316 
PRO CG    CD     sing N N 317 
PRO CG    HG2    sing N N 318 
PRO CG    HG3    sing N N 319 
PRO CD    HD2    sing N N 320 
PRO CD    HD3    sing N N 321 
PRO OXT   HXT    sing N N 322 
SER N     CA     sing N N 323 
SER N     H      sing N N 324 
SER N     H2     sing N N 325 
SER CA    C      sing N N 326 
SER CA    CB     sing N N 327 
SER CA    HA     sing N N 328 
SER C     O      doub N N 329 
SER C     OXT    sing N N 330 
SER CB    OG     sing N N 331 
SER CB    HB2    sing N N 332 
SER CB    HB3    sing N N 333 
SER OG    HG     sing N N 334 
SER OXT   HXT    sing N N 335 
THR N     CA     sing N N 336 
THR N     H      sing N N 337 
THR N     H2     sing N N 338 
THR CA    C      sing N N 339 
THR CA    CB     sing N N 340 
THR CA    HA     sing N N 341 
THR C     O      doub N N 342 
THR C     OXT    sing N N 343 
THR CB    OG1    sing N N 344 
THR CB    CG2    sing N N 345 
THR CB    HB     sing N N 346 
THR OG1   HG1    sing N N 347 
THR CG2   HG21   sing N N 348 
THR CG2   HG22   sing N N 349 
THR CG2   HG23   sing N N 350 
THR OXT   HXT    sing N N 351 
TRP N     CA     sing N N 352 
TRP N     H      sing N N 353 
TRP N     H2     sing N N 354 
TRP CA    C      sing N N 355 
TRP CA    CB     sing N N 356 
TRP CA    HA     sing N N 357 
TRP C     O      doub N N 358 
TRP C     OXT    sing N N 359 
TRP CB    CG     sing N N 360 
TRP CB    HB2    sing N N 361 
TRP CB    HB3    sing N N 362 
TRP CG    CD1    doub Y N 363 
TRP CG    CD2    sing Y N 364 
TRP CD1   NE1    sing Y N 365 
TRP CD1   HD1    sing N N 366 
TRP CD2   CE2    doub Y N 367 
TRP CD2   CE3    sing Y N 368 
TRP NE1   CE2    sing Y N 369 
TRP NE1   HE1    sing N N 370 
TRP CE2   CZ2    sing Y N 371 
TRP CE3   CZ3    doub Y N 372 
TRP CE3   HE3    sing N N 373 
TRP CZ2   CH2    doub Y N 374 
TRP CZ2   HZ2    sing N N 375 
TRP CZ3   CH2    sing Y N 376 
TRP CZ3   HZ3    sing N N 377 
TRP CH2   HH2    sing N N 378 
TRP OXT   HXT    sing N N 379 
TYR N     CA     sing N N 380 
TYR N     H      sing N N 381 
TYR N     H2     sing N N 382 
TYR CA    C      sing N N 383 
TYR CA    CB     sing N N 384 
TYR CA    HA     sing N N 385 
TYR C     O      doub N N 386 
TYR C     OXT    sing N N 387 
TYR CB    CG     sing N N 388 
TYR CB    HB2    sing N N 389 
TYR CB    HB3    sing N N 390 
TYR CG    CD1    doub Y N 391 
TYR CG    CD2    sing Y N 392 
TYR CD1   CE1    sing Y N 393 
TYR CD1   HD1    sing N N 394 
TYR CD2   CE2    doub Y N 395 
TYR CD2   HD2    sing N N 396 
TYR CE1   CZ     doub Y N 397 
TYR CE1   HE1    sing N N 398 
TYR CE2   CZ     sing Y N 399 
TYR CE2   HE2    sing N N 400 
TYR CZ    OH     sing N N 401 
TYR OH    HH     sing N N 402 
TYR OXT   HXT    sing N N 403 
VAL N     CA     sing N N 404 
VAL N     H      sing N N 405 
VAL N     H2     sing N N 406 
VAL CA    C      sing N N 407 
VAL CA    CB     sing N N 408 
VAL CA    HA     sing N N 409 
VAL C     O      doub N N 410 
VAL C     OXT    sing N N 411 
VAL CB    CG1    sing N N 412 
VAL CB    CG2    sing N N 413 
VAL CB    HB     sing N N 414 
VAL CG1   HG11   sing N N 415 
VAL CG1   HG12   sing N N 416 
VAL CG1   HG13   sing N N 417 
VAL CG2   HG21   sing N N 418 
VAL CG2   HG22   sing N N 419 
VAL CG2   HG23   sing N N 420 
VAL OXT   HXT    sing N N 421 
# 
_em_admin.current_status     REL 
_em_admin.deposition_date    2024-08-08 
_em_admin.deposition_site    PDBJ 
_em_admin.entry_id           9J3M 
_em_admin.last_update        2025-03-26 
_em_admin.map_release_date   2025-03-19 
_em_admin.title              'ADP/Pi bound 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 ? ? ? ? 
'VOLUME SELECTION'              ? 14 1 1 1 ? ? 
'SERIES ALIGNMENT'              ? 15 1 1 1 ? ? 
'MOLECULAR REPLACEMENT'         ? 16 1 1 1 ? ? 
'LATTICE DISTORTION CORRECTION' ? 17 1 1 1 ? ? 
'SYMMETRY DETERMINATION'        ? 18 1 1 1 ? ? 
'CRYSTALLOGRAPHY MERGING'       ? 19 1 1 1 ? ? 
# 
_em_specimen.concentration           ? 
_em_specimen.details                 ? 
_em_specimen.embedding_applied       NO 
_em_specimen.experiment_id           1 
_em_specimen.id                      1 
_em_specimen.shadowing_applied       NO 
_em_specimen.staining_applied        NO 
_em_specimen.vitrification_applied   YES 
# 
_pdbx_audit_support.funding_organization   'Chinese Academy of Sciences' 
_pdbx_audit_support.country                China 
_pdbx_audit_support.grant_number           XDB0630101 
_pdbx_audit_support.ordinal                1 
# 
_atom_sites.entry_id                    9J3M 
_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 
P 
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  ? 125.868 100.234 178.265 1.00 152.07 ? 101 ALA A N     1 
ATOM   2    C CA    . ALA A 1 16  ? 127.233 100.639 177.950 1.00 151.04 ? 101 ALA A CA    1 
ATOM   3    C C     . ALA A 1 16  ? 127.403 100.863 176.451 1.00 149.92 ? 101 ALA A C     1 
ATOM   4    O O     . ALA A 1 16  ? 128.370 100.396 175.850 1.00 149.11 ? 101 ALA A O     1 
ATOM   5    C CB    . ALA A 1 16  ? 128.223 99.597  178.447 1.00 145.81 ? 101 ALA A CB    1 
ATOM   6    N N     . SER A 1 17  ? 126.459 101.578 175.856 1.00 149.05 ? 102 SER A N     1 
ATOM   7    C CA    . SER A 1 17  ? 126.510 101.857 174.425 1.00 146.03 ? 102 SER A CA    1 
ATOM   8    C C     . SER A 1 17  ? 127.656 102.812 174.120 1.00 145.45 ? 102 SER A C     1 
ATOM   9    O O     . SER A 1 17  ? 127.728 103.892 174.723 1.00 142.83 ? 102 SER A O     1 
ATOM   10   C CB    . SER A 1 17  ? 125.184 102.445 173.952 1.00 139.76 ? 102 SER A CB    1 
ATOM   11   O OG    . SER A 1 17  ? 124.770 103.511 174.790 1.00 133.49 ? 102 SER A OG    1 
ATOM   12   N N     . PRO A 1 18  ? 128.565 102.468 173.211 1.00 144.06 ? 103 PRO A N     1 
ATOM   13   C CA    . PRO A 1 18  ? 129.682 103.366 172.902 1.00 140.31 ? 103 PRO A CA    1 
ATOM   14   C C     . PRO A 1 18  ? 129.211 104.638 172.212 1.00 134.19 ? 103 PRO A C     1 
ATOM   15   O O     . PRO A 1 18  ? 128.122 104.707 171.638 1.00 132.36 ? 103 PRO A O     1 
ATOM   16   C CB    . PRO A 1 18  ? 130.573 102.528 171.976 1.00 135.83 ? 103 PRO A CB    1 
ATOM   17   C CG    . PRO A 1 18  ? 130.134 101.109 172.185 1.00 136.60 ? 103 PRO A CG    1 
ATOM   18   C CD    . PRO A 1 18  ? 128.675 101.182 172.504 1.00 139.03 ? 103 PRO A CD    1 
ATOM   19   N N     . LYS A 1 19  ? 130.060 105.660 172.285 1.00 132.32 ? 104 LYS A N     1 
ATOM   20   C CA    . LYS A 1 19  ? 129.760 107.004 171.798 1.00 129.80 ? 104 LYS A CA    1 
ATOM   21   C C     . LYS A 1 19  ? 130.917 107.542 170.964 1.00 128.08 ? 104 LYS A C     1 
ATOM   22   O O     . LYS A 1 19  ? 131.446 108.627 171.219 1.00 126.74 ? 104 LYS A O     1 
ATOM   23   C CB    . LYS A 1 19  ? 129.440 107.949 172.952 1.00 129.44 ? 104 LYS A CB    1 
ATOM   24   C CG    . LYS A 1 19  ? 128.109 107.665 173.630 1.00 129.01 ? 104 LYS A CG    1 
ATOM   25   C CD    . LYS A 1 19  ? 127.881 108.592 174.810 1.00 125.44 ? 104 LYS A CD    1 
ATOM   26   C CE    . LYS A 1 19  ? 127.616 110.015 174.344 1.00 123.01 ? 104 LYS A CE    1 
ATOM   27   N NZ    . LYS A 1 19  ? 127.284 110.921 175.477 1.00 120.00 ? 104 LYS A NZ    1 
ATOM   28   N N     . ILE A 1 20  ? 131.348 106.755 169.974 1.00 127.59 ? 105 ILE A N     1 
ATOM   29   C CA    . ILE A 1 20  ? 132.431 107.115 169.060 1.00 127.50 ? 105 ILE A CA    1 
ATOM   30   C C     . ILE A 1 20  ? 132.273 108.548 168.565 1.00 128.72 ? 105 ILE A C     1 
ATOM   31   O O     . ILE A 1 20  ? 131.202 108.935 168.083 1.00 129.33 ? 105 ILE A O     1 
ATOM   32   C CB    . ILE A 1 20  ? 132.489 106.139 167.869 1.00 126.52 ? 105 ILE A CB    1 
ATOM   33   C CG1   . ILE A 1 20  ? 132.823 104.724 168.344 1.00 127.23 ? 105 ILE A CG1   1 
ATOM   34   C CG2   . ILE A 1 20  ? 133.502 106.612 166.836 1.00 124.39 ? 105 ILE A CG2   1 
ATOM   35   C CD1   . ILE A 1 20  ? 132.668 103.670 167.268 1.00 120.43 ? 105 ILE A CD1   1 
ATOM   36   N N     . PHE A 1 21  ? 133.338 109.342 168.694 1.00 129.57 ? 106 PHE A N     1 
ATOM   37   C CA    . PHE A 1 21  ? 133.369 110.748 168.289 1.00 128.62 ? 106 PHE A CA    1 
ATOM   38   C C     . PHE A 1 21  ? 132.346 111.592 169.042 1.00 127.14 ? 106 PHE A C     1 
ATOM   39   O O     . PHE A 1 21  ? 131.942 112.657 168.562 1.00 125.71 ? 106 PHE A O     1 
ATOM   40   C CB    . PHE A 1 21  ? 133.160 110.907 166.775 1.00 129.46 ? 106 PHE A CB    1 
ATOM   41   C CG    . PHE A 1 21  ? 134.335 110.470 165.939 1.00 131.60 ? 106 PHE A CG    1 
ATOM   42   C CD1   . PHE A 1 21  ? 135.419 109.822 166.509 1.00 130.21 ? 106 PHE A CD1   1 
ATOM   43   C CD2   . PHE A 1 21  ? 134.349 110.711 164.575 1.00 129.15 ? 106 PHE A CD2   1 
ATOM   44   C CE1   . PHE A 1 21  ? 136.493 109.424 165.735 1.00 127.91 ? 106 PHE A CE1   1 
ATOM   45   C CE2   . PHE A 1 21  ? 135.419 110.316 163.796 1.00 126.82 ? 106 PHE A CE2   1 
ATOM   46   C CZ    . PHE A 1 21  ? 136.492 109.671 164.377 1.00 125.72 ? 106 PHE A CZ    1 
ATOM   47   N N     . GLY A 1 22  ? 131.918 111.142 170.219 1.00 127.55 ? 107 GLY A N     1 
ATOM   48   C CA    . GLY A 1 22  ? 130.880 111.825 170.959 1.00 129.63 ? 107 GLY A CA    1 
ATOM   49   C C     . GLY A 1 22  ? 129.474 111.554 170.473 1.00 128.14 ? 107 GLY A C     1 
ATOM   50   O O     . GLY A 1 22  ? 128.524 112.122 171.027 1.00 126.70 ? 107 GLY A O     1 
ATOM   51   N N     . VAL A 1 23  ? 129.310 110.707 169.460 1.00 127.04 ? 108 VAL A N     1 
ATOM   52   C CA    . VAL A 1 23  ? 128.012 110.381 168.885 1.00 124.67 ? 108 VAL A CA    1 
ATOM   53   C C     . VAL A 1 23  ? 127.757 108.896 169.098 1.00 122.45 ? 108 VAL A C     1 
ATOM   54   O O     . VAL A 1 23  ? 128.655 108.070 168.898 1.00 123.30 ? 108 VAL A O     1 
ATOM   55   C CB    . VAL A 1 23  ? 127.951 110.743 167.386 1.00 120.34 ? 108 VAL A CB    1 
ATOM   56   C CG1   . VAL A 1 23  ? 126.565 110.478 166.826 1.00 113.14 ? 108 VAL A CG1   1 
ATOM   57   C CG2   . VAL A 1 23  ? 128.349 112.196 167.174 1.00 119.59 ? 108 VAL A CG2   1 
ATOM   58   N N     . GLU A 1 24  ? 126.536 108.561 169.509 1.00 121.64 ? 109 GLU A N     1 
ATOM   59   C CA    . GLU A 1 24  ? 126.202 107.178 169.820 1.00 121.98 ? 109 GLU A CA    1 
ATOM   60   C C     . GLU A 1 24  ? 126.372 106.289 168.594 1.00 117.45 ? 109 GLU A C     1 
ATOM   61   O O     . GLU A 1 24  ? 126.083 106.686 167.462 1.00 114.98 ? 109 GLU A O     1 
ATOM   62   C CB    . GLU A 1 24  ? 124.768 107.080 170.340 1.00 122.91 ? 109 GLU A CB    1 
ATOM   63   C CG    . GLU A 1 24  ? 124.497 105.841 171.178 1.00 125.84 ? 109 GLU A CG    1 
ATOM   64   C CD    . GLU A 1 24  ? 123.038 105.428 171.156 1.00 129.51 ? 109 GLU A CD    1 
ATOM   65   O OE1   . GLU A 1 24  ? 122.181 106.280 170.842 1.00 129.14 ? 109 GLU A OE1   1 
ATOM   66   O OE2   . GLU A 1 24  ? 122.749 104.251 171.458 1.00 132.63 ? 109 GLU A OE2   1 
ATOM   67   N N     . VAL A 1 25  ? 126.855 105.065 168.832 1.00 119.54 ? 110 VAL A N     1 
ATOM   68   C CA    . VAL A 1 25  ? 127.063 104.110 167.744 1.00 116.25 ? 110 VAL A CA    1 
ATOM   69   C C     . VAL A 1 25  ? 125.765 103.542 167.197 1.00 110.02 ? 110 VAL A C     1 
ATOM   70   O O     . VAL A 1 25  ? 125.791 102.852 166.171 1.00 108.58 ? 110 VAL A O     1 
ATOM   71   C CB    . VAL A 1 25  ? 127.975 102.951 168.189 1.00 121.59 ? 110 VAL A CB    1 
ATOM   72   C CG1   . VAL A 1 25  ? 129.257 103.498 168.795 1.00 124.20 ? 110 VAL A CG1   1 
ATOM   73   C CG2   . VAL A 1 25  ? 127.251 102.057 169.182 1.00 123.23 ? 110 VAL A CG2   1 
ATOM   74   N N     . ALA A 1 26  ? 124.634 103.796 167.855 1.00 110.65 ? 111 ALA A N     1 
ATOM   75   C CA    . ALA A 1 26  ? 123.341 103.428 167.294 1.00 110.27 ? 111 ALA A CA    1 
ATOM   76   C C     . ALA A 1 26  ? 122.824 104.486 166.329 1.00 108.50 ? 111 ALA A C     1 
ATOM   77   O O     . ALA A 1 26  ? 122.260 104.149 165.283 1.00 106.84 ? 111 ALA A O     1 
ATOM   78   C CB    . ALA A 1 26  ? 122.322 103.196 168.413 1.00 111.77 ? 111 ALA A CB    1 
ATOM   79   N N     . THR A 1 27  ? 123.007 105.765 166.664 1.00 109.24 ? 112 THR A N     1 
ATOM   80   C CA    . THR A 1 27  ? 122.673 106.828 165.723 1.00 107.36 ? 112 THR A CA    1 
ATOM   81   C C     . THR A 1 27  ? 123.663 106.879 164.568 1.00 102.38 ? 112 THR A C     1 
ATOM   82   O O     . THR A 1 27  ? 123.288 107.247 163.450 1.00 99.12  ? 112 THR A O     1 
ATOM   83   C CB    . THR A 1 27  ? 122.627 108.178 166.441 1.00 110.78 ? 112 THR A CB    1 
ATOM   84   O OG1   . THR A 1 27  ? 123.961 108.665 166.627 1.00 108.90 ? 112 THR A OG1   1 
ATOM   85   C CG2   . THR A 1 27  ? 121.951 108.039 167.796 1.00 114.39 ? 112 THR A CG2   1 
ATOM   86   N N     . LEU A 1 28  ? 124.924 106.512 164.816 1.00 102.18 ? 113 LEU A N     1 
ATOM   87   C CA    . LEU A 1 28  ? 125.919 106.504 163.748 1.00 94.31  ? 113 LEU A CA    1 
ATOM   88   C C     . LEU A 1 28  ? 125.547 105.508 162.657 1.00 89.99  ? 113 LEU A C     1 
ATOM   89   O O     . LEU A 1 28  ? 125.725 105.788 161.465 1.00 90.19  ? 113 LEU A O     1 
ATOM   90   C CB    . LEU A 1 28  ? 127.302 106.187 164.317 1.00 99.65  ? 113 LEU A CB    1 
ATOM   91   C CG    . LEU A 1 28  ? 128.111 107.379 164.833 1.00 103.10 ? 113 LEU A CG    1 
ATOM   92   C CD1   . LEU A 1 28  ? 129.542 106.965 165.137 1.00 106.78 ? 113 LEU A CD1   1 
ATOM   93   C CD2   . LEU A 1 28  ? 128.082 108.522 163.829 1.00 99.20  ? 113 LEU A CD2   1 
ATOM   94   N N     . LYS A 1 29  ? 125.024 104.343 163.042 1.00 90.57  ? 114 LYS A N     1 
ATOM   95   C CA    . LYS A 1 29  ? 124.537 103.383 162.059 1.00 88.66  ? 114 LYS A CA    1 
ATOM   96   C C     . LYS A 1 29  ? 123.336 103.903 161.282 1.00 89.75  ? 114 LYS A C     1 
ATOM   97   O O     . LYS A 1 29  ? 122.983 103.315 160.255 1.00 90.51  ? 114 LYS A O     1 
ATOM   98   C CB    . LYS A 1 29  ? 124.177 102.063 162.743 1.00 88.45  ? 114 LYS A CB    1 
ATOM   99   C CG    . LYS A 1 29  ? 125.353 101.369 163.414 1.00 87.46  ? 114 LYS A CG    1 
ATOM   100  C CD    . LYS A 1 29  ? 125.218 99.854  163.358 1.00 87.55  ? 114 LYS A CD    1 
ATOM   101  C CE    . LYS A 1 29  ? 123.792 99.408  163.640 1.00 92.42  ? 114 LYS A CE    1 
ATOM   102  N NZ    . LYS A 1 29  ? 123.671 97.925  163.680 1.00 93.39  ? 114 LYS A NZ    1 
ATOM   103  N N     . LYS A 1 30  ? 122.706 104.980 161.745 1.00 91.43  ? 115 LYS A N     1 
ATOM   104  C CA    . LYS A 1 30  ? 121.587 105.599 161.048 1.00 89.60  ? 115 LYS A CA    1 
ATOM   105  C C     . LYS A 1 30  ? 121.997 106.812 160.226 1.00 84.71  ? 115 LYS A C     1 
ATOM   106  O O     . LYS A 1 30  ? 121.440 107.032 159.145 1.00 83.92  ? 115 LYS A O     1 
ATOM   107  C CB    . LYS A 1 30  ? 120.508 106.009 162.058 1.00 90.37  ? 115 LYS A CB    1 
ATOM   108  C CG    . LYS A 1 30  ? 119.388 106.864 161.493 1.00 93.23  ? 115 LYS A CG    1 
ATOM   109  C CD    . LYS A 1 30  ? 118.365 107.187 162.567 1.00 95.69  ? 115 LYS A CD    1 
ATOM   110  C CE    . LYS A 1 30  ? 117.617 105.939 163.005 1.00 99.30  ? 115 LYS A CE    1 
ATOM   111  N NZ    . LYS A 1 30  ? 116.529 106.255 163.970 1.00 103.38 ? 115 LYS A NZ    1 
ATOM   112  N N     . ILE A 1 31  ? 122.969 107.589 160.698 1.00 82.17  ? 116 ILE A N     1 
ATOM   113  C CA    . ILE A 1 31  ? 123.369 108.814 160.012 1.00 79.03  ? 116 ILE A CA    1 
ATOM   114  C C     . ILE A 1 31  ? 124.452 108.556 158.972 1.00 76.74  ? 116 ILE A C     1 
ATOM   115  O O     . ILE A 1 31  ? 124.415 109.131 157.881 1.00 75.70  ? 116 ILE A O     1 
ATOM   116  C CB    . ILE A 1 31  ? 123.818 109.869 161.041 1.00 80.16  ? 116 ILE A CB    1 
ATOM   117  C CG1   . ILE A 1 31  ? 122.758 110.033 162.133 1.00 87.73  ? 116 ILE A CG1   1 
ATOM   118  C CG2   . ILE A 1 31  ? 124.115 111.187 160.353 1.00 78.11  ? 116 ILE A CG2   1 
ATOM   119  C CD1   . ILE A 1 31  ? 121.459 110.630 161.635 1.00 87.83  ? 116 ILE A CD1   1 
ATOM   120  N N     . ILE A 1 32  ? 125.437 107.709 159.288 1.00 77.57  ? 117 ILE A N     1 
ATOM   121  C CA    . ILE A 1 32  ? 126.507 107.427 158.328 1.00 72.32  ? 117 ILE A CA    1 
ATOM   122  C C     . ILE A 1 32  ? 125.967 106.848 157.024 1.00 70.05  ? 117 ILE A C     1 
ATOM   123  O O     . ILE A 1 32  ? 126.341 107.350 155.952 1.00 74.11  ? 117 ILE A O     1 
ATOM   124  C CB    . ILE A 1 32  ? 127.582 106.539 158.977 1.00 73.91  ? 117 ILE A CB    1 
ATOM   125  C CG1   . ILE A 1 32  ? 128.320 107.305 160.077 1.00 76.86  ? 117 ILE A CG1   1 
ATOM   126  C CG2   . ILE A 1 32  ? 128.561 106.029 157.929 1.00 69.77  ? 117 ILE A CG2   1 
ATOM   127  C CD1   . ILE A 1 32  ? 129.106 108.494 159.572 1.00 75.97  ? 117 ILE A CD1   1 
ATOM   128  N N     . PRO A 1 33  ? 125.099 105.828 157.028 1.00 68.78  ? 118 PRO A N     1 
ATOM   129  C CA    . PRO A 1 33  ? 124.539 105.349 155.753 1.00 65.92  ? 118 PRO A CA    1 
ATOM   130  C C     . PRO A 1 33  ? 123.513 106.288 155.141 1.00 68.11  ? 118 PRO A C     1 
ATOM   131  O O     . PRO A 1 33  ? 123.112 106.067 153.991 1.00 66.17  ? 118 PRO A O     1 
ATOM   132  C CB    . PRO A 1 33  ? 123.900 104.003 156.131 1.00 70.36  ? 118 PRO A CB    1 
ATOM   133  C CG    . PRO A 1 33  ? 124.504 103.649 157.457 1.00 74.74  ? 118 PRO A CG    1 
ATOM   134  C CD    . PRO A 1 33  ? 124.665 104.963 158.136 1.00 75.62  ? 118 PRO A CD    1 
ATOM   135  N N     . LEU A 1 34  ? 123.071 107.317 155.864 1.00 71.92  ? 119 LEU A N     1 
ATOM   136  C CA    . LEU A 1 34  ? 122.111 108.270 155.320 1.00 64.20  ? 119 LEU A CA    1 
ATOM   137  C C     . LEU A 1 34  ? 122.797 109.417 154.590 1.00 59.18  ? 119 LEU A C     1 
ATOM   138  O O     . LEU A 1 34  ? 122.360 109.806 153.502 1.00 62.50  ? 119 LEU A O     1 
ATOM   139  C CB    . LEU A 1 34  ? 121.218 108.813 156.439 1.00 64.50  ? 119 LEU A CB    1 
ATOM   140  C CG    . LEU A 1 34  ? 119.811 109.249 156.026 1.00 69.58  ? 119 LEU A CG    1 
ATOM   141  C CD1   . LEU A 1 34  ? 119.055 108.085 155.409 1.00 69.44  ? 119 LEU A CD1   1 
ATOM   142  C CD2   . LEU A 1 34  ? 119.055 109.801 157.224 1.00 72.87  ? 119 LEU A CD2   1 
ATOM   143  N N     . GLY A 1 35  ? 123.868 109.969 155.167 1.00 58.71  ? 120 GLY A N     1 
ATOM   144  C CA    . GLY A 1 35  ? 124.678 110.932 154.444 1.00 56.77  ? 120 GLY A CA    1 
ATOM   145  C C     . GLY A 1 35  ? 125.526 110.323 153.352 1.00 56.24  ? 120 GLY A C     1 
ATOM   146  O O     . GLY A 1 35  ? 125.901 111.024 152.407 1.00 58.46  ? 120 GLY A O     1 
ATOM   147  N N     . LEU A 1 36  ? 125.838 109.030 153.464 1.00 56.94  ? 121 LEU A N     1 
ATOM   148  C CA    . LEU A 1 36  ? 126.503 108.319 152.380 1.00 53.57  ? 121 LEU A CA    1 
ATOM   149  C C     . LEU A 1 36  ? 125.554 108.066 151.218 1.00 50.03  ? 121 LEU A C     1 
ATOM   150  O O     . LEU A 1 36  ? 125.987 108.041 150.061 1.00 55.21  ? 121 LEU A O     1 
ATOM   151  C CB    . LEU A 1 36  ? 127.077 106.999 152.897 1.00 57.52  ? 121 LEU A CB    1 
ATOM   152  C CG    . LEU A 1 36  ? 128.270 106.395 152.156 1.00 63.64  ? 121 LEU A CG    1 
ATOM   153  C CD1   . LEU A 1 36  ? 129.546 107.146 152.502 1.00 64.05  ? 121 LEU A CD1   1 
ATOM   154  C CD2   . LEU A 1 36  ? 128.408 104.919 152.496 1.00 58.57  ? 121 LEU A CD2   1 
ATOM   155  N N     . MET A 1 37  ? 124.264 107.876 151.507 1.00 49.17  ? 122 MET A N     1 
ATOM   156  C CA    . MET A 1 37  ? 123.261 107.763 150.454 1.00 48.81  ? 122 MET A CA    1 
ATOM   157  C C     . MET A 1 37  ? 123.060 109.086 149.727 1.00 48.61  ? 122 MET A C     1 
ATOM   158  O O     . MET A 1 37  ? 123.048 109.124 148.491 1.00 54.91  ? 122 MET A O     1 
ATOM   159  C CB    . MET A 1 37  ? 121.932 107.295 151.044 1.00 54.84  ? 122 MET A CB    1 
ATOM   160  C CG    . MET A 1 37  ? 120.862 107.035 150.006 1.00 59.59  ? 122 MET A CG    1 
ATOM   161  S SD    . MET A 1 37  ? 119.329 106.477 150.760 1.00 79.69  ? 122 MET A SD    1 
ATOM   162  C CE    . MET A 1 37  ? 119.808 104.832 151.250 1.00 66.48  ? 122 MET A CE    1 
ATOM   163  N N     . PHE A 1 38  ? 122.895 110.175 150.480 1.00 44.56  ? 123 PHE A N     1 
ATOM   164  C CA    . PHE A 1 38  ? 122.729 111.491 149.879 1.00 42.49  ? 123 PHE A CA    1 
ATOM   165  C C     . PHE A 1 38  ? 123.992 111.935 149.156 1.00 47.95  ? 123 PHE A C     1 
ATOM   166  O O     . PHE A 1 38  ? 123.919 112.789 148.266 1.00 54.41  ? 123 PHE A O     1 
ATOM   167  C CB    . PHE A 1 38  ? 122.318 112.487 150.966 1.00 50.86  ? 123 PHE A CB    1 
ATOM   168  C CG    . PHE A 1 38  ? 121.914 113.839 150.450 1.00 59.06  ? 123 PHE A CG    1 
ATOM   169  C CD1   . PHE A 1 38  ? 120.870 113.968 149.550 1.00 61.72  ? 123 PHE A CD1   1 
ATOM   170  C CD2   . PHE A 1 38  ? 122.522 114.986 150.928 1.00 53.39  ? 123 PHE A CD2   1 
ATOM   171  C CE1   . PHE A 1 38  ? 120.481 115.212 149.089 1.00 61.24  ? 123 PHE A CE1   1 
ATOM   172  C CE2   . PHE A 1 38  ? 122.136 116.235 150.474 1.00 52.03  ? 123 PHE A CE2   1 
ATOM   173  C CZ    . PHE A 1 38  ? 121.114 116.347 149.554 1.00 56.30  ? 123 PHE A CZ    1 
ATOM   174  N N     . PHE A 1 39  ? 125.145 111.370 149.523 1.00 48.44  ? 124 PHE A N     1 
ATOM   175  C CA    . PHE A 1 39  ? 126.346 111.502 148.706 1.00 48.72  ? 124 PHE A CA    1 
ATOM   176  C C     . PHE A 1 39  ? 126.165 110.808 147.361 1.00 50.75  ? 124 PHE A C     1 
ATOM   177  O O     . PHE A 1 39  ? 126.426 111.397 146.306 1.00 52.64  ? 124 PHE A O     1 
ATOM   178  C CB    . PHE A 1 39  ? 127.547 110.928 149.466 1.00 49.46  ? 124 PHE A CB    1 
ATOM   179  C CG    . PHE A 1 39  ? 128.815 110.850 148.655 1.00 51.00  ? 124 PHE A CG    1 
ATOM   180  C CD1   . PHE A 1 39  ? 129.081 109.749 147.853 1.00 49.77  ? 124 PHE A CD1   1 
ATOM   181  C CD2   . PHE A 1 39  ? 129.750 111.869 148.709 1.00 50.30  ? 124 PHE A CD2   1 
ATOM   182  C CE1   . PHE A 1 39  ? 130.244 109.675 147.113 1.00 48.92  ? 124 PHE A CE1   1 
ATOM   183  C CE2   . PHE A 1 39  ? 130.917 111.799 147.973 1.00 50.45  ? 124 PHE A CE2   1 
ATOM   184  C CZ    . PHE A 1 39  ? 131.164 110.701 147.174 1.00 50.42  ? 124 PHE A CZ    1 
ATOM   185  N N     . CYS A 1 40  ? 125.714 109.551 147.382 1.00 48.35  ? 125 CYS A N     1 
ATOM   186  C CA    . CYS A 1 40  ? 125.524 108.807 146.141 1.00 44.03  ? 125 CYS A CA    1 
ATOM   187  C C     . CYS A 1 40  ? 124.383 109.381 145.312 1.00 42.74  ? 125 CYS A C     1 
ATOM   188  O O     . CYS A 1 40  ? 124.425 109.323 144.077 1.00 46.11  ? 125 CYS A O     1 
ATOM   189  C CB    . CYS A 1 40  ? 125.261 107.332 146.445 1.00 44.60  ? 125 CYS A CB    1 
ATOM   190  S SG    . CYS A 1 40  ? 126.579 106.496 147.358 1.00 54.18  ? 125 CYS A SG    1 
ATOM   191  N N     . ILE A 1 41  ? 123.358 109.926 145.968 1.00 44.79  ? 126 ILE A N     1 
ATOM   192  C CA    . ILE A 1 41  ? 122.219 110.481 145.246 1.00 43.47  ? 126 ILE A CA    1 
ATOM   193  C C     . ILE A 1 41  ? 122.638 111.719 144.461 1.00 40.24  ? 126 ILE A C     1 
ATOM   194  O O     . ILE A 1 41  ? 122.321 111.858 143.273 1.00 41.52  ? 126 ILE A O     1 
ATOM   195  C CB    . ILE A 1 41  ? 121.068 110.784 146.222 1.00 44.85  ? 126 ILE A CB    1 
ATOM   196  C CG1   . ILE A 1 41  ? 120.293 109.505 146.538 1.00 45.63  ? 126 ILE A CG1   1 
ATOM   197  C CG2   . ILE A 1 41  ? 120.134 111.823 145.644 1.00 42.20  ? 126 ILE A CG2   1 
ATOM   198  C CD1   . ILE A 1 41  ? 119.204 109.690 147.567 1.00 49.47  ? 126 ILE A CD1   1 
ATOM   199  N N     . LEU A 1 42  ? 123.365 112.632 145.106 1.00 39.71  ? 127 LEU A N     1 
ATOM   200  C CA    . LEU A 1 42  ? 123.871 113.810 144.414 1.00 42.59  ? 127 LEU A CA    1 
ATOM   201  C C     . LEU A 1 42  ? 125.089 113.511 143.552 1.00 43.60  ? 127 LEU A C     1 
ATOM   202  O O     . LEU A 1 42  ? 125.464 114.352 142.727 1.00 44.47  ? 127 LEU A O     1 
ATOM   203  C CB    . LEU A 1 42  ? 124.202 114.919 145.418 1.00 47.56  ? 127 LEU A CB    1 
ATOM   204  C CG    . LEU A 1 42  ? 123.028 115.835 145.774 1.00 40.59  ? 127 LEU A CG    1 
ATOM   205  C CD1   . LEU A 1 42  ? 123.496 117.042 146.566 1.00 45.92  ? 127 LEU A CD1   1 
ATOM   206  C CD2   . LEU A 1 42  ? 122.303 116.277 144.515 1.00 43.20  ? 127 LEU A CD2   1 
ATOM   207  N N     . PHE A 1 43  ? 125.720 112.348 143.726 1.00 47.03  ? 128 PHE A N     1 
ATOM   208  C CA    . PHE A 1 43  ? 126.750 111.921 142.786 1.00 40.40  ? 128 PHE A CA    1 
ATOM   209  C C     . PHE A 1 43  ? 126.137 111.598 141.429 1.00 40.09  ? 128 PHE A C     1 
ATOM   210  O O     . PHE A 1 43  ? 126.660 112.006 140.385 1.00 44.79  ? 128 PHE A O     1 
ATOM   211  C CB    . PHE A 1 43  ? 127.502 110.712 143.345 1.00 39.13  ? 128 PHE A CB    1 
ATOM   212  C CG    . PHE A 1 43  ? 128.803 110.425 142.646 1.00 42.92  ? 128 PHE A CG    1 
ATOM   213  C CD1   . PHE A 1 43  ? 128.825 109.732 141.446 1.00 46.67  ? 128 PHE A CD1   1 
ATOM   214  C CD2   . PHE A 1 43  ? 130.005 110.844 143.193 1.00 42.13  ? 128 PHE A CD2   1 
ATOM   215  C CE1   . PHE A 1 43  ? 130.019 109.467 140.804 1.00 42.24  ? 128 PHE A CE1   1 
ATOM   216  C CE2   . PHE A 1 43  ? 131.202 110.580 142.555 1.00 45.56  ? 128 PHE A CE2   1 
ATOM   217  C CZ    . PHE A 1 43  ? 131.209 109.891 141.359 1.00 44.13  ? 128 PHE A CZ    1 
ATOM   218  N N     . ASN A 1 44  ? 125.024 110.860 141.428 1.00 42.32  ? 129 ASN A N     1 
ATOM   219  C CA    . ASN A 1 44  ? 124.332 110.561 140.178 1.00 37.09  ? 129 ASN A CA    1 
ATOM   220  C C     . ASN A 1 44  ? 123.764 111.823 139.545 1.00 39.69  ? 129 ASN A C     1 
ATOM   221  O O     . ASN A 1 44  ? 123.883 112.023 138.331 1.00 44.41  ? 129 ASN A O     1 
ATOM   222  C CB    . ASN A 1 44  ? 123.221 109.541 140.425 1.00 39.47  ? 129 ASN A CB    1 
ATOM   223  C CG    . ASN A 1 44  ? 123.729 108.116 140.425 1.00 44.48  ? 129 ASN A CG    1 
ATOM   224  O OD1   . ASN A 1 44  ? 124.935 107.878 140.433 1.00 51.82  ? 129 ASN A OD1   1 
ATOM   225  N ND2   . ASN A 1 44  ? 122.810 107.158 140.417 1.00 43.17  ? 129 ASN A ND2   1 
ATOM   226  N N     . TYR A 1 45  ? 123.150 112.691 140.353 1.00 42.77  ? 130 TYR A N     1 
ATOM   227  C CA    . TYR A 1 45  ? 122.532 113.897 139.810 1.00 40.57  ? 130 TYR A CA    1 
ATOM   228  C C     . TYR A 1 45  ? 123.567 114.813 139.173 1.00 38.03  ? 130 TYR A C     1 
ATOM   229  O O     . TYR A 1 45  ? 123.293 115.450 138.149 1.00 46.71  ? 130 TYR A O     1 
ATOM   230  C CB    . TYR A 1 45  ? 121.762 114.638 140.901 1.00 43.60  ? 130 TYR A CB    1 
ATOM   231  C CG    . TYR A 1 45  ? 120.863 115.721 140.355 1.00 46.99  ? 130 TYR A CG    1 
ATOM   232  C CD1   . TYR A 1 45  ? 120.101 115.503 139.216 1.00 45.15  ? 130 TYR A CD1   1 
ATOM   233  C CD2   . TYR A 1 45  ? 120.778 116.961 140.973 1.00 41.87  ? 130 TYR A CD2   1 
ATOM   234  C CE1   . TYR A 1 45  ? 119.280 116.489 138.707 1.00 49.07  ? 130 TYR A CE1   1 
ATOM   235  C CE2   . TYR A 1 45  ? 119.958 117.953 140.472 1.00 44.13  ? 130 TYR A CE2   1 
ATOM   236  C CZ    . TYR A 1 45  ? 119.211 117.711 139.339 1.00 55.73  ? 130 TYR A CZ    1 
ATOM   237  O OH    . TYR A 1 45  ? 118.391 118.693 138.833 1.00 66.21  ? 130 TYR A OH    1 
ATOM   238  N N     . THR A 1 46  ? 124.760 114.896 139.765 1.00 39.99  ? 131 THR A N     1 
ATOM   239  C CA    . THR A 1 46  ? 125.824 115.694 139.167 1.00 38.97  ? 131 THR A CA    1 
ATOM   240  C C     . THR A 1 46  ? 126.209 115.162 137.793 1.00 43.19  ? 131 THR A C     1 
ATOM   241  O O     . THR A 1 46  ? 126.470 115.947 136.874 1.00 48.51  ? 131 THR A O     1 
ATOM   242  C CB    . THR A 1 46  ? 127.040 115.718 140.094 1.00 44.19  ? 131 THR A CB    1 
ATOM   243  O OG1   . THR A 1 46  ? 126.643 116.177 141.392 1.00 47.06  ? 131 THR A OG1   1 
ATOM   244  C CG2   . THR A 1 46  ? 128.113 116.639 139.544 1.00 40.92  ? 131 THR A CG2   1 
ATOM   245  N N     . ILE A 1 47  ? 126.247 113.840 137.633 1.00 45.40  ? 132 ILE A N     1 
ATOM   246  C CA    . ILE A 1 47  ? 126.486 113.258 136.317 1.00 40.64  ? 132 ILE A CA    1 
ATOM   247  C C     . ILE A 1 47  ? 125.287 113.482 135.403 1.00 41.89  ? 132 ILE A C     1 
ATOM   248  O O     . ILE A 1 47  ? 125.444 113.844 134.232 1.00 47.52  ? 132 ILE A O     1 
ATOM   249  C CB    . ILE A 1 47  ? 126.821 111.761 136.454 1.00 43.87  ? 132 ILE A CB    1 
ATOM   250  C CG1   . ILE A 1 47  ? 128.197 111.575 137.096 1.00 45.62  ? 132 ILE A CG1   1 
ATOM   251  C CG2   . ILE A 1 47  ? 126.766 111.071 135.098 1.00 46.92  ? 132 ILE A CG2   1 
ATOM   252  C CD1   . ILE A 1 47  ? 128.699 110.147 137.069 1.00 47.14  ? 132 ILE A CD1   1 
ATOM   253  N N     . LEU A 1 48  ? 124.073 113.281 135.923 1.00 41.31  ? 133 LEU A N     1 
ATOM   254  C CA    . LEU A 1 48  ? 122.877 113.335 135.089 1.00 39.13  ? 133 LEU A CA    1 
ATOM   255  C C     . LEU A 1 48  ? 122.544 114.758 134.656 1.00 37.81  ? 133 LEU A C     1 
ATOM   256  O O     . LEU A 1 48  ? 122.318 115.014 133.468 1.00 47.81  ? 133 LEU A O     1 
ATOM   257  C CB    . LEU A 1 48  ? 121.695 112.716 135.836 1.00 40.13  ? 133 LEU A CB    1 
ATOM   258  C CG    . LEU A 1 48  ? 121.805 111.215 136.100 1.00 35.85  ? 133 LEU A CG    1 
ATOM   259  C CD1   . LEU A 1 48  ? 120.675 110.748 137.001 1.00 37.36  ? 133 LEU A CD1   1 
ATOM   260  C CD2   . LEU A 1 48  ? 121.825 110.439 134.795 1.00 40.00  ? 133 LEU A CD2   1 
ATOM   261  N N     . ARG A 1 49  ? 122.506 115.700 135.603 1.00 36.17  ? 134 ARG A N     1 
ATOM   262  C CA    . ARG A 1 49  ? 122.150 117.071 135.255 1.00 40.59  ? 134 ARG A CA    1 
ATOM   263  C C     . ARG A 1 49  ? 123.213 117.738 134.393 1.00 47.26  ? 134 ARG A C     1 
ATOM   264  O O     . ARG A 1 49  ? 122.909 118.717 133.703 1.00 53.26  ? 134 ARG A O     1 
ATOM   265  C CB    . ARG A 1 49  ? 121.895 117.896 136.519 1.00 42.26  ? 134 ARG A CB    1 
ATOM   266  C CG    . ARG A 1 49  ? 123.138 118.498 137.153 1.00 40.82  ? 134 ARG A CG    1 
ATOM   267  C CD    . ARG A 1 49  ? 122.767 119.407 138.313 1.00 46.44  ? 134 ARG A CD    1 
ATOM   268  N NE    . ARG A 1 49  ? 122.190 120.665 137.854 1.00 51.04  ? 134 ARG A NE    1 
ATOM   269  C CZ    . ARG A 1 49  ? 121.290 121.369 138.528 1.00 56.31  ? 134 ARG A CZ    1 
ATOM   270  N NH1   . ARG A 1 49  ? 120.838 120.967 139.704 1.00 56.27  ? 134 ARG A NH1   1 
ATOM   271  N NH2   . ARG A 1 49  ? 120.833 122.504 138.008 1.00 60.18  ? 134 ARG A NH2   1 
ATOM   272  N N     . ASP A 1 50  ? 124.447 117.233 134.418 1.00 46.12  ? 135 ASP A N     1 
ATOM   273  C CA    . ASP A 1 50  ? 125.463 117.704 133.485 1.00 48.21  ? 135 ASP A CA    1 
ATOM   274  C C     . ASP A 1 50  ? 125.273 117.072 132.112 1.00 49.59  ? 135 ASP A C     1 
ATOM   275  O O     . ASP A 1 50  ? 125.315 117.764 131.090 1.00 50.42  ? 135 ASP A O     1 
ATOM   276  C CB    . ASP A 1 50  ? 126.859 117.395 134.026 1.00 45.12  ? 135 ASP A CB    1 
ATOM   277  C CG    . ASP A 1 50  ? 127.280 118.345 135.128 1.00 56.75  ? 135 ASP A CG    1 
ATOM   278  O OD1   . ASP A 1 50  ? 126.482 119.236 135.486 1.00 56.57  ? 135 ASP A OD1   1 
ATOM   279  O OD2   . ASP A 1 50  ? 128.410 118.199 135.639 1.00 64.18  ? 135 ASP A OD2   1 
ATOM   280  N N     . THR A 1 51  ? 125.051 115.755 132.076 1.00 49.04  ? 136 THR A N     1 
ATOM   281  C CA    . THR A 1 51  ? 124.896 115.053 130.806 1.00 44.82  ? 136 THR A CA    1 
ATOM   282  C C     . THR A 1 51  ? 123.635 115.484 130.069 1.00 44.43  ? 136 THR A C     1 
ATOM   283  O O     . THR A 1 51  ? 123.640 115.569 128.835 1.00 49.68  ? 136 THR A O     1 
ATOM   284  C CB    . THR A 1 51  ? 124.882 113.541 131.041 1.00 46.46  ? 136 THR A CB    1 
ATOM   285  O OG1   . THR A 1 51  ? 126.054 113.159 131.772 1.00 51.23  ? 136 THR A OG1   1 
ATOM   286  C CG2   . THR A 1 51  ? 124.857 112.790 129.717 1.00 53.33  ? 136 THR A CG2   1 
ATOM   287  N N     . LYS A 1 52  ? 122.551 115.764 130.800 1.00 45.16  ? 137 LYS A N     1 
ATOM   288  C CA    . LYS A 1 52  ? 121.302 116.140 130.147 1.00 41.83  ? 137 LYS A CA    1 
ATOM   289  C C     . LYS A 1 52  ? 121.437 117.451 129.380 1.00 47.61  ? 137 LYS A C     1 
ATOM   290  O O     . LYS A 1 52  ? 120.790 117.625 128.342 1.00 49.09  ? 137 LYS A O     1 
ATOM   291  C CB    . LYS A 1 52  ? 120.172 116.226 131.178 1.00 42.44  ? 137 LYS A CB    1 
ATOM   292  C CG    . LYS A 1 52  ? 120.189 117.471 132.048 1.00 41.47  ? 137 LYS A CG    1 
ATOM   293  C CD    . LYS A 1 52  ? 118.914 117.593 132.862 1.00 39.37  ? 137 LYS A CD    1 
ATOM   294  C CE    . LYS A 1 52  ? 119.030 118.697 133.899 1.00 44.15  ? 137 LYS A CE    1 
ATOM   295  N NZ    . LYS A 1 52  ? 119.628 119.933 133.323 1.00 46.32  ? 137 LYS A NZ    1 
ATOM   296  N N     . ASP A 1 53  ? 122.266 118.378 129.865 1.00 50.53  ? 138 ASP A N     1 
ATOM   297  C CA    . ASP A 1 53  ? 122.531 119.598 129.111 1.00 48.81  ? 138 ASP A CA    1 
ATOM   298  C C     . ASP A 1 53  ? 123.458 119.332 127.933 1.00 47.98  ? 138 ASP A C     1 
ATOM   299  O O     . ASP A 1 53  ? 123.255 119.881 126.846 1.00 46.75  ? 138 ASP A O     1 
ATOM   300  C CB    . ASP A 1 53  ? 123.119 120.670 130.029 1.00 53.29  ? 138 ASP A CB    1 
ATOM   301  C CG    . ASP A 1 53  ? 122.113 121.185 131.038 1.00 67.59  ? 138 ASP A CG    1 
ATOM   302  O OD1   . ASP A 1 53  ? 120.903 121.173 130.730 1.00 65.92  ? 138 ASP A OD1   1 
ATOM   303  O OD2   . ASP A 1 53  ? 122.531 121.599 132.139 1.00 74.26  ? 138 ASP A OD2   1 
ATOM   304  N N     . VAL A 1 54  ? 124.478 118.493 128.129 1.00 52.29  ? 139 VAL A N     1 
ATOM   305  C CA    . VAL A 1 54  ? 125.352 118.102 127.025 1.00 52.48  ? 139 VAL A CA    1 
ATOM   306  C C     . VAL A 1 54  ? 124.551 117.421 125.928 1.00 51.68  ? 139 VAL A C     1 
ATOM   307  O O     . VAL A 1 54  ? 124.879 117.530 124.740 1.00 59.68  ? 139 VAL A O     1 
ATOM   308  C CB    . VAL A 1 54  ? 126.481 117.185 127.542 1.00 51.70  ? 139 VAL A CB    1 
ATOM   309  C CG1   . VAL A 1 54  ? 127.389 116.756 126.404 1.00 52.07  ? 139 VAL A CG1   1 
ATOM   310  C CG2   . VAL A 1 54  ? 127.274 117.873 128.634 1.00 49.33  ? 139 VAL A CG2   1 
ATOM   311  N N     . LEU A 1 55  ? 123.479 116.727 126.304 1.00 48.47  ? 140 LEU A N     1 
ATOM   312  C CA    . LEU A 1 55  ? 122.753 115.886 125.363 1.00 44.65  ? 140 LEU A CA    1 
ATOM   313  C C     . LEU A 1 55  ? 121.809 116.693 124.478 1.00 45.71  ? 140 LEU A C     1 
ATOM   314  O O     . LEU A 1 55  ? 121.740 116.457 123.267 1.00 54.38  ? 140 LEU A O     1 
ATOM   315  C CB    . LEU A 1 55  ? 121.981 114.820 126.134 1.00 44.80  ? 140 LEU A CB    1 
ATOM   316  C CG    . LEU A 1 55  ? 121.703 113.500 125.427 1.00 47.25  ? 140 LEU A CG    1 
ATOM   317  C CD1   . LEU A 1 55  ? 123.003 112.817 125.033 1.00 45.55  ? 140 LEU A CD1   1 
ATOM   318  C CD2   . LEU A 1 55  ? 120.889 112.625 126.348 1.00 45.10  ? 140 LEU A CD2   1 
ATOM   319  N N     . VAL A 1 56  ? 121.076 117.642 125.056 1.00 44.77  ? 141 VAL A N     1 
ATOM   320  C CA    . VAL A 1 56  ? 120.074 118.370 124.285 1.00 45.38  ? 141 VAL A CA    1 
ATOM   321  C C     . VAL A 1 56  ? 120.625 119.667 123.698 1.00 45.44  ? 141 VAL A C     1 
ATOM   322  O O     . VAL A 1 56  ? 120.105 120.156 122.690 1.00 50.30  ? 141 VAL A O     1 
ATOM   323  C CB    . VAL A 1 56  ? 118.828 118.649 125.144 1.00 44.92  ? 141 VAL A CB    1 
ATOM   324  C CG1   . VAL A 1 56  ? 118.164 117.344 125.561 1.00 47.42  ? 141 VAL A CG1   1 
ATOM   325  C CG2   . VAL A 1 56  ? 119.186 119.497 126.356 1.00 48.39  ? 141 VAL A CG2   1 
ATOM   326  N N     . VAL A 1 57  ? 121.666 120.239 124.302 1.00 46.87  ? 142 VAL A N     1 
ATOM   327  C CA    . VAL A 1 57  ? 122.177 121.520 123.827 1.00 50.20  ? 142 VAL A CA    1 
ATOM   328  C C     . VAL A 1 57  ? 123.178 121.320 122.694 1.00 49.86  ? 142 VAL A C     1 
ATOM   329  O O     . VAL A 1 57  ? 123.161 122.056 121.702 1.00 56.71  ? 142 VAL A O     1 
ATOM   330  C CB    . VAL A 1 57  ? 122.788 122.311 124.998 1.00 48.54  ? 142 VAL A CB    1 
ATOM   331  C CG1   . VAL A 1 57  ? 123.496 123.553 124.498 1.00 49.39  ? 142 VAL A CG1   1 
ATOM   332  C CG2   . VAL A 1 57  ? 121.711 122.677 126.009 1.00 43.76  ? 142 VAL A CG2   1 
ATOM   333  N N     . THR A 1 58  ? 124.050 120.320 122.808 1.00 52.75  ? 143 THR A N     1 
ATOM   334  C CA    . THR A 1 58  ? 125.111 120.096 121.836 1.00 52.88  ? 143 THR A CA    1 
ATOM   335  C C     . THR A 1 58  ? 124.746 119.059 120.781 1.00 54.87  ? 143 THR A C     1 
ATOM   336  O O     . THR A 1 58  ? 125.626 118.614 120.037 1.00 64.34  ? 143 THR A O     1 
ATOM   337  C CB    . THR A 1 58  ? 126.401 119.678 122.542 1.00 53.84  ? 143 THR A CB    1 
ATOM   338  O OG1   . THR A 1 58  ? 126.197 118.434 123.223 1.00 58.90  ? 143 THR A OG1   1 
ATOM   339  C CG2   . THR A 1 58  ? 126.819 120.735 123.544 1.00 52.81  ? 143 THR A CG2   1 
ATOM   340  N N     . ALA A 1 59  ? 123.480 118.661 120.699 1.00 51.73  ? 144 ALA A N     1 
ATOM   341  C CA    . ALA A 1 59  ? 123.062 117.762 119.637 1.00 51.83  ? 144 ALA A CA    1 
ATOM   342  C C     . ALA A 1 59  ? 123.021 118.507 118.304 1.00 55.06  ? 144 ALA A C     1 
ATOM   343  O O     . ALA A 1 59  ? 123.087 119.738 118.243 1.00 59.32  ? 144 ALA A O     1 
ATOM   344  C CB    . ALA A 1 59  ? 121.699 117.150 119.955 1.00 45.87  ? 144 ALA A CB    1 
ATOM   345  N N     . LYS A 1 60  ? 122.919 117.742 117.222 1.00 55.67  ? 145 LYS A N     1 
ATOM   346  C CA    . LYS A 1 60  ? 122.903 118.304 115.878 1.00 53.85  ? 145 LYS A CA    1 
ATOM   347  C C     . LYS A 1 60  ? 121.485 118.750 115.542 1.00 58.64  ? 145 LYS A C     1 
ATOM   348  O O     . LYS A 1 60  ? 120.543 117.953 115.618 1.00 60.35  ? 145 LYS A O     1 
ATOM   349  C CB    . LYS A 1 60  ? 123.410 117.285 114.859 1.00 58.82  ? 145 LYS A CB    1 
ATOM   350  C CG    . LYS A 1 60  ? 124.903 117.016 114.952 1.00 64.91  ? 145 LYS A CG    1 
ATOM   351  C CD    . LYS A 1 60  ? 125.716 118.241 114.567 1.00 68.36  ? 145 LYS A CD    1 
ATOM   352  C CE    . LYS A 1 60  ? 127.192 117.901 114.433 1.00 66.11  ? 145 LYS A CE    1 
ATOM   353  N NZ    . LYS A 1 60  ? 128.026 119.114 114.214 1.00 69.77  ? 145 LYS A NZ    1 
ATOM   354  N N     . GLY A 1 61  ? 121.336 120.020 115.167 1.00 55.82  ? 146 GLY A N     1 
ATOM   355  C CA    . GLY A 1 61  ? 120.037 120.595 114.899 1.00 54.70  ? 146 GLY A CA    1 
ATOM   356  C C     . GLY A 1 61  ? 119.363 121.234 116.093 1.00 57.11  ? 146 GLY A C     1 
ATOM   357  O O     . GLY A 1 61  ? 118.290 121.830 115.933 1.00 59.09  ? 146 GLY A O     1 
ATOM   358  N N     . SER A 1 62  ? 119.952 121.131 117.281 1.00 61.71  ? 147 SER A N     1 
ATOM   359  C CA    . SER A 1 62  ? 119.404 121.727 118.487 1.00 56.48  ? 147 SER A CA    1 
ATOM   360  C C     . SER A 1 62  ? 120.364 122.779 119.025 1.00 56.35  ? 147 SER A C     1 
ATOM   361  O O     . SER A 1 62  ? 121.548 122.806 118.682 1.00 54.26  ? 147 SER A O     1 
ATOM   362  C CB    . SER A 1 62  ? 119.137 120.669 119.566 1.00 52.58  ? 147 SER A CB    1 
ATOM   363  O OG    . SER A 1 62  ? 120.336 120.021 119.948 1.00 56.70  ? 147 SER A OG    1 
ATOM   364  N N     . SER A 1 63  ? 119.831 123.650 119.876 1.00 59.32  ? 148 SER A N     1 
ATOM   365  C CA    . SER A 1 63  ? 120.606 124.701 120.520 1.00 52.21  ? 148 SER A CA    1 
ATOM   366  C C     . SER A 1 63  ? 120.197 124.743 121.987 1.00 52.13  ? 148 SER A C     1 
ATOM   367  O O     . SER A 1 63  ? 119.543 123.828 122.494 1.00 54.95  ? 148 SER A O     1 
ATOM   368  C CB    . SER A 1 63  ? 120.392 126.047 119.815 1.00 55.54  ? 148 SER A CB    1 
ATOM   369  O OG    . SER A 1 63  ? 119.055 126.493 119.965 1.00 59.32  ? 148 SER A OG    1 
ATOM   370  N N     . ALA A 1 64  ? 120.592 125.806 122.681 1.00 49.41  ? 149 ALA A N     1 
ATOM   371  C CA    . ALA A 1 64  ? 120.121 126.014 124.043 1.00 45.90  ? 149 ALA A CA    1 
ATOM   372  C C     . ALA A 1 64  ? 118.734 126.637 124.088 1.00 44.77  ? 149 ALA A C     1 
ATOM   373  O O     . ALA A 1 64  ? 118.197 126.840 125.183 1.00 48.58  ? 149 ALA A O     1 
ATOM   374  C CB    . ALA A 1 64  ? 121.106 126.883 124.823 1.00 47.22  ? 149 ALA A CB    1 
ATOM   375  N N     . GLU A 1 65  ? 118.149 126.952 122.934 1.00 45.60  ? 150 GLU A N     1 
ATOM   376  C CA    . GLU A 1 65  ? 116.777 127.434 122.870 1.00 44.32  ? 150 GLU A CA    1 
ATOM   377  C C     . GLU A 1 65  ? 115.757 126.304 122.931 1.00 42.58  ? 150 GLU A C     1 
ATOM   378  O O     . GLU A 1 65  ? 114.553 126.580 122.955 1.00 43.62  ? 150 GLU A O     1 
ATOM   379  C CB    . GLU A 1 65  ? 116.572 128.268 121.601 1.00 47.08  ? 150 GLU A CB    1 
ATOM   380  C CG    . GLU A 1 65  ? 117.355 129.574 121.604 1.00 51.14  ? 150 GLU A CG    1 
ATOM   381  C CD    . GLU A 1 65  ? 117.161 130.383 120.337 1.00 70.97  ? 150 GLU A CD    1 
ATOM   382  O OE1   . GLU A 1 65  ? 116.515 129.875 119.396 1.00 76.23  ? 150 GLU A OE1   1 
ATOM   383  O OE2   . GLU A 1 65  ? 117.654 131.529 120.283 1.00 67.78  ? 150 GLU A OE2   1 
ATOM   384  N N     . ILE A 1 66  ? 116.206 125.046 122.942 1.00 42.17  ? 151 ILE A N     1 
ATOM   385  C CA    . ILE A 1 66  ? 115.313 123.936 123.261 1.00 42.10  ? 151 ILE A CA    1 
ATOM   386  C C     . ILE A 1 66  ? 114.919 123.944 124.733 1.00 43.29  ? 151 ILE A C     1 
ATOM   387  O O     . ILE A 1 66  ? 113.824 123.483 125.078 1.00 45.27  ? 151 ILE A O     1 
ATOM   388  C CB    . ILE A 1 66  ? 115.955 122.585 122.891 1.00 41.41  ? 151 ILE A CB    1 
ATOM   389  C CG1   . ILE A 1 66  ? 114.929 121.454 122.985 1.00 38.67  ? 151 ILE A CG1   1 
ATOM   390  C CG2   . ILE A 1 66  ? 117.147 122.279 123.783 1.00 42.44  ? 151 ILE A CG2   1 
ATOM   391  C CD1   . ILE A 1 66  ? 115.381 120.166 122.340 1.00 44.16  ? 151 ILE A CD1   1 
ATOM   392  N N     . ILE A 1 67  ? 115.781 124.463 125.604 1.00 43.68  ? 152 ILE A N     1 
ATOM   393  C CA    . ILE A 1 67  ? 115.577 124.455 127.051 1.00 41.53  ? 152 ILE A CA    1 
ATOM   394  C C     . ILE A 1 67  ? 114.309 125.216 127.435 1.00 45.71  ? 152 ILE A C     1 
ATOM   395  O O     . ILE A 1 67  ? 113.548 124.723 128.280 1.00 53.81  ? 152 ILE A O     1 
ATOM   396  C CB    . ILE A 1 67  ? 116.809 125.017 127.779 1.00 40.20  ? 152 ILE A CB    1 
ATOM   397  C CG1   . ILE A 1 67  ? 118.073 124.313 127.284 1.00 44.53  ? 152 ILE A CG1   1 
ATOM   398  C CG2   . ILE A 1 67  ? 116.664 124.847 129.282 1.00 45.75  ? 152 ILE A CG2   1 
ATOM   399  C CD1   . ILE A 1 67  ? 119.348 124.905 127.822 1.00 46.65  ? 152 ILE A CD1   1 
ATOM   400  N N     . PRO A 1 68  ? 114.033 126.406 126.879 1.00 42.43  ? 153 PRO A N     1 
ATOM   401  C CA    . PRO A 1 68  ? 112.740 127.044 127.178 1.00 38.93  ? 153 PRO A CA    1 
ATOM   402  C C     . PRO A 1 68  ? 111.544 126.190 126.803 1.00 40.62  ? 153 PRO A C     1 
ATOM   403  O O     . PRO A 1 68  ? 110.512 126.247 127.484 1.00 45.42  ? 153 PRO A O     1 
ATOM   404  C CB    . PRO A 1 68  ? 112.789 128.336 126.352 1.00 36.69  ? 153 PRO A CB    1 
ATOM   405  C CG    . PRO A 1 68  ? 114.223 128.650 126.251 1.00 43.75  ? 153 PRO A CG    1 
ATOM   406  C CD    . PRO A 1 68  ? 114.920 127.325 126.138 1.00 43.64  ? 153 PRO A CD    1 
ATOM   407  N N     . PHE A 1 69  ? 111.649 125.395 125.742 1.00 44.59  ? 154 PHE A N     1 
ATOM   408  C CA    . PHE A 1 69  ? 110.546 124.547 125.315 1.00 42.12  ? 154 PHE A CA    1 
ATOM   409  C C     . PHE A 1 69  ? 110.588 123.169 125.960 1.00 43.66  ? 154 PHE A C     1 
ATOM   410  O O     . PHE A 1 69  ? 109.540 122.530 126.108 1.00 43.72  ? 154 PHE A O     1 
ATOM   411  C CB    . PHE A 1 69  ? 110.556 124.422 123.790 1.00 35.23  ? 154 PHE A CB    1 
ATOM   412  C CG    . PHE A 1 69  ? 110.366 125.732 123.080 1.00 33.81  ? 154 PHE A CG    1 
ATOM   413  C CD1   . PHE A 1 69  ? 111.454 126.536 122.783 1.00 33.76  ? 154 PHE A CD1   1 
ATOM   414  C CD2   . PHE A 1 69  ? 109.103 126.163 122.713 1.00 33.84  ? 154 PHE A CD2   1 
ATOM   415  C CE1   . PHE A 1 69  ? 111.288 127.745 122.138 1.00 33.89  ? 154 PHE A CE1   1 
ATOM   416  C CE2   . PHE A 1 69  ? 108.930 127.370 122.062 1.00 32.84  ? 154 PHE A CE2   1 
ATOM   417  C CZ    . PHE A 1 69  ? 110.024 128.161 121.773 1.00 34.16  ? 154 PHE A CZ    1 
ATOM   418  N N     . LEU A 1 70  ? 111.777 122.699 126.342 1.00 44.57  ? 155 LEU A N     1 
ATOM   419  C CA    . LEU A 1 70  ? 111.885 121.449 127.087 1.00 43.04  ? 155 LEU A CA    1 
ATOM   420  C C     . LEU A 1 70  ? 111.200 121.554 128.443 1.00 45.41  ? 155 LEU A C     1 
ATOM   421  O O     . LEU A 1 70  ? 110.483 120.639 128.865 1.00 51.36  ? 155 LEU A O     1 
ATOM   422  C CB    . LEU A 1 70  ? 113.355 121.074 127.269 1.00 41.22  ? 155 LEU A CB    1 
ATOM   423  C CG    . LEU A 1 70  ? 113.969 120.085 126.283 1.00 40.92  ? 155 LEU A CG    1 
ATOM   424  C CD1   . LEU A 1 70  ? 115.479 120.058 126.433 1.00 37.11  ? 155 LEU A CD1   1 
ATOM   425  C CD2   . LEU A 1 70  ? 113.385 118.713 126.538 1.00 37.81  ? 155 LEU A CD2   1 
ATOM   426  N N     . LYS A 1 71  ? 111.414 122.669 129.143 1.00 45.11  ? 156 LYS A N     1 
ATOM   427  C CA    . LYS A 1 71  ? 110.987 122.762 130.533 1.00 44.94  ? 156 LYS A CA    1 
ATOM   428  C C     . LYS A 1 71  ? 109.484 122.967 130.662 1.00 45.97  ? 156 LYS A C     1 
ATOM   429  O O     . LYS A 1 71  ? 108.880 122.497 131.633 1.00 52.03  ? 156 LYS A O     1 
ATOM   430  C CB    . LYS A 1 71  ? 111.743 123.890 131.231 1.00 42.07  ? 156 LYS A CB    1 
ATOM   431  C CG    . LYS A 1 71  ? 113.205 123.567 131.486 1.00 45.96  ? 156 LYS A CG    1 
ATOM   432  C CD    . LYS A 1 71  ? 113.754 124.367 132.647 1.00 47.04  ? 156 LYS A CD    1 
ATOM   433  C CE    . LYS A 1 71  ? 115.125 123.870 133.060 1.00 49.08  ? 156 LYS A CE    1 
ATOM   434  N NZ    . LYS A 1 71  ? 115.061 122.521 133.684 1.00 49.13  ? 156 LYS A NZ    1 
ATOM   435  N N     . THR A 1 72  ? 108.863 123.659 129.708 1.00 43.49  ? 157 THR A N     1 
ATOM   436  C CA    . THR A 1 72  ? 107.449 123.993 129.823 1.00 43.35  ? 157 THR A CA    1 
ATOM   437  C C     . THR A 1 72  ? 106.535 122.919 129.243 1.00 46.50  ? 157 THR A C     1 
ATOM   438  O O     . THR A 1 72  ? 105.522 122.574 129.860 1.00 50.96  ? 157 THR A O     1 
ATOM   439  C CB    . THR A 1 72  ? 107.165 125.331 129.136 1.00 44.11  ? 157 THR A CB    1 
ATOM   440  O OG1   . THR A 1 72  ? 108.147 126.295 129.538 1.00 49.10  ? 157 THR A OG1   1 
ATOM   441  C CG2   . THR A 1 72  ? 105.782 125.839 129.515 1.00 43.06  ? 157 THR A CG2   1 
ATOM   442  N N     . TRP A 1 73  ? 106.867 122.380 128.070 1.00 49.01  ? 158 TRP A N     1 
ATOM   443  C CA    . TRP A 1 73  ? 105.980 121.449 127.385 1.00 49.38  ? 158 TRP A CA    1 
ATOM   444  C C     . TRP A 1 73  ? 106.348 119.988 127.587 1.00 51.60  ? 158 TRP A C     1 
ATOM   445  O O     . TRP A 1 73  ? 105.503 119.118 127.347 1.00 58.24  ? 158 TRP A O     1 
ATOM   446  C CB    . TRP A 1 73  ? 105.950 121.749 125.882 1.00 48.83  ? 158 TRP A CB    1 
ATOM   447  C CG    . TRP A 1 73  ? 105.679 123.183 125.575 1.00 49.85  ? 158 TRP A CG    1 
ATOM   448  C CD1   . TRP A 1 73  ? 106.522 124.062 124.964 1.00 47.93  ? 158 TRP A CD1   1 
ATOM   449  C CD2   . TRP A 1 73  ? 104.489 123.917 125.886 1.00 51.24  ? 158 TRP A CD2   1 
ATOM   450  N NE1   . TRP A 1 73  ? 105.926 125.295 124.861 1.00 48.45  ? 158 TRP A NE1   1 
ATOM   451  C CE2   . TRP A 1 73  ? 104.678 125.232 125.423 1.00 50.90  ? 158 TRP A CE2   1 
ATOM   452  C CE3   . TRP A 1 73  ? 103.280 123.587 126.507 1.00 53.97  ? 158 TRP A CE3   1 
ATOM   453  C CZ2   . TRP A 1 73  ? 103.704 126.219 125.559 1.00 54.81  ? 158 TRP A CZ2   1 
ATOM   454  C CZ3   . TRP A 1 73  ? 102.315 124.567 126.642 1.00 56.25  ? 158 TRP A CZ3   1 
ATOM   455  C CH2   . TRP A 1 73  ? 102.532 125.867 126.171 1.00 58.40  ? 158 TRP A CH2   1 
ATOM   456  N N     . VAL A 1 74  ? 107.576 119.692 128.009 1.00 51.50  ? 159 VAL A N     1 
ATOM   457  C CA    . VAL A 1 74  ? 108.028 118.325 128.231 1.00 50.33  ? 159 VAL A CA    1 
ATOM   458  C C     . VAL A 1 74  ? 108.347 118.075 129.700 1.00 48.58  ? 159 VAL A C     1 
ATOM   459  O O     . VAL A 1 74  ? 107.802 117.157 130.318 1.00 51.76  ? 159 VAL A O     1 
ATOM   460  C CB    . VAL A 1 74  ? 109.245 117.982 127.342 1.00 51.72  ? 159 VAL A CB    1 
ATOM   461  C CG1   . VAL A 1 74  ? 109.494 116.483 127.340 1.00 47.92  ? 159 VAL A CG1   1 
ATOM   462  C CG2   . VAL A 1 74  ? 109.032 118.493 125.926 1.00 51.21  ? 159 VAL A CG2   1 
ATOM   463  N N     . ASN A 1 75  ? 109.224 118.895 130.282 1.00 48.91  ? 160 ASN A N     1 
ATOM   464  C CA    . ASN A 1 75  ? 109.656 118.660 131.656 1.00 52.02  ? 160 ASN A CA    1 
ATOM   465  C C     . ASN A 1 75  ? 108.575 119.003 132.675 1.00 52.70  ? 160 ASN A C     1 
ATOM   466  O O     . ASN A 1 75  ? 108.522 118.383 133.743 1.00 63.06  ? 160 ASN A O     1 
ATOM   467  C CB    . ASN A 1 75  ? 110.930 119.458 131.945 1.00 50.59  ? 160 ASN A CB    1 
ATOM   468  C CG    . ASN A 1 75  ? 111.329 119.413 133.406 1.00 53.67  ? 160 ASN A CG    1 
ATOM   469  O OD1   . ASN A 1 75  ? 111.450 118.340 133.996 1.00 56.45  ? 160 ASN A OD1   1 
ATOM   470  N ND2   . ASN A 1 75  ? 111.541 120.583 133.997 1.00 57.87  ? 160 ASN A ND2   1 
ATOM   471  N N     . LEU A 1 76  ? 107.707 119.968 132.373 1.00 50.82  ? 161 LEU A N     1 
ATOM   472  C CA    . LEU A 1 76  ? 106.690 120.381 133.336 1.00 50.65  ? 161 LEU A CA    1 
ATOM   473  C C     . LEU A 1 76  ? 105.560 119.355 133.439 1.00 52.54  ? 161 LEU A C     1 
ATOM   474  O O     . LEU A 1 76  ? 105.246 118.917 134.553 1.00 54.87  ? 161 LEU A O     1 
ATOM   475  C CB    . LEU A 1 76  ? 106.135 121.765 132.982 1.00 50.03  ? 161 LEU A CB    1 
ATOM   476  C CG    . LEU A 1 76  ? 104.906 122.242 133.758 1.00 46.51  ? 161 LEU A CG    1 
ATOM   477  C CD1   . LEU A 1 76  ? 105.209 122.301 135.250 1.00 46.57  ? 161 LEU A CD1   1 
ATOM   478  C CD2   . LEU A 1 76  ? 104.434 123.595 133.250 1.00 45.00  ? 161 LEU A CD2   1 
ATOM   479  N N     . PRO A 1 77  ? 104.915 118.943 132.336 1.00 51.94  ? 162 PRO A N     1 
ATOM   480  C CA    . PRO A 1 77  ? 103.828 117.959 132.470 1.00 49.44  ? 162 PRO A CA    1 
ATOM   481  C C     . PRO A 1 77  ? 104.295 116.581 132.908 1.00 52.19  ? 162 PRO A C     1 
ATOM   482  O O     . PRO A 1 77  ? 103.497 115.837 133.491 1.00 55.08  ? 162 PRO A O     1 
ATOM   483  C CB    . PRO A 1 77  ? 103.212 117.922 131.067 1.00 48.17  ? 162 PRO A CB    1 
ATOM   484  C CG    . PRO A 1 77  ? 104.336 118.256 130.178 1.00 45.90  ? 162 PRO A CG    1 
ATOM   485  C CD    . PRO A 1 77  ? 105.127 119.300 130.918 1.00 50.97  ? 162 PRO A CD    1 
ATOM   486  N N     . MET A 1 78  ? 105.550 116.210 132.644 1.00 55.08  ? 163 MET A N     1 
ATOM   487  C CA    . MET A 1 78  ? 106.058 114.939 133.147 1.00 52.08  ? 163 MET A CA    1 
ATOM   488  C C     . MET A 1 78  ? 106.314 114.988 134.647 1.00 57.17  ? 163 MET A C     1 
ATOM   489  O O     . MET A 1 78  ? 106.232 113.953 135.319 1.00 57.45  ? 163 MET A O     1 
ATOM   490  C CB    . MET A 1 78  ? 107.334 114.538 132.402 1.00 50.50  ? 163 MET A CB    1 
ATOM   491  C CG    . MET A 1 78  ? 107.125 114.237 130.925 1.00 53.60  ? 163 MET A CG    1 
ATOM   492  S SD    . MET A 1 78  ? 105.996 112.865 130.624 1.00 87.47  ? 163 MET A SD    1 
ATOM   493  C CE    . MET A 1 78  ? 106.973 111.488 131.219 1.00 63.54  ? 163 MET A CE    1 
ATOM   494  N N     . ALA A 1 79  ? 106.632 116.167 135.186 1.00 54.82  ? 164 ALA A N     1 
ATOM   495  C CA    . ALA A 1 79  ? 106.732 116.317 136.632 1.00 50.99  ? 164 ALA A CA    1 
ATOM   496  C C     . ALA A 1 79  ? 105.357 116.265 137.287 1.00 57.59  ? 164 ALA A C     1 
ATOM   497  O O     . ALA A 1 79  ? 105.191 115.639 138.340 1.00 66.86  ? 164 ALA A O     1 
ATOM   498  C CB    . ALA A 1 79  ? 107.443 117.625 136.980 1.00 53.78  ? 164 ALA A CB    1 
ATOM   499  N N     . ILE A 1 80  ? 104.363 116.918 136.679 1.00 55.46  ? 165 ILE A N     1 
ATOM   500  C CA    . ILE A 1 80  ? 102.993 116.797 137.166 1.00 56.38  ? 165 ILE A CA    1 
ATOM   501  C C     . ILE A 1 80  ? 102.500 115.366 137.003 1.00 56.67  ? 165 ILE A C     1 
ATOM   502  O O     . ILE A 1 80  ? 101.820 114.831 137.886 1.00 62.27  ? 165 ILE A O     1 
ATOM   503  C CB    . ILE A 1 80  ? 102.072 117.797 136.442 1.00 55.76  ? 165 ILE A CB    1 
ATOM   504  C CG1   . ILE A 1 80  ? 102.528 119.233 136.705 1.00 55.63  ? 165 ILE A CG1   1 
ATOM   505  C CG2   . ILE A 1 80  ? 100.627 117.614 136.880 1.00 55.89  ? 165 ILE A CG2   1 
ATOM   506  C CD1   . ILE A 1 80  ? 102.297 120.162 135.537 1.00 54.78  ? 165 ILE A CD1   1 
ATOM   507  N N     . GLY A 1 81  ? 102.835 114.724 135.881 1.00 55.62  ? 166 GLY A N     1 
ATOM   508  C CA    . GLY A 1 81  ? 102.470 113.333 135.695 1.00 56.55  ? 166 GLY A CA    1 
ATOM   509  C C     . GLY A 1 81  ? 103.114 112.408 136.706 1.00 60.89  ? 166 GLY A C     1 
ATOM   510  O O     . GLY A 1 81  ? 102.508 111.412 137.113 1.00 68.32  ? 166 GLY A O     1 
ATOM   511  N N     . PHE A 1 82  ? 104.344 112.713 137.125 1.00 61.84  ? 167 PHE A N     1 
ATOM   512  C CA    . PHE A 1 82  ? 104.991 111.881 138.133 1.00 62.20  ? 167 PHE A CA    1 
ATOM   513  C C     . PHE A 1 82  ? 104.382 112.123 139.508 1.00 63.89  ? 167 PHE A C     1 
ATOM   514  O O     . PHE A 1 82  ? 104.186 111.173 140.275 1.00 68.11  ? 167 PHE A O     1 
ATOM   515  C CB    . PHE A 1 82  ? 106.503 112.137 138.143 1.00 58.80  ? 167 PHE A CB    1 
ATOM   516  C CG    . PHE A 1 82  ? 107.268 111.255 139.100 1.00 66.00  ? 167 PHE A CG    1 
ATOM   517  C CD1   . PHE A 1 82  ? 107.201 111.443 140.473 1.00 69.20  ? 167 PHE A CD1   1 
ATOM   518  C CD2   . PHE A 1 82  ? 108.041 110.215 138.614 1.00 64.02  ? 167 PHE A CD2   1 
ATOM   519  C CE1   . PHE A 1 82  ? 107.889 110.618 141.332 1.00 65.05  ? 167 PHE A CE1   1 
ATOM   520  C CE2   . PHE A 1 82  ? 108.737 109.390 139.472 1.00 61.73  ? 167 PHE A CE2   1 
ATOM   521  C CZ    . PHE A 1 82  ? 108.660 109.592 140.831 1.00 63.14  ? 167 PHE A CZ    1 
ATOM   522  N N     . MET A 1 83  ? 104.085 113.385 139.836 1.00 62.22  ? 168 MET A N     1 
ATOM   523  C CA    . MET A 1 83  ? 103.402 113.689 141.091 1.00 66.04  ? 168 MET A CA    1 
ATOM   524  C C     . MET A 1 83  ? 102.143 112.854 141.266 1.00 69.48  ? 168 MET A C     1 
ATOM   525  O O     . MET A 1 83  ? 101.931 112.250 142.325 1.00 75.07  ? 168 MET A O     1 
ATOM   526  C CB    . MET A 1 83  ? 103.041 115.170 141.154 1.00 70.99  ? 168 MET A CB    1 
ATOM   527  C CG    . MET A 1 83  ? 102.403 115.543 142.470 1.00 84.30  ? 168 MET A CG    1 
ATOM   528  S SD    . MET A 1 83  ? 102.023 117.285 142.675 1.00 113.20 ? 168 MET A SD    1 
ATOM   529  C CE    . MET A 1 83  ? 101.219 117.210 144.269 1.00 101.21 ? 168 MET A CE    1 
ATOM   530  N N     . LEU A 1 84  ? 101.290 112.815 140.243 1.00 68.00  ? 169 LEU A N     1 
ATOM   531  C CA    . LEU A 1 84  ? 100.050 112.058 140.351 1.00 69.41  ? 169 LEU A CA    1 
ATOM   532  C C     . LEU A 1 84  ? 100.325 110.563 140.440 1.00 67.47  ? 169 LEU A C     1 
ATOM   533  O O     . LEU A 1 84  ? 99.639  109.844 141.175 1.00 71.84  ? 169 LEU A O     1 
ATOM   534  C CB    . LEU A 1 84  ? 99.140  112.379 139.166 1.00 66.29  ? 169 LEU A CB    1 
ATOM   535  C CG    . LEU A 1 84  ? 98.872  113.873 138.962 1.00 65.32  ? 169 LEU A CG    1 
ATOM   536  C CD1   . LEU A 1 84  ? 98.562  114.177 137.503 1.00 62.08  ? 169 LEU A CD1   1 
ATOM   537  C CD2   . LEU A 1 84  ? 97.751  114.359 139.871 1.00 71.53  ? 169 LEU A CD2   1 
ATOM   538  N N     . LEU A 1 85  ? 101.323 110.077 139.698 1.00 66.94  ? 170 LEU A N     1 
ATOM   539  C CA    . LEU A 1 85  ? 101.673 108.663 139.770 1.00 66.84  ? 170 LEU A CA    1 
ATOM   540  C C     . LEU A 1 85  ? 102.300 108.314 141.115 1.00 70.85  ? 170 LEU A C     1 
ATOM   541  O O     . LEU A 1 85  ? 101.975 107.277 141.705 1.00 75.59  ? 170 LEU A O     1 
ATOM   542  C CB    . LEU A 1 85  ? 102.617 108.295 138.626 1.00 66.59  ? 170 LEU A CB    1 
ATOM   543  C CG    . LEU A 1 85  ? 103.143 106.859 138.629 1.00 71.77  ? 170 LEU A CG    1 
ATOM   544  C CD1   . LEU A 1 85  ? 101.994 105.865 138.546 1.00 68.98  ? 170 LEU A CD1   1 
ATOM   545  C CD2   . LEU A 1 85  ? 104.126 106.641 137.488 1.00 78.75  ? 170 LEU A CD2   1 
ATOM   546  N N     . TYR A 1 86  ? 103.200 109.165 141.615 1.00 70.22  ? 171 TYR A N     1 
ATOM   547  C CA    . TYR A 1 86  ? 103.831 108.897 142.903 1.00 68.80  ? 171 TYR A CA    1 
ATOM   548  C C     . TYR A 1 86  ? 102.825 108.973 144.044 1.00 70.60  ? 171 TYR A C     1 
ATOM   549  O O     . TYR A 1 86  ? 102.935 108.219 145.018 1.00 77.88  ? 171 TYR A O     1 
ATOM   550  C CB    . TYR A 1 86  ? 104.985 109.874 143.140 1.00 67.96  ? 171 TYR A CB    1 
ATOM   551  C CG    . TYR A 1 86  ? 105.571 109.820 144.534 1.00 69.97  ? 171 TYR A CG    1 
ATOM   552  C CD1   . TYR A 1 86  ? 106.480 108.831 144.886 1.00 71.76  ? 171 TYR A CD1   1 
ATOM   553  C CD2   . TYR A 1 86  ? 105.225 110.763 145.493 1.00 70.04  ? 171 TYR A CD2   1 
ATOM   554  C CE1   . TYR A 1 86  ? 107.022 108.778 146.156 1.00 73.99  ? 171 TYR A CE1   1 
ATOM   555  C CE2   . TYR A 1 86  ? 105.761 110.717 146.767 1.00 71.33  ? 171 TYR A CE2   1 
ATOM   556  C CZ    . TYR A 1 86  ? 106.658 109.722 147.093 1.00 73.85  ? 171 TYR A CZ    1 
ATOM   557  O OH    . TYR A 1 86  ? 107.196 109.673 148.358 1.00 74.32  ? 171 TYR A OH    1 
ATOM   558  N N     . THR A 1 87  ? 101.850 109.879 143.948 1.00 72.89  ? 172 THR A N     1 
ATOM   559  C CA    . THR A 1 87  ? 100.798 109.951 144.956 1.00 74.42  ? 172 THR A CA    1 
ATOM   560  C C     . THR A 1 87  ? 99.879  108.736 144.884 1.00 73.08  ? 172 THR A C     1 
ATOM   561  O O     . THR A 1 87  ? 99.471  108.200 145.921 1.00 76.44  ? 172 THR A O     1 
ATOM   562  C CB    . THR A 1 87  ? 99.998  111.244 144.786 1.00 73.46  ? 172 THR A CB    1 
ATOM   563  O OG1   . THR A 1 87  ? 100.872 112.370 144.939 1.00 71.89  ? 172 THR A OG1   1 
ATOM   564  C CG2   . THR A 1 87  ? 98.891  111.332 145.826 1.00 79.97  ? 172 THR A CG2   1 
ATOM   565  N N     . LYS A 1 88  ? 99.546  108.287 143.671 1.00 71.96  ? 173 LYS A N     1 
ATOM   566  C CA    . LYS A 1 88  ? 98.779  107.055 143.523 1.00 73.65  ? 173 LYS A CA    1 
ATOM   567  C C     . LYS A 1 88  ? 99.578  105.844 143.987 1.00 74.25  ? 173 LYS A C     1 
ATOM   568  O O     . LYS A 1 88  ? 99.012  104.917 144.576 1.00 77.32  ? 173 LYS A O     1 
ATOM   569  C CB    . LYS A 1 88  ? 98.340  106.882 142.067 1.00 74.94  ? 173 LYS A CB    1 
ATOM   570  C CG    . LYS A 1 88  ? 97.527  105.623 141.797 1.00 79.40  ? 173 LYS A CG    1 
ATOM   571  C CD    . LYS A 1 88  ? 96.167  105.681 142.476 1.00 83.96  ? 173 LYS A CD    1 
ATOM   572  C CE    . LYS A 1 88  ? 95.300  104.497 142.077 1.00 80.34  ? 173 LYS A CE    1 
ATOM   573  N NZ    . LYS A 1 88  ? 95.849  103.207 142.579 1.00 76.09  ? 173 LYS A NZ    1 
ATOM   574  N N     . LEU A 1 89  ? 100.888 105.835 143.730 1.00 74.23  ? 174 LEU A N     1 
ATOM   575  C CA    . LEU A 1 89  ? 101.737 104.734 144.169 1.00 72.67  ? 174 LEU A CA    1 
ATOM   576  C C     . LEU A 1 89  ? 101.943 104.722 145.678 1.00 74.67  ? 174 LEU A C     1 
ATOM   577  O O     . LEU A 1 89  ? 102.261 103.667 146.238 1.00 75.25  ? 174 LEU A O     1 
ATOM   578  C CB    . LEU A 1 89  ? 103.094 104.807 143.466 1.00 70.91  ? 174 LEU A CB    1 
ATOM   579  C CG    . LEU A 1 89  ? 103.207 104.140 142.095 1.00 72.27  ? 174 LEU A CG    1 
ATOM   580  C CD1   . LEU A 1 89  ? 104.610 104.313 141.533 1.00 69.84  ? 174 LEU A CD1   1 
ATOM   581  C CD2   . LEU A 1 89  ? 102.837 102.668 142.178 1.00 71.64  ? 174 LEU A CD2   1 
ATOM   582  N N     . SER A 1 90  ? 101.774 105.866 146.345 1.00 72.47  ? 175 SER A N     1 
ATOM   583  C CA    . SER A 1 90  ? 102.040 105.937 147.778 1.00 70.41  ? 175 SER A CA    1 
ATOM   584  C C     . SER A 1 90  ? 101.035 105.126 148.587 1.00 79.52  ? 175 SER A C     1 
ATOM   585  O O     . SER A 1 90  ? 101.372 104.630 149.668 1.00 85.95  ? 175 SER A O     1 
ATOM   586  C CB    . SER A 1 90  ? 102.035 107.394 148.241 1.00 67.24  ? 175 SER A CB    1 
ATOM   587  O OG    . SER A 1 90  ? 103.252 108.039 147.909 1.00 71.78  ? 175 SER A OG    1 
ATOM   588  N N     . ASN A 1 91  ? 99.806  104.979 148.091 1.00 80.79  ? 176 ASN A N     1 
ATOM   589  C CA    . ASN A 1 91  ? 98.749  104.284 148.814 1.00 80.02  ? 176 ASN A CA    1 
ATOM   590  C C     . ASN A 1 91  ? 98.485  102.885 148.267 1.00 78.72  ? 176 ASN A C     1 
ATOM   591  O O     . ASN A 1 91  ? 97.470  102.270 148.608 1.00 84.01  ? 176 ASN A O     1 
ATOM   592  C CB    . ASN A 1 91  ? 97.467  105.116 148.801 1.00 83.68  ? 176 ASN A CB    1 
ATOM   593  C CG    . ASN A 1 91  ? 97.627  106.438 149.527 1.00 89.03  ? 176 ASN A CG    1 
ATOM   594  O OD1   . ASN A 1 91  ? 97.555  107.507 148.921 1.00 89.24  ? 176 ASN A OD1   1 
ATOM   595  N ND2   . ASN A 1 91  ? 97.852  106.370 150.834 1.00 85.79  ? 176 ASN A ND2   1 
ATOM   596  N N     . VAL A 1 92  ? 99.376  102.372 147.420 1.00 76.00  ? 177 VAL A N     1 
ATOM   597  C CA    . VAL A 1 92  ? 99.286  100.990 146.959 1.00 79.54  ? 177 VAL A CA    1 
ATOM   598  C C     . VAL A 1 92  ? 100.513 100.167 147.317 1.00 87.85  ? 177 VAL A C     1 
ATOM   599  O O     . VAL A 1 92  ? 100.438 98.923  147.331 1.00 88.49  ? 177 VAL A O     1 
ATOM   600  C CB    . VAL A 1 92  ? 99.036  100.945 145.432 1.00 83.22  ? 177 VAL A CB    1 
ATOM   601  C CG1   . VAL A 1 92  ? 100.277 101.386 144.669 1.00 79.18  ? 177 VAL A CG1   1 
ATOM   602  C CG2   . VAL A 1 92  ? 98.568  99.562  144.986 1.00 82.34  ? 177 VAL A CG2   1 
ATOM   603  N N     . LEU A 1 93  ? 101.643 100.788 147.640 1.00 86.34  ? 178 LEU A N     1 
ATOM   604  C CA    . LEU A 1 93  ? 102.876 100.092 147.960 1.00 78.13  ? 178 LEU A CA    1 
ATOM   605  C C     . LEU A 1 93  ? 103.357 100.505 149.344 1.00 80.25  ? 178 LEU A C     1 
ATOM   606  O O     . LEU A 1 93  ? 103.001 101.570 149.858 1.00 77.67  ? 178 LEU A O     1 
ATOM   607  C CB    . LEU A 1 93  ? 103.962 100.392 146.919 1.00 71.55  ? 178 LEU A CB    1 
ATOM   608  C CG    . LEU A 1 93  ? 103.701 99.876  145.503 1.00 75.87  ? 178 LEU A CG    1 
ATOM   609  C CD1   . LEU A 1 93  ? 104.761 100.390 144.546 1.00 75.70  ? 178 LEU A CD1   1 
ATOM   610  C CD2   . LEU A 1 93  ? 103.653 98.358  145.486 1.00 74.34  ? 178 LEU A CD2   1 
ATOM   611  N N     . SER A 1 94  ? 104.171 99.644  149.949 1.00 82.42  ? 179 SER A N     1 
ATOM   612  C CA    . SER A 1 94  ? 104.762 99.959  151.238 1.00 77.33  ? 179 SER A CA    1 
ATOM   613  C C     . SER A 1 94  ? 105.795 101.076 151.086 1.00 73.32  ? 179 SER A C     1 
ATOM   614  O O     . SER A 1 94  ? 106.185 101.455 149.978 1.00 77.78  ? 179 SER A O     1 
ATOM   615  C CB    . SER A 1 94  ? 105.409 98.718  151.850 1.00 77.43  ? 179 SER A CB    1 
ATOM   616  O OG    . SER A 1 94  ? 104.447 97.708  152.097 1.00 87.77  ? 179 SER A OG    1 
ATOM   617  N N     . LYS A 1 95  ? 106.235 101.611 152.227 1.00 72.17  ? 180 LYS A N     1 
ATOM   618  C CA    . LYS A 1 95  ? 107.278 102.632 152.202 1.00 74.78  ? 180 LYS A CA    1 
ATOM   619  C C     . LYS A 1 95  ? 108.569 102.079 151.612 1.00 72.91  ? 180 LYS A C     1 
ATOM   620  O O     . LYS A 1 95  ? 109.260 102.768 150.852 1.00 68.80  ? 180 LYS A O     1 
ATOM   621  C CB    . LYS A 1 95  ? 107.518 103.176 153.610 1.00 75.96  ? 180 LYS A CB    1 
ATOM   622  C CG    . LYS A 1 95  ? 106.429 104.111 154.109 1.00 76.95  ? 180 LYS A CG    1 
ATOM   623  C CD    . LYS A 1 95  ? 106.503 105.462 153.416 1.00 83.33  ? 180 LYS A CD    1 
ATOM   624  C CE    . LYS A 1 95  ? 107.804 106.179 153.742 1.00 85.75  ? 180 LYS A CE    1 
ATOM   625  N NZ    . LYS A 1 95  ? 107.817 107.573 153.218 1.00 86.05  ? 180 LYS A NZ    1 
ATOM   626  N N     . LYS A 1 96  ? 108.912 100.836 151.956 1.00 73.78  ? 181 LYS A N     1 
ATOM   627  C CA    . LYS A 1 96  ? 110.078 100.193 151.360 1.00 70.64  ? 181 LYS A CA    1 
ATOM   628  C C     . LYS A 1 96  ? 109.893 100.010 149.858 1.00 70.85  ? 181 LYS A C     1 
ATOM   629  O O     . LYS A 1 96  ? 110.776 100.355 149.065 1.00 73.35  ? 181 LYS A O     1 
ATOM   630  C CB    . LYS A 1 96  ? 110.330 98.844  152.035 1.00 72.69  ? 181 LYS A CB    1 
ATOM   631  C CG    . LYS A 1 96  ? 110.941 98.937  153.421 1.00 77.31  ? 181 LYS A CG    1 
ATOM   632  C CD    . LYS A 1 96  ? 111.044 97.562  154.060 1.00 85.13  ? 181 LYS A CD    1 
ATOM   633  C CE    . LYS A 1 96  ? 111.714 96.566  153.126 1.00 90.91  ? 181 LYS A CE    1 
ATOM   634  N NZ    . LYS A 1 96  ? 111.634 95.173  153.646 1.00 89.32  ? 181 LYS A NZ    1 
ATOM   635  N N     . ALA A 1 97  ? 108.740 99.472  149.450 1.00 71.19  ? 182 ALA A N     1 
ATOM   636  C CA    . ALA A 1 97  ? 108.506 99.200  148.036 1.00 68.07  ? 182 ALA A CA    1 
ATOM   637  C C     . ALA A 1 97  ? 108.385 100.483 147.225 1.00 66.42  ? 182 ALA A C     1 
ATOM   638  O O     . ALA A 1 97  ? 108.784 100.513 146.056 1.00 71.63  ? 182 ALA A O     1 
ATOM   639  C CB    . ALA A 1 97  ? 107.251 98.344  147.865 1.00 68.92  ? 182 ALA A CB    1 
ATOM   640  N N     . LEU A 1 98  ? 107.837 101.546 147.819 1.00 66.89  ? 183 LEU A N     1 
ATOM   641  C CA    . LEU A 1 98  ? 107.714 102.809 147.100 1.00 67.27  ? 183 LEU A CA    1 
ATOM   642  C C     . LEU A 1 98  ? 109.078 103.374 146.725 1.00 65.56  ? 183 LEU A C     1 
ATOM   643  O O     . LEU A 1 98  ? 109.221 103.985 145.661 1.00 70.09  ? 183 LEU A O     1 
ATOM   644  C CB    . LEU A 1 98  ? 106.928 103.817 147.941 1.00 70.36  ? 183 LEU A CB    1 
ATOM   645  C CG    . LEU A 1 98  ? 106.728 105.216 147.357 1.00 69.84  ? 183 LEU A CG    1 
ATOM   646  C CD1   . LEU A 1 98  ? 105.758 105.176 146.186 1.00 69.51  ? 183 LEU A CD1   1 
ATOM   647  C CD2   . LEU A 1 98  ? 106.233 106.170 148.432 1.00 71.48  ? 183 LEU A CD2   1 
ATOM   648  N N     . PHE A 1 99  ? 110.086 103.181 147.578 1.00 66.50  ? 184 PHE A N     1 
ATOM   649  C CA    . PHE A 1 99  ? 111.429 103.650 147.255 1.00 62.11  ? 184 PHE A CA    1 
ATOM   650  C C     . PHE A 1 99  ? 111.996 102.915 146.045 1.00 61.91  ? 184 PHE A C     1 
ATOM   651  O O     . PHE A 1 99  ? 112.554 103.538 145.135 1.00 65.37  ? 184 PHE A O     1 
ATOM   652  C CB    . PHE A 1 99  ? 112.345 103.481 148.468 1.00 61.79  ? 184 PHE A CB    1 
ATOM   653  C CG    . PHE A 1 99  ? 113.716 104.072 148.286 1.00 60.28  ? 184 PHE A CG    1 
ATOM   654  C CD1   . PHE A 1 99  ? 113.963 105.395 148.611 1.00 58.38  ? 184 PHE A CD1   1 
ATOM   655  C CD2   . PHE A 1 99  ? 114.760 103.300 147.802 1.00 59.14  ? 184 PHE A CD2   1 
ATOM   656  C CE1   . PHE A 1 99  ? 115.223 105.940 148.447 1.00 56.50  ? 184 PHE A CE1   1 
ATOM   657  C CE2   . PHE A 1 99  ? 116.022 103.839 147.636 1.00 57.70  ? 184 PHE A CE2   1 
ATOM   658  C CZ    . PHE A 1 99  ? 116.253 105.161 147.960 1.00 58.78  ? 184 PHE A CZ    1 
ATOM   659  N N     . TYR A 1 100 ? 111.854 101.587 146.013 1.00 60.39  ? 185 TYR A N     1 
ATOM   660  C CA    . TYR A 1 100 ? 112.458 100.805 144.939 1.00 57.14  ? 185 TYR A CA    1 
ATOM   661  C C     . TYR A 1 100 ? 111.720 101.001 143.620 1.00 58.24  ? 185 TYR A C     1 
ATOM   662  O O     . TYR A 1 100 ? 112.346 101.199 142.573 1.00 61.51  ? 185 TYR A O     1 
ATOM   663  C CB    . TYR A 1 100 ? 112.501 99.326  145.322 1.00 60.93  ? 185 TYR A CB    1 
ATOM   664  C CG    . TYR A 1 100 ? 113.502 99.008  146.410 1.00 63.71  ? 185 TYR A CG    1 
ATOM   665  C CD1   . TYR A 1 100 ? 114.853 98.871  146.117 1.00 66.24  ? 185 TYR A CD1   1 
ATOM   666  C CD2   . TYR A 1 100 ? 113.098 98.844  147.728 1.00 65.52  ? 185 TYR A CD2   1 
ATOM   667  C CE1   . TYR A 1 100 ? 115.773 98.582  147.107 1.00 66.33  ? 185 TYR A CE1   1 
ATOM   668  C CE2   . TYR A 1 100 ? 114.011 98.555  148.724 1.00 69.32  ? 185 TYR A CE2   1 
ATOM   669  C CZ    . TYR A 1 100 ? 115.346 98.425  148.408 1.00 67.53  ? 185 TYR A CZ    1 
ATOM   670  O OH    . TYR A 1 100 ? 116.258 98.136  149.397 1.00 71.55  ? 185 TYR A OH    1 
ATOM   671  N N     . THR A 1 101 ? 110.387 100.969 143.649 1.00 57.04  ? 186 THR A N     1 
ATOM   672  C CA    . THR A 1 101 ? 109.619 101.110 142.416 1.00 58.27  ? 186 THR A CA    1 
ATOM   673  C C     . THR A 1 101 ? 109.733 102.497 141.797 1.00 58.41  ? 186 THR A C     1 
ATOM   674  O O     . THR A 1 101 ? 109.212 102.705 140.695 1.00 63.84  ? 186 THR A O     1 
ATOM   675  C CB    . THR A 1 101 ? 108.146 100.778 142.665 1.00 64.98  ? 186 THR A CB    1 
ATOM   676  O OG1   . THR A 1 101 ? 107.592 101.714 143.599 1.00 67.64  ? 186 THR A OG1   1 
ATOM   677  C CG2   . THR A 1 101 ? 108.000 99.361  143.203 1.00 61.85  ? 186 THR A CG2   1 
ATOM   678  N N     . VAL A 1 102 ? 110.387 103.442 142.469 1.00 56.54  ? 187 VAL A N     1 
ATOM   679  C CA    . VAL A 1 102 ? 110.625 104.764 141.904 1.00 55.94  ? 187 VAL A CA    1 
ATOM   680  C C     . VAL A 1 102 ? 112.071 104.865 141.434 1.00 57.26  ? 187 VAL A C     1 
ATOM   681  O O     . VAL A 1 102 ? 112.345 105.404 140.357 1.00 60.48  ? 187 VAL A O     1 
ATOM   682  C CB    . VAL A 1 102 ? 110.289 105.873 142.919 1.00 55.35  ? 187 VAL A CB    1 
ATOM   683  C CG1   . VAL A 1 102 ? 110.722 107.226 142.388 1.00 55.68  ? 187 VAL A CG1   1 
ATOM   684  C CG2   . VAL A 1 102 ? 108.797 105.882 143.205 1.00 62.01  ? 187 VAL A CG2   1 
ATOM   685  N N     . ILE A 1 103 ? 113.005 104.333 142.222 1.00 57.21  ? 188 ILE A N     1 
ATOM   686  C CA    . ILE A 1 103 ? 114.425 104.524 141.940 1.00 53.25  ? 188 ILE A CA    1 
ATOM   687  C C     . ILE A 1 103 ? 115.022 103.437 141.045 1.00 52.03  ? 188 ILE A C     1 
ATOM   688  O O     . ILE A 1 103 ? 116.005 103.709 140.338 1.00 54.44  ? 188 ILE A O     1 
ATOM   689  C CB    . ILE A 1 103 ? 115.232 104.641 143.252 1.00 52.30  ? 188 ILE A CB    1 
ATOM   690  C CG1   . ILE A 1 103 ? 116.567 105.342 142.999 1.00 50.65  ? 188 ILE A CG1   1 
ATOM   691  C CG2   . ILE A 1 103 ? 115.465 103.273 143.879 1.00 48.54  ? 188 ILE A CG2   1 
ATOM   692  C CD1   . ILE A 1 103 ? 117.425 105.471 144.228 1.00 48.15  ? 188 ILE A CD1   1 
ATOM   693  N N     . VAL A 1 104 ? 114.471 102.225 141.053 1.00 52.55  ? 189 VAL A N     1 
ATOM   694  C CA    . VAL A 1 104 ? 114.954 101.156 140.178 1.00 49.19  ? 189 VAL A CA    1 
ATOM   695  C C     . VAL A 1 104 ? 114.659 101.477 138.714 1.00 49.18  ? 189 VAL A C     1 
ATOM   696  O O     . VAL A 1 104 ? 115.554 101.310 137.872 1.00 48.56  ? 189 VAL A O     1 
ATOM   697  C CB    . VAL A 1 104 ? 114.373 99.790  140.584 1.00 48.01  ? 189 VAL A CB    1 
ATOM   698  C CG1   . VAL A 1 104 ? 114.731 98.731  139.554 1.00 47.39  ? 189 VAL A CG1   1 
ATOM   699  C CG2   . VAL A 1 104 ? 114.893 99.387  141.956 1.00 50.19  ? 189 VAL A CG2   1 
ATOM   700  N N     . PRO A 1 105 ? 113.448 101.924 138.344 1.00 51.20  ? 190 PRO A N     1 
ATOM   701  C CA    . PRO A 1 105 ? 113.235 102.317 136.940 1.00 45.31  ? 190 PRO A CA    1 
ATOM   702  C C     . PRO A 1 105 ? 114.178 103.410 136.472 1.00 46.02  ? 190 PRO A C     1 
ATOM   703  O O     . PRO A 1 105 ? 114.533 103.442 135.287 1.00 51.76  ? 190 PRO A O     1 
ATOM   704  C CB    . PRO A 1 105 ? 111.775 102.786 136.929 1.00 46.34  ? 190 PRO A CB    1 
ATOM   705  C CG    . PRO A 1 105 ? 111.142 101.995 138.006 1.00 48.55  ? 190 PRO A CG    1 
ATOM   706  C CD    . PRO A 1 105 ? 112.176 101.949 139.093 1.00 53.36  ? 190 PRO A CD    1 
ATOM   707  N N     . PHE A 1 106 ? 114.587 104.313 137.365 1.00 48.69  ? 191 PHE A N     1 
ATOM   708  C CA    . PHE A 1 106 ? 115.610 105.288 137.006 1.00 46.34  ? 191 PHE A CA    1 
ATOM   709  C C     . PHE A 1 106 ? 116.934 104.601 136.696 1.00 45.97  ? 191 PHE A C     1 
ATOM   710  O O     . PHE A 1 106 ? 117.594 104.930 135.704 1.00 49.19  ? 191 PHE A O     1 
ATOM   711  C CB    . PHE A 1 106 ? 115.788 106.303 138.135 1.00 47.34  ? 191 PHE A CB    1 
ATOM   712  C CG    . PHE A 1 106 ? 114.866 107.484 138.040 1.00 48.69  ? 191 PHE A CG    1 
ATOM   713  C CD1   . PHE A 1 106 ? 115.130 108.521 137.165 1.00 48.38  ? 191 PHE A CD1   1 
ATOM   714  C CD2   . PHE A 1 106 ? 113.737 107.558 138.835 1.00 50.01  ? 191 PHE A CD2   1 
ATOM   715  C CE1   . PHE A 1 106 ? 114.280 109.605 137.082 1.00 46.48  ? 191 PHE A CE1   1 
ATOM   716  C CE2   . PHE A 1 106 ? 112.885 108.639 138.756 1.00 51.20  ? 191 PHE A CE2   1 
ATOM   717  C CZ    . PHE A 1 106 ? 113.157 109.663 137.879 1.00 47.70  ? 191 PHE A CZ    1 
ATOM   718  N N     . ILE A 1 107 ? 117.328 103.634 137.527 1.00 48.75  ? 192 ILE A N     1 
ATOM   719  C CA    . ILE A 1 107 ? 118.587 102.928 137.314 1.00 47.22  ? 192 ILE A CA    1 
ATOM   720  C C     . ILE A 1 107 ? 118.548 102.144 136.008 1.00 46.34  ? 192 ILE A C     1 
ATOM   721  O O     . ILE A 1 107 ? 119.518 102.143 135.239 1.00 50.75  ? 192 ILE A O     1 
ATOM   722  C CB    . ILE A 1 107 ? 118.893 102.017 138.517 1.00 45.52  ? 192 ILE A CB    1 
ATOM   723  C CG1   . ILE A 1 107 ? 119.154 102.858 139.767 1.00 41.46  ? 192 ILE A CG1   1 
ATOM   724  C CG2   . ILE A 1 107 ? 120.082 101.116 138.222 1.00 44.04  ? 192 ILE A CG2   1 
ATOM   725  C CD1   . ILE A 1 107 ? 119.030 102.083 141.059 1.00 47.86  ? 192 ILE A CD1   1 
ATOM   726  N N     . ILE A 1 108 ? 117.432 101.465 135.736 1.00 45.99  ? 193 ILE A N     1 
ATOM   727  C CA    . ILE A 1 108 ? 117.311 100.698 134.500 1.00 44.42  ? 193 ILE A CA    1 
ATOM   728  C C     . ILE A 1 108 ? 117.345 101.620 133.288 1.00 45.06  ? 193 ILE A C     1 
ATOM   729  O O     . ILE A 1 108 ? 117.991 101.314 132.280 1.00 51.50  ? 193 ILE A O     1 
ATOM   730  C CB    . ILE A 1 108 ? 116.033 99.839  134.526 1.00 46.05  ? 193 ILE A CB    1 
ATOM   731  C CG1   . ILE A 1 108 ? 116.060 98.880  135.718 1.00 46.39  ? 193 ILE A CG1   1 
ATOM   732  C CG2   . ILE A 1 108 ? 115.881 99.065  133.226 1.00 47.47  ? 193 ILE A CG2   1 
ATOM   733  C CD1   . ILE A 1 108 ? 117.217 97.904  135.689 1.00 46.01  ? 193 ILE A CD1   1 
ATOM   734  N N     . TYR A 1 109 ? 116.655 102.762 133.364 1.00 43.10  ? 194 TYR A N     1 
ATOM   735  C CA    . TYR A 1 109 ? 116.615 103.680 132.229 1.00 43.54  ? 194 TYR A CA    1 
ATOM   736  C C     . TYR A 1 109 ? 118.002 104.214 131.895 1.00 46.65  ? 194 TYR A C     1 
ATOM   737  O O     . TYR A 1 109 ? 118.446 104.142 130.743 1.00 57.14  ? 194 TYR A O     1 
ATOM   738  C CB    . TYR A 1 109 ? 115.657 104.838 132.515 1.00 44.20  ? 194 TYR A CB    1 
ATOM   739  C CG    . TYR A 1 109 ? 115.610 105.856 131.396 1.00 48.29  ? 194 TYR A CG    1 
ATOM   740  C CD1   . TYR A 1 109 ? 114.808 105.657 130.280 1.00 49.26  ? 194 TYR A CD1   1 
ATOM   741  C CD2   . TYR A 1 109 ? 116.381 107.010 131.451 1.00 48.01  ? 194 TYR A CD2   1 
ATOM   742  C CE1   . TYR A 1 109 ? 114.772 106.584 129.253 1.00 52.26  ? 194 TYR A CE1   1 
ATOM   743  C CE2   . TYR A 1 109 ? 116.353 107.939 130.431 1.00 43.87  ? 194 TYR A CE2   1 
ATOM   744  C CZ    . TYR A 1 109 ? 115.547 107.722 129.335 1.00 49.67  ? 194 TYR A CZ    1 
ATOM   745  O OH    . TYR A 1 109 ? 115.519 108.647 128.319 1.00 57.35  ? 194 TYR A OH    1 
ATOM   746  N N     . PHE A 1 110 ? 118.704 104.760 132.891 1.00 43.88  ? 195 PHE A N     1 
ATOM   747  C CA    . PHE A 1 110 ? 119.995 105.380 132.616 1.00 42.76  ? 195 PHE A CA    1 
ATOM   748  C C     . PHE A 1 110 ? 121.032 104.350 132.187 1.00 49.09  ? 195 PHE A C     1 
ATOM   749  O O     . PHE A 1 110 ? 121.884 104.646 131.341 1.00 53.26  ? 195 PHE A O     1 
ATOM   750  C CB    . PHE A 1 110 ? 120.476 106.164 133.837 1.00 41.24  ? 195 PHE A CB    1 
ATOM   751  C CG    . PHE A 1 110 ? 119.637 107.374 134.141 1.00 45.79  ? 195 PHE A CG    1 
ATOM   752  C CD1   . PHE A 1 110 ? 119.450 108.358 133.186 1.00 43.65  ? 195 PHE A CD1   1 
ATOM   753  C CD2   . PHE A 1 110 ? 119.041 107.530 135.380 1.00 46.32  ? 195 PHE A CD2   1 
ATOM   754  C CE1   . PHE A 1 110 ? 118.678 109.472 133.458 1.00 41.77  ? 195 PHE A CE1   1 
ATOM   755  C CE2   . PHE A 1 110 ? 118.266 108.640 135.658 1.00 41.63  ? 195 PHE A CE2   1 
ATOM   756  C CZ    . PHE A 1 110 ? 118.087 109.613 134.696 1.00 46.04  ? 195 PHE A CZ    1 
ATOM   757  N N     . GLY A 1 111 ? 120.981 103.144 132.753 1.00 48.82  ? 196 GLY A N     1 
ATOM   758  C CA    . GLY A 1 111 ? 121.845 102.079 132.272 1.00 46.19  ? 196 GLY A CA    1 
ATOM   759  C C     . GLY A 1 111 ? 121.501 101.644 130.861 1.00 53.95  ? 196 GLY A C     1 
ATOM   760  O O     . GLY A 1 111 ? 122.392 101.426 130.035 1.00 62.57  ? 196 GLY A O     1 
ATOM   761  N N     . ALA A 1 112 ? 120.205 101.511 130.565 1.00 53.18  ? 197 ALA A N     1 
ATOM   762  C CA    . ALA A 1 112 ? 119.791 101.174 129.207 1.00 48.99  ? 197 ALA A CA    1 
ATOM   763  C C     . ALA A 1 112 ? 120.144 102.286 128.231 1.00 52.06  ? 197 ALA A C     1 
ATOM   764  O O     . ALA A 1 112 ? 120.519 102.018 127.084 1.00 62.97  ? 197 ALA A O     1 
ATOM   765  C CB    . ALA A 1 112 ? 118.290 100.884 129.164 1.00 50.29  ? 197 ALA A CB    1 
ATOM   766  N N     . PHE A 1 113 ? 120.011 103.544 128.659 1.00 51.54  ? 198 PHE A N     1 
ATOM   767  C CA    . PHE A 1 113 ? 120.322 104.659 127.767 1.00 52.19  ? 198 PHE A CA    1 
ATOM   768  C C     . PHE A 1 113 ? 121.797 104.659 127.379 1.00 55.70  ? 198 PHE A C     1 
ATOM   769  O O     . PHE A 1 113 ? 122.141 104.854 126.208 1.00 58.18  ? 198 PHE A O     1 
ATOM   770  C CB    . PHE A 1 113 ? 119.943 105.986 128.419 1.00 50.22  ? 198 PHE A CB    1 
ATOM   771  C CG    . PHE A 1 113 ? 120.162 107.168 127.523 1.00 50.14  ? 198 PHE A CG    1 
ATOM   772  C CD1   . PHE A 1 113 ? 119.189 107.538 126.610 1.00 50.51  ? 198 PHE A CD1   1 
ATOM   773  C CD2   . PHE A 1 113 ? 121.340 107.892 127.568 1.00 45.89  ? 198 PHE A CD2   1 
ATOM   774  C CE1   . PHE A 1 113 ? 119.376 108.615 125.778 1.00 48.81  ? 198 PHE A CE1   1 
ATOM   775  C CE2   . PHE A 1 113 ? 121.537 108.977 126.727 1.00 45.30  ? 198 PHE A CE2   1 
ATOM   776  C CZ    . PHE A 1 113 ? 120.546 109.332 125.828 1.00 45.87  ? 198 PHE A CZ    1 
ATOM   777  N N     . GLY A 1 114 ? 122.687 104.446 128.349 1.00 59.41  ? 199 GLY A N     1 
ATOM   778  C CA    . GLY A 1 114 ? 124.100 104.393 128.024 1.00 60.20  ? 199 GLY A CA    1 
ATOM   779  C C     . GLY A 1 114 ? 124.431 103.271 127.059 1.00 64.41  ? 199 GLY A C     1 
ATOM   780  O O     . GLY A 1 114 ? 125.093 103.490 126.042 1.00 68.33  ? 199 GLY A O     1 
ATOM   781  N N     . PHE A 1 115 ? 123.938 102.068 127.338 1.00 61.87  ? 200 PHE A N     1 
ATOM   782  C CA    . PHE A 1 115 ? 124.365 100.891 126.595 1.00 61.85  ? 200 PHE A CA    1 
ATOM   783  C C     . PHE A 1 115 ? 123.529 100.628 125.351 1.00 65.28  ? 200 PHE A C     1 
ATOM   784  O O     . PHE A 1 115 ? 124.048 100.071 124.375 1.00 77.19  ? 200 PHE A O     1 
ATOM   785  C CB    . PHE A 1 115 ? 124.320 99.663  127.507 1.00 64.39  ? 200 PHE A CB    1 
ATOM   786  C CG    . PHE A 1 115 ? 125.465 99.588  128.476 1.00 73.77  ? 200 PHE A CG    1 
ATOM   787  C CD1   . PHE A 1 115 ? 125.428 100.304 129.662 1.00 77.19  ? 200 PHE A CD1   1 
ATOM   788  C CD2   . PHE A 1 115 ? 126.581 98.817  128.201 1.00 79.98  ? 200 PHE A CD2   1 
ATOM   789  C CE1   . PHE A 1 115 ? 126.476 100.243 130.560 1.00 82.33  ? 200 PHE A CE1   1 
ATOM   790  C CE2   . PHE A 1 115 ? 127.635 98.754  129.096 1.00 88.90  ? 200 PHE A CE2   1 
ATOM   791  C CZ    . PHE A 1 115 ? 127.581 99.468  130.277 1.00 88.42  ? 200 PHE A CZ    1 
ATOM   792  N N     . VAL A 1 116 ? 122.253 101.016 125.354 1.00 59.76  ? 201 VAL A N     1 
ATOM   793  C CA    . VAL A 1 116 ? 121.342 100.625 124.282 1.00 56.76  ? 201 VAL A CA    1 
ATOM   794  C C     . VAL A 1 116 ? 120.749 101.843 123.584 1.00 59.54  ? 201 VAL A C     1 
ATOM   795  O O     . VAL A 1 116 ? 120.878 101.991 122.363 1.00 64.99  ? 201 VAL A O     1 
ATOM   796  C CB    . VAL A 1 116 ? 120.221 99.714  124.818 1.00 58.48  ? 201 VAL A CB    1 
ATOM   797  C CG1   . VAL A 1 116 ? 119.191 99.438  123.732 1.00 65.71  ? 201 VAL A CG1   1 
ATOM   798  C CG2   . VAL A 1 116 ? 120.798 98.418  125.368 1.00 57.93  ? 201 VAL A CG2   1 
ATOM   799  N N     . MET A 1 117 ? 120.090 102.723 124.345 1.00 59.28  ? 202 MET A N     1 
ATOM   800  C CA    . MET A 1 117 ? 119.270 103.753 123.714 1.00 58.27  ? 202 MET A CA    1 
ATOM   801  C C     . MET A 1 117 ? 120.103 104.835 123.025 1.00 59.47  ? 202 MET A C     1 
ATOM   802  O O     . MET A 1 117 ? 119.680 105.372 121.992 1.00 62.74  ? 202 MET A O     1 
ATOM   803  C CB    . MET A 1 117 ? 118.307 104.385 124.729 1.00 55.91  ? 202 MET A CB    1 
ATOM   804  C CG    . MET A 1 117 ? 117.140 103.470 125.138 1.00 59.83  ? 202 MET A CG    1 
ATOM   805  S SD    . MET A 1 117 ? 115.930 104.107 126.327 1.00 83.80  ? 202 MET A SD    1 
ATOM   806  C CE    . MET A 1 117 ? 116.806 104.113 127.857 1.00 54.10  ? 202 MET A CE    1 
ATOM   807  N N     . TYR A 1 118 ? 121.269 105.180 123.565 1.00 55.23  ? 203 TYR A N     1 
ATOM   808  C CA    . TYR A 1 118 ? 122.046 106.235 122.921 1.00 54.37  ? 203 TYR A CA    1 
ATOM   809  C C     . TYR A 1 118 ? 122.640 105.784 121.586 1.00 65.19  ? 203 TYR A C     1 
ATOM   810  O O     . TYR A 1 118 ? 122.589 106.553 120.618 1.00 64.31  ? 203 TYR A O     1 
ATOM   811  C CB    . TYR A 1 118 ? 123.152 106.761 123.841 1.00 52.49  ? 203 TYR A CB    1 
ATOM   812  C CG    . TYR A 1 118 ? 123.961 107.868 123.197 1.00 53.40  ? 203 TYR A CG    1 
ATOM   813  C CD1   . TYR A 1 118 ? 123.518 109.184 123.228 1.00 52.31  ? 203 TYR A CD1   1 
ATOM   814  C CD2   . TYR A 1 118 ? 125.161 107.597 122.551 1.00 60.77  ? 203 TYR A CD2   1 
ATOM   815  C CE1   . TYR A 1 118 ? 124.246 110.196 122.638 1.00 59.69  ? 203 TYR A CE1   1 
ATOM   816  C CE2   . TYR A 1 118 ? 125.894 108.603 121.957 1.00 68.11  ? 203 TYR A CE2   1 
ATOM   817  C CZ    . TYR A 1 118 ? 125.432 109.901 122.004 1.00 67.00  ? 203 TYR A CZ    1 
ATOM   818  O OH    . TYR A 1 118 ? 126.160 110.906 121.413 1.00 63.82  ? 203 TYR A OH    1 
ATOM   819  N N     . PRO A 1 119 ? 123.232 104.585 121.479 1.00 64.94  ? 204 PRO A N     1 
ATOM   820  C CA    . PRO A 1 119 ? 123.715 104.145 120.158 1.00 61.53  ? 204 PRO A CA    1 
ATOM   821  C C     . PRO A 1 119 ? 122.623 104.079 119.105 1.00 65.79  ? 204 PRO A C     1 
ATOM   822  O O     . PRO A 1 119 ? 122.903 104.292 117.919 1.00 73.74  ? 204 PRO A O     1 
ATOM   823  C CB    . PRO A 1 119 ? 124.303 102.758 120.447 1.00 66.52  ? 204 PRO A CB    1 
ATOM   824  C CG    . PRO A 1 119 ? 124.723 102.830 121.861 1.00 62.94  ? 204 PRO A CG    1 
ATOM   825  C CD    . PRO A 1 119 ? 123.674 103.660 122.540 1.00 61.59  ? 204 PRO A CD    1 
ATOM   826  N N     . LEU A 1 120 ? 121.385 103.794 119.503 1.00 60.11  ? 205 LEU A N     1 
ATOM   827  C CA    . LEU A 1 120 ? 120.268 103.706 118.573 1.00 63.42  ? 205 LEU A CA    1 
ATOM   828  C C     . LEU A 1 120 ? 119.619 105.055 118.294 1.00 68.34  ? 205 LEU A C     1 
ATOM   829  O O     . LEU A 1 120 ? 118.589 105.098 117.612 1.00 72.62  ? 205 LEU A O     1 
ATOM   830  C CB    . LEU A 1 120 ? 119.216 102.732 119.112 1.00 68.04  ? 205 LEU A CB    1 
ATOM   831  C CG    . LEU A 1 120 ? 119.667 101.279 119.274 1.00 73.59  ? 205 LEU A CG    1 
ATOM   832  C CD1   . LEU A 1 120 ? 118.585 100.453 119.954 1.00 74.25  ? 205 LEU A CD1   1 
ATOM   833  C CD2   . LEU A 1 120 ? 120.043 100.676 117.929 1.00 76.52  ? 205 LEU A CD2   1 
ATOM   834  N N     . SER A 1 121 ? 120.189 106.150 118.806 1.00 69.58  ? 206 SER A N     1 
ATOM   835  C CA    . SER A 1 121 ? 119.586 107.465 118.606 1.00 63.09  ? 206 SER A CA    1 
ATOM   836  C C     . SER A 1 121 ? 119.572 107.855 117.133 1.00 65.38  ? 206 SER A C     1 
ATOM   837  O O     . SER A 1 121 ? 118.618 108.482 116.660 1.00 70.14  ? 206 SER A O     1 
ATOM   838  C CB    . SER A 1 121 ? 120.329 108.515 119.432 1.00 63.29  ? 206 SER A CB    1 
ATOM   839  O OG    . SER A 1 121 ? 121.680 108.629 119.017 1.00 66.47  ? 206 SER A OG    1 
ATOM   840  N N     . ASN A 1 122 ? 120.624 107.496 116.392 1.00 68.38  ? 207 ASN A N     1 
ATOM   841  C CA    . ASN A 1 122 ? 120.678 107.835 114.973 1.00 70.53  ? 207 ASN A CA    1 
ATOM   842  C C     . ASN A 1 122 ? 119.554 107.168 114.190 1.00 70.82  ? 207 ASN A C     1 
ATOM   843  O O     . ASN A 1 122 ? 119.120 107.692 113.157 1.00 75.33  ? 207 ASN A O     1 
ATOM   844  C CB    . ASN A 1 122 ? 122.034 107.440 114.388 1.00 73.91  ? 207 ASN A CB    1 
ATOM   845  C CG    . ASN A 1 122 ? 123.189 107.783 115.307 1.00 80.29  ? 207 ASN A CG    1 
ATOM   846  O OD1   . ASN A 1 122 ? 123.634 106.953 116.100 1.00 77.90  ? 207 ASN A OD1   1 
ATOM   847  N ND2   . ASN A 1 122 ? 123.683 109.011 115.203 1.00 82.97  ? 207 ASN A ND2   1 
ATOM   848  N N     . TYR A 1 123 ? 119.073 106.016 114.660 1.00 72.40  ? 208 TYR A N     1 
ATOM   849  C CA    . TYR A 1 123 ? 118.009 105.303 113.963 1.00 69.99  ? 208 TYR A CA    1 
ATOM   850  C C     . TYR A 1 123 ? 116.632 105.853 114.303 1.00 67.15  ? 208 TYR A C     1 
ATOM   851  O O     . TYR A 1 123 ? 115.742 105.867 113.445 1.00 72.77  ? 208 TYR A O     1 
ATOM   852  C CB    . TYR A 1 123 ? 118.065 103.815 114.310 1.00 74.86  ? 208 TYR A CB    1 
ATOM   853  C CG    . TYR A 1 123 ? 119.277 103.097 113.766 1.00 82.04  ? 208 TYR A CG    1 
ATOM   854  C CD1   . TYR A 1 123 ? 120.068 103.675 112.781 1.00 85.85  ? 208 TYR A CD1   1 
ATOM   855  C CD2   . TYR A 1 123 ? 119.638 101.846 114.246 1.00 87.68  ? 208 TYR A CD2   1 
ATOM   856  C CE1   . TYR A 1 123 ? 121.180 103.023 112.286 1.00 93.12  ? 208 TYR A CE1   1 
ATOM   857  C CE2   . TYR A 1 123 ? 120.748 101.186 113.758 1.00 98.63  ? 208 TYR A CE2   1 
ATOM   858  C CZ    . TYR A 1 123 ? 121.515 101.779 112.778 1.00 99.00  ? 208 TYR A CZ    1 
ATOM   859  O OH    . TYR A 1 123 ? 122.622 101.126 112.288 1.00 92.49  ? 208 TYR A OH    1 
ATOM   860  N N     . ILE A 1 124 ? 116.443 106.309 115.539 1.00 67.14  ? 209 ILE A N     1 
ATOM   861  C CA    . ILE A 1 124 ? 115.128 106.699 116.031 1.00 61.26  ? 209 ILE A CA    1 
ATOM   862  C C     . ILE A 1 124 ? 114.887 108.205 115.998 1.00 59.43  ? 209 ILE A C     1 
ATOM   863  O O     . ILE A 1 124 ? 113.737 108.638 116.168 1.00 62.68  ? 209 ILE A O     1 
ATOM   864  C CB    . ILE A 1 124 ? 114.921 106.152 117.458 1.00 61.77  ? 209 ILE A CB    1 
ATOM   865  C CG1   . ILE A 1 124 ? 115.825 106.894 118.442 1.00 61.23  ? 209 ILE A CG1   1 
ATOM   866  C CG2   . ILE A 1 124 ? 115.194 104.658 117.502 1.00 61.59  ? 209 ILE A CG2   1 
ATOM   867  C CD1   . ILE A 1 124 ? 115.319 106.882 119.856 1.00 63.42  ? 209 ILE A CD1   1 
ATOM   868  N N     . HIS A 1 125 ? 115.921 109.009 115.783 1.00 58.94  ? 210 HIS A N     1 
ATOM   869  C CA    . HIS A 1 125 ? 115.753 110.456 115.745 1.00 57.32  ? 210 HIS A CA    1 
ATOM   870  C C     . HIS A 1 125 ? 115.327 110.893 114.349 1.00 63.68  ? 210 HIS A C     1 
ATOM   871  O O     . HIS A 1 125 ? 116.082 110.689 113.392 1.00 70.64  ? 210 HIS A O     1 
ATOM   872  C CB    . HIS A 1 125 ? 117.047 111.153 116.143 1.00 58.39  ? 210 HIS A CB    1 
ATOM   873  C CG    . HIS A 1 125 ? 117.268 111.218 117.622 1.00 56.54  ? 210 HIS A CG    1 
ATOM   874  N ND1   . HIS A 1 125 ? 118.428 111.708 118.181 1.00 53.04  ? 210 HIS A ND1   1 
ATOM   875  C CD2   . HIS A 1 125 ? 116.475 110.857 118.659 1.00 50.03  ? 210 HIS A CD2   1 
ATOM   876  C CE1   . HIS A 1 125 ? 118.342 111.644 119.498 1.00 49.25  ? 210 HIS A CE1   1 
ATOM   877  N NE2   . HIS A 1 125 ? 117.166 111.132 119.814 1.00 47.59  ? 210 HIS A NE2   1 
ATOM   878  N N     . PRO A 1 126 ? 114.145 111.490 114.185 1.00 61.95  ? 211 PRO A N     1 
ATOM   879  C CA    . PRO A 1 126 ? 113.692 111.942 112.851 1.00 63.05  ? 211 PRO A CA    1 
ATOM   880  C C     . PRO A 1 126 ? 114.374 113.236 112.410 1.00 63.39  ? 211 PRO A C     1 
ATOM   881  O O     . PRO A 1 126 ? 113.833 114.340 112.476 1.00 63.15  ? 211 PRO A O     1 
ATOM   882  C CB    . PRO A 1 126 ? 112.186 112.121 113.052 1.00 59.79  ? 211 PRO A CB    1 
ATOM   883  C CG    . PRO A 1 126 ? 112.048 112.474 114.492 1.00 57.12  ? 211 PRO A CG    1 
ATOM   884  C CD    . PRO A 1 126 ? 113.130 111.729 115.226 1.00 60.75  ? 211 PRO A CD    1 
ATOM   885  N N     . GLU A 1 127 ? 115.615 113.093 111.938 1.00 63.23  ? 212 GLU A N     1 
ATOM   886  C CA    . GLU A 1 127 ? 116.392 114.250 111.511 1.00 64.24  ? 212 GLU A CA    1 
ATOM   887  C C     . GLU A 1 127 ? 115.906 114.821 110.185 1.00 66.24  ? 212 GLU A C     1 
ATOM   888  O O     . GLU A 1 127 ? 116.109 116.012 109.928 1.00 65.56  ? 212 GLU A O     1 
ATOM   889  C CB    . GLU A 1 127 ? 117.871 113.875 111.405 1.00 65.47  ? 212 GLU A CB    1 
ATOM   890  C CG    . GLU A 1 127 ? 118.505 113.460 112.724 1.00 70.62  ? 212 GLU A CG    1 
ATOM   891  C CD    . GLU A 1 127 ? 118.594 114.602 113.718 1.00 78.99  ? 212 GLU A CD    1 
ATOM   892  O OE1   . GLU A 1 127 ? 118.767 115.760 113.283 1.00 82.34  ? 212 GLU A OE1   1 
ATOM   893  O OE2   . GLU A 1 127 ? 118.490 114.340 114.935 1.00 75.66  ? 212 GLU A OE2   1 
ATOM   894  N N     . ALA A 1 128 ? 115.274 114.005 109.341 1.00 65.66  ? 213 ALA A N     1 
ATOM   895  C CA    . ALA A 1 128 ? 114.796 114.460 108.041 1.00 61.32  ? 213 ALA A CA    1 
ATOM   896  C C     . ALA A 1 128 ? 113.469 115.205 108.146 1.00 57.92  ? 213 ALA A C     1 
ATOM   897  O O     . ALA A 1 128 ? 113.305 116.273 107.548 1.00 59.85  ? 213 ALA A O     1 
ATOM   898  C CB    . ALA A 1 128 ? 114.661 113.271 107.085 1.00 64.78  ? 213 ALA A CB    1 
ATOM   899  N N     . LEU A 1 129 ? 112.513 114.651 108.898 1.00 58.66  ? 214 LEU A N     1 
ATOM   900  C CA    . LEU A 1 129 ? 111.236 115.330 109.096 1.00 61.50  ? 214 LEU A CA    1 
ATOM   901  C C     . LEU A 1 129 ? 111.417 116.656 109.819 1.00 61.20  ? 214 LEU A C     1 
ATOM   902  O O     . LEU A 1 129 ? 110.683 117.615 109.555 1.00 64.60  ? 214 LEU A O     1 
ATOM   903  C CB    . LEU A 1 129 ? 110.279 114.427 109.875 1.00 61.84  ? 214 LEU A CB    1 
ATOM   904  C CG    . LEU A 1 129 ? 108.863 114.953 110.121 1.00 64.49  ? 214 LEU A CG    1 
ATOM   905  C CD1   . LEU A 1 129 ? 108.124 115.164 108.809 1.00 73.41  ? 214 LEU A CD1   1 
ATOM   906  C CD2   . LEU A 1 129 ? 108.092 114.009 111.033 1.00 62.89  ? 214 LEU A CD2   1 
ATOM   907  N N     . ALA A 1 130 ? 112.383 116.728 110.734 1.00 65.41  ? 215 ALA A N     1 
ATOM   908  C CA    . ALA A 1 130 ? 112.630 117.961 111.469 1.00 60.87  ? 215 ALA A CA    1 
ATOM   909  C C     . ALA A 1 130 ? 113.296 119.021 110.604 1.00 60.13  ? 215 ALA A C     1 
ATOM   910  O O     . ALA A 1 130 ? 113.007 120.212 110.762 1.00 61.83  ? 215 ALA A O     1 
ATOM   911  C CB    . ALA A 1 130 ? 113.491 117.670 112.694 1.00 57.12  ? 215 ALA A CB    1 
ATOM   912  N N     . ASP A 1 131 ? 114.194 118.617 109.703 1.00 60.86  ? 216 ASP A N     1 
ATOM   913  C CA    . ASP A 1 131 ? 114.778 119.572 108.771 1.00 62.28  ? 216 ASP A CA    1 
ATOM   914  C C     . ASP A 1 131 ? 113.747 120.097 107.787 1.00 62.20  ? 216 ASP A C     1 
ATOM   915  O O     . ASP A 1 131 ? 113.892 121.220 107.295 1.00 59.92  ? 216 ASP A O     1 
ATOM   916  C CB    . ASP A 1 131 ? 115.943 118.937 108.014 1.00 63.34  ? 216 ASP A CB    1 
ATOM   917  C CG    . ASP A 1 131 ? 117.232 119.006 108.789 1.00 64.71  ? 216 ASP A CG    1 
ATOM   918  O OD1   . ASP A 1 131 ? 117.500 120.065 109.388 1.00 68.20  ? 216 ASP A OD1   1 
ATOM   919  O OD2   . ASP A 1 131 ? 117.985 118.011 108.790 1.00 65.99  ? 216 ASP A OD2   1 
ATOM   920  N N     . LYS A 1 132 ? 112.719 119.305 107.485 1.00 62.42  ? 217 LYS A N     1 
ATOM   921  C CA    . LYS A 1 132 ? 111.628 119.797 106.656 1.00 59.26  ? 217 LYS A CA    1 
ATOM   922  C C     . LYS A 1 132 ? 110.773 120.800 107.420 1.00 58.43  ? 217 LYS A C     1 
ATOM   923  O O     . LYS A 1 132 ? 110.385 121.835 106.868 1.00 61.00  ? 217 LYS A O     1 
ATOM   924  C CB    . LYS A 1 132 ? 110.783 118.625 106.159 1.00 61.82  ? 217 LYS A CB    1 
ATOM   925  C CG    . LYS A 1 132 ? 109.648 119.020 105.236 1.00 71.95  ? 217 LYS A CG    1 
ATOM   926  C CD    . LYS A 1 132 ? 108.931 117.792 104.701 1.00 79.17  ? 217 LYS A CD    1 
ATOM   927  C CE    . LYS A 1 132 ? 107.704 118.180 103.896 1.00 81.03  ? 217 LYS A CE    1 
ATOM   928  N NZ    . LYS A 1 132 ? 108.082 118.913 102.656 1.00 80.11  ? 217 LYS A NZ    1 
ATOM   929  N N     . LEU A 1 133 ? 110.488 120.521 108.696 1.00 58.10  ? 218 LEU A N     1 
ATOM   930  C CA    . LEU A 1 133 ? 109.774 121.490 109.520 1.00 55.01  ? 218 LEU A CA    1 
ATOM   931  C C     . LEU A 1 133 ? 110.575 122.771 109.697 1.00 53.51  ? 218 LEU A C     1 
ATOM   932  O O     . LEU A 1 133 ? 109.993 123.858 109.773 1.00 54.76  ? 218 LEU A O     1 
ATOM   933  C CB    . LEU A 1 133 ? 109.444 120.889 110.887 1.00 56.07  ? 218 LEU A CB    1 
ATOM   934  C CG    . LEU A 1 133 ? 108.443 119.736 110.939 1.00 61.20  ? 218 LEU A CG    1 
ATOM   935  C CD1   . LEU A 1 133 ? 108.575 118.982 112.251 1.00 63.40  ? 218 LEU A CD1   1 
ATOM   936  C CD2   . LEU A 1 133 ? 107.025 120.256 110.760 1.00 61.12  ? 218 LEU A CD2   1 
ATOM   937  N N     . LEU A 1 134 ? 111.904 122.666 109.757 1.00 52.26  ? 219 LEU A N     1 
ATOM   938  C CA    . LEU A 1 134 ? 112.725 123.846 109.997 1.00 51.26  ? 219 LEU A CA    1 
ATOM   939  C C     . LEU A 1 134 ? 112.652 124.817 108.822 1.00 56.03  ? 219 LEU A C     1 
ATOM   940  O O     . LEU A 1 134 ? 112.635 126.036 109.020 1.00 59.56  ? 219 LEU A O     1 
ATOM   941  C CB    . LEU A 1 134 ? 114.167 123.423 110.286 1.00 52.81  ? 219 LEU A CB    1 
ATOM   942  C CG    . LEU A 1 134 ? 115.089 124.484 110.888 1.00 53.83  ? 219 LEU A CG    1 
ATOM   943  C CD1   . LEU A 1 134 ? 114.399 125.224 112.025 1.00 46.41  ? 219 LEU A CD1   1 
ATOM   944  C CD2   . LEU A 1 134 ? 116.370 123.831 111.377 1.00 56.67  ? 219 LEU A CD2   1 
ATOM   945  N N     . THR A 1 135 ? 112.608 124.301 107.592 1.00 58.56  ? 220 THR A N     1 
ATOM   946  C CA    . THR A 1 135 ? 112.505 125.175 106.428 1.00 56.05  ? 220 THR A CA    1 
ATOM   947  C C     . THR A 1 135 ? 111.089 125.700 106.268 1.00 55.86  ? 220 THR A C     1 
ATOM   948  O O     . THR A 1 135 ? 110.881 126.892 106.016 1.00 56.96  ? 220 THR A O     1 
ATOM   949  C CB    . THR A 1 135 ? 112.890 124.417 105.167 1.00 58.18  ? 220 THR A CB    1 
ATOM   950  O OG1   . THR A 1 135 ? 111.974 123.331 105.005 1.00 62.77  ? 220 THR A OG1   1 
ATOM   951  C CG2   . THR A 1 135 ? 114.289 123.849 105.289 1.00 61.11  ? 220 THR A CG2   1 
ATOM   952  N N     . THR A 1 136 ? 110.105 124.812 106.411 1.00 53.94  ? 221 THR A N     1 
ATOM   953  C CA    . THR A 1 136 ? 108.719 125.230 106.263 1.00 55.39  ? 221 THR A CA    1 
ATOM   954  C C     . THR A 1 136 ? 108.321 126.217 107.349 1.00 58.98  ? 221 THR A C     1 
ATOM   955  O O     . THR A 1 136 ? 107.448 127.063 107.127 1.00 65.25  ? 221 THR A O     1 
ATOM   956  C CB    . THR A 1 136 ? 107.790 124.017 106.277 1.00 59.66  ? 221 THR A CB    1 
ATOM   957  O OG1   . THR A 1 136 ? 107.908 123.335 107.533 1.00 63.45  ? 221 THR A OG1   1 
ATOM   958  C CG2   . THR A 1 136 ? 108.126 123.063 105.132 1.00 61.56  ? 221 THR A CG2   1 
ATOM   959  N N     . LEU A 1 137 ? 108.966 126.151 108.510 1.00 56.15  ? 222 LEU A N     1 
ATOM   960  C CA    . LEU A 1 137 ? 108.580 126.983 109.639 1.00 53.32  ? 222 LEU A CA    1 
ATOM   961  C C     . LEU A 1 137 ? 109.655 127.974 110.066 1.00 54.97  ? 222 LEU A C     1 
ATOM   962  O O     . LEU A 1 137 ? 109.378 128.848 110.879 1.00 61.99  ? 222 LEU A O     1 
ATOM   963  C CB    . LEU A 1 137 ? 108.180 126.095 110.825 1.00 52.37  ? 222 LEU A CB    1 
ATOM   964  C CG    . LEU A 1 137 ? 107.446 126.724 112.010 1.00 55.95  ? 222 LEU A CG    1 
ATOM   965  C CD1   . LEU A 1 137 ? 106.152 127.370 111.544 1.00 52.17  ? 222 LEU A CD1   1 
ATOM   966  C CD2   . LEU A 1 137 ? 107.171 125.679 113.085 1.00 55.00  ? 222 LEU A CD2   1 
ATOM   967  N N     . GLY A 1 138 ? 110.882 127.875 109.557 1.00 57.33  ? 223 GLY A N     1 
ATOM   968  C CA    . GLY A 1 138 ? 111.815 128.971 109.691 1.00 53.22  ? 223 GLY A CA    1 
ATOM   969  C C     . GLY A 1 138 ? 112.783 128.896 110.856 1.00 54.13  ? 223 GLY A C     1 
ATOM   970  O O     . GLY A 1 138 ? 112.704 128.021 111.726 1.00 58.25  ? 223 GLY A O     1 
ATOM   971  N N     . PRO A 1 139 ? 113.725 129.845 110.886 1.00 53.19  ? 224 PRO A N     1 
ATOM   972  C CA    . PRO A 1 139 ? 114.813 129.780 111.876 1.00 52.75  ? 224 PRO A CA    1 
ATOM   973  C C     . PRO A 1 139 ? 114.372 130.017 113.311 1.00 53.53  ? 224 PRO A C     1 
ATOM   974  O O     . PRO A 1 139 ? 115.020 129.498 114.228 1.00 55.06  ? 224 PRO A O     1 
ATOM   975  C CB    . PRO A 1 139 ? 115.776 130.880 111.407 1.00 51.96  ? 224 PRO A CB    1 
ATOM   976  C CG    . PRO A 1 139 ? 115.429 131.120 109.973 1.00 49.01  ? 224 PRO A CG    1 
ATOM   977  C CD    . PRO A 1 139 ? 113.955 130.888 109.874 1.00 52.12  ? 224 PRO A CD    1 
ATOM   978  N N     . ARG A 1 140 ? 113.308 130.795 113.540 1.00 55.45  ? 225 ARG A N     1 
ATOM   979  C CA    . ARG A 1 140 ? 112.884 131.086 114.908 1.00 52.14  ? 225 ARG A CA    1 
ATOM   980  C C     . ARG A 1 140 ? 112.510 129.824 115.669 1.00 54.25  ? 225 ARG A C     1 
ATOM   981  O O     . ARG A 1 140 ? 112.573 129.799 116.903 1.00 57.99  ? 225 ARG A O     1 
ATOM   982  C CB    . ARG A 1 140 ? 111.694 132.046 114.909 1.00 51.79  ? 225 ARG A CB    1 
ATOM   983  C CG    . ARG A 1 140 ? 111.960 133.434 114.360 1.00 61.05  ? 225 ARG A CG    1 
ATOM   984  C CD    . ARG A 1 140 ? 110.798 134.351 114.714 1.00 49.13  ? 225 ARG A CD    1 
ATOM   985  N NE    . ARG A 1 140 ? 111.036 135.740 114.345 1.00 47.66  ? 225 ARG A NE    1 
ATOM   986  C CZ    . ARG A 1 140 ? 110.284 136.757 114.746 1.00 58.91  ? 225 ARG A CZ    1 
ATOM   987  N NH1   . ARG A 1 140 ? 109.234 136.571 115.530 1.00 65.52  ? 225 ARG A NH1   1 
ATOM   988  N NH2   . ARG A 1 140 ? 110.594 137.989 114.354 1.00 58.57  ? 225 ARG A NH2   1 
ATOM   989  N N     . PHE A 1 141 ? 112.123 128.769 114.954 1.00 49.46  ? 226 PHE A N     1 
ATOM   990  C CA    . PHE A 1 141 ? 111.524 127.585 115.547 1.00 47.48  ? 226 PHE A CA    1 
ATOM   991  C C     . PHE A 1 141 ? 112.502 126.424 115.675 1.00 48.32  ? 226 PHE A C     1 
ATOM   992  O O     . PHE A 1 141 ? 112.071 125.283 115.862 1.00 50.09  ? 226 PHE A O     1 
ATOM   993  C CB    . PHE A 1 141 ? 110.301 127.172 114.731 1.00 46.12  ? 226 PHE A CB    1 
ATOM   994  C CG    . PHE A 1 141 ? 109.250 128.240 114.644 1.00 44.91  ? 226 PHE A CG    1 
ATOM   995  C CD1   . PHE A 1 141 ? 109.314 129.210 113.664 1.00 46.45  ? 226 PHE A CD1   1 
ATOM   996  C CD2   . PHE A 1 141 ? 108.179 128.253 115.518 1.00 48.13  ? 226 PHE A CD2   1 
ATOM   997  C CE1   . PHE A 1 141 ? 108.349 130.191 113.566 1.00 51.36  ? 226 PHE A CE1   1 
ATOM   998  C CE2   . PHE A 1 141 ? 107.205 129.231 115.426 1.00 45.53  ? 226 PHE A CE2   1 
ATOM   999  C CZ    . PHE A 1 141 ? 107.292 130.201 114.448 1.00 49.04  ? 226 PHE A CZ    1 
ATOM   1000 N N     . MET A 1 142 ? 113.808 126.691 115.592 1.00 44.81  ? 227 MET A N     1 
ATOM   1001 C CA    . MET A 1 142 ? 114.783 125.620 115.774 1.00 44.12  ? 227 MET A CA    1 
ATOM   1002 C C     . MET A 1 142 ? 114.634 124.974 117.146 1.00 50.01  ? 227 MET A C     1 
ATOM   1003 O O     . MET A 1 142 ? 114.703 123.747 117.273 1.00 53.22  ? 227 MET A O     1 
ATOM   1004 C CB    . MET A 1 142 ? 116.202 126.156 115.587 1.00 50.98  ? 227 MET A CB    1 
ATOM   1005 C CG    . MET A 1 142 ? 117.272 125.282 116.221 1.00 55.65  ? 227 MET A CG    1 
ATOM   1006 S SD    . MET A 1 142 ? 118.908 125.543 115.518 1.00 70.60  ? 227 MET A SD    1 
ATOM   1007 C CE    . MET A 1 142 ? 118.710 124.819 113.894 1.00 62.08  ? 227 MET A CE    1 
ATOM   1008 N N     . GLY A 1 143 ? 114.413 125.784 118.179 1.00 52.05  ? 228 GLY A N     1 
ATOM   1009 C CA    . GLY A 1 143 ? 114.208 125.290 119.520 1.00 43.77  ? 228 GLY A CA    1 
ATOM   1010 C C     . GLY A 1 143 ? 113.027 124.346 119.650 1.00 41.07  ? 228 GLY A C     1 
ATOM   1011 O O     . GLY A 1 143 ? 113.184 123.179 120.024 1.00 43.86  ? 228 GLY A O     1 
ATOM   1012 N N     . PRO A 1 144 ? 111.816 124.835 119.362 1.00 42.26  ? 229 PRO A N     1 
ATOM   1013 C CA    . PRO A 1 144 ? 110.635 123.959 119.470 1.00 40.99  ? 229 PRO A CA    1 
ATOM   1014 C C     . PRO A 1 144 ? 110.695 122.740 118.565 1.00 46.85  ? 229 PRO A C     1 
ATOM   1015 O O     . PRO A 1 144 ? 110.206 121.671 118.952 1.00 50.40  ? 229 PRO A O     1 
ATOM   1016 C CB    . PRO A 1 144 ? 109.468 124.885 119.093 1.00 39.58  ? 229 PRO A CB    1 
ATOM   1017 C CG    . PRO A 1 144 ? 110.086 126.090 118.470 1.00 37.82  ? 229 PRO A CG    1 
ATOM   1018 C CD    . PRO A 1 144 ? 111.445 126.228 119.063 1.00 40.60  ? 229 PRO A CD    1 
ATOM   1019 N N     . ILE A 1 145 ? 111.271 122.868 117.369 1.00 47.63  ? 230 ILE A N     1 
ATOM   1020 C CA    . ILE A 1 145 ? 111.426 121.709 116.496 1.00 47.73  ? 230 ILE A CA    1 
ATOM   1021 C C     . ILE A 1 145 ? 112.481 120.751 117.041 1.00 48.40  ? 230 ILE A C     1 
ATOM   1022 O O     . ILE A 1 145 ? 112.376 119.533 116.848 1.00 52.88  ? 230 ILE A O     1 
ATOM   1023 C CB    . ILE A 1 145 ? 111.748 122.165 115.060 1.00 47.74  ? 230 ILE A CB    1 
ATOM   1024 C CG1   . ILE A 1 145 ? 110.583 122.980 114.491 1.00 47.62  ? 230 ILE A CG1   1 
ATOM   1025 C CG2   . ILE A 1 145 ? 112.041 120.976 114.157 1.00 53.79  ? 230 ILE A CG2   1 
ATOM   1026 C CD1   . ILE A 1 145 ? 110.907 123.684 113.194 1.00 56.86  ? 230 ILE A CD1   1 
ATOM   1027 N N     . ALA A 1 146 ? 113.494 121.268 117.743 1.00 48.67  ? 231 ALA A N     1 
ATOM   1028 C CA    . ALA A 1 146 ? 114.556 120.415 118.267 1.00 47.38  ? 231 ALA A CA    1 
ATOM   1029 C C     . ALA A 1 146 ? 114.038 119.380 119.256 1.00 45.30  ? 231 ALA A C     1 
ATOM   1030 O O     . ALA A 1 146 ? 114.690 118.348 119.449 1.00 43.53  ? 231 ALA A O     1 
ATOM   1031 C CB    . ALA A 1 146 ? 115.641 121.265 118.928 1.00 46.65  ? 231 ALA A CB    1 
ATOM   1032 N N     . ILE A 1 147 ? 112.888 119.629 119.887 1.00 48.60  ? 232 ILE A N     1 
ATOM   1033 C CA    . ILE A 1 147 ? 112.295 118.629 120.770 1.00 47.09  ? 232 ILE A CA    1 
ATOM   1034 C C     . ILE A 1 147 ? 111.945 117.371 119.990 1.00 49.02  ? 232 ILE A C     1 
ATOM   1035 O O     . ILE A 1 147 ? 112.103 116.252 120.493 1.00 53.07  ? 232 ILE A O     1 
ATOM   1036 C CB    . ILE A 1 147 ? 111.064 119.218 121.489 1.00 46.62  ? 232 ILE A CB    1 
ATOM   1037 C CG1   . ILE A 1 147 ? 111.494 120.291 122.489 1.00 47.13  ? 232 ILE A CG1   1 
ATOM   1038 C CG2   . ILE A 1 147 ? 110.271 118.127 122.194 1.00 49.83  ? 232 ILE A CG2   1 
ATOM   1039 C CD1   . ILE A 1 147 ? 110.355 120.850 123.305 1.00 49.79  ? 232 ILE A CD1   1 
ATOM   1040 N N     . LEU A 1 148 ? 111.478 117.526 118.753 1.00 52.96  ? 233 LEU A N     1 
ATOM   1041 C CA    . LEU A 1 148 ? 111.123 116.385 117.920 1.00 48.65  ? 233 LEU A CA    1 
ATOM   1042 C C     . LEU A 1 148 ? 112.338 115.718 117.285 1.00 51.37  ? 233 LEU A C     1 
ATOM   1043 O O     . LEU A 1 148 ? 112.288 114.517 116.993 1.00 58.91  ? 233 LEU A O     1 
ATOM   1044 C CB    . LEU A 1 148 ? 110.125 116.824 116.842 1.00 52.10  ? 233 LEU A CB    1 
ATOM   1045 C CG    . LEU A 1 148 ? 109.416 115.775 115.982 1.00 67.52  ? 233 LEU A CG    1 
ATOM   1046 C CD1   . LEU A 1 148 ? 108.007 116.240 115.659 1.00 68.59  ? 233 LEU A CD1   1 
ATOM   1047 C CD2   . LEU A 1 148 ? 110.179 115.525 114.693 1.00 64.04  ? 233 LEU A CD2   1 
ATOM   1048 N N     . ARG A 1 149 ? 113.428 116.460 117.063 1.00 47.24  ? 234 ARG A N     1 
ATOM   1049 C CA    . ARG A 1 149 ? 114.639 115.852 116.515 1.00 47.00  ? 234 ARG A CA    1 
ATOM   1050 C C     . ARG A 1 149 ? 115.225 114.831 117.478 1.00 52.46  ? 234 ARG A C     1 
ATOM   1051 O O     . ARG A 1 149 ? 115.480 113.680 117.108 1.00 57.60  ? 234 ARG A O     1 
ATOM   1052 C CB    . ARG A 1 149 ? 115.687 116.923 116.207 1.00 49.31  ? 234 ARG A CB    1 
ATOM   1053 C CG    . ARG A 1 149 ? 115.158 118.203 115.609 1.00 54.29  ? 234 ARG A CG    1 
ATOM   1054 C CD    . ARG A 1 149 ? 116.294 119.030 115.027 1.00 58.90  ? 234 ARG A CD    1 
ATOM   1055 N NE    . ARG A 1 149 ? 117.011 118.311 113.981 1.00 60.61  ? 234 ARG A NE    1 
ATOM   1056 C CZ    . ARG A 1 149 ? 117.379 118.841 112.823 1.00 61.26  ? 234 ARG A CZ    1 
ATOM   1057 N NH1   . ARG A 1 149 ? 117.109 120.101 112.522 1.00 56.33  ? 234 ARG A NH1   1 
ATOM   1058 N NH2   . ARG A 1 149 ? 118.035 118.088 111.944 1.00 64.79  ? 234 ARG A NH2   1 
ATOM   1059 N N     . ILE A 1 150 ? 115.437 115.237 118.727 1.00 50.08  ? 235 ILE A N     1 
ATOM   1060 C CA    . ILE A 1 150 ? 116.194 114.458 119.700 1.00 46.19  ? 235 ILE A CA    1 
ATOM   1061 C C     . ILE A 1 150 ? 115.284 114.062 120.854 1.00 44.19  ? 235 ILE A C     1 
ATOM   1062 O O     . ILE A 1 150 ? 115.706 114.050 122.015 1.00 47.57  ? 235 ILE A O     1 
ATOM   1063 C CB    . ILE A 1 150 ? 117.426 115.239 120.192 1.00 44.54  ? 235 ILE A CB    1 
ATOM   1064 C CG1   . ILE A 1 150 ? 117.013 116.609 120.730 1.00 46.82  ? 235 ILE A CG1   1 
ATOM   1065 C CG2   . ILE A 1 150 ? 118.444 115.388 119.071 1.00 43.79  ? 235 ILE A CG2   1 
ATOM   1066 C CD1   . ILE A 1 150 ? 118.102 117.316 121.491 1.00 48.57  ? 235 ILE A CD1   1 
ATOM   1067 N N     . TRP A 1 151 ? 114.017 113.769 120.536 1.00 43.98  ? 236 TRP A N     1 
ATOM   1068 C CA    . TRP A 1 151 ? 113.030 113.396 121.547 1.00 44.33  ? 236 TRP A CA    1 
ATOM   1069 C C     . TRP A 1 151 ? 113.560 112.370 122.543 1.00 49.90  ? 236 TRP A C     1 
ATOM   1070 O O     . TRP A 1 151 ? 113.195 112.409 123.724 1.00 54.66  ? 236 TRP A O     1 
ATOM   1071 C CB    . TRP A 1 151 ? 111.772 112.861 120.862 1.00 45.13  ? 236 TRP A CB    1 
ATOM   1072 C CG    . TRP A 1 151 ? 111.987 111.561 120.148 1.00 51.73  ? 236 TRP A CG    1 
ATOM   1073 C CD1   . TRP A 1 151 ? 112.393 111.393 118.855 1.00 50.88  ? 236 TRP A CD1   1 
ATOM   1074 C CD2   . TRP A 1 151 ? 111.820 110.246 120.689 1.00 54.36  ? 236 TRP A CD2   1 
ATOM   1075 N NE1   . TRP A 1 151 ? 112.482 110.056 118.557 1.00 56.34  ? 236 TRP A NE1   1 
ATOM   1076 C CE2   . TRP A 1 151 ? 112.137 109.330 119.667 1.00 55.16  ? 236 TRP A CE2   1 
ATOM   1077 C CE3   . TRP A 1 151 ? 111.433 109.753 121.939 1.00 52.14  ? 236 TRP A CE3   1 
ATOM   1078 C CZ2   . TRP A 1 151 ? 112.074 107.951 119.854 1.00 59.49  ? 236 TRP A CZ2   1 
ATOM   1079 C CZ3   . TRP A 1 151 ? 111.374 108.384 122.124 1.00 54.25  ? 236 TRP A CZ3   1 
ATOM   1080 C CH2   . TRP A 1 151 ? 111.694 107.500 121.088 1.00 61.49  ? 236 TRP A CH2   1 
ATOM   1081 N N     . SER A 1 152 ? 114.411 111.444 122.094 1.00 51.65  ? 237 SER A N     1 
ATOM   1082 C CA    . SER A 1 152 ? 115.020 110.498 123.022 1.00 43.86  ? 237 SER A CA    1 
ATOM   1083 C C     . SER A 1 152 ? 115.980 111.187 123.981 1.00 46.72  ? 237 SER A C     1 
ATOM   1084 O O     . SER A 1 152 ? 116.067 110.797 125.151 1.00 50.36  ? 237 SER A O     1 
ATOM   1085 C CB    . SER A 1 152 ? 115.752 109.397 122.255 1.00 49.82  ? 237 SER A CB    1 
ATOM   1086 O OG    . SER A 1 152 ? 116.376 108.488 123.145 1.00 64.94  ? 237 SER A OG    1 
ATOM   1087 N N     . PHE A 1 153 ? 116.712 112.196 123.507 1.00 46.44  ? 238 PHE A N     1 
ATOM   1088 C CA    . PHE A 1 153 ? 117.532 113.012 124.393 1.00 42.52  ? 238 PHE A CA    1 
ATOM   1089 C C     . PHE A 1 153 ? 116.683 113.916 125.272 1.00 41.00  ? 238 PHE A C     1 
ATOM   1090 O O     . PHE A 1 153 ? 117.094 114.239 126.392 1.00 45.06  ? 238 PHE A O     1 
ATOM   1091 C CB    . PHE A 1 153 ? 118.516 113.858 123.578 1.00 41.84  ? 238 PHE A CB    1 
ATOM   1092 C CG    . PHE A 1 153 ? 119.533 113.052 122.814 1.00 42.24  ? 238 PHE A CG    1 
ATOM   1093 C CD1   . PHE A 1 153 ? 119.628 111.679 122.980 1.00 43.09  ? 238 PHE A CD1   1 
ATOM   1094 C CD2   . PHE A 1 153 ? 120.391 113.672 121.922 1.00 47.94  ? 238 PHE A CD2   1 
ATOM   1095 C CE1   . PHE A 1 153 ? 120.559 110.944 122.275 1.00 47.80  ? 238 PHE A CE1   1 
ATOM   1096 C CE2   . PHE A 1 153 ? 121.324 112.942 121.214 1.00 52.64  ? 238 PHE A CE2   1 
ATOM   1097 C CZ    . PHE A 1 153 ? 121.407 111.576 121.391 1.00 51.97  ? 238 PHE A CZ    1 
ATOM   1098 N N     . CYS A 1 154 ? 115.513 114.329 124.783 1.00 44.34  ? 239 CYS A N     1 
ATOM   1099 C CA    . CYS A 1 154 ? 114.559 115.070 125.594 1.00 40.70  ? 239 CYS A CA    1 
ATOM   1100 C C     . CYS A 1 154 ? 113.928 114.205 126.675 1.00 41.75  ? 239 CYS A C     1 
ATOM   1101 O O     . CYS A 1 154 ? 113.563 114.726 127.734 1.00 46.94  ? 239 CYS A O     1 
ATOM   1102 C CB    . CYS A 1 154 ? 113.467 115.665 124.703 1.00 39.80  ? 239 CYS A CB    1 
ATOM   1103 S SG    . CYS A 1 154 ? 114.060 116.915 123.537 1.00 43.93  ? 239 CYS A SG    1 
ATOM   1104 N N     . LEU A 1 155 ? 113.782 112.901 126.427 1.00 44.60  ? 240 LEU A N     1 
ATOM   1105 C CA    . LEU A 1 155 ? 113.301 111.998 127.466 1.00 43.66  ? 240 LEU A CA    1 
ATOM   1106 C C     . LEU A 1 155 ? 114.365 111.778 128.535 1.00 44.35  ? 240 LEU A C     1 
ATOM   1107 O O     . LEU A 1 155 ? 114.044 111.705 129.726 1.00 45.51  ? 240 LEU A O     1 
ATOM   1108 C CB    . LEU A 1 155 ? 112.865 110.669 126.844 1.00 45.62  ? 240 LEU A CB    1 
ATOM   1109 C CG    . LEU A 1 155 ? 112.494 109.531 127.797 1.00 55.19  ? 240 LEU A CG    1 
ATOM   1110 C CD1   . LEU A 1 155 ? 111.362 109.949 128.721 1.00 56.16  ? 240 LEU A CD1   1 
ATOM   1111 C CD2   . LEU A 1 155 ? 112.116 108.284 127.014 1.00 58.21  ? 240 LEU A CD2   1 
ATOM   1112 N N     . PHE A 1 156 ? 115.634 111.673 128.130 1.00 46.99  ? 241 PHE A N     1 
ATOM   1113 C CA    . PHE A 1 156 ? 116.722 111.640 129.102 1.00 38.83  ? 241 PHE A CA    1 
ATOM   1114 C C     . PHE A 1 156 ? 116.756 112.913 129.934 1.00 44.40  ? 241 PHE A C     1 
ATOM   1115 O O     . PHE A 1 156 ? 117.098 112.872 131.121 1.00 54.23  ? 241 PHE A O     1 
ATOM   1116 C CB    . PHE A 1 156 ? 118.059 111.433 128.384 1.00 36.83  ? 241 PHE A CB    1 
ATOM   1117 C CG    . PHE A 1 156 ? 119.247 111.328 129.308 1.00 46.73  ? 241 PHE A CG    1 
ATOM   1118 C CD1   . PHE A 1 156 ? 119.914 112.464 129.743 1.00 47.45  ? 241 PHE A CD1   1 
ATOM   1119 C CD2   . PHE A 1 156 ? 119.707 110.091 129.727 1.00 49.51  ? 241 PHE A CD2   1 
ATOM   1120 C CE1   . PHE A 1 156 ? 121.006 112.368 130.586 1.00 44.52  ? 241 PHE A CE1   1 
ATOM   1121 C CE2   . PHE A 1 156 ? 120.801 109.989 130.568 1.00 49.21  ? 241 PHE A CE2   1 
ATOM   1122 C CZ    . PHE A 1 156 ? 121.449 111.129 130.998 1.00 46.31  ? 241 PHE A CZ    1 
ATOM   1123 N N     . TYR A 1 157 ? 116.410 114.050 129.327 1.00 45.12  ? 242 TYR A N     1 
ATOM   1124 C CA    . TYR A 1 157 ? 116.433 115.321 130.044 1.00 37.85  ? 242 TYR A CA    1 
ATOM   1125 C C     . TYR A 1 157 ? 115.421 115.329 131.184 1.00 38.31  ? 242 TYR A C     1 
ATOM   1126 O O     . TYR A 1 157 ? 115.742 115.731 132.308 1.00 44.18  ? 242 TYR A O     1 
ATOM   1127 C CB    . TYR A 1 157 ? 116.164 116.466 129.066 1.00 38.75  ? 242 TYR A CB    1 
ATOM   1128 C CG    . TYR A 1 157 ? 116.319 117.850 129.656 1.00 38.55  ? 242 TYR A CG    1 
ATOM   1129 C CD1   . TYR A 1 157 ? 115.244 118.499 130.252 1.00 39.92  ? 242 TYR A CD1   1 
ATOM   1130 C CD2   . TYR A 1 157 ? 117.538 118.512 129.609 1.00 41.02  ? 242 TYR A CD2   1 
ATOM   1131 C CE1   . TYR A 1 157 ? 115.382 119.765 130.788 1.00 38.20  ? 242 TYR A CE1   1 
ATOM   1132 C CE2   . TYR A 1 157 ? 117.686 119.777 130.142 1.00 41.25  ? 242 TYR A CE2   1 
ATOM   1133 C CZ    . TYR A 1 157 ? 116.605 120.399 130.730 1.00 45.68  ? 242 TYR A CZ    1 
ATOM   1134 O OH    . TYR A 1 157 ? 116.749 121.659 131.262 1.00 58.00  ? 242 TYR A OH    1 
ATOM   1135 N N     . VAL A 1 158 ? 114.192 114.882 130.915 1.00 38.89  ? 243 VAL A N     1 
ATOM   1136 C CA    . VAL A 1 158 ? 113.167 114.898 131.954 1.00 41.15  ? 243 VAL A CA    1 
ATOM   1137 C C     . VAL A 1 158 ? 113.444 113.839 133.016 1.00 44.85  ? 243 VAL A C     1 
ATOM   1138 O O     . VAL A 1 158 ? 113.115 114.034 134.192 1.00 53.06  ? 243 VAL A O     1 
ATOM   1139 C CB    . VAL A 1 158 ? 111.763 114.742 131.335 1.00 44.66  ? 243 VAL A CB    1 
ATOM   1140 C CG1   . VAL A 1 158 ? 111.584 115.727 130.193 1.00 44.99  ? 243 VAL A CG1   1 
ATOM   1141 C CG2   . VAL A 1 158 ? 111.525 113.319 130.852 1.00 45.81  ? 243 VAL A CG2   1 
ATOM   1142 N N     . MET A 1 159 ? 114.048 112.709 132.637 1.00 43.61  ? 244 MET A N     1 
ATOM   1143 C CA    . MET A 1 159 ? 114.411 111.708 133.635 1.00 39.50  ? 244 MET A CA    1 
ATOM   1144 C C     . MET A 1 159 ? 115.573 112.186 134.497 1.00 42.29  ? 244 MET A C     1 
ATOM   1145 O O     . MET A 1 159 ? 115.583 111.956 135.711 1.00 49.25  ? 244 MET A O     1 
ATOM   1146 C CB    . MET A 1 159 ? 114.748 110.378 132.958 1.00 42.75  ? 244 MET A CB    1 
ATOM   1147 C CG    . MET A 1 159 ? 113.620 109.817 132.103 1.00 46.55  ? 244 MET A CG    1 
ATOM   1148 S SD    . MET A 1 159 ? 112.442 108.811 133.026 1.00 68.39  ? 244 MET A SD    1 
ATOM   1149 C CE    . MET A 1 159 ? 113.547 107.795 134.002 1.00 45.89  ? 244 MET A CE    1 
ATOM   1150 N N     . ALA A 1 160 ? 116.558 112.855 133.893 1.00 39.20  ? 245 ALA A N     1 
ATOM   1151 C CA    . ALA A 1 160 ? 117.609 113.482 134.682 1.00 36.36  ? 245 ALA A CA    1 
ATOM   1152 C C     . ALA A 1 160 ? 117.075 114.636 135.520 1.00 44.21  ? 245 ALA A C     1 
ATOM   1153 O O     . ALA A 1 160 ? 117.610 114.900 136.602 1.00 50.01  ? 245 ALA A O     1 
ATOM   1154 C CB    . ALA A 1 160 ? 118.737 113.972 133.773 1.00 35.12  ? 245 ALA A CB    1 
ATOM   1155 N N     . GLU A 1 161 ? 116.038 115.328 135.043 1.00 45.56  ? 246 GLU A N     1 
ATOM   1156 C CA    . GLU A 1 161 ? 115.398 116.367 135.841 1.00 39.76  ? 246 GLU A CA    1 
ATOM   1157 C C     . GLU A 1 161 ? 114.576 115.770 136.977 1.00 39.20  ? 246 GLU A C     1 
ATOM   1158 O O     . GLU A 1 161 ? 114.538 116.330 138.079 1.00 50.96  ? 246 GLU A O     1 
ATOM   1159 C CB    . GLU A 1 161 ? 114.516 117.245 134.952 1.00 41.48  ? 246 GLU A CB    1 
ATOM   1160 C CG    . GLU A 1 161 ? 115.274 118.307 134.175 1.00 41.62  ? 246 GLU A CG    1 
ATOM   1161 C CD    . GLU A 1 161 ? 115.363 119.620 134.926 1.00 52.24  ? 246 GLU A CD    1 
ATOM   1162 O OE1   . GLU A 1 161 ? 114.413 119.947 135.667 1.00 58.51  ? 246 GLU A OE1   1 
ATOM   1163 O OE2   . GLU A 1 161 ? 116.380 120.327 134.773 1.00 57.68  ? 246 GLU A OE2   1 
ATOM   1164 N N     . LEU A 1 162 ? 113.910 114.640 136.728 1.00 38.47  ? 247 LEU A N     1 
ATOM   1165 C CA    . LEU A 1 162 ? 113.122 113.996 137.771 1.00 39.55  ? 247 LEU A CA    1 
ATOM   1166 C C     . LEU A 1 162 ? 113.991 113.380 138.857 1.00 45.16  ? 247 LEU A C     1 
ATOM   1167 O O     . LEU A 1 162 ? 113.516 113.203 139.984 1.00 51.33  ? 247 LEU A O     1 
ATOM   1168 C CB    . LEU A 1 162 ? 112.212 112.926 137.165 1.00 42.16  ? 247 LEU A CB    1 
ATOM   1169 C CG    . LEU A 1 162 ? 110.914 113.400 136.509 1.00 42.82  ? 247 LEU A CG    1 
ATOM   1170 C CD1   . LEU A 1 162 ? 110.263 112.265 135.732 1.00 46.92  ? 247 LEU A CD1   1 
ATOM   1171 C CD2   . LEU A 1 162 ? 109.957 113.955 137.552 1.00 50.42  ? 247 LEU A CD2   1 
ATOM   1172 N N     . TRP A 1 163 ? 115.246 113.042 138.549 1.00 44.62  ? 248 TRP A N     1 
ATOM   1173 C CA    . TRP A 1 163 ? 116.134 112.502 139.573 1.00 41.69  ? 248 TRP A CA    1 
ATOM   1174 C C     . TRP A 1 163 ? 116.399 113.530 140.666 1.00 46.31  ? 248 TRP A C     1 
ATOM   1175 O O     . TRP A 1 163 ? 116.324 113.217 141.859 1.00 51.79  ? 248 TRP A O     1 
ATOM   1176 C CB    . TRP A 1 163 ? 117.446 112.035 138.941 1.00 45.84  ? 248 TRP A CB    1 
ATOM   1177 C CG    . TRP A 1 163 ? 118.405 111.441 139.931 1.00 44.63  ? 248 TRP A CG    1 
ATOM   1178 C CD1   . TRP A 1 163 ? 119.324 112.110 140.686 1.00 43.24  ? 248 TRP A CD1   1 
ATOM   1179 C CD2   . TRP A 1 163 ? 118.534 110.056 140.277 1.00 40.90  ? 248 TRP A CD2   1 
ATOM   1180 N NE1   . TRP A 1 163 ? 120.018 111.229 141.479 1.00 38.66  ? 248 TRP A NE1   1 
ATOM   1181 C CE2   . TRP A 1 163 ? 119.553 109.962 141.247 1.00 39.71  ? 248 TRP A CE2   1 
ATOM   1182 C CE3   . TRP A 1 163 ? 117.890 108.888 139.860 1.00 42.60  ? 248 TRP A CE3   1 
ATOM   1183 C CZ2   . TRP A 1 163 ? 119.941 108.747 141.806 1.00 42.74  ? 248 TRP A CZ2   1 
ATOM   1184 C CZ3   . TRP A 1 163 ? 118.276 107.682 140.417 1.00 43.94  ? 248 TRP A CZ3   1 
ATOM   1185 C CH2   . TRP A 1 163 ? 119.292 107.621 141.379 1.00 46.21  ? 248 TRP A CH2   1 
ATOM   1186 N N     . GLY A 1 164 ? 116.703 114.767 140.277 1.00 45.99  ? 249 GLY A N     1 
ATOM   1187 C CA    . GLY A 1 164 ? 116.926 115.815 141.256 1.00 45.95  ? 249 GLY A CA    1 
ATOM   1188 C C     . GLY A 1 164 ? 115.688 116.233 142.019 1.00 51.94  ? 249 GLY A C     1 
ATOM   1189 O O     . GLY A 1 164 ? 115.811 116.684 143.162 1.00 62.07  ? 249 GLY A O     1 
ATOM   1190 N N     . SER A 1 165 ? 114.506 116.090 141.425 1.00 49.55  ? 250 SER A N     1 
ATOM   1191 C CA    . SER A 1 165 ? 113.262 116.493 142.068 1.00 46.96  ? 250 SER A CA    1 
ATOM   1192 C C     . SER A 1 165 ? 112.640 115.391 142.913 1.00 50.32  ? 250 SER A C     1 
ATOM   1193 O O     . SER A 1 165 ? 111.980 115.686 143.913 1.00 62.81  ? 250 SER A O     1 
ATOM   1194 C CB    . SER A 1 165 ? 112.252 116.958 141.015 1.00 49.43  ? 250 SER A CB    1 
ATOM   1195 O OG    . SER A 1 165 ? 111.661 115.854 140.353 1.00 54.85  ? 250 SER A OG    1 
ATOM   1196 N N     . VAL A 1 166 ? 112.832 114.130 142.541 1.00 47.99  ? 251 VAL A N     1 
ATOM   1197 C CA    . VAL A 1 166 ? 112.233 113.012 143.256 1.00 50.08  ? 251 VAL A CA    1 
ATOM   1198 C C     . VAL A 1 166 ? 113.240 112.307 144.155 1.00 49.96  ? 251 VAL A C     1 
ATOM   1199 O O     . VAL A 1 166 ? 112.965 112.073 145.331 1.00 55.75  ? 251 VAL A O     1 
ATOM   1200 C CB    . VAL A 1 166 ? 111.596 112.019 142.263 1.00 45.14  ? 251 VAL A CB    1 
ATOM   1201 C CG1   . VAL A 1 166 ? 110.928 110.888 143.021 1.00 52.97  ? 251 VAL A CG1   1 
ATOM   1202 C CG2   . VAL A 1 166 ? 110.607 112.735 141.359 1.00 47.34  ? 251 VAL A CG2   1 
ATOM   1203 N N     . VAL A 1 167 ? 114.403 111.945 143.618 1.00 49.02  ? 252 VAL A N     1 
ATOM   1204 C CA    . VAL A 1 167 ? 115.377 111.196 144.405 1.00 49.70  ? 252 VAL A CA    1 
ATOM   1205 C C     . VAL A 1 167 ? 116.075 112.104 145.409 1.00 50.15  ? 252 VAL A C     1 
ATOM   1206 O O     . VAL A 1 167 ? 116.238 111.747 146.582 1.00 56.76  ? 252 VAL A O     1 
ATOM   1207 C CB    . VAL A 1 167 ? 116.383 110.492 143.477 1.00 48.95  ? 252 VAL A CB    1 
ATOM   1208 C CG1   . VAL A 1 167 ? 117.364 109.663 144.289 1.00 44.08  ? 252 VAL A CG1   1 
ATOM   1209 C CG2   . VAL A 1 167 ? 115.646 109.622 142.471 1.00 46.87  ? 252 VAL A CG2   1 
ATOM   1210 N N     . VAL A 1 168 ? 116.497 113.292 144.970 1.00 46.36  ? 253 VAL A N     1 
ATOM   1211 C CA    . VAL A 1 168 ? 117.189 114.208 145.871 1.00 50.11  ? 253 VAL A CA    1 
ATOM   1212 C C     . VAL A 1 168 ? 116.227 114.756 146.918 1.00 53.94  ? 253 VAL A C     1 
ATOM   1213 O O     . VAL A 1 168 ? 116.561 114.842 148.105 1.00 66.93  ? 253 VAL A O     1 
ATOM   1214 C CB    . VAL A 1 168 ? 117.857 115.344 145.075 1.00 52.61  ? 253 VAL A CB    1 
ATOM   1215 C CG1   . VAL A 1 168 ? 118.352 116.437 146.014 1.00 54.02  ? 253 VAL A CG1   1 
ATOM   1216 C CG2   . VAL A 1 168 ? 118.982 114.813 144.204 1.00 48.67  ? 253 VAL A CG2   1 
ATOM   1217 N N     . SER A 1 169 ? 115.016 115.125 146.499 1.00 54.84  ? 254 SER A N     1 
ATOM   1218 C CA    . SER A 1 169 ? 114.070 115.827 147.361 1.00 59.29  ? 254 SER A CA    1 
ATOM   1219 C C     . SER A 1 169 ? 113.027 114.895 147.970 1.00 52.72  ? 254 SER A C     1 
ATOM   1220 O O     . SER A 1 169 ? 112.870 114.850 149.194 1.00 62.70  ? 254 SER A O     1 
ATOM   1221 C CB    . SER A 1 169 ? 113.384 116.948 146.570 1.00 60.33  ? 254 SER A CB    1 
ATOM   1222 O OG    . SER A 1 169 ? 114.321 117.919 146.139 1.00 57.71  ? 254 SER A OG    1 
ATOM   1223 N N     . VAL A 1 170 ? 112.303 114.149 147.137 1.00 49.56  ? 255 VAL A N     1 
ATOM   1224 C CA    . VAL A 1 170 ? 111.171 113.372 147.634 1.00 53.19  ? 255 VAL A CA    1 
ATOM   1225 C C     . VAL A 1 170 ? 111.637 112.057 148.249 1.00 57.24  ? 255 VAL A C     1 
ATOM   1226 O O     . VAL A 1 170 ? 111.295 111.738 149.393 1.00 61.34  ? 255 VAL A O     1 
ATOM   1227 C CB    . VAL A 1 170 ? 110.151 113.138 146.504 1.00 56.11  ? 255 VAL A CB    1 
ATOM   1228 C CG1   . VAL A 1 170 ? 109.179 112.036 146.887 1.00 57.94  ? 255 VAL A CG1   1 
ATOM   1229 C CG2   . VAL A 1 170 ? 109.407 114.425 146.191 1.00 57.77  ? 255 VAL A CG2   1 
ATOM   1230 N N     . LEU A 1 171 ? 112.418 111.273 147.501 1.00 59.83  ? 256 LEU A N     1 
ATOM   1231 C CA    . LEU A 1 171 ? 112.791 109.940 147.968 1.00 56.72  ? 256 LEU A CA    1 
ATOM   1232 C C     . LEU A 1 171 ? 113.701 110.004 149.189 1.00 59.36  ? 256 LEU A C     1 
ATOM   1233 O O     . LEU A 1 171 ? 113.447 109.337 150.198 1.00 63.16  ? 256 LEU A O     1 
ATOM   1234 C CB    . LEU A 1 171 ? 113.461 109.155 146.840 1.00 53.59  ? 256 LEU A CB    1 
ATOM   1235 C CG    . LEU A 1 171 ? 112.537 108.463 145.837 1.00 54.10  ? 256 LEU A CG    1 
ATOM   1236 C CD1   . LEU A 1 171 ? 113.316 107.452 145.012 1.00 55.36  ? 256 LEU A CD1   1 
ATOM   1237 C CD2   . LEU A 1 171 ? 111.372 107.794 146.550 1.00 59.78  ? 256 LEU A CD2   1 
ATOM   1238 N N     . PHE A 1 172 ? 114.771 110.799 149.118 1.00 53.27  ? 257 PHE A N     1 
ATOM   1239 C CA    . PHE A 1 172 ? 115.739 110.824 150.211 1.00 56.93  ? 257 PHE A CA    1 
ATOM   1240 C C     . PHE A 1 172 ? 115.155 111.479 151.455 1.00 62.22  ? 257 PHE A C     1 
ATOM   1241 O O     . PHE A 1 172 ? 115.071 110.856 152.520 1.00 68.36  ? 257 PHE A O     1 
ATOM   1242 C CB    . PHE A 1 172 ? 117.014 111.549 149.786 1.00 56.87  ? 257 PHE A CB    1 
ATOM   1243 C CG    . PHE A 1 172 ? 117.961 111.794 150.923 1.00 56.85  ? 257 PHE A CG    1 
ATOM   1244 C CD1   . PHE A 1 172 ? 118.614 110.737 151.535 1.00 56.95  ? 257 PHE A CD1   1 
ATOM   1245 C CD2   . PHE A 1 172 ? 118.170 113.074 151.406 1.00 59.08  ? 257 PHE A CD2   1 
ATOM   1246 C CE1   . PHE A 1 172 ? 119.475 110.955 152.592 1.00 59.27  ? 257 PHE A CE1   1 
ATOM   1247 C CE2   . PHE A 1 172 ? 119.031 113.297 152.463 1.00 59.85  ? 257 PHE A CE2   1 
ATOM   1248 C CZ    . PHE A 1 172 ? 119.680 112.236 153.059 1.00 58.44  ? 257 PHE A CZ    1 
ATOM   1249 N N     . TRP A 1 173 ? 114.757 112.749 151.343 1.00 60.39  ? 258 TRP A N     1 
ATOM   1250 C CA    . TRP A 1 173 ? 114.261 113.477 152.504 1.00 63.11  ? 258 TRP A CA    1 
ATOM   1251 C C     . TRP A 1 173 ? 112.993 112.855 153.070 1.00 69.24  ? 258 TRP A C     1 
ATOM   1252 O O     . TRP A 1 173 ? 112.713 113.022 154.262 1.00 78.40  ? 258 TRP A O     1 
ATOM   1253 C CB    . TRP A 1 173 ? 114.023 114.943 152.141 1.00 61.31  ? 258 TRP A CB    1 
ATOM   1254 C CG    . TRP A 1 173 ? 115.285 115.687 151.801 1.00 61.84  ? 258 TRP A CG    1 
ATOM   1255 C CD1   . TRP A 1 173 ? 115.572 116.316 150.625 1.00 59.73  ? 258 TRP A CD1   1 
ATOM   1256 C CD2   . TRP A 1 173 ? 116.427 115.881 152.648 1.00 67.92  ? 258 TRP A CD2   1 
ATOM   1257 N NE1   . TRP A 1 173 ? 116.821 116.886 150.684 1.00 64.39  ? 258 TRP A NE1   1 
ATOM   1258 C CE2   . TRP A 1 173 ? 117.366 116.635 151.915 1.00 67.58  ? 258 TRP A CE2   1 
ATOM   1259 C CE3   . TRP A 1 173 ? 116.746 115.492 153.952 1.00 66.20  ? 258 TRP A CE3   1 
ATOM   1260 C CZ2   . TRP A 1 173 ? 118.601 117.005 152.443 1.00 63.22  ? 258 TRP A CZ2   1 
ATOM   1261 C CZ3   . TRP A 1 173 ? 117.974 115.861 154.474 1.00 67.46  ? 258 TRP A CZ3   1 
ATOM   1262 C CH2   . TRP A 1 173 ? 118.886 116.610 153.720 1.00 64.36  ? 258 TRP A CH2   1 
ATOM   1263 N N     . GLY A 1 174 ? 112.221 112.142 152.248 1.00 66.91  ? 259 GLY A N     1 
ATOM   1264 C CA    . GLY A 1 174 ? 111.118 111.363 152.785 1.00 70.53  ? 259 GLY A CA    1 
ATOM   1265 C C     . GLY A 1 174 ? 111.596 110.223 153.662 1.00 73.99  ? 259 GLY A C     1 
ATOM   1266 O O     . GLY A 1 174 ? 111.035 109.973 154.733 1.00 78.83  ? 259 GLY A O     1 
ATOM   1267 N N     . PHE A 1 175 ? 112.639 109.516 153.222 1.00 76.37  ? 260 PHE A N     1 
ATOM   1268 C CA    . PHE A 1 175 ? 113.241 108.475 154.047 1.00 79.97  ? 260 PHE A CA    1 
ATOM   1269 C C     . PHE A 1 175 ? 114.062 109.063 155.187 1.00 77.32  ? 260 PHE A C     1 
ATOM   1270 O O     . PHE A 1 175 ? 114.156 108.451 156.256 1.00 81.03  ? 260 PHE A O     1 
ATOM   1271 C CB    . PHE A 1 175 ? 114.116 107.562 153.187 1.00 76.13  ? 260 PHE A CB    1 
ATOM   1272 C CG    . PHE A 1 175 ? 114.752 106.433 153.949 1.00 74.16  ? 260 PHE A CG    1 
ATOM   1273 C CD1   . PHE A 1 175 ? 113.974 105.528 154.653 1.00 75.59  ? 260 PHE A CD1   1 
ATOM   1274 C CD2   . PHE A 1 175 ? 116.128 106.272 153.956 1.00 75.56  ? 260 PHE A CD2   1 
ATOM   1275 C CE1   . PHE A 1 175 ? 114.558 104.486 155.349 1.00 75.81  ? 260 PHE A CE1   1 
ATOM   1276 C CE2   . PHE A 1 175 ? 116.717 105.233 154.652 1.00 76.72  ? 260 PHE A CE2   1 
ATOM   1277 C CZ    . PHE A 1 175 ? 115.930 104.339 155.349 1.00 77.84  ? 260 PHE A CZ    1 
ATOM   1278 N N     . ALA A 1 176 ? 114.661 110.236 154.978 1.00 75.99  ? 261 ALA A N     1 
ATOM   1279 C CA    . ALA A 1 176 ? 115.430 110.879 156.036 1.00 80.36  ? 261 ALA A CA    1 
ATOM   1280 C C     . ALA A 1 176 ? 114.524 111.317 157.181 1.00 85.21  ? 261 ALA A C     1 
ATOM   1281 O O     . ALA A 1 176 ? 114.773 110.993 158.346 1.00 90.26  ? 261 ALA A O     1 
ATOM   1282 C CB    . ALA A 1 176 ? 116.207 112.068 155.471 1.00 73.82  ? 261 ALA A CB    1 
ATOM   1283 N N     . ASN A 1 177 ? 113.444 112.030 156.862 1.00 82.13  ? 262 ASN A N     1 
ATOM   1284 C CA    . ASN A 1 177 ? 112.571 112.587 157.891 1.00 81.29  ? 262 ASN A CA    1 
ATOM   1285 C C     . ASN A 1 177 ? 111.721 111.515 158.564 1.00 86.05  ? 262 ASN A C     1 
ATOM   1286 O O     . ASN A 1 177 ? 110.951 111.816 159.482 1.00 89.67  ? 262 ASN A O     1 
ATOM   1287 C CB    . ASN A 1 177 ? 111.671 113.674 157.298 1.00 79.73  ? 262 ASN A CB    1 
ATOM   1288 C CG    . ASN A 1 177 ? 112.459 114.803 156.666 1.00 83.43  ? 262 ASN A CG    1 
ATOM   1289 O OD1   . ASN A 1 177 ? 113.519 115.187 157.158 1.00 86.69  ? 262 ASN A OD1   1 
ATOM   1290 N ND2   . ASN A 1 177 ? 111.942 115.344 155.569 1.00 83.25  ? 262 ASN A ND2   1 
ATOM   1291 N N     . GLN A 1 178 ? 111.842 110.266 158.117 1.00 86.09  ? 263 GLN A N     1 
ATOM   1292 C CA    . GLN A 1 178 ? 111.099 109.159 158.707 1.00 86.97  ? 263 GLN A CA    1 
ATOM   1293 C C     . GLN A 1 178 ? 111.902 108.414 159.766 1.00 95.23  ? 263 GLN A C     1 
ATOM   1294 O O     . GLN A 1 178 ? 111.414 108.208 160.881 1.00 100.72 ? 263 GLN A O     1 
ATOM   1295 C CB    . GLN A 1 178 ? 110.643 108.187 157.611 1.00 84.48  ? 263 GLN A CB    1 
ATOM   1296 C CG    . GLN A 1 178 ? 109.806 107.028 158.125 1.00 88.78  ? 263 GLN A CG    1 
ATOM   1297 C CD    . GLN A 1 178 ? 109.662 105.916 157.107 1.00 92.77  ? 263 GLN A CD    1 
ATOM   1298 O OE1   . GLN A 1 178 ? 110.332 105.914 156.074 1.00 92.34  ? 263 GLN A OE1   1 
ATOM   1299 N NE2   . GLN A 1 178 ? 108.782 104.964 157.392 1.00 89.41  ? 263 GLN A NE2   1 
ATOM   1300 N N     . ILE A 1 179 ? 113.130 108.004 159.442 1.00 95.34  ? 264 ILE A N     1 
ATOM   1301 C CA    . ILE A 1 179 ? 113.959 107.300 160.415 1.00 96.58  ? 264 ILE A CA    1 
ATOM   1302 C C     . ILE A 1 179 ? 114.668 108.251 161.371 1.00 99.29  ? 264 ILE A C     1 
ATOM   1303 O O     . ILE A 1 179 ? 115.100 107.824 162.449 1.00 104.47 ? 264 ILE A O     1 
ATOM   1304 C CB    . ILE A 1 179 ? 114.996 106.410 159.711 1.00 93.03  ? 264 ILE A CB    1 
ATOM   1305 C CG1   . ILE A 1 179 ? 116.060 107.270 159.023 1.00 85.86  ? 264 ILE A CG1   1 
ATOM   1306 C CG2   . ILE A 1 179 ? 114.315 105.483 158.717 1.00 89.61  ? 264 ILE A CG2   1 
ATOM   1307 C CD1   . ILE A 1 179 ? 116.964 106.501 158.086 1.00 83.18  ? 264 ILE A CD1   1 
ATOM   1308 N N     . THR A 1 180 ? 114.795 109.524 161.013 1.00 96.97  ? 265 THR A N     1 
ATOM   1309 C CA    . THR A 1 180 ? 115.519 110.490 161.826 1.00 100.43 ? 265 THR A CA    1 
ATOM   1310 C C     . THR A 1 180 ? 114.560 111.232 162.747 1.00 105.23 ? 265 THR A C     1 
ATOM   1311 O O     . THR A 1 180 ? 113.467 111.632 162.335 1.00 102.67 ? 265 THR A O     1 
ATOM   1312 C CB    . THR A 1 180 ? 116.268 111.484 160.935 1.00 96.47  ? 265 THR A CB    1 
ATOM   1313 O OG1   . THR A 1 180 ? 117.172 110.775 160.079 1.00 95.80  ? 265 THR A OG1   1 
ATOM   1314 C CG2   . THR A 1 180 ? 117.047 112.481 161.763 1.00 99.26  ? 265 THR A CG2   1 
ATOM   1315 N N     . THR A 1 181 ? 114.972 111.405 164.000 1.00 107.96 ? 266 THR A N     1 
ATOM   1316 C CA    . THR A 1 181 ? 114.192 112.171 164.957 1.00 106.14 ? 266 THR A CA    1 
ATOM   1317 C C     . THR A 1 181 ? 114.381 113.666 164.703 1.00 105.26 ? 266 THR A C     1 
ATOM   1318 O O     . THR A 1 181 ? 115.186 114.086 163.868 1.00 108.16 ? 266 THR A O     1 
ATOM   1319 C CB    . THR A 1 181 ? 114.588 111.805 166.386 1.00 106.15 ? 266 THR A CB    1 
ATOM   1320 O OG1   . THR A 1 181 ? 115.799 112.484 166.738 1.00 108.01 ? 266 THR A OG1   1 
ATOM   1321 C CG2   . THR A 1 181 ? 114.802 110.303 166.509 1.00 103.02 ? 266 THR A CG2   1 
ATOM   1322 N N     . VAL A 1 182 ? 113.622 114.484 165.434 1.00 106.32 ? 267 VAL A N     1 
ATOM   1323 C CA    . VAL A 1 182 ? 113.714 115.929 165.250 1.00 107.55 ? 267 VAL A CA    1 
ATOM   1324 C C     . VAL A 1 182 ? 115.062 116.456 165.734 1.00 106.12 ? 267 VAL A C     1 
ATOM   1325 O O     . VAL A 1 182 ? 115.585 117.436 165.188 1.00 100.77 ? 267 VAL A O     1 
ATOM   1326 C CB    . VAL A 1 182 ? 112.533 116.632 165.949 1.00 108.09 ? 267 VAL A CB    1 
ATOM   1327 C CG1   . VAL A 1 182 ? 112.608 116.458 167.461 1.00 104.26 ? 267 VAL A CG1   1 
ATOM   1328 C CG2   . VAL A 1 182 ? 112.486 118.108 165.572 1.00 104.98 ? 267 VAL A CG2   1 
ATOM   1329 N N     . ASP A 1 183 ? 115.650 115.823 166.752 1.00 109.88 ? 268 ASP A N     1 
ATOM   1330 C CA    . ASP A 1 183 ? 116.932 116.284 167.273 1.00 108.93 ? 268 ASP A CA    1 
ATOM   1331 C C     . ASP A 1 183 ? 118.083 115.935 166.335 1.00 104.82 ? 268 ASP A C     1 
ATOM   1332 O O     . ASP A 1 183 ? 118.975 116.762 166.113 1.00 104.37 ? 268 ASP A O     1 
ATOM   1333 C CB    . ASP A 1 183 ? 117.175 115.695 168.663 1.00 109.66 ? 268 ASP A CB    1 
ATOM   1334 C CG    . ASP A 1 183 ? 115.955 115.795 169.556 1.00 113.81 ? 268 ASP A CG    1 
ATOM   1335 O OD1   . ASP A 1 183 ? 115.516 116.929 169.838 1.00 114.26 ? 268 ASP A OD1   1 
ATOM   1336 O OD2   . ASP A 1 183 ? 115.433 114.740 169.974 1.00 113.41 ? 268 ASP A OD2   1 
ATOM   1337 N N     . GLU A 1 184 ? 118.087 114.720 165.782 1.00 102.32 ? 269 GLU A N     1 
ATOM   1338 C CA    . GLU A 1 184 ? 119.133 114.354 164.833 1.00 101.29 ? 269 GLU A CA    1 
ATOM   1339 C C     . GLU A 1 184 ? 118.987 115.127 163.528 1.00 100.08 ? 269 GLU A C     1 
ATOM   1340 O O     . GLU A 1 184 ? 119.986 115.454 162.878 1.00 95.72  ? 269 GLU A O     1 
ATOM   1341 C CB    . GLU A 1 184 ? 119.108 112.849 164.568 1.00 101.39 ? 269 GLU A CB    1 
ATOM   1342 C CG    . GLU A 1 184 ? 118.832 111.991 165.788 1.00 106.66 ? 269 GLU A CG    1 
ATOM   1343 C CD    . GLU A 1 184 ? 118.723 110.517 165.444 1.00 110.86 ? 269 GLU A CD    1 
ATOM   1344 O OE1   . GLU A 1 184 ? 118.125 110.193 164.396 1.00 107.21 ? 269 GLU A OE1   1 
ATOM   1345 O OE2   . GLU A 1 184 ? 119.234 109.682 166.220 1.00 112.57 ? 269 GLU A OE2   1 
ATOM   1346 N N     . ALA A 1 185 ? 117.747 115.425 163.128 1.00 100.17 ? 270 ALA A N     1 
ATOM   1347 C CA    . ALA A 1 185 ? 117.519 116.193 161.910 1.00 92.87  ? 270 ALA A CA    1 
ATOM   1348 C C     . ALA A 1 185 ? 118.013 117.628 162.033 1.00 96.10  ? 270 ALA A C     1 
ATOM   1349 O O     . ALA A 1 185 ? 118.219 118.291 161.011 1.00 94.98  ? 270 ALA A O     1 
ATOM   1350 C CB    . ALA A 1 185 ? 116.033 116.183 161.551 1.00 88.98  ? 270 ALA A CB    1 
ATOM   1351 N N     . LYS A 1 186 ? 118.198 118.123 163.254 1.00 98.11  ? 271 LYS A N     1 
ATOM   1352 C CA    . LYS A 1 186 ? 118.746 119.452 163.476 1.00 97.18  ? 271 LYS A CA    1 
ATOM   1353 C C     . LYS A 1 186 ? 120.267 119.447 163.582 1.00 97.64  ? 271 LYS A C     1 
ATOM   1354 O O     . LYS A 1 186 ? 120.891 120.505 163.443 1.00 100.61 ? 271 LYS A O     1 
ATOM   1355 C CB    . LYS A 1 186 ? 118.127 120.060 164.743 1.00 97.31  ? 271 LYS A CB    1 
ATOM   1356 C CG    . LYS A 1 186 ? 118.504 121.507 165.021 1.00 104.25 ? 271 LYS A CG    1 
ATOM   1357 C CD    . LYS A 1 186 ? 117.837 122.015 166.288 1.00 102.52 ? 271 LYS A CD    1 
ATOM   1358 C CE    . LYS A 1 186 ? 116.341 122.200 166.084 1.00 104.18 ? 271 LYS A CE    1 
ATOM   1359 N NZ    . LYS A 1 186 ? 116.045 123.298 165.122 1.00 105.11 ? 271 LYS A NZ    1 
ATOM   1360 N N     . LYS A 1 187 ? 120.875 118.283 163.792 1.00 94.24  ? 272 LYS A N     1 
ATOM   1361 C CA    . LYS A 1 187 ? 122.320 118.155 163.941 1.00 91.58  ? 272 LYS A CA    1 
ATOM   1362 C C     . LYS A 1 187 ? 123.015 117.607 162.705 1.00 88.82  ? 272 LYS A C     1 
ATOM   1363 O O     . LYS A 1 187 ? 124.117 118.053 162.376 1.00 88.15  ? 272 LYS A O     1 
ATOM   1364 C CB    . LYS A 1 187 ? 122.643 117.251 165.139 1.00 88.32  ? 272 LYS A CB    1 
ATOM   1365 C CG    . LYS A 1 187 ? 124.103 116.837 165.241 1.00 88.85  ? 272 LYS A CG    1 
ATOM   1366 C CD    . LYS A 1 187 ? 124.417 116.237 166.601 1.00 91.35  ? 272 LYS A CD    1 
ATOM   1367 C CE    . LYS A 1 187 ? 125.910 116.257 166.879 1.00 98.28  ? 272 LYS A CE    1 
ATOM   1368 N NZ    . LYS A 1 187 ? 126.362 117.575 167.403 1.00 101.23 ? 272 LYS A NZ    1 
ATOM   1369 N N     . PHE A 1 188 ? 122.396 116.662 161.998 1.00 88.09  ? 273 PHE A N     1 
ATOM   1370 C CA    . PHE A 1 188 ? 123.065 115.942 160.926 1.00 84.42  ? 273 PHE A CA    1 
ATOM   1371 C C     . PHE A 1 188 ? 122.623 116.354 159.528 1.00 78.97  ? 273 PHE A C     1 
ATOM   1372 O O     . PHE A 1 188 ? 123.328 116.040 158.562 1.00 79.44  ? 273 PHE A O     1 
ATOM   1373 C CB    . PHE A 1 188 ? 122.851 114.432 161.100 1.00 86.16  ? 273 PHE A CB    1 
ATOM   1374 C CG    . PHE A 1 188 ? 123.403 113.890 162.389 1.00 88.77  ? 273 PHE A CG    1 
ATOM   1375 C CD1   . PHE A 1 188 ? 124.771 113.810 162.593 1.00 85.92  ? 273 PHE A CD1   1 
ATOM   1376 C CD2   . PHE A 1 188 ? 122.554 113.470 163.399 1.00 92.35  ? 273 PHE A CD2   1 
ATOM   1377 C CE1   . PHE A 1 188 ? 125.281 113.313 163.776 1.00 88.96  ? 273 PHE A CE1   1 
ATOM   1378 C CE2   . PHE A 1 188 ? 123.059 112.973 164.585 1.00 96.59  ? 273 PHE A CE2   1 
ATOM   1379 C CZ    . PHE A 1 188 ? 124.424 112.895 164.774 1.00 95.73  ? 273 PHE A CZ    1 
ATOM   1380 N N     . TYR A 1 189 ? 121.484 117.029 159.389 1.00 78.04  ? 274 TYR A N     1 
ATOM   1381 C CA    . TYR A 1 189 ? 121.043 117.519 158.086 1.00 74.20  ? 274 TYR A CA    1 
ATOM   1382 C C     . TYR A 1 189 ? 122.037 118.515 157.488 1.00 74.53  ? 274 TYR A C     1 
ATOM   1383 O O     . TYR A 1 189 ? 122.329 118.427 156.288 1.00 74.30  ? 274 TYR A O     1 
ATOM   1384 C CB    . TYR A 1 189 ? 119.646 118.138 158.180 1.00 78.69  ? 274 TYR A CB    1 
ATOM   1385 C CG    . TYR A 1 189 ? 118.529 117.119 158.145 1.00 75.63  ? 274 TYR A CG    1 
ATOM   1386 C CD1   . TYR A 1 189 ? 118.803 115.758 158.179 1.00 75.88  ? 274 TYR A CD1   1 
ATOM   1387 C CD2   . TYR A 1 189 ? 117.201 117.517 158.072 1.00 73.97  ? 274 TYR A CD2   1 
ATOM   1388 C CE1   . TYR A 1 189 ? 117.788 114.823 158.146 1.00 78.43  ? 274 TYR A CE1   1 
ATOM   1389 C CE2   . TYR A 1 189 ? 116.179 116.590 158.037 1.00 76.40  ? 274 TYR A CE2   1 
ATOM   1390 C CZ    . TYR A 1 189 ? 116.478 115.244 158.075 1.00 80.24  ? 274 TYR A CZ    1 
ATOM   1391 O OH    . TYR A 1 189 ? 115.465 114.315 158.042 1.00 83.64  ? 274 TYR A OH    1 
ATOM   1392 N N     . PRO A 1 190 ? 122.565 119.481 158.254 1.00 75.67  ? 275 PRO A N     1 
ATOM   1393 C CA    . PRO A 1 190 ? 123.635 120.324 157.692 1.00 75.34  ? 275 PRO A CA    1 
ATOM   1394 C C     . PRO A 1 190 ? 124.849 119.532 157.245 1.00 69.20  ? 275 PRO A C     1 
ATOM   1395 O O     . PRO A 1 190 ? 125.501 119.914 156.265 1.00 65.25  ? 275 PRO A O     1 
ATOM   1396 C CB    . PRO A 1 190 ? 123.974 121.276 158.847 1.00 80.30  ? 275 PRO A CB    1 
ATOM   1397 C CG    . PRO A 1 190 ? 122.727 121.351 159.638 1.00 80.62  ? 275 PRO A CG    1 
ATOM   1398 C CD    . PRO A 1 190 ? 122.143 119.972 159.580 1.00 77.80  ? 275 PRO A CD    1 
ATOM   1399 N N     . LEU A 1 191 ? 125.175 118.435 157.933 1.00 68.28  ? 276 LEU A N     1 
ATOM   1400 C CA    . LEU A 1 191 ? 126.271 117.581 157.497 1.00 64.35  ? 276 LEU A CA    1 
ATOM   1401 C C     . LEU A 1 191 ? 125.932 116.814 156.226 1.00 65.35  ? 276 LEU A C     1 
ATOM   1402 O O     . LEU A 1 191 ? 126.843 116.460 155.470 1.00 70.45  ? 276 LEU A O     1 
ATOM   1403 C CB    . LEU A 1 191 ? 126.653 116.602 158.609 1.00 68.03  ? 276 LEU A CB    1 
ATOM   1404 C CG    . LEU A 1 191 ? 127.246 117.217 159.877 1.00 71.22  ? 276 LEU A CG    1 
ATOM   1405 C CD1   . LEU A 1 191 ? 127.448 116.155 160.946 1.00 72.98  ? 276 LEU A CD1   1 
ATOM   1406 C CD2   . LEU A 1 191 ? 128.555 117.926 159.566 1.00 70.46  ? 276 LEU A CD2   1 
ATOM   1407 N N     . PHE A 1 192 ? 124.648 116.542 155.981 1.00 64.34  ? 277 PHE A N     1 
ATOM   1408 C CA    . PHE A 1 192 ? 124.258 115.854 154.754 1.00 59.61  ? 277 PHE A CA    1 
ATOM   1409 C C     . PHE A 1 192 ? 124.577 116.696 153.526 1.00 60.07  ? 277 PHE A C     1 
ATOM   1410 O O     . PHE A 1 192 ? 125.078 116.176 152.522 1.00 65.07  ? 277 PHE A O     1 
ATOM   1411 C CB    . PHE A 1 192 ? 122.769 115.509 154.795 1.00 59.78  ? 277 PHE A CB    1 
ATOM   1412 C CG    . PHE A 1 192 ? 122.439 114.340 155.680 1.00 63.60  ? 277 PHE A CG    1 
ATOM   1413 C CD1   . PHE A 1 192 ? 123.436 113.668 156.368 1.00 65.47  ? 277 PHE A CD1   1 
ATOM   1414 C CD2   . PHE A 1 192 ? 121.130 113.915 155.825 1.00 67.27  ? 277 PHE A CD2   1 
ATOM   1415 C CE1   . PHE A 1 192 ? 123.133 112.595 157.183 1.00 67.63  ? 277 PHE A CE1   1 
ATOM   1416 C CE2   . PHE A 1 192 ? 120.820 112.843 156.638 1.00 65.97  ? 277 PHE A CE2   1 
ATOM   1417 C CZ    . PHE A 1 192 ? 121.823 112.182 157.317 1.00 68.34  ? 277 PHE A CZ    1 
ATOM   1418 N N     . GLY A 1 193 ? 124.290 117.998 153.585 1.00 56.58  ? 278 GLY A N     1 
ATOM   1419 C CA    . GLY A 1 193 ? 124.629 118.875 152.479 1.00 51.11  ? 278 GLY A CA    1 
ATOM   1420 C C     . GLY A 1 193 ? 126.122 119.035 152.280 1.00 56.52  ? 278 GLY A C     1 
ATOM   1421 O O     . GLY A 1 193 ? 126.589 119.155 151.144 1.00 61.13  ? 278 GLY A O     1 
ATOM   1422 N N     . LEU A 1 194 ? 126.888 119.050 153.374 1.00 59.02  ? 279 LEU A N     1 
ATOM   1423 C CA    . LEU A 1 194 ? 128.338 119.168 153.265 1.00 59.24  ? 279 LEU A CA    1 
ATOM   1424 C C     . LEU A 1 194 ? 128.938 117.957 152.561 1.00 57.56  ? 279 LEU A C     1 
ATOM   1425 O O     . LEU A 1 194 ? 129.761 118.100 151.650 1.00 61.49  ? 279 LEU A O     1 
ATOM   1426 C CB    . LEU A 1 194 ? 128.955 119.338 154.654 1.00 58.81  ? 279 LEU A CB    1 
ATOM   1427 C CG    . LEU A 1 194 ? 128.622 120.621 155.415 1.00 60.81  ? 279 LEU A CG    1 
ATOM   1428 C CD1   . LEU A 1 194 ? 129.195 120.569 156.822 1.00 64.27  ? 279 LEU A CD1   1 
ATOM   1429 C CD2   . LEU A 1 194 ? 129.145 121.835 154.667 1.00 60.94  ? 279 LEU A CD2   1 
ATOM   1430 N N     . GLY A 1 195 ? 128.531 116.753 152.968 1.00 56.21  ? 280 GLY A N     1 
ATOM   1431 C CA    . GLY A 1 195 ? 129.065 115.545 152.365 1.00 59.72  ? 280 GLY A CA    1 
ATOM   1432 C C     . GLY A 1 195 ? 128.582 115.295 150.953 1.00 60.30  ? 280 GLY A C     1 
ATOM   1433 O O     . GLY A 1 195 ? 129.264 114.602 150.191 1.00 61.41  ? 280 GLY A O     1 
ATOM   1434 N N     . ALA A 1 196 ? 127.428 115.844 150.585 1.00 53.07  ? 281 ALA A N     1 
ATOM   1435 C CA    . ALA A 1 196 ? 126.889 115.685 149.243 1.00 52.27  ? 281 ALA A CA    1 
ATOM   1436 C C     . ALA A 1 196 ? 127.391 116.745 148.275 1.00 51.37  ? 281 ALA A C     1 
ATOM   1437 O O     . ALA A 1 196 ? 127.078 116.674 147.083 1.00 57.70  ? 281 ALA A O     1 
ATOM   1438 C CB    . ALA A 1 196 ? 125.362 115.706 149.280 1.00 52.82  ? 281 ALA A CB    1 
ATOM   1439 N N     . ASN A 1 197 ? 128.139 117.736 148.758 1.00 47.68  ? 282 ASN A N     1 
ATOM   1440 C CA    . ASN A 1 197 ? 128.868 118.632 147.876 1.00 45.48  ? 282 ASN A CA    1 
ATOM   1441 C C     . ASN A 1 197 ? 130.283 118.149 147.605 1.00 46.56  ? 282 ASN A C     1 
ATOM   1442 O O     . ASN A 1 197 ? 130.865 118.521 146.580 1.00 49.77  ? 282 ASN A O     1 
ATOM   1443 C CB    . ASN A 1 197 ? 128.904 120.048 148.460 1.00 54.59  ? 282 ASN A CB    1 
ATOM   1444 C CG    . ASN A 1 197 ? 127.574 120.759 148.323 1.00 50.86  ? 282 ASN A CG    1 
ATOM   1445 O OD1   . ASN A 1 197 ? 127.157 121.105 147.218 1.00 48.02  ? 282 ASN A OD1   1 
ATOM   1446 N ND2   . ASN A 1 197 ? 126.899 120.975 149.444 1.00 51.93  ? 282 ASN A ND2   1 
ATOM   1447 N N     . VAL A 1 198 ? 130.842 117.331 148.500 1.00 49.57  ? 283 VAL A N     1 
ATOM   1448 C CA    . VAL A 1 198 ? 132.004 116.525 148.146 1.00 48.47  ? 283 VAL A CA    1 
ATOM   1449 C C     . VAL A 1 198 ? 131.641 115.580 147.011 1.00 51.38  ? 283 VAL A C     1 
ATOM   1450 O O     . VAL A 1 198 ? 132.491 115.227 146.183 1.00 54.79  ? 283 VAL A O     1 
ATOM   1451 C CB    . VAL A 1 198 ? 132.522 115.765 149.384 1.00 48.97  ? 283 VAL A CB    1 
ATOM   1452 C CG1   . VAL A 1 198 ? 133.731 114.911 149.030 1.00 52.52  ? 283 VAL A CG1   1 
ATOM   1453 C CG2   . VAL A 1 198 ? 132.859 116.739 150.502 1.00 53.89  ? 283 VAL A CG2   1 
ATOM   1454 N N     . ALA A 1 199 ? 130.373 115.161 146.949 1.00 52.30  ? 284 ALA A N     1 
ATOM   1455 C CA    . ALA A 1 199 ? 129.903 114.377 145.813 1.00 47.70  ? 284 ALA A CA    1 
ATOM   1456 C C     . ALA A 1 199 ? 130.009 115.169 144.517 1.00 47.03  ? 284 ALA A C     1 
ATOM   1457 O O     . ALA A 1 199 ? 130.429 114.631 143.488 1.00 51.80  ? 284 ALA A O     1 
ATOM   1458 C CB    . ALA A 1 199 ? 128.463 113.922 146.049 1.00 46.79  ? 284 ALA A CB    1 
ATOM   1459 N N     . LEU A 1 200 ? 129.634 116.451 144.548 1.00 47.30  ? 285 LEU A N     1 
ATOM   1460 C CA    . LEU A 1 200 ? 129.778 117.287 143.360 1.00 43.16  ? 285 LEU A CA    1 
ATOM   1461 C C     . LEU A 1 200 ? 131.242 117.455 142.976 1.00 45.72  ? 285 LEU A C     1 
ATOM   1462 O O     . LEU A 1 200 ? 131.583 117.437 141.787 1.00 47.00  ? 285 LEU A O     1 
ATOM   1463 C CB    . LEU A 1 200 ? 129.129 118.651 143.587 1.00 44.20  ? 285 LEU A CB    1 
ATOM   1464 C CG    . LEU A 1 200 ? 127.685 118.799 143.108 1.00 51.00  ? 285 LEU A CG    1 
ATOM   1465 C CD1   . LEU A 1 200 ? 126.735 118.026 144.010 1.00 46.49  ? 285 LEU A CD1   1 
ATOM   1466 C CD2   . LEU A 1 200 ? 127.296 120.267 143.020 1.00 45.39  ? 285 LEU A CD2   1 
ATOM   1467 N N     . ILE A 1 201 ? 132.118 117.631 143.966 1.00 46.87  ? 286 ILE A N     1 
ATOM   1468 C CA    . ILE A 1 201 ? 133.544 117.761 143.684 1.00 43.90  ? 286 ILE A CA    1 
ATOM   1469 C C     . ILE A 1 201 ? 134.077 116.486 143.045 1.00 46.72  ? 286 ILE A C     1 
ATOM   1470 O O     . ILE A 1 201 ? 134.860 116.533 142.088 1.00 52.26  ? 286 ILE A O     1 
ATOM   1471 C CB    . ILE A 1 201 ? 134.313 118.113 144.972 1.00 41.22  ? 286 ILE A CB    1 
ATOM   1472 C CG1   . ILE A 1 201 ? 133.787 119.421 145.567 1.00 42.32  ? 286 ILE A CG1   1 
ATOM   1473 C CG2   . ILE A 1 201 ? 135.804 118.219 144.693 1.00 49.56  ? 286 ILE A CG2   1 
ATOM   1474 C CD1   . ILE A 1 201 ? 134.184 119.636 147.012 1.00 48.39  ? 286 ILE A CD1   1 
ATOM   1475 N N     . PHE A 1 202 ? 133.659 115.328 143.557 1.00 47.45  ? 287 PHE A N     1 
ATOM   1476 C CA    . PHE A 1 202 ? 134.161 114.061 143.038 1.00 49.33  ? 287 PHE A CA    1 
ATOM   1477 C C     . PHE A 1 202 ? 133.447 113.631 141.762 1.00 47.53  ? 287 PHE A C     1 
ATOM   1478 O O     . PHE A 1 202 ? 134.086 113.077 140.861 1.00 53.25  ? 287 PHE A O     1 
ATOM   1479 C CB    . PHE A 1 202 ? 134.043 112.975 144.108 1.00 53.69  ? 287 PHE A CB    1 
ATOM   1480 C CG    . PHE A 1 202 ? 135.041 113.118 145.222 1.00 53.99  ? 287 PHE A CG    1 
ATOM   1481 C CD1   . PHE A 1 202 ? 136.118 113.981 145.096 1.00 50.77  ? 287 PHE A CD1   1 
ATOM   1482 C CD2   . PHE A 1 202 ? 134.904 112.394 146.393 1.00 56.50  ? 287 PHE A CD2   1 
ATOM   1483 C CE1   . PHE A 1 202 ? 137.038 114.119 146.115 1.00 53.48  ? 287 PHE A CE1   1 
ATOM   1484 C CE2   . PHE A 1 202 ? 135.822 112.526 147.417 1.00 57.59  ? 287 PHE A CE2   1 
ATOM   1485 C CZ    . PHE A 1 202 ? 136.890 113.391 147.278 1.00 59.49  ? 287 PHE A CZ    1 
ATOM   1486 N N     . SER A 1 203 ? 132.137 113.868 141.660 1.00 46.56  ? 288 SER A N     1 
ATOM   1487 C CA    . SER A 1 203 ? 131.428 113.541 140.429 1.00 47.46  ? 288 SER A CA    1 
ATOM   1488 C C     . SER A 1 203 ? 131.731 114.526 139.309 1.00 51.87  ? 288 SER A C     1 
ATOM   1489 O O     . SER A 1 203 ? 131.681 114.144 138.136 1.00 57.15  ? 288 SER A O     1 
ATOM   1490 C CB    . SER A 1 203 ? 129.919 113.486 140.672 1.00 43.55  ? 288 SER A CB    1 
ATOM   1491 O OG    . SER A 1 203 ? 129.210 113.489 139.447 1.00 47.58  ? 288 SER A OG    1 
ATOM   1492 N N     . GLY A 1 204 ? 132.034 115.783 139.643 1.00 50.32  ? 289 GLY A N     1 
ATOM   1493 C CA    . GLY A 1 204 ? 132.510 116.708 138.629 1.00 47.77  ? 289 GLY A CA    1 
ATOM   1494 C C     . GLY A 1 204 ? 133.848 116.286 138.056 1.00 52.50  ? 289 GLY A C     1 
ATOM   1495 O O     . GLY A 1 204 ? 134.065 116.356 136.843 1.00 56.58  ? 289 GLY A O     1 
ATOM   1496 N N     . ARG A 1 205 ? 134.766 115.845 138.921 1.00 56.03  ? 290 ARG A N     1 
ATOM   1497 C CA    . ARG A 1 205 ? 136.003 115.242 138.440 1.00 52.91  ? 290 ARG A CA    1 
ATOM   1498 C C     . ARG A 1 205 ? 135.718 113.970 137.656 1.00 53.09  ? 290 ARG A C     1 
ATOM   1499 O O     . ARG A 1 205 ? 136.444 113.645 136.709 1.00 59.81  ? 290 ARG A O     1 
ATOM   1500 C CB    . ARG A 1 205 ? 136.936 114.939 139.614 1.00 48.04  ? 290 ARG A CB    1 
ATOM   1501 C CG    . ARG A 1 205 ? 137.522 116.169 140.288 1.00 51.06  ? 290 ARG A CG    1 
ATOM   1502 C CD    . ARG A 1 205 ? 138.395 116.962 139.334 1.00 53.85  ? 290 ARG A CD    1 
ATOM   1503 N NE    . ARG A 1 205 ? 137.680 118.105 138.781 1.00 64.18  ? 290 ARG A NE    1 
ATOM   1504 C CZ    . ARG A 1 205 ? 138.065 118.783 137.708 1.00 69.98  ? 290 ARG A CZ    1 
ATOM   1505 N NH1   . ARG A 1 205 ? 139.165 118.464 137.048 1.00 75.70  ? 290 ARG A NH1   1 
ATOM   1506 N NH2   . ARG A 1 205 ? 137.330 119.809 137.292 1.00 65.64  ? 290 ARG A NH2   1 
ATOM   1507 N N     . THR A 1 206 ? 134.673 113.237 138.044 1.00 50.72  ? 291 THR A N     1 
ATOM   1508 C CA    . THR A 1 206 ? 134.274 112.045 137.305 1.00 50.41  ? 291 THR A CA    1 
ATOM   1509 C C     . THR A 1 206 ? 133.721 112.404 135.932 1.00 53.62  ? 291 THR A C     1 
ATOM   1510 O O     . THR A 1 206 ? 134.043 111.747 134.935 1.00 58.15  ? 291 THR A O     1 
ATOM   1511 C CB    . THR A 1 206 ? 133.241 111.259 138.112 1.00 53.60  ? 291 THR A CB    1 
ATOM   1512 O OG1   . THR A 1 206 ? 133.754 111.002 139.426 1.00 53.08  ? 291 THR A OG1   1 
ATOM   1513 C CG2   . THR A 1 206 ? 132.918 109.948 137.432 1.00 56.40  ? 291 THR A CG2   1 
ATOM   1514 N N     . VAL A 1 207 ? 132.887 113.445 135.858 1.00 55.08  ? 292 VAL A N     1 
ATOM   1515 C CA    . VAL A 1 207 ? 132.329 113.851 134.574 1.00 52.51  ? 292 VAL A CA    1 
ATOM   1516 C C     . VAL A 1 207 ? 133.431 114.325 133.636 1.00 55.22  ? 292 VAL A C     1 
ATOM   1517 O O     . VAL A 1 207 ? 133.425 113.991 132.446 1.00 59.91  ? 292 VAL A O     1 
ATOM   1518 C CB    . VAL A 1 207 ? 131.248 114.930 134.777 1.00 55.15  ? 292 VAL A CB    1 
ATOM   1519 C CG1   . VAL A 1 207 ? 130.936 115.638 133.467 1.00 56.63  ? 292 VAL A CG1   1 
ATOM   1520 C CG2   . VAL A 1 207 ? 129.987 114.310 135.359 1.00 47.87  ? 292 VAL A CG2   1 
ATOM   1521 N N     . LYS A 1 208 ? 134.397 115.092 134.144 1.00 58.22  ? 293 LYS A N     1 
ATOM   1522 C CA    . LYS A 1 208 ? 135.473 115.582 133.289 1.00 58.29  ? 293 LYS A CA    1 
ATOM   1523 C C     . LYS A 1 208 ? 136.418 114.465 132.859 1.00 62.51  ? 293 LYS A C     1 
ATOM   1524 O O     . LYS A 1 208 ? 136.857 114.436 131.703 1.00 64.70  ? 293 LYS A O     1 
ATOM   1525 C CB    . LYS A 1 208 ? 136.265 116.675 134.002 1.00 54.30  ? 293 LYS A CB    1 
ATOM   1526 C CG    . LYS A 1 208 ? 137.365 117.277 133.145 1.00 63.53  ? 293 LYS A CG    1 
ATOM   1527 C CD    . LYS A 1 208 ? 138.049 118.411 133.858 1.00 61.58  ? 293 LYS A CD    1 
ATOM   1528 C CE    . LYS A 1 208 ? 139.238 118.935 133.076 1.00 68.50  ? 293 LYS A CE    1 
ATOM   1529 N NZ    . LYS A 1 208 ? 138.823 119.482 131.755 1.00 65.65  ? 293 LYS A NZ    1 
ATOM   1530 N N     . TYR A 1 209 ? 136.765 113.561 133.779 1.00 59.26  ? 294 TYR A N     1 
ATOM   1531 C CA    . TYR A 1 209 ? 137.683 112.474 133.446 1.00 59.39  ? 294 TYR A CA    1 
ATOM   1532 C C     . TYR A 1 209 ? 137.140 111.617 132.312 1.00 62.90  ? 294 TYR A C     1 
ATOM   1533 O O     . TYR A 1 209 ? 137.845 111.339 131.335 1.00 72.10  ? 294 TYR A O     1 
ATOM   1534 C CB    . TYR A 1 209 ? 137.954 111.611 134.678 1.00 64.21  ? 294 TYR A CB    1 
ATOM   1535 C CG    . TYR A 1 209 ? 138.897 110.459 134.406 1.00 65.01  ? 294 TYR A CG    1 
ATOM   1536 C CD1   . TYR A 1 209 ? 140.273 110.644 134.384 1.00 67.96  ? 294 TYR A CD1   1 
ATOM   1537 C CD2   . TYR A 1 209 ? 138.405 109.181 134.166 1.00 64.65  ? 294 TYR A CD2   1 
ATOM   1538 C CE1   . TYR A 1 209 ? 141.132 109.587 134.130 1.00 77.23  ? 294 TYR A CE1   1 
ATOM   1539 C CE2   . TYR A 1 209 ? 139.254 108.121 133.912 1.00 72.00  ? 294 TYR A CE2   1 
ATOM   1540 C CZ    . TYR A 1 209 ? 140.616 108.329 133.896 1.00 82.62  ? 294 TYR A CZ    1 
ATOM   1541 O OH    . TYR A 1 209 ? 141.463 107.274 133.644 1.00 90.76  ? 294 TYR A OH    1 
ATOM   1542 N N     . PHE A 1 210 ? 135.887 111.192 132.422 1.00 61.62  ? 295 PHE A N     1 
ATOM   1543 C CA    . PHE A 1 210 ? 135.287 110.331 131.416 1.00 60.24  ? 295 PHE A CA    1 
ATOM   1544 C C     . PHE A 1 210 ? 134.794 111.101 130.200 1.00 63.96  ? 295 PHE A C     1 
ATOM   1545 O O     . PHE A 1 210 ? 134.336 110.477 129.239 1.00 74.39  ? 295 PHE A O     1 
ATOM   1546 C CB    . PHE A 1 210 ? 134.153 109.514 132.040 1.00 60.69  ? 295 PHE A CB    1 
ATOM   1547 C CG    . PHE A 1 210 ? 134.624 108.537 133.082 1.00 65.24  ? 295 PHE A CG    1 
ATOM   1548 C CD1   . PHE A 1 210 ? 135.308 107.390 132.713 1.00 64.04  ? 295 PHE A CD1   1 
ATOM   1549 C CD2   . PHE A 1 210 ? 134.409 108.776 134.428 1.00 65.68  ? 295 PHE A CD2   1 
ATOM   1550 C CE1   . PHE A 1 210 ? 135.749 106.490 133.666 1.00 67.42  ? 295 PHE A CE1   1 
ATOM   1551 C CE2   . PHE A 1 210 ? 134.853 107.883 135.384 1.00 68.41  ? 295 PHE A CE2   1 
ATOM   1552 C CZ    . PHE A 1 210 ? 135.521 106.739 135.004 1.00 71.81  ? 295 PHE A CZ    1 
ATOM   1553 N N     . SER A 1 211 ? 134.886 112.430 130.214 1.00 66.05  ? 296 SER A N     1 
ATOM   1554 C CA    . SER A 1 211 ? 134.604 113.238 129.034 1.00 66.71  ? 296 SER A CA    1 
ATOM   1555 C C     . SER A 1 211 ? 135.832 113.491 128.176 1.00 75.03  ? 296 SER A C     1 
ATOM   1556 O O     . SER A 1 211 ? 135.691 113.714 126.969 1.00 82.92  ? 296 SER A O     1 
ATOM   1557 C CB    . SER A 1 211 ? 133.999 114.587 129.433 1.00 62.04  ? 296 SER A CB    1 
ATOM   1558 O OG    . SER A 1 211 ? 132.934 114.420 130.349 1.00 68.61  ? 296 SER A OG    1 
ATOM   1559 N N     . ASN A 1 212 ? 137.028 113.474 128.767 1.00 76.27  ? 297 ASN A N     1 
ATOM   1560 C CA    . ASN A 1 212 ? 138.251 113.652 127.998 1.00 80.67  ? 297 ASN A CA    1 
ATOM   1561 C C     . ASN A 1 212 ? 138.324 112.596 126.907 1.00 90.53  ? 297 ASN A C     1 
ATOM   1562 O O     . ASN A 1 212 ? 138.458 111.403 127.205 1.00 86.94  ? 297 ASN A O     1 
ATOM   1563 C CB    . ASN A 1 212 ? 139.486 113.569 128.900 1.00 81.93  ? 297 ASN A CB    1 
ATOM   1564 C CG    . ASN A 1 212 ? 139.700 114.827 129.720 1.00 86.02  ? 297 ASN A CG    1 
ATOM   1565 O OD1   . ASN A 1 212 ? 139.172 115.890 129.394 1.00 84.25  ? 297 ASN A OD1   1 
ATOM   1566 N ND2   . ASN A 1 212 ? 140.476 114.712 130.792 1.00 84.28  ? 297 ASN A ND2   1 
ATOM   1567 N N     . LEU A 1 213 ? 138.201 113.024 125.653 1.00 100.22 ? 298 LEU A N     1 
ATOM   1568 C CA    . LEU A 1 213 ? 138.305 112.104 124.528 1.00 104.82 ? 298 LEU A CA    1 
ATOM   1569 C C     . LEU A 1 213 ? 139.545 111.241 124.659 1.00 116.07 ? 298 LEU A C     1 
ATOM   1570 O O     . LEU A 1 213 ? 140.668 111.752 124.720 1.00 119.17 ? 298 LEU A O     1 
ATOM   1571 C CB    . LEU A 1 213 ? 138.322 112.871 123.207 1.00 102.81 ? 298 LEU A CB    1 
ATOM   1572 C CG    . LEU A 1 213 ? 137.021 113.598 122.901 1.00 98.00  ? 298 LEU A CG    1 
ATOM   1573 C CD1   . LEU A 1 213 ? 137.145 114.450 121.655 1.00 96.63  ? 298 LEU A CD1   1 
ATOM   1574 C CD2   . LEU A 1 213 ? 135.984 112.522 122.688 1.00 90.39  ? 298 LEU A CD2   1 
ATOM   1575 N N     . ARG A 1 214 ? 139.322 109.927 124.736 1.00 122.03 ? 299 ARG A N     1 
ATOM   1576 C CA    . ARG A 1 214 ? 140.410 108.963 124.755 1.00 128.83 ? 299 ARG A CA    1 
ATOM   1577 C C     . ARG A 1 214 ? 141.447 109.306 123.698 1.00 135.56 ? 299 ARG A C     1 
ATOM   1578 O O     . ARG A 1 214 ? 142.654 109.184 123.927 1.00 136.76 ? 299 ARG A O     1 
ATOM   1579 C CB    . ARG A 1 214 ? 139.852 107.558 124.510 1.00 129.74 ? 299 ARG A CB    1 
ATOM   1580 C CG    . ARG A 1 214 ? 138.944 107.025 125.599 1.00 122.87 ? 299 ARG A CG    1 
ATOM   1581 C CD    . ARG A 1 214 ? 138.509 105.598 125.287 1.00 124.04 ? 299 ARG A CD    1 
ATOM   1582 N NE    . ARG A 1 214 ? 137.613 105.056 126.301 1.00 126.66 ? 299 ARG A NE    1 
ATOM   1583 C CZ    . ARG A 1 214 ? 138.014 104.511 127.441 1.00 130.00 ? 299 ARG A CZ    1 
ATOM   1584 N NH1   . ARG A 1 214 ? 139.298 104.407 127.741 1.00 127.31 ? 299 ARG A NH1   1 
ATOM   1585 N NH2   . ARG A 1 214 ? 137.105 104.062 128.302 1.00 129.91 ? 299 ARG A NH2   1 
ATOM   1586 N N     . LYS A 1 215 ? 140.976 109.714 122.521 1.00 137.62 ? 300 LYS A N     1 
ATOM   1587 C CA    . LYS A 1 215 ? 141.722 109.926 121.291 1.00 142.01 ? 300 LYS A CA    1 
ATOM   1588 C C     . LYS A 1 215 ? 142.232 108.587 120.786 1.00 147.48 ? 300 LYS A C     1 
ATOM   1589 O O     . LYS A 1 215 ? 142.770 108.517 119.678 1.00 146.46 ? 300 LYS A O     1 
ATOM   1590 C CB    . LYS A 1 215 ? 142.889 110.922 121.445 1.00 136.24 ? 300 LYS A CB    1 
ATOM   1591 C CG    . LYS A 1 215 ? 142.427 112.346 121.722 1.00 128.89 ? 300 LYS A CG    1 
ATOM   1592 C CD    . LYS A 1 215 ? 143.599 113.296 121.892 1.00 124.93 ? 300 LYS A CD    1 
ATOM   1593 C CE    . LYS A 1 215 ? 143.119 114.716 122.145 1.00 117.51 ? 300 LYS A CE    1 
ATOM   1594 N NZ    . LYS A 1 215 ? 144.254 115.659 122.337 1.00 111.13 ? 300 LYS A NZ    1 
ATOM   1595 N N     . ASN A 1 216 ? 142.070 107.520 121.564 1.00 147.12 ? 301 ASN A N     1 
ATOM   1596 C CA    . ASN A 1 216 ? 142.246 106.163 121.086 1.00 150.01 ? 301 ASN A CA    1 
ATOM   1597 C C     . ASN A 1 216 ? 141.104 105.833 120.139 1.00 151.71 ? 301 ASN A C     1 
ATOM   1598 O O     . ASN A 1 216 ? 139.930 106.012 120.477 1.00 149.64 ? 301 ASN A O     1 
ATOM   1599 C CB    . ASN A 1 216 ? 142.254 105.200 122.273 1.00 148.41 ? 301 ASN A CB    1 
ATOM   1600 C CG    . ASN A 1 216 ? 143.281 104.100 122.133 1.00 149.89 ? 301 ASN A CG    1 
ATOM   1601 O OD1   . ASN A 1 216 ? 143.571 103.639 121.030 1.00 150.04 ? 301 ASN A OD1   1 
ATOM   1602 N ND2   . ASN A 1 216 ? 143.843 103.674 123.259 1.00 147.91 ? 301 ASN A ND2   1 
ATOM   1603 N N     . LEU A 1 217 ? 141.451 105.359 118.944 1.00 155.05 ? 302 LEU A N     1 
ATOM   1604 C CA    . LEU A 1 217 ? 140.492 105.196 117.855 1.00 154.02 ? 302 LEU A CA    1 
ATOM   1605 C C     . LEU A 1 217 ? 139.817 106.534 117.539 1.00 155.05 ? 302 LEU A C     1 
ATOM   1606 O O     . LEU A 1 217 ? 138.612 106.723 117.709 1.00 153.42 ? 302 LEU A O     1 
ATOM   1607 C CB    . LEU A 1 217 ? 139.458 104.116 118.185 1.00 151.39 ? 302 LEU A CB    1 
ATOM   1608 C CG    . LEU A 1 217 ? 139.987 102.690 118.327 1.00 145.50 ? 302 LEU A CG    1 
ATOM   1609 C CD1   . LEU A 1 217 ? 138.885 101.756 118.797 1.00 137.76 ? 302 LEU A CD1   1 
ATOM   1610 C CD2   . LEU A 1 217 ? 140.578 102.211 117.011 1.00 139.90 ? 302 LEU A CD2   1 
ATOM   1611 N N     . GLY A 1 218 ? 140.655 107.473 117.083 1.00 154.20 ? 303 GLY A N     1 
ATOM   1612 C CA    . GLY A 1 218 ? 140.195 108.780 116.672 1.00 154.42 ? 303 GLY A CA    1 
ATOM   1613 C C     . GLY A 1 218 ? 139.108 108.780 115.623 1.00 159.89 ? 303 GLY A C     1 
ATOM   1614 O O     . GLY A 1 218 ? 138.141 109.543 115.749 1.00 159.42 ? 303 GLY A O     1 
ATOM   1615 N N     . PRO A 1 219 ? 139.209 107.967 114.574 1.00 161.51 ? 304 PRO A N     1 
ATOM   1616 C CA    . PRO A 1 219 ? 138.076 107.799 113.660 1.00 158.39 ? 304 PRO A CA    1 
ATOM   1617 C C     . PRO A 1 219 ? 137.145 106.681 114.107 1.00 154.47 ? 304 PRO A C     1 
ATOM   1618 O O     . PRO A 1 219 ? 137.493 105.822 114.920 1.00 153.25 ? 304 PRO A O     1 
ATOM   1619 C CB    . PRO A 1 219 ? 138.765 107.439 112.340 1.00 154.05 ? 304 PRO A CB    1 
ATOM   1620 C CG    . PRO A 1 219 ? 139.948 106.645 112.779 1.00 155.19 ? 304 PRO A CG    1 
ATOM   1621 C CD    . PRO A 1 219 ? 140.406 107.252 114.084 1.00 157.74 ? 304 PRO A CD    1 
ATOM   1622 N N     . GLY A 1 220 ? 135.934 106.715 113.558 1.00 149.13 ? 305 GLY A N     1 
ATOM   1623 C CA    . GLY A 1 220 ? 134.990 105.638 113.777 1.00 140.70 ? 305 GLY A CA    1 
ATOM   1624 C C     . GLY A 1 220 ? 134.145 105.785 115.024 1.00 133.99 ? 305 GLY A C     1 
ATOM   1625 O O     . GLY A 1 220 ? 133.136 106.497 115.018 1.00 129.37 ? 305 GLY A O     1 
ATOM   1626 N N     . VAL A 1 221 ? 134.551 105.099 116.097 1.00 134.35 ? 306 VAL A N     1 
ATOM   1627 C CA    . VAL A 1 221 ? 133.770 105.085 117.327 1.00 127.18 ? 306 VAL A CA    1 
ATOM   1628 C C     . VAL A 1 221 ? 133.548 106.507 117.826 1.00 121.95 ? 306 VAL A C     1 
ATOM   1629 O O     . VAL A 1 221 ? 134.457 107.343 117.811 1.00 124.59 ? 306 VAL A O     1 
ATOM   1630 C CB    . VAL A 1 221 ? 134.460 104.207 118.387 1.00 123.64 ? 306 VAL A CB    1 
ATOM   1631 C CG1   . VAL A 1 221 ? 134.622 102.787 117.872 1.00 120.44 ? 306 VAL A CG1   1 
ATOM   1632 C CG2   . VAL A 1 221 ? 135.817 104.782 118.773 1.00 126.70 ? 306 VAL A CG2   1 
ATOM   1633 N N     . ASP A 1 222 ? 132.316 106.789 118.244 1.00 113.70 ? 307 ASP A N     1 
ATOM   1634 C CA    . ASP A 1 222 ? 131.968 108.112 118.737 1.00 102.11 ? 307 ASP A CA    1 
ATOM   1635 C C     . ASP A 1 222 ? 132.664 108.353 120.069 1.00 94.85  ? 307 ASP A C     1 
ATOM   1636 O O     . ASP A 1 222 ? 132.587 107.522 120.982 1.00 94.68  ? 307 ASP A O     1 
ATOM   1637 C CB    . ASP A 1 222 ? 130.454 108.245 118.887 1.00 96.12  ? 307 ASP A CB    1 
ATOM   1638 C CG    . ASP A 1 222 ? 130.017 109.656 119.241 1.00 91.05  ? 307 ASP A CG    1 
ATOM   1639 O OD1   . ASP A 1 222 ? 130.886 110.548 119.365 1.00 87.83  ? 307 ASP A OD1   1 
ATOM   1640 O OD2   . ASP A 1 222 ? 128.797 109.875 119.399 1.00 89.11  ? 307 ASP A OD2   1 
ATOM   1641 N N     . GLY A 1 223 ? 133.350 109.493 120.175 1.00 89.16  ? 308 GLY A N     1 
ATOM   1642 C CA    . GLY A 1 223 ? 134.035 109.815 121.414 1.00 86.74  ? 308 GLY A CA    1 
ATOM   1643 C C     . GLY A 1 223 ? 133.080 110.064 122.564 1.00 81.96  ? 308 GLY A C     1 
ATOM   1644 O O     . GLY A 1 223 ? 133.366 109.706 123.710 1.00 82.75  ? 308 GLY A O     1 
ATOM   1645 N N     . TRP A 1 224 ? 131.936 110.689 122.280 1.00 78.13  ? 309 TRP A N     1 
ATOM   1646 C CA    . TRP A 1 224 ? 130.964 110.953 123.332 1.00 71.28  ? 309 TRP A CA    1 
ATOM   1647 C C     . TRP A 1 224 ? 130.163 109.707 123.694 1.00 71.09  ? 309 TRP A C     1 
ATOM   1648 O O     . TRP A 1 224 ? 129.605 109.640 124.794 1.00 72.19  ? 309 TRP A O     1 
ATOM   1649 C CB    . TRP A 1 224 ? 130.032 112.091 122.907 1.00 67.97  ? 309 TRP A CB    1 
ATOM   1650 C CG    . TRP A 1 224 ? 128.904 112.348 123.855 1.00 64.98  ? 309 TRP A CG    1 
ATOM   1651 C CD1   . TRP A 1 224 ? 127.572 112.220 123.602 1.00 66.53  ? 309 TRP A CD1   1 
ATOM   1652 C CD2   . TRP A 1 224 ? 129.015 112.776 125.217 1.00 65.15  ? 309 TRP A CD2   1 
ATOM   1653 N NE1   . TRP A 1 224 ? 126.844 112.544 124.721 1.00 65.55  ? 309 TRP A NE1   1 
ATOM   1654 C CE2   . TRP A 1 224 ? 127.707 112.889 125.727 1.00 65.56  ? 309 TRP A CE2   1 
ATOM   1655 C CE3   . TRP A 1 224 ? 130.094 113.076 126.053 1.00 62.46  ? 309 TRP A CE3   1 
ATOM   1656 C CZ2   . TRP A 1 224 ? 127.449 113.287 127.034 1.00 61.22  ? 309 TRP A CZ2   1 
ATOM   1657 C CZ3   . TRP A 1 224 ? 129.836 113.468 127.348 1.00 63.51  ? 309 TRP A CZ3   1 
ATOM   1658 C CH2   . TRP A 1 224 ? 128.524 113.578 127.826 1.00 66.05  ? 309 TRP A CH2   1 
ATOM   1659 N N     . ALA A 1 225 ? 130.102 108.718 122.799 1.00 73.39  ? 310 ALA A N     1 
ATOM   1660 C CA    . ALA A 1 225 ? 129.405 107.475 123.111 1.00 73.27  ? 310 ALA A CA    1 
ATOM   1661 C C     . ALA A 1 225 ? 130.129 106.665 124.178 1.00 70.89  ? 310 ALA A C     1 
ATOM   1662 O O     . ALA A 1 225 ? 129.485 106.156 125.101 1.00 69.32  ? 310 ALA A O     1 
ATOM   1663 C CB    . ALA A 1 225 ? 129.229 106.633 121.846 1.00 80.16  ? 310 ALA A CB    1 
ATOM   1664 N N     . VAL A 1 226 ? 131.453 106.529 124.072 1.00 72.82  ? 311 VAL A N     1 
ATOM   1665 C CA    . VAL A 1 226 ? 132.205 105.839 125.116 1.00 73.94  ? 311 VAL A CA    1 
ATOM   1666 C C     . VAL A 1 226 ? 132.184 106.652 126.405 1.00 74.03  ? 311 VAL A C     1 
ATOM   1667 O O     . VAL A 1 226 ? 132.184 106.093 127.509 1.00 72.97  ? 311 VAL A O     1 
ATOM   1668 C CB    . VAL A 1 226 ? 133.641 105.536 124.643 1.00 81.43  ? 311 VAL A CB    1 
ATOM   1669 C CG1   . VAL A 1 226 ? 134.426 106.819 124.409 1.00 80.53  ? 311 VAL A CG1   1 
ATOM   1670 C CG2   . VAL A 1 226 ? 134.355 104.638 125.646 1.00 85.33  ? 311 VAL A CG2   1 
ATOM   1671 N N     . SER A 1 227 ? 132.166 107.981 126.286 1.00 76.98  ? 312 SER A N     1 
ATOM   1672 C CA    . SER A 1 227 ? 132.045 108.835 127.463 1.00 69.57  ? 312 SER A CA    1 
ATOM   1673 C C     . SER A 1 227 ? 130.712 108.613 128.167 1.00 68.59  ? 312 SER A C     1 
ATOM   1674 O O     . SER A 1 227 ? 130.657 108.480 129.395 1.00 69.41  ? 312 SER A O     1 
ATOM   1675 C CB    . SER A 1 227 ? 132.197 110.302 127.056 1.00 69.72  ? 312 SER A CB    1 
ATOM   1676 O OG    . SER A 1 227 ? 133.460 110.540 126.460 1.00 73.69  ? 312 SER A OG    1 
ATOM   1677 N N     . LEU A 1 228 ? 129.624 108.564 127.396 1.00 68.77  ? 313 LEU A N     1 
ATOM   1678 C CA    . LEU A 1 228 ? 128.296 108.472 127.992 1.00 66.48  ? 313 LEU A CA    1 
ATOM   1679 C C     . LEU A 1 228 ? 128.047 107.093 128.591 1.00 61.82  ? 313 LEU A C     1 
ATOM   1680 O O     . LEU A 1 228 ? 127.315 106.969 129.579 1.00 65.95  ? 313 LEU A O     1 
ATOM   1681 C CB    . LEU A 1 228 ? 127.242 108.833 126.939 1.00 62.49  ? 313 LEU A CB    1 
ATOM   1682 C CG    . LEU A 1 228 ? 125.764 108.992 127.309 1.00 61.26  ? 313 LEU A CG    1 
ATOM   1683 C CD1   . LEU A 1 228 ? 125.101 109.939 126.328 1.00 64.43  ? 313 LEU A CD1   1 
ATOM   1684 C CD2   . LEU A 1 228 ? 125.041 107.666 127.293 1.00 61.86  ? 313 LEU A CD2   1 
ATOM   1685 N N     . LYS A 1 229 ? 128.649 106.048 128.018 1.00 61.72  ? 314 LYS A N     1 
ATOM   1686 C CA    . LYS A 1 229 ? 128.485 104.704 128.559 1.00 63.69  ? 314 LYS A CA    1 
ATOM   1687 C C     . LYS A 1 229 ? 129.219 104.519 129.880 1.00 62.82  ? 314 LYS A C     1 
ATOM   1688 O O     . LYS A 1 229 ? 128.708 103.838 130.776 1.00 63.67  ? 314 LYS A O     1 
ATOM   1689 C CB    . LYS A 1 229 ? 128.967 103.667 127.543 1.00 68.76  ? 314 LYS A CB    1 
ATOM   1690 C CG    . LYS A 1 229 ? 128.111 103.601 126.296 1.00 73.95  ? 314 LYS A CG    1 
ATOM   1691 C CD    . LYS A 1 229 ? 128.513 102.458 125.385 1.00 80.26  ? 314 LYS A CD    1 
ATOM   1692 C CE    . LYS A 1 229 ? 129.815 102.761 124.673 1.00 82.98  ? 314 LYS A CE    1 
ATOM   1693 N NZ    . LYS A 1 229 ? 130.161 101.695 123.695 1.00 74.86  ? 314 LYS A NZ    1 
ATOM   1694 N N     . ALA A 1 230 ? 130.411 105.104 130.019 1.00 64.05  ? 315 ALA A N     1 
ATOM   1695 C CA    . ALA A 1 230 ? 131.142 104.997 131.277 1.00 59.73  ? 315 ALA A CA    1 
ATOM   1696 C C     . ALA A 1 230 ? 130.412 105.717 132.404 1.00 63.05  ? 315 ALA A C     1 
ATOM   1697 O O     . ALA A 1 230 ? 130.351 105.215 133.532 1.00 69.11  ? 315 ALA A O     1 
ATOM   1698 C CB    . ALA A 1 230 ? 132.557 105.550 131.113 1.00 64.03  ? 315 ALA A CB    1 
ATOM   1699 N N     . MET A 1 231 ? 129.854 106.896 132.120 1.00 62.77  ? 316 MET A N     1 
ATOM   1700 C CA    . MET A 1 231 ? 129.173 107.663 133.158 1.00 57.73  ? 316 MET A CA    1 
ATOM   1701 C C     . MET A 1 231 ? 127.850 107.017 133.556 1.00 51.94  ? 316 MET A C     1 
ATOM   1702 O O     . MET A 1 231 ? 127.525 106.945 134.747 1.00 53.07  ? 316 MET A O     1 
ATOM   1703 C CB    . MET A 1 231 ? 128.956 109.098 132.686 1.00 60.50  ? 316 MET A CB    1 
ATOM   1704 C CG    . MET A 1 231 ? 130.241 109.811 132.309 1.00 67.24  ? 316 MET A CG    1 
ATOM   1705 S SD    . MET A 1 231 ? 130.002 111.580 132.100 1.00 78.97  ? 316 MET A SD    1 
ATOM   1706 C CE    . MET A 1 231 ? 129.263 111.595 130.474 1.00 62.24  ? 316 MET A CE    1 
ATOM   1707 N N     . MET A 1 232 ? 127.069 106.549 132.579 1.00 53.31  ? 317 MET A N     1 
ATOM   1708 C CA    . MET A 1 232 ? 125.823 105.863 132.901 1.00 44.15  ? 317 MET A CA    1 
ATOM   1709 C C     . MET A 1 232 ? 126.061 104.534 133.606 1.00 49.10  ? 317 MET A C     1 
ATOM   1710 O O     . MET A 1 232 ? 125.153 104.033 134.278 1.00 51.39  ? 317 MET A O     1 
ATOM   1711 C CB    . MET A 1 232 ? 124.987 105.645 131.638 1.00 50.36  ? 317 MET A CB    1 
ATOM   1712 C CG    . MET A 1 232 ? 124.523 106.928 130.966 1.00 55.32  ? 317 MET A CG    1 
ATOM   1713 S SD    . MET A 1 232 ? 123.573 107.992 132.071 1.00 62.18  ? 317 MET A SD    1 
ATOM   1714 C CE    . MET A 1 232 ? 124.632 109.434 132.147 1.00 56.94  ? 317 MET A CE    1 
ATOM   1715 N N     . SER A 1 233 ? 127.252 103.948 133.461 1.00 56.33  ? 318 SER A N     1 
ATOM   1716 C CA    . SER A 1 233 ? 127.599 102.775 134.254 1.00 53.34  ? 318 SER A CA    1 
ATOM   1717 C C     . SER A 1 233 ? 127.804 103.144 135.718 1.00 51.46  ? 318 SER A C     1 
ATOM   1718 O O     . SER A 1 233 ? 127.416 102.387 136.614 1.00 52.99  ? 318 SER A O     1 
ATOM   1719 C CB    . SER A 1 233 ? 128.854 102.109 133.689 1.00 56.89  ? 318 SER A CB    1 
ATOM   1720 O OG    . SER A 1 233 ? 129.986 102.949 133.828 1.00 62.42  ? 318 SER A OG    1 
ATOM   1721 N N     . ILE A 1 234 ? 128.417 104.301 135.974 1.00 52.21  ? 319 ILE A N     1 
ATOM   1722 C CA    . ILE A 1 234 ? 128.586 104.771 137.345 1.00 48.65  ? 319 ILE A CA    1 
ATOM   1723 C C     . ILE A 1 234 ? 127.242 105.157 137.947 1.00 46.56  ? 319 ILE A C     1 
ATOM   1724 O O     . ILE A 1 234 ? 126.993 104.932 139.137 1.00 47.83  ? 319 ILE A O     1 
ATOM   1725 C CB    . ILE A 1 234 ? 129.588 105.939 137.384 1.00 46.13  ? 319 ILE A CB    1 
ATOM   1726 C CG1   . ILE A 1 234 ? 130.887 105.531 136.692 1.00 48.67  ? 319 ILE A CG1   1 
ATOM   1727 C CG2   . ILE A 1 234 ? 129.859 106.371 138.815 1.00 53.69  ? 319 ILE A CG2   1 
ATOM   1728 C CD1   . ILE A 1 234 ? 131.938 106.598 136.707 1.00 53.52  ? 319 ILE A CD1   1 
ATOM   1729 N N     . VAL A 1 235 ? 126.355 105.744 137.138 1.00 49.07  ? 320 VAL A N     1 
ATOM   1730 C CA    . VAL A 1 235 ? 125.020 106.091 137.616 1.00 42.86  ? 320 VAL A CA    1 
ATOM   1731 C C     . VAL A 1 235 ? 124.286 104.848 138.100 1.00 44.90  ? 320 VAL A C     1 
ATOM   1732 O O     . VAL A 1 235 ? 123.614 104.877 139.139 1.00 48.78  ? 320 VAL A O     1 
ATOM   1733 C CB    . VAL A 1 235 ? 124.234 106.823 136.509 1.00 43.83  ? 320 VAL A CB    1 
ATOM   1734 C CG1   . VAL A 1 235 ? 122.737 106.762 136.774 1.00 45.39  ? 320 VAL A CG1   1 
ATOM   1735 C CG2   . VAL A 1 235 ? 124.702 108.267 136.396 1.00 41.88  ? 320 VAL A CG2   1 
ATOM   1736 N N     . VAL A 1 236 ? 124.408 103.739 137.370 1.00 45.78  ? 321 VAL A N     1 
ATOM   1737 C CA    . VAL A 1 236 ? 123.829 102.481 137.828 1.00 45.02  ? 321 VAL A CA    1 
ATOM   1738 C C     . VAL A 1 236 ? 124.561 101.966 139.060 1.00 47.51  ? 321 VAL A C     1 
ATOM   1739 O O     . VAL A 1 236 ? 123.931 101.575 140.049 1.00 49.07  ? 321 VAL A O     1 
ATOM   1740 C CB    . VAL A 1 236 ? 123.843 101.448 136.688 1.00 46.65  ? 321 VAL A CB    1 
ATOM   1741 C CG1   . VAL A 1 236 ? 123.503 100.063 137.218 1.00 47.48  ? 321 VAL A CG1   1 
ATOM   1742 C CG2   . VAL A 1 236 ? 122.868 101.856 135.606 1.00 44.03  ? 321 VAL A CG2   1 
ATOM   1743 N N     . GLY A 1 237 ? 125.895 101.964 139.027 1.00 47.69  ? 322 GLY A N     1 
ATOM   1744 C CA    . GLY A 1 237 ? 126.652 101.464 140.164 1.00 44.82  ? 322 GLY A CA    1 
ATOM   1745 C C     . GLY A 1 237 ? 126.449 102.297 141.415 1.00 46.40  ? 322 GLY A C     1 
ATOM   1746 O O     . GLY A 1 237 ? 126.242 101.757 142.504 1.00 53.04  ? 322 GLY A O     1 
ATOM   1747 N N     . MET A 1 238 ? 126.505 103.624 141.278 1.00 50.55  ? 323 MET A N     1 
ATOM   1748 C CA    . MET A 1 238 ? 126.215 104.496 142.408 1.00 48.44  ? 323 MET A CA    1 
ATOM   1749 C C     . MET A 1 238 ? 124.730 104.509 142.743 1.00 46.97  ? 323 MET A C     1 
ATOM   1750 O O     . MET A 1 238 ? 124.365 104.829 143.879 1.00 53.04  ? 323 MET A O     1 
ATOM   1751 C CB    . MET A 1 238 ? 126.704 105.916 142.117 1.00 47.04  ? 323 MET A CB    1 
ATOM   1752 C CG    . MET A 1 238 ? 128.216 106.043 141.989 1.00 56.99  ? 323 MET A CG    1 
ATOM   1753 S SD    . MET A 1 238 ? 129.134 105.582 143.469 1.00 84.31  ? 323 MET A SD    1 
ATOM   1754 C CE    . MET A 1 238 ? 128.679 106.921 144.567 1.00 49.88  ? 323 MET A CE    1 
ATOM   1755 N N     . GLY A 1 239 ? 123.871 104.181 141.778 1.00 46.64  ? 324 GLY A N     1 
ATOM   1756 C CA    . GLY A 1 239 ? 122.449 104.056 142.026 1.00 44.26  ? 324 GLY A CA    1 
ATOM   1757 C C     . GLY A 1 239 ? 122.097 102.773 142.748 1.00 45.11  ? 324 GLY A C     1 
ATOM   1758 O O     . GLY A 1 239 ? 121.189 102.754 143.584 1.00 47.89  ? 324 GLY A O     1 
ATOM   1759 N N     . LEU A 1 240 ? 122.807 101.687 142.428 1.00 46.01  ? 325 LEU A N     1 
ATOM   1760 C CA    . LEU A 1 240 ? 122.644 100.458 143.196 1.00 48.82  ? 325 LEU A CA    1 
ATOM   1761 C C     . LEU A 1 240 ? 123.138 100.634 144.625 1.00 50.02  ? 325 LEU A C     1 
ATOM   1762 O O     . LEU A 1 240 ? 122.551 100.070 145.555 1.00 56.23  ? 325 LEU A O     1 
ATOM   1763 C CB    . LEU A 1 240 ? 123.376 99.299  142.516 1.00 51.24  ? 325 LEU A CB    1 
ATOM   1764 C CG    . LEU A 1 240 ? 122.803 98.808  141.184 1.00 52.99  ? 325 LEU A CG    1 
ATOM   1765 C CD1   . LEU A 1 240 ? 123.631 97.658  140.634 1.00 54.05  ? 325 LEU A CD1   1 
ATOM   1766 C CD2   . LEU A 1 240 ? 121.347 98.395  141.347 1.00 47.05  ? 325 LEU A CD2   1 
ATOM   1767 N N     . ALA A 1 241 ? 124.204 101.416 144.819 1.00 48.93  ? 326 ALA A N     1 
ATOM   1768 C CA    . ALA A 1 241 ? 124.669 101.713 146.168 1.00 43.57  ? 326 ALA A CA    1 
ATOM   1769 C C     . ALA A 1 241 ? 123.589 102.396 146.994 1.00 48.84  ? 326 ALA A C     1 
ATOM   1770 O O     . ALA A 1 241 ? 123.528 102.205 148.213 1.00 58.33  ? 326 ALA A O     1 
ATOM   1771 C CB    . ALA A 1 241 ? 125.926 102.582 146.113 1.00 43.73  ? 326 ALA A CB    1 
ATOM   1772 N N     . ILE A 1 242 ? 122.729 103.191 146.352 1.00 52.19  ? 327 ILE A N     1 
ATOM   1773 C CA    . ILE A 1 242 ? 121.602 103.787 147.060 1.00 51.03  ? 327 ILE A CA    1 
ATOM   1774 C C     . ILE A 1 242 ? 120.616 102.707 147.491 1.00 49.52  ? 327 ILE A C     1 
ATOM   1775 O O     . ILE A 1 242 ? 120.055 102.762 148.591 1.00 54.95  ? 327 ILE A O     1 
ATOM   1776 C CB    . ILE A 1 242 ? 120.927 104.857 146.184 1.00 44.87  ? 327 ILE A CB    1 
ATOM   1777 C CG1   . ILE A 1 242 ? 121.943 105.923 145.770 1.00 43.55  ? 327 ILE A CG1   1 
ATOM   1778 C CG2   . ILE A 1 242 ? 119.770 105.501 146.927 1.00 49.34  ? 327 ILE A CG2   1 
ATOM   1779 C CD1   . ILE A 1 242 ? 121.530 106.721 144.553 1.00 44.85  ? 327 ILE A CD1   1 
ATOM   1780 N N     . CYS A 1 243 ? 120.390 101.709 146.632 1.00 50.89  ? 328 CYS A N     1 
ATOM   1781 C CA    . CYS A 1 243 ? 119.480 100.624 146.981 1.00 49.92  ? 328 CYS A CA    1 
ATOM   1782 C C     . CYS A 1 243 ? 120.077 99.700  148.037 1.00 56.21  ? 328 CYS A C     1 
ATOM   1783 O O     . CYS A 1 243 ? 119.341 99.166  148.874 1.00 64.05  ? 328 CYS A O     1 
ATOM   1784 C CB    . CYS A 1 243 ? 119.103 99.831  145.729 1.00 47.89  ? 328 CYS A CB    1 
ATOM   1785 S SG    . CYS A 1 243 ? 118.271 100.809 144.456 1.00 74.39  ? 328 CYS A SG    1 
ATOM   1786 N N     . LEU A 1 244 ? 121.395 99.491  148.013 1.00 55.33  ? 329 LEU A N     1 
ATOM   1787 C CA    . LEU A 1 244 ? 122.033 98.692  149.057 1.00 51.86  ? 329 LEU A CA    1 
ATOM   1788 C C     . LEU A 1 244 ? 122.125 99.454  150.374 1.00 52.97  ? 329 LEU A C     1 
ATOM   1789 O O     . LEU A 1 244 ? 121.934 98.866  151.444 1.00 60.72  ? 329 LEU A O     1 
ATOM   1790 C CB    . LEU A 1 244 ? 123.421 98.226  148.608 1.00 54.61  ? 329 LEU A CB    1 
ATOM   1791 C CG    . LEU A 1 244 ? 123.536 96.974  147.727 1.00 62.04  ? 329 LEU A CG    1 
ATOM   1792 C CD1   . LEU A 1 244 ? 123.042 95.757  148.497 1.00 56.70  ? 329 LEU A CD1   1 
ATOM   1793 C CD2   . LEU A 1 244 ? 122.798 97.096  146.404 1.00 59.08  ? 329 LEU A CD2   1 
ATOM   1794 N N     . LEU A 1 245 ? 122.418 100.756 150.323 1.00 52.96  ? 330 LEU A N     1 
ATOM   1795 C CA    . LEU A 1 245 ? 122.401 101.556 151.541 1.00 53.40  ? 330 LEU A CA    1 
ATOM   1796 C C     . LEU A 1 245 ? 120.996 101.689 152.114 1.00 59.64  ? 330 LEU A C     1 
ATOM   1797 O O     . LEU A 1 245 ? 120.850 101.955 153.311 1.00 67.02  ? 330 LEU A O     1 
ATOM   1798 C CB    . LEU A 1 245 ? 122.991 102.944 151.279 1.00 53.31  ? 330 LEU A CB    1 
ATOM   1799 C CG    . LEU A 1 245 ? 124.519 103.043 151.217 1.00 54.25  ? 330 LEU A CG    1 
ATOM   1800 C CD1   . LEU A 1 245 ? 124.945 104.358 150.582 1.00 53.38  ? 330 LEU A CD1   1 
ATOM   1801 C CD2   . LEU A 1 245 ? 125.127 102.892 152.603 1.00 55.06  ? 330 LEU A CD2   1 
ATOM   1802 N N     . TYR A 1 246 ? 119.966 101.516 151.287 1.00 61.85  ? 331 TYR A N     1 
ATOM   1803 C CA    . TYR A 1 246 ? 118.578 101.547 151.732 1.00 59.60  ? 331 TYR A CA    1 
ATOM   1804 C C     . TYR A 1 246 ? 118.140 100.212 152.317 1.00 61.41  ? 331 TYR A C     1 
ATOM   1805 O O     . TYR A 1 246 ? 117.390 100.178 153.298 1.00 71.64  ? 331 TYR A O     1 
ATOM   1806 C CB    . TYR A 1 246 ? 117.673 101.945 150.562 1.00 60.34  ? 331 TYR A CB    1 
ATOM   1807 C CG    . TYR A 1 246 ? 116.249 102.280 150.940 1.00 66.80  ? 331 TYR A CG    1 
ATOM   1808 C CD1   . TYR A 1 246 ? 115.915 103.543 151.409 1.00 64.85  ? 331 TYR A CD1   1 
ATOM   1809 C CD2   . TYR A 1 246 ? 115.232 101.346 150.792 1.00 66.42  ? 331 TYR A CD2   1 
ATOM   1810 C CE1   . TYR A 1 246 ? 114.613 103.859 151.745 1.00 65.22  ? 331 TYR A CE1   1 
ATOM   1811 C CE2   . TYR A 1 246 ? 113.926 101.655 151.120 1.00 63.36  ? 331 TYR A CE2   1 
ATOM   1812 C CZ    . TYR A 1 246 ? 113.624 102.912 151.600 1.00 65.76  ? 331 TYR A CZ    1 
ATOM   1813 O OH    . TYR A 1 246 ? 112.325 103.222 151.929 1.00 74.44  ? 331 TYR A OH    1 
ATOM   1814 N N     . TRP A 1 247 ? 118.605 99.107  151.729 1.00 58.92  ? 332 TRP A N     1 
ATOM   1815 C CA    . TRP A 1 247 ? 118.322 97.788  152.283 1.00 61.97  ? 332 TRP A CA    1 
ATOM   1816 C C     . TRP A 1 247 ? 118.964 97.603  153.652 1.00 68.28  ? 332 TRP A C     1 
ATOM   1817 O O     . TRP A 1 247 ? 118.458 96.833  154.476 1.00 73.25  ? 332 TRP A O     1 
ATOM   1818 C CB    . TRP A 1 247 ? 118.806 96.709  151.313 1.00 63.96  ? 332 TRP A CB    1 
ATOM   1819 C CG    . TRP A 1 247 ? 118.822 95.330  151.889 1.00 69.22  ? 332 TRP A CG    1 
ATOM   1820 C CD1   . TRP A 1 247 ? 117.770 94.467  151.988 1.00 75.09  ? 332 TRP A CD1   1 
ATOM   1821 C CD2   . TRP A 1 247 ? 119.951 94.652  152.451 1.00 71.26  ? 332 TRP A CD2   1 
ATOM   1822 N NE1   . TRP A 1 247 ? 118.175 93.293  152.576 1.00 76.86  ? 332 TRP A NE1   1 
ATOM   1823 C CE2   . TRP A 1 247 ? 119.510 93.382  152.870 1.00 74.93  ? 332 TRP A CE2   1 
ATOM   1824 C CE3   . TRP A 1 247 ? 121.293 94.998  152.640 1.00 75.85  ? 332 TRP A CE3   1 
ATOM   1825 C CZ2   . TRP A 1 247 ? 120.363 92.456  153.466 1.00 81.69  ? 332 TRP A CZ2   1 
ATOM   1826 C CZ3   . TRP A 1 247 ? 122.137 94.077  153.232 1.00 81.54  ? 332 TRP A CZ3   1 
ATOM   1827 C CH2   . TRP A 1 247 ? 121.670 92.822  153.638 1.00 85.98  ? 332 TRP A CH2   1 
ATOM   1828 N N     . TRP A 1 248 ? 120.070 98.300  153.917 1.00 69.81  ? 333 TRP A N     1 
ATOM   1829 C CA    . TRP A 1 248 ? 120.798 98.098  155.165 1.00 72.29  ? 333 TRP A CA    1 
ATOM   1830 C C     . TRP A 1 248 ? 120.135 98.826  156.330 1.00 80.50  ? 333 TRP A C     1 
ATOM   1831 O O     . TRP A 1 248 ? 119.957 98.251  157.409 1.00 90.34  ? 333 TRP A O     1 
ATOM   1832 C CB    . TRP A 1 248 ? 122.249 98.553  155.003 1.00 67.99  ? 333 TRP A CB    1 
ATOM   1833 C CG    . TRP A 1 248 ? 123.138 98.093  156.113 1.00 74.52  ? 333 TRP A CG    1 
ATOM   1834 C CD1   . TRP A 1 248 ? 123.773 96.890  156.208 1.00 74.84  ? 333 TRP A CD1   1 
ATOM   1835 C CD2   . TRP A 1 248 ? 123.488 98.826  157.291 1.00 74.46  ? 333 TRP A CD2   1 
ATOM   1836 N NE1   . TRP A 1 248 ? 124.500 96.829  157.372 1.00 74.21  ? 333 TRP A NE1   1 
ATOM   1837 C CE2   . TRP A 1 248 ? 124.341 98.006  158.055 1.00 77.35  ? 333 TRP A CE2   1 
ATOM   1838 C CE3   . TRP A 1 248 ? 123.165 100.098 157.774 1.00 74.64  ? 333 TRP A CE3   1 
ATOM   1839 C CZ2   . TRP A 1 248 ? 124.875 98.415  159.275 1.00 83.02  ? 333 TRP A CZ2   1 
ATOM   1840 C CZ3   . TRP A 1 248 ? 123.695 100.502 158.985 1.00 77.03  ? 333 TRP A CZ3   1 
ATOM   1841 C CH2   . TRP A 1 248 ? 124.541 99.664  159.721 1.00 81.46  ? 333 TRP A CH2   1 
ATOM   1842 N N     . VAL A 1 249 ? 119.770 100.096 156.134 1.00 73.79  ? 334 VAL A N     1 
ATOM   1843 C CA    . VAL A 1 249 ? 119.136 100.861 157.205 1.00 74.52  ? 334 VAL A CA    1 
ATOM   1844 C C     . VAL A 1 249 ? 117.771 100.280 157.553 1.00 80.57  ? 334 VAL A C     1 
ATOM   1845 O O     . VAL A 1 249 ? 117.319 100.376 158.700 1.00 89.13  ? 334 VAL A O     1 
ATOM   1846 C CB    . VAL A 1 249 ? 119.035 102.350 156.814 1.00 77.19  ? 334 VAL A CB    1 
ATOM   1847 C CG1   . VAL A 1 249 ? 118.590 103.188 158.002 1.00 79.94  ? 334 VAL A CG1   1 
ATOM   1848 C CG2   . VAL A 1 249 ? 120.370 102.850 156.294 1.00 75.52  ? 334 VAL A CG2   1 
ATOM   1849 N N     . ASN A 1 250 ? 117.097 99.665  156.582 1.00 77.57  ? 335 ASN A N     1 
ATOM   1850 C CA    . ASN A 1 250 ? 115.780 99.093  156.826 1.00 78.04  ? 335 ASN A CA    1 
ATOM   1851 C C     . ASN A 1 250 ? 115.830 97.701  157.441 1.00 85.35  ? 335 ASN A C     1 
ATOM   1852 O O     . ASN A 1 250 ? 114.797 97.212  157.911 1.00 93.05  ? 335 ASN A O     1 
ATOM   1853 C CB    . ASN A 1 250 ? 114.982 99.041  155.522 1.00 75.04  ? 335 ASN A CB    1 
ATOM   1854 C CG    . ASN A 1 250 ? 114.576 100.414 155.035 1.00 80.11  ? 335 ASN A CG    1 
ATOM   1855 O OD1   . ASN A 1 250 ? 114.645 100.709 153.845 1.00 81.03  ? 335 ASN A OD1   1 
ATOM   1856 N ND2   . ASN A 1 250 ? 114.153 101.268 155.962 1.00 84.68  ? 335 ASN A ND2   1 
ATOM   1857 N N     . ARG A 1 251 ? 116.995 97.054  157.455 1.00 84.29  ? 336 ARG A N     1 
ATOM   1858 C CA    . ARG A 1 251 ? 117.127 95.719  158.025 1.00 86.03  ? 336 ARG A CA    1 
ATOM   1859 C C     . ARG A 1 251 ? 117.950 95.675  159.303 1.00 88.88  ? 336 ARG A C     1 
ATOM   1860 O O     . ARG A 1 251 ? 117.717 94.798  160.138 1.00 92.26  ? 336 ARG A O     1 
ATOM   1861 C CB    . ARG A 1 251 ? 117.754 94.760  157.003 1.00 85.06  ? 336 ARG A CB    1 
ATOM   1862 C CG    . ARG A 1 251 ? 117.603 93.287  157.363 1.00 88.97  ? 336 ARG A CG    1 
ATOM   1863 C CD    . ARG A 1 251 ? 118.586 92.417  156.598 1.00 91.90  ? 336 ARG A CD    1 
ATOM   1864 N NE    . ARG A 1 251 ? 118.349 90.998  156.831 1.00 99.52  ? 336 ARG A NE    1 
ATOM   1865 C CZ    . ARG A 1 251 ? 117.507 90.253  156.128 1.00 102.28 ? 336 ARG A CZ    1 
ATOM   1866 N NH1   . ARG A 1 251 ? 116.804 90.760  155.128 1.00 98.80  ? 336 ARG A NH1   1 
ATOM   1867 N NH2   . ARG A 1 251 ? 117.365 88.967  156.437 1.00 102.95 ? 336 ARG A NH2   1 
ATOM   1868 N N     . TYR A 1 252 ? 118.895 96.597  159.484 1.00 88.27  ? 337 TYR A N     1 
ATOM   1869 C CA    . TYR A 1 252 ? 119.794 96.558  160.626 1.00 90.17  ? 337 TYR A CA    1 
ATOM   1870 C C     . TYR A 1 252 ? 119.707 97.779  161.530 1.00 95.11  ? 337 TYR A C     1 
ATOM   1871 O O     . TYR A 1 252 ? 120.336 97.780  162.594 1.00 100.49 ? 337 TYR A O     1 
ATOM   1872 C CB    . TYR A 1 252 ? 121.246 96.388  160.152 1.00 87.68  ? 337 TYR A CB    1 
ATOM   1873 C CG    . TYR A 1 252 ? 121.503 95.061  159.476 1.00 89.37  ? 337 TYR A CG    1 
ATOM   1874 C CD1   . TYR A 1 252 ? 121.623 93.892  160.217 1.00 89.02  ? 337 TYR A CD1   1 
ATOM   1875 C CD2   . TYR A 1 252 ? 121.617 94.974  158.094 1.00 88.67  ? 337 TYR A CD2   1 
ATOM   1876 C CE1   . TYR A 1 252 ? 121.854 92.677  159.601 1.00 90.76  ? 337 TYR A CE1   1 
ATOM   1877 C CE2   . TYR A 1 252 ? 121.848 93.763  157.470 1.00 91.51  ? 337 TYR A CE2   1 
ATOM   1878 C CZ    . TYR A 1 252 ? 121.965 92.618  158.228 1.00 95.63  ? 337 TYR A CZ    1 
ATOM   1879 O OH    . TYR A 1 252 ? 122.195 91.410  157.611 1.00 100.28 ? 337 TYR A OH    1 
ATOM   1880 N N     . VAL A 1 253 ? 118.959 98.803  161.151 1.00 94.83  ? 338 VAL A N     1 
ATOM   1881 C CA    . VAL A 1 253 ? 118.789 100.013 161.952 1.00 100.52 ? 338 VAL A CA    1 
ATOM   1882 C C     . VAL A 1 253 ? 117.353 100.045 162.457 1.00 108.94 ? 338 VAL A C     1 
ATOM   1883 O O     . VAL A 1 253 ? 116.424 99.914  161.653 1.00 108.65 ? 338 VAL A O     1 
ATOM   1884 C CB    . VAL A 1 253 ? 119.108 101.286 161.145 1.00 93.63  ? 338 VAL A CB    1 
ATOM   1885 C CG1   . VAL A 1 253 ? 118.660 102.527 161.905 1.00 95.68  ? 338 VAL A CG1   1 
ATOM   1886 C CG2   . VAL A 1 253 ? 120.590 101.349 160.829 1.00 89.54  ? 338 VAL A CG2   1 
ATOM   1887 N N     . PRO A 1 254 ? 117.127 100.202 163.762 1.00 113.30 ? 339 PRO A N     1 
ATOM   1888 C CA    . PRO A 1 254 ? 115.750 100.231 164.275 1.00 118.11 ? 339 PRO A CA    1 
ATOM   1889 C C     . PRO A 1 254 ? 114.996 101.449 163.757 1.00 123.66 ? 339 PRO A C     1 
ATOM   1890 O O     . PRO A 1 254 ? 115.425 102.589 163.943 1.00 121.49 ? 339 PRO A O     1 
ATOM   1891 C CB    . PRO A 1 254 ? 115.939 100.287 165.796 1.00 115.85 ? 339 PRO A CB    1 
ATOM   1892 C CG    . PRO A 1 254 ? 117.306 100.872 165.981 1.00 111.49 ? 339 PRO A CG    1 
ATOM   1893 C CD    . PRO A 1 254 ? 118.121 100.340 164.839 1.00 108.46 ? 339 PRO A CD    1 
ATOM   1894 N N     . LEU A 1 255 ? 113.867 101.193 163.099 1.00 129.76 ? 340 LEU A N     1 
ATOM   1895 C CA    . LEU A 1 255 ? 113.023 102.269 162.590 1.00 134.82 ? 340 LEU A CA    1 
ATOM   1896 C C     . LEU A 1 255 ? 112.124 102.797 163.705 1.00 141.47 ? 340 LEU A C     1 
ATOM   1897 O O     . LEU A 1 255 ? 111.431 102.009 164.360 1.00 145.08 ? 340 LEU A O     1 
ATOM   1898 C CB    . LEU A 1 255 ? 112.191 101.792 161.401 1.00 136.69 ? 340 LEU A CB    1 
ATOM   1899 C CG    . LEU A 1 255 ? 110.998 100.843 161.553 1.00 138.47 ? 340 LEU A CG    1 
ATOM   1900 C CD1   . LEU A 1 255 ? 110.158 100.849 160.285 1.00 132.32 ? 340 LEU A CD1   1 
ATOM   1901 C CD2   . LEU A 1 255 ? 111.447 99.428  161.888 1.00 133.42 ? 340 LEU A CD2   1 
ATOM   1902 N N     . PRO A 1 256 ? 112.151 104.105 163.977 1.00 140.66 ? 341 PRO A N     1 
ATOM   1903 C CA    . PRO A 1 256 ? 111.401 104.627 165.134 1.00 146.19 ? 341 PRO A CA    1 
ATOM   1904 C C     . PRO A 1 256 ? 109.903 104.387 165.070 1.00 153.02 ? 341 PRO A C     1 
ATOM   1905 O O     . PRO A 1 256 ? 109.291 104.087 166.103 1.00 154.34 ? 341 PRO A O     1 
ATOM   1906 C CB    . PRO A 1 256 ? 111.733 106.126 165.110 1.00 141.02 ? 341 PRO A CB    1 
ATOM   1907 C CG    . PRO A 1 256 ? 113.027 106.219 164.373 1.00 128.91 ? 341 PRO A CG    1 
ATOM   1908 C CD    . PRO A 1 256 ? 112.965 105.146 163.328 1.00 126.83 ? 341 PRO A CD    1 
ATOM   1909 N N     . THR A 1 257 ? 109.298 104.490 163.885 1.00 153.85 ? 342 THR A N     1 
ATOM   1910 C CA    . THR A 1 257 ? 107.841 104.464 163.729 1.00 157.13 ? 342 THR A CA    1 
ATOM   1911 C C     . THR A 1 257 ? 107.175 105.423 164.714 1.00 159.86 ? 342 THR A C     1 
ATOM   1912 O O     . THR A 1 257 ? 106.267 105.055 165.464 1.00 159.92 ? 342 THR A O     1 
ATOM   1913 C CB    . THR A 1 257 ? 107.281 103.047 163.886 1.00 154.78 ? 342 THR A CB    1 
ATOM   1914 O OG1   . THR A 1 257 ? 107.550 102.560 165.207 1.00 156.01 ? 342 THR A OG1   1 
ATOM   1915 C CG2   . THR A 1 257 ? 107.898 102.110 162.865 1.00 146.29 ? 342 THR A CG2   1 
ATOM   1916 N N     . ARG A 1 258 ? 107.652 106.667 164.714 1.00 160.43 ? 343 ARG A N     1 
ATOM   1917 C CA    . ARG A 1 258 ? 107.179 107.658 165.672 1.00 162.53 ? 343 ARG A CA    1 
ATOM   1918 C C     . ARG A 1 258 ? 105.677 107.870 165.539 1.00 168.18 ? 343 ARG A C     1 
ATOM   1919 O O     . ARG A 1 258 ? 105.148 107.990 164.430 1.00 166.04 ? 343 ARG A O     1 
ATOM   1920 C CB    . ARG A 1 258 ? 107.923 108.979 165.476 1.00 158.46 ? 343 ARG A CB    1 
ATOM   1921 C CG    . ARG A 1 258 ? 109.416 108.911 165.781 1.00 154.98 ? 343 ARG A CG    1 
ATOM   1922 C CD    . ARG A 1 258 ? 109.681 108.610 167.253 1.00 157.56 ? 343 ARG A CD    1 
ATOM   1923 N NE    . ARG A 1 258 ? 109.737 107.179 167.529 1.00 158.71 ? 343 ARG A NE    1 
ATOM   1924 C CZ    . ARG A 1 258 ? 109.665 106.645 168.741 1.00 156.73 ? 343 ARG A CZ    1 
ATOM   1925 N NH1   . ARG A 1 258 ? 109.530 107.397 169.821 1.00 156.25 ? 343 ARG A NH1   1 
ATOM   1926 N NH2   . ARG A 1 258 ? 109.728 105.323 168.872 1.00 152.85 ? 343 ARG A NH2   1 
ATOM   1927 N N     . SER A 1 259 ? 104.994 107.909 166.680 1.00 171.33 ? 344 SER A N     1 
ATOM   1928 C CA    . SER A 1 259 ? 103.543 108.017 166.688 1.00 172.62 ? 344 SER A CA    1 
ATOM   1929 C C     . SER A 1 259 ? 103.094 109.360 166.126 1.00 174.52 ? 344 SER A C     1 
ATOM   1930 O O     . SER A 1 259 ? 103.667 110.408 166.435 1.00 173.62 ? 344 SER A O     1 
ATOM   1931 C CB    . SER A 1 259 ? 103.006 107.837 168.107 1.00 168.11 ? 344 SER A CB    1 
ATOM   1932 O OG    . SER A 1 259 ? 101.596 107.980 168.139 1.00 165.58 ? 344 SER A OG    1 
ATOM   1933 N N     . LYS A 1 260 ? 102.061 109.316 165.294 1.00 174.64 ? 345 LYS A N     1 
ATOM   1934 C CA    . LYS A 1 260 ? 101.471 110.511 164.719 1.00 172.08 ? 345 LYS A CA    1 
ATOM   1935 C C     . LYS A 1 260 ? 100.440 111.110 165.671 1.00 173.03 ? 345 LYS A C     1 
ATOM   1936 O O     . LYS A 1 260 ? 99.905  110.436 166.556 1.00 172.46 ? 345 LYS A O     1 
ATOM   1937 C CB    . LYS A 1 260 ? 100.817 110.182 163.379 1.00 169.49 ? 345 LYS A CB    1 
ATOM   1938 C CG    . LYS A 1 260 ? 99.648  109.226 163.521 1.00 170.53 ? 345 LYS A CG    1 
ATOM   1939 C CD    . LYS A 1 260 ? 99.036  108.866 162.186 1.00 170.11 ? 345 LYS A CD    1 
ATOM   1940 C CE    . LYS A 1 260 ? 97.836  107.961 162.390 1.00 169.57 ? 345 LYS A CE    1 
ATOM   1941 N NZ    . LYS A 1 260 ? 98.228  106.640 162.956 1.00 163.25 ? 345 LYS A NZ    1 
ATOM   1942 N N     . ASN A 1 261 ? 100.165 112.399 165.481 1.00 173.13 ? 346 ASN A N     1 
ATOM   1943 C CA    . ASN A 1 261 ? 99.133  113.072 166.259 1.00 173.62 ? 346 ASN A CA    1 
ATOM   1944 C C     . ASN A 1 261 ? 97.785  113.061 165.550 1.00 173.52 ? 346 ASN A C     1 
ATOM   1945 O O     . ASN A 1 261 ? 96.741  112.962 166.204 1.00 171.15 ? 346 ASN A O     1 
ATOM   1946 C CB    . ASN A 1 261 ? 99.547  114.517 166.555 1.00 172.04 ? 346 ASN A CB    1 
ATOM   1947 C CG    . ASN A 1 261 ? 100.810 114.602 167.387 1.00 171.71 ? 346 ASN A CG    1 
ATOM   1948 O OD1   . ASN A 1 261 ? 101.838 115.100 166.926 1.00 171.46 ? 346 ASN A OD1   1 
ATOM   1949 N ND2   . ASN A 1 261 ? 100.740 114.118 168.621 1.00 171.19 ? 346 ASN A ND2   1 
ATOM   1950 N N     . LYS A 1 262 ? 97.790  113.156 164.224 1.00 175.90 ? 347 LYS A N     1 
ATOM   1951 C CA    . LYS A 1 262 ? 96.556  113.206 163.459 1.00 176.85 ? 347 LYS A CA    1 
ATOM   1952 C C     . LYS A 1 262 ? 95.998  111.805 163.232 1.00 177.66 ? 347 LYS A C     1 
ATOM   1953 O O     . LYS A 1 262 ? 96.696  110.796 163.359 1.00 175.51 ? 347 LYS A O     1 
ATOM   1954 C CB    . LYS A 1 262 ? 96.784  113.898 162.114 1.00 173.91 ? 347 LYS A CB    1 
ATOM   1955 C CG    . LYS A 1 262 ? 97.068  115.386 162.217 1.00 167.75 ? 347 LYS A CG    1 
ATOM   1956 C CD    . LYS A 1 262 ? 97.427  115.968 160.860 1.00 160.34 ? 347 LYS A CD    1 
ATOM   1957 C CE    . LYS A 1 262 ? 96.251  115.890 159.899 1.00 162.46 ? 347 LYS A CE    1 
ATOM   1958 N NZ    . LYS A 1 262 ? 96.545  116.564 158.604 1.00 160.50 ? 347 LYS A NZ    1 
ATOM   1959 N N     . LYS A 1 263 ? 94.714  111.760 162.895 1.00 178.97 ? 348 LYS A N     1 
ATOM   1960 C CA    . LYS A 1 263 ? 94.060  110.513 162.537 1.00 178.02 ? 348 LYS A CA    1 
ATOM   1961 C C     . LYS A 1 263 ? 94.507  110.056 161.150 1.00 177.02 ? 348 LYS A C     1 
ATOM   1962 O O     . LYS A 1 263 ? 95.098  110.814 160.376 1.00 174.44 ? 348 LYS A O     1 
ATOM   1963 C CB    . LYS A 1 263 ? 92.543  110.688 162.570 1.00 174.83 ? 348 LYS A CB    1 
ATOM   1964 C CG    . LYS A 1 263 ? 92.059  111.855 161.721 1.00 173.82 ? 348 LYS A CG    1 
ATOM   1965 C CD    . LYS A 1 263 ? 90.682  112.340 162.138 1.00 169.90 ? 348 LYS A CD    1 
ATOM   1966 C CE    . LYS A 1 263 ? 90.247  113.527 161.291 1.00 166.69 ? 348 LYS A CE    1 
ATOM   1967 N NZ    . LYS A 1 263 ? 91.158  114.695 161.461 1.00 168.71 ? 348 LYS A NZ    1 
ATOM   1968 N N     . GLU A 1 264 ? 94.227  108.790 160.843 1.00 175.81 ? 349 GLU A N     1 
ATOM   1969 C CA    . GLU A 1 264 ? 94.453  108.272 159.499 1.00 174.83 ? 349 GLU A CA    1 
ATOM   1970 C C     . GLU A 1 264 ? 93.351  108.672 158.527 1.00 175.53 ? 349 GLU A C     1 
ATOM   1971 O O     . GLU A 1 264 ? 93.473  108.397 157.330 1.00 174.53 ? 349 GLU A O     1 
ATOM   1972 C CB    . GLU A 1 264 ? 94.581  106.746 159.524 1.00 171.23 ? 349 GLU A CB    1 
ATOM   1973 C CG    . GLU A 1 264 ? 95.923  106.237 160.022 1.00 168.91 ? 349 GLU A CG    1 
ATOM   1974 C CD    . GLU A 1 264 ? 97.045  106.475 159.027 1.00 168.99 ? 349 GLU A CD    1 
ATOM   1975 O OE1   . GLU A 1 264 ? 96.777  106.449 157.808 1.00 167.20 ? 349 GLU A OE1   1 
ATOM   1976 O OE2   . GLU A 1 264 ? 98.196  106.689 159.463 1.00 169.22 ? 349 GLU A OE2   1 
ATOM   1977 N N     . LYS A 1 265 ? 92.287  109.307 159.014 1.00 177.54 ? 350 LYS A N     1 
ATOM   1978 C CA    . LYS A 1 265 ? 91.183  109.682 158.141 1.00 177.18 ? 350 LYS A CA    1 
ATOM   1979 C C     . LYS A 1 265 ? 91.566  110.624 157.003 1.00 178.30 ? 350 LYS A C     1 
ATOM   1980 O O     . LYS A 1 265 ? 90.857  110.607 155.981 1.00 176.10 ? 350 LYS A O     1 
ATOM   1981 C CB    . LYS A 1 265 ? 90.050  110.288 158.979 1.00 174.60 ? 350 LYS A CB    1 
ATOM   1982 C CG    . LYS A 1 265 ? 89.054  109.261 159.499 1.00 171.16 ? 350 LYS A CG    1 
ATOM   1983 C CD    . LYS A 1 265 ? 89.665  108.366 160.566 1.00 168.35 ? 350 LYS A CD    1 
ATOM   1984 C CE    . LYS A 1 265 ? 88.649  107.376 161.111 1.00 160.33 ? 350 LYS A CE    1 
ATOM   1985 N NZ    . LYS A 1 265 ? 89.280  106.410 162.052 1.00 153.19 ? 350 LYS A NZ    1 
ATOM   1986 N N     . PRO A 1 266 ? 92.623  111.455 157.085 1.00 179.22 ? 351 PRO A N     1 
ATOM   1987 C CA    . PRO A 1 266 ? 93.007  112.203 155.883 1.00 177.84 ? 351 PRO A CA    1 
ATOM   1988 C C     . PRO A 1 266 ? 93.520  111.274 154.799 1.00 177.28 ? 351 PRO A C     1 
ATOM   1989 O O     . PRO A 1 266 ? 94.681  110.849 154.806 1.00 176.46 ? 351 PRO A O     1 
ATOM   1990 C CB    . PRO A 1 266 ? 94.115  113.131 156.391 1.00 174.97 ? 351 PRO A CB    1 
ATOM   1991 C CG    . PRO A 1 266 ? 93.745  113.400 157.791 1.00 173.94 ? 351 PRO A CG    1 
ATOM   1992 C CD    . PRO A 1 266 ? 93.081  112.140 158.309 1.00 176.31 ? 351 PRO A CD    1 
ATOM   1993 N N     . LYS A 1 267 ? 92.642  111.005 153.833 1.00 176.17 ? 352 LYS A N     1 
ATOM   1994 C CA    . LYS A 1 267 ? 92.839  110.078 152.725 1.00 174.42 ? 352 LYS A CA    1 
ATOM   1995 C C     . LYS A 1 267 ? 91.804  110.419 151.664 1.00 173.21 ? 352 LYS A C     1 
ATOM   1996 O O     . LYS A 1 267 ? 91.089  111.418 151.801 1.00 171.31 ? 352 LYS A O     1 
ATOM   1997 C CB    . LYS A 1 267 ? 92.693  108.608 153.156 1.00 171.68 ? 352 LYS A CB    1 
ATOM   1998 C CG    . LYS A 1 267 ? 93.763  108.079 154.103 1.00 170.99 ? 352 LYS A CG    1 
ATOM   1999 C CD    . LYS A 1 267 ? 93.520  106.630 154.488 1.00 167.35 ? 352 LYS A CD    1 
ATOM   2000 C CE    . LYS A 1 267 ? 94.617  106.124 155.416 1.00 166.47 ? 352 LYS A CE    1 
ATOM   2001 N NZ    . LYS A 1 267 ? 94.407  104.712 155.838 1.00 164.28 ? 352 LYS A NZ    1 
ATOM   2002 N N     . MET A 1 268 ? 91.717  109.608 150.609 1.00 173.43 ? 353 MET A N     1 
ATOM   2003 C CA    . MET A 1 268 ? 90.720  109.792 149.554 1.00 172.41 ? 353 MET A CA    1 
ATOM   2004 C C     . MET A 1 268 ? 90.813  111.177 148.921 1.00 170.03 ? 353 MET A C     1 
ATOM   2005 O O     . MET A 1 268 ? 89.811  111.731 148.460 1.00 168.60 ? 353 MET A O     1 
ATOM   2006 C CB    . MET A 1 268 ? 89.302  109.542 150.080 1.00 172.06 ? 353 MET A CB    1 
ATOM   2007 C CG    . MET A 1 268 ? 89.028  108.104 150.490 1.00 171.59 ? 353 MET A CG    1 
ATOM   2008 S SD    . MET A 1 268 ? 87.330  107.851 151.043 1.00 170.42 ? 353 MET A SD    1 
ATOM   2009 C CE    . MET A 1 268 ? 87.377  108.636 152.652 1.00 163.29 ? 353 MET A CE    1 
ATOM   2010 N N     . GLY A 1 269 ? 92.014  111.746 148.898 1.00 165.89 ? 354 GLY A N     1 
ATOM   2011 C CA    . GLY A 1 269 ? 92.222  113.059 148.322 1.00 158.99 ? 354 GLY A CA    1 
ATOM   2012 C C     . GLY A 1 269 ? 93.187  113.026 147.157 1.00 152.91 ? 354 GLY A C     1 
ATOM   2013 O O     . GLY A 1 269 ? 94.365  112.697 147.326 1.00 151.13 ? 354 GLY A O     1 
ATOM   2014 N N     . THR A 1 270 ? 92.698  113.364 145.966 1.00 149.88 ? 355 THR A N     1 
ATOM   2015 C CA    . THR A 1 270 ? 93.528  113.320 144.770 1.00 148.96 ? 355 THR A CA    1 
ATOM   2016 C C     . THR A 1 270 ? 93.489  114.648 144.024 1.00 148.60 ? 355 THR A C     1 
ATOM   2017 O O     . THR A 1 270 ? 94.428  114.983 143.296 1.00 146.90 ? 355 THR A O     1 
ATOM   2018 C CB    . THR A 1 270 ? 93.084  112.175 143.853 1.00 148.65 ? 355 THR A CB    1 
ATOM   2019 O OG1   . THR A 1 270 ? 93.978  112.075 142.738 1.00 144.92 ? 355 THR A OG1   1 
ATOM   2020 C CG2   . THR A 1 270 ? 91.664  112.399 143.348 1.00 147.33 ? 355 THR A CG2   1 
ATOM   2021 N N     . MET A 1 271 ? 92.418  115.415 144.208 1.00 149.92 ? 356 MET A N     1 
ATOM   2022 C CA    . MET A 1 271 ? 92.243  116.682 143.509 1.00 149.96 ? 356 MET A CA    1 
ATOM   2023 C C     . MET A 1 271 ? 92.127  117.876 144.440 1.00 147.80 ? 356 MET A C     1 
ATOM   2024 O O     . MET A 1 271 ? 92.639  118.951 144.117 1.00 146.54 ? 356 MET A O     1 
ATOM   2025 C CB    . MET A 1 271 ? 91.005  116.618 142.602 1.00 149.24 ? 356 MET A CB    1 
ATOM   2026 C CG    . MET A 1 271 ? 91.174  115.735 141.373 1.00 150.63 ? 356 MET A CG    1 
ATOM   2027 S SD    . MET A 1 271 ? 92.740  116.005 140.516 1.00 157.68 ? 356 MET A SD    1 
ATOM   2028 C CE    . MET A 1 271 ? 93.336  114.323 140.350 1.00 143.79 ? 356 MET A CE    1 
ATOM   2029 N N     . GLU A 1 272 ? 91.467  117.727 145.588 1.00 147.38 ? 357 GLU A N     1 
ATOM   2030 C CA    . GLU A 1 272 ? 91.369  118.815 146.553 1.00 143.91 ? 357 GLU A CA    1 
ATOM   2031 C C     . GLU A 1 272 ? 92.499  118.813 147.572 1.00 141.62 ? 357 GLU A C     1 
ATOM   2032 O O     . GLU A 1 272 ? 92.535  119.696 148.435 1.00 139.29 ? 357 GLU A O     1 
ATOM   2033 C CB    . GLU A 1 272 ? 90.018  118.782 147.274 1.00 143.99 ? 357 GLU A CB    1 
ATOM   2034 C CG    . GLU A 1 272 ? 88.824  118.961 146.353 1.00 145.44 ? 357 GLU A CG    1 
ATOM   2035 C CD    . GLU A 1 272 ? 87.653  119.629 147.047 1.00 147.35 ? 357 GLU A CD    1 
ATOM   2036 O OE1   . GLU A 1 272 ? 87.613  119.612 148.295 1.00 150.52 ? 357 GLU A OE1   1 
ATOM   2037 O OE2   . GLU A 1 272 ? 86.779  120.182 146.345 1.00 143.26 ? 357 GLU A OE2   1 
ATOM   2038 N N     . SER A 1 273 ? 93.428  117.857 147.495 1.00 142.62 ? 358 SER A N     1 
ATOM   2039 C CA    . SER A 1 273 ? 94.674  118.009 148.233 1.00 137.63 ? 358 SER A CA    1 
ATOM   2040 C C     . SER A 1 273 ? 95.413  119.266 147.798 1.00 136.96 ? 358 SER A C     1 
ATOM   2041 O O     . SER A 1 273 ? 95.964  119.981 148.643 1.00 136.12 ? 358 SER A O     1 
ATOM   2042 C CB    . SER A 1 273 ? 95.560  116.778 148.039 1.00 134.43 ? 358 SER A CB    1 
ATOM   2043 O OG    . SER A 1 273 ? 94.948  115.620 148.578 1.00 132.24 ? 358 SER A OG    1 
ATOM   2044 N N     . LEU A 1 274 ? 95.405  119.564 146.497 1.00 136.95 ? 359 LEU A N     1 
ATOM   2045 C CA    . LEU A 1 274 ? 95.959  120.815 145.997 1.00 137.81 ? 359 LEU A CA    1 
ATOM   2046 C C     . LEU A 1 274 ? 95.202  122.025 146.534 1.00 135.45 ? 359 LEU A C     1 
ATOM   2047 O O     . LEU A 1 274 ? 95.822  123.045 146.851 1.00 130.90 ? 359 LEU A O     1 
ATOM   2048 C CB    . LEU A 1 274 ? 95.939  120.824 144.466 1.00 137.16 ? 359 LEU A CB    1 
ATOM   2049 C CG    . LEU A 1 274 ? 97.098  120.157 143.711 1.00 135.98 ? 359 LEU A CG    1 
ATOM   2050 C CD1   . LEU A 1 274 ? 98.417  120.855 144.014 1.00 130.42 ? 359 LEU A CD1   1 
ATOM   2051 C CD2   . LEU A 1 274 ? 97.190  118.661 144.000 1.00 130.95 ? 359 LEU A CD2   1 
ATOM   2052 N N     . LYS A 1 275 ? 93.873  121.934 146.640 1.00 134.83 ? 360 LYS A N     1 
ATOM   2053 C CA    . LYS A 1 275 ? 93.101  123.037 147.205 1.00 132.11 ? 360 LYS A CA    1 
ATOM   2054 C C     . LYS A 1 275 ? 93.449  123.264 148.671 1.00 130.39 ? 360 LYS A C     1 
ATOM   2055 O O     . LYS A 1 275 ? 93.556  124.411 149.121 1.00 128.20 ? 360 LYS A O     1 
ATOM   2056 C CB    . LYS A 1 275 ? 91.605  122.772 147.043 1.00 134.03 ? 360 LYS A CB    1 
ATOM   2057 C CG    . LYS A 1 275 ? 90.725  123.911 147.534 1.00 131.40 ? 360 LYS A CG    1 
ATOM   2058 C CD    . LYS A 1 275 ? 89.307  123.791 147.002 1.00 130.70 ? 360 LYS A CD    1 
ATOM   2059 C CE    . LYS A 1 275 ? 88.673  125.161 146.822 1.00 123.61 ? 360 LYS A CE    1 
ATOM   2060 N NZ    . LYS A 1 275 ? 87.829  125.541 147.988 1.00 118.65 ? 360 LYS A NZ    1 
ATOM   2061 N N     . PHE A 1 276 ? 93.616  122.182 149.435 1.00 132.36 ? 361 PHE A N     1 
ATOM   2062 C CA    . PHE A 1 276 ? 94.059  122.319 150.820 1.00 130.62 ? 361 PHE A CA    1 
ATOM   2063 C C     . PHE A 1 276 ? 95.446  122.944 150.892 1.00 130.24 ? 361 PHE A C     1 
ATOM   2064 O O     . PHE A 1 276 ? 95.707  123.798 151.747 1.00 127.46 ? 361 PHE A O     1 
ATOM   2065 C CB    . PHE A 1 276 ? 94.047  120.959 151.520 1.00 129.15 ? 361 PHE A CB    1 
ATOM   2066 C CG    . PHE A 1 276 ? 94.375  121.029 152.988 1.00 132.52 ? 361 PHE A CG    1 
ATOM   2067 C CD1   . PHE A 1 276 ? 95.688  120.934 153.424 1.00 131.58 ? 361 PHE A CD1   1 
ATOM   2068 C CD2   . PHE A 1 276 ? 93.374  121.199 153.930 1.00 132.59 ? 361 PHE A CD2   1 
ATOM   2069 C CE1   . PHE A 1 276 ? 95.995  121.002 154.769 1.00 128.69 ? 361 PHE A CE1   1 
ATOM   2070 C CE2   . PHE A 1 276 ? 93.675  121.268 155.278 1.00 131.26 ? 361 PHE A CE2   1 
ATOM   2071 C CZ    . PHE A 1 276 ? 94.988  121.169 155.698 1.00 128.58 ? 361 PHE A CZ    1 
ATOM   2072 N N     . LEU A 1 277 ? 96.350  122.529 150.007 1.00 128.45 ? 362 LEU A N     1 
ATOM   2073 C CA    . LEU A 1 277 ? 97.707  123.055 150.012 1.00 126.09 ? 362 LEU A CA    1 
ATOM   2074 C C     . LEU A 1 277 ? 97.780  124.507 149.548 1.00 123.45 ? 362 LEU A C     1 
ATOM   2075 O O     . LEU A 1 277 ? 98.734  125.208 149.905 1.00 120.76 ? 362 LEU A O     1 
ATOM   2076 C CB    . LEU A 1 277 ? 98.604  122.174 149.137 1.00 126.71 ? 362 LEU A CB    1 
ATOM   2077 C CG    . LEU A 1 277 ? 100.107 122.455 149.171 1.00 124.41 ? 362 LEU A CG    1 
ATOM   2078 C CD1   . LEU A 1 277 ? 100.659 122.192 150.564 1.00 116.09 ? 362 LEU A CD1   1 
ATOM   2079 C CD2   . LEU A 1 277 ? 100.822 121.604 148.141 1.00 117.84 ? 362 LEU A CD2   1 
ATOM   2080 N N     . VAL A 1 278 ? 96.804  124.974 148.769 1.00 124.02 ? 363 VAL A N     1 
ATOM   2081 C CA    . VAL A 1 278 ? 96.785  126.365 148.327 1.00 121.88 ? 363 VAL A CA    1 
ATOM   2082 C C     . VAL A 1 278 ? 95.957  127.257 149.251 1.00 120.86 ? 363 VAL A C     1 
ATOM   2083 O O     . VAL A 1 278 ? 96.125  128.486 149.218 1.00 116.89 ? 363 VAL A O     1 
ATOM   2084 C CB    . VAL A 1 278 ? 96.272  126.476 146.873 1.00 120.62 ? 363 VAL A CB    1 
ATOM   2085 C CG1   . VAL A 1 278 ? 94.777  126.215 146.803 1.00 120.37 ? 363 VAL A CG1   1 
ATOM   2086 C CG2   . VAL A 1 278 ? 96.626  127.831 146.264 1.00 118.91 ? 363 VAL A CG2   1 
ATOM   2087 N N     . SER A 1 279 ? 95.082  126.680 150.080 1.00 121.65 ? 364 SER A N     1 
ATOM   2088 C CA    . SER A 1 279 ? 94.288  127.490 150.999 1.00 121.04 ? 364 SER A CA    1 
ATOM   2089 C C     . SER A 1 279 ? 95.172  128.206 152.011 1.00 121.40 ? 364 SER A C     1 
ATOM   2090 O O     . SER A 1 279 ? 94.882  129.341 152.408 1.00 120.70 ? 364 SER A O     1 
ATOM   2091 C CB    . SER A 1 279 ? 93.257  126.617 151.714 1.00 121.57 ? 364 SER A CB    1 
ATOM   2092 O OG    . SER A 1 279 ? 93.891  125.626 152.506 1.00 118.17 ? 364 SER A OG    1 
ATOM   2093 N N     . SER A 1 280 ? 96.245  127.559 152.443 1.00 118.94 ? 365 SER A N     1 
ATOM   2094 C CA    . SER A 1 280 ? 97.136  128.139 153.437 1.00 111.79 ? 365 SER A CA    1 
ATOM   2095 C C     . SER A 1 280 ? 97.855  129.355 152.865 1.00 108.70 ? 365 SER A C     1 
ATOM   2096 O O     . SER A 1 280 ? 98.495  129.245 151.808 1.00 108.73 ? 365 SER A O     1 
ATOM   2097 C CB    . SER A 1 280 ? 98.156  127.102 153.901 1.00 103.72 ? 365 SER A CB    1 
ATOM   2098 O OG    . SER A 1 280 ? 97.522  126.004 154.532 1.00 105.96 ? 365 SER A OG    1 
ATOM   2099 N N     . PRO A 1 281 ? 97.781  130.520 153.514 1.00 105.84 ? 366 PRO A N     1 
ATOM   2100 C CA    . PRO A 1 281 ? 98.624  131.653 153.113 1.00 103.17 ? 366 PRO A CA    1 
ATOM   2101 C C     . PRO A 1 281 ? 100.094 131.458 153.442 1.00 99.87  ? 366 PRO A C     1 
ATOM   2102 O O     . PRO A 1 281 ? 100.905 132.340 153.138 1.00 99.12  ? 366 PRO A O     1 
ATOM   2103 C CB    . PRO A 1 281 ? 98.030  132.831 153.911 1.00 100.61 ? 366 PRO A CB    1 
ATOM   2104 C CG    . PRO A 1 281 ? 96.722  132.327 154.471 1.00 99.26  ? 366 PRO A CG    1 
ATOM   2105 C CD    . PRO A 1 281 ? 96.906  130.860 154.644 1.00 103.54 ? 366 PRO A CD    1 
ATOM   2106 N N     . TYR A 1 282 ? 100.446 130.331 154.059 1.00 98.76  ? 367 TYR A N     1 
ATOM   2107 C CA    . TYR A 1 282 ? 101.824 129.980 154.381 1.00 98.39  ? 367 TYR A CA    1 
ATOM   2108 C C     . TYR A 1 282 ? 102.493 129.293 153.192 1.00 94.04  ? 367 TYR A C     1 
ATOM   2109 O O     . TYR A 1 282 ? 103.503 129.776 152.665 1.00 94.36  ? 367 TYR A O     1 
ATOM   2110 C CB    . TYR A 1 282 ? 101.835 129.075 155.618 1.00 98.92  ? 367 TYR A CB    1 
ATOM   2111 C CG    . TYR A 1 282 ? 103.151 129.012 156.351 1.00 102.27 ? 367 TYR A CG    1 
ATOM   2112 C CD1   . TYR A 1 282 ? 103.541 130.033 157.204 1.00 103.29 ? 367 TYR A CD1   1 
ATOM   2113 C CD2   . TYR A 1 282 ? 103.999 127.927 156.198 1.00 101.75 ? 367 TYR A CD2   1 
ATOM   2114 C CE1   . TYR A 1 282 ? 104.741 129.982 157.879 1.00 104.27 ? 367 TYR A CE1   1 
ATOM   2115 C CE2   . TYR A 1 282 ? 105.199 127.866 156.867 1.00 106.02 ? 367 TYR A CE2   1 
ATOM   2116 C CZ    . TYR A 1 282 ? 105.567 128.895 157.708 1.00 109.80 ? 367 TYR A CZ    1 
ATOM   2117 O OH    . TYR A 1 282 ? 106.766 128.837 158.380 1.00 113.31 ? 367 TYR A OH    1 
ATOM   2118 N N     . ILE A 1 283 ? 101.922 128.169 152.752 1.00 91.28  ? 368 ILE A N     1 
ATOM   2119 C CA    . ILE A 1 283 ? 102.378 127.521 151.531 1.00 92.75  ? 368 ILE A CA    1 
ATOM   2120 C C     . ILE A 1 283 ? 102.235 128.455 150.340 1.00 91.81  ? 368 ILE A C     1 
ATOM   2121 O O     . ILE A 1 283 ? 103.009 128.363 149.385 1.00 90.30  ? 368 ILE A O     1 
ATOM   2122 C CB    . ILE A 1 283 ? 101.606 126.204 151.302 1.00 98.51  ? 368 ILE A CB    1 
ATOM   2123 C CG1   . ILE A 1 283 ? 101.685 125.317 152.546 1.00 95.36  ? 368 ILE A CG1   1 
ATOM   2124 C CG2   . ILE A 1 283 ? 102.155 125.461 150.094 1.00 99.08  ? 368 ILE A CG2   1 
ATOM   2125 C CD1   . ILE A 1 283 ? 103.093 124.907 152.916 1.00 98.54  ? 368 ILE A CD1   1 
ATOM   2126 N N     . ARG A 1 284 ? 101.270 129.377 150.386 1.00 95.05  ? 369 ARG A N     1 
ATOM   2127 C CA    . ARG A 1 284 ? 101.101 130.351 149.314 1.00 90.13  ? 369 ARG A CA    1 
ATOM   2128 C C     . ARG A 1 284 ? 102.326 131.241 149.135 1.00 86.71  ? 369 ARG A C     1 
ATOM   2129 O O     . ARG A 1 284 ? 102.536 131.769 148.039 1.00 88.98  ? 369 ARG A O     1 
ATOM   2130 C CB    . ARG A 1 284 ? 99.860  131.202 149.588 1.00 95.44  ? 369 ARG A CB    1 
ATOM   2131 C CG    . ARG A 1 284 ? 99.339  131.974 148.390 1.00 99.75  ? 369 ARG A CG    1 
ATOM   2132 C CD    . ARG A 1 284 ? 97.820  132.013 148.406 1.00 107.41 ? 369 ARG A CD    1 
ATOM   2133 N NE    . ARG A 1 284 ? 97.304  132.738 149.561 1.00 111.10 ? 369 ARG A NE    1 
ATOM   2134 C CZ    . ARG A 1 284 ? 96.723  133.928 149.503 1.00 116.46 ? 369 ARG A CZ    1 
ATOM   2135 N NH1   . ARG A 1 284 ? 96.561  134.563 148.353 1.00 120.55 ? 369 ARG A NH1   1 
ATOM   2136 N NH2   . ARG A 1 284 ? 96.291  134.494 150.626 1.00 112.05 ? 369 ARG A NH2   1 
ATOM   2137 N N     . ASP A 1 285 ? 103.136 131.420 150.180 1.00 85.65  ? 370 ASP A N     1 
ATOM   2138 C CA    . ASP A 1 285 ? 104.385 132.165 150.081 1.00 82.70  ? 370 ASP A CA    1 
ATOM   2139 C C     . ASP A 1 285 ? 105.612 131.276 149.959 1.00 78.10  ? 370 ASP A C     1 
ATOM   2140 O O     . ASP A 1 285 ? 106.577 131.663 149.289 1.00 77.48  ? 370 ASP A O     1 
ATOM   2141 C CB    . ASP A 1 285 ? 104.553 133.090 151.293 1.00 87.15  ? 370 ASP A CB    1 
ATOM   2142 C CG    . ASP A 1 285 ? 103.593 134.263 151.263 1.00 92.12  ? 370 ASP A CG    1 
ATOM   2143 O OD1   . ASP A 1 285 ? 103.223 134.700 150.153 1.00 91.09  ? 370 ASP A OD1   1 
ATOM   2144 O OD2   . ASP A 1 285 ? 103.208 134.747 152.348 1.00 92.65  ? 370 ASP A OD2   1 
ATOM   2145 N N     . LEU A 1 286 ? 105.600 130.096 150.585 1.00 80.04  ? 371 LEU A N     1 
ATOM   2146 C CA    . LEU A 1 286 ? 106.638 129.109 150.296 1.00 77.83  ? 371 LEU A CA    1 
ATOM   2147 C C     . LEU A 1 286 ? 106.725 128.843 148.795 1.00 76.58  ? 371 LEU A C     1 
ATOM   2148 O O     . LEU A 1 286 ? 107.798 128.953 148.190 1.00 76.29  ? 371 LEU A O     1 
ATOM   2149 C CB    . LEU A 1 286 ? 106.382 127.804 151.061 1.00 83.32  ? 371 LEU A CB    1 
ATOM   2150 C CG    . LEU A 1 286 ? 106.819 127.632 152.523 1.00 93.53  ? 371 LEU A CG    1 
ATOM   2151 C CD1   . LEU A 1 286 ? 108.336 127.704 152.621 1.00 91.06  ? 371 LEU A CD1   1 
ATOM   2152 C CD2   . LEU A 1 286 ? 106.191 128.639 153.462 1.00 95.36  ? 371 LEU A CD2   1 
ATOM   2153 N N     . ALA A 1 287 ? 105.586 128.525 148.174 1.00 77.25  ? 372 ALA A N     1 
ATOM   2154 C CA    . ALA A 1 287 ? 105.553 128.299 146.736 1.00 68.44  ? 372 ALA A CA    1 
ATOM   2155 C C     . ALA A 1 287 ? 105.954 129.545 145.963 1.00 66.06  ? 372 ALA A C     1 
ATOM   2156 O O     . ALA A 1 287 ? 106.598 129.440 144.918 1.00 68.39  ? 372 ALA A O     1 
ATOM   2157 C CB    . ALA A 1 287 ? 104.159 127.840 146.306 1.00 70.62  ? 372 ALA A CB    1 
ATOM   2158 N N     . THR A 1 288 ? 105.585 130.730 146.453 1.00 66.20  ? 373 THR A N     1 
ATOM   2159 C CA    . THR A 1 288 ? 105.977 131.955 145.765 1.00 61.65  ? 373 THR A CA    1 
ATOM   2160 C C     . THR A 1 288 ? 107.494 132.073 145.695 1.00 62.43  ? 373 THR A C     1 
ATOM   2161 O O     . THR A 1 288 ? 108.055 132.408 144.646 1.00 63.81  ? 373 THR A O     1 
ATOM   2162 C CB    . THR A 1 288 ? 105.373 133.172 146.466 1.00 64.06  ? 373 THR A CB    1 
ATOM   2163 O OG1   . THR A 1 288 ? 104.011 132.896 146.816 1.00 74.23  ? 373 THR A OG1   1 
ATOM   2164 C CG2   . THR A 1 288 ? 105.413 134.383 145.548 1.00 64.43  ? 373 THR A CG2   1 
ATOM   2165 N N     . LEU A 1 289 ? 108.175 131.783 146.805 1.00 64.97  ? 374 LEU A N     1 
ATOM   2166 C CA    . LEU A 1 289 ? 109.637 131.798 146.796 1.00 58.70  ? 374 LEU A CA    1 
ATOM   2167 C C     . LEU A 1 289 ? 110.202 130.714 145.879 1.00 56.30  ? 374 LEU A C     1 
ATOM   2168 O O     . LEU A 1 289 ? 111.132 130.970 145.099 1.00 57.69  ? 374 LEU A O     1 
ATOM   2169 C CB    . LEU A 1 289 ? 110.175 131.633 148.218 1.00 59.86  ? 374 LEU A CB    1 
ATOM   2170 C CG    . LEU A 1 289 ? 109.759 132.678 149.257 1.00 61.19  ? 374 LEU A CG    1 
ATOM   2171 C CD1   . LEU A 1 289 ? 110.678 132.620 150.468 1.00 66.99  ? 374 LEU A CD1   1 
ATOM   2172 C CD2   . LEU A 1 289 ? 109.755 134.075 148.656 1.00 63.33  ? 374 LEU A CD2   1 
ATOM   2173 N N     . VAL A 1 290 ? 109.653 129.496 145.960 1.00 57.90  ? 375 VAL A N     1 
ATOM   2174 C CA    . VAL A 1 290 ? 110.175 128.383 145.165 1.00 56.42  ? 375 VAL A CA    1 
ATOM   2175 C C     . VAL A 1 290 ? 109.896 128.557 143.673 1.00 56.13  ? 375 VAL A C     1 
ATOM   2176 O O     . VAL A 1 290 ? 110.518 127.879 142.847 1.00 59.06  ? 375 VAL A O     1 
ATOM   2177 C CB    . VAL A 1 290 ? 109.621 127.037 145.680 1.00 61.01  ? 375 VAL A CB    1 
ATOM   2178 C CG1   . VAL A 1 290 ? 110.369 125.866 145.064 1.00 66.00  ? 375 VAL A CG1   1 
ATOM   2179 C CG2   . VAL A 1 290 ? 109.766 126.951 147.184 1.00 67.29  ? 375 VAL A CG2   1 
ATOM   2180 N N     . VAL A 1 291 ? 108.973 129.438 143.299 1.00 56.45  ? 376 VAL A N     1 
ATOM   2181 C CA    . VAL A 1 291 ? 108.771 129.762 141.888 1.00 46.75  ? 376 VAL A CA    1 
ATOM   2182 C C     . VAL A 1 291 ? 109.615 130.957 141.458 1.00 48.03  ? 376 VAL A C     1 
ATOM   2183 O O     . VAL A 1 291 ? 110.163 130.961 140.350 1.00 55.86  ? 376 VAL A O     1 
ATOM   2184 C CB    . VAL A 1 291 ? 107.274 129.992 141.593 1.00 49.31  ? 376 VAL A CB    1 
ATOM   2185 C CG1   . VAL A 1 291 ? 107.056 130.209 140.111 1.00 51.03  ? 376 VAL A CG1   1 
ATOM   2186 C CG2   . VAL A 1 291 ? 106.471 128.777 142.011 1.00 54.45  ? 376 VAL A CG2   1 
ATOM   2187 N N     . ALA A 1 292 ? 109.719 131.987 142.305 1.00 50.10  ? 377 ALA A N     1 
ATOM   2188 C CA    . ALA A 1 292 ? 110.553 133.139 141.974 1.00 48.31  ? 377 ALA A CA    1 
ATOM   2189 C C     . ALA A 1 292 ? 111.992 132.708 141.736 1.00 51.84  ? 377 ALA A C     1 
ATOM   2190 O O     . ALA A 1 292 ? 112.618 133.093 140.732 1.00 57.43  ? 377 ALA A O     1 
ATOM   2191 C CB    . ALA A 1 292 ? 110.472 134.182 143.088 1.00 53.66  ? 377 ALA A CB    1 
ATOM   2192 N N     . TYR A 1 293 ? 112.540 131.904 142.649 1.00 52.80  ? 378 TYR A N     1 
ATOM   2193 C CA    . TYR A 1 293 ? 113.730 131.151 142.297 1.00 49.02  ? 378 TYR A CA    1 
ATOM   2194 C C     . TYR A 1 293 ? 113.299 130.040 141.358 1.00 49.42  ? 378 TYR A C     1 
ATOM   2195 O O     . TYR A 1 293 ? 112.413 129.246 141.684 1.00 57.82  ? 378 TYR A O     1 
ATOM   2196 C CB    . TYR A 1 293 ? 114.439 130.568 143.516 1.00 49.88  ? 378 TYR A CB    1 
ATOM   2197 C CG    . TYR A 1 293 ? 115.664 129.771 143.109 1.00 43.00  ? 378 TYR A CG    1 
ATOM   2198 C CD1   . TYR A 1 293 ? 115.565 128.433 142.741 1.00 40.87  ? 378 TYR A CD1   1 
ATOM   2199 C CD2   . TYR A 1 293 ? 116.914 130.372 143.053 1.00 46.52  ? 378 TYR A CD2   1 
ATOM   2200 C CE1   . TYR A 1 293 ? 116.675 127.720 142.343 1.00 42.01  ? 378 TYR A CE1   1 
ATOM   2201 C CE2   . TYR A 1 293 ? 118.033 129.662 142.664 1.00 46.25  ? 378 TYR A CE2   1 
ATOM   2202 C CZ    . TYR A 1 293 ? 117.908 128.337 142.310 1.00 46.79  ? 378 TYR A CZ    1 
ATOM   2203 O OH    . TYR A 1 293 ? 119.019 127.623 141.923 1.00 49.61  ? 378 TYR A OH    1 
ATOM   2204 N N     . GLY A 1 294 ? 113.922 129.984 140.199 1.00 42.22  ? 379 GLY A N     1 
ATOM   2205 C CA    . GLY A 1 294 ? 113.518 129.067 139.163 1.00 44.35  ? 379 GLY A CA    1 
ATOM   2206 C C     . GLY A 1 294 ? 113.059 129.877 137.978 1.00 49.46  ? 379 GLY A C     1 
ATOM   2207 O O     . GLY A 1 294 ? 113.624 129.723 136.895 1.00 59.27  ? 379 GLY A O     1 
ATOM   2208 N N     . ILE A 1 295 ? 112.180 130.860 138.197 1.00 43.76  ? 380 ILE A N     1 
ATOM   2209 C CA    . ILE A 1 295 ? 111.911 131.830 137.140 1.00 40.31  ? 380 ILE A CA    1 
ATOM   2210 C C     . ILE A 1 295 ? 113.164 132.645 136.861 1.00 45.13  ? 380 ILE A C     1 
ATOM   2211 O O     . ILE A 1 295 ? 113.642 132.720 135.721 1.00 53.00  ? 380 ILE A O     1 
ATOM   2212 C CB    . ILE A 1 295 ? 110.726 132.739 137.516 1.00 43.45  ? 380 ILE A CB    1 
ATOM   2213 C CG1   . ILE A 1 295 ? 109.412 131.957 137.521 1.00 42.65  ? 380 ILE A CG1   1 
ATOM   2214 C CG2   . ILE A 1 295 ? 110.642 133.920 136.561 1.00 44.32  ? 380 ILE A CG2   1 
ATOM   2215 C CD1   . ILE A 1 295 ? 108.190 132.825 137.737 1.00 41.16  ? 380 ILE A CD1   1 
ATOM   2216 N N     . SER A 1 296 ? 113.742 133.229 137.913 1.00 46.35  ? 381 SER A N     1 
ATOM   2217 C CA    . SER A 1 296 ? 114.932 134.052 137.721 1.00 44.58  ? 381 SER A CA    1 
ATOM   2218 C C     . SER A 1 296 ? 116.123 133.212 137.265 1.00 43.92  ? 381 SER A C     1 
ATOM   2219 O O     . SER A 1 296 ? 116.866 133.605 136.346 1.00 51.25  ? 381 SER A O     1 
ATOM   2220 C CB    . SER A 1 296 ? 115.244 134.796 139.015 1.00 52.18  ? 381 SER A CB    1 
ATOM   2221 O OG    . SER A 1 296 ? 114.186 135.668 139.373 1.00 56.61  ? 381 SER A OG    1 
ATOM   2222 N N     . ILE A 1 297 ? 116.310 132.043 137.887 1.00 45.65  ? 382 ILE A N     1 
ATOM   2223 C CA    . ILE A 1 297 ? 117.449 131.211 137.527 1.00 45.69  ? 382 ILE A CA    1 
ATOM   2224 C C     . ILE A 1 297 ? 117.332 130.752 136.081 1.00 50.54  ? 382 ILE A C     1 
ATOM   2225 O O     . ILE A 1 297 ? 118.334 130.732 135.368 1.00 52.35  ? 382 ILE A O     1 
ATOM   2226 C CB    . ILE A 1 297 ? 117.621 130.029 138.507 1.00 41.68  ? 382 ILE A CB    1 
ATOM   2227 C CG1   . ILE A 1 297 ? 119.088 129.600 138.565 1.00 47.86  ? 382 ILE A CG1   1 
ATOM   2228 C CG2   . ILE A 1 297 ? 116.794 128.824 138.102 1.00 43.60  ? 382 ILE A CG2   1 
ATOM   2229 C CD1   . ILE A 1 297 ? 120.035 130.696 138.997 1.00 44.49  ? 382 ILE A CD1   1 
ATOM   2230 N N     . ASN A 1 298 ? 116.123 130.419 135.608 1.00 49.48  ? 383 ASN A N     1 
ATOM   2231 C CA    . ASN A 1 298 ? 115.932 130.067 134.206 1.00 44.64  ? 383 ASN A CA    1 
ATOM   2232 C C     . ASN A 1 298 ? 116.255 131.245 133.299 1.00 50.44  ? 383 ASN A C     1 
ATOM   2233 O O     . ASN A 1 298 ? 117.000 131.101 132.315 1.00 55.96  ? 383 ASN A O     1 
ATOM   2234 C CB    . ASN A 1 298 ? 114.490 129.603 133.995 1.00 47.99  ? 383 ASN A CB    1 
ATOM   2235 C CG    . ASN A 1 298 ? 114.350 128.639 132.844 1.00 56.64  ? 383 ASN A CG    1 
ATOM   2236 O OD1   . ASN A 1 298 ? 114.839 128.892 131.749 1.00 56.64  ? 383 ASN A OD1   1 
ATOM   2237 N ND2   . ASN A 1 298 ? 113.676 127.525 133.085 1.00 58.42  ? 383 ASN A ND2   1 
ATOM   2238 N N     . LEU A 1 299 ? 115.720 132.426 133.641 1.00 48.22  ? 384 LEU A N     1 
ATOM   2239 C CA    . LEU A 1 299 ? 115.925 133.620 132.829 1.00 46.63  ? 384 LEU A CA    1 
ATOM   2240 C C     . LEU A 1 299 ? 117.405 133.887 132.606 1.00 51.69  ? 384 LEU A C     1 
ATOM   2241 O O     . LEU A 1 299 ? 117.804 134.369 131.540 1.00 58.44  ? 384 LEU A O     1 
ATOM   2242 C CB    . LEU A 1 299 ? 115.268 134.829 133.500 1.00 43.68  ? 384 LEU A CB    1 
ATOM   2243 C CG    . LEU A 1 299 ? 113.740 134.925 133.521 1.00 48.22  ? 384 LEU A CG    1 
ATOM   2244 C CD1   . LEU A 1 299 ? 113.289 135.946 134.558 1.00 49.77  ? 384 LEU A CD1   1 
ATOM   2245 C CD2   . LEU A 1 299 ? 113.175 135.264 132.154 1.00 47.54  ? 384 LEU A CD2   1 
ATOM   2246 N N     . VAL A 1 300 ? 118.236 133.582 133.599 1.00 51.76  ? 385 VAL A N     1 
ATOM   2247 C CA    . VAL A 1 300 ? 119.674 133.787 133.413 1.00 45.88  ? 385 VAL A CA    1 
ATOM   2248 C C     . VAL A 1 300 ? 120.347 132.578 132.755 1.00 49.49  ? 385 VAL A C     1 
ATOM   2249 O O     . VAL A 1 300 ? 121.169 132.731 131.841 1.00 55.38  ? 385 VAL A O     1 
ATOM   2250 C CB    . VAL A 1 300 ? 120.338 134.136 134.759 1.00 47.29  ? 385 VAL A CB    1 
ATOM   2251 C CG1   . VAL A 1 300 ? 121.787 134.533 134.539 1.00 49.99  ? 385 VAL A CG1   1 
ATOM   2252 C CG2   . VAL A 1 300 ? 119.575 135.256 135.450 1.00 46.31  ? 385 VAL A CG2   1 
ATOM   2253 N N     . GLU A 1 301 ? 120.012 131.359 133.184 1.00 53.22  ? 386 GLU A N     1 
ATOM   2254 C CA    . GLU A 1 301 ? 120.805 130.196 132.814 1.00 53.12  ? 386 GLU A CA    1 
ATOM   2255 C C     . GLU A 1 301 ? 120.550 129.723 131.393 1.00 49.19  ? 386 GLU A C     1 
ATOM   2256 O O     . GLU A 1 301 ? 121.446 129.120 130.802 1.00 56.08  ? 386 GLU A O     1 
ATOM   2257 C CB    . GLU A 1 301 ? 120.554 129.031 133.777 1.00 54.26  ? 386 GLU A CB    1 
ATOM   2258 C CG    . GLU A 1 301 ? 119.149 128.463 133.743 1.00 59.67  ? 386 GLU A CG    1 
ATOM   2259 C CD    . GLU A 1 301 ? 118.946 127.361 134.761 1.00 63.54  ? 386 GLU A CD    1 
ATOM   2260 O OE1   . GLU A 1 301 ? 119.901 127.058 135.508 1.00 60.70  ? 386 GLU A OE1   1 
ATOM   2261 O OE2   . GLU A 1 301 ? 117.828 126.811 134.826 1.00 62.43  ? 386 GLU A OE2   1 
ATOM   2262 N N     . VAL A 1 302 ? 119.364 129.958 130.822 1.00 47.40  ? 387 VAL A N     1 
ATOM   2263 C CA    . VAL A 1 302 ? 119.184 129.565 129.425 1.00 47.87  ? 387 VAL A CA    1 
ATOM   2264 C C     . VAL A 1 302 ? 120.091 130.392 128.518 1.00 48.20  ? 387 VAL A C     1 
ATOM   2265 O O     . VAL A 1 302 ? 120.727 129.861 127.597 1.00 49.35  ? 387 VAL A O     1 
ATOM   2266 C CB    . VAL A 1 302 ? 117.705 129.660 129.013 1.00 49.27  ? 387 VAL A CB    1 
ATOM   2267 C CG1   . VAL A 1 302 ? 117.574 129.623 127.505 1.00 46.22  ? 387 VAL A CG1   1 
ATOM   2268 C CG2   . VAL A 1 302 ? 116.943 128.501 129.605 1.00 49.25  ? 387 VAL A CG2   1 
ATOM   2269 N N     . THR A 1 303 ? 120.187 131.697 128.778 1.00 50.06  ? 388 THR A N     1 
ATOM   2270 C CA    . THR A 1 303 ? 121.134 132.529 128.041 1.00 46.67  ? 388 THR A CA    1 
ATOM   2271 C C     . THR A 1 303 ? 122.572 132.096 128.310 1.00 46.07  ? 388 THR A C     1 
ATOM   2272 O O     . THR A 1 303 ? 123.404 132.061 127.388 1.00 49.68  ? 388 THR A O     1 
ATOM   2273 C CB    . THR A 1 303 ? 120.933 133.998 128.410 1.00 50.59  ? 388 THR A CB    1 
ATOM   2274 O OG1   . THR A 1 303 ? 119.584 134.383 128.119 1.00 54.09  ? 388 THR A OG1   1 
ATOM   2275 C CG2   . THR A 1 303 ? 121.878 134.880 127.615 1.00 51.66  ? 388 THR A CG2   1 
ATOM   2276 N N     . TRP A 1 304 ? 122.884 131.754 129.566 1.00 46.77  ? 389 TRP A N     1 
ATOM   2277 C CA    . TRP A 1 304 ? 124.237 131.293 129.873 1.00 43.80  ? 389 TRP A CA    1 
ATOM   2278 C C     . TRP A 1 304 ? 124.570 130.037 129.078 1.00 46.09  ? 389 TRP A C     1 
ATOM   2279 O O     . TRP A 1 304 ? 125.687 129.883 128.575 1.00 52.47  ? 389 TRP A O     1 
ATOM   2280 C CB    . TRP A 1 304 ? 124.382 130.990 131.359 1.00 42.67  ? 389 TRP A CB    1 
ATOM   2281 C CG    . TRP A 1 304 ? 125.703 130.353 131.689 1.00 41.62  ? 389 TRP A CG    1 
ATOM   2282 C CD1   . TRP A 1 304 ? 126.938 130.867 131.423 1.00 38.61  ? 389 TRP A CD1   1 
ATOM   2283 C CD2   . TRP A 1 304 ? 125.927 129.054 132.253 1.00 41.27  ? 389 TRP A CD2   1 
ATOM   2284 N NE1   . TRP A 1 304 ? 127.915 130.001 131.841 1.00 37.39  ? 389 TRP A NE1   1 
ATOM   2285 C CE2   . TRP A 1 304 ? 127.321 128.875 132.346 1.00 38.35  ? 389 TRP A CE2   1 
ATOM   2286 C CE3   . TRP A 1 304 ? 125.087 128.026 132.686 1.00 40.44  ? 389 TRP A CE3   1 
ATOM   2287 C CZ2   . TRP A 1 304 ? 127.892 127.721 132.876 1.00 42.48  ? 389 TRP A CZ2   1 
ATOM   2288 C CZ3   . TRP A 1 304 ? 125.655 126.889 133.231 1.00 40.78  ? 389 TRP A CZ3   1 
ATOM   2289 C CH2   . TRP A 1 304 ? 127.043 126.742 133.313 1.00 47.01  ? 389 TRP A CH2   1 
ATOM   2290 N N     . LYS A 1 305 ? 123.607 129.122 128.963 1.00 43.99  ? 390 LYS A N     1 
ATOM   2291 C CA    . LYS A 1 305 ? 123.832 127.870 128.253 1.00 44.50  ? 390 LYS A CA    1 
ATOM   2292 C C     . LYS A 1 305 ? 123.894 128.087 126.748 1.00 47.77  ? 390 LYS A C     1 
ATOM   2293 O O     . LYS A 1 305 ? 124.564 127.327 126.041 1.00 50.34  ? 390 LYS A O     1 
ATOM   2294 C CB    . LYS A 1 305 ? 122.736 126.869 128.617 1.00 49.22  ? 390 LYS A CB    1 
ATOM   2295 C CG    . LYS A 1 305 ? 122.875 126.304 130.026 1.00 52.56  ? 390 LYS A CG    1 
ATOM   2296 C CD    . LYS A 1 305 ? 121.611 125.587 130.468 1.00 59.04  ? 390 LYS A CD    1 
ATOM   2297 C CE    . LYS A 1 305 ? 121.844 124.766 131.725 1.00 55.36  ? 390 LYS A CE    1 
ATOM   2298 N NZ    . LYS A 1 305 ? 122.048 125.629 132.921 1.00 54.52  ? 390 LYS A NZ    1 
ATOM   2299 N N     . SER A 1 306 ? 123.209 129.113 126.239 1.00 52.27  ? 391 SER A N     1 
ATOM   2300 C CA    . SER A 1 306 ? 123.416 129.508 124.848 1.00 47.03  ? 391 SER A CA    1 
ATOM   2301 C C     . SER A 1 306 ? 124.857 129.950 124.627 1.00 44.81  ? 391 SER A C     1 
ATOM   2302 O O     . SER A 1 306 ? 125.505 129.552 123.648 1.00 46.96  ? 391 SER A O     1 
ATOM   2303 C CB    . SER A 1 306 ? 122.441 130.621 124.465 1.00 49.89  ? 391 SER A CB    1 
ATOM   2304 O OG    . SER A 1 306 ? 122.733 131.819 125.162 1.00 52.17  ? 391 SER A OG    1 
ATOM   2305 N N     . LYS A 1 307 ? 125.382 130.762 125.548 1.00 48.00  ? 392 LYS A N     1 
ATOM   2306 C CA    . LYS A 1 307 ? 126.799 131.118 125.490 1.00 46.94  ? 392 LYS A CA    1 
ATOM   2307 C C     . LYS A 1 307 ? 127.681 129.876 125.579 1.00 48.56  ? 392 LYS A C     1 
ATOM   2308 O O     . LYS A 1 307 ? 128.716 129.788 124.907 1.00 52.75  ? 392 LYS A O     1 
ATOM   2309 C CB    . LYS A 1 307 ? 127.144 132.102 126.607 1.00 50.13  ? 392 LYS A CB    1 
ATOM   2310 C CG    . LYS A 1 307 ? 126.277 133.347 126.631 1.00 48.23  ? 392 LYS A CG    1 
ATOM   2311 C CD    . LYS A 1 307 ? 126.486 134.181 125.379 1.00 45.46  ? 392 LYS A CD    1 
ATOM   2312 C CE    . LYS A 1 307 ? 125.543 135.371 125.344 1.00 52.94  ? 392 LYS A CE    1 
ATOM   2313 N NZ    . LYS A 1 307 ? 125.875 136.304 124.233 1.00 60.97  ? 392 LYS A NZ    1 
ATOM   2314 N N     . LEU A 1 308 ? 127.286 128.913 126.412 1.00 50.49  ? 393 LEU A N     1 
ATOM   2315 C CA    . LEU A 1 308 ? 128.048 127.675 126.559 1.00 47.05  ? 393 LEU A CA    1 
ATOM   2316 C C     . LEU A 1 308 ? 128.120 126.914 125.242 1.00 43.52  ? 393 LEU A C     1 
ATOM   2317 O O     . LEU A 1 308 ? 129.194 126.459 124.830 1.00 51.28  ? 393 LEU A O     1 
ATOM   2318 C CB    . LEU A 1 308 ? 127.412 126.794 127.631 1.00 48.63  ? 393 LEU A CB    1 
ATOM   2319 C CG    . LEU A 1 308 ? 127.559 127.195 129.093 1.00 40.38  ? 393 LEU A CG    1 
ATOM   2320 C CD1   . LEU A 1 308 ? 127.170 126.018 129.967 1.00 39.58  ? 393 LEU A CD1   1 
ATOM   2321 C CD2   . LEU A 1 308 ? 128.970 127.653 129.374 1.00 39.63  ? 393 LEU A CD2   1 
ATOM   2322 N N     . LYS A 1 309 ? 126.975 126.752 124.577 1.00 46.28  ? 394 LYS A N     1 
ATOM   2323 C CA    . LYS A 1 309 ? 126.956 126.072 123.287 1.00 47.67  ? 394 LYS A CA    1 
ATOM   2324 C C     . LYS A 1 309 ? 127.792 126.824 122.264 1.00 45.49  ? 394 LYS A C     1 
ATOM   2325 O O     . LYS A 1 309 ? 128.468 126.209 121.431 1.00 49.35  ? 394 LYS A O     1 
ATOM   2326 C CB    . LYS A 1 309 ? 125.525 125.916 122.781 1.00 47.23  ? 394 LYS A CB    1 
ATOM   2327 C CG    . LYS A 1 309 ? 125.395 124.865 121.693 1.00 52.05  ? 394 LYS A CG    1 
ATOM   2328 C CD    . LYS A 1 309 ? 124.290 125.207 120.713 1.00 52.68  ? 394 LYS A CD    1 
ATOM   2329 C CE    . LYS A 1 309 ? 124.239 124.193 119.584 1.00 53.73  ? 394 LYS A CE    1 
ATOM   2330 N NZ    . LYS A 1 309 ? 125.589 123.927 119.016 1.00 57.05  ? 394 LYS A NZ    1 
ATOM   2331 N N     . ALA A 1 310 ? 127.751 128.157 122.305 1.00 48.14  ? 395 ALA A N     1 
ATOM   2332 C CA    . ALA A 1 310 ? 128.598 128.936 121.410 1.00 44.30  ? 395 ALA A CA    1 
ATOM   2333 C C     . ALA A 1 310 ? 130.078 128.697 121.689 1.00 47.77  ? 395 ALA A C     1 
ATOM   2334 O O     . ALA A 1 310 ? 130.889 128.682 120.756 1.00 53.68  ? 395 ALA A O     1 
ATOM   2335 C CB    . ALA A 1 310 ? 128.263 130.421 121.529 1.00 45.01  ? 395 ALA A CB    1 
ATOM   2336 N N     . GLN A 1 311 ? 130.448 128.502 122.956 1.00 52.08  ? 396 GLN A N     1 
ATOM   2337 C CA    . GLN A 1 311 ? 131.852 128.336 123.318 1.00 47.68  ? 396 GLN A CA    1 
ATOM   2338 C C     . GLN A 1 311 ? 132.326 126.891 123.204 1.00 49.26  ? 396 GLN A C     1 
ATOM   2339 O O     . GLN A 1 311 ? 133.422 126.642 122.689 1.00 52.62  ? 396 GLN A O     1 
ATOM   2340 C CB    . GLN A 1 311 ? 132.092 128.853 124.738 1.00 43.92  ? 396 GLN A CB    1 
ATOM   2341 C CG    . GLN A 1 311 ? 133.410 128.414 125.353 1.00 47.17  ? 396 GLN A CG    1 
ATOM   2342 C CD    . GLN A 1 311 ? 134.613 128.995 124.638 1.00 51.91  ? 396 GLN A CD    1 
ATOM   2343 O OE1   . GLN A 1 311 ? 134.803 130.211 124.605 1.00 57.18  ? 396 GLN A OE1   1 
ATOM   2344 N NE2   . GLN A 1 311 ? 135.436 128.126 124.063 1.00 52.98  ? 396 GLN A NE2   1 
ATOM   2345 N N     . PHE A 1 312 ? 131.527 125.926 123.666 1.00 53.01  ? 397 PHE A N     1 
ATOM   2346 C CA    . PHE A 1 312 ? 131.870 124.506 123.592 1.00 50.79  ? 397 PHE A CA    1 
ATOM   2347 C C     . PHE A 1 312 ? 130.864 123.816 122.680 1.00 56.82  ? 397 PHE A C     1 
ATOM   2348 O O     . PHE A 1 312 ? 129.809 123.351 123.141 1.00 59.72  ? 397 PHE A O     1 
ATOM   2349 C CB    . PHE A 1 312 ? 131.883 123.858 124.976 1.00 48.32  ? 397 PHE A CB    1 
ATOM   2350 C CG    . PHE A 1 312 ? 132.578 124.676 126.029 1.00 49.72  ? 397 PHE A CG    1 
ATOM   2351 C CD1   . PHE A 1 312 ? 133.954 124.617 126.176 1.00 48.86  ? 397 PHE A CD1   1 
ATOM   2352 C CD2   . PHE A 1 312 ? 131.852 125.485 126.888 1.00 47.80  ? 397 PHE A CD2   1 
ATOM   2353 C CE1   . PHE A 1 312 ? 134.594 125.362 127.147 1.00 46.19  ? 397 PHE A CE1   1 
ATOM   2354 C CE2   . PHE A 1 312 ? 132.487 126.231 127.863 1.00 46.60  ? 397 PHE A CE2   1 
ATOM   2355 C CZ    . PHE A 1 312 ? 133.861 126.170 127.990 1.00 46.51  ? 397 PHE A CZ    1 
ATOM   2356 N N     . PRO A 1 313 ? 131.150 123.718 121.377 1.00 59.11  ? 398 PRO A N     1 
ATOM   2357 C CA    . PRO A 1 313 ? 130.182 123.099 120.459 1.00 62.06  ? 398 PRO A CA    1 
ATOM   2358 C C     . PRO A 1 313 ? 130.186 121.580 120.476 1.00 67.32  ? 398 PRO A C     1 
ATOM   2359 O O     . PRO A 1 313 ? 129.147 120.978 120.173 1.00 68.23  ? 398 PRO A O     1 
ATOM   2360 C CB    . PRO A 1 313 ? 130.619 123.637 119.092 1.00 60.70  ? 398 PRO A CB    1 
ATOM   2361 C CG    . PRO A 1 313 ? 132.097 123.798 119.234 1.00 58.64  ? 398 PRO A CG    1 
ATOM   2362 C CD    . PRO A 1 313 ? 132.345 124.214 120.669 1.00 56.67  ? 398 PRO A CD    1 
ATOM   2363 N N     . SER A 1 314 ? 131.314 120.939 120.806 1.00 63.76  ? 399 SER A N     1 
ATOM   2364 C CA    . SER A 1 314 ? 131.300 119.485 120.847 1.00 59.49  ? 399 SER A CA    1 
ATOM   2365 C C     . SER A 1 314 ? 130.725 118.994 122.172 1.00 62.80  ? 399 SER A C     1 
ATOM   2366 O O     . SER A 1 314 ? 130.842 119.674 123.197 1.00 65.16  ? 399 SER A O     1 
ATOM   2367 C CB    . SER A 1 314 ? 132.712 118.935 120.664 1.00 67.76  ? 399 SER A CB    1 
ATOM   2368 O OG    . SER A 1 314 ? 132.749 117.530 120.844 1.00 73.89  ? 399 SER A OG    1 
ATOM   2369 N N     . PRO A 1 315 ? 130.083 117.821 122.176 1.00 62.18  ? 400 PRO A N     1 
ATOM   2370 C CA    . PRO A 1 315 ? 129.577 117.281 123.449 1.00 60.58  ? 400 PRO A CA    1 
ATOM   2371 C C     . PRO A 1 315 ? 130.662 117.067 124.489 1.00 58.75  ? 400 PRO A C     1 
ATOM   2372 O O     . PRO A 1 315 ? 130.404 117.226 125.686 1.00 61.20  ? 400 PRO A O     1 
ATOM   2373 C CB    . PRO A 1 315 ? 128.923 115.959 123.026 1.00 57.67  ? 400 PRO A CB    1 
ATOM   2374 C CG    . PRO A 1 315 ? 128.546 116.171 121.601 1.00 56.38  ? 400 PRO A CG    1 
ATOM   2375 C CD    . PRO A 1 315 ? 129.643 117.017 121.022 1.00 59.51  ? 400 PRO A CD    1 
ATOM   2376 N N     . ASN A 1 316 ? 131.877 116.715 124.067 1.00 57.61  ? 401 ASN A N     1 
ATOM   2377 C CA    . ASN A 1 316 ? 132.924 116.415 125.039 1.00 58.93  ? 401 ASN A CA    1 
ATOM   2378 C C     . ASN A 1 316 ? 133.492 117.682 125.667 1.00 60.62  ? 401 ASN A C     1 
ATOM   2379 O O     . ASN A 1 316 ? 133.779 117.704 126.869 1.00 64.77  ? 401 ASN A O     1 
ATOM   2380 C CB    . ASN A 1 316 ? 134.019 115.584 124.382 1.00 66.86  ? 401 ASN A CB    1 
ATOM   2381 C CG    . ASN A 1 316 ? 133.536 114.200 124.011 1.00 74.36  ? 401 ASN A CG    1 
ATOM   2382 O OD1   . ASN A 1 316 ? 133.030 113.979 122.910 1.00 77.64  ? 401 ASN A OD1   1 
ATOM   2383 N ND2   . ASN A 1 316 ? 133.683 113.256 124.934 1.00 72.04  ? 401 ASN A ND2   1 
ATOM   2384 N N     . GLU A 1 317 ? 133.661 118.749 124.881 1.00 58.46  ? 402 GLU A N     1 
ATOM   2385 C CA    . GLU A 1 317 ? 134.064 120.026 125.462 1.00 56.24  ? 402 GLU A CA    1 
ATOM   2386 C C     . GLU A 1 317 ? 133.020 120.514 126.456 1.00 53.74  ? 402 GLU A C     1 
ATOM   2387 O O     . GLU A 1 317 ? 133.349 120.950 127.568 1.00 54.23  ? 402 GLU A O     1 
ATOM   2388 C CB    . GLU A 1 317 ? 134.275 121.069 124.364 1.00 62.81  ? 402 GLU A CB    1 
ATOM   2389 C CG    . GLU A 1 317 ? 135.446 120.809 123.434 1.00 69.05  ? 402 GLU A CG    1 
ATOM   2390 C CD    . GLU A 1 317 ? 135.571 121.879 122.366 1.00 79.93  ? 402 GLU A CD    1 
ATOM   2391 O OE1   . GLU A 1 317 ? 134.674 122.743 122.280 1.00 75.92  ? 402 GLU A OE1   1 
ATOM   2392 O OE2   . GLU A 1 317 ? 136.566 121.854 121.612 1.00 90.33  ? 402 GLU A OE2   1 
ATOM   2393 N N     . TYR A 1 318 ? 131.745 120.430 126.070 1.00 52.54  ? 403 TYR A N     1 
ATOM   2394 C CA    . TYR A 1 318 ? 130.663 120.865 126.943 1.00 52.09  ? 403 TYR A CA    1 
ATOM   2395 C C     . TYR A 1 318 ? 130.627 120.033 128.218 1.00 53.16  ? 403 TYR A C     1 
ATOM   2396 O O     . TYR A 1 318 ? 130.430 120.570 129.311 1.00 57.46  ? 403 TYR A O     1 
ATOM   2397 C CB    . TYR A 1 318 ? 129.334 120.776 126.190 1.00 51.48  ? 403 TYR A CB    1 
ATOM   2398 C CG    . TYR A 1 318 ? 128.201 121.601 126.764 1.00 54.23  ? 403 TYR A CG    1 
ATOM   2399 C CD1   . TYR A 1 318 ? 127.520 121.195 127.902 1.00 52.54  ? 403 TYR A CD1   1 
ATOM   2400 C CD2   . TYR A 1 318 ? 127.801 122.782 126.152 1.00 48.97  ? 403 TYR A CD2   1 
ATOM   2401 C CE1   . TYR A 1 318 ? 126.480 121.943 128.420 1.00 47.26  ? 403 TYR A CE1   1 
ATOM   2402 C CE2   . TYR A 1 318 ? 126.762 123.535 126.659 1.00 46.97  ? 403 TYR A CE2   1 
ATOM   2403 C CZ    . TYR A 1 318 ? 126.105 123.113 127.795 1.00 46.53  ? 403 TYR A CZ    1 
ATOM   2404 O OH    . TYR A 1 318 ? 125.071 123.862 128.306 1.00 58.11  ? 403 TYR A OH    1 
ATOM   2405 N N     . SER A 1 319 ? 130.843 118.721 128.101 1.00 53.89  ? 404 SER A N     1 
ATOM   2406 C CA    . SER A 1 319 ? 130.810 117.843 129.266 1.00 49.48  ? 404 SER A CA    1 
ATOM   2407 C C     . SER A 1 319 ? 132.000 118.072 130.190 1.00 51.48  ? 404 SER A C     1 
ATOM   2408 O O     . SER A 1 319 ? 131.849 118.038 131.415 1.00 57.41  ? 404 SER A O     1 
ATOM   2409 C CB    . SER A 1 319 ? 130.761 116.383 128.820 1.00 56.54  ? 404 SER A CB    1 
ATOM   2410 O OG    . SER A 1 319 ? 130.760 115.510 129.935 1.00 67.49  ? 404 SER A OG    1 
ATOM   2411 N N     . ALA A 1 320 ? 133.192 118.290 129.629 1.00 50.06  ? 405 ALA A N     1 
ATOM   2412 C CA    . ALA A 1 320 ? 134.344 118.611 130.464 1.00 48.71  ? 405 ALA A CA    1 
ATOM   2413 C C     . ALA A 1 320 ? 134.131 119.927 131.200 1.00 50.71  ? 405 ALA A C     1 
ATOM   2414 O O     . ALA A 1 320 ? 134.445 120.043 132.394 1.00 55.21  ? 405 ALA A O     1 
ATOM   2415 C CB    . ALA A 1 320 ? 135.613 118.665 129.613 1.00 52.99  ? 405 ALA A CB    1 
ATOM   2416 N N     . PHE A 1 321 ? 133.586 120.931 130.505 1.00 50.05  ? 406 PHE A N     1 
ATOM   2417 C CA    . PHE A 1 321 ? 133.279 122.186 131.180 1.00 45.81  ? 406 PHE A CA    1 
ATOM   2418 C C     . PHE A 1 321 ? 132.220 121.991 132.255 1.00 49.40  ? 406 PHE A C     1 
ATOM   2419 O O     . PHE A 1 321 ? 132.291 122.620 133.313 1.00 50.21  ? 406 PHE A O     1 
ATOM   2420 C CB    . PHE A 1 321 ? 132.821 123.250 130.186 1.00 41.85  ? 406 PHE A CB    1 
ATOM   2421 C CG    . PHE A 1 321 ? 132.410 124.534 130.847 1.00 44.72  ? 406 PHE A CG    1 
ATOM   2422 C CD1   . PHE A 1 321 ? 133.359 125.472 131.217 1.00 41.67  ? 406 PHE A CD1   1 
ATOM   2423 C CD2   . PHE A 1 321 ? 131.078 124.790 131.127 1.00 47.68  ? 406 PHE A CD2   1 
ATOM   2424 C CE1   . PHE A 1 321 ? 132.985 126.649 131.836 1.00 39.80  ? 406 PHE A CE1   1 
ATOM   2425 C CE2   . PHE A 1 321 ? 130.701 125.961 131.752 1.00 41.96  ? 406 PHE A CE2   1 
ATOM   2426 C CZ    . PHE A 1 321 ? 131.654 126.893 132.103 1.00 40.86  ? 406 PHE A CZ    1 
ATOM   2427 N N     . MET A 1 322 ? 131.216 121.151 131.997 1.00 50.49  ? 407 MET A N     1 
ATOM   2428 C CA    . MET A 1 322 ? 130.192 120.910 133.007 1.00 47.39  ? 407 MET A CA    1 
ATOM   2429 C C     . MET A 1 322 ? 130.764 120.183 134.216 1.00 51.57  ? 407 MET A C     1 
ATOM   2430 O O     . MET A 1 322 ? 130.334 120.438 135.342 1.00 58.11  ? 407 MET A O     1 
ATOM   2431 C CB    . MET A 1 322 ? 129.021 120.126 132.412 1.00 47.59  ? 407 MET A CB    1 
ATOM   2432 C CG    . MET A 1 322 ? 128.185 120.922 131.418 1.00 47.59  ? 407 MET A CG    1 
ATOM   2433 S SD    . MET A 1 322 ? 127.518 122.451 132.106 1.00 58.75  ? 407 MET A SD    1 
ATOM   2434 C CE    . MET A 1 322 ? 126.450 121.812 133.394 1.00 53.54  ? 407 MET A CE    1 
ATOM   2435 N N     . GLY A 1 323 ? 131.732 119.289 134.009 1.00 49.48  ? 408 GLY A N     1 
ATOM   2436 C CA    . GLY A 1 323 ? 132.398 118.664 135.143 1.00 48.41  ? 408 GLY A CA    1 
ATOM   2437 C C     . GLY A 1 323 ? 133.195 119.662 135.966 1.00 48.63  ? 408 GLY A C     1 
ATOM   2438 O O     . GLY A 1 323 ? 133.135 119.661 137.202 1.00 52.25  ? 408 GLY A O     1 
ATOM   2439 N N     . ASP A 1 324 ? 133.950 120.533 135.289 1.00 50.73  ? 409 ASP A N     1 
ATOM   2440 C CA    . ASP A 1 324 ? 134.660 121.600 135.994 1.00 52.33  ? 409 ASP A CA    1 
ATOM   2441 C C     . ASP A 1 324 ? 133.693 122.504 136.750 1.00 51.52  ? 409 ASP A C     1 
ATOM   2442 O O     . ASP A 1 324 ? 133.940 122.874 137.906 1.00 50.33  ? 409 ASP A O     1 
ATOM   2443 C CB    . ASP A 1 324 ? 135.488 122.421 135.005 1.00 60.06  ? 409 ASP A CB    1 
ATOM   2444 C CG    . ASP A 1 324 ? 136.721 121.691 134.538 1.00 68.65  ? 409 ASP A CG    1 
ATOM   2445 O OD1   . ASP A 1 324 ? 137.313 120.967 135.362 1.00 71.80  ? 409 ASP A OD1   1 
ATOM   2446 O OD2   . ASP A 1 324 ? 137.087 121.822 133.352 1.00 68.13  ? 409 ASP A OD2   1 
ATOM   2447 N N     . PHE A 1 325 ? 132.585 122.867 136.107 1.00 51.96  ? 410 PHE A N     1 
ATOM   2448 C CA    . PHE A 1 325 ? 131.587 123.731 136.718 1.00 49.36  ? 410 PHE A CA    1 
ATOM   2449 C C     . PHE A 1 325 ? 130.930 123.053 137.913 1.00 49.11  ? 410 PHE A C     1 
ATOM   2450 O O     . PHE A 1 325 ? 130.635 123.706 138.916 1.00 52.86  ? 410 PHE A O     1 
ATOM   2451 C CB    . PHE A 1 325 ? 130.554 124.122 135.662 1.00 47.66  ? 410 PHE A CB    1 
ATOM   2452 C CG    . PHE A 1 325 ? 129.341 124.805 136.210 1.00 53.29  ? 410 PHE A CG    1 
ATOM   2453 C CD1   . PHE A 1 325 ? 129.394 126.131 136.602 1.00 51.88  ? 410 PHE A CD1   1 
ATOM   2454 C CD2   . PHE A 1 325 ? 128.139 124.127 136.313 1.00 51.50  ? 410 PHE A CD2   1 
ATOM   2455 C CE1   . PHE A 1 325 ? 128.272 126.765 137.099 1.00 48.59  ? 410 PHE A CE1   1 
ATOM   2456 C CE2   . PHE A 1 325 ? 127.014 124.755 136.810 1.00 50.37  ? 410 PHE A CE2   1 
ATOM   2457 C CZ    . PHE A 1 325 ? 127.081 126.075 137.203 1.00 48.02  ? 410 PHE A CZ    1 
ATOM   2458 N N     . SER A 1 326 ? 130.699 121.743 137.823 1.00 47.97  ? 411 SER A N     1 
ATOM   2459 C CA    . SER A 1 326 ? 130.142 121.000 138.946 1.00 46.59  ? 411 SER A CA    1 
ATOM   2460 C C     . SER A 1 326 ? 131.114 120.957 140.116 1.00 46.74  ? 411 SER A C     1 
ATOM   2461 O O     . SER A 1 326 ? 130.703 121.090 141.273 1.00 50.01  ? 411 SER A O     1 
ATOM   2462 C CB    . SER A 1 326 ? 129.773 119.586 138.502 1.00 53.18  ? 411 SER A CB    1 
ATOM   2463 O OG    . SER A 1 326 ? 128.776 119.612 137.495 1.00 55.34  ? 411 SER A OG    1 
ATOM   2464 N N     . THR A 1 327 ? 132.406 120.769 139.837 1.00 48.47  ? 412 THR A N     1 
ATOM   2465 C CA    . THR A 1 327 ? 133.396 120.800 140.911 1.00 44.94  ? 412 THR A CA    1 
ATOM   2466 C C     . THR A 1 327 ? 133.439 122.171 141.580 1.00 46.55  ? 412 THR A C     1 
ATOM   2467 O O     . THR A 1 327 ? 133.483 122.273 142.816 1.00 47.99  ? 412 THR A O     1 
ATOM   2468 C CB    . THR A 1 327 ? 134.775 120.424 140.367 1.00 48.14  ? 412 THR A CB    1 
ATOM   2469 O OG1   . THR A 1 327 ? 134.746 119.077 139.877 1.00 49.72  ? 412 THR A OG1   1 
ATOM   2470 C CG2   . THR A 1 327 ? 135.830 120.535 141.458 1.00 50.22  ? 412 THR A CG2   1 
ATOM   2471 N N     . CYS A 1 328 ? 133.418 123.238 140.778 1.00 49.83  ? 413 CYS A N     1 
ATOM   2472 C CA    . CYS A 1 328 ? 133.422 124.587 141.340 1.00 44.54  ? 413 CYS A CA    1 
ATOM   2473 C C     . CYS A 1 328 ? 132.156 124.853 142.148 1.00 45.06  ? 413 CYS A C     1 
ATOM   2474 O O     . CYS A 1 328 ? 132.213 125.468 143.222 1.00 47.66  ? 413 CYS A O     1 
ATOM   2475 C CB    . CYS A 1 328 ? 133.578 125.618 140.223 1.00 53.26  ? 413 CYS A CB    1 
ATOM   2476 S SG    . CYS A 1 328 ? 135.149 125.527 139.334 1.00 74.49  ? 413 CYS A SG    1 
ATOM   2477 N N     . THR A 1 329 ? 131.005 124.399 141.648 1.00 46.85  ? 414 THR A N     1 
ATOM   2478 C CA    . THR A 1 329 ? 129.760 124.530 142.393 1.00 43.40  ? 414 THR A CA    1 
ATOM   2479 C C     . THR A 1 329 ? 129.840 123.784 143.715 1.00 47.21  ? 414 THR A C     1 
ATOM   2480 O O     . THR A 1 329 ? 129.383 124.285 144.747 1.00 53.89  ? 414 THR A O     1 
ATOM   2481 C CB    . THR A 1 329 ? 128.589 124.010 141.557 1.00 44.47  ? 414 THR A CB    1 
ATOM   2482 O OG1   . THR A 1 329 ? 128.528 124.725 140.316 1.00 48.19  ? 414 THR A OG1   1 
ATOM   2483 C CG2   . THR A 1 329 ? 127.274 124.186 142.303 1.00 49.04  ? 414 THR A CG2   1 
ATOM   2484 N N     . GLY A 1 330 ? 130.430 122.588 143.704 1.00 47.51  ? 415 GLY A N     1 
ATOM   2485 C CA    . GLY A 1 330 ? 130.567 121.829 144.935 1.00 44.56  ? 415 GLY A CA    1 
ATOM   2486 C C     . GLY A 1 330 ? 131.424 122.539 145.964 1.00 45.29  ? 415 GLY A C     1 
ATOM   2487 O O     . GLY A 1 330 ? 131.062 122.620 147.139 1.00 49.37  ? 415 GLY A O     1 
ATOM   2488 N N     . VAL A 1 331 ? 132.570 123.076 145.535 1.00 44.88  ? 416 VAL A N     1 
ATOM   2489 C CA    . VAL A 1 331 ? 133.449 123.742 146.496 1.00 44.16  ? 416 VAL A CA    1 
ATOM   2490 C C     . VAL A 1 331 ? 132.807 125.027 147.022 1.00 50.23  ? 416 VAL A C     1 
ATOM   2491 O O     . VAL A 1 331 ? 132.866 125.317 148.228 1.00 57.81  ? 416 VAL A O     1 
ATOM   2492 C CB    . VAL A 1 331 ? 134.851 123.985 145.895 1.00 43.77  ? 416 VAL A CB    1 
ATOM   2493 C CG1   . VAL A 1 331 ? 135.400 122.701 145.291 1.00 48.03  ? 416 VAL A CG1   1 
ATOM   2494 C CG2   . VAL A 1 331 ? 134.846 125.092 144.851 1.00 46.88  ? 416 VAL A CG2   1 
ATOM   2495 N N     . ALA A 1 332 ? 132.159 125.802 146.144 1.00 46.98  ? 417 ALA A N     1 
ATOM   2496 C CA    . ALA A 1 332 ? 131.508 127.030 146.592 1.00 44.62  ? 417 ALA A CA    1 
ATOM   2497 C C     . ALA A 1 332 ? 130.354 126.728 147.540 1.00 50.00  ? 417 ALA A C     1 
ATOM   2498 O O     . ALA A 1 332 ? 130.180 127.411 148.558 1.00 58.04  ? 417 ALA A O     1 
ATOM   2499 C CB    . ALA A 1 332 ? 131.022 127.837 145.390 1.00 43.27  ? 417 ALA A CB    1 
ATOM   2500 N N     . THR A 1 333 ? 129.565 125.695 147.233 1.00 46.94  ? 418 THR A N     1 
ATOM   2501 C CA    . THR A 1 333 ? 128.450 125.327 148.092 1.00 47.57  ? 418 THR A CA    1 
ATOM   2502 C C     . THR A 1 333 ? 128.930 124.779 149.428 1.00 51.21  ? 418 THR A C     1 
ATOM   2503 O O     . THR A 1 333 ? 128.297 125.030 150.456 1.00 59.02  ? 418 THR A O     1 
ATOM   2504 C CB    . THR A 1 333 ? 127.566 124.304 147.381 1.00 47.14  ? 418 THR A CB    1 
ATOM   2505 O OG1   . THR A 1 333 ? 127.273 124.766 146.056 1.00 47.33  ? 418 THR A OG1   1 
ATOM   2506 C CG2   . THR A 1 333 ? 126.263 124.111 148.138 1.00 45.89  ? 418 THR A CG2   1 
ATOM   2507 N N     . PHE A 1 334 ? 130.042 124.038 149.437 1.00 51.41  ? 419 PHE A N     1 
ATOM   2508 C CA    . PHE A 1 334 ? 130.628 123.586 150.695 1.00 56.27  ? 419 PHE A CA    1 
ATOM   2509 C C     . PHE A 1 334 ? 131.041 124.771 151.562 1.00 58.91  ? 419 PHE A C     1 
ATOM   2510 O O     . PHE A 1 334 ? 130.677 124.847 152.748 1.00 65.51  ? 419 PHE A O     1 
ATOM   2511 C CB    . PHE A 1 334 ? 131.827 122.685 150.395 1.00 54.77  ? 419 PHE A CB    1 
ATOM   2512 C CG    . PHE A 1 334 ? 132.309 121.885 151.570 1.00 61.20  ? 419 PHE A CG    1 
ATOM   2513 C CD1   . PHE A 1 334 ? 133.231 122.413 152.460 1.00 60.98  ? 419 PHE A CD1   1 
ATOM   2514 C CD2   . PHE A 1 334 ? 131.854 120.595 151.773 1.00 65.28  ? 419 PHE A CD2   1 
ATOM   2515 C CE1   . PHE A 1 334 ? 133.679 121.669 153.534 1.00 65.04  ? 419 PHE A CE1   1 
ATOM   2516 C CE2   . PHE A 1 334 ? 132.297 119.848 152.846 1.00 66.53  ? 419 PHE A CE2   1 
ATOM   2517 C CZ    . PHE A 1 334 ? 133.211 120.386 153.727 1.00 63.16  ? 419 PHE A CZ    1 
ATOM   2518 N N     . THR A 1 335 ? 131.768 125.725 150.973 1.00 54.45  ? 420 THR A N     1 
ATOM   2519 C CA    . THR A 1 335 ? 132.162 126.915 151.722 1.00 54.24  ? 420 THR A CA    1 
ATOM   2520 C C     . THR A 1 335 ? 130.947 127.646 152.261 1.00 58.73  ? 420 THR A C     1 
ATOM   2521 O O     . THR A 1 335 ? 130.933 128.117 153.407 1.00 66.56  ? 420 THR A O     1 
ATOM   2522 C CB    . THR A 1 335 ? 132.977 127.852 150.837 1.00 59.12  ? 420 THR A CB    1 
ATOM   2523 O OG1   . THR A 1 335 ? 133.927 127.091 150.083 1.00 63.34  ? 420 THR A OG1   1 
ATOM   2524 C CG2   . THR A 1 335 ? 133.694 128.889 151.680 1.00 62.08  ? 420 THR A CG2   1 
ATOM   2525 N N     . MET A 1 336 ? 129.908 127.744 151.460 1.00 59.53  ? 421 MET A N     1 
ATOM   2526 C CA    . MET A 1 336 ? 128.853 128.628 151.889 1.00 63.23  ? 421 MET A CA    1 
ATOM   2527 C C     . MET A 1 336 ? 127.865 127.930 152.832 1.00 63.26  ? 421 MET A C     1 
ATOM   2528 O O     . MET A 1 336 ? 127.211 128.594 153.642 1.00 70.12  ? 421 MET A O     1 
ATOM   2529 C CB    . MET A 1 336 ? 128.200 129.213 150.654 1.00 57.59  ? 421 MET A CB    1 
ATOM   2530 C CG    . MET A 1 336 ? 127.178 130.173 151.039 1.00 65.41  ? 421 MET A CG    1 
ATOM   2531 S SD    . MET A 1 336 ? 126.439 130.958 149.645 1.00 81.64  ? 421 MET A SD    1 
ATOM   2532 C CE    . MET A 1 336 ? 125.249 131.907 150.502 1.00 69.14  ? 421 MET A CE    1 
ATOM   2533 N N     . MET A 1 337 ? 127.749 126.601 152.763 1.00 57.57  ? 422 MET A N     1 
ATOM   2534 C CA    . MET A 1 337 ? 127.084 125.864 153.832 1.00 58.09  ? 422 MET A CA    1 
ATOM   2535 C C     . MET A 1 337 ? 127.876 125.900 155.130 1.00 66.59  ? 422 MET A C     1 
ATOM   2536 O O     . MET A 1 337 ? 127.289 125.722 156.203 1.00 73.01  ? 422 MET A O     1 
ATOM   2537 C CB    . MET A 1 337 ? 126.839 124.407 153.428 1.00 55.34  ? 422 MET A CB    1 
ATOM   2538 C CG    . MET A 1 337 ? 125.651 124.193 152.510 1.00 53.74  ? 422 MET A CG    1 
ATOM   2539 S SD    . MET A 1 337 ? 125.786 122.680 151.540 1.00 70.82  ? 422 MET A SD    1 
ATOM   2540 C CE    . MET A 1 337 ? 124.054 122.303 151.275 1.00 57.07  ? 422 MET A CE    1 
ATOM   2541 N N     . LEU A 1 338 ? 129.196 126.102 155.068 1.00 66.22  ? 423 LEU A N     1 
ATOM   2542 C CA    . LEU A 1 338 ? 129.904 126.376 156.317 1.00 65.06  ? 423 LEU A CA    1 
ATOM   2543 C C     . LEU A 1 338 ? 129.627 127.788 156.833 1.00 69.43  ? 423 LEU A C     1 
ATOM   2544 O O     . LEU A 1 338 ? 129.532 127.991 158.050 1.00 80.75  ? 423 LEU A O     1 
ATOM   2545 C CB    . LEU A 1 338 ? 131.410 126.153 156.154 1.00 61.92  ? 423 LEU A CB    1 
ATOM   2546 C CG    . LEU A 1 338 ? 131.848 124.718 155.851 1.00 60.58  ? 423 LEU A CG    1 
ATOM   2547 C CD1   . LEU A 1 338 ? 133.220 124.716 155.201 1.00 60.36  ? 423 LEU A CD1   1 
ATOM   2548 C CD2   . LEU A 1 338 ? 131.846 123.875 157.118 1.00 60.89  ? 423 LEU A CD2   1 
ATOM   2549 N N     . LEU A 1 339 ? 129.494 128.767 155.932 1.00 68.97  ? 424 LEU A N     1 
ATOM   2550 C CA    . LEU A 1 339 ? 129.250 130.147 156.362 1.00 73.66  ? 424 LEU A CA    1 
ATOM   2551 C C     . LEU A 1 339 ? 127.810 130.368 156.836 1.00 80.49  ? 424 LEU A C     1 
ATOM   2552 O O     . LEU A 1 339 ? 127.553 131.258 157.665 1.00 88.82  ? 424 LEU A O     1 
ATOM   2553 C CB    . LEU A 1 339 ? 129.585 131.115 155.223 1.00 74.51  ? 424 LEU A CB    1 
ATOM   2554 C CG    . LEU A 1 339 ? 131.023 131.082 154.694 1.00 79.48  ? 424 LEU A CG    1 
ATOM   2555 C CD1   . LEU A 1 339 ? 131.204 132.099 153.581 1.00 79.12  ? 424 LEU A CD1   1 
ATOM   2556 C CD2   . LEU A 1 339 ? 132.013 131.345 155.819 1.00 82.22  ? 424 LEU A CD2   1 
ATOM   2557 N N     . SER A 1 340 ? 126.856 129.595 156.308 1.00 78.28  ? 425 SER A N     1 
ATOM   2558 C CA    . SER A 1 340 ? 125.450 129.791 156.658 1.00 84.52  ? 425 SER A CA    1 
ATOM   2559 C C     . SER A 1 340 ? 125.187 129.574 158.142 1.00 92.05  ? 425 SER A C     1 
ATOM   2560 O O     . SER A 1 340 ? 124.432 130.339 158.762 1.00 94.27  ? 425 SER A O     1 
ATOM   2561 C CB    . SER A 1 340 ? 124.572 128.844 155.837 1.00 81.34  ? 425 SER A CB    1 
ATOM   2562 O OG    . SER A 1 340 ? 124.772 127.500 156.251 1.00 82.42  ? 425 SER A OG    1 
ATOM   2563 N N     . GLN A 1 341 ? 125.792 128.538 158.735 1.00 91.66  ? 426 GLN A N     1 
ATOM   2564 C CA    . GLN A 1 341 ? 125.553 128.234 160.137 1.00 94.48  ? 426 GLN A CA    1 
ATOM   2565 C C     . GLN A 1 341 ? 126.060 129.326 161.075 1.00 97.00  ? 426 GLN A C     1 
ATOM   2566 O O     . GLN A 1 341 ? 125.942 129.188 162.298 1.00 104.66 ? 426 GLN A O     1 
ATOM   2567 C CB    . GLN A 1 341 ? 126.178 126.886 160.495 1.00 95.31  ? 426 GLN A CB    1 
ATOM   2568 C CG    . GLN A 1 341 ? 125.533 125.718 159.764 1.00 99.24  ? 426 GLN A CG    1 
ATOM   2569 C CD    . GLN A 1 341 ? 124.091 125.502 160.199 1.00 104.67 ? 426 GLN A CD    1 
ATOM   2570 O OE1   . GLN A 1 341 ? 123.749 125.661 161.373 1.00 107.11 ? 426 GLN A OE1   1 
ATOM   2571 N NE2   . GLN A 1 341 ? 123.238 125.140 159.250 1.00 99.12  ? 426 GLN A NE2   1 
ATOM   2572 N N     . TYR A 1 342 ? 126.624 130.395 160.528 1.00 94.25  ? 427 TYR A N     1 
ATOM   2573 C CA    . TYR A 1 342 ? 126.893 131.635 161.244 1.00 99.34  ? 427 TYR A CA    1 
ATOM   2574 C C     . TYR A 1 342 ? 125.991 132.766 160.784 1.00 99.12  ? 427 TYR A C     1 
ATOM   2575 O O     . TYR A 1 342 ? 125.521 133.556 161.618 1.00 102.14 ? 427 TYR A O     1 
ATOM   2576 C CB    . TYR A 1 342 ? 128.378 132.019 161.067 1.00 100.83 ? 427 TYR A CB    1 
ATOM   2577 C CG    . TYR A 1 342 ? 128.798 133.369 161.620 1.00 108.40 ? 427 TYR A CG    1 
ATOM   2578 C CD1   . TYR A 1 342 ? 128.605 134.542 160.896 1.00 104.53 ? 427 TYR A CD1   1 
ATOM   2579 C CD2   . TYR A 1 342 ? 129.410 133.465 162.864 1.00 111.54 ? 427 TYR A CD2   1 
ATOM   2580 C CE1   . TYR A 1 342 ? 128.999 135.768 161.402 1.00 109.52 ? 427 TYR A CE1   1 
ATOM   2581 C CE2   . TYR A 1 342 ? 129.806 134.687 163.378 1.00 115.85 ? 427 TYR A CE2   1 
ATOM   2582 C CZ    . TYR A 1 342 ? 129.598 135.832 162.644 1.00 117.93 ? 427 TYR A CZ    1 
ATOM   2583 O OH    . TYR A 1 342 ? 129.993 137.045 163.155 1.00 122.35 ? 427 TYR A OH    1 
ATOM   2584 N N     . VAL A 1 343 ? 125.721 132.851 159.475 1.00 102.15 ? 428 VAL A N     1 
ATOM   2585 C CA    . VAL A 1 343 ? 124.840 133.908 158.964 1.00 101.92 ? 428 VAL A CA    1 
ATOM   2586 C C     . VAL A 1 343 ? 123.451 133.816 159.596 1.00 98.52  ? 428 VAL A C     1 
ATOM   2587 O O     . VAL A 1 343 ? 122.884 134.820 160.042 1.00 98.62  ? 428 VAL A O     1 
ATOM   2588 C CB    . VAL A 1 343 ? 124.751 133.857 157.428 1.00 95.44  ? 428 VAL A CB    1 
ATOM   2589 C CG1   . VAL A 1 343 ? 123.907 135.009 156.928 1.00 90.16  ? 428 VAL A CG1   1 
ATOM   2590 C CG2   . VAL A 1 343 ? 126.133 133.935 156.819 1.00 91.71  ? 428 VAL A CG2   1 
ATOM   2591 N N     . PHE A 1 344 ? 122.878 132.612 159.627 1.00 97.59  ? 429 PHE A N     1 
ATOM   2592 C CA    . PHE A 1 344 ? 121.563 132.409 160.227 1.00 96.08  ? 429 PHE A CA    1 
ATOM   2593 C C     . PHE A 1 344 ? 121.518 132.926 161.655 1.00 99.09  ? 429 PHE A C     1 
ATOM   2594 O O     . PHE A 1 344 ? 120.731 133.821 161.978 1.00 95.47  ? 429 PHE A O     1 
ATOM   2595 C CB    . PHE A 1 344 ? 121.189 130.932 160.187 1.00 95.21  ? 429 PHE A CB    1 
ATOM   2596 C CG    . PHE A 1 344 ? 120.365 130.555 158.997 1.00 98.30  ? 429 PHE A CG    1 
ATOM   2597 C CD1   . PHE A 1 344 ? 120.817 129.618 158.076 1.00 95.90  ? 429 PHE A CD1   1 
ATOM   2598 C CD2   . PHE A 1 344 ? 119.094 131.109 158.824 1.00 93.25  ? 429 PHE A CD2   1 
ATOM   2599 C CE1   . PHE A 1 344 ? 120.041 129.262 156.982 1.00 88.97  ? 429 PHE A CE1   1 
ATOM   2600 C CE2   . PHE A 1 344 ? 118.307 130.748 157.732 1.00 91.77  ? 429 PHE A CE2   1 
ATOM   2601 C CZ    . PHE A 1 344 ? 118.794 129.839 156.805 1.00 88.39  ? 429 PHE A CZ    1 
ATOM   2602 N N     . ASN A 1 345 ? 122.395 132.399 162.515 1.00 102.90 ? 430 ASN A N     1 
ATOM   2603 C CA    . ASN A 1 345 ? 122.368 132.759 163.927 1.00 99.18  ? 430 ASN A CA    1 
ATOM   2604 C C     . ASN A 1 345 ? 122.574 134.253 164.115 1.00 99.36  ? 430 ASN A C     1 
ATOM   2605 O O     . ASN A 1 345 ? 121.916 134.874 164.956 1.00 100.23 ? 430 ASN A O     1 
ATOM   2606 C CB    . ASN A 1 345 ? 123.426 131.964 164.697 1.00 96.55  ? 430 ASN A CB    1 
ATOM   2607 C CG    . ASN A 1 345 ? 123.231 130.472 164.585 1.00 99.38  ? 430 ASN A CG    1 
ATOM   2608 O OD1   . ASN A 1 345 ? 122.442 129.993 163.783 1.00 98.27  ? 430 ASN A OD1   1 
ATOM   2609 N ND2   . ASN A 1 345 ? 123.966 129.721 165.409 1.00 101.19 ? 430 ASN A ND2   1 
ATOM   2610 N N     . LYS A 1 346 ? 123.489 134.853 163.348 1.00 100.78 ? 431 LYS A N     1 
ATOM   2611 C CA    . LYS A 1 346 ? 123.793 136.260 163.580 1.00 101.04 ? 431 LYS A CA    1 
ATOM   2612 C C     . LYS A 1 346 ? 122.661 137.168 163.116 1.00 102.25 ? 431 LYS A C     1 
ATOM   2613 O O     . LYS A 1 346 ? 122.336 138.150 163.793 1.00 102.72 ? 431 LYS A O     1 
ATOM   2614 C CB    . LYS A 1 346 ? 125.101 136.640 162.893 1.00 106.13 ? 431 LYS A CB    1 
ATOM   2615 C CG    . LYS A 1 346 ? 125.509 138.086 163.144 1.00 107.94 ? 431 LYS A CG    1 
ATOM   2616 C CD    . LYS A 1 346 ? 126.866 138.402 162.543 1.00 112.19 ? 431 LYS A CD    1 
ATOM   2617 C CE    . LYS A 1 346 ? 127.189 139.881 162.672 1.00 117.25 ? 431 LYS A CE    1 
ATOM   2618 N NZ    . LYS A 1 346 ? 127.357 140.289 164.095 1.00 123.05 ? 431 LYS A NZ    1 
ATOM   2619 N N     . TYR A 1 347 ? 122.037 136.865 161.977 1.00 101.52 ? 432 TYR A N     1 
ATOM   2620 C CA    . TYR A 1 347 ? 121.109 137.807 161.364 1.00 96.55  ? 432 TYR A CA    1 
ATOM   2621 C C     . TYR A 1 347 ? 119.650 137.387 161.458 1.00 97.58  ? 432 TYR A C     1 
ATOM   2622 O O     . TYR A 1 347 ? 118.813 138.178 161.904 1.00 99.88  ? 432 TYR A O     1 
ATOM   2623 C CB    . TYR A 1 347 ? 121.500 138.031 159.897 1.00 96.24  ? 432 TYR A CB    1 
ATOM   2624 C CG    . TYR A 1 347 ? 122.782 138.816 159.752 1.00 99.71  ? 432 TYR A CG    1 
ATOM   2625 C CD1   . TYR A 1 347 ? 122.793 140.197 159.897 1.00 99.16  ? 432 TYR A CD1   1 
ATOM   2626 C CD2   . TYR A 1 347 ? 123.985 138.175 159.489 1.00 103.15 ? 432 TYR A CD2   1 
ATOM   2627 C CE1   . TYR A 1 347 ? 123.964 140.919 159.774 1.00 106.14 ? 432 TYR A CE1   1 
ATOM   2628 C CE2   . TYR A 1 347 ? 125.161 138.888 159.363 1.00 106.55 ? 432 TYR A CE2   1 
ATOM   2629 C CZ    . TYR A 1 347 ? 125.145 140.259 159.507 1.00 111.49 ? 432 TYR A CZ    1 
ATOM   2630 O OH    . TYR A 1 347 ? 126.314 140.973 159.383 1.00 118.73 ? 432 TYR A OH    1 
ATOM   2631 N N     . GLY A 1 348 ? 119.310 136.168 161.049 1.00 97.10  ? 433 GLY A N     1 
ATOM   2632 C CA    . GLY A 1 348 ? 117.915 135.787 161.044 1.00 91.39  ? 433 GLY A CA    1 
ATOM   2633 C C     . GLY A 1 348 ? 117.424 135.136 159.767 1.00 87.81  ? 433 GLY A C     1 
ATOM   2634 O O     . GLY A 1 348 ? 118.051 135.238 158.701 1.00 88.08  ? 433 GLY A O     1 
ATOM   2635 N N     . TRP A 1 349 ? 116.283 134.452 159.889 1.00 86.41  ? 434 TRP A N     1 
ATOM   2636 C CA    . TRP A 1 349 ? 115.648 133.833 158.732 1.00 82.91  ? 434 TRP A CA    1 
ATOM   2637 C C     . TRP A 1 349 ? 115.320 134.867 157.665 1.00 83.85  ? 434 TRP A C     1 
ATOM   2638 O O     . TRP A 1 349 ? 115.471 134.601 156.469 1.00 87.53  ? 434 TRP A O     1 
ATOM   2639 C CB    . TRP A 1 349 ? 114.385 133.089 159.171 1.00 83.27  ? 434 TRP A CB    1 
ATOM   2640 C CG    . TRP A 1 349 ? 113.752 132.265 158.091 1.00 84.99  ? 434 TRP A CG    1 
ATOM   2641 C CD1   . TRP A 1 349 ? 113.880 130.922 157.901 1.00 86.62  ? 434 TRP A CD1   1 
ATOM   2642 C CD2   . TRP A 1 349 ? 112.867 132.732 157.065 1.00 85.01  ? 434 TRP A CD2   1 
ATOM   2643 N NE1   . TRP A 1 349 ? 113.143 130.524 156.812 1.00 86.78  ? 434 TRP A NE1   1 
ATOM   2644 C CE2   . TRP A 1 349 ? 112.511 131.617 156.282 1.00 85.30  ? 434 TRP A CE2   1 
ATOM   2645 C CE3   . TRP A 1 349 ? 112.345 133.985 156.728 1.00 84.11  ? 434 TRP A CE3   1 
ATOM   2646 C CZ2   . TRP A 1 349 ? 111.659 131.717 155.184 1.00 83.28  ? 434 TRP A CZ2   1 
ATOM   2647 C CZ3   . TRP A 1 349 ? 111.502 134.082 155.638 1.00 85.38  ? 434 TRP A CZ3   1 
ATOM   2648 C CH2   . TRP A 1 349 ? 111.168 132.956 154.879 1.00 84.57  ? 434 TRP A CH2   1 
ATOM   2649 N N     . GLY A 1 350 ? 114.870 136.054 158.077 1.00 84.83  ? 435 GLY A N     1 
ATOM   2650 C CA    . GLY A 1 350 ? 114.479 137.065 157.110 1.00 84.75  ? 435 GLY A CA    1 
ATOM   2651 C C     . GLY A 1 350 ? 115.638 137.635 156.320 1.00 83.69  ? 435 GLY A C     1 
ATOM   2652 O O     . GLY A 1 350 ? 115.464 138.043 155.167 1.00 83.77  ? 435 GLY A O     1 
ATOM   2653 N N     . VAL A 1 351 ? 116.824 137.689 156.922 1.00 83.07  ? 436 VAL A N     1 
ATOM   2654 C CA    . VAL A 1 351 ? 117.999 138.163 156.198 1.00 78.84  ? 436 VAL A CA    1 
ATOM   2655 C C     . VAL A 1 351 ? 118.565 137.058 155.311 1.00 78.25  ? 436 VAL A C     1 
ATOM   2656 O O     . VAL A 1 351 ? 118.983 137.308 154.170 1.00 78.28  ? 436 VAL A O     1 
ATOM   2657 C CB    . VAL A 1 351 ? 119.052 138.693 157.187 1.00 78.29  ? 436 VAL A CB    1 
ATOM   2658 C CG1   . VAL A 1 351 ? 120.137 139.461 156.447 1.00 74.94  ? 436 VAL A CG1   1 
ATOM   2659 C CG2   . VAL A 1 351 ? 118.394 139.566 158.240 1.00 83.10  ? 436 VAL A CG2   1 
ATOM   2660 N N     . ALA A 1 352 ? 118.595 135.820 155.819 1.00 78.68  ? 437 ALA A N     1 
ATOM   2661 C CA    . ALA A 1 352 ? 119.066 134.712 154.996 1.00 75.46  ? 437 ALA A CA    1 
ATOM   2662 C C     . ALA A 1 352 ? 118.144 134.460 153.811 1.00 76.31  ? 437 ALA A C     1 
ATOM   2663 O O     . ALA A 1 352 ? 118.612 134.046 152.745 1.00 74.47  ? 437 ALA A O     1 
ATOM   2664 C CB    . ALA A 1 352 ? 119.209 133.450 155.843 1.00 74.65  ? 437 ALA A CB    1 
ATOM   2665 N N     . ALA A 1 353 ? 116.845 134.727 153.965 1.00 76.15  ? 438 ALA A N     1 
ATOM   2666 C CA    . ALA A 1 353 ? 115.914 134.640 152.848 1.00 69.18  ? 438 ALA A CA    1 
ATOM   2667 C C     . ALA A 1 353 ? 116.042 135.814 151.890 1.00 70.15  ? 438 ALA A C     1 
ATOM   2668 O O     . ALA A 1 353 ? 115.509 135.744 150.779 1.00 75.69  ? 438 ALA A O     1 
ATOM   2669 C CB    . ALA A 1 353 ? 114.477 134.548 153.365 1.00 68.20  ? 438 ALA A CB    1 
ATOM   2670 N N     . LYS A 1 354 ? 116.715 136.889 152.299 1.00 69.53  ? 439 LYS A N     1 
ATOM   2671 C CA    . LYS A 1 354 ? 117.022 137.989 151.398 1.00 69.38  ? 439 LYS A CA    1 
ATOM   2672 C C     . LYS A 1 354 ? 118.313 137.777 150.628 1.00 66.85  ? 439 LYS A C     1 
ATOM   2673 O O     . LYS A 1 354 ? 118.452 138.314 149.524 1.00 63.54  ? 439 LYS A O     1 
ATOM   2674 C CB    . LYS A 1 354 ? 117.127 139.308 152.172 1.00 73.36  ? 439 LYS A CB    1 
ATOM   2675 C CG    . LYS A 1 354 ? 115.798 139.941 152.534 1.00 76.02  ? 439 LYS A CG    1 
ATOM   2676 C CD    . LYS A 1 354 ? 115.903 141.457 152.491 1.00 82.82  ? 439 LYS A CD    1 
ATOM   2677 C CE    . LYS A 1 354 ? 115.273 142.094 153.715 1.00 88.53  ? 439 LYS A CE    1 
ATOM   2678 N NZ    . LYS A 1 354 ? 115.311 143.581 153.646 1.00 87.41  ? 439 LYS A NZ    1 
ATOM   2679 N N     . ILE A 1 355 ? 119.262 137.023 151.188 1.00 68.71  ? 440 ILE A N     1 
ATOM   2680 C CA    . ILE A 1 355 ? 120.557 136.877 150.523 1.00 64.55  ? 440 ILE A CA    1 
ATOM   2681 C C     . ILE A 1 355 ? 120.406 136.246 149.140 1.00 61.34  ? 440 ILE A C     1 
ATOM   2682 O O     . ILE A 1 355 ? 120.944 136.762 148.154 1.00 63.07  ? 440 ILE A O     1 
ATOM   2683 C CB    . ILE A 1 355 ? 121.540 136.081 151.399 1.00 68.14  ? 440 ILE A CB    1 
ATOM   2684 C CG1   . ILE A 1 355 ? 121.653 136.714 152.786 1.00 67.14  ? 440 ILE A CG1   1 
ATOM   2685 C CG2   . ILE A 1 355 ? 122.903 135.995 150.723 1.00 64.81  ? 440 ILE A CG2   1 
ATOM   2686 C CD1   . ILE A 1 355 ? 122.340 135.852 153.814 1.00 67.88  ? 440 ILE A CD1   1 
ATOM   2687 N N     . THR A 1 356 ? 119.675 135.126 149.037 1.00 63.00  ? 441 THR A N     1 
ATOM   2688 C CA    . THR A 1 356 ? 119.602 134.424 147.754 1.00 59.98  ? 441 THR A CA    1 
ATOM   2689 C C     . THR A 1 356 ? 118.955 135.264 146.656 1.00 57.12  ? 441 THR A C     1 
ATOM   2690 O O     . THR A 1 356 ? 119.539 135.360 145.560 1.00 62.78  ? 441 THR A O     1 
ATOM   2691 C CB    . THR A 1 356 ? 118.892 133.076 147.930 1.00 59.59  ? 441 THR A CB    1 
ATOM   2692 O OG1   . THR A 1 356 ? 119.508 132.341 148.996 1.00 63.44  ? 441 THR A OG1   1 
ATOM   2693 C CG2   . THR A 1 356 ? 118.965 132.261 146.644 1.00 50.62  ? 441 THR A CG2   1 
ATOM   2694 N N     . PRO A 1 357 ? 117.781 135.882 146.854 1.00 55.13  ? 442 PRO A N     1 
ATOM   2695 C CA    . PRO A 1 357 ? 117.241 136.738 145.783 1.00 51.58  ? 442 PRO A CA    1 
ATOM   2696 C C     . PRO A 1 357 ? 118.175 137.867 145.395 1.00 56.02  ? 442 PRO A C     1 
ATOM   2697 O O     . PRO A 1 357 ? 118.329 138.156 144.203 1.00 58.27  ? 442 PRO A O     1 
ATOM   2698 C CB    . PRO A 1 357 ? 115.930 137.273 146.382 1.00 54.31  ? 442 PRO A CB    1 
ATOM   2699 C CG    . PRO A 1 357 ? 116.021 137.010 147.841 1.00 60.35  ? 442 PRO A CG    1 
ATOM   2700 C CD    . PRO A 1 357 ? 116.832 135.772 147.975 1.00 60.31  ? 442 PRO A CD    1 
ATOM   2701 N N     . THR A 1 358 ? 118.832 138.495 146.372 1.00 58.06  ? 443 THR A N     1 
ATOM   2702 C CA    . THR A 1 358 ? 119.698 139.628 146.063 1.00 55.75  ? 443 THR A CA    1 
ATOM   2703 C C     . THR A 1 358 ? 120.955 139.186 145.326 1.00 54.59  ? 443 THR A C     1 
ATOM   2704 O O     . THR A 1 358 ? 121.362 139.831 144.353 1.00 55.85  ? 443 THR A O     1 
ATOM   2705 C CB    . THR A 1 358 ? 120.062 140.383 147.340 1.00 56.03  ? 443 THR A CB    1 
ATOM   2706 O OG1   . THR A 1 358 ? 120.634 139.476 148.291 1.00 61.29  ? 443 THR A OG1   1 
ATOM   2707 C CG2   . THR A 1 358 ? 118.829 141.047 147.938 1.00 59.57  ? 443 THR A CG2   1 
ATOM   2708 N N     . VAL A 1 359 ? 121.590 138.099 145.770 1.00 54.68  ? 444 VAL A N     1 
ATOM   2709 C CA    . VAL A 1 359 ? 122.784 137.635 145.070 1.00 52.64  ? 444 VAL A CA    1 
ATOM   2710 C C     . VAL A 1 359 ? 122.429 137.207 143.653 1.00 52.70  ? 444 VAL A C     1 
ATOM   2711 O O     . VAL A 1 359 ? 123.157 137.516 142.699 1.00 57.35  ? 444 VAL A O     1 
ATOM   2712 C CB    . VAL A 1 359 ? 123.493 136.513 145.857 1.00 55.95  ? 444 VAL A CB    1 
ATOM   2713 C CG1   . VAL A 1 359 ? 122.636 135.265 145.956 1.00 52.97  ? 444 VAL A CG1   1 
ATOM   2714 C CG2   . VAL A 1 359 ? 124.834 136.181 145.213 1.00 51.62  ? 444 VAL A CG2   1 
ATOM   2715 N N     . LEU A 1 360 ? 121.293 136.522 143.481 1.00 51.13  ? 445 LEU A N     1 
ATOM   2716 C CA    . LEU A 1 360 ? 120.892 136.123 142.139 1.00 45.39  ? 445 LEU A CA    1 
ATOM   2717 C C     . LEU A 1 360 ? 120.625 137.344 141.267 1.00 51.82  ? 445 LEU A C     1 
ATOM   2718 O O     . LEU A 1 360 ? 121.050 137.385 140.110 1.00 56.92  ? 445 LEU A O     1 
ATOM   2719 C CB    . LEU A 1 360 ? 119.661 135.216 142.196 1.00 44.51  ? 445 LEU A CB    1 
ATOM   2720 C CG    . LEU A 1 360 ? 119.218 134.564 140.879 1.00 45.26  ? 445 LEU A CG    1 
ATOM   2721 C CD1   . LEU A 1 360 ? 118.476 133.262 141.153 1.00 39.32  ? 445 LEU A CD1   1 
ATOM   2722 C CD2   . LEU A 1 360 ? 118.374 135.488 140.020 1.00 47.69  ? 445 LEU A CD2   1 
ATOM   2723 N N     . LEU A 1 361 ? 119.924 138.347 141.805 1.00 52.48  ? 446 LEU A N     1 
ATOM   2724 C CA    . LEU A 1 361 ? 119.607 139.537 141.022 1.00 50.44  ? 446 LEU A CA    1 
ATOM   2725 C C     . LEU A 1 361 ? 120.871 140.279 140.611 1.00 53.08  ? 446 LEU A C     1 
ATOM   2726 O O     . LEU A 1 361 ? 121.022 140.672 139.449 1.00 59.48  ? 446 LEU A O     1 
ATOM   2727 C CB    . LEU A 1 361 ? 118.682 140.459 141.817 1.00 56.74  ? 446 LEU A CB    1 
ATOM   2728 C CG    . LEU A 1 361 ? 118.340 141.796 141.151 1.00 59.43  ? 446 LEU A CG    1 
ATOM   2729 C CD1   . LEU A 1 361 ? 117.534 141.581 139.878 1.00 56.70  ? 446 LEU A CD1   1 
ATOM   2730 C CD2   . LEU A 1 361 ? 117.606 142.721 142.113 1.00 54.38  ? 446 LEU A CD2   1 
ATOM   2731 N N     . LEU A 1 362 ? 121.791 140.487 141.556 1.00 53.48  ? 447 LEU A N     1 
ATOM   2732 C CA    . LEU A 1 362 ? 123.013 141.217 141.237 1.00 52.04  ? 447 LEU A CA    1 
ATOM   2733 C C     . LEU A 1 362 ? 123.867 140.458 140.229 1.00 51.99  ? 447 LEU A C     1 
ATOM   2734 O O     . LEU A 1 362 ? 124.382 141.053 139.275 1.00 55.43  ? 447 LEU A O     1 
ATOM   2735 C CB    . LEU A 1 362 ? 123.807 141.508 142.511 1.00 57.19  ? 447 LEU A CB    1 
ATOM   2736 C CG    . LEU A 1 362 ? 123.068 142.300 143.591 1.00 60.85  ? 447 LEU A CG    1 
ATOM   2737 C CD1   . LEU A 1 362 ? 123.859 142.317 144.890 1.00 60.34  ? 447 LEU A CD1   1 
ATOM   2738 C CD2   . LEU A 1 362 ? 122.772 143.716 143.117 1.00 59.03  ? 447 LEU A CD2   1 
ATOM   2739 N N     . THR A 1 363 ? 124.016 139.143 140.408 1.00 53.82  ? 448 THR A N     1 
ATOM   2740 C CA    . THR A 1 363 ? 124.802 138.367 139.455 1.00 51.88  ? 448 THR A CA    1 
ATOM   2741 C C     . THR A 1 363 ? 124.146 138.353 138.078 1.00 54.70  ? 448 THR A C     1 
ATOM   2742 O O     . THR A 1 363 ? 124.832 138.459 137.054 1.00 58.35  ? 448 THR A O     1 
ATOM   2743 C CB    . THR A 1 363 ? 125.001 136.946 139.981 1.00 49.18  ? 448 THR A CB    1 
ATOM   2744 O OG1   . THR A 1 363 ? 123.772 136.462 140.535 1.00 50.88  ? 448 THR A OG1   1 
ATOM   2745 C CG2   . THR A 1 363 ? 126.080 136.921 141.053 1.00 46.65  ? 448 THR A CG2   1 
ATOM   2746 N N     . GLY A 1 364 ? 122.816 138.244 138.032 1.00 53.35  ? 449 GLY A N     1 
ATOM   2747 C CA    . GLY A 1 364 ? 122.125 138.238 136.755 1.00 51.35  ? 449 GLY A CA    1 
ATOM   2748 C C     . GLY A 1 364 ? 122.220 139.562 136.023 1.00 56.52  ? 449 GLY A C     1 
ATOM   2749 O O     . GLY A 1 364 ? 122.412 139.591 134.805 1.00 63.96  ? 449 GLY A O     1 
ATOM   2750 N N     . VAL A 1 365 ? 122.079 140.676 136.746 1.00 57.04  ? 450 VAL A N     1 
ATOM   2751 C CA    . VAL A 1 365 ? 122.221 141.971 136.090 1.00 56.92  ? 450 VAL A CA    1 
ATOM   2752 C C     . VAL A 1 365 ? 123.668 142.213 135.678 1.00 60.53  ? 450 VAL A C     1 
ATOM   2753 O O     . VAL A 1 365 ? 123.919 142.834 134.642 1.00 62.17  ? 450 VAL A O     1 
ATOM   2754 C CB    . VAL A 1 365 ? 121.670 143.116 136.966 1.00 52.45  ? 450 VAL A CB    1 
ATOM   2755 C CG1   . VAL A 1 365 ? 120.232 142.831 137.371 1.00 53.16  ? 450 VAL A CG1   1 
ATOM   2756 C CG2   . VAL A 1 365 ? 122.538 143.345 138.192 1.00 51.66  ? 450 VAL A CG2   1 
ATOM   2757 N N     . ALA A 1 366 ? 124.642 141.715 136.448 1.00 57.67  ? 451 ALA A N     1 
ATOM   2758 C CA    . ALA A 1 366 ? 126.035 141.834 136.024 1.00 54.46  ? 451 ALA A CA    1 
ATOM   2759 C C     . ALA A 1 366 ? 126.310 141.019 134.766 1.00 56.64  ? 451 ALA A C     1 
ATOM   2760 O O     . ALA A 1 366 ? 127.098 141.442 133.913 1.00 63.26  ? 451 ALA A O     1 
ATOM   2761 C CB    . ALA A 1 366 ? 126.968 141.400 137.154 1.00 54.27  ? 451 ALA A CB    1 
ATOM   2762 N N     . PHE A 1 367 ? 125.678 139.851 134.642 1.00 55.93  ? 452 PHE A N     1 
ATOM   2763 C CA    . PHE A 1 367 ? 125.821 139.021 133.450 1.00 52.98  ? 452 PHE A CA    1 
ATOM   2764 C C     . PHE A 1 367 ? 125.138 139.659 132.241 1.00 57.30  ? 452 PHE A C     1 
ATOM   2765 O O     . PHE A 1 367 ? 125.699 139.680 131.136 1.00 66.00  ? 452 PHE A O     1 
ATOM   2766 C CB    . PHE A 1 367 ? 125.250 137.632 133.750 1.00 48.38  ? 452 PHE A CB    1 
ATOM   2767 C CG    . PHE A 1 367 ? 125.332 136.664 132.608 1.00 49.85  ? 452 PHE A CG    1 
ATOM   2768 C CD1   . PHE A 1 367 ? 126.549 136.353 132.029 1.00 48.82  ? 452 PHE A CD1   1 
ATOM   2769 C CD2   . PHE A 1 367 ? 124.194 136.022 132.149 1.00 50.29  ? 452 PHE A CD2   1 
ATOM   2770 C CE1   . PHE A 1 367 ? 126.624 135.447 130.989 1.00 48.26  ? 452 PHE A CE1   1 
ATOM   2771 C CE2   . PHE A 1 367 ? 124.263 135.113 131.113 1.00 47.13  ? 452 PHE A CE2   1 
ATOM   2772 C CZ    . PHE A 1 367 ? 125.481 134.823 130.533 1.00 44.90  ? 452 PHE A CZ    1 
ATOM   2773 N N     . PHE A 1 368 ? 123.936 140.205 132.443 1.00 55.38  ? 453 PHE A N     1 
ATOM   2774 C CA    . PHE A 1 368 ? 123.208 140.837 131.349 1.00 58.60  ? 453 PHE A CA    1 
ATOM   2775 C C     . PHE A 1 368 ? 123.852 142.150 130.922 1.00 64.84  ? 453 PHE A C     1 
ATOM   2776 O O     . PHE A 1 368 ? 123.793 142.505 129.743 1.00 73.63  ? 453 PHE A O     1 
ATOM   2777 C CB    . PHE A 1 368 ? 121.748 141.058 131.748 1.00 62.03  ? 453 PHE A CB    1 
ATOM   2778 C CG    . PHE A 1 368 ? 120.952 139.787 131.856 1.00 62.45  ? 453 PHE A CG    1 
ATOM   2779 C CD1   . PHE A 1 368 ? 121.218 138.715 131.019 1.00 60.12  ? 453 PHE A CD1   1 
ATOM   2780 C CD2   . PHE A 1 368 ? 119.938 139.665 132.790 1.00 60.09  ? 453 PHE A CD2   1 
ATOM   2781 C CE1   . PHE A 1 368 ? 120.490 137.545 131.114 1.00 53.78  ? 453 PHE A CE1   1 
ATOM   2782 C CE2   . PHE A 1 368 ? 119.205 138.497 132.890 1.00 56.43  ? 453 PHE A CE2   1 
ATOM   2783 C CZ    . PHE A 1 368 ? 119.482 137.436 132.050 1.00 52.74  ? 453 PHE A CZ    1 
ATOM   2784 N N     . SER A 1 369 ? 124.480 142.874 131.848 1.00 62.76  ? 454 SER A N     1 
ATOM   2785 C CA    . SER A 1 369 ? 125.178 144.111 131.530 1.00 66.70  ? 454 SER A CA    1 
ATOM   2786 C C     . SER A 1 369 ? 126.560 143.859 130.947 1.00 71.77  ? 454 SER A C     1 
ATOM   2787 O O     . SER A 1 369 ? 127.257 144.816 130.593 1.00 80.28  ? 454 SER A O     1 
ATOM   2788 C CB    . SER A 1 369 ? 125.284 144.994 132.777 1.00 66.60  ? 454 SER A CB    1 
ATOM   2789 O OG    . SER A 1 369 ? 123.997 145.356 133.252 1.00 74.05  ? 454 SER A OG    1 
ATOM   2790 N N     . LEU A 1 370 ? 126.977 142.600 130.863 1.00 67.19  ? 455 LEU A N     1 
ATOM   2791 C CA    . LEU A 1 370 ? 128.141 142.199 130.087 1.00 65.55  ? 455 LEU A CA    1 
ATOM   2792 C C     . LEU A 1 370 ? 127.764 141.670 128.715 1.00 66.77  ? 455 LEU A C     1 
ATOM   2793 O O     . LEU A 1 370 ? 128.492 141.902 127.747 1.00 71.07  ? 455 LEU A O     1 
ATOM   2794 C CB    . LEU A 1 370 ? 128.944 141.136 130.847 1.00 61.18  ? 455 LEU A CB    1 
ATOM   2795 C CG    . LEU A 1 370 ? 130.019 140.378 130.067 1.00 59.09  ? 455 LEU A CG    1 
ATOM   2796 C CD1   . LEU A 1 370 ? 131.291 141.207 129.964 1.00 67.17  ? 455 LEU A CD1   1 
ATOM   2797 C CD2   . LEU A 1 370 ? 130.303 139.044 130.723 1.00 52.55  ? 455 LEU A CD2   1 
ATOM   2798 N N     . ILE A 1 371 ? 126.632 140.969 128.611 1.00 66.12  ? 456 ILE A N     1 
ATOM   2799 C CA    . ILE A 1 371 ? 126.129 140.599 127.290 1.00 63.22  ? 456 ILE A CA    1 
ATOM   2800 C C     . ILE A 1 371 ? 125.667 141.831 126.515 1.00 71.22  ? 456 ILE A C     1 
ATOM   2801 O O     . ILE A 1 371 ? 125.825 141.896 125.290 1.00 72.80  ? 456 ILE A O     1 
ATOM   2802 C CB    . ILE A 1 371 ? 125.005 139.553 127.403 1.00 58.47  ? 456 ILE A CB    1 
ATOM   2803 C CG1   . ILE A 1 371 ? 125.441 138.396 128.300 1.00 54.45  ? 456 ILE A CG1   1 
ATOM   2804 C CG2   . ILE A 1 371 ? 124.610 139.034 126.028 1.00 58.26  ? 456 ILE A CG2   1 
ATOM   2805 C CD1   . ILE A 1 371 ? 124.436 137.285 128.363 1.00 55.78  ? 456 ILE A CD1   1 
ATOM   2806 N N     . LEU A 1 372 ? 125.091 142.820 127.202 1.00 72.08  ? 457 LEU A N     1 
ATOM   2807 C CA    . LEU A 1 372 ? 124.594 144.040 126.569 1.00 71.28  ? 457 LEU A CA    1 
ATOM   2808 C C     . LEU A 1 372 ? 125.662 145.123 126.465 1.00 76.42  ? 457 LEU A C     1 
ATOM   2809 O O     . LEU A 1 372 ? 125.968 145.594 125.366 1.00 84.53  ? 457 LEU A O     1 
ATOM   2810 C CB    . LEU A 1 372 ? 123.377 144.579 127.338 1.00 73.60  ? 457 LEU A CB    1 
ATOM   2811 C CG    . LEU A 1 372 ? 122.117 143.719 127.389 1.00 74.01  ? 457 LEU A CG    1 
ATOM   2812 C CD1   . LEU A 1 372 ? 121.203 144.171 128.513 1.00 73.92  ? 457 LEU A CD1   1 
ATOM   2813 C CD2   . LEU A 1 372 ? 121.404 143.834 126.060 1.00 72.27  ? 457 LEU A CD2   1 
ATOM   2814 N N     . PHE A 1 373 ? 126.235 145.534 127.594 1.00 77.82  ? 458 PHE A N     1 
ATOM   2815 C CA    . PHE A 1 373 ? 127.121 146.692 127.655 1.00 84.26  ? 458 PHE A CA    1 
ATOM   2816 C C     . PHE A 1 373 ? 128.567 146.295 127.942 1.00 92.23  ? 458 PHE A C     1 
ATOM   2817 O O     . PHE A 1 373 ? 129.281 146.981 128.676 1.00 104.72 ? 458 PHE A O     1 
ATOM   2818 C CB    . PHE A 1 373 ? 126.624 147.689 128.701 1.00 83.60  ? 458 PHE A CB    1 
ATOM   2819 C CG    . PHE A 1 373 ? 125.129 147.862 128.715 1.00 85.20  ? 458 PHE A CG    1 
ATOM   2820 C CD1   . PHE A 1 373 ? 124.439 148.169 127.553 1.00 84.90  ? 458 PHE A CD1   1 
ATOM   2821 C CD2   . PHE A 1 373 ? 124.413 147.718 129.893 1.00 84.09  ? 458 PHE A CD2   1 
ATOM   2822 C CE1   . PHE A 1 373 ? 123.065 148.328 127.565 1.00 85.38  ? 458 PHE A CE1   1 
ATOM   2823 C CE2   . PHE A 1 373 ? 123.038 147.876 129.911 1.00 86.26  ? 458 PHE A CE2   1 
ATOM   2824 C CZ    . PHE A 1 373 ? 122.364 148.181 128.746 1.00 89.16  ? 458 PHE A CZ    1 
ATOM   2825 N N     . GLY A 1 374 ? 129.015 145.183 127.363 1.00 92.26  ? 459 GLY A N     1 
ATOM   2826 C CA    . GLY A 1 374 ? 130.390 144.747 127.527 1.00 99.48  ? 459 GLY A CA    1 
ATOM   2827 C C     . GLY A 1 374 ? 131.185 144.806 126.238 1.00 110.12 ? 459 GLY A C     1 
ATOM   2828 O O     . GLY A 1 374 ? 132.422 144.822 126.255 1.00 115.64 ? 459 GLY A O     1 
ATOM   2829 N N     . GLY A 1 375 ? 130.477 144.834 125.111 1.00 108.60 ? 460 GLY A N     1 
ATOM   2830 C CA    . GLY A 1 375 ? 131.103 144.957 123.817 1.00 113.71 ? 460 GLY A CA    1 
ATOM   2831 C C     . GLY A 1 375 ? 131.979 146.190 123.731 1.00 119.26 ? 460 GLY A C     1 
ATOM   2832 O O     . GLY A 1 375 ? 133.149 146.119 123.344 1.00 117.27 ? 460 GLY A O     1 
ATOM   2833 N N     . PRO A 1 376 ? 131.423 147.355 124.081 1.00 121.59 ? 461 PRO A N     1 
ATOM   2834 C CA    . PRO A 1 376 ? 132.288 148.531 124.269 1.00 121.79 ? 461 PRO A CA    1 
ATOM   2835 C C     . PRO A 1 376 ? 133.354 148.324 125.331 1.00 121.85 ? 461 PRO A C     1 
ATOM   2836 O O     . PRO A 1 376 ? 134.491 148.780 125.152 1.00 120.21 ? 461 PRO A O     1 
ATOM   2837 C CB    . PRO A 1 376 ? 131.293 149.630 124.664 1.00 119.86 ? 461 PRO A CB    1 
ATOM   2838 C CG    . PRO A 1 376 ? 130.024 149.233 124.004 1.00 118.92 ? 461 PRO A CG    1 
ATOM   2839 C CD    . PRO A 1 376 ? 129.998 147.723 124.007 1.00 116.64 ? 461 PRO A CD    1 
ATOM   2840 N N     . PHE A 1 377 ? 133.027 147.644 126.433 1.00 120.34 ? 462 PHE A N     1 
ATOM   2841 C CA    . PHE A 1 377 ? 134.014 147.412 127.482 1.00 118.33 ? 462 PHE A CA    1 
ATOM   2842 C C     . PHE A 1 377 ? 134.737 146.091 127.254 1.00 114.92 ? 462 PHE A C     1 
ATOM   2843 O O     . PHE A 1 377 ? 134.894 145.282 128.175 1.00 112.00 ? 462 PHE A O     1 
ATOM   2844 C CB    . PHE A 1 377 ? 133.348 147.423 128.859 1.00 118.73 ? 462 PHE A CB    1 
ATOM   2845 C CG    . PHE A 1 377 ? 133.212 148.795 129.459 1.00 126.79 ? 462 PHE A CG    1 
ATOM   2846 C CD1   . PHE A 1 377 ? 132.424 149.758 128.852 1.00 128.19 ? 462 PHE A CD1   1 
ATOM   2847 C CD2   . PHE A 1 377 ? 133.874 149.120 130.632 1.00 129.84 ? 462 PHE A CD2   1 
ATOM   2848 C CE1   . PHE A 1 377 ? 132.299 151.021 129.401 1.00 132.96 ? 462 PHE A CE1   1 
ATOM   2849 C CE2   . PHE A 1 377 ? 133.752 150.382 131.188 1.00 130.06 ? 462 PHE A CE2   1 
ATOM   2850 C CZ    . PHE A 1 377 ? 132.963 151.333 130.570 1.00 131.65 ? 462 PHE A CZ    1 
ATOM   2851 N N     . ALA A 1 378 ? 135.168 145.873 126.018 1.00 115.93 ? 463 ALA A N     1 
ATOM   2852 C CA    . ALA A 1 378 ? 136.044 144.785 125.598 1.00 112.16 ? 463 ALA A CA    1 
ATOM   2853 C C     . ALA A 1 378 ? 137.486 144.922 126.094 1.00 116.58 ? 463 ALA A C     1 
ATOM   2854 O O     . ALA A 1 378 ? 138.172 143.899 126.227 1.00 115.38 ? 463 ALA A O     1 
ATOM   2855 C CB    . ALA A 1 378 ? 136.038 144.672 124.071 1.00 109.27 ? 463 ALA A CB    1 
ATOM   2856 N N     . PRO A 1 379 ? 138.025 146.159 126.305 1.00 121.35 ? 464 PRO A N     1 
ATOM   2857 C CA    . PRO A 1 379 ? 139.379 146.286 126.867 1.00 118.53 ? 464 PRO A CA    1 
ATOM   2858 C C     . PRO A 1 379 ? 139.678 145.372 128.046 1.00 115.18 ? 464 PRO A C     1 
ATOM   2859 O O     . PRO A 1 379 ? 140.687 144.665 128.029 1.00 114.44 ? 464 PRO A O     1 
ATOM   2860 C CB    . PRO A 1 379 ? 139.439 147.762 127.292 1.00 116.48 ? 464 PRO A CB    1 
ATOM   2861 C CG    . PRO A 1 379 ? 138.266 148.448 126.595 1.00 117.03 ? 464 PRO A CG    1 
ATOM   2862 C CD    . PRO A 1 379 ? 137.629 147.436 125.689 1.00 118.71 ? 464 PRO A CD    1 
ATOM   2863 N N     . LEU A 1 380 ? 138.823 145.366 129.072 1.00 113.99 ? 465 LEU A N     1 
ATOM   2864 C CA    . LEU A 1 380 ? 139.084 144.520 130.234 1.00 117.60 ? 465 LEU A CA    1 
ATOM   2865 C C     . LEU A 1 380 ? 138.954 143.041 129.883 1.00 116.38 ? 465 LEU A C     1 
ATOM   2866 O O     . LEU A 1 380 ? 139.689 142.198 130.419 1.00 117.64 ? 465 LEU A O     1 
ATOM   2867 C CB    . LEU A 1 380 ? 138.136 144.890 131.374 1.00 119.23 ? 465 LEU A CB    1 
ATOM   2868 C CG    . LEU A 1 380 ? 138.354 144.163 132.702 1.00 117.85 ? 465 LEU A CG    1 
ATOM   2869 C CD1   . LEU A 1 380 ? 139.732 144.478 133.262 1.00 116.44 ? 465 LEU A CD1   1 
ATOM   2870 C CD2   . LEU A 1 380 ? 137.269 144.530 133.703 1.00 113.59 ? 465 LEU A CD2   1 
ATOM   2871 N N     . VAL A 1 381 ? 138.026 142.710 128.981 1.00 112.25 ? 466 VAL A N     1 
ATOM   2872 C CA    . VAL A 1 381 ? 137.853 141.324 128.556 1.00 109.63 ? 466 VAL A CA    1 
ATOM   2873 C C     . VAL A 1 381 ? 139.135 140.802 127.919 1.00 109.66 ? 466 VAL A C     1 
ATOM   2874 O O     . VAL A 1 381 ? 139.571 139.677 128.192 1.00 105.61 ? 466 VAL A O     1 
ATOM   2875 C CB    . VAL A 1 381 ? 136.651 141.210 127.599 1.00 102.83 ? 466 VAL A CB    1 
ATOM   2876 C CG1   . VAL A 1 381 ? 136.734 139.933 126.776 1.00 94.37  ? 466 VAL A CG1   1 
ATOM   2877 C CG2   . VAL A 1 381 ? 135.344 141.271 128.378 1.00 98.45  ? 466 VAL A CG2   1 
ATOM   2878 N N     . ALA A 1 382 ? 139.765 141.617 127.069 1.00 112.95 ? 467 ALA A N     1 
ATOM   2879 C CA    . ALA A 1 382 ? 141.053 141.236 126.497 1.00 110.79 ? 467 ALA A CA    1 
ATOM   2880 C C     . ALA A 1 382 ? 142.168 141.305 127.533 1.00 111.56 ? 467 ALA A C     1 
ATOM   2881 O O     . ALA A 1 382 ? 143.151 140.562 127.434 1.00 109.34 ? 467 ALA A O     1 
ATOM   2882 C CB    . ALA A 1 382 ? 141.384 142.127 125.301 1.00 107.46 ? 467 ALA A CB    1 
ATOM   2883 N N     . LYS A 1 383 ? 142.033 142.191 128.523 1.00 111.79 ? 468 LYS A N     1 
ATOM   2884 C CA    . LYS A 1 383 ? 143.013 142.268 129.602 1.00 111.44 ? 468 LYS A CA    1 
ATOM   2885 C C     . LYS A 1 383 ? 143.102 140.952 130.358 1.00 111.43 ? 468 LYS A C     1 
ATOM   2886 O O     . LYS A 1 383 ? 144.198 140.505 130.714 1.00 109.73 ? 468 LYS A O     1 
ATOM   2887 C CB    . LYS A 1 383 ? 142.647 143.403 130.558 1.00 114.07 ? 468 LYS A CB    1 
ATOM   2888 C CG    . LYS A 1 383 ? 143.586 143.572 131.744 1.00 116.13 ? 468 LYS A CG    1 
ATOM   2889 C CD    . LYS A 1 383 ? 144.922 144.166 131.337 1.00 118.03 ? 468 LYS A CD    1 
ATOM   2890 C CE    . LYS A 1 383 ? 145.778 144.447 132.562 1.00 110.35 ? 468 LYS A CE    1 
ATOM   2891 N NZ    . LYS A 1 383 ? 147.106 145.011 132.202 1.00 111.75 ? 468 LYS A NZ    1 
ATOM   2892 N N     . LEU A 1 384 ? 141.965 140.321 130.620 1.00 110.79 ? 469 LEU A N     1 
ATOM   2893 C CA    . LEU A 1 384 ? 141.965 139.033 131.303 1.00 108.65 ? 469 LEU A CA    1 
ATOM   2894 C C     . LEU A 1 384 ? 142.287 137.868 130.370 1.00 105.24 ? 469 LEU A C     1 
ATOM   2895 O O     . LEU A 1 384 ? 142.144 136.707 130.776 1.00 102.10 ? 469 LEU A O     1 
ATOM   2896 C CB    . LEU A 1 384 ? 140.617 138.795 131.986 1.00 107.89 ? 469 LEU A CB    1 
ATOM   2897 C CG    . LEU A 1 384 ? 140.413 139.354 133.399 1.00 108.86 ? 469 LEU A CG    1 
ATOM   2898 C CD1   . LEU A 1 384 ? 140.108 140.843 133.342 1.00 108.73 ? 469 LEU A CD1   1 
ATOM   2899 C CD2   . LEU A 1 384 ? 139.312 138.610 134.139 1.00 106.04 ? 469 LEU A CD2   1 
ATOM   2900 N N     . GLY A 1 385 ? 142.736 138.146 129.147 1.00 105.35 ? 470 GLY A N     1 
ATOM   2901 C CA    . GLY A 1 385 ? 143.082 137.100 128.203 1.00 101.40 ? 470 GLY A CA    1 
ATOM   2902 C C     . GLY A 1 385 ? 141.916 136.222 127.800 1.00 98.25  ? 470 GLY A C     1 
ATOM   2903 O O     . GLY A 1 385 ? 142.019 134.990 127.834 1.00 95.02  ? 470 GLY A O     1 
ATOM   2904 N N     . MET A 1 386 ? 140.798 136.843 127.425 1.00 97.89  ? 471 MET A N     1 
ATOM   2905 C CA    . MET A 1 386 ? 139.599 136.109 127.057 1.00 88.64  ? 471 MET A CA    1 
ATOM   2906 C C     . MET A 1 386 ? 138.920 136.795 125.879 1.00 88.58  ? 471 MET A C     1 
ATOM   2907 O O     . MET A 1 386 ? 139.179 137.961 125.571 1.00 91.70  ? 471 MET A O     1 
ATOM   2908 C CB    . MET A 1 386 ? 138.609 136.008 128.223 1.00 82.88  ? 471 MET A CB    1 
ATOM   2909 C CG    . MET A 1 386 ? 139.076 135.178 129.408 1.00 88.22  ? 471 MET A CG    1 
ATOM   2910 S SD    . MET A 1 386 ? 137.798 135.089 130.677 1.00 90.27  ? 471 MET A SD    1 
ATOM   2911 C CE    . MET A 1 386 ? 137.871 136.720 131.384 1.00 87.06  ? 471 MET A CE    1 
ATOM   2912 N N     . THR A 1 387 ? 138.049 136.051 125.217 1.00 83.55  ? 472 THR A N     1 
ATOM   2913 C CA    . THR A 1 387 ? 137.126 136.584 124.232 1.00 76.06  ? 472 THR A CA    1 
ATOM   2914 C C     . THR A 1 387 ? 135.863 137.075 124.923 1.00 75.34  ? 472 THR A C     1 
ATOM   2915 O O     . THR A 1 387 ? 135.572 136.680 126.056 1.00 75.52  ? 472 THR A O     1 
ATOM   2916 C CB    . THR A 1 387 ? 136.768 135.511 123.196 1.00 71.33  ? 472 THR A CB    1 
ATOM   2917 O OG1   . THR A 1 387 ? 136.124 134.407 123.845 1.00 74.46  ? 472 THR A OG1   1 
ATOM   2918 C CG2   . THR A 1 387 ? 138.022 135.014 122.491 1.00 71.85  ? 472 THR A CG2   1 
ATOM   2919 N N     . PRO A 1 388 ? 135.093 137.960 124.284 1.00 72.82  ? 473 PRO A N     1 
ATOM   2920 C CA    . PRO A 1 388 ? 133.807 138.361 124.877 1.00 71.29  ? 473 PRO A CA    1 
ATOM   2921 C C     . PRO A 1 388 ? 132.892 137.186 125.162 1.00 63.38  ? 473 PRO A C     1 
ATOM   2922 O O     . PRO A 1 388 ? 132.213 137.183 126.197 1.00 63.13  ? 473 PRO A O     1 
ATOM   2923 C CB    . PRO A 1 388 ? 133.206 139.302 123.821 1.00 67.77  ? 473 PRO A CB    1 
ATOM   2924 C CG    . PRO A 1 388 ? 134.004 139.057 122.569 1.00 71.81  ? 473 PRO A CG    1 
ATOM   2925 C CD    . PRO A 1 388 ? 135.374 138.707 123.047 1.00 73.06  ? 473 PRO A CD    1 
ATOM   2926 N N     . LEU A 1 389 ? 132.870 136.177 124.293 1.00 63.02  ? 474 LEU A N     1 
ATOM   2927 C CA    . LEU A 1 389 ? 132.075 134.980 124.529 1.00 59.93  ? 474 LEU A CA    1 
ATOM   2928 C C     . LEU A 1 389 ? 132.598 134.154 125.698 1.00 58.10  ? 474 LEU A C     1 
ATOM   2929 O O     . LEU A 1 389 ? 131.808 133.686 126.521 1.00 59.54  ? 474 LEU A O     1 
ATOM   2930 C CB    . LEU A 1 389 ? 132.026 134.122 123.263 1.00 61.92  ? 474 LEU A CB    1 
ATOM   2931 C CG    . LEU A 1 389 ? 131.476 132.710 123.451 1.00 54.70  ? 474 LEU A CG    1 
ATOM   2932 C CD1   . LEU A 1 389 ? 129.972 132.758 123.640 1.00 54.08  ? 474 LEU A CD1   1 
ATOM   2933 C CD2   . LEU A 1 389 ? 131.843 131.840 122.262 1.00 50.86  ? 474 LEU A CD2   1 
ATOM   2934 N N     . LEU A 1 390 ? 133.917 133.964 125.797 1.00 61.56  ? 475 LEU A N     1 
ATOM   2935 C CA    . LEU A 1 390 ? 134.466 133.232 126.936 1.00 59.09  ? 475 LEU A CA    1 
ATOM   2936 C C     . LEU A 1 390 ? 134.280 134.011 128.232 1.00 61.15  ? 475 LEU A C     1 
ATOM   2937 O O     . LEU A 1 390 ? 134.031 133.420 129.292 1.00 62.31  ? 475 LEU A O     1 
ATOM   2938 C CB    . LEU A 1 390 ? 135.944 132.919 126.702 1.00 63.18  ? 475 LEU A CB    1 
ATOM   2939 C CG    . LEU A 1 390 ? 136.605 132.003 127.734 1.00 62.87  ? 475 LEU A CG    1 
ATOM   2940 C CD1   . LEU A 1 390 ? 135.863 130.679 127.830 1.00 57.75  ? 475 LEU A CD1   1 
ATOM   2941 C CD2   . LEU A 1 390 ? 138.070 131.777 127.394 1.00 66.82  ? 475 LEU A CD2   1 
ATOM   2942 N N     . ALA A 1 391 ? 134.406 135.339 128.169 1.00 64.75  ? 476 ALA A N     1 
ATOM   2943 C CA    . ALA A 1 391 ? 134.126 136.162 129.340 1.00 60.35  ? 476 ALA A CA    1 
ATOM   2944 C C     . ALA A 1 391 ? 132.676 136.008 129.778 1.00 54.14  ? 476 ALA A C     1 
ATOM   2945 O O     . ALA A 1 391 ? 132.394 135.878 130.975 1.00 55.83  ? 476 ALA A O     1 
ATOM   2946 C CB    . ALA A 1 391 ? 134.449 137.626 129.045 1.00 66.64  ? 476 ALA A CB    1 
ATOM   2947 N N     . ALA A 1 392 ? 131.744 136.008 128.821 1.00 57.45  ? 477 ALA A N     1 
ATOM   2948 C CA    . ALA A 1 392 ? 130.342 135.778 129.156 1.00 52.46  ? 477 ALA A CA    1 
ATOM   2949 C C     . ALA A 1 392 ? 130.142 134.389 129.748 1.00 47.10  ? 477 ALA A C     1 
ATOM   2950 O O     . ALA A 1 392 ? 129.378 134.219 130.704 1.00 51.70  ? 477 ALA A O     1 
ATOM   2951 C CB    . ALA A 1 392 ? 129.467 135.967 127.917 1.00 53.94  ? 477 ALA A CB    1 
ATOM   2952 N N     . VAL A 1 393 ? 130.826 133.387 129.193 1.00 50.36  ? 478 VAL A N     1 
ATOM   2953 C CA    . VAL A 1 393 ? 130.716 132.022 129.704 1.00 51.27  ? 478 VAL A CA    1 
ATOM   2954 C C     . VAL A 1 393 ? 131.137 131.965 131.166 1.00 48.48  ? 478 VAL A C     1 
ATOM   2955 O O     . VAL A 1 393 ? 130.420 131.425 132.016 1.00 49.88  ? 478 VAL A O     1 
ATOM   2956 C CB    . VAL A 1 393 ? 131.554 131.062 128.840 1.00 50.04  ? 478 VAL A CB    1 
ATOM   2957 C CG1   . VAL A 1 393 ? 131.822 129.767 129.589 1.00 50.82  ? 478 VAL A CG1   1 
ATOM   2958 C CG2   . VAL A 1 393 ? 130.843 130.778 127.530 1.00 48.35  ? 478 VAL A CG2   1 
ATOM   2959 N N     . TYR A 1 394 ? 132.298 132.541 131.485 1.00 49.69  ? 479 TYR A N     1 
ATOM   2960 C CA    . TYR A 1 394 ? 132.788 132.477 132.858 1.00 47.03  ? 479 TYR A CA    1 
ATOM   2961 C C     . TYR A 1 394 ? 131.955 133.335 133.804 1.00 50.17  ? 479 TYR A C     1 
ATOM   2962 O O     . TYR A 1 394 ? 131.739 132.947 134.959 1.00 52.46  ? 479 TYR A O     1 
ATOM   2963 C CB    . TYR A 1 394 ? 134.261 132.882 132.913 1.00 51.65  ? 479 TYR A CB    1 
ATOM   2964 C CG    . TYR A 1 394 ? 135.196 131.808 132.401 1.00 53.93  ? 479 TYR A CG    1 
ATOM   2965 C CD1   . TYR A 1 394 ? 134.880 130.463 132.545 1.00 52.07  ? 479 TYR A CD1   1 
ATOM   2966 C CD2   . TYR A 1 394 ? 136.391 132.136 131.778 1.00 52.58  ? 479 TYR A CD2   1 
ATOM   2967 C CE1   . TYR A 1 394 ? 135.727 129.475 132.082 1.00 52.85  ? 479 TYR A CE1   1 
ATOM   2968 C CE2   . TYR A 1 394 ? 137.247 131.154 131.311 1.00 55.69  ? 479 TYR A CE2   1 
ATOM   2969 C CZ    . TYR A 1 394 ? 136.909 129.826 131.466 1.00 62.51  ? 479 TYR A CZ    1 
ATOM   2970 O OH    . TYR A 1 394 ? 137.756 128.845 131.003 1.00 65.38  ? 479 TYR A OH    1 
ATOM   2971 N N     . VAL A 1 395 ? 131.462 134.487 133.341 1.00 52.00  ? 480 VAL A N     1 
ATOM   2972 C CA    . VAL A 1 395 ? 130.635 135.328 134.201 1.00 44.77  ? 480 VAL A CA    1 
ATOM   2973 C C     . VAL A 1 395 ? 129.302 134.650 134.497 1.00 44.94  ? 480 VAL A C     1 
ATOM   2974 O O     . VAL A 1 395 ? 128.813 134.692 135.629 1.00 48.03  ? 480 VAL A O     1 
ATOM   2975 C CB    . VAL A 1 395 ? 130.448 136.720 133.573 1.00 42.67  ? 480 VAL A CB    1 
ATOM   2976 C CG1   . VAL A 1 395 ? 129.356 137.492 134.295 1.00 46.66  ? 480 VAL A CG1   1 
ATOM   2977 C CG2   . VAL A 1 395 ? 131.755 137.494 133.632 1.00 44.31  ? 480 VAL A CG2   1 
ATOM   2978 N N     . GLY A 1 396 ? 128.696 134.007 133.496 1.00 43.46  ? 481 GLY A N     1 
ATOM   2979 C CA    . GLY A 1 396 ? 127.491 133.234 133.750 1.00 37.08  ? 481 GLY A CA    1 
ATOM   2980 C C     . GLY A 1 396 ? 127.737 132.018 134.621 1.00 42.49  ? 481 GLY A C     1 
ATOM   2981 O O     . GLY A 1 396 ? 126.876 131.637 135.423 1.00 46.09  ? 481 GLY A O     1 
ATOM   2982 N N     . ALA A 1 397 ? 128.905 131.388 134.473 1.00 48.61  ? 482 ALA A N     1 
ATOM   2983 C CA    . ALA A 1 397 ? 129.267 130.285 135.355 1.00 41.94  ? 482 ALA A CA    1 
ATOM   2984 C C     . ALA A 1 397 ? 129.347 130.754 136.800 1.00 44.43  ? 482 ALA A C     1 
ATOM   2985 O O     . ALA A 1 397 ? 128.842 130.087 137.707 1.00 52.44  ? 482 ALA A O     1 
ATOM   2986 C CB    . ALA A 1 397 ? 130.593 129.669 134.909 1.00 40.85  ? 482 ALA A CB    1 
ATOM   2987 N N     . LEU A 1 398 ? 129.974 131.911 137.031 1.00 45.75  ? 483 LEU A N     1 
ATOM   2988 C CA    . LEU A 1 398 ? 129.999 132.483 138.374 1.00 40.27  ? 483 LEU A CA    1 
ATOM   2989 C C     . LEU A 1 398 ? 128.605 132.885 138.840 1.00 43.54  ? 483 LEU A C     1 
ATOM   2990 O O     . LEU A 1 398 ? 128.285 132.737 140.024 1.00 51.95  ? 483 LEU A O     1 
ATOM   2991 C CB    . LEU A 1 398 ? 130.944 133.682 138.427 1.00 46.41  ? 483 LEU A CB    1 
ATOM   2992 C CG    . LEU A 1 398 ? 132.431 133.359 138.281 1.00 54.29  ? 483 LEU A CG    1 
ATOM   2993 C CD1   . LEU A 1 398 ? 133.247 134.635 138.165 1.00 54.00  ? 483 LEU A CD1   1 
ATOM   2994 C CD2   . LEU A 1 398 ? 132.909 132.515 139.453 1.00 50.51  ? 483 LEU A CD2   1 
ATOM   2995 N N     . GLN A 1 399 ? 127.773 133.398 137.931 1.00 46.02  ? 484 GLN A N     1 
ATOM   2996 C CA    . GLN A 1 399 ? 126.383 133.705 138.254 1.00 39.98  ? 484 GLN A CA    1 
ATOM   2997 C C     . GLN A 1 399 ? 125.683 132.488 138.840 1.00 41.70  ? 484 GLN A C     1 
ATOM   2998 O O     . GLN A 1 399 ? 125.110 132.548 139.936 1.00 49.52  ? 484 GLN A O     1 
ATOM   2999 C CB    . GLN A 1 399 ? 125.660 134.180 136.989 1.00 42.91  ? 484 GLN A CB    1 
ATOM   3000 C CG    . GLN A 1 399 ? 124.387 134.982 137.216 1.00 44.29  ? 484 GLN A CG    1 
ATOM   3001 C CD    . GLN A 1 399 ? 123.221 134.119 137.665 1.00 47.70  ? 484 GLN A CD    1 
ATOM   3002 O OE1   . GLN A 1 399 ? 122.992 133.036 137.129 1.00 50.64  ? 484 GLN A OE1   1 
ATOM   3003 N NE2   . GLN A 1 399 ? 122.475 134.599 138.655 1.00 48.52  ? 484 GLN A NE2   1 
ATOM   3004 N N     . ASN A 1 400 ? 125.742 131.364 138.125 1.00 42.94  ? 485 ASN A N     1 
ATOM   3005 C CA    . ASN A 1 400 ? 125.051 130.165 138.585 1.00 41.89  ? 485 ASN A CA    1 
ATOM   3006 C C     . ASN A 1 400 ? 125.715 129.581 139.819 1.00 44.49  ? 485 ASN A C     1 
ATOM   3007 O O     . ASN A 1 400 ? 125.028 129.102 140.724 1.00 51.61  ? 485 ASN A O     1 
ATOM   3008 C CB    . ASN A 1 400 ? 124.981 129.141 137.461 1.00 44.74  ? 485 ASN A CB    1 
ATOM   3009 C CG    . ASN A 1 400 ? 124.048 129.571 136.361 1.00 54.78  ? 485 ASN A CG    1 
ATOM   3010 O OD1   . ASN A 1 400 ? 124.352 129.408 135.188 1.00 63.09  ? 485 ASN A OD1   1 
ATOM   3011 N ND2   . ASN A 1 400 ? 122.896 130.057 136.724 1.00 63.59  ? 485 ASN A ND2   1 
ATOM   3012 N N     . ILE A 1 401 ? 127.045 129.627 139.887 1.00 46.42  ? 486 ILE A N     1 
ATOM   3013 C CA    . ILE A 1 401 ? 127.740 129.110 141.060 1.00 42.17  ? 486 ILE A CA    1 
ATOM   3014 C C     . ILE A 1 401 ? 127.290 129.858 142.303 1.00 44.72  ? 486 ILE A C     1 
ATOM   3015 O O     . ILE A 1 401 ? 126.860 129.250 143.289 1.00 49.80  ? 486 ILE A O     1 
ATOM   3016 C CB    . ILE A 1 401 ? 129.264 129.205 140.865 1.00 45.16  ? 486 ILE A CB    1 
ATOM   3017 C CG1   . ILE A 1 401 ? 129.760 128.070 139.967 1.00 45.33  ? 486 ILE A CG1   1 
ATOM   3018 C CG2   . ILE A 1 401 ? 129.980 129.178 142.205 1.00 46.16  ? 486 ILE A CG2   1 
ATOM   3019 C CD1   . ILE A 1 401 ? 131.204 128.207 139.564 1.00 47.28  ? 486 ILE A CD1   1 
ATOM   3020 N N     . PHE A 1 402 ? 127.336 131.192 142.257 1.00 44.04  ? 487 PHE A N     1 
ATOM   3021 C CA    . PHE A 1 402 ? 126.956 131.988 143.414 1.00 43.95  ? 487 PHE A CA    1 
ATOM   3022 C C     . PHE A 1 402 ? 125.480 131.811 143.743 1.00 46.84  ? 487 PHE A C     1 
ATOM   3023 O O     . PHE A 1 402 ? 125.124 131.553 144.895 1.00 49.47  ? 487 PHE A O     1 
ATOM   3024 C CB    . PHE A 1 402 ? 127.283 133.460 143.166 1.00 51.00  ? 487 PHE A CB    1 
ATOM   3025 C CG    . PHE A 1 402 ? 128.755 133.781 143.204 1.00 57.03  ? 487 PHE A CG    1 
ATOM   3026 C CD1   . PHE A 1 402 ? 129.186 135.095 143.230 1.00 60.76  ? 487 PHE A CD1   1 
ATOM   3027 C CD2   . PHE A 1 402 ? 129.709 132.772 143.226 1.00 56.37  ? 487 PHE A CD2   1 
ATOM   3028 C CE1   . PHE A 1 402 ? 130.539 135.400 143.267 1.00 69.19  ? 487 PHE A CE1   1 
ATOM   3029 C CE2   . PHE A 1 402 ? 131.054 133.068 143.261 1.00 63.36  ? 487 PHE A CE2   1 
ATOM   3030 C CZ    . PHE A 1 402 ? 131.471 134.384 143.284 1.00 68.96  ? 487 PHE A CZ    1 
ATOM   3031 N N     . SER A 1 403 ? 124.610 131.906 142.733 1.00 47.33  ? 488 SER A N     1 
ATOM   3032 C CA    . SER A 1 403 ? 123.175 131.820 142.981 1.00 41.04  ? 488 SER A CA    1 
ATOM   3033 C C     . SER A 1 403 ? 122.786 130.458 143.543 1.00 41.34  ? 488 SER A C     1 
ATOM   3034 O O     . SER A 1 403 ? 122.015 130.371 144.505 1.00 49.49  ? 488 SER A O     1 
ATOM   3035 C CB    . SER A 1 403 ? 122.406 132.108 141.692 1.00 43.57  ? 488 SER A CB    1 
ATOM   3036 O OG    . SER A 1 403 ? 122.657 133.425 141.231 1.00 49.86  ? 488 SER A OG    1 
ATOM   3037 N N     . LYS A 1 404 ? 123.316 129.377 142.964 1.00 43.35  ? 489 LYS A N     1 
ATOM   3038 C CA    . LYS A 1 404 ? 122.910 128.037 143.362 1.00 40.72  ? 489 LYS A CA    1 
ATOM   3039 C C     . LYS A 1 404 ? 123.556 127.605 144.671 1.00 43.39  ? 489 LYS A C     1 
ATOM   3040 O O     . LYS A 1 404 ? 122.907 126.929 145.473 1.00 50.90  ? 489 LYS A O     1 
ATOM   3041 C CB    . LYS A 1 404 ? 123.236 127.046 142.247 1.00 42.86  ? 489 LYS A CB    1 
ATOM   3042 C CG    . LYS A 1 404 ? 122.420 127.283 140.990 1.00 40.22  ? 489 LYS A CG    1 
ATOM   3043 C CD    . LYS A 1 404 ? 121.973 125.998 140.324 1.00 49.15  ? 489 LYS A CD    1 
ATOM   3044 C CE    . LYS A 1 404 ? 121.023 126.306 139.175 1.00 58.07  ? 489 LYS A CE    1 
ATOM   3045 N NZ    . LYS A 1 404 ? 120.027 125.231 138.937 1.00 55.89  ? 489 LYS A NZ    1 
ATOM   3046 N N     . SER A 1 405 ? 124.817 127.976 144.923 1.00 41.07  ? 490 SER A N     1 
ATOM   3047 C CA    . SER A 1 405 ? 125.376 127.766 146.253 1.00 40.21  ? 490 SER A CA    1 
ATOM   3048 C C     . SER A 1 405 ? 124.598 128.553 147.295 1.00 48.92  ? 490 SER A C     1 
ATOM   3049 O O     . SER A 1 405 ? 124.314 128.032 148.383 1.00 57.42  ? 490 SER A O     1 
ATOM   3050 C CB    . SER A 1 405 ? 126.850 128.168 146.275 1.00 44.31  ? 490 SER A CB    1 
ATOM   3051 O OG    . SER A 1 405 ? 127.003 129.576 146.365 1.00 47.42  ? 490 SER A OG    1 
ATOM   3052 N N     . ALA A 1 406 ? 124.217 129.793 146.969 1.00 49.66  ? 491 ALA A N     1 
ATOM   3053 C CA    . ALA A 1 406 ? 123.364 130.575 147.855 1.00 43.62  ? 491 ALA A CA    1 
ATOM   3054 C C     . ALA A 1 406 ? 122.055 129.874 148.131 1.00 48.03  ? 491 ALA A C     1 
ATOM   3055 O O     . ALA A 1 406 ? 121.584 129.848 149.271 1.00 57.78  ? 491 ALA A O     1 
ATOM   3056 C CB    . ALA A 1 406 ? 123.118 131.957 147.245 1.00 44.98  ? 491 ALA A CB    1 
ATOM   3057 N N     . LYS A 1 407 ? 121.452 129.310 147.098 1.00 45.77  ? 492 LYS A N     1 
ATOM   3058 C CA    . LYS A 1 407 ? 120.241 128.514 147.290 1.00 43.26  ? 492 LYS A CA    1 
ATOM   3059 C C     . LYS A 1 407 ? 120.488 127.364 148.259 1.00 49.88  ? 492 LYS A C     1 
ATOM   3060 O O     . LYS A 1 407 ? 119.946 127.350 149.367 1.00 60.60  ? 492 LYS A O     1 
ATOM   3061 C CB    . LYS A 1 407 ? 119.732 127.965 145.958 1.00 40.05  ? 492 LYS A CB    1 
ATOM   3062 C CG    . LYS A 1 407 ? 118.484 127.147 146.113 1.00 43.18  ? 492 LYS A CG    1 
ATOM   3063 C CD    . LYS A 1 407 ? 118.247 126.280 144.920 1.00 47.36  ? 492 LYS A CD    1 
ATOM   3064 C CE    . LYS A 1 407 ? 116.999 125.478 145.124 1.00 48.52  ? 492 LYS A CE    1 
ATOM   3065 N NZ    . LYS A 1 407 ? 116.766 124.527 144.021 1.00 49.42  ? 492 LYS A NZ    1 
ATOM   3066 N N     . TYR A 1 408 ? 121.397 126.452 147.891 1.00 46.32  ? 493 TYR A N     1 
ATOM   3067 C CA    . TYR A 1 408 ? 121.590 125.222 148.655 1.00 47.95  ? 493 TYR A CA    1 
ATOM   3068 C C     . TYR A 1 408 ? 121.977 125.512 150.099 1.00 56.58  ? 493 TYR A C     1 
ATOM   3069 O O     . TYR A 1 408 ? 121.718 124.691 150.988 1.00 64.34  ? 493 TYR A O     1 
ATOM   3070 C CB    . TYR A 1 408 ? 122.674 124.350 148.016 1.00 46.55  ? 493 TYR A CB    1 
ATOM   3071 C CG    . TYR A 1 408 ? 122.510 124.112 146.535 1.00 42.86  ? 493 TYR A CG    1 
ATOM   3072 C CD1   . TYR A 1 408 ? 121.258 123.939 145.966 1.00 42.66  ? 493 TYR A CD1   1 
ATOM   3073 C CD2   . TYR A 1 408 ? 123.623 124.024 145.708 1.00 42.95  ? 493 TYR A CD2   1 
ATOM   3074 C CE1   . TYR A 1 408 ? 121.117 123.719 144.609 1.00 42.14  ? 493 TYR A CE1   1 
ATOM   3075 C CE2   . TYR A 1 408 ? 123.493 123.800 144.354 1.00 43.66  ? 493 TYR A CE2   1 
ATOM   3076 C CZ    . TYR A 1 408 ? 122.238 123.646 143.809 1.00 42.88  ? 493 TYR A CZ    1 
ATOM   3077 O OH    . TYR A 1 408 ? 122.104 123.419 142.458 1.00 46.99  ? 493 TYR A OH    1 
ATOM   3078 N N     . SER A 1 409 ? 122.594 126.669 150.356 1.00 55.05  ? 494 SER A N     1 
ATOM   3079 C CA    . SER A 1 409 ? 123.078 126.991 151.692 1.00 55.11  ? 494 SER A CA    1 
ATOM   3080 C C     . SER A 1 409 ? 122.161 127.895 152.509 1.00 63.96  ? 494 SER A C     1 
ATOM   3081 O O     . SER A 1 409 ? 122.256 127.878 153.740 1.00 77.60  ? 494 SER A O     1 
ATOM   3082 C CB    . SER A 1 409 ? 124.457 127.647 151.596 1.00 57.48  ? 494 SER A CB    1 
ATOM   3083 O OG    . SER A 1 409 ? 124.444 128.666 150.617 1.00 57.83  ? 494 SER A OG    1 
ATOM   3084 N N     . LEU A 1 410 ? 121.301 128.683 151.893 1.00 58.81  ? 495 LEU A N     1 
ATOM   3085 C CA    . LEU A 1 410 ? 120.396 129.486 152.714 1.00 64.28  ? 495 LEU A CA    1 
ATOM   3086 C C     . LEU A 1 410 ? 118.935 129.332 152.334 1.00 67.99  ? 495 LEU A C     1 
ATOM   3087 O O     . LEU A 1 410 ? 118.076 129.324 153.217 1.00 77.74  ? 495 LEU A O     1 
ATOM   3088 C CB    . LEU A 1 410 ? 120.769 130.959 152.617 1.00 64.88  ? 495 LEU A CB    1 
ATOM   3089 C CG    . LEU A 1 410 ? 122.159 131.468 152.977 1.00 63.64  ? 495 LEU A CG    1 
ATOM   3090 C CD1   . LEU A 1 410 ? 122.295 132.786 152.272 1.00 63.73  ? 495 LEU A CD1   1 
ATOM   3091 C CD2   . LEU A 1 410 ? 122.401 131.589 154.502 1.00 73.23  ? 495 LEU A CD2   1 
ATOM   3092 N N     . PHE A 1 411 ? 118.630 129.257 151.039 1.00 58.78  ? 496 PHE A N     1 
ATOM   3093 C CA    . PHE A 1 411 ? 117.248 129.209 150.592 1.00 60.31  ? 496 PHE A CA    1 
ATOM   3094 C C     . PHE A 1 411 ? 116.616 127.870 150.920 1.00 65.73  ? 496 PHE A C     1 
ATOM   3095 O O     . PHE A 1 411 ? 115.499 127.825 151.442 1.00 73.11  ? 496 PHE A O     1 
ATOM   3096 C CB    . PHE A 1 411 ? 117.185 129.492 149.088 1.00 60.65  ? 496 PHE A CB    1 
ATOM   3097 C CG    . PHE A 1 411 ? 115.797 129.409 148.502 1.00 60.86  ? 496 PHE A CG    1 
ATOM   3098 C CD1   . PHE A 1 411 ? 114.966 130.519 148.479 1.00 60.85  ? 496 PHE A CD1   1 
ATOM   3099 C CD2   . PHE A 1 411 ? 115.338 128.227 147.939 1.00 61.37  ? 496 PHE A CD2   1 
ATOM   3100 C CE1   . PHE A 1 411 ? 113.695 130.440 147.933 1.00 62.34  ? 496 PHE A CE1   1 
ATOM   3101 C CE2   . PHE A 1 411 ? 114.071 128.145 147.391 1.00 61.97  ? 496 PHE A CE2   1 
ATOM   3102 C CZ    . PHE A 1 411 ? 113.250 129.252 147.387 1.00 62.78  ? 496 PHE A CZ    1 
ATOM   3103 N N     . ASP A 1 412 ? 117.312 126.775 150.619 1.00 60.75  ? 497 ASP A N     1 
ATOM   3104 C CA    . ASP A 1 412 ? 116.852 125.446 150.994 1.00 65.37  ? 497 ASP A CA    1 
ATOM   3105 C C     . ASP A 1 412 ? 116.819 125.302 152.514 1.00 72.33  ? 497 ASP A C     1 
ATOM   3106 O O     . ASP A 1 412 ? 115.845 124.758 153.048 1.00 79.35  ? 497 ASP A O     1 
ATOM   3107 C CB    . ASP A 1 412 ? 117.725 124.365 150.352 1.00 64.52  ? 497 ASP A CB    1 
ATOM   3108 C CG    . ASP A 1 412 ? 117.454 124.200 148.872 1.00 64.34  ? 497 ASP A CG    1 
ATOM   3109 O OD1   . ASP A 1 412 ? 116.543 124.878 148.352 1.00 70.39  ? 497 ASP A OD1   1 
ATOM   3110 O OD2   . ASP A 1 412 ? 118.155 123.394 148.228 1.00 59.15  ? 497 ASP A OD2   1 
ATOM   3111 N N     . PRO A 1 413 ? 117.855 125.734 153.250 1.00 72.06  ? 498 PRO A N     1 
ATOM   3112 C CA    . PRO A 1 413 ? 117.705 125.778 154.716 1.00 73.01  ? 498 PRO A CA    1 
ATOM   3113 C C     . PRO A 1 413 ? 116.556 126.658 155.180 1.00 75.82  ? 498 PRO A C     1 
ATOM   3114 O O     . PRO A 1 413 ? 115.825 126.269 156.096 1.00 83.81  ? 498 PRO A O     1 
ATOM   3115 C CB    . PRO A 1 413 ? 119.068 126.302 155.182 1.00 69.91  ? 498 PRO A CB    1 
ATOM   3116 C CG    . PRO A 1 413 ? 120.004 125.798 154.165 1.00 66.95  ? 498 PRO A CG    1 
ATOM   3117 C CD    . PRO A 1 413 ? 119.266 125.925 152.860 1.00 67.61  ? 498 PRO A CD    1 
ATOM   3118 N N     . CYS A 1 414 ? 116.358 127.828 154.560 1.00 73.56  ? 499 CYS A N     1 
ATOM   3119 C CA    . CYS A 1 414 ? 115.201 128.654 154.902 1.00 76.56  ? 499 CYS A CA    1 
ATOM   3120 C C     . CYS A 1 414 ? 113.896 127.955 154.556 1.00 81.89  ? 499 CYS A C     1 
ATOM   3121 O O     . CYS A 1 414 ? 112.899 128.105 155.272 1.00 84.93  ? 499 CYS A O     1 
ATOM   3122 C CB    . CYS A 1 414 ? 115.261 130.006 154.186 1.00 76.20  ? 499 CYS A CB    1 
ATOM   3123 S SG    . CYS A 1 414 ? 116.239 131.284 155.003 1.00 85.96  ? 499 CYS A SG    1 
ATOM   3124 N N     . LYS A 1 415 ? 113.880 127.201 153.457 1.00 81.30  ? 500 LYS A N     1 
ATOM   3125 C CA    . LYS A 1 415 ? 112.672 126.483 153.069 1.00 83.93  ? 500 LYS A CA    1 
ATOM   3126 C C     . LYS A 1 415 ? 112.333 125.399 154.084 1.00 89.99  ? 500 LYS A C     1 
ATOM   3127 O O     . LYS A 1 415 ? 111.201 125.326 154.572 1.00 97.55  ? 500 LYS A O     1 
ATOM   3128 C CB    . LYS A 1 415 ? 112.849 125.892 151.671 1.00 82.27  ? 500 LYS A CB    1 
ATOM   3129 C CG    . LYS A 1 415 ? 111.683 125.047 151.191 1.00 85.16  ? 500 LYS A CG    1 
ATOM   3130 C CD    . LYS A 1 415 ? 111.872 124.641 149.738 1.00 80.83  ? 500 LYS A CD    1 
ATOM   3131 C CE    . LYS A 1 415 ? 113.193 123.915 149.535 1.00 79.76  ? 500 LYS A CE    1 
ATOM   3132 N NZ    . LYS A 1 415 ? 113.519 123.748 148.091 1.00 74.33  ? 500 LYS A NZ    1 
ATOM   3133 N N     . GLU A 1 416 ? 113.311 124.562 154.433 1.00 90.21  ? 501 GLU A N     1 
ATOM   3134 C CA    . GLU A 1 416 ? 113.089 123.476 155.378 1.00 92.21  ? 501 GLU A CA    1 
ATOM   3135 C C     . GLU A 1 416 ? 112.991 123.947 156.823 1.00 93.02  ? 501 GLU A C     1 
ATOM   3136 O O     . GLU A 1 416 ? 112.565 123.167 157.682 1.00 94.62  ? 501 GLU A O     1 
ATOM   3137 C CB    . GLU A 1 416 ? 114.200 122.427 155.253 1.00 87.34  ? 501 GLU A CB    1 
ATOM   3138 C CG    . GLU A 1 416 ? 114.397 121.851 153.850 1.00 95.72  ? 501 GLU A CG    1 
ATOM   3139 C CD    . GLU A 1 416 ? 113.275 120.918 153.398 1.00 100.37 ? 501 GLU A CD    1 
ATOM   3140 O OE1   . GLU A 1 416 ? 112.109 121.099 153.812 1.00 101.22 ? 501 GLU A OE1   1 
ATOM   3141 O OE2   . GLU A 1 416 ? 113.567 119.986 152.620 1.00 96.74  ? 501 GLU A OE2   1 
ATOM   3142 N N     . MET A 1 417 ? 113.373 125.190 157.114 1.00 91.08  ? 502 MET A N     1 
ATOM   3143 C CA    . MET A 1 417 ? 113.199 125.774 158.435 1.00 94.03  ? 502 MET A CA    1 
ATOM   3144 C C     . MET A 1 417 ? 111.845 126.469 158.561 1.00 99.13  ? 502 MET A C     1 
ATOM   3145 O O     . MET A 1 417 ? 111.525 127.026 159.616 1.00 102.72 ? 502 MET A O     1 
ATOM   3146 C CB    . MET A 1 417 ? 114.367 126.727 158.725 1.00 92.01  ? 502 MET A CB    1 
ATOM   3147 C CG    . MET A 1 417 ? 114.424 127.350 160.114 1.00 102.48 ? 502 MET A CG    1 
ATOM   3148 S SD    . MET A 1 417 ? 115.851 128.430 160.306 1.00 113.26 ? 502 MET A SD    1 
ATOM   3149 C CE    . MET A 1 417 ? 117.172 127.225 160.372 1.00 105.43 ? 502 MET A CE    1 
ATOM   3150 N N     . ALA A 1 418 ? 111.029 126.411 157.508 1.00 102.77 ? 503 ALA A N     1 
ATOM   3151 C CA    . ALA A 1 418 ? 109.673 126.935 157.544 1.00 105.95 ? 503 ALA A CA    1 
ATOM   3152 C C     . ALA A 1 418 ? 108.600 125.858 157.576 1.00 107.67 ? 503 ALA A C     1 
ATOM   3153 O O     . ALA A 1 418 ? 107.436 126.190 157.818 1.00 109.70 ? 503 ALA A O     1 
ATOM   3154 C CB    . ALA A 1 418 ? 109.417 127.854 156.340 1.00 100.33 ? 503 ALA A CB    1 
ATOM   3155 N N     . TYR A 1 419 ? 108.938 124.591 157.340 1.00 106.43 ? 504 TYR A N     1 
ATOM   3156 C CA    . TYR A 1 419 ? 107.971 123.506 157.437 1.00 114.23 ? 504 TYR A CA    1 
ATOM   3157 C C     . TYR A 1 419 ? 107.855 122.944 158.846 1.00 121.45 ? 504 TYR A C     1 
ATOM   3158 O O     . TYR A 1 419 ? 106.998 122.088 159.088 1.00 123.84 ? 504 TYR A O     1 
ATOM   3159 C CB    . TYR A 1 419 ? 108.327 122.377 156.466 1.00 111.86 ? 504 TYR A CB    1 
ATOM   3160 C CG    . TYR A 1 419 ? 108.007 122.690 155.025 1.00 114.29 ? 504 TYR A CG    1 
ATOM   3161 C CD1   . TYR A 1 419 ? 108.849 123.486 154.265 1.00 111.01 ? 504 TYR A CD1   1 
ATOM   3162 C CD2   . TYR A 1 419 ? 106.851 122.204 154.430 1.00 115.32 ? 504 TYR A CD2   1 
ATOM   3163 C CE1   . TYR A 1 419 ? 108.559 123.780 152.949 1.00 111.24 ? 504 TYR A CE1   1 
ATOM   3164 C CE2   . TYR A 1 419 ? 106.549 122.495 153.116 1.00 111.98 ? 504 TYR A CE2   1 
ATOM   3165 C CZ    . TYR A 1 419 ? 107.408 123.282 152.379 1.00 110.90 ? 504 TYR A CZ    1 
ATOM   3166 O OH    . TYR A 1 419 ? 107.115 123.574 151.069 1.00 109.99 ? 504 TYR A OH    1 
ATOM   3167 N N     . ILE A 1 420 ? 108.696 123.394 159.772 1.00 120.63 ? 505 ILE A N     1 
ATOM   3168 C CA    . ILE A 1 420 ? 108.649 122.909 161.151 1.00 121.75 ? 505 ILE A CA    1 
ATOM   3169 C C     . ILE A 1 420 ? 107.311 123.215 161.830 1.00 123.07 ? 505 ILE A C     1 
ATOM   3170 O O     . ILE A 1 420 ? 106.812 122.344 162.557 1.00 125.57 ? 505 ILE A O     1 
ATOM   3171 C CB    . ILE A 1 420 ? 109.859 123.410 161.969 1.00 120.38 ? 505 ILE A CB    1 
ATOM   3172 C CG1   . ILE A 1 420 ? 109.923 124.934 162.098 1.00 118.82 ? 505 ILE A CG1   1 
ATOM   3173 C CG2   . ILE A 1 420 ? 111.159 122.898 161.360 1.00 113.84 ? 505 ILE A CG2   1 
ATOM   3174 C CD1   . ILE A 1 420 ? 110.961 125.434 163.082 1.00 119.13 ? 505 ILE A CD1   1 
ATOM   3175 N N     . PRO A 1 421 ? 106.658 124.420 161.650 1.00 124.12 ? 506 PRO A N     1 
ATOM   3176 C CA    . PRO A 1 421 ? 105.431 124.719 162.399 1.00 126.42 ? 506 PRO A CA    1 
ATOM   3177 C C     . PRO A 1 421 ? 104.157 124.326 161.655 1.00 128.25 ? 506 PRO A C     1 
ATOM   3178 O O     . PRO A 1 421 ? 103.242 125.140 161.478 1.00 125.95 ? 506 PRO A O     1 
ATOM   3179 C CB    . PRO A 1 421 ? 105.519 126.236 162.582 1.00 118.90 ? 506 PRO A CB    1 
ATOM   3180 C CG    . PRO A 1 421 ? 106.107 126.679 161.302 1.00 119.51 ? 506 PRO A CG    1 
ATOM   3181 C CD    . PRO A 1 421 ? 107.057 125.601 160.856 1.00 120.63 ? 506 PRO A CD    1 
ATOM   3182 N N     . LEU A 1 422 ? 104.086 123.077 161.204 1.00 129.64 ? 507 LEU A N     1 
ATOM   3183 C CA    . LEU A 1 422 ? 102.943 122.635 160.415 1.00 132.15 ? 507 LEU A CA    1 
ATOM   3184 C C     . LEU A 1 422 ? 102.378 121.330 160.954 1.00 138.82 ? 507 LEU A C     1 
ATOM   3185 O O     . LEU A 1 422 ? 102.828 120.833 161.991 1.00 142.23 ? 507 LEU A O     1 
ATOM   3186 C CB    . LEU A 1 422 ? 103.344 122.457 158.947 1.00 128.40 ? 507 LEU A CB    1 
ATOM   3187 C CG    . LEU A 1 422 ? 103.716 123.700 158.139 1.00 123.42 ? 507 LEU A CG    1 
ATOM   3188 C CD1   . LEU A 1 422 ? 104.185 123.304 156.747 1.00 118.72 ? 507 LEU A CD1   1 
ATOM   3189 C CD2   . LEU A 1 422 ? 102.545 124.665 158.058 1.00 121.23 ? 507 LEU A CD2   1 
ATOM   3190 N N     . ASP A 1 423 ? 101.385 120.777 160.265 1.00 140.18 ? 508 ASP A N     1 
ATOM   3191 C CA    . ASP A 1 423 ? 100.974 119.411 160.531 1.00 142.42 ? 508 ASP A CA    1 
ATOM   3192 C C     . ASP A 1 423 ? 102.016 118.449 159.963 1.00 141.37 ? 508 ASP A C     1 
ATOM   3193 O O     . ASP A 1 423 ? 102.828 118.807 159.106 1.00 138.50 ? 508 ASP A O     1 
ATOM   3194 C CB    . ASP A 1 423 ? 99.597  119.131 159.927 1.00 143.36 ? 508 ASP A CB    1 
ATOM   3195 C CG    . ASP A 1 423 ? 98.494  119.945 160.577 1.00 145.57 ? 508 ASP A CG    1 
ATOM   3196 O OD1   . ASP A 1 423 ? 98.639  120.308 161.763 1.00 145.34 ? 508 ASP A OD1   1 
ATOM   3197 O OD2   . ASP A 1 423 ? 97.482  120.223 159.900 1.00 144.11 ? 508 ASP A OD2   1 
ATOM   3198 N N     . GLU A 1 424 ? 101.997 117.213 160.454 1.00 146.12 ? 509 GLU A N     1 
ATOM   3199 C CA    . GLU A 1 424 ? 102.957 116.208 160.020 1.00 149.27 ? 509 GLU A CA    1 
ATOM   3200 C C     . GLU A 1 424 ? 102.505 115.449 158.780 1.00 146.83 ? 509 GLU A C     1 
ATOM   3201 O O     . GLU A 1 424 ? 103.273 114.637 158.255 1.00 145.83 ? 509 GLU A O     1 
ATOM   3202 C CB    . GLU A 1 424 ? 103.244 115.222 161.155 1.00 153.34 ? 509 GLU A CB    1 
ATOM   3203 C CG    . GLU A 1 424 ? 102.023 114.484 161.654 1.00 157.39 ? 509 GLU A CG    1 
ATOM   3204 C CD    . GLU A 1 424 ? 101.424 115.130 162.883 1.00 161.73 ? 509 GLU A CD    1 
ATOM   3205 O OE1   . GLU A 1 424 ? 101.565 116.362 163.041 1.00 157.59 ? 509 GLU A OE1   1 
ATOM   3206 O OE2   . GLU A 1 424 ? 100.815 114.405 163.695 1.00 166.54 ? 509 GLU A OE2   1 
ATOM   3207 N N     . ASP A 1 425 ? 101.282 115.685 158.303 1.00 145.56 ? 510 ASP A N     1 
ATOM   3208 C CA    . ASP A 1 425 ? 100.837 115.129 157.034 1.00 146.97 ? 510 ASP A CA    1 
ATOM   3209 C C     . ASP A 1 425 ? 100.666 116.169 155.941 1.00 140.99 ? 510 ASP A C     1 
ATOM   3210 O O     . ASP A 1 425 ? 100.720 115.809 154.761 1.00 137.40 ? 510 ASP A O     1 
ATOM   3211 C CB    . ASP A 1 425 ? 99.516  114.366 157.208 1.00 154.86 ? 510 ASP A CB    1 
ATOM   3212 C CG    . ASP A 1 425 ? 99.708  113.021 157.877 1.00 158.15 ? 510 ASP A CG    1 
ATOM   3213 O OD1   . ASP A 1 425 ? 100.789 112.420 157.699 1.00 156.10 ? 510 ASP A OD1   1 
ATOM   3214 O OD2   . ASP A 1 425 ? 98.780  112.561 158.573 1.00 157.51 ? 510 ASP A OD2   1 
ATOM   3215 N N     . THR A 1 426 ? 100.457 117.440 156.293 1.00 140.42 ? 511 THR A N     1 
ATOM   3216 C CA    . THR A 1 426 ? 100.505 118.473 155.267 1.00 137.06 ? 511 THR A CA    1 
ATOM   3217 C C     . THR A 1 426 ? 101.915 118.607 154.708 1.00 132.91 ? 511 THR A C     1 
ATOM   3218 O O     . THR A 1 426 ? 102.088 118.754 153.498 1.00 128.61 ? 511 THR A O     1 
ATOM   3219 C CB    . THR A 1 426 ? 99.994  119.814 155.809 1.00 133.51 ? 511 THR A CB    1 
ATOM   3220 O OG1   . THR A 1 426 ? 99.937  120.768 154.741 1.00 125.35 ? 511 THR A OG1   1 
ATOM   3221 C CG2   . THR A 1 426 ? 100.894 120.360 156.908 1.00 133.64 ? 511 THR A CG2   1 
ATOM   3222 N N     . LYS A 1 427 ? 102.936 118.510 155.566 1.00 134.91 ? 512 LYS A N     1 
ATOM   3223 C CA    . LYS A 1 427 ? 104.309 118.692 155.107 1.00 129.70 ? 512 LYS A CA    1 
ATOM   3224 C C     . LYS A 1 427 ? 104.754 117.574 154.171 1.00 129.68 ? 512 LYS A C     1 
ATOM   3225 O O     . LYS A 1 427 ? 105.400 117.852 153.154 1.00 127.29 ? 512 LYS A O     1 
ATOM   3226 C CB    . LYS A 1 427 ? 105.253 118.814 156.309 1.00 128.29 ? 512 LYS A CB    1 
ATOM   3227 C CG    . LYS A 1 427 ? 105.516 117.515 157.066 1.00 130.79 ? 512 LYS A CG    1 
ATOM   3228 C CD    . LYS A 1 427 ? 106.092 117.766 158.454 1.00 132.66 ? 512 LYS A CD    1 
ATOM   3229 C CE    . LYS A 1 427 ? 107.124 118.881 158.446 1.00 126.24 ? 512 LYS A CE    1 
ATOM   3230 N NZ    . LYS A 1 427 ? 107.576 119.224 159.823 1.00 120.26 ? 512 LYS A NZ    1 
ATOM   3231 N N     . VAL A 1 428 ? 104.374 116.326 154.462 1.00 131.69 ? 513 VAL A N     1 
ATOM   3232 C CA    . VAL A 1 428 ? 104.890 115.183 153.711 1.00 129.40 ? 513 VAL A CA    1 
ATOM   3233 C C     . VAL A 1 428 ? 104.494 115.277 152.243 1.00 126.49 ? 513 VAL A C     1 
ATOM   3234 O O     . VAL A 1 428 ? 105.337 115.153 151.347 1.00 124.02 ? 513 VAL A O     1 
ATOM   3235 C CB    . VAL A 1 428 ? 104.399 113.867 154.341 1.00 130.33 ? 513 VAL A CB    1 
ATOM   3236 C CG1   . VAL A 1 428 ? 104.715 112.690 153.431 1.00 123.24 ? 513 VAL A CG1   1 
ATOM   3237 C CG2   . VAL A 1 428 ? 105.026 113.670 155.711 1.00 132.22 ? 513 VAL A CG2   1 
ATOM   3238 N N     . LYS A 1 429 ? 103.210 115.500 151.976 1.00 123.38 ? 514 LYS A N     1 
ATOM   3239 C CA    . LYS A 1 429 ? 102.710 115.606 150.614 1.00 119.74 ? 514 LYS A CA    1 
ATOM   3240 C C     . LYS A 1 429 ? 102.627 117.058 150.153 1.00 119.38 ? 514 LYS A C     1 
ATOM   3241 O O     . LYS A 1 429 ? 102.157 117.325 149.042 1.00 118.81 ? 514 LYS A O     1 
ATOM   3242 C CB    . LYS A 1 429 ? 101.349 114.908 150.508 1.00 118.60 ? 514 LYS A CB    1 
ATOM   3243 C CG    . LYS A 1 429 ? 100.872 114.615 149.090 1.00 117.32 ? 514 LYS A CG    1 
ATOM   3244 C CD    . LYS A 1 429 ? 99.581  113.815 149.101 1.00 115.05 ? 514 LYS A CD    1 
ATOM   3245 C CE    . LYS A 1 429 ? 99.840  112.375 149.517 1.00 114.27 ? 514 LYS A CE    1 
ATOM   3246 N NZ    . LYS A 1 429 ? 98.610  111.539 149.455 1.00 116.63 ? 514 LYS A NZ    1 
ATOM   3247 N N     . GLY A 1 430 ? 103.097 117.998 150.970 1.00 119.93 ? 515 GLY A N     1 
ATOM   3248 C CA    . GLY A 1 430 ? 103.126 119.388 150.585 1.00 113.54 ? 515 GLY A CA    1 
ATOM   3249 C C     . GLY A 1 430 ? 104.475 119.827 150.072 1.00 106.82 ? 515 GLY A C     1 
ATOM   3250 O O     . GLY A 1 430 ? 104.535 120.543 149.079 1.00 103.44 ? 515 GLY A O     1 
ATOM   3251 N N     . LYS A 1 431 ? 105.567 119.410 150.712 1.00 109.15 ? 516 LYS A N     1 
ATOM   3252 C CA    . LYS A 1 431 ? 106.880 119.711 150.158 1.00 106.50 ? 516 LYS A CA    1 
ATOM   3253 C C     . LYS A 1 431 ? 107.375 118.634 149.202 1.00 105.47 ? 516 LYS A C     1 
ATOM   3254 O O     . LYS A 1 431 ? 108.464 118.779 148.640 1.00 104.35 ? 516 LYS A O     1 
ATOM   3255 C CB    . LYS A 1 431 ? 107.901 119.960 151.272 1.00 111.59 ? 516 LYS A CB    1 
ATOM   3256 C CG    . LYS A 1 431 ? 108.248 118.780 152.148 1.00 112.50 ? 516 LYS A CG    1 
ATOM   3257 C CD    . LYS A 1 431 ? 109.252 119.217 153.206 1.00 109.73 ? 516 LYS A CD    1 
ATOM   3258 C CE    . LYS A 1 431 ? 109.582 118.098 154.173 1.00 112.60 ? 516 LYS A CE    1 
ATOM   3259 N NZ    . LYS A 1 431 ? 108.435 117.817 155.080 1.00 119.35 ? 516 LYS A NZ    1 
ATOM   3260 N N     . ALA A 1 432 ? 106.613 117.555 149.016 1.00 107.64 ? 517 ALA A N     1 
ATOM   3261 C CA    . ALA A 1 432 ? 106.754 116.772 147.794 1.00 102.41 ? 517 ALA A CA    1 
ATOM   3262 C C     . ALA A 1 432 ? 106.125 117.516 146.624 1.00 97.44  ? 517 ALA A C     1 
ATOM   3263 O O     . ALA A 1 432 ? 106.720 117.617 145.545 1.00 96.21  ? 517 ALA A O     1 
ATOM   3264 C CB    . ALA A 1 432 ? 106.116 115.393 147.968 1.00 100.05 ? 517 ALA A CB    1 
ATOM   3265 N N     . ALA A 1 433 ? 104.925 118.062 146.841 1.00 100.68 ? 518 ALA A N     1 
ATOM   3266 C CA    . ALA A 1 433 ? 104.273 118.888 145.833 1.00 98.71  ? 518 ALA A CA    1 
ATOM   3267 C C     . ALA A 1 433 ? 105.120 120.104 145.491 1.00 92.68  ? 518 ALA A C     1 
ATOM   3268 O O     . ALA A 1 433 ? 105.372 120.391 144.317 1.00 86.25  ? 518 ALA A O     1 
ATOM   3269 C CB    . ALA A 1 433 ? 102.901 119.330 146.337 1.00 103.95 ? 518 ALA A CB    1 
ATOM   3270 N N     . ILE A 1 434 ? 105.581 120.822 146.516 1.00 94.42  ? 519 ILE A N     1 
ATOM   3271 C CA    . ILE A 1 434 ? 106.324 122.059 146.308 1.00 89.63  ? 519 ILE A CA    1 
ATOM   3272 C C     . ILE A 1 434 ? 107.538 121.787 145.437 1.00 86.51  ? 519 ILE A C     1 
ATOM   3273 O O     . ILE A 1 434 ? 107.725 122.416 144.395 1.00 86.92  ? 519 ILE A O     1 
ATOM   3274 C CB    . ILE A 1 434 ? 106.722 122.676 147.660 1.00 90.15  ? 519 ILE A CB    1 
ATOM   3275 C CG1   . ILE A 1 434 ? 105.530 123.401 148.284 1.00 89.96  ? 519 ILE A CG1   1 
ATOM   3276 C CG2   . ILE A 1 434 ? 107.894 123.629 147.493 1.00 83.86  ? 519 ILE A CG2   1 
ATOM   3277 C CD1   . ILE A 1 434 ? 105.104 124.630 147.538 1.00 83.10  ? 519 ILE A CD1   1 
ATOM   3278 N N     . ASP A 1 435 ? 108.327 120.779 145.802 1.00 89.51  ? 520 ASP A N     1 
ATOM   3279 C CA    . ASP A 1 435 ? 109.471 120.413 144.978 1.00 89.64  ? 520 ASP A CA    1 
ATOM   3280 C C     . ASP A 1 435 ? 109.027 120.049 143.564 1.00 88.05  ? 520 ASP A C     1 
ATOM   3281 O O     . ASP A 1 435 ? 109.289 120.795 142.609 1.00 93.03  ? 520 ASP A O     1 
ATOM   3282 C CB    . ASP A 1 435 ? 110.230 119.258 145.633 1.00 89.35  ? 520 ASP A CB    1 
ATOM   3283 C CG    . ASP A 1 435 ? 110.912 119.670 146.924 1.00 95.26  ? 520 ASP A CG    1 
ATOM   3284 O OD1   . ASP A 1 435 ? 111.218 120.871 147.078 1.00 91.71  ? 520 ASP A OD1   1 
ATOM   3285 O OD2   . ASP A 1 435 ? 111.135 118.797 147.788 1.00 93.73  ? 520 ASP A OD2   1 
ATOM   3286 N N     . VAL A 1 436 ? 108.260 118.960 143.434 1.00 87.28  ? 521 VAL A N     1 
ATOM   3287 C CA    . VAL A 1 436 ? 108.039 118.317 142.141 1.00 83.83  ? 521 VAL A CA    1 
ATOM   3288 C C     . VAL A 1 436 ? 107.313 119.230 141.158 1.00 86.10  ? 521 VAL A C     1 
ATOM   3289 O O     . VAL A 1 436 ? 107.564 119.166 139.949 1.00 82.32  ? 521 VAL A O     1 
ATOM   3290 C CB    . VAL A 1 436 ? 107.285 116.986 142.345 1.00 80.88  ? 521 VAL A CB    1 
ATOM   3291 C CG1   . VAL A 1 436 ? 106.926 116.351 141.011 1.00 76.58  ? 521 VAL A CG1   1 
ATOM   3292 C CG2   . VAL A 1 436 ? 108.128 116.027 143.168 1.00 74.43  ? 521 VAL A CG2   1 
ATOM   3293 N N     . VAL A 1 437 ? 106.401 120.080 141.633 1.00 85.91  ? 522 VAL A N     1 
ATOM   3294 C CA    . VAL A 1 437 ? 105.661 120.942 140.717 1.00 81.72  ? 522 VAL A CA    1 
ATOM   3295 C C     . VAL A 1 437 ? 105.791 122.409 141.118 1.00 79.13  ? 522 VAL A C     1 
ATOM   3296 O O     . VAL A 1 437 ? 104.864 123.200 140.915 1.00 85.65  ? 522 VAL A O     1 
ATOM   3297 C CB    . VAL A 1 437 ? 104.180 120.518 140.614 1.00 88.66  ? 522 VAL A CB    1 
ATOM   3298 C CG1   . VAL A 1 437 ? 104.069 119.084 140.121 1.00 76.69  ? 522 VAL A CG1   1 
ATOM   3299 C CG2   . VAL A 1 437 ? 103.462 120.676 141.948 1.00 90.95  ? 522 VAL A CG2   1 
ATOM   3300 N N     . CYS A 1 438 ? 106.935 122.788 141.694 1.00 76.75  ? 523 CYS A N     1 
ATOM   3301 C CA    . CYS A 1 438 ? 107.228 124.202 141.876 1.00 73.24  ? 523 CYS A CA    1 
ATOM   3302 C C     . CYS A 1 438 ? 108.648 124.522 141.430 1.00 72.81  ? 523 CYS A C     1 
ATOM   3303 O O     . CYS A 1 438 ? 108.922 125.650 141.009 1.00 69.24  ? 523 CYS A O     1 
ATOM   3304 C CB    . CYS A 1 438 ? 107.020 124.613 143.335 1.00 72.21  ? 523 CYS A CB    1 
ATOM   3305 S SG    . CYS A 1 438 ? 105.298 124.555 143.884 1.00 85.37  ? 523 CYS A SG    1 
ATOM   3306 N N     . ASN A 1 439 ? 109.570 123.550 141.514 1.00 74.19  ? 524 ASN A N     1 
ATOM   3307 C CA    . ASN A 1 439 ? 110.856 123.753 140.849 1.00 74.05  ? 524 ASN A CA    1 
ATOM   3308 C C     . ASN A 1 439 ? 110.693 123.642 139.339 1.00 70.90  ? 524 ASN A C     1 
ATOM   3309 O O     . ASN A 1 439 ? 111.077 124.588 138.624 1.00 68.19  ? 524 ASN A O     1 
ATOM   3310 C CB    . ASN A 1 439 ? 111.903 122.784 141.409 1.00 77.03  ? 524 ASN A CB    1 
ATOM   3311 C CG    . ASN A 1 439 ? 113.253 122.928 140.734 1.00 79.05  ? 524 ASN A CG    1 
ATOM   3312 O OD1   . ASN A 1 439 ? 113.477 122.391 139.648 1.00 74.75  ? 524 ASN A OD1   1 
ATOM   3313 N ND2   . ASN A 1 439 ? 114.162 123.652 141.375 1.00 75.19  ? 524 ASN A ND2   1 
ATOM   3314 N N     . PRO A 1 440 ? 110.118 122.565 138.787 1.00 71.28  ? 525 PRO A N     1 
ATOM   3315 C CA    . PRO A 1 440 ? 109.746 122.608 137.368 1.00 68.21  ? 525 PRO A CA    1 
ATOM   3316 C C     . PRO A 1 440 ? 108.745 123.698 137.049 1.00 61.16  ? 525 PRO A C     1 
ATOM   3317 O O     . PRO A 1 440 ? 108.815 124.263 135.959 1.00 63.11  ? 525 PRO A O     1 
ATOM   3318 C CB    . PRO A 1 440 ? 109.167 121.209 137.114 1.00 67.51  ? 525 PRO A CB    1 
ATOM   3319 C CG    . PRO A 1 440 ? 109.791 120.360 138.154 1.00 75.80  ? 525 PRO A CG    1 
ATOM   3320 C CD    . PRO A 1 440 ? 109.827 121.240 139.363 1.00 71.75  ? 525 PRO A CD    1 
ATOM   3321 N N     . LEU A 1 441 ? 107.829 124.031 137.962 1.00 59.89  ? 526 LEU A N     1 
ATOM   3322 C CA    . LEU A 1 441 ? 106.873 125.099 137.676 1.00 53.33  ? 526 LEU A CA    1 
ATOM   3323 C C     . LEU A 1 441 ? 107.565 126.451 137.548 1.00 53.25  ? 526 LEU A C     1 
ATOM   3324 O O     . LEU A 1 441 ? 107.271 127.218 136.625 1.00 57.87  ? 526 LEU A O     1 
ATOM   3325 C CB    . LEU A 1 441 ? 105.795 125.159 138.756 1.00 61.16  ? 526 LEU A CB    1 
ATOM   3326 C CG    . LEU A 1 441 ? 104.732 126.248 138.588 1.00 60.98  ? 526 LEU A CG    1 
ATOM   3327 C CD1   . LEU A 1 441 ? 103.845 125.958 137.386 1.00 57.63  ? 526 LEU A CD1   1 
ATOM   3328 C CD2   . LEU A 1 441 ? 103.897 126.390 139.853 1.00 53.60  ? 526 LEU A CD2   1 
ATOM   3329 N N     . GLY A 1 442 ? 108.480 126.767 138.465 1.00 53.55  ? 527 GLY A N     1 
ATOM   3330 C CA    . GLY A 1 442 ? 109.192 128.033 138.367 1.00 49.24  ? 527 GLY A CA    1 
ATOM   3331 C C     . GLY A 1 442 ? 110.101 128.093 137.154 1.00 47.66  ? 527 GLY A C     1 
ATOM   3332 O O     . GLY A 1 442 ? 110.119 129.089 136.415 1.00 47.51  ? 527 GLY A O     1 
ATOM   3333 N N     . LYS A 1 443 ? 110.863 127.020 136.922 1.00 53.73  ? 528 LYS A N     1 
ATOM   3334 C CA    . LYS A 1 443 ? 111.726 127.007 135.750 1.00 48.81  ? 528 LYS A CA    1 
ATOM   3335 C C     . LYS A 1 443 ? 110.915 127.014 134.461 1.00 49.74  ? 528 LYS A C     1 
ATOM   3336 O O     . LYS A 1 443 ? 111.358 127.582 133.462 1.00 52.49  ? 528 LYS A O     1 
ATOM   3337 C CB    . LYS A 1 443 ? 112.677 125.812 135.805 1.00 51.40  ? 528 LYS A CB    1 
ATOM   3338 C CG    . LYS A 1 443 ? 113.836 126.023 136.769 1.00 51.14  ? 528 LYS A CG    1 
ATOM   3339 C CD    . LYS A 1 443 ? 114.854 124.899 136.699 1.00 59.50  ? 528 LYS A CD    1 
ATOM   3340 C CE    . LYS A 1 443 ? 115.733 124.885 137.940 1.00 59.87  ? 528 LYS A CE    1 
ATOM   3341 N NZ    . LYS A 1 443 ? 116.198 123.514 138.284 1.00 58.74  ? 528 LYS A NZ    1 
ATOM   3342 N N     . SER A 1 444 ? 109.706 126.450 134.478 1.00 52.22  ? 529 SER A N     1 
ATOM   3343 C CA    . SER A 1 444 ? 108.841 126.471 133.308 1.00 43.93  ? 529 SER A CA    1 
ATOM   3344 C C     . SER A 1 444 ? 108.185 127.827 133.106 1.00 44.89  ? 529 SER A C     1 
ATOM   3345 O O     . SER A 1 444 ? 107.914 128.203 131.968 1.00 50.66  ? 529 SER A O     1 
ATOM   3346 C CB    . SER A 1 444 ? 107.771 125.384 133.424 1.00 43.88  ? 529 SER A CB    1 
ATOM   3347 O OG    . SER A 1 444 ? 108.349 124.137 133.767 1.00 53.10  ? 529 SER A OG    1 
ATOM   3348 N N     . GLY A 1 445 ? 107.913 128.569 134.179 1.00 45.04  ? 530 GLY A N     1 
ATOM   3349 C CA    . GLY A 1 445 ? 107.467 129.944 134.009 1.00 39.85  ? 530 GLY A CA    1 
ATOM   3350 C C     . GLY A 1 445 ? 108.543 130.811 133.382 1.00 45.57  ? 530 GLY A C     1 
ATOM   3351 O O     . GLY A 1 445 ? 108.284 131.572 132.439 1.00 51.48  ? 530 GLY A O     1 
ATOM   3352 N N     . GLY A 1 446 ? 109.774 130.690 133.884 1.00 45.89  ? 531 GLY A N     1 
ATOM   3353 C CA    . GLY A 1 446 ? 110.884 131.386 133.249 1.00 40.16  ? 531 GLY A CA    1 
ATOM   3354 C C     . GLY A 1 446 ? 111.087 130.951 131.809 1.00 46.74  ? 531 GLY A C     1 
ATOM   3355 O O     . GLY A 1 446 ? 111.347 131.774 130.925 1.00 56.07  ? 531 GLY A O     1 
ATOM   3356 N N     . ALA A 1 447 ? 110.949 129.649 131.552 1.00 51.91  ? 532 ALA A N     1 
ATOM   3357 C CA    . ALA A 1 447 ? 111.093 129.115 130.205 1.00 44.01  ? 532 ALA A CA    1 
ATOM   3358 C C     . ALA A 1 447 ? 109.980 129.602 129.288 1.00 44.75  ? 532 ALA A C     1 
ATOM   3359 O O     . ALA A 1 447 ? 110.214 129.845 128.103 1.00 54.46  ? 532 ALA A O     1 
ATOM   3360 C CB    . ALA A 1 447 ? 111.119 127.589 130.262 1.00 43.26  ? 532 ALA A CB    1 
ATOM   3361 N N     . LEU A 1 448 ? 108.759 129.729 129.810 1.00 41.68  ? 533 LEU A N     1 
ATOM   3362 C CA    . LEU A 1 448 ? 107.655 130.269 129.026 1.00 39.96  ? 533 LEU A CA    1 
ATOM   3363 C C     . LEU A 1 448 ? 107.907 131.722 128.661 1.00 45.09  ? 533 LEU A C     1 
ATOM   3364 O O     . LEU A 1 448 ? 107.645 132.136 127.526 1.00 50.54  ? 533 LEU A O     1 
ATOM   3365 C CB    . LEU A 1 448 ? 106.345 130.130 129.801 1.00 39.54  ? 533 LEU A CB    1 
ATOM   3366 C CG    . LEU A 1 448 ? 105.048 130.384 129.029 1.00 45.69  ? 533 LEU A CG    1 
ATOM   3367 C CD1   . LEU A 1 448 ? 104.573 129.121 128.333 1.00 48.55  ? 533 LEU A CD1   1 
ATOM   3368 C CD2   . LEU A 1 448 ? 103.971 130.926 129.957 1.00 42.19  ? 533 LEU A CD2   1 
ATOM   3369 N N     . ILE A 1 449 ? 108.420 132.508 129.610 1.00 45.05  ? 534 ILE A N     1 
ATOM   3370 C CA    . ILE A 1 449 ? 108.800 133.885 129.299 1.00 45.39  ? 534 ILE A CA    1 
ATOM   3371 C C     . ILE A 1 449 ? 109.839 133.906 128.182 1.00 49.42  ? 534 ILE A C     1 
ATOM   3372 O O     . ILE A 1 449 ? 109.688 134.609 127.171 1.00 54.94  ? 534 ILE A O     1 
ATOM   3373 C CB    . ILE A 1 449 ? 109.320 134.594 130.562 1.00 43.65  ? 534 ILE A CB    1 
ATOM   3374 C CG1   . ILE A 1 449 ? 108.182 134.825 131.559 1.00 42.10  ? 534 ILE A CG1   1 
ATOM   3375 C CG2   . ILE A 1 449 ? 110.000 135.900 130.197 1.00 52.08  ? 534 ILE A CG2   1 
ATOM   3376 C CD1   . ILE A 1 449 ? 108.652 135.301 132.918 1.00 47.38  ? 534 ILE A CD1   1 
ATOM   3377 N N     . GLN A 1 450 ? 110.898 133.106 128.340 1.00 51.43  ? 535 GLN A N     1 
ATOM   3378 C CA    . GLN A 1 450 ? 111.983 133.109 127.365 1.00 48.72  ? 535 GLN A CA    1 
ATOM   3379 C C     . GLN A 1 450 ? 111.529 132.600 126.002 1.00 52.03  ? 535 GLN A C     1 
ATOM   3380 O O     . GLN A 1 450 ? 111.983 133.108 124.976 1.00 57.71  ? 535 GLN A O     1 
ATOM   3381 C CB    . GLN A 1 450 ? 113.159 132.280 127.880 1.00 45.34  ? 535 GLN A CB    1 
ATOM   3382 C CG    . GLN A 1 450 ? 113.933 132.959 128.993 1.00 47.30  ? 535 GLN A CG    1 
ATOM   3383 C CD    . GLN A 1 450 ? 115.079 132.118 129.508 1.00 54.06  ? 535 GLN A CD    1 
ATOM   3384 O OE1   . GLN A 1 450 ? 116.246 132.477 129.347 1.00 52.30  ? 535 GLN A OE1   1 
ATOM   3385 N NE2   . GLN A 1 450 ? 114.755 130.992 130.131 1.00 56.31  ? 535 GLN A NE2   1 
ATOM   3386 N N     . GLN A 1 451 ? 110.632 131.618 125.964 1.00 53.31  ? 536 GLN A N     1 
ATOM   3387 C CA    . GLN A 1 451 ? 110.153 131.062 124.706 1.00 46.57  ? 536 GLN A CA    1 
ATOM   3388 C C     . GLN A 1 451 ? 109.144 131.965 124.008 1.00 48.60  ? 536 GLN A C     1 
ATOM   3389 O O     . GLN A 1 451 ? 109.147 132.037 122.772 1.00 54.97  ? 536 GLN A O     1 
ATOM   3390 C CB    . GLN A 1 451 ? 109.564 129.666 124.950 1.00 41.38  ? 536 GLN A CB    1 
ATOM   3391 C CG    . GLN A 1 451 ? 108.079 129.624 125.253 1.00 42.26  ? 536 GLN A CG    1 
ATOM   3392 C CD    . GLN A 1 451 ? 107.608 128.239 125.637 1.00 48.02  ? 536 GLN A CD    1 
ATOM   3393 O OE1   . GLN A 1 451 ? 108.415 127.341 125.883 1.00 43.34  ? 536 GLN A OE1   1 
ATOM   3394 N NE2   . GLN A 1 451 ? 106.297 128.059 125.701 1.00 56.82  ? 536 GLN A NE2   1 
ATOM   3395 N N     . PHE A 1 452 ? 108.302 132.680 124.761 1.00 49.62  ? 537 PHE A N     1 
ATOM   3396 C CA    . PHE A 1 452 ? 107.501 133.733 124.151 1.00 49.36  ? 537 PHE A CA    1 
ATOM   3397 C C     . PHE A 1 452 ? 108.399 134.791 123.531 1.00 49.13  ? 537 PHE A C     1 
ATOM   3398 O O     . PHE A 1 452 ? 108.159 135.238 122.403 1.00 54.56  ? 537 PHE A O     1 
ATOM   3399 C CB    . PHE A 1 452 ? 106.563 134.361 125.185 1.00 51.70  ? 537 PHE A CB    1 
ATOM   3400 C CG    . PHE A 1 452 ? 105.996 135.694 124.765 1.00 56.97  ? 537 PHE A CG    1 
ATOM   3401 C CD1   . PHE A 1 452 ? 104.836 135.764 124.012 1.00 61.10  ? 537 PHE A CD1   1 
ATOM   3402 C CD2   . PHE A 1 452 ? 106.615 136.878 125.142 1.00 62.52  ? 537 PHE A CD2   1 
ATOM   3403 C CE1   . PHE A 1 452 ? 104.314 136.987 123.628 1.00 65.69  ? 537 PHE A CE1   1 
ATOM   3404 C CE2   . PHE A 1 452 ? 106.098 138.102 124.760 1.00 61.22  ? 537 PHE A CE2   1 
ATOM   3405 C CZ    . PHE A 1 452 ? 104.945 138.157 124.004 1.00 61.63  ? 537 PHE A CZ    1 
ATOM   3406 N N     . MET A 1 453 ? 109.454 135.189 124.244 1.00 51.56  ? 538 MET A N     1 
ATOM   3407 C CA    . MET A 1 453 ? 110.352 136.193 123.689 1.00 52.83  ? 538 MET A CA    1 
ATOM   3408 C C     . MET A 1 453 ? 111.158 135.648 122.514 1.00 48.25  ? 538 MET A C     1 
ATOM   3409 O O     . MET A 1 453 ? 111.533 136.412 121.619 1.00 55.08  ? 538 MET A O     1 
ATOM   3410 C CB    . MET A 1 453 ? 111.262 136.732 124.788 1.00 56.29  ? 538 MET A CB    1 
ATOM   3411 C CG    . MET A 1 453 ? 110.521 137.639 125.756 1.00 62.48  ? 538 MET A CG    1 
ATOM   3412 S SD    . MET A 1 453 ? 111.607 138.746 126.662 1.00 78.57  ? 538 MET A SD    1 
ATOM   3413 C CE    . MET A 1 453 ? 112.742 137.560 127.355 1.00 62.56  ? 538 MET A CE    1 
ATOM   3414 N N     . ILE A 1 454 ? 111.430 134.342 122.492 1.00 48.83  ? 539 ILE A N     1 
ATOM   3415 C CA    . ILE A 1 454 ? 112.100 133.738 121.344 1.00 48.87  ? 539 ILE A CA    1 
ATOM   3416 C C     . ILE A 1 454 ? 111.192 133.772 120.120 1.00 50.36  ? 539 ILE A C     1 
ATOM   3417 O O     . ILE A 1 454 ? 111.599 134.206 119.037 1.00 55.09  ? 539 ILE A O     1 
ATOM   3418 C CB    . ILE A 1 454 ? 112.542 132.300 121.674 1.00 47.69  ? 539 ILE A CB    1 
ATOM   3419 C CG1   . ILE A 1 454 ? 113.836 132.305 122.488 1.00 53.30  ? 539 ILE A CG1   1 
ATOM   3420 C CG2   . ILE A 1 454 ? 112.722 131.484 120.401 1.00 48.26  ? 539 ILE A CG2   1 
ATOM   3421 C CD1   . ILE A 1 454 ? 114.091 131.013 123.234 1.00 50.65  ? 539 ILE A CD1   1 
ATOM   3422 N N     . LEU A 1 455 ? 109.943 133.332 120.278 1.00 49.07  ? 540 LEU A N     1 
ATOM   3423 C CA    . LEU A 1 455 ? 109.021 133.322 119.149 1.00 46.51  ? 540 LEU A CA    1 
ATOM   3424 C C     . LEU A 1 455 ? 108.539 134.715 118.767 1.00 50.11  ? 540 LEU A C     1 
ATOM   3425 O O     . LEU A 1 455 ? 107.950 134.872 117.692 1.00 57.82  ? 540 LEU A O     1 
ATOM   3426 C CB    . LEU A 1 455 ? 107.824 132.417 119.449 1.00 48.69  ? 540 LEU A CB    1 
ATOM   3427 C CG    . LEU A 1 455 ? 108.158 130.942 119.682 1.00 47.59  ? 540 LEU A CG    1 
ATOM   3428 C CD1   . LEU A 1 455 ? 106.908 130.157 120.051 1.00 51.85  ? 540 LEU A CD1   1 
ATOM   3429 C CD2   . LEU A 1 455 ? 108.830 130.343 118.456 1.00 43.55  ? 540 LEU A CD2   1 
ATOM   3430 N N     . SER A 1 456 ? 108.769 135.722 119.609 1.00 52.96  ? 541 SER A N     1 
ATOM   3431 C CA    . SER A 1 456 ? 108.385 137.093 119.296 1.00 52.44  ? 541 SER A CA    1 
ATOM   3432 C C     . SER A 1 456 ? 109.522 137.920 118.708 1.00 52.67  ? 541 SER A C     1 
ATOM   3433 O O     . SER A 1 456 ? 109.289 138.717 117.795 1.00 60.24  ? 541 SER A O     1 
ATOM   3434 C CB    . SER A 1 456 ? 107.852 137.788 120.554 1.00 55.74  ? 541 SER A CB    1 
ATOM   3435 O OG    . SER A 1 456 ? 106.934 136.958 121.244 1.00 59.59  ? 541 SER A OG    1 
ATOM   3436 N N     . PHE A 1 457 ? 110.747 137.754 119.208 1.00 50.91  ? 542 PHE A N     1 
ATOM   3437 C CA    . PHE A 1 457 ? 111.887 138.553 118.779 1.00 54.16  ? 542 PHE A CA    1 
ATOM   3438 C C     . PHE A 1 457 ? 112.887 137.761 117.945 1.00 57.77  ? 542 PHE A C     1 
ATOM   3439 O O     . PHE A 1 457 ? 113.946 138.295 117.599 1.00 61.90  ? 542 PHE A O     1 
ATOM   3440 C CB    . PHE A 1 457 ? 112.595 139.157 119.995 1.00 57.88  ? 542 PHE A CB    1 
ATOM   3441 C CG    . PHE A 1 457 ? 111.724 140.060 120.820 1.00 62.36  ? 542 PHE A CG    1 
ATOM   3442 C CD1   . PHE A 1 457 ? 111.098 141.155 120.248 1.00 64.60  ? 542 PHE A CD1   1 
ATOM   3443 C CD2   . PHE A 1 457 ? 111.537 139.818 122.171 1.00 60.41  ? 542 PHE A CD2   1 
ATOM   3444 C CE1   . PHE A 1 457 ? 110.298 141.988 121.007 1.00 66.33  ? 542 PHE A CE1   1 
ATOM   3445 C CE2   . PHE A 1 457 ? 110.738 140.647 122.936 1.00 66.64  ? 542 PHE A CE2   1 
ATOM   3446 C CZ    . PHE A 1 457 ? 110.118 141.734 122.353 1.00 72.44  ? 542 PHE A CZ    1 
ATOM   3447 N N     . GLY A 1 458 ? 112.585 136.508 117.618 1.00 57.55  ? 543 GLY A N     1 
ATOM   3448 C CA    . GLY A 1 458 ? 113.512 135.705 116.844 1.00 57.34  ? 543 GLY A CA    1 
ATOM   3449 C C     . GLY A 1 458 ? 114.462 134.893 117.700 1.00 60.40  ? 543 GLY A C     1 
ATOM   3450 O O     . GLY A 1 458 ? 114.123 133.795 118.150 1.00 57.81  ? 543 GLY A O     1 
ATOM   3451 N N     . SER A 1 459 ? 115.665 135.413 117.914 1.00 64.52  ? 544 SER A N     1 
ATOM   3452 C CA    . SER A 1 459 ? 116.662 134.733 118.723 1.00 62.77  ? 544 SER A CA    1 
ATOM   3453 C C     . SER A 1 459 ? 116.544 135.151 120.187 1.00 62.50  ? 544 SER A C     1 
ATOM   3454 O O     . SER A 1 459 ? 115.874 136.125 120.535 1.00 62.11  ? 544 SER A O     1 
ATOM   3455 C CB    . SER A 1 459 ? 118.067 135.028 118.199 1.00 66.97  ? 544 SER A CB    1 
ATOM   3456 O OG    . SER A 1 459 ? 118.274 136.424 118.061 1.00 70.70  ? 544 SER A OG    1 
ATOM   3457 N N     . LEU A 1 460 ? 117.210 134.387 121.054 1.00 67.15  ? 545 LEU A N     1 
ATOM   3458 C CA    . LEU A 1 460 ? 117.292 134.747 122.463 1.00 63.04  ? 545 LEU A CA    1 
ATOM   3459 C C     . LEU A 1 460 ? 118.251 135.903 122.709 1.00 65.29  ? 545 LEU A C     1 
ATOM   3460 O O     . LEU A 1 460 ? 118.134 136.582 123.735 1.00 68.67  ? 545 LEU A O     1 
ATOM   3461 C CB    . LEU A 1 460 ? 117.722 133.535 123.293 1.00 59.52  ? 545 LEU A CB    1 
ATOM   3462 C CG    . LEU A 1 460 ? 117.505 133.616 124.805 1.00 59.55  ? 545 LEU A CG    1 
ATOM   3463 C CD1   . LEU A 1 460 ? 116.023 133.573 125.153 1.00 58.52  ? 545 LEU A CD1   1 
ATOM   3464 C CD2   . LEU A 1 460 ? 118.260 132.503 125.508 1.00 55.31  ? 545 LEU A CD2   1 
ATOM   3465 N N     . ALA A 1 461 ? 119.192 136.142 121.792 1.00 64.48  ? 546 ALA A N     1 
ATOM   3466 C CA    . ALA A 1 461 ? 120.098 137.276 121.937 1.00 66.56  ? 546 ALA A CA    1 
ATOM   3467 C C     . ALA A 1 461 ? 119.370 138.601 121.753 1.00 67.65  ? 546 ALA A C     1 
ATOM   3468 O O     . ALA A 1 461 ? 119.752 139.606 122.363 1.00 71.76  ? 546 ALA A O     1 
ATOM   3469 C CB    . ALA A 1 461 ? 121.251 137.159 120.941 1.00 65.53  ? 546 ALA A CB    1 
ATOM   3470 N N     . ASN A 1 462 ? 118.331 138.626 120.917 1.00 67.75  ? 547 ASN A N     1 
ATOM   3471 C CA    . ASN A 1 462 ? 117.510 139.821 120.770 1.00 69.32  ? 547 ASN A CA    1 
ATOM   3472 C C     . ASN A 1 462 ? 116.598 140.056 121.966 1.00 71.54  ? 547 ASN A C     1 
ATOM   3473 O O     . ASN A 1 462 ? 116.002 141.133 122.066 1.00 72.33  ? 547 ASN A O     1 
ATOM   3474 C CB    . ASN A 1 462 ? 116.666 139.730 119.496 1.00 68.34  ? 547 ASN A CB    1 
ATOM   3475 C CG    . ASN A 1 462 ? 117.503 139.485 118.256 1.00 73.66  ? 547 ASN A CG    1 
ATOM   3476 O OD1   . ASN A 1 462 ? 117.187 138.618 117.441 1.00 71.33  ? 547 ASN A OD1   1 
ATOM   3477 N ND2   . ASN A 1 462 ? 118.577 140.252 118.105 1.00 78.43  ? 547 ASN A ND2   1 
ATOM   3478 N N     . SER A 1 463 ? 116.476 139.081 122.869 1.00 71.61  ? 548 SER A N     1 
ATOM   3479 C CA    . SER A 1 463 ? 115.572 139.173 124.005 1.00 67.09  ? 548 SER A CA    1 
ATOM   3480 C C     . SER A 1 463 ? 116.267 139.492 125.320 1.00 67.50  ? 548 SER A C     1 
ATOM   3481 O O     . SER A 1 463 ? 115.583 139.649 126.337 1.00 71.67  ? 548 SER A O     1 
ATOM   3482 C CB    . SER A 1 463 ? 114.790 137.861 124.163 1.00 65.50  ? 548 SER A CB    1 
ATOM   3483 O OG    . SER A 1 463 ? 115.658 136.796 124.511 1.00 67.17  ? 548 SER A OG    1 
ATOM   3484 N N     . THR A 1 464 ? 117.595 139.594 125.332 1.00 64.42  ? 549 THR A N     1 
ATOM   3485 C CA    . THR A 1 464 ? 118.331 139.810 126.573 1.00 70.11  ? 549 THR A CA    1 
ATOM   3486 C C     . THR A 1 464 ? 118.106 141.175 127.238 1.00 70.88  ? 549 THR A C     1 
ATOM   3487 O O     . THR A 1 464 ? 118.272 141.264 128.461 1.00 67.29  ? 549 THR A O     1 
ATOM   3488 C CB    . THR A 1 464 ? 119.830 139.556 126.349 1.00 72.16  ? 549 THR A CB    1 
ATOM   3489 O OG1   . THR A 1 464 ? 120.523 139.604 127.604 1.00 70.49  ? 549 THR A OG1   1 
ATOM   3490 C CG2   . THR A 1 464 ? 120.446 140.542 125.379 1.00 72.47  ? 549 THR A CG2   1 
ATOM   3491 N N     . PRO A 1 465 ? 117.751 142.258 126.525 1.00 72.09  ? 550 PRO A N     1 
ATOM   3492 C CA    . PRO A 1 465 ? 117.381 143.479 127.264 1.00 67.05  ? 550 PRO A CA    1 
ATOM   3493 C C     . PRO A 1 465 ? 116.129 143.311 128.107 1.00 72.33  ? 550 PRO A C     1 
ATOM   3494 O O     . PRO A 1 465 ? 116.053 143.881 129.203 1.00 76.74  ? 550 PRO A O     1 
ATOM   3495 C CB    . PRO A 1 465 ? 117.179 144.524 126.156 1.00 68.70  ? 550 PRO A CB    1 
ATOM   3496 C CG    . PRO A 1 465 ? 117.895 143.982 124.983 1.00 70.10  ? 550 PRO A CG    1 
ATOM   3497 C CD    . PRO A 1 465 ? 117.705 142.509 125.072 1.00 72.38  ? 550 PRO A CD    1 
ATOM   3498 N N     . TYR A 1 466 ? 115.145 142.545 127.632 1.00 73.05  ? 551 TYR A N     1 
ATOM   3499 C CA    . TYR A 1 466 ? 113.911 142.349 128.382 1.00 71.20  ? 551 TYR A CA    1 
ATOM   3500 C C     . TYR A 1 466 ? 114.035 141.265 129.444 1.00 69.60  ? 551 TYR A C     1 
ATOM   3501 O O     . TYR A 1 466 ? 113.233 141.246 130.384 1.00 70.76  ? 551 TYR A O     1 
ATOM   3502 C CB    . TYR A 1 466 ? 112.763 142.017 127.427 1.00 73.31  ? 551 TYR A CB    1 
ATOM   3503 C CG    . TYR A 1 466 ? 112.798 142.813 126.141 1.00 73.42  ? 551 TYR A CG    1 
ATOM   3504 C CD1   . TYR A 1 466 ? 112.224 144.075 126.067 1.00 75.42  ? 551 TYR A CD1   1 
ATOM   3505 C CD2   . TYR A 1 466 ? 113.406 142.302 125.001 1.00 74.45  ? 551 TYR A CD2   1 
ATOM   3506 C CE1   . TYR A 1 466 ? 112.255 144.807 124.896 1.00 80.30  ? 551 TYR A CE1   1 
ATOM   3507 C CE2   . TYR A 1 466 ? 113.442 143.027 123.825 1.00 77.91  ? 551 TYR A CE2   1 
ATOM   3508 C CZ    . TYR A 1 466 ? 112.865 144.278 123.778 1.00 80.16  ? 551 TYR A CZ    1 
ATOM   3509 O OH    . TYR A 1 466 ? 112.898 145.003 122.609 1.00 77.56  ? 551 TYR A OH    1 
ATOM   3510 N N     . LEU A 1 467 ? 115.015 140.365 129.314 1.00 70.32  ? 552 LEU A N     1 
ATOM   3511 C CA    . LEU A 1 467 ? 115.291 139.413 130.385 1.00 65.45  ? 552 LEU A CA    1 
ATOM   3512 C C     . LEU A 1 467 ? 115.682 140.125 131.673 1.00 67.00  ? 552 LEU A C     1 
ATOM   3513 O O     . LEU A 1 467 ? 115.344 139.658 132.766 1.00 62.50  ? 552 LEU A O     1 
ATOM   3514 C CB    . LEU A 1 467 ? 116.397 138.442 129.961 1.00 61.72  ? 552 LEU A CB    1 
ATOM   3515 C CG    . LEU A 1 467 ? 116.090 137.407 128.877 1.00 56.91  ? 552 LEU A CG    1 
ATOM   3516 C CD1   . LEU A 1 467 ? 117.370 136.823 128.317 1.00 61.30  ? 552 LEU A CD1   1 
ATOM   3517 C CD2   . LEU A 1 467 ? 115.246 136.302 129.467 1.00 56.34  ? 552 LEU A CD2   1 
ATOM   3518 N N     . GLY A 1 468 ? 116.392 141.251 131.565 1.00 67.37  ? 553 GLY A N     1 
ATOM   3519 C CA    . GLY A 1 468 ? 116.803 141.980 132.751 1.00 65.32  ? 553 GLY A CA    1 
ATOM   3520 C C     . GLY A 1 468 ? 115.681 142.724 133.441 1.00 70.98  ? 553 GLY A C     1 
ATOM   3521 O O     . GLY A 1 468 ? 115.681 142.839 134.670 1.00 73.93  ? 553 GLY A O     1 
ATOM   3522 N N     . MET A 1 469 ? 114.723 143.251 132.674 1.00 71.68  ? 554 MET A N     1 
ATOM   3523 C CA    . MET A 1 469 ? 113.580 143.916 133.291 1.00 72.61  ? 554 MET A CA    1 
ATOM   3524 C C     . MET A 1 469 ? 112.680 142.913 134.000 1.00 69.68  ? 554 MET A C     1 
ATOM   3525 O O     . MET A 1 469 ? 112.209 143.172 135.113 1.00 71.17  ? 554 MET A O     1 
ATOM   3526 C CB    . MET A 1 469 ? 112.789 144.698 132.242 1.00 72.62  ? 554 MET A CB    1 
ATOM   3527 C CG    . MET A 1 469 ? 113.646 145.406 131.208 1.00 78.38  ? 554 MET A CG    1 
ATOM   3528 S SD    . MET A 1 469 ? 112.668 146.440 130.102 1.00 116.68 ? 554 MET A SD    1 
ATOM   3529 C CE    . MET A 1 469 ? 113.687 146.425 128.630 1.00 87.20  ? 554 MET A CE    1 
ATOM   3530 N N     . ILE A 1 470 ? 112.431 141.763 133.370 1.00 66.27  ? 555 ILE A N     1 
ATOM   3531 C CA    . ILE A 1 470 ? 111.642 140.716 134.009 1.00 62.89  ? 555 ILE A CA    1 
ATOM   3532 C C     . ILE A 1 470 ? 112.379 140.152 135.217 1.00 68.46  ? 555 ILE A C     1 
ATOM   3533 O O     . ILE A 1 470 ? 111.754 139.800 136.225 1.00 70.92  ? 555 ILE A O     1 
ATOM   3534 C CB    . ILE A 1 470 ? 111.294 139.622 132.983 1.00 54.22  ? 555 ILE A CB    1 
ATOM   3535 C CG1   . ILE A 1 470 ? 110.481 140.225 131.836 1.00 61.73  ? 555 ILE A CG1   1 
ATOM   3536 C CG2   . ILE A 1 470 ? 110.526 138.486 133.641 1.00 55.81  ? 555 ILE A CG2   1 
ATOM   3537 C CD1   . ILE A 1 470 ? 110.516 139.415 130.565 1.00 64.23  ? 555 ILE A CD1   1 
ATOM   3538 N N     . LEU A 1 471 ? 113.710 140.067 135.145 1.00 67.89  ? 556 LEU A N     1 
ATOM   3539 C CA    . LEU A 1 471 ? 114.487 139.590 136.284 1.00 64.11  ? 556 LEU A CA    1 
ATOM   3540 C C     . LEU A 1 471 ? 114.287 140.483 137.502 1.00 65.18  ? 556 LEU A C     1 
ATOM   3541 O O     . LEU A 1 471 ? 114.151 139.988 138.626 1.00 67.47  ? 556 LEU A O     1 
ATOM   3542 C CB    . LEU A 1 471 ? 115.968 139.514 135.911 1.00 66.90  ? 556 LEU A CB    1 
ATOM   3543 C CG    . LEU A 1 471 ? 116.951 139.131 137.019 1.00 62.84  ? 556 LEU A CG    1 
ATOM   3544 C CD1   . LEU A 1 471 ? 116.773 137.676 137.415 1.00 56.45  ? 556 LEU A CD1   1 
ATOM   3545 C CD2   . LEU A 1 471 ? 118.383 139.399 136.582 1.00 60.58  ? 556 LEU A CD2   1 
ATOM   3546 N N     . LEU A 1 472 ? 114.260 141.802 137.298 1.00 65.19  ? 557 LEU A N     1 
ATOM   3547 C CA    . LEU A 1 472 ? 114.031 142.715 138.413 1.00 66.62  ? 557 LEU A CA    1 
ATOM   3548 C C     . LEU A 1 472 ? 112.611 142.600 138.955 1.00 67.42  ? 557 LEU A C     1 
ATOM   3549 O O     . LEU A 1 472 ? 112.402 142.726 140.167 1.00 68.39  ? 557 LEU A O     1 
ATOM   3550 C CB    . LEU A 1 472 ? 114.324 144.152 137.980 1.00 68.87  ? 557 LEU A CB    1 
ATOM   3551 C CG    . LEU A 1 472 ? 114.197 145.241 139.048 1.00 73.16  ? 557 LEU A CG    1 
ATOM   3552 C CD1   . LEU A 1 472 ? 115.200 145.014 140.168 1.00 70.89  ? 557 LEU A CD1   1 
ATOM   3553 C CD2   . LEU A 1 472 ? 114.381 146.619 138.432 1.00 70.80  ? 557 LEU A CD2   1 
ATOM   3554 N N     . VAL A 1 473 ? 111.629 142.361 138.083 1.00 67.10  ? 558 VAL A N     1 
ATOM   3555 C CA    . VAL A 1 473 ? 110.242 142.257 138.530 1.00 66.41  ? 558 VAL A CA    1 
ATOM   3556 C C     . VAL A 1 473 ? 110.036 141.001 139.369 1.00 63.63  ? 558 VAL A C     1 
ATOM   3557 O O     . VAL A 1 473 ? 109.351 141.032 140.398 1.00 65.40  ? 558 VAL A O     1 
ATOM   3558 C CB    . VAL A 1 473 ? 109.287 142.296 137.323 1.00 68.46  ? 558 VAL A CB    1 
ATOM   3559 C CG1   . VAL A 1 473 ? 107.850 142.081 137.774 1.00 69.72  ? 558 VAL A CG1   1 
ATOM   3560 C CG2   . VAL A 1 473 ? 109.417 143.620 136.590 1.00 69.13  ? 558 VAL A CG2   1 
ATOM   3561 N N     . ILE A 1 474 ? 110.610 139.874 138.943 1.00 65.32  ? 559 ILE A N     1 
ATOM   3562 C CA    . ILE A 1 474 ? 110.447 138.643 139.710 1.00 63.25  ? 559 ILE A CA    1 
ATOM   3563 C C     . ILE A 1 474 ? 111.180 138.732 141.042 1.00 62.30  ? 559 ILE A C     1 
ATOM   3564 O O     . ILE A 1 474 ? 110.683 138.245 142.065 1.00 62.64  ? 559 ILE A O     1 
ATOM   3565 C CB    . ILE A 1 474 ? 110.912 137.430 138.882 1.00 58.73  ? 559 ILE A CB    1 
ATOM   3566 C CG1   . ILE A 1 474 ? 110.182 137.393 137.538 1.00 56.00  ? 559 ILE A CG1   1 
ATOM   3567 C CG2   . ILE A 1 474 ? 110.676 136.137 139.646 1.00 51.18  ? 559 ILE A CG2   1 
ATOM   3568 C CD1   . ILE A 1 474 ? 108.674 137.338 137.663 1.00 57.86  ? 559 ILE A CD1   1 
ATOM   3569 N N     . VAL A 1 475 ? 112.360 139.355 141.062 1.00 61.29  ? 560 VAL A N     1 
ATOM   3570 C CA    . VAL A 1 475 ? 113.110 139.479 142.308 1.00 62.19  ? 560 VAL A CA    1 
ATOM   3571 C C     . VAL A 1 475 ? 112.433 140.458 143.262 1.00 68.10  ? 560 VAL A C     1 
ATOM   3572 O O     . VAL A 1 475 ? 112.358 140.207 144.471 1.00 70.60  ? 560 VAL A O     1 
ATOM   3573 C CB    . VAL A 1 475 ? 114.568 139.879 142.020 1.00 64.58  ? 560 VAL A CB    1 
ATOM   3574 C CG1   . VAL A 1 475 ? 115.292 140.208 143.314 1.00 62.05  ? 560 VAL A CG1   1 
ATOM   3575 C CG2   . VAL A 1 475 ? 115.287 138.754 141.293 1.00 63.43  ? 560 VAL A CG2   1 
ATOM   3576 N N     . THR A 1 476 ? 111.925 141.583 142.749 1.00 66.02  ? 561 THR A N     1 
ATOM   3577 C CA    . THR A 1 476 ? 111.269 142.548 143.627 1.00 65.56  ? 561 THR A CA    1 
ATOM   3578 C C     . THR A 1 476 ? 109.978 141.996 144.220 1.00 67.89  ? 561 THR A C     1 
ATOM   3579 O O     . THR A 1 476 ? 109.502 142.521 145.232 1.00 72.72  ? 561 THR A O     1 
ATOM   3580 C CB    . THR A 1 476 ? 110.991 143.860 142.886 1.00 70.40  ? 561 THR A CB    1 
ATOM   3581 O OG1   . THR A 1 476 ? 110.677 144.886 143.836 1.00 76.13  ? 561 THR A OG1   1 
ATOM   3582 C CG2   . THR A 1 476 ? 109.823 143.709 141.930 1.00 68.88  ? 561 THR A CG2   1 
ATOM   3583 N N     . ALA A 1 477 ? 109.404 140.955 143.616 1.00 65.96  ? 562 ALA A N     1 
ATOM   3584 C CA    . ALA A 1 477 ? 108.326 140.202 144.242 1.00 63.92  ? 562 ALA A CA    1 
ATOM   3585 C C     . ALA A 1 477 ? 108.851 139.013 145.032 1.00 63.15  ? 562 ALA A C     1 
ATOM   3586 O O     . ALA A 1 477 ? 108.183 138.550 145.965 1.00 68.18  ? 562 ALA A O     1 
ATOM   3587 C CB    . ALA A 1 477 ? 107.327 139.722 143.186 1.00 65.06  ? 562 ALA A CB    1 
ATOM   3588 N N     . TRP A 1 478 ? 110.033 138.510 144.668 1.00 64.88  ? 563 TRP A N     1 
ATOM   3589 C CA    . TRP A 1 478 ? 110.699 137.488 145.469 1.00 61.95  ? 563 TRP A CA    1 
ATOM   3590 C C     . TRP A 1 478 ? 110.998 138.012 146.868 1.00 64.14  ? 563 TRP A C     1 
ATOM   3591 O O     . TRP A 1 478 ? 110.789 137.308 147.863 1.00 66.84  ? 563 TRP A O     1 
ATOM   3592 C CB    . TRP A 1 478 ? 111.981 137.050 144.756 1.00 59.57  ? 563 TRP A CB    1 
ATOM   3593 C CG    . TRP A 1 478 ? 112.712 135.874 145.338 1.00 57.67  ? 563 TRP A CG    1 
ATOM   3594 C CD1   . TRP A 1 478 ? 112.440 135.218 146.503 1.00 60.40  ? 563 TRP A CD1   1 
ATOM   3595 C CD2   . TRP A 1 478 ? 113.857 135.225 144.771 1.00 55.78  ? 563 TRP A CD2   1 
ATOM   3596 N NE1   . TRP A 1 478 ? 113.343 134.199 146.695 1.00 60.47  ? 563 TRP A NE1   1 
ATOM   3597 C CE2   . TRP A 1 478 ? 114.224 134.184 145.646 1.00 59.65  ? 563 TRP A CE2   1 
ATOM   3598 C CE3   . TRP A 1 478 ? 114.609 135.427 143.609 1.00 51.96  ? 563 TRP A CE3   1 
ATOM   3599 C CZ2   . TRP A 1 478 ? 115.307 133.346 145.393 1.00 55.09  ? 563 TRP A CZ2   1 
ATOM   3600 C CZ3   . TRP A 1 478 ? 115.682 134.594 143.360 1.00 54.51  ? 563 TRP A CZ3   1 
ATOM   3601 C CH2   . TRP A 1 478 ? 116.022 133.567 144.248 1.00 50.92  ? 563 TRP A CH2   1 
ATOM   3602 N N     . LEU A 1 479 ? 111.480 139.253 146.962 1.00 65.06  ? 564 LEU A N     1 
ATOM   3603 C CA    . LEU A 1 479 ? 111.704 139.874 148.262 1.00 66.34  ? 564 LEU A CA    1 
ATOM   3604 C C     . LEU A 1 479 ? 110.392 140.286 148.919 1.00 70.14  ? 564 LEU A C     1 
ATOM   3605 O O     . LEU A 1 479 ? 110.247 140.177 150.142 1.00 75.59  ? 564 LEU A O     1 
ATOM   3606 C CB    . LEU A 1 479 ? 112.628 141.083 148.111 1.00 66.80  ? 564 LEU A CB    1 
ATOM   3607 C CG    . LEU A 1 479 ? 114.009 140.801 147.517 1.00 61.93  ? 564 LEU A CG    1 
ATOM   3608 C CD1   . LEU A 1 479 ? 114.500 141.992 146.711 1.00 62.53  ? 564 LEU A CD1   1 
ATOM   3609 C CD2   . LEU A 1 479 ? 114.999 140.450 148.616 1.00 59.16  ? 564 LEU A CD2   1 
ATOM   3610 N N     . ALA A 1 480 ? 109.428 140.761 148.125 1.00 68.30  ? 565 ALA A N     1 
ATOM   3611 C CA    . ALA A 1 480 ? 108.137 141.159 148.673 1.00 72.53  ? 565 ALA A CA    1 
ATOM   3612 C C     . ALA A 1 480 ? 107.336 139.970 149.187 1.00 75.88  ? 565 ALA A C     1 
ATOM   3613 O O     . ALA A 1 480 ? 106.422 140.158 149.996 1.00 80.46  ? 565 ALA A O     1 
ATOM   3614 C CB    . ALA A 1 480 ? 107.326 141.917 147.621 1.00 70.66  ? 565 ALA A CB    1 
ATOM   3615 N N     . ALA A 1 481 ? 107.653 138.757 148.734 1.00 75.78  ? 566 ALA A N     1 
ATOM   3616 C CA    . ALA A 1 481 ? 107.022 137.552 149.252 1.00 74.80  ? 566 ALA A CA    1 
ATOM   3617 C C     . ALA A 1 481 ? 107.816 136.902 150.375 1.00 77.48  ? 566 ALA A C     1 
ATOM   3618 O O     . ALA A 1 481 ? 107.232 136.168 151.181 1.00 83.75  ? 566 ALA A O     1 
ATOM   3619 C CB    . ALA A 1 481 ? 106.814 136.531 148.127 1.00 75.51  ? 566 ALA A CB    1 
ATOM   3620 N N     . ALA A 1 482 ? 109.126 137.144 150.442 1.00 76.27  ? 567 ALA A N     1 
ATOM   3621 C CA    . ALA A 1 482 ? 109.909 136.675 151.578 1.00 78.62  ? 567 ALA A CA    1 
ATOM   3622 C C     . ALA A 1 482 ? 109.591 137.478 152.832 1.00 84.70  ? 567 ALA A C     1 
ATOM   3623 O O     . ALA A 1 482 ? 109.509 136.915 153.929 1.00 89.67  ? 567 ALA A O     1 
ATOM   3624 C CB    . ALA A 1 482 ? 111.402 136.749 151.258 1.00 74.64  ? 567 ALA A CB    1 
ATOM   3625 N N     . LYS A 1 483 ? 109.412 138.794 152.687 1.00 83.67  ? 568 LYS A N     1 
ATOM   3626 C CA    . LYS A 1 483 ? 108.996 139.618 153.818 1.00 86.23  ? 568 LYS A CA    1 
ATOM   3627 C C     . LYS A 1 483 ? 107.600 139.237 154.293 1.00 88.71  ? 568 LYS A C     1 
ATOM   3628 O O     . LYS A 1 483 ? 107.335 139.208 155.501 1.00 93.34  ? 568 LYS A O     1 
ATOM   3629 C CB    . LYS A 1 483 ? 109.046 141.097 153.439 1.00 86.36  ? 568 LYS A CB    1 
ATOM   3630 C CG    . LYS A 1 483 ? 108.712 142.039 154.584 1.00 91.45  ? 568 LYS A CG    1 
ATOM   3631 C CD    . LYS A 1 483 ? 108.831 143.493 154.159 1.00 93.54  ? 568 LYS A CD    1 
ATOM   3632 C CE    . LYS A 1 483 ? 108.587 144.430 155.330 1.00 97.65  ? 568 LYS A CE    1 
ATOM   3633 N NZ    . LYS A 1 483 ? 107.174 144.374 155.797 1.00 93.37  ? 568 LYS A NZ    1 
ATOM   3634 N N     . SER A 1 484 ? 106.692 138.950 153.356 1.00 89.20  ? 569 SER A N     1 
ATOM   3635 C CA    . SER A 1 484 ? 105.361 138.487 153.734 1.00 93.57  ? 569 SER A CA    1 
ATOM   3636 C C     . SER A 1 484 ? 105.442 137.182 154.513 1.00 94.20  ? 569 SER A C     1 
ATOM   3637 O O     . SER A 1 484 ? 104.707 136.982 155.487 1.00 95.17  ? 569 SER A O     1 
ATOM   3638 C CB    . SER A 1 484 ? 104.488 138.319 152.490 1.00 94.22  ? 569 SER A CB    1 
ATOM   3639 O OG    . SER A 1 484 ? 103.209 137.813 152.829 1.00 101.16 ? 569 SER A OG    1 
ATOM   3640 N N     . LEU A 1 485 ? 106.331 136.281 154.097 1.00 92.47  ? 570 LEU A N     1 
ATOM   3641 C CA    . LEU A 1 485 ? 106.583 135.070 154.863 1.00 91.62  ? 570 LEU A CA    1 
ATOM   3642 C C     . LEU A 1 485 ? 107.412 135.344 156.113 1.00 95.18  ? 570 LEU A C     1 
ATOM   3643 O O     . LEU A 1 485 ? 107.250 134.635 157.111 1.00 100.21 ? 570 LEU A O     1 
ATOM   3644 C CB    . LEU A 1 485 ? 107.269 134.027 153.976 1.00 91.41  ? 570 LEU A CB    1 
ATOM   3645 C CG    . LEU A 1 485 ? 107.541 132.640 154.561 1.00 91.79  ? 570 LEU A CG    1 
ATOM   3646 C CD1   . LEU A 1 485 ? 106.244 131.997 155.020 1.00 96.34  ? 570 LEU A CD1   1 
ATOM   3647 C CD2   . LEU A 1 485 ? 108.223 131.762 153.524 1.00 84.38  ? 570 LEU A CD2   1 
ATOM   3648 N N     . GLU A 1 486 ? 108.282 136.360 156.086 1.00 96.17  ? 571 GLU A N     1 
ATOM   3649 C CA    . GLU A 1 486 ? 109.032 136.745 157.279 1.00 98.45  ? 571 GLU A CA    1 
ATOM   3650 C C     . GLU A 1 486 ? 108.119 137.305 158.362 1.00 103.41 ? 571 GLU A C     1 
ATOM   3651 O O     . GLU A 1 486 ? 108.186 136.880 159.520 1.00 110.00 ? 571 GLU A O     1 
ATOM   3652 C CB    . GLU A 1 486 ? 110.103 137.779 156.929 1.00 97.82  ? 571 GLU A CB    1 
ATOM   3653 C CG    . GLU A 1 486 ? 110.972 138.161 158.115 1.00 101.19 ? 571 GLU A CG    1 
ATOM   3654 C CD    . GLU A 1 486 ? 112.060 139.145 157.751 1.00 104.65 ? 571 GLU A CD    1 
ATOM   3655 O OE1   . GLU A 1 486 ? 112.128 139.550 156.572 1.00 102.89 ? 571 GLU A OE1   1 
ATOM   3656 O OE2   . GLU A 1 486 ? 112.853 139.511 158.644 1.00 102.35 ? 571 GLU A OE2   1 
ATOM   3657 N N     . GLY A 1 487 ? 107.261 138.261 158.003 1.00 102.51 ? 572 GLY A N     1 
ATOM   3658 C CA    . GLY A 1 487 ? 106.315 138.815 158.952 1.00 104.71 ? 572 GLY A CA    1 
ATOM   3659 C C     . GLY A 1 487 ? 105.301 137.827 159.472 1.00 109.74 ? 572 GLY A C     1 
ATOM   3660 O O     . GLY A 1 487 ? 104.559 138.143 160.406 1.00 113.69 ? 572 GLY A O     1 
ATOM   3661 N N     . GLN A 1 488 ? 105.249 136.638 158.875 1.00 109.09 ? 573 GLN A N     1 
ATOM   3662 C CA    . GLN A 1 488 ? 104.405 135.550 159.330 1.00 108.76 ? 573 GLN A CA    1 
ATOM   3663 C C     . GLN A 1 488 ? 105.201 134.374 159.884 1.00 111.35 ? 573 GLN A C     1 
ATOM   3664 O O     . GLN A 1 488 ? 104.656 133.601 160.681 1.00 113.67 ? 573 GLN A O     1 
ATOM   3665 C CB    . GLN A 1 488 ? 103.489 135.100 158.179 1.00 106.02 ? 573 GLN A CB    1 
ATOM   3666 C CG    . GLN A 1 488 ? 102.569 133.933 158.453 1.00 109.24 ? 573 GLN A CG    1 
ATOM   3667 C CD    . GLN A 1 488 ? 102.175 133.228 157.173 1.00 105.46 ? 573 GLN A CD    1 
ATOM   3668 O OE1   . GLN A 1 488 ? 103.029 132.835 156.382 1.00 103.66 ? 573 GLN A OE1   1 
ATOM   3669 N NE2   . GLN A 1 488 ? 100.874 133.070 156.960 1.00 104.96 ? 573 GLN A NE2   1 
ATOM   3670 N N     . PHE A 1 489 ? 106.475 134.230 159.512 1.00 110.92 ? 574 PHE A N     1 
ATOM   3671 C CA    . PHE A 1 489 ? 107.393 133.349 160.222 1.00 111.75 ? 574 PHE A CA    1 
ATOM   3672 C C     . PHE A 1 489 ? 107.820 133.929 161.563 1.00 116.81 ? 574 PHE A C     1 
ATOM   3673 O O     . PHE A 1 489 ? 108.193 133.167 162.463 1.00 117.97 ? 574 PHE A O     1 
ATOM   3674 C CB    . PHE A 1 489 ? 108.632 133.062 159.359 1.00 104.54 ? 574 PHE A CB    1 
ATOM   3675 C CG    . PHE A 1 489 ? 109.614 132.110 159.984 1.00 105.99 ? 574 PHE A CG    1 
ATOM   3676 C CD1   . PHE A 1 489 ? 109.434 130.742 159.875 1.00 104.22 ? 574 PHE A CD1   1 
ATOM   3677 C CD2   . PHE A 1 489 ? 110.733 132.582 160.652 1.00 108.21 ? 574 PHE A CD2   1 
ATOM   3678 C CE1   . PHE A 1 489 ? 110.337 129.861 160.439 1.00 104.71 ? 574 PHE A CE1   1 
ATOM   3679 C CE2   . PHE A 1 489 ? 111.642 131.705 161.218 1.00 106.35 ? 574 PHE A CE2   1 
ATOM   3680 C CZ    . PHE A 1 489 ? 111.444 130.343 161.111 1.00 104.16 ? 574 PHE A CZ    1 
ATOM   3681 N N     . ASN A 1 490 ? 107.780 135.254 161.712 1.00 116.04 ? 575 ASN A N     1 
ATOM   3682 C CA    . ASN A 1 490 ? 108.015 135.908 162.991 1.00 116.99 ? 575 ASN A CA    1 
ATOM   3683 C C     . ASN A 1 490 ? 106.792 135.906 163.896 1.00 120.77 ? 575 ASN A C     1 
ATOM   3684 O O     . ASN A 1 490 ? 106.948 135.957 165.120 1.00 124.29 ? 575 ASN A O     1 
ATOM   3685 C CB    . ASN A 1 490 ? 108.461 137.361 162.772 1.00 115.78 ? 575 ASN A CB    1 
ATOM   3686 C CG    . ASN A 1 490 ? 109.901 137.471 162.320 1.00 118.34 ? 575 ASN A CG    1 
ATOM   3687 O OD1   . ASN A 1 490 ? 110.719 136.591 162.589 1.00 120.23 ? 575 ASN A OD1   1 
ATOM   3688 N ND2   . ASN A 1 490 ? 110.224 138.563 161.642 1.00 111.24 ? 575 ASN A ND2   1 
ATOM   3689 N N     . SER A 1 491 ? 105.588 135.846 163.329 1.00 120.12 ? 576 SER A N     1 
ATOM   3690 C CA    . SER A 1 491 ? 104.352 135.940 164.095 1.00 121.65 ? 576 SER A CA    1 
ATOM   3691 C C     . SER A 1 491 ? 103.819 134.581 164.532 1.00 121.79 ? 576 SER A C     1 
ATOM   3692 O O     . SER A 1 491 ? 102.775 134.519 165.187 1.00 121.28 ? 576 SER A O     1 
ATOM   3693 C CB    . SER A 1 491 ? 103.286 136.682 163.288 1.00 118.98 ? 576 SER A CB    1 
ATOM   3694 O OG    . SER A 1 491 ? 103.756 137.959 162.895 1.00 117.49 ? 576 SER A OG    1 
ATOM   3695 N N     . LEU A 1 492 ? 104.497 133.495 164.170 1.00 121.46 ? 577 LEU A N     1 
ATOM   3696 C CA    . LEU A 1 492 ? 104.312 132.212 164.832 1.00 123.24 ? 577 LEU A CA    1 
ATOM   3697 C C     . LEU A 1 492 ? 105.501 131.941 165.752 1.00 125.50 ? 577 LEU A C     1 
ATOM   3698 O O     . LEU A 1 492 ? 105.976 130.813 165.901 1.00 124.03 ? 577 LEU A O     1 
ATOM   3699 C CB    . LEU A 1 492 ? 104.067 131.120 163.790 1.00 120.89 ? 577 LEU A CB    1 
ATOM   3700 C CG    . LEU A 1 492 ? 103.893 129.639 164.089 1.00 120.25 ? 577 LEU A CG    1 
ATOM   3701 C CD1   . LEU A 1 492 ? 102.664 129.404 164.938 1.00 117.68 ? 577 LEU A CD1   1 
ATOM   3702 C CD2   . LEU A 1 492 ? 103.672 129.011 162.743 1.00 117.33 ? 577 LEU A CD2   1 
ATOM   3703 N N     . ARG A 1 493 ? 105.993 133.024 166.349 1.00 127.80 ? 578 ARG A N     1 
ATOM   3704 C CA    . ARG A 1 493 ? 107.049 133.082 167.345 1.00 131.03 ? 578 ARG A CA    1 
ATOM   3705 C C     . ARG A 1 493 ? 106.810 134.371 168.120 1.00 134.04 ? 578 ARG A C     1 
ATOM   3706 O O     . ARG A 1 493 ? 106.004 135.206 167.700 1.00 131.67 ? 578 ARG A O     1 
ATOM   3707 C CB    . ARG A 1 493 ? 108.439 133.050 166.693 1.00 127.98 ? 578 ARG A CB    1 
ATOM   3708 C CG    . ARG A 1 493 ? 109.615 132.979 167.658 1.00 129.41 ? 578 ARG A CG    1 
ATOM   3709 C CD    . ARG A 1 493 ? 110.937 132.883 166.913 1.00 128.30 ? 578 ARG A CD    1 
ATOM   3710 N NE    . ARG A 1 493 ? 111.219 134.076 166.125 1.00 129.23 ? 578 ARG A NE    1 
ATOM   3711 C CZ    . ARG A 1 493 ? 111.266 134.102 164.800 1.00 125.62 ? 578 ARG A CZ    1 
ATOM   3712 N NH1   . ARG A 1 493 ? 111.035 133.016 164.078 1.00 121.32 ? 578 ARG A NH1   1 
ATOM   3713 N NH2   . ARG A 1 493 ? 111.548 135.246 164.184 1.00 122.20 ? 578 ARG A NH2   1 
ATOM   3714 N N     . SER A 1 494 ? 107.485 134.515 169.258 1.00 135.99 ? 579 SER A N     1 
ATOM   3715 C CA    . SER A 1 494 ? 107.313 135.676 170.139 1.00 136.03 ? 579 SER A CA    1 
ATOM   3716 C C     . SER A 1 494 ? 107.271 137.014 169.399 1.00 136.21 ? 579 SER A C     1 
ATOM   3717 O O     . SER A 1 494 ? 106.481 137.898 169.740 1.00 134.63 ? 579 SER A O     1 
ATOM   3718 C CB    . SER A 1 494 ? 108.433 135.717 171.181 1.00 133.67 ? 579 SER A CB    1 
ATOM   3719 O OG    . SER A 1 494 ? 108.375 134.594 172.041 1.00 136.29 ? 579 SER A OG    1 
ATOM   3720 N N     . GLU B 2 1   ? 120.856 148.957 105.320 1.00 85.38  ? 1   GLU B N     1 
ATOM   3721 C CA    . GLU B 2 1   ? 122.307 149.025 105.447 1.00 89.29  ? 1   GLU B CA    1 
ATOM   3722 C C     . GLU B 2 1   ? 122.926 147.631 105.416 1.00 87.59  ? 1   GLU B C     1 
ATOM   3723 O O     . GLU B 2 1   ? 124.135 147.474 105.579 1.00 87.10  ? 1   GLU B O     1 
ATOM   3724 C CB    . GLU B 2 1   ? 122.698 149.750 106.736 1.00 92.09  ? 1   GLU B CB    1 
ATOM   3725 C CG    . GLU B 2 1   ? 122.292 149.022 108.007 1.00 96.34  ? 1   GLU B CG    1 
ATOM   3726 C CD    . GLU B 2 1   ? 122.647 149.798 109.260 1.00 105.88 ? 1   GLU B CD    1 
ATOM   3727 O OE1   . GLU B 2 1   ? 123.195 150.913 109.135 1.00 110.39 ? 1   GLU B OE1   1 
ATOM   3728 O OE2   . GLU B 2 1   ? 122.376 149.294 110.370 1.00 104.90 ? 1   GLU B OE2   1 
ATOM   3729 N N     . VAL B 2 2   ? 122.087 146.622 105.202 1.00 82.73  ? 2   VAL B N     1 
ATOM   3730 C CA    . VAL B 2 2   ? 122.553 145.243 105.122 1.00 77.25  ? 2   VAL B CA    1 
ATOM   3731 C C     . VAL B 2 2   ? 123.065 144.973 103.713 1.00 77.94  ? 2   VAL B C     1 
ATOM   3732 O O     . VAL B 2 2   ? 122.358 145.210 102.727 1.00 82.27  ? 2   VAL B O     1 
ATOM   3733 C CB    . VAL B 2 2   ? 121.430 144.265 105.501 1.00 71.76  ? 2   VAL B CB    1 
ATOM   3734 C CG1   . VAL B 2 2   ? 121.850 142.837 105.195 1.00 67.57  ? 2   VAL B CG1   1 
ATOM   3735 C CG2   . VAL B 2 2   ? 121.066 144.418 106.969 1.00 74.07  ? 2   VAL B CG2   1 
ATOM   3736 N N     . GLN B 2 3   ? 124.299 144.482 103.615 1.00 74.98  ? 3   GLN B N     1 
ATOM   3737 C CA    . GLN B 2 3   ? 124.907 144.178 102.329 1.00 71.19  ? 3   GLN B CA    1 
ATOM   3738 C C     . GLN B 2 3   ? 125.627 142.840 102.401 1.00 71.90  ? 3   GLN B C     1 
ATOM   3739 O O     . GLN B 2 3   ? 126.166 142.459 103.443 1.00 74.02  ? 3   GLN B O     1 
ATOM   3740 C CB    . GLN B 2 3   ? 125.888 145.275 101.892 1.00 73.26  ? 3   GLN B CB    1 
ATOM   3741 C CG    . GLN B 2 3   ? 125.228 146.609 101.592 1.00 81.60  ? 3   GLN B CG    1 
ATOM   3742 C CD    . GLN B 2 3   ? 124.314 146.542 100.385 1.00 86.72  ? 3   GLN B CD    1 
ATOM   3743 O OE1   . GLN B 2 3   ? 124.619 145.872 99.398  1.00 84.70  ? 3   GLN B OE1   1 
ATOM   3744 N NE2   . GLN B 2 3   ? 123.184 147.235 100.458 1.00 83.89  ? 3   GLN B NE2   1 
ATOM   3745 N N     . LEU B 2 4   ? 125.626 142.130 101.274 1.00 70.48  ? 4   LEU B N     1 
ATOM   3746 C CA    . LEU B 2 4   ? 126.330 140.862 101.131 1.00 64.49  ? 4   LEU B CA    1 
ATOM   3747 C C     . LEU B 2 4   ? 127.127 140.900 99.837  1.00 64.41  ? 4   LEU B C     1 
ATOM   3748 O O     . LEU B 2 4   ? 126.558 141.133 98.765  1.00 68.58  ? 4   LEU B O     1 
ATOM   3749 C CB    . LEU B 2 4   ? 125.353 139.682 101.125 1.00 60.21  ? 4   LEU B CB    1 
ATOM   3750 C CG    . LEU B 2 4   ? 124.491 139.474 102.371 1.00 61.84  ? 4   LEU B CG    1 
ATOM   3751 C CD1   . LEU B 2 4   ? 123.348 138.518 102.072 1.00 59.94  ? 4   LEU B CD1   1 
ATOM   3752 C CD2   . LEU B 2 4   ? 125.331 138.954 103.521 1.00 67.10  ? 4   LEU B CD2   1 
ATOM   3753 N N     . VAL B 2 5   ? 128.434 140.665 99.934  1.00 62.60  ? 5   VAL B N     1 
ATOM   3754 C CA    . VAL B 2 5   ? 129.332 140.664 98.786  1.00 63.72  ? 5   VAL B CA    1 
ATOM   3755 C C     . VAL B 2 5   ? 130.005 139.303 98.708  1.00 65.01  ? 5   VAL B C     1 
ATOM   3756 O O     . VAL B 2 5   ? 130.548 138.814 99.706  1.00 67.14  ? 5   VAL B O     1 
ATOM   3757 C CB    . VAL B 2 5   ? 130.379 141.789 98.875  1.00 59.97  ? 5   VAL B CB    1 
ATOM   3758 C CG1   . VAL B 2 5   ? 131.484 141.569 97.851  1.00 61.38  ? 5   VAL B CG1   1 
ATOM   3759 C CG2   . VAL B 2 5   ? 129.719 143.143 98.671  1.00 58.92  ? 5   VAL B CG2   1 
ATOM   3760 N N     . GLU B 2 6   ? 129.970 138.698 97.528  1.00 63.59  ? 6   GLU B N     1 
ATOM   3761 C CA    . GLU B 2 6   ? 130.436 137.337 97.331  1.00 58.74  ? 6   GLU B CA    1 
ATOM   3762 C C     . GLU B 2 6   ? 131.759 137.374 96.580  1.00 63.80  ? 6   GLU B C     1 
ATOM   3763 O O     . GLU B 2 6   ? 132.003 138.274 95.772  1.00 70.08  ? 6   GLU B O     1 
ATOM   3764 C CB    . GLU B 2 6   ? 129.416 136.532 96.526  1.00 62.40  ? 6   GLU B CB    1 
ATOM   3765 C CG    . GLU B 2 6   ? 128.271 135.954 97.319  1.00 60.95  ? 6   GLU B CG    1 
ATOM   3766 C CD    . GLU B 2 6   ? 127.082 136.850 97.203  1.00 63.99  ? 6   GLU B CD    1 
ATOM   3767 O OE1   . GLU B 2 6   ? 127.223 137.889 96.528  1.00 69.20  ? 6   GLU B OE1   1 
ATOM   3768 O OE2   . GLU B 2 6   ? 126.020 136.542 97.754  1.00 63.27  ? 6   GLU B OE2   1 
ATOM   3769 N N     . SER B 2 7   ? 132.614 136.390 96.844  1.00 60.22  ? 7   SER B N     1 
ATOM   3770 C CA    . SER B 2 7   ? 133.884 136.290 96.138  1.00 63.58  ? 7   SER B CA    1 
ATOM   3771 C C     . SER B 2 7   ? 134.332 134.835 96.125  1.00 65.07  ? 7   SER B C     1 
ATOM   3772 O O     . SER B 2 7   ? 133.734 133.974 96.774  1.00 62.42  ? 7   SER B O     1 
ATOM   3773 C CB    . SER B 2 7   ? 134.955 137.186 96.771  1.00 62.50  ? 7   SER B CB    1 
ATOM   3774 O OG    . SER B 2 7   ? 135.286 136.741 98.074  1.00 71.00  ? 7   SER B OG    1 
ATOM   3775 N N     . GLY B 2 8   ? 135.395 134.567 95.366  1.00 65.55  ? 8   GLY B N     1 
ATOM   3776 C CA    . GLY B 2 8   ? 135.996 133.255 95.299  1.00 64.09  ? 8   GLY B CA    1 
ATOM   3777 C C     . GLY B 2 8   ? 135.630 132.441 94.075  1.00 63.50  ? 8   GLY B C     1 
ATOM   3778 O O     . GLY B 2 8   ? 136.311 131.451 93.783  1.00 66.68  ? 8   GLY B O     1 
ATOM   3779 N N     . GLY B 2 9   ? 134.577 132.824 93.358  1.00 60.73  ? 9   GLY B N     1 
ATOM   3780 C CA    . GLY B 2 9   ? 134.183 132.073 92.182  1.00 59.13  ? 9   GLY B CA    1 
ATOM   3781 C C     . GLY B 2 9   ? 135.195 132.195 91.059  1.00 63.31  ? 9   GLY B C     1 
ATOM   3782 O O     . GLY B 2 9   ? 135.877 133.209 90.909  1.00 70.26  ? 9   GLY B O     1 
ATOM   3783 N N     . GLY B 2 10  ? 135.288 131.142 90.256  1.00 63.07  ? 10  GLY B N     1 
ATOM   3784 C CA    . GLY B 2 10  ? 136.237 131.138 89.160  1.00 65.87  ? 10  GLY B CA    1 
ATOM   3785 C C     . GLY B 2 10  ? 136.236 129.810 88.437  1.00 64.85  ? 10  GLY B C     1 
ATOM   3786 O O     . GLY B 2 10  ? 135.361 128.966 88.641  1.00 66.17  ? 10  GLY B O     1 
ATOM   3787 N N     . LEU B 2 11  ? 137.242 129.639 87.581  1.00 63.16  ? 11  LEU B N     1 
ATOM   3788 C CA    . LEU B 2 11  ? 137.396 128.432 86.781  1.00 58.51  ? 11  LEU B CA    1 
ATOM   3789 C C     . LEU B 2 11  ? 138.174 127.374 87.551  1.00 60.40  ? 11  LEU B C     1 
ATOM   3790 O O     . LEU B 2 11  ? 139.247 127.654 88.096  1.00 65.89  ? 11  LEU B O     1 
ATOM   3791 C CB    . LEU B 2 11  ? 138.119 128.742 85.469  1.00 61.70  ? 11  LEU B CB    1 
ATOM   3792 C CG    . LEU B 2 11  ? 137.360 129.409 84.325  1.00 59.80  ? 11  LEU B CG    1 
ATOM   3793 C CD1   . LEU B 2 11  ? 138.328 129.837 83.237  1.00 65.58  ? 11  LEU B CD1   1 
ATOM   3794 C CD2   . LEU B 2 11  ? 136.334 128.450 83.759  1.00 53.69  ? 11  LEU B CD2   1 
ATOM   3795 N N     . VAL B 2 12  ? 137.628 126.156 87.590  1.00 56.68  ? 12  VAL B N     1 
ATOM   3796 C CA    . VAL B 2 12  ? 138.345 124.980 88.066  1.00 60.66  ? 12  VAL B CA    1 
ATOM   3797 C C     . VAL B 2 12  ? 138.034 123.791 87.170  1.00 58.91  ? 12  VAL B C     1 
ATOM   3798 O O     . VAL B 2 12  ? 137.022 123.752 86.465  1.00 61.37  ? 12  VAL B O     1 
ATOM   3799 C CB    . VAL B 2 12  ? 138.020 124.615 89.531  1.00 61.20  ? 12  VAL B CB    1 
ATOM   3800 C CG1   . VAL B 2 12  ? 138.544 125.659 90.478  1.00 61.50  ? 12  VAL B CG1   1 
ATOM   3801 C CG2   . VAL B 2 12  ? 136.518 124.453 89.700  1.00 56.93  ? 12  VAL B CG2   1 
ATOM   3802 N N     . GLN B 2 13  ? 138.933 122.816 87.201  1.00 59.51  ? 13  GLN B N     1 
ATOM   3803 C CA    . GLN B 2 13  ? 138.714 121.563 86.507  1.00 57.72  ? 13  GLN B CA    1 
ATOM   3804 C C     . GLN B 2 13  ? 137.717 120.707 87.282  1.00 59.67  ? 13  GLN B C     1 
ATOM   3805 O O     . GLN B 2 13  ? 137.457 120.932 88.468  1.00 61.58  ? 13  GLN B O     1 
ATOM   3806 C CB    . GLN B 2 13  ? 140.032 120.809 86.335  1.00 63.30  ? 13  GLN B CB    1 
ATOM   3807 C CG    . GLN B 2 13  ? 140.840 121.245 85.125  1.00 67.19  ? 13  GLN B CG    1 
ATOM   3808 C CD    . GLN B 2 13  ? 140.165 120.915 83.812  1.00 68.15  ? 13  GLN B CD    1 
ATOM   3809 O OE1   . GLN B 2 13  ? 139.470 119.906 83.693  1.00 68.11  ? 13  GLN B OE1   1 
ATOM   3810 N NE2   . GLN B 2 13  ? 140.376 121.762 82.810  1.00 67.85  ? 13  GLN B NE2   1 
ATOM   3811 N N     . ALA B 2 14  ? 137.153 119.718 86.595  1.00 64.47  ? 14  ALA B N     1 
ATOM   3812 C CA    . ALA B 2 14  ? 136.247 118.785 87.247  1.00 67.16  ? 14  ALA B CA    1 
ATOM   3813 C C     . ALA B 2 14  ? 136.984 118.017 88.336  1.00 65.65  ? 14  ALA B C     1 
ATOM   3814 O O     . ALA B 2 14  ? 138.073 117.481 88.108  1.00 62.21  ? 14  ALA B O     1 
ATOM   3815 C CB    . ALA B 2 14  ? 135.651 117.825 86.220  1.00 63.13  ? 14  ALA B CB    1 
ATOM   3816 N N     . GLY B 2 15  ? 136.386 117.966 89.525  1.00 60.71  ? 15  GLY B N     1 
ATOM   3817 C CA    . GLY B 2 15  ? 137.023 117.370 90.676  1.00 57.95  ? 15  GLY B CA    1 
ATOM   3818 C C     . GLY B 2 15  ? 137.865 118.316 91.505  1.00 61.62  ? 15  GLY B C     1 
ATOM   3819 O O     . GLY B 2 15  ? 138.450 117.881 92.505  1.00 67.91  ? 15  GLY B O     1 
ATOM   3820 N N     . GLY B 2 16  ? 137.947 119.590 91.127  1.00 60.37  ? 16  GLY B N     1 
ATOM   3821 C CA    . GLY B 2 16  ? 138.716 120.567 91.869  1.00 57.43  ? 16  GLY B CA    1 
ATOM   3822 C C     . GLY B 2 16  ? 137.973 121.063 93.092  1.00 60.54  ? 16  GLY B C     1 
ATOM   3823 O O     . GLY B 2 16  ? 137.019 120.444 93.571  1.00 61.12  ? 16  GLY B O     1 
ATOM   3824 N N     . SER B 2 17  ? 138.424 122.206 93.607  1.00 61.28  ? 17  SER B N     1 
ATOM   3825 C CA    . SER B 2 17  ? 137.845 122.760 94.822  1.00 55.86  ? 17  SER B CA    1 
ATOM   3826 C C     . SER B 2 17  ? 137.811 124.280 94.743  1.00 55.75  ? 17  SER B C     1 
ATOM   3827 O O     . SER B 2 17  ? 138.683 124.908 94.137  1.00 60.16  ? 17  SER B O     1 
ATOM   3828 C CB    . SER B 2 17  ? 138.623 122.316 96.068  1.00 60.87  ? 17  SER B CB    1 
ATOM   3829 O OG    . SER B 2 17  ? 138.584 120.908 96.218  1.00 70.87  ? 17  SER B OG    1 
ATOM   3830 N N     . LEU B 2 18  ? 136.788 124.858 95.371  1.00 56.17  ? 18  LEU B N     1 
ATOM   3831 C CA    . LEU B 2 18  ? 136.644 126.299 95.526  1.00 54.20  ? 18  LEU B CA    1 
ATOM   3832 C C     . LEU B 2 18  ? 136.127 126.626 96.917  1.00 56.78  ? 18  LEU B C     1 
ATOM   3833 O O     . LEU B 2 18  ? 135.579 125.775 97.622  1.00 57.75  ? 18  LEU B O     1 
ATOM   3834 C CB    . LEU B 2 18  ? 135.710 126.912 94.473  1.00 51.57  ? 18  LEU B CB    1 
ATOM   3835 C CG    . LEU B 2 18  ? 136.198 126.849 93.035  1.00 60.94  ? 18  LEU B CG    1 
ATOM   3836 C CD1   . LEU B 2 18  ? 135.142 127.352 92.094  1.00 60.67  ? 18  LEU B CD1   1 
ATOM   3837 C CD2   . LEU B 2 18  ? 137.403 127.771 92.975  1.00 59.54  ? 18  LEU B CD2   1 
ATOM   3838 N N     . ARG B 2 19  ? 136.325 127.884 97.304  1.00 57.42  ? 19  ARG B N     1 
ATOM   3839 C CA    . ARG B 2 19  ? 135.855 128.405 98.585  1.00 58.23  ? 19  ARG B CA    1 
ATOM   3840 C C     . ARG B 2 19  ? 135.218 129.766 98.325  1.00 58.17  ? 19  ARG B C     1 
ATOM   3841 O O     . ARG B 2 19  ? 135.924 130.767 98.173  1.00 57.07  ? 19  ARG B O     1 
ATOM   3842 C CB    . ARG B 2 19  ? 136.994 128.512 99.591  1.00 58.91  ? 19  ARG B CB    1 
ATOM   3843 C CG    . ARG B 2 19  ? 136.546 128.961 100.969 1.00 58.53  ? 19  ARG B CG    1 
ATOM   3844 C CD    . ARG B 2 19  ? 137.698 128.971 101.956 1.00 66.00  ? 19  ARG B CD    1 
ATOM   3845 N NE    . ARG B 2 19  ? 137.275 129.436 103.271 1.00 69.61  ? 19  ARG B NE    1 
ATOM   3846 C CZ    . ARG B 2 19  ? 138.075 129.530 104.325 1.00 69.64  ? 19  ARG B CZ    1 
ATOM   3847 N NH1   . ARG B 2 19  ? 139.355 129.203 104.251 1.00 76.85  ? 19  ARG B NH1   1 
ATOM   3848 N NH2   . ARG B 2 19  ? 137.578 129.966 105.479 1.00 68.04  ? 19  ARG B NH2   1 
ATOM   3849 N N     . LEU B 2 20  ? 133.889 129.800 98.273  1.00 58.16  ? 20  LEU B N     1 
ATOM   3850 C CA    . LEU B 2 20  ? 133.178 131.058 98.097  1.00 56.61  ? 20  LEU B CA    1 
ATOM   3851 C C     . LEU B 2 20  ? 133.085 131.792 99.427  1.00 59.57  ? 20  LEU B C     1 
ATOM   3852 O O     . LEU B 2 20  ? 132.821 131.181 100.467 1.00 62.33  ? 20  LEU B O     1 
ATOM   3853 C CB    . LEU B 2 20  ? 131.782 130.818 97.528  1.00 52.74  ? 20  LEU B CB    1 
ATOM   3854 C CG    . LEU B 2 20  ? 131.656 129.806 96.394  1.00 48.69  ? 20  LEU B CG    1 
ATOM   3855 C CD1   . LEU B 2 20  ? 130.204 129.703 95.978  1.00 45.16  ? 20  LEU B CD1   1 
ATOM   3856 C CD2   . LEU B 2 20  ? 132.534 130.193 95.216  1.00 53.56  ? 20  LEU B CD2   1 
ATOM   3857 N N     . SER B 2 21  ? 133.298 133.103 99.388  1.00 61.23  ? 21  SER B N     1 
ATOM   3858 C CA    . SER B 2 21  ? 133.323 133.938 100.579 1.00 59.27  ? 21  SER B CA    1 
ATOM   3859 C C     . SER B 2 21  ? 132.151 134.910 100.563 1.00 62.14  ? 21  SER B C     1 
ATOM   3860 O O     . SER B 2 21  ? 131.814 135.474 99.517  1.00 67.28  ? 21  SER B O     1 
ATOM   3861 C CB    . SER B 2 21  ? 134.644 134.705 100.672 1.00 62.38  ? 21  SER B CB    1 
ATOM   3862 O OG    . SER B 2 21  ? 134.664 135.558 101.801 1.00 69.34  ? 21  SER B OG    1 
ATOM   3863 N N     . CYS B 2 22  ? 131.535 135.102 101.730 1.00 62.12  ? 22  CYS B N     1 
ATOM   3864 C CA    . CYS B 2 22  ? 130.395 136.002 101.907 1.00 59.84  ? 22  CYS B CA    1 
ATOM   3865 C C     . CYS B 2 22  ? 130.717 137.037 102.980 1.00 64.40  ? 22  CYS B C     1 
ATOM   3866 O O     . CYS B 2 22  ? 130.484 136.794 104.167 1.00 65.62  ? 22  CYS B O     1 
ATOM   3867 C CB    . CYS B 2 22  ? 129.139 135.225 102.286 1.00 61.55  ? 22  CYS B CB    1 
ATOM   3868 S SG    . CYS B 2 22  ? 127.586 136.101 102.013 1.00 81.63  ? 22  CYS B SG    1 
ATOM   3869 N N     . ALA B 2 23  ? 131.223 138.194 102.567 1.00 64.45  ? 23  ALA B N     1 
ATOM   3870 C CA    . ALA B 2 23  ? 131.434 139.298 103.495 1.00 65.23  ? 23  ALA B CA    1 
ATOM   3871 C C     . ALA B 2 23  ? 130.102 139.990 103.752 1.00 71.30  ? 23  ALA B C     1 
ATOM   3872 O O     . ALA B 2 23  ? 129.469 140.497 102.820 1.00 72.45  ? 23  ALA B O     1 
ATOM   3873 C CB    . ALA B 2 23  ? 132.462 140.281 102.939 1.00 65.61  ? 23  ALA B CB    1 
ATOM   3874 N N     . ALA B 2 24  ? 129.677 140.011 105.011 1.00 71.56  ? 24  ALA B N     1 
ATOM   3875 C CA    . ALA B 2 24  ? 128.402 140.589 105.403 1.00 68.84  ? 24  ALA B CA    1 
ATOM   3876 C C     . ALA B 2 24  ? 128.619 141.895 106.155 1.00 73.78  ? 24  ALA B C     1 
ATOM   3877 O O     . ALA B 2 24  ? 129.589 142.048 106.903 1.00 76.31  ? 24  ALA B O     1 
ATOM   3878 C CB    . ALA B 2 24  ? 127.603 139.619 106.275 1.00 65.49  ? 24  ALA B CB    1 
ATOM   3879 N N     . SER B 2 25  ? 127.706 142.839 105.942 1.00 69.81  ? 25  SER B N     1 
ATOM   3880 C CA    . SER B 2 25  ? 127.754 144.132 106.609 1.00 68.09  ? 25  SER B CA    1 
ATOM   3881 C C     . SER B 2 25  ? 126.356 144.508 107.071 1.00 73.43  ? 25  SER B C     1 
ATOM   3882 O O     . SER B 2 25  ? 125.373 144.252 106.371 1.00 77.17  ? 25  SER B O     1 
ATOM   3883 C CB    . SER B 2 25  ? 128.317 145.218 105.684 1.00 72.64  ? 25  SER B CB    1 
ATOM   3884 O OG    . SER B 2 25  ? 129.733 145.171 105.647 1.00 75.21  ? 25  SER B OG    1 
ATOM   3885 N N     . GLY B 2 26  ? 126.273 145.117 108.252 1.00 75.00  ? 26  GLY B N     1 
ATOM   3886 C CA    . GLY B 2 26  ? 125.007 145.533 108.814 1.00 75.22  ? 26  GLY B CA    1 
ATOM   3887 C C     . GLY B 2 26  ? 124.361 144.549 109.765 1.00 70.87  ? 26  GLY B C     1 
ATOM   3888 O O     . GLY B 2 26  ? 123.283 144.847 110.294 1.00 78.65  ? 26  GLY B O     1 
ATOM   3889 N N     . PHE B 2 27  ? 124.979 143.390 109.999 1.00 67.55  ? 27  PHE B N     1 
ATOM   3890 C CA    . PHE B 2 27  ? 124.439 142.390 110.911 1.00 63.10  ? 27  PHE B CA    1 
ATOM   3891 C C     . PHE B 2 27  ? 125.506 141.358 111.249 1.00 64.40  ? 27  PHE B C     1 
ATOM   3892 O O     . PHE B 2 27  ? 126.376 141.067 110.416 1.00 67.76  ? 27  PHE B O     1 
ATOM   3893 C CB    . PHE B 2 27  ? 123.215 141.702 110.299 1.00 63.38  ? 27  PHE B CB    1 
ATOM   3894 C CG    . PHE B 2 27  ? 123.541 140.810 109.135 1.00 63.82  ? 27  PHE B CG    1 
ATOM   3895 C CD1   . PHE B 2 27  ? 123.701 141.336 107.865 1.00 68.39  ? 27  PHE B CD1   1 
ATOM   3896 C CD2   . PHE B 2 27  ? 123.684 139.443 109.310 1.00 61.85  ? 27  PHE B CD2   1 
ATOM   3897 C CE1   . PHE B 2 27  ? 124.001 140.518 106.793 1.00 66.23  ? 27  PHE B CE1   1 
ATOM   3898 C CE2   . PHE B 2 27  ? 123.985 138.621 108.242 1.00 61.34  ? 27  PHE B CE2   1 
ATOM   3899 C CZ    . PHE B 2 27  ? 124.142 139.159 106.982 1.00 63.26  ? 27  PHE B CZ    1 
ATOM   3900 N N     . PRO B 2 28  ? 125.483 140.786 112.454 1.00 64.03  ? 28  PRO B N     1 
ATOM   3901 C CA    . PRO B 2 28  ? 126.417 139.696 112.776 1.00 65.04  ? 28  PRO B CA    1 
ATOM   3902 C C     . PRO B 2 28  ? 125.944 138.384 112.164 1.00 62.29  ? 28  PRO B C     1 
ATOM   3903 O O     . PRO B 2 28  ? 124.765 138.032 112.250 1.00 62.90  ? 28  PRO B O     1 
ATOM   3904 C CB    . PRO B 2 28  ? 126.385 139.648 114.305 1.00 65.79  ? 28  PRO B CB    1 
ATOM   3905 C CG    . PRO B 2 28  ? 125.032 140.179 114.655 1.00 70.40  ? 28  PRO B CG    1 
ATOM   3906 C CD    . PRO B 2 28  ? 124.710 141.227 113.632 1.00 65.54  ? 28  PRO B CD    1 
ATOM   3907 N N     . VAL B 2 29  ? 126.877 137.658 111.543 1.00 60.56  ? 29  VAL B N     1 
ATOM   3908 C CA    . VAL B 2 29  ? 126.521 136.420 110.857 1.00 58.59  ? 29  VAL B CA    1 
ATOM   3909 C C     . VAL B 2 29  ? 126.169 135.298 111.826 1.00 59.88  ? 29  VAL B C     1 
ATOM   3910 O O     . VAL B 2 29  ? 125.492 134.341 111.436 1.00 64.79  ? 29  VAL B O     1 
ATOM   3911 C CB    . VAL B 2 29  ? 127.656 135.980 109.912 1.00 59.32  ? 29  VAL B CB    1 
ATOM   3912 C CG1   . VAL B 2 29  ? 127.849 137.005 108.805 1.00 61.27  ? 29  VAL B CG1   1 
ATOM   3913 C CG2   . VAL B 2 29  ? 128.949 135.785 110.687 1.00 62.46  ? 29  VAL B CG2   1 
ATOM   3914 N N     . ASP B 2 30  ? 126.608 135.385 113.081 1.00 58.22  ? 30  ASP B N     1 
ATOM   3915 C CA    . ASP B 2 30  ? 126.283 134.356 114.060 1.00 59.86  ? 30  ASP B CA    1 
ATOM   3916 C C     . ASP B 2 30  ? 124.852 134.438 114.554 1.00 62.11  ? 30  ASP B C     1 
ATOM   3917 O O     . ASP B 2 30  ? 124.369 133.474 115.161 1.00 63.07  ? 30  ASP B O     1 
ATOM   3918 C CB    . ASP B 2 30  ? 127.227 134.434 115.257 1.00 65.43  ? 30  ASP B CB    1 
ATOM   3919 C CG    . ASP B 2 30  ? 127.186 135.789 115.948 1.00 75.64  ? 30  ASP B CG    1 
ATOM   3920 O OD1   . ASP B 2 30  ? 126.477 136.697 115.458 1.00 79.43  ? 30  ASP B OD1   1 
ATOM   3921 O OD2   . ASP B 2 30  ? 127.864 135.946 116.984 1.00 78.90  ? 30  ASP B OD2   1 
ATOM   3922 N N     . GLU B 2 31  ? 124.179 135.561 114.331 1.00 62.54  ? 31  GLU B N     1 
ATOM   3923 C CA    . GLU B 2 31  ? 122.795 135.732 114.737 1.00 64.32  ? 31  GLU B CA    1 
ATOM   3924 C C     . GLU B 2 31  ? 121.835 135.586 113.568 1.00 62.43  ? 31  GLU B C     1 
ATOM   3925 O O     . GLU B 2 31  ? 120.633 135.818 113.731 1.00 63.79  ? 31  GLU B O     1 
ATOM   3926 C CB    . GLU B 2 31  ? 122.611 137.097 115.401 1.00 67.12  ? 31  GLU B CB    1 
ATOM   3927 C CG    . GLU B 2 31  ? 123.300 137.222 116.751 1.00 73.67  ? 31  GLU B CG    1 
ATOM   3928 C CD    . GLU B 2 31  ? 122.538 138.102 117.716 1.00 88.72  ? 31  GLU B CD    1 
ATOM   3929 O OE1   . GLU B 2 31  ? 121.328 138.313 117.494 1.00 87.14  ? 31  GLU B OE1   1 
ATOM   3930 O OE2   . GLU B 2 31  ? 123.152 138.592 118.687 1.00 93.47  ? 31  GLU B OE2   1 
ATOM   3931 N N     . ALA B 2 32  ? 122.335 135.188 112.403 1.00 57.79  ? 32  ALA B N     1 
ATOM   3932 C CA    . ALA B 2 32  ? 121.575 135.228 111.167 1.00 50.91  ? 32  ALA B CA    1 
ATOM   3933 C C     . ALA B 2 32  ? 121.463 133.842 110.551 1.00 55.34  ? 32  ALA B C     1 
ATOM   3934 O O     . ALA B 2 32  ? 122.279 132.950 110.802 1.00 55.19  ? 32  ALA B O     1 
ATOM   3935 C CB    . ALA B 2 32  ? 122.219 136.190 110.163 1.00 56.45  ? 32  ALA B CB    1 
ATOM   3936 N N     . TYR B 2 33  ? 120.426 133.681 109.736 1.00 58.61  ? 33  TYR B N     1 
ATOM   3937 C CA    . TYR B 2 33  ? 120.196 132.471 108.956 1.00 46.92  ? 33  TYR B CA    1 
ATOM   3938 C C     . TYR B 2 33  ? 120.735 132.709 107.550 1.00 50.14  ? 33  TYR B C     1 
ATOM   3939 O O     . TYR B 2 33  ? 120.123 133.430 106.756 1.00 54.34  ? 33  TYR B O     1 
ATOM   3940 C CB    . TYR B 2 33  ? 118.709 132.125 108.937 1.00 49.99  ? 33  TYR B CB    1 
ATOM   3941 C CG    . TYR B 2 33  ? 118.330 131.036 107.961 1.00 49.39  ? 33  TYR B CG    1 
ATOM   3942 C CD1   . TYR B 2 33  ? 118.942 129.791 108.002 1.00 48.91  ? 33  TYR B CD1   1 
ATOM   3943 C CD2   . TYR B 2 33  ? 117.347 131.250 107.007 1.00 47.94  ? 33  TYR B CD2   1 
ATOM   3944 C CE1   . TYR B 2 33  ? 118.590 128.794 107.110 1.00 50.84  ? 33  TYR B CE1   1 
ATOM   3945 C CE2   . TYR B 2 33  ? 116.989 130.262 106.117 1.00 49.24  ? 33  TYR B CE2   1 
ATOM   3946 C CZ    . TYR B 2 33  ? 117.612 129.036 106.171 1.00 52.37  ? 33  TYR B CZ    1 
ATOM   3947 O OH    . TYR B 2 33  ? 117.252 128.054 105.279 1.00 61.33  ? 33  TYR B OH    1 
ATOM   3948 N N     . MET B 2 34  ? 121.878 132.103 107.247 1.00 49.98  ? 34  MET B N     1 
ATOM   3949 C CA    . MET B 2 34  ? 122.592 132.344 106.004 1.00 45.81  ? 34  MET B CA    1 
ATOM   3950 C C     . MET B 2 34  ? 122.415 131.153 105.071 1.00 49.02  ? 34  MET B C     1 
ATOM   3951 O O     . MET B 2 34  ? 122.409 129.999 105.508 1.00 49.50  ? 34  MET B O     1 
ATOM   3952 C CB    . MET B 2 34  ? 124.082 132.575 106.271 1.00 48.37  ? 34  MET B CB    1 
ATOM   3953 C CG    . MET B 2 34  ? 124.382 133.841 107.060 1.00 47.05  ? 34  MET B CG    1 
ATOM   3954 S SD    . MET B 2 34  ? 123.864 135.369 106.267 1.00 69.65  ? 34  MET B SD    1 
ATOM   3955 C CE    . MET B 2 34  ? 125.003 135.452 104.895 1.00 62.04  ? 34  MET B CE    1 
ATOM   3956 N N     . THR B 2 35  ? 122.264 131.439 103.779 1.00 52.08  ? 35  THR B N     1 
ATOM   3957 C CA    . THR B 2 35  ? 122.064 130.400 102.778 1.00 48.81  ? 35  THR B CA    1 
ATOM   3958 C C     . THR B 2 35  ? 122.894 130.700 101.539 1.00 47.97  ? 35  THR B C     1 
ATOM   3959 O O     . THR B 2 35  ? 123.181 131.859 101.227 1.00 49.72  ? 35  THR B O     1 
ATOM   3960 C CB    . THR B 2 35  ? 120.587 130.266 102.368 1.00 49.74  ? 35  THR B CB    1 
ATOM   3961 O OG1   . THR B 2 35  ? 120.137 131.497 101.788 1.00 60.32  ? 35  THR B OG1   1 
ATOM   3962 C CG2   . THR B 2 35  ? 119.712 129.914 103.561 1.00 49.02  ? 35  THR B CG2   1 
ATOM   3963 N N     . TRP B 2 36  ? 123.272 129.637 100.836 1.00 48.40  ? 36  TRP B N     1 
ATOM   3964 C CA    . TRP B 2 36  ? 123.881 129.727 99.516  1.00 47.54  ? 36  TRP B CA    1 
ATOM   3965 C C     . TRP B 2 36  ? 122.926 129.149 98.482  1.00 49.43  ? 36  TRP B C     1 
ATOM   3966 O O     . TRP B 2 36  ? 122.467 128.010 98.620  1.00 47.72  ? 36  TRP B O     1 
ATOM   3967 C CB    . TRP B 2 36  ? 125.222 128.989 99.460  1.00 43.74  ? 36  TRP B CB    1 
ATOM   3968 C CG    . TRP B 2 36  ? 126.355 129.707 100.127 1.00 45.84  ? 36  TRP B CG    1 
ATOM   3969 C CD1   . TRP B 2 36  ? 126.818 129.516 101.394 1.00 44.24  ? 36  TRP B CD1   1 
ATOM   3970 C CD2   . TRP B 2 36  ? 127.186 130.719 99.544  1.00 46.19  ? 36  TRP B CD2   1 
ATOM   3971 N NE1   . TRP B 2 36  ? 127.878 130.354 101.643 1.00 44.68  ? 36  TRP B NE1   1 
ATOM   3972 C CE2   . TRP B 2 36  ? 128.124 131.102 100.522 1.00 44.74  ? 36  TRP B CE2   1 
ATOM   3973 C CE3   . TRP B 2 36  ? 127.224 131.341 98.293  1.00 48.38  ? 36  TRP B CE3   1 
ATOM   3974 C CZ2   . TRP B 2 36  ? 129.090 132.080 100.288 1.00 51.54  ? 36  TRP B CZ2   1 
ATOM   3975 C CZ3   . TRP B 2 36  ? 128.183 132.311 98.062  1.00 50.22  ? 36  TRP B CZ3   1 
ATOM   3976 C CH2   . TRP B 2 36  ? 129.102 132.671 99.055  1.00 54.04  ? 36  TRP B CH2   1 
ATOM   3977 N N     . TYR B 2 37  ? 122.624 129.939 97.459  1.00 52.35  ? 37  TYR B N     1 
ATOM   3978 C CA    . TYR B 2 37  ? 121.856 129.500 96.306  1.00 50.04  ? 37  TYR B CA    1 
ATOM   3979 C C     . TYR B 2 37  ? 122.767 129.447 95.088  1.00 52.04  ? 37  TYR B C     1 
ATOM   3980 O O     . TYR B 2 37  ? 123.857 130.022 95.080  1.00 53.14  ? 37  TYR B O     1 
ATOM   3981 C CB    . TYR B 2 37  ? 120.678 130.442 96.028  1.00 50.72  ? 37  TYR B CB    1 
ATOM   3982 C CG    . TYR B 2 37  ? 119.546 130.362 97.027  1.00 52.63  ? 37  TYR B CG    1 
ATOM   3983 C CD1   . TYR B 2 37  ? 119.672 130.905 98.298  1.00 49.68  ? 37  TYR B CD1   1 
ATOM   3984 C CD2   . TYR B 2 37  ? 118.340 129.761 96.690  1.00 53.39  ? 37  TYR B CD2   1 
ATOM   3985 C CE1   . TYR B 2 37  ? 118.635 130.839 99.209  1.00 48.85  ? 37  TYR B CE1   1 
ATOM   3986 C CE2   . TYR B 2 37  ? 117.298 129.690 97.595  1.00 52.99  ? 37  TYR B CE2   1 
ATOM   3987 C CZ    . TYR B 2 37  ? 117.451 130.230 98.853  1.00 52.14  ? 37  TYR B CZ    1 
ATOM   3988 O OH    . TYR B 2 37  ? 116.417 130.163 99.758  1.00 56.81  ? 37  TYR B OH    1 
ATOM   3989 N N     . ARG B 2 38  ? 122.317 128.739 94.055  1.00 57.15  ? 38  ARG B N     1 
ATOM   3990 C CA    . ARG B 2 38  ? 122.989 128.783 92.765  1.00 54.53  ? 38  ARG B CA    1 
ATOM   3991 C C     . ARG B 2 38  ? 121.945 128.805 91.660  1.00 57.23  ? 38  ARG B C     1 
ATOM   3992 O O     . ARG B 2 38  ? 120.864 128.225 91.790  1.00 62.76  ? 38  ARG B O     1 
ATOM   3993 C CB    . ARG B 2 38  ? 123.957 127.606 92.559  1.00 51.50  ? 38  ARG B CB    1 
ATOM   3994 C CG    . ARG B 2 38  ? 123.312 126.265 92.247  1.00 51.45  ? 38  ARG B CG    1 
ATOM   3995 C CD    . ARG B 2 38  ? 124.377 125.180 92.161  1.00 52.96  ? 38  ARG B CD    1 
ATOM   3996 N NE    . ARG B 2 38  ? 123.816 123.838 92.071  1.00 57.98  ? 38  ARG B NE    1 
ATOM   3997 C CZ    . ARG B 2 38  ? 124.513 122.724 92.250  1.00 55.83  ? 38  ARG B CZ    1 
ATOM   3998 N NH1   . ARG B 2 38  ? 125.805 122.756 92.533  1.00 52.24  ? 38  ARG B NH1   1 
ATOM   3999 N NH2   . ARG B 2 38  ? 123.900 121.549 92.141  1.00 59.56  ? 38  ARG B NH2   1 
ATOM   4000 N N     . GLN B 2 39  ? 122.280 129.493 90.571  1.00 54.05  ? 39  GLN B N     1 
ATOM   4001 C CA    . GLN B 2 39  ? 121.389 129.623 89.425  1.00 59.02  ? 39  GLN B CA    1 
ATOM   4002 C C     . GLN B 2 39  ? 122.200 129.439 88.154  1.00 60.68  ? 39  GLN B C     1 
ATOM   4003 O O     . GLN B 2 39  ? 123.166 130.172 87.922  1.00 63.14  ? 39  GLN B O     1 
ATOM   4004 C CB    . GLN B 2 39  ? 120.688 130.984 89.417  1.00 64.50  ? 39  GLN B CB    1 
ATOM   4005 C CG    . GLN B 2 39  ? 119.606 131.110 88.358  1.00 67.96  ? 39  GLN B CG    1 
ATOM   4006 C CD    . GLN B 2 39  ? 118.944 132.473 88.361  1.00 72.92  ? 39  GLN B CD    1 
ATOM   4007 O OE1   . GLN B 2 39  ? 117.718 132.580 88.355  1.00 79.72  ? 39  GLN B OE1   1 
ATOM   4008 N NE2   . GLN B 2 39  ? 119.755 133.524 88.367  1.00 76.33  ? 39  GLN B NE2   1 
ATOM   4009 N N     . ALA B 2 40  ? 121.813 128.479 87.350  1.00 60.67  ? 40  ALA B N     1 
ATOM   4010 C CA    . ALA B 2 40  ? 122.441 128.333 86.051  1.00 66.95  ? 40  ALA B CA    1 
ATOM   4011 C C     . ALA B 2 40  ? 121.530 128.889 84.964  1.00 79.55  ? 40  ALA B C     1 
ATOM   4012 O O     . ALA B 2 40  ? 120.303 128.857 85.100  1.00 86.52  ? 40  ALA B O     1 
ATOM   4013 C CB    . ALA B 2 40  ? 122.751 126.863 85.756  1.00 67.35  ? 40  ALA B CB    1 
ATOM   4014 N N     . PRO B 2 41  ? 122.098 129.426 83.885  1.00 80.30  ? 41  PRO B N     1 
ATOM   4015 C CA    . PRO B 2 41  ? 121.260 129.935 82.792  1.00 75.58  ? 41  PRO B CA    1 
ATOM   4016 C C     . PRO B 2 41  ? 120.383 128.832 82.216  1.00 80.11  ? 41  PRO B C     1 
ATOM   4017 O O     . PRO B 2 41  ? 120.864 127.759 81.847  1.00 83.73  ? 41  PRO B O     1 
ATOM   4018 C CB    . PRO B 2 41  ? 122.283 130.442 81.770  1.00 76.90  ? 41  PRO B CB    1 
ATOM   4019 C CG    . PRO B 2 41  ? 123.502 130.743 82.581  1.00 79.08  ? 41  PRO B CG    1 
ATOM   4020 C CD    . PRO B 2 41  ? 123.527 129.701 83.660  1.00 81.75  ? 41  PRO B CD    1 
ATOM   4021 N N     . GLY B 2 42  ? 119.082 129.107 82.145  1.00 83.15  ? 42  GLY B N     1 
ATOM   4022 C CA    . GLY B 2 42  ? 118.107 128.142 81.687  1.00 87.95  ? 42  GLY B CA    1 
ATOM   4023 C C     . GLY B 2 42  ? 117.391 127.387 82.787  1.00 87.56  ? 42  GLY B C     1 
ATOM   4024 O O     . GLY B 2 42  ? 116.391 126.716 82.503  1.00 90.87  ? 42  GLY B O     1 
ATOM   4025 N N     . LYS B 2 43  ? 117.867 127.475 84.027  1.00 85.29  ? 43  LYS B N     1 
ATOM   4026 C CA    . LYS B 2 43  ? 117.241 126.812 85.160  1.00 85.90  ? 43  LYS B CA    1 
ATOM   4027 C C     . LYS B 2 43  ? 116.907 127.832 86.241  1.00 85.38  ? 43  LYS B C     1 
ATOM   4028 O O     . LYS B 2 43  ? 117.498 128.913 86.312  1.00 81.71  ? 43  LYS B O     1 
ATOM   4029 C CB    . LYS B 2 43  ? 118.145 125.717 85.742  1.00 81.03  ? 43  LYS B CB    1 
ATOM   4030 C CG    . LYS B 2 43  ? 118.765 124.792 84.706  1.00 79.91  ? 43  LYS B CG    1 
ATOM   4031 C CD    . LYS B 2 43  ? 119.144 123.454 85.323  1.00 82.13  ? 43  LYS B CD    1 
ATOM   4032 C CE    . LYS B 2 43  ? 120.321 123.592 86.276  1.00 79.42  ? 43  LYS B CE    1 
ATOM   4033 N NZ    . LYS B 2 43  ? 121.615 123.702 85.548  1.00 75.50  ? 43  LYS B NZ    1 
ATOM   4034 N N     . GLU B 2 44  ? 115.941 127.475 87.083  1.00 85.29  ? 44  GLU B N     1 
ATOM   4035 C CA    . GLU B 2 44  ? 115.528 128.340 88.176  1.00 81.01  ? 44  GLU B CA    1 
ATOM   4036 C C     . GLU B 2 44  ? 116.546 128.297 89.312  1.00 75.05  ? 44  GLU B C     1 
ATOM   4037 O O     . GLU B 2 44  ? 117.347 127.366 89.433  1.00 74.98  ? 44  GLU B O     1 
ATOM   4038 C CB    . GLU B 2 44  ? 114.144 127.938 88.688  1.00 82.84  ? 44  GLU B CB    1 
ATOM   4039 C CG    . GLU B 2 44  ? 114.106 126.602 89.410  1.00 86.38  ? 44  GLU B CG    1 
ATOM   4040 C CD    . GLU B 2 44  ? 113.717 125.456 88.496  1.00 97.19  ? 44  GLU B CD    1 
ATOM   4041 O OE1   . GLU B 2 44  ? 114.315 125.331 87.407  1.00 96.04  ? 44  GLU B OE1   1 
ATOM   4042 O OE2   . GLU B 2 44  ? 112.809 124.681 88.865  1.00 98.20  ? 44  GLU B OE2   1 
ATOM   4043 N N     . ARG B 2 45  ? 116.509 129.334 90.148  1.00 69.78  ? 45  ARG B N     1 
ATOM   4044 C CA    . ARG B 2 45  ? 117.447 129.444 91.258  1.00 62.72  ? 45  ARG B CA    1 
ATOM   4045 C C     . ARG B 2 45  ? 117.268 128.278 92.223  1.00 62.88  ? 45  ARG B C     1 
ATOM   4046 O O     . ARG B 2 45  ? 116.152 127.977 92.656  1.00 69.79  ? 45  ARG B O     1 
ATOM   4047 C CB    . ARG B 2 45  ? 117.243 130.776 91.981  1.00 61.88  ? 45  ARG B CB    1 
ATOM   4048 C CG    . ARG B 2 45  ? 118.320 131.117 92.997  1.00 57.57  ? 45  ARG B CG    1 
ATOM   4049 C CD    . ARG B 2 45  ? 118.169 132.548 93.492  1.00 58.04  ? 45  ARG B CD    1 
ATOM   4050 N NE    . ARG B 2 45  ? 118.584 133.519 92.486  1.00 62.40  ? 45  ARG B NE    1 
ATOM   4051 C CZ    . ARG B 2 45  ? 118.632 134.830 92.683  1.00 59.51  ? 45  ARG B CZ    1 
ATOM   4052 N NH1   . ARG B 2 45  ? 118.292 135.367 93.843  1.00 52.11  ? 45  ARG B NH1   1 
ATOM   4053 N NH2   . ARG B 2 45  ? 119.028 135.621 91.691  1.00 62.95  ? 45  ARG B NH2   1 
ATOM   4054 N N     . GLU B 2 46  ? 118.377 127.626 92.563  1.00 62.03  ? 46  GLU B N     1 
ATOM   4055 C CA    . GLU B 2 46  ? 118.369 126.414 93.371  1.00 58.74  ? 46  GLU B CA    1 
ATOM   4056 C C     . GLU B 2 46  ? 119.086 126.665 94.690  1.00 58.74  ? 46  GLU B C     1 
ATOM   4057 O O     . GLU B 2 46  ? 120.181 127.235 94.708  1.00 58.26  ? 46  GLU B O     1 
ATOM   4058 C CB    . GLU B 2 46  ? 119.036 125.258 92.623  1.00 60.67  ? 46  GLU B CB    1 
ATOM   4059 C CG    . GLU B 2 46  ? 119.064 123.949 93.393  1.00 64.24  ? 46  GLU B CG    1 
ATOM   4060 C CD    . GLU B 2 46  ? 120.047 122.952 92.811  1.00 72.44  ? 46  GLU B CD    1 
ATOM   4061 O OE1   . GLU B 2 46  ? 120.959 123.377 92.071  1.00 66.62  ? 46  GLU B OE1   1 
ATOM   4062 O OE2   . GLU B 2 46  ? 119.908 121.743 93.093  1.00 79.95  ? 46  GLU B OE2   1 
ATOM   4063 N N     . TRP B 2 47  ? 118.467 126.235 95.788  1.00 60.86  ? 47  TRP B N     1 
ATOM   4064 C CA    . TRP B 2 47  ? 119.077 126.351 97.105  1.00 52.98  ? 47  TRP B CA    1 
ATOM   4065 C C     . TRP B 2 47  ? 120.150 125.282 97.271  1.00 52.87  ? 47  TRP B C     1 
ATOM   4066 O O     . TRP B 2 47  ? 119.920 124.106 96.970  1.00 51.83  ? 47  TRP B O     1 
ATOM   4067 C CB    . TRP B 2 47  ? 118.014 126.221 98.195  1.00 49.59  ? 47  TRP B CB    1 
ATOM   4068 C CG    . TRP B 2 47  ? 118.562 125.841 99.532  1.00 50.13  ? 47  TRP B CG    1 
ATOM   4069 C CD1   . TRP B 2 47  ? 119.148 126.669 100.443 1.00 51.83  ? 47  TRP B CD1   1 
ATOM   4070 C CD2   . TRP B 2 47  ? 118.575 124.532 100.113 1.00 51.79  ? 47  TRP B CD2   1 
ATOM   4071 N NE1   . TRP B 2 47  ? 119.526 125.958 101.556 1.00 57.75  ? 47  TRP B NE1   1 
ATOM   4072 C CE2   . TRP B 2 47  ? 119.186 124.643 101.378 1.00 53.60  ? 47  TRP B CE2   1 
ATOM   4073 C CE3   . TRP B 2 47  ? 118.130 123.277 99.687  1.00 52.42  ? 47  TRP B CE3   1 
ATOM   4074 C CZ2   . TRP B 2 47  ? 119.362 123.548 102.220 1.00 53.08  ? 47  TRP B CZ2   1 
ATOM   4075 C CZ3   . TRP B 2 47  ? 118.307 122.191 100.524 1.00 58.21  ? 47  TRP B CZ3   1 
ATOM   4076 C CH2   . TRP B 2 47  ? 118.917 122.333 101.776 1.00 56.85  ? 47  TRP B CH2   1 
ATOM   4077 N N     . VAL B 2 48  ? 121.323 125.689 97.755  1.00 52.70  ? 48  VAL B N     1 
ATOM   4078 C CA    . VAL B 2 48  ? 122.467 124.788 97.843  1.00 49.72  ? 48  VAL B CA    1 
ATOM   4079 C C     . VAL B 2 48  ? 122.736 124.408 99.293  1.00 49.23  ? 48  VAL B C     1 
ATOM   4080 O O     . VAL B 2 48  ? 122.688 123.226 99.654  1.00 51.03  ? 48  VAL B O     1 
ATOM   4081 C CB    . VAL B 2 48  ? 123.717 125.422 97.205  1.00 48.23  ? 48  VAL B CB    1 
ATOM   4082 C CG1   . VAL B 2 48  ? 124.969 124.667 97.619  1.00 50.91  ? 48  VAL B CG1   1 
ATOM   4083 C CG2   . VAL B 2 48  ? 123.582 125.447 95.698  1.00 52.88  ? 48  VAL B CG2   1 
ATOM   4084 N N     . ALA B 2 49  ? 123.020 125.401 100.133 1.00 50.98  ? 49  ALA B N     1 
ATOM   4085 C CA    . ALA B 2 49  ? 123.407 125.152 101.512 1.00 44.24  ? 49  ALA B CA    1 
ATOM   4086 C C     . ALA B 2 49  ? 122.777 126.201 102.415 1.00 47.16  ? 49  ALA B C     1 
ATOM   4087 O O     . ALA B 2 49  ? 122.321 127.252 101.960 1.00 53.22  ? 49  ALA B O     1 
ATOM   4088 C CB    . ALA B 2 49  ? 124.933 125.158 101.680 1.00 47.87  ? 49  ALA B CB    1 
ATOM   4089 N N     . ALA B 2 50  ? 122.752 125.896 103.711 1.00 52.43  ? 50  ALA B N     1 
ATOM   4090 C CA    . ALA B 2 50  ? 122.192 126.799 104.703 1.00 45.39  ? 50  ALA B CA    1 
ATOM   4091 C C     . ALA B 2 50  ? 122.892 126.577 106.036 1.00 45.85  ? 50  ALA B C     1 
ATOM   4092 O O     . ALA B 2 50  ? 123.191 125.439 106.406 1.00 52.99  ? 50  ALA B O     1 
ATOM   4093 C CB    . ALA B 2 50  ? 120.680 126.592 104.859 1.00 45.56  ? 50  ALA B CB    1 
ATOM   4094 N N     . ILE B 2 51  ? 123.148 127.671 106.748 1.00 48.27  ? 51  ILE B N     1 
ATOM   4095 C CA    . ILE B 2 51  ? 123.718 127.630 108.089 1.00 43.81  ? 51  ILE B CA    1 
ATOM   4096 C C     . ILE B 2 51  ? 122.835 128.461 109.010 1.00 46.48  ? 51  ILE B C     1 
ATOM   4097 O O     . ILE B 2 51  ? 122.293 129.495 108.604 1.00 51.20  ? 51  ILE B O     1 
ATOM   4098 C CB    . ILE B 2 51  ? 125.183 128.126 108.114 1.00 41.61  ? 51  ILE B CB    1 
ATOM   4099 C CG1   . ILE B 2 51  ? 125.864 127.726 109.425 1.00 41.88  ? 51  ILE B CG1   1 
ATOM   4100 C CG2   . ILE B 2 51  ? 125.268 129.627 107.893 1.00 43.10  ? 51  ILE B CG2   1 
ATOM   4101 C CD1   . ILE B 2 51  ? 127.351 128.003 109.450 1.00 44.79  ? 51  ILE B CD1   1 
ATOM   4102 N N     . TYR B 2 52  ? 122.661 127.987 110.239 1.00 46.25  ? 52  TYR B N     1 
ATOM   4103 C CA    . TYR B 2 52  ? 121.808 128.638 111.219 1.00 45.76  ? 52  TYR B CA    1 
ATOM   4104 C C     . TYR B 2 52  ? 122.652 129.319 112.288 1.00 52.10  ? 52  TYR B C     1 
ATOM   4105 O O     . TYR B 2 52  ? 123.851 129.062 112.424 1.00 52.75  ? 52  TYR B O     1 
ATOM   4106 C CB    . TYR B 2 52  ? 120.853 127.633 111.872 1.00 46.74  ? 52  TYR B CB    1 
ATOM   4107 C CG    . TYR B 2 52  ? 119.696 127.234 110.989 1.00 53.32  ? 52  TYR B CG    1 
ATOM   4108 C CD1   . TYR B 2 52  ? 119.828 126.211 110.060 1.00 52.99  ? 52  TYR B CD1   1 
ATOM   4109 C CD2   . TYR B 2 52  ? 118.472 127.885 111.078 1.00 55.05  ? 52  TYR B CD2   1 
ATOM   4110 C CE1   . TYR B 2 52  ? 118.772 125.844 109.247 1.00 52.49  ? 52  TYR B CE1   1 
ATOM   4111 C CE2   . TYR B 2 52  ? 117.411 127.525 110.270 1.00 54.90  ? 52  TYR B CE2   1 
ATOM   4112 C CZ    . TYR B 2 52  ? 117.568 126.505 109.357 1.00 55.33  ? 52  TYR B CZ    1 
ATOM   4113 O OH    . TYR B 2 52  ? 116.515 126.144 108.549 1.00 56.38  ? 52  TYR B OH    1 
ATOM   4114 N N     . SER B 2 53  ? 121.999 130.200 113.051 1.00 54.95  ? 53  SER B N     1 
ATOM   4115 C CA    . SER B 2 53  ? 122.680 130.891 114.142 1.00 54.08  ? 53  SER B CA    1 
ATOM   4116 C C     . SER B 2 53  ? 123.232 129.911 115.168 1.00 57.12  ? 53  SER B C     1 
ATOM   4117 O O     . SER B 2 53  ? 124.231 130.205 115.835 1.00 59.60  ? 53  SER B O     1 
ATOM   4118 C CB    . SER B 2 53  ? 121.726 131.881 114.810 1.00 53.93  ? 53  SER B CB    1 
ATOM   4119 O OG    . SER B 2 53  ? 120.624 131.213 115.396 1.00 64.89  ? 53  SER B OG    1 
ATOM   4120 N N     . SER B 2 54  ? 122.601 128.745 115.307 1.00 54.65  ? 54  SER B N     1 
ATOM   4121 C CA    . SER B 2 54  ? 123.110 127.696 116.181 1.00 50.91  ? 54  SER B CA    1 
ATOM   4122 C C     . SER B 2 54  ? 124.312 126.973 115.593 1.00 52.83  ? 54  SER B C     1 
ATOM   4123 O O     . SER B 2 54  ? 124.884 126.110 116.268 1.00 60.08  ? 54  SER B O     1 
ATOM   4124 C CB    . SER B 2 54  ? 122.002 126.689 116.484 1.00 54.01  ? 54  SER B CB    1 
ATOM   4125 O OG    . SER B 2 54  ? 122.493 125.592 117.233 1.00 64.13  ? 54  SER B OG    1 
ATOM   4126 N N     . GLY B 2 55  ? 124.704 127.295 114.362 1.00 52.60  ? 55  GLY B N     1 
ATOM   4127 C CA    . GLY B 2 55  ? 125.750 126.571 113.679 1.00 50.27  ? 55  GLY B CA    1 
ATOM   4128 C C     . GLY B 2 55  ? 125.285 125.328 112.957 1.00 50.10  ? 55  GLY B C     1 
ATOM   4129 O O     . GLY B 2 55  ? 126.115 124.625 112.367 1.00 50.64  ? 55  GLY B O     1 
ATOM   4130 N N     . TYR B 2 56  ? 123.988 125.033 112.987 1.00 50.39  ? 56  TYR B N     1 
ATOM   4131 C CA    . TYR B 2 56  ? 123.468 123.855 112.311 1.00 46.98  ? 56  TYR B CA    1 
ATOM   4132 C C     . TYR B 2 56  ? 123.515 124.054 110.801 1.00 50.51  ? 56  TYR B C     1 
ATOM   4133 O O     . TYR B 2 56  ? 123.126 125.109 110.290 1.00 55.05  ? 56  TYR B O     1 
ATOM   4134 C CB    . TYR B 2 56  ? 122.040 123.575 112.768 1.00 50.22  ? 56  TYR B CB    1 
ATOM   4135 C CG    . TYR B 2 56  ? 121.428 122.375 112.100 1.00 53.95  ? 56  TYR B CG    1 
ATOM   4136 C CD1   . TYR B 2 56  ? 122.100 121.162 112.070 1.00 55.64  ? 56  TYR B CD1   1 
ATOM   4137 C CD2   . TYR B 2 56  ? 120.186 122.453 111.493 1.00 51.56  ? 56  TYR B CD2   1 
ATOM   4138 C CE1   . TYR B 2 56  ? 121.550 120.058 111.460 1.00 54.80  ? 56  TYR B CE1   1 
ATOM   4139 C CE2   . TYR B 2 56  ? 119.629 121.356 110.880 1.00 52.61  ? 56  TYR B CE2   1 
ATOM   4140 C CZ    . TYR B 2 56  ? 120.315 120.159 110.866 1.00 55.82  ? 56  TYR B CZ    1 
ATOM   4141 O OH    . TYR B 2 56  ? 119.771 119.055 110.257 1.00 67.73  ? 56  TYR B OH    1 
ATOM   4142 N N     . THR B 2 57  ? 123.982 123.035 110.087 1.00 53.36  ? 57  THR B N     1 
ATOM   4143 C CA    . THR B 2 57  ? 124.201 123.117 108.651 1.00 45.46  ? 57  THR B CA    1 
ATOM   4144 C C     . THR B 2 57  ? 123.277 122.158 107.916 1.00 49.33  ? 57  THR B C     1 
ATOM   4145 O O     . THR B 2 57  ? 123.091 121.010 108.335 1.00 56.62  ? 57  THR B O     1 
ATOM   4146 C CB    . THR B 2 57  ? 125.657 122.801 108.299 1.00 44.10  ? 57  THR B CB    1 
ATOM   4147 O OG1   . THR B 2 57  ? 126.030 121.551 108.890 1.00 57.40  ? 57  THR B OG1   1 
ATOM   4148 C CG2   . THR B 2 57  ? 126.575 123.893 108.822 1.00 45.26  ? 57  THR B CG2   1 
ATOM   4149 N N     . ARG B 2 58  ? 122.705 122.636 106.818 1.00 49.67  ? 58  ARG B N     1 
ATOM   4150 C CA    . ARG B 2 58  ? 121.840 121.836 105.968 1.00 48.49  ? 58  ARG B CA    1 
ATOM   4151 C C     . ARG B 2 58  ? 122.296 121.972 104.525 1.00 49.04  ? 58  ARG B C     1 
ATOM   4152 O O     . ARG B 2 58  ? 122.701 123.056 104.095 1.00 49.94  ? 58  ARG B O     1 
ATOM   4153 C CB    . ARG B 2 58  ? 120.393 122.270 106.095 1.00 47.24  ? 58  ARG B CB    1 
ATOM   4154 C CG    . ARG B 2 58  ? 119.600 121.559 107.172 1.00 51.27  ? 58  ARG B CG    1 
ATOM   4155 C CD    . ARG B 2 58  ? 118.140 121.871 106.944 1.00 60.45  ? 58  ARG B CD    1 
ATOM   4156 N NE    . ARG B 2 58  ? 118.007 123.227 106.427 1.00 65.82  ? 58  ARG B NE    1 
ATOM   4157 C CZ    . ARG B 2 58  ? 117.453 123.530 105.262 1.00 69.76  ? 58  ARG B CZ    1 
ATOM   4158 N NH1   . ARG B 2 58  ? 116.999 122.594 104.449 1.00 68.68  ? 58  ARG B NH1   1 
ATOM   4159 N NH2   . ARG B 2 58  ? 117.364 124.803 104.900 1.00 60.68  ? 58  ARG B NH2   1 
ATOM   4160 N N     . TYR B 2 59  ? 122.227 120.872 103.778 1.00 50.38  ? 59  TYR B N     1 
ATOM   4161 C CA    . TYR B 2 59  ? 122.747 120.828 102.421 1.00 50.88  ? 59  TYR B CA    1 
ATOM   4162 C C     . TYR B 2 59  ? 121.740 120.165 101.493 1.00 55.19  ? 59  TYR B C     1 
ATOM   4163 O O     . TYR B 2 59  ? 120.926 119.340 101.918 1.00 56.99  ? 59  TYR B O     1 
ATOM   4164 C CB    . TYR B 2 59  ? 124.077 120.066 102.360 1.00 49.96  ? 59  TYR B CB    1 
ATOM   4165 C CG    . TYR B 2 59  ? 125.148 120.645 103.253 1.00 48.89  ? 59  TYR B CG    1 
ATOM   4166 C CD1   . TYR B 2 59  ? 125.986 121.654 102.801 1.00 49.27  ? 59  TYR B CD1   1 
ATOM   4167 C CD2   . TYR B 2 59  ? 125.321 120.181 104.551 1.00 46.78  ? 59  TYR B CD2   1 
ATOM   4168 C CE1   . TYR B 2 59  ? 126.965 122.186 103.616 1.00 45.23  ? 59  TYR B CE1   1 
ATOM   4169 C CE2   . TYR B 2 59  ? 126.298 120.705 105.372 1.00 48.15  ? 59  TYR B CE2   1 
ATOM   4170 C CZ    . TYR B 2 59  ? 127.118 121.707 104.900 1.00 45.68  ? 59  TYR B CZ    1 
ATOM   4171 O OH    . TYR B 2 59  ? 128.092 122.232 105.717 1.00 52.81  ? 59  TYR B OH    1 
ATOM   4172 N N     . ALA B 2 60  ? 121.802 120.540 100.219 1.00 55.64  ? 60  ALA B N     1 
ATOM   4173 C CA    . ALA B 2 60  ? 121.005 119.885 99.195  1.00 54.38  ? 60  ALA B CA    1 
ATOM   4174 C C     . ALA B 2 60  ? 121.613 118.533 98.843  1.00 60.12  ? 60  ALA B C     1 
ATOM   4175 O O     . ALA B 2 60  ? 122.820 118.316 98.984  1.00 62.72  ? 60  ALA B O     1 
ATOM   4176 C CB    . ALA B 2 60  ? 120.904 120.759 97.946  1.00 52.46  ? 60  ALA B CB    1 
ATOM   4177 N N     . ASP B 2 61  ? 120.758 117.618 98.376  1.00 60.05  ? 61  ASP B N     1 
ATOM   4178 C CA    . ASP B 2 61  ? 121.214 116.266 98.068  1.00 63.44  ? 61  ASP B CA    1 
ATOM   4179 C C     . ASP B 2 61  ? 122.269 116.258 96.969  1.00 67.66  ? 61  ASP B C     1 
ATOM   4180 O O     . ASP B 2 61  ? 123.166 115.407 96.978  1.00 72.40  ? 61  ASP B O     1 
ATOM   4181 C CB    . ASP B 2 61  ? 120.027 115.390 97.668  1.00 70.56  ? 61  ASP B CB    1 
ATOM   4182 C CG    . ASP B 2 61  ? 119.094 115.107 98.828  1.00 76.58  ? 61  ASP B CG    1 
ATOM   4183 O OD1   . ASP B 2 61  ? 119.579 115.032 99.977  1.00 78.43  ? 61  ASP B OD1   1 
ATOM   4184 O OD2   . ASP B 2 61  ? 117.877 114.959 98.591  1.00 80.14  ? 61  ASP B OD2   1 
ATOM   4185 N N     . SER B 2 62  ? 122.184 117.191 96.020  1.00 63.91  ? 62  SER B N     1 
ATOM   4186 C CA    . SER B 2 62  ? 123.143 117.241 94.924  1.00 62.70  ? 62  SER B CA    1 
ATOM   4187 C C     . SER B 2 62  ? 124.519 117.729 95.359  1.00 63.87  ? 62  SER B C     1 
ATOM   4188 O O     . SER B 2 62  ? 125.482 117.556 94.604  1.00 66.85  ? 62  SER B O     1 
ATOM   4189 C CB    . SER B 2 62  ? 122.611 118.137 93.804  1.00 65.39  ? 62  SER B CB    1 
ATOM   4190 O OG    . SER B 2 62  ? 122.503 119.482 94.236  1.00 65.42  ? 62  SER B OG    1 
ATOM   4191 N N     . VAL B 2 63  ? 124.638 118.329 96.542  1.00 62.57  ? 63  VAL B N     1 
ATOM   4192 C CA    . VAL B 2 63  ? 125.910 118.874 97.002  1.00 59.43  ? 63  VAL B CA    1 
ATOM   4193 C C     . VAL B 2 63  ? 126.277 118.272 98.352  1.00 59.64  ? 63  VAL B C     1 
ATOM   4194 O O     . VAL B 2 63  ? 127.365 118.529 98.881  1.00 60.63  ? 63  VAL B O     1 
ATOM   4195 C CB    . VAL B 2 63  ? 125.859 120.410 97.090  1.00 63.20  ? 63  VAL B CB    1 
ATOM   4196 C CG1   . VAL B 2 63  ? 125.410 121.010 95.767  1.00 62.56  ? 63  VAL B CG1   1 
ATOM   4197 C CG2   . VAL B 2 63  ? 124.943 120.847 98.223  1.00 60.42  ? 63  VAL B CG2   1 
ATOM   4198 N N     . LYS B 2 64  ? 125.375 117.474 98.920  1.00 64.01  ? 64  LYS B N     1 
ATOM   4199 C CA    . LYS B 2 64  ? 125.606 116.906 100.242 1.00 59.25  ? 64  LYS B CA    1 
ATOM   4200 C C     . LYS B 2 64  ? 126.810 115.974 100.219 1.00 61.03  ? 64  LYS B C     1 
ATOM   4201 O O     . LYS B 2 64  ? 126.887 115.055 99.398  1.00 63.83  ? 64  LYS B O     1 
ATOM   4202 C CB    . LYS B 2 64  ? 124.361 116.160 100.720 1.00 60.13  ? 64  LYS B CB    1 
ATOM   4203 C CG    . LYS B 2 64  ? 124.330 115.890 102.215 1.00 64.32  ? 64  LYS B CG    1 
ATOM   4204 C CD    . LYS B 2 64  ? 123.005 115.272 102.630 1.00 67.34  ? 64  LYS B CD    1 
ATOM   4205 C CE    . LYS B 2 64  ? 121.848 116.216 102.341 1.00 66.70  ? 64  LYS B CE    1 
ATOM   4206 N NZ    . LYS B 2 64  ? 120.534 115.515 102.346 1.00 70.77  ? 64  LYS B NZ    1 
ATOM   4207 N N     . GLY B 2 65  ? 127.753 116.215 101.131 1.00 60.15  ? 65  GLY B N     1 
ATOM   4208 C CA    . GLY B 2 65  ? 128.997 115.490 101.199 1.00 58.06  ? 65  GLY B CA    1 
ATOM   4209 C C     . GLY B 2 65  ? 130.152 116.185 100.505 1.00 57.30  ? 65  GLY B C     1 
ATOM   4210 O O     . GLY B 2 65  ? 131.301 116.038 100.936 1.00 56.47  ? 65  GLY B O     1 
ATOM   4211 N N     . ARG B 2 66  ? 129.872 116.942 99.444  1.00 57.69  ? 66  ARG B N     1 
ATOM   4212 C CA    . ARG B 2 66  ? 130.911 117.661 98.717  1.00 57.47  ? 66  ARG B CA    1 
ATOM   4213 C C     . ARG B 2 66  ? 131.043 119.109 99.174  1.00 55.03  ? 66  ARG B C     1 
ATOM   4214 O O     . ARG B 2 66  ? 132.158 119.640 99.230  1.00 52.81  ? 66  ARG B O     1 
ATOM   4215 C CB    . ARG B 2 66  ? 130.629 117.620 97.213  1.00 57.56  ? 66  ARG B CB    1 
ATOM   4216 C CG    . ARG B 2 66  ? 130.433 116.222 96.651  1.00 56.61  ? 66  ARG B CG    1 
ATOM   4217 C CD    . ARG B 2 66  ? 130.231 116.262 95.144  1.00 61.05  ? 66  ARG B CD    1 
ATOM   4218 N NE    . ARG B 2 66  ? 129.045 117.024 94.771  1.00 63.03  ? 66  ARG B NE    1 
ATOM   4219 C CZ    . ARG B 2 66  ? 129.060 118.104 94.002  1.00 59.14  ? 66  ARG B CZ    1 
ATOM   4220 N NH1   . ARG B 2 66  ? 130.188 118.583 93.504  1.00 55.11  ? 66  ARG B NH1   1 
ATOM   4221 N NH2   . ARG B 2 66  ? 127.914 118.720 93.727  1.00 60.05  ? 66  ARG B NH2   1 
ATOM   4222 N N     . PHE B 2 67  ? 129.931 119.758 99.503  1.00 58.08  ? 67  PHE B N     1 
ATOM   4223 C CA    . PHE B 2 67  ? 129.938 121.151 99.923  1.00 57.21  ? 67  PHE B CA    1 
ATOM   4224 C C     . PHE B 2 67  ? 129.883 121.244 101.443 1.00 53.95  ? 67  PHE B C     1 
ATOM   4225 O O     . PHE B 2 67  ? 129.360 120.355 102.120 1.00 51.29  ? 67  PHE B O     1 
ATOM   4226 C CB    . PHE B 2 67  ? 128.762 121.926 99.318  1.00 57.38  ? 67  PHE B CB    1 
ATOM   4227 C CG    . PHE B 2 67  ? 128.878 122.173 97.833  1.00 57.92  ? 67  PHE B CG    1 
ATOM   4228 C CD1   . PHE B 2 67  ? 129.766 121.454 97.049  1.00 55.93  ? 67  PHE B CD1   1 
ATOM   4229 C CD2   . PHE B 2 67  ? 128.097 123.141 97.225  1.00 56.10  ? 67  PHE B CD2   1 
ATOM   4230 C CE1   . PHE B 2 67  ? 129.863 121.687 95.690  1.00 53.61  ? 67  PHE B CE1   1 
ATOM   4231 C CE2   . PHE B 2 67  ? 128.191 123.381 95.867  1.00 56.00  ? 67  PHE B CE2   1 
ATOM   4232 C CZ    . PHE B 2 67  ? 129.076 122.654 95.100  1.00 57.13  ? 67  PHE B CZ    1 
ATOM   4233 N N     . THR B 2 68  ? 130.433 122.334 101.973 1.00 52.88  ? 68  THR B N     1 
ATOM   4234 C CA    . THR B 2 68  ? 130.444 122.565 103.414 1.00 50.83  ? 68  THR B CA    1 
ATOM   4235 C C     . THR B 2 68  ? 130.294 124.056 103.668 1.00 50.43  ? 68  THR B C     1 
ATOM   4236 O O     . THR B 2 68  ? 131.135 124.847 103.230 1.00 52.12  ? 68  THR B O     1 
ATOM   4237 C CB    . THR B 2 68  ? 131.731 122.038 104.051 1.00 52.90  ? 68  THR B CB    1 
ATOM   4238 O OG1   . THR B 2 68  ? 131.840 120.628 103.818 1.00 55.76  ? 68  THR B OG1   1 
ATOM   4239 C CG2   . THR B 2 68  ? 131.728 122.300 105.550 1.00 48.81  ? 68  THR B CG2   1 
ATOM   4240 N N     . ILE B 2 69  ? 129.232 124.435 104.373 1.00 48.94  ? 69  ILE B N     1 
ATOM   4241 C CA    . ILE B 2 69  ? 128.979 125.826 104.733 1.00 46.42  ? 69  ILE B CA    1 
ATOM   4242 C C     . ILE B 2 69  ? 129.460 126.066 106.156 1.00 48.96  ? 69  ILE B C     1 
ATOM   4243 O O     . ILE B 2 69  ? 129.241 125.241 107.054 1.00 51.15  ? 69  ILE B O     1 
ATOM   4244 C CB    . ILE B 2 69  ? 127.488 126.192 104.569 1.00 43.51  ? 69  ILE B CB    1 
ATOM   4245 C CG1   . ILE B 2 69  ? 127.282 127.698 104.751 1.00 47.01  ? 69  ILE B CG1   1 
ATOM   4246 C CG2   . ILE B 2 69  ? 126.604 125.386 105.513 1.00 40.84  ? 69  ILE B CG2   1 
ATOM   4247 C CD1   . ILE B 2 69  ? 125.884 128.170 104.416 1.00 44.91  ? 69  ILE B CD1   1 
ATOM   4248 N N     . SER B 2 70  ? 130.151 127.185 106.356 1.00 51.36  ? 70  SER B N     1 
ATOM   4249 C CA    . SER B 2 70  ? 130.658 127.569 107.664 1.00 51.85  ? 70  SER B CA    1 
ATOM   4250 C C     . SER B 2 70  ? 130.665 129.090 107.741 1.00 56.48  ? 70  SER B C     1 
ATOM   4251 O O     . SER B 2 70  ? 130.219 129.780 106.820 1.00 56.39  ? 70  SER B O     1 
ATOM   4252 C CB    . SER B 2 70  ? 132.052 126.985 107.911 1.00 54.80  ? 70  SER B CB    1 
ATOM   4253 O OG    . SER B 2 70  ? 132.988 127.485 106.973 1.00 57.57  ? 70  SER B OG    1 
ATOM   4254 N N     . ARG B 2 71  ? 131.174 129.614 108.853 1.00 59.68  ? 71  ARG B N     1 
ATOM   4255 C CA    . ARG B 2 71  ? 131.235 131.056 109.025 1.00 59.16  ? 71  ARG B CA    1 
ATOM   4256 C C     . ARG B 2 71  ? 132.357 131.409 109.986 1.00 59.62  ? 71  ARG B C     1 
ATOM   4257 O O     . ARG B 2 71  ? 132.691 130.635 110.888 1.00 61.01  ? 71  ARG B O     1 
ATOM   4258 C CB    . ARG B 2 71  ? 129.903 131.621 109.534 1.00 56.54  ? 71  ARG B CB    1 
ATOM   4259 C CG    . ARG B 2 71  ? 129.548 131.202 110.949 1.00 53.53  ? 71  ARG B CG    1 
ATOM   4260 C CD    . ARG B 2 71  ? 128.075 131.429 111.229 1.00 50.59  ? 71  ARG B CD    1 
ATOM   4261 N NE    . ARG B 2 71  ? 127.707 131.035 112.583 1.00 53.71  ? 71  ARG B NE    1 
ATOM   4262 C CZ    . ARG B 2 71  ? 126.508 130.585 112.926 1.00 55.92  ? 71  ARG B CZ    1 
ATOM   4263 N NH1   . ARG B 2 71  ? 125.535 130.471 112.038 1.00 49.39  ? 71  ARG B NH1   1 
ATOM   4264 N NH2   . ARG B 2 71  ? 126.280 130.242 114.191 1.00 60.75  ? 71  ARG B NH2   1 
ATOM   4265 N N     . ASP B 2 72  ? 132.938 132.588 109.774 1.00 63.23  ? 72  ASP B N     1 
ATOM   4266 C CA    . ASP B 2 72  ? 133.928 133.156 110.682 1.00 62.72  ? 72  ASP B CA    1 
ATOM   4267 C C     . ASP B 2 72  ? 133.289 134.359 111.362 1.00 67.47  ? 72  ASP B C     1 
ATOM   4268 O O     . ASP B 2 72  ? 132.955 135.349 110.702 1.00 70.44  ? 72  ASP B O     1 
ATOM   4269 C CB    . ASP B 2 72  ? 135.208 133.552 109.946 1.00 68.40  ? 72  ASP B CB    1 
ATOM   4270 C CG    . ASP B 2 72  ? 136.358 133.848 110.895 1.00 77.37  ? 72  ASP B CG    1 
ATOM   4271 O OD1   . ASP B 2 72  ? 136.151 133.786 112.127 1.00 80.17  ? 72  ASP B OD1   1 
ATOM   4272 O OD2   . ASP B 2 72  ? 137.468 134.145 110.411 1.00 82.52  ? 72  ASP B OD2   1 
ATOM   4273 N N     . ASN B 2 73  ? 133.125 134.263 112.682 1.00 70.48  ? 73  ASN B N     1 
ATOM   4274 C CA    . ASN B 2 73  ? 132.526 135.332 113.472 1.00 68.61  ? 73  ASN B CA    1 
ATOM   4275 C C     . ASN B 2 73  ? 133.397 136.579 113.501 1.00 69.34  ? 73  ASN B C     1 
ATOM   4276 O O     . ASN B 2 73  ? 132.880 137.696 113.389 1.00 69.13  ? 73  ASN B O     1 
ATOM   4277 C CB    . ASN B 2 73  ? 132.291 134.821 114.889 1.00 73.64  ? 73  ASN B CB    1 
ATOM   4278 C CG    . ASN B 2 73  ? 131.146 133.856 114.968 1.00 73.12  ? 73  ASN B CG    1 
ATOM   4279 O OD1   . ASN B 2 73  ? 131.188 132.783 114.384 1.00 69.33  ? 73  ASN B OD1   1 
ATOM   4280 N ND2   . ASN B 2 73  ? 130.149 134.196 115.754 1.00 78.57  ? 73  ASN B ND2   1 
ATOM   4281 N N     . SER B 2 74  ? 134.710 136.413 113.665 1.00 69.80  ? 74  SER B N     1 
ATOM   4282 C CA    . SER B 2 74  ? 135.602 137.564 113.747 1.00 74.94  ? 74  SER B CA    1 
ATOM   4283 C C     . SER B 2 74  ? 135.595 138.357 112.446 1.00 78.09  ? 74  SER B C     1 
ATOM   4284 O O     . SER B 2 74  ? 135.575 139.595 112.453 1.00 83.42  ? 74  SER B O     1 
ATOM   4285 C CB    . SER B 2 74  ? 137.015 137.096 114.094 1.00 80.09  ? 74  SER B CB    1 
ATOM   4286 O OG    . SER B 2 74  ? 137.959 138.129 113.894 1.00 88.73  ? 74  SER B OG    1 
ATOM   4287 N N     . LYS B 2 75  ? 135.608 137.657 111.314 1.00 74.91  ? 75  LYS B N     1 
ATOM   4288 C CA    . LYS B 2 75  ? 135.574 138.311 110.015 1.00 71.52  ? 75  LYS B CA    1 
ATOM   4289 C C     . LYS B 2 75  ? 134.161 138.637 109.550 1.00 71.39  ? 75  LYS B C     1 
ATOM   4290 O O     . LYS B 2 75  ? 134.010 139.342 108.546 1.00 75.54  ? 75  LYS B O     1 
ATOM   4291 C CB    . LYS B 2 75  ? 136.264 137.436 108.965 1.00 72.09  ? 75  LYS B CB    1 
ATOM   4292 C CG    . LYS B 2 75  ? 137.763 137.289 109.156 1.00 76.77  ? 75  LYS B CG    1 
ATOM   4293 C CD    . LYS B 2 75  ? 138.362 136.383 108.091 1.00 79.17  ? 75  LYS B CD    1 
ATOM   4294 C CE    . LYS B 2 75  ? 139.880 136.373 108.157 1.00 83.51  ? 75  LYS B CE    1 
ATOM   4295 N NZ    . LYS B 2 75  ? 140.372 135.908 109.484 1.00 86.90  ? 75  LYS B NZ    1 
ATOM   4296 N N     . ASN B 2 76  ? 133.136 138.153 110.256 1.00 68.60  ? 76  ASN B N     1 
ATOM   4297 C CA    . ASN B 2 76  ? 131.738 138.314 109.848 1.00 63.63  ? 76  ASN B CA    1 
ATOM   4298 C C     . ASN B 2 76  ? 131.534 137.820 108.416 1.00 63.96  ? 76  ASN B C     1 
ATOM   4299 O O     . ASN B 2 76  ? 130.926 138.490 107.578 1.00 64.56  ? 76  ASN B O     1 
ATOM   4300 C CB    . ASN B 2 76  ? 131.278 139.765 110.006 1.00 63.91  ? 76  ASN B CB    1 
ATOM   4301 C CG    . ASN B 2 76  ? 129.819 139.873 110.400 1.00 64.81  ? 76  ASN B CG    1 
ATOM   4302 O OD1   . ASN B 2 76  ? 129.344 139.141 111.269 1.00 66.09  ? 76  ASN B OD1   1 
ATOM   4303 N ND2   . ASN B 2 76  ? 129.099 140.789 109.763 1.00 64.97  ? 76  ASN B ND2   1 
ATOM   4304 N N     . THR B 2 77  ? 132.057 136.628 108.142 1.00 66.54  ? 77  THR B N     1 
ATOM   4305 C CA    . THR B 2 77  ? 132.054 136.046 106.810 1.00 59.85  ? 77  THR B CA    1 
ATOM   4306 C C     . THR B 2 77  ? 131.443 134.653 106.857 1.00 56.13  ? 77  THR B C     1 
ATOM   4307 O O     . THR B 2 77  ? 131.587 133.930 107.844 1.00 59.24  ? 77  THR B O     1 
ATOM   4308 C CB    . THR B 2 77  ? 133.478 135.973 106.234 1.00 63.71  ? 77  THR B CB    1 
ATOM   4309 O OG1   . THR B 2 77  ? 134.183 137.181 106.544 1.00 72.00  ? 77  THR B OG1   1 
ATOM   4310 C CG2   . THR B 2 77  ? 133.448 135.783 104.729 1.00 58.55  ? 77  THR B CG2   1 
ATOM   4311 N N     . VAL B 2 78  ? 130.755 134.288 105.777 1.00 59.15  ? 78  VAL B N     1 
ATOM   4312 C CA    . VAL B 2 78  ? 130.170 132.962 105.612 1.00 54.22  ? 78  VAL B CA    1 
ATOM   4313 C C     . VAL B 2 78  ? 130.837 132.301 104.415 1.00 56.09  ? 78  VAL B C     1 
ATOM   4314 O O     . VAL B 2 78  ? 130.881 132.881 103.324 1.00 56.47  ? 78  VAL B O     1 
ATOM   4315 C CB    . VAL B 2 78  ? 128.644 133.032 105.424 1.00 51.97  ? 78  VAL B CB    1 
ATOM   4316 C CG1   . VAL B 2 78  ? 128.085 131.660 105.077 1.00 48.75  ? 78  VAL B CG1   1 
ATOM   4317 C CG2   . VAL B 2 78  ? 127.983 133.579 106.679 1.00 56.79  ? 78  VAL B CG2   1 
ATOM   4318 N N     . TYR B 2 79  ? 131.355 131.094 104.617 1.00 56.63  ? 79  TYR B N     1 
ATOM   4319 C CA    . TYR B 2 79  ? 132.120 130.395 103.597 1.00 55.03  ? 79  TYR B CA    1 
ATOM   4320 C C     . TYR B 2 79  ? 131.352 129.190 103.072 1.00 50.31  ? 79  TYR B C     1 
ATOM   4321 O O     . TYR B 2 79  ? 130.590 128.548 103.800 1.00 48.67  ? 79  TYR B O     1 
ATOM   4322 C CB    . TYR B 2 79  ? 133.475 129.934 104.141 1.00 56.35  ? 79  TYR B CB    1 
ATOM   4323 C CG    . TYR B 2 79  ? 134.305 131.037 104.754 1.00 57.56  ? 79  TYR B CG    1 
ATOM   4324 C CD1   . TYR B 2 79  ? 135.021 131.918 103.955 1.00 61.55  ? 79  TYR B CD1   1 
ATOM   4325 C CD2   . TYR B 2 79  ? 134.378 131.193 106.131 1.00 54.63  ? 79  TYR B CD2   1 
ATOM   4326 C CE1   . TYR B 2 79  ? 135.784 132.926 104.510 1.00 62.50  ? 79  TYR B CE1   1 
ATOM   4327 C CE2   . TYR B 2 79  ? 135.138 132.198 106.695 1.00 58.95  ? 79  TYR B CE2   1 
ATOM   4328 C CZ    . TYR B 2 79  ? 135.839 133.062 105.881 1.00 64.02  ? 79  TYR B CZ    1 
ATOM   4329 O OH    . TYR B 2 79  ? 136.597 134.064 106.440 1.00 72.40  ? 79  TYR B OH    1 
ATOM   4330 N N     . LEU B 2 80  ? 131.560 128.897 101.790 1.00 53.24  ? 80  LEU B N     1 
ATOM   4331 C CA    . LEU B 2 80  ? 131.053 127.685 101.157 1.00 53.55  ? 80  LEU B CA    1 
ATOM   4332 C C     . LEU B 2 80  ? 132.228 126.970 100.505 1.00 54.73  ? 80  LEU B C     1 
ATOM   4333 O O     . LEU B 2 80  ? 132.703 127.390 99.445  1.00 53.07  ? 80  LEU B O     1 
ATOM   4334 C CB    . LEU B 2 80  ? 129.969 128.001 100.127 1.00 46.14  ? 80  LEU B CB    1 
ATOM   4335 C CG    . LEU B 2 80  ? 129.272 126.781 99.521  1.00 44.49  ? 80  LEU B CG    1 
ATOM   4336 C CD1   . LEU B 2 80  ? 128.308 126.158 100.517 1.00 44.61  ? 80  LEU B CD1   1 
ATOM   4337 C CD2   . LEU B 2 80  ? 128.555 127.148 98.230  1.00 51.65  ? 80  LEU B CD2   1 
ATOM   4338 N N     . GLN B 2 81  ? 132.697 125.898 101.137 1.00 51.66  ? 81  GLN B N     1 
ATOM   4339 C CA    . GLN B 2 81  ? 133.789 125.099 100.597 1.00 49.00  ? 81  GLN B CA    1 
ATOM   4340 C C     . GLN B 2 81  ? 133.211 124.025 99.686  1.00 54.14  ? 81  GLN B C     1 
ATOM   4341 O O     . GLN B 2 81  ? 132.504 123.124 100.150 1.00 57.19  ? 81  GLN B O     1 
ATOM   4342 C CB    . GLN B 2 81  ? 134.614 124.472 101.719 1.00 48.71  ? 81  GLN B CB    1 
ATOM   4343 C CG    . GLN B 2 81  ? 135.692 123.517 101.231 1.00 48.20  ? 81  GLN B CG    1 
ATOM   4344 C CD    . GLN B 2 81  ? 136.832 124.232 100.532 1.00 54.06  ? 81  GLN B CD    1 
ATOM   4345 O OE1   . GLN B 2 81  ? 137.380 125.204 101.050 1.00 57.93  ? 81  GLN B OE1   1 
ATOM   4346 N NE2   . GLN B 2 81  ? 137.192 123.753 99.347  1.00 55.49  ? 81  GLN B NE2   1 
ATOM   4347 N N     . MET B 2 82  ? 133.513 124.120 98.395  1.00 53.10  ? 82  MET B N     1 
ATOM   4348 C CA    . MET B 2 82  ? 132.983 123.219 97.379  1.00 49.96  ? 82  MET B CA    1 
ATOM   4349 C C     . MET B 2 82  ? 134.104 122.294 96.923  1.00 51.91  ? 82  MET B C     1 
ATOM   4350 O O     . MET B 2 82  ? 135.024 122.724 96.221  1.00 54.15  ? 82  MET B O     1 
ATOM   4351 C CB    . MET B 2 82  ? 132.400 124.016 96.213  1.00 55.49  ? 82  MET B CB    1 
ATOM   4352 C CG    . MET B 2 82  ? 131.409 125.077 96.665  1.00 53.20  ? 82  MET B CG    1 
ATOM   4353 S SD    . MET B 2 82  ? 131.111 126.420 95.502  1.00 56.23  ? 82  MET B SD    1 
ATOM   4354 C CE    . MET B 2 82  ? 131.107 125.591 93.929  1.00 49.95  ? 82  MET B CE    1 
ATOM   4355 N N     . ASN B 2 83  ? 134.022 121.027 97.318  1.00 56.66  ? 83  ASN B N     1 
ATOM   4356 C CA    . ASN B 2 83  ? 135.008 120.018 96.965  1.00 53.59  ? 83  ASN B CA    1 
ATOM   4357 C C     . ASN B 2 83  ? 134.422 119.046 95.949  1.00 58.82  ? 83  ASN B C     1 
ATOM   4358 O O     . ASN B 2 83  ? 133.203 118.891 95.839  1.00 62.90  ? 83  ASN B O     1 
ATOM   4359 C CB    . ASN B 2 83  ? 135.481 119.252 98.206  1.00 52.20  ? 83  ASN B CB    1 
ATOM   4360 C CG    . ASN B 2 83  ? 136.182 120.144 99.210  1.00 54.77  ? 83  ASN B CG    1 
ATOM   4361 O OD1   . ASN B 2 83  ? 137.043 120.946 98.851  1.00 56.06  ? 83  ASN B OD1   1 
ATOM   4362 N ND2   . ASN B 2 83  ? 135.816 120.006 100.480 1.00 55.11  ? 83  ASN B ND2   1 
ATOM   4363 N N     . SER B 2 84  ? 135.316 118.389 95.207  1.00 58.84  ? 84  SER B N     1 
ATOM   4364 C CA    . SER B 2 84  ? 134.937 117.417 94.180  1.00 59.13  ? 84  SER B CA    1 
ATOM   4365 C C     . SER B 2 84  ? 133.931 118.024 93.205  1.00 57.16  ? 84  SER B C     1 
ATOM   4366 O O     . SER B 2 84  ? 132.852 117.480 92.962  1.00 59.02  ? 84  SER B O     1 
ATOM   4367 C CB    . SER B 2 84  ? 134.389 116.136 94.810  1.00 64.96  ? 84  SER B CB    1 
ATOM   4368 O OG    . SER B 2 84  ? 135.385 115.480 95.575  1.00 68.42  ? 84  SER B OG    1 
ATOM   4369 N N     . LEU B 2 85  ? 134.296 119.176 92.651  1.00 56.88  ? 85  LEU B N     1 
ATOM   4370 C CA    . LEU B 2 85  ? 133.366 119.941 91.833  1.00 54.80  ? 85  LEU B CA    1 
ATOM   4371 C C     . LEU B 2 85  ? 133.079 119.233 90.516  1.00 57.80  ? 85  LEU B C     1 
ATOM   4372 O O     . LEU B 2 85  ? 133.998 118.884 89.769  1.00 62.18  ? 85  LEU B O     1 
ATOM   4373 C CB    . LEU B 2 85  ? 133.921 121.338 91.572  1.00 54.40  ? 85  LEU B CB    1 
ATOM   4374 C CG    . LEU B 2 85  ? 133.645 122.276 92.741  1.00 50.64  ? 85  LEU B CG    1 
ATOM   4375 C CD1   . LEU B 2 85  ? 134.400 123.591 92.610  1.00 50.74  ? 85  LEU B CD1   1 
ATOM   4376 C CD2   . LEU B 2 85  ? 132.151 122.497 92.849  1.00 50.79  ? 85  LEU B CD2   1 
ATOM   4377 N N     . LYS B 2 86  ? 131.797 119.032 90.233  1.00 55.58  ? 86  LYS B N     1 
ATOM   4378 C CA    . LYS B 2 86  ? 131.324 118.458 88.986  1.00 51.87  ? 86  LYS B CA    1 
ATOM   4379 C C     . LYS B 2 86  ? 131.030 119.557 87.975  1.00 54.29  ? 86  LYS B C     1 
ATOM   4380 O O     . LYS B 2 86  ? 130.781 120.707 88.348  1.00 59.19  ? 86  LYS B O     1 
ATOM   4381 C CB    . LYS B 2 86  ? 130.065 117.631 89.234  1.00 53.18  ? 86  LYS B CB    1 
ATOM   4382 C CG    . LYS B 2 86  ? 130.226 116.535 90.273  1.00 60.61  ? 86  LYS B CG    1 
ATOM   4383 C CD    . LYS B 2 86  ? 128.880 115.929 90.634  1.00 64.78  ? 86  LYS B CD    1 
ATOM   4384 C CE    . LYS B 2 86  ? 129.013 114.908 91.751  1.00 65.55  ? 86  LYS B CE    1 
ATOM   4385 N NZ    . LYS B 2 86  ? 127.686 114.391 92.186  1.00 70.98  ? 86  LYS B NZ    1 
ATOM   4386 N N     . PRO B 2 87  ? 131.049 119.236 86.679  1.00 53.97  ? 87  PRO B N     1 
ATOM   4387 C CA    . PRO B 2 87  ? 130.677 120.244 85.672  1.00 52.73  ? 87  PRO B CA    1 
ATOM   4388 C C     . PRO B 2 87  ? 129.251 120.745 85.817  1.00 55.50  ? 87  PRO B C     1 
ATOM   4389 O O     . PRO B 2 87  ? 128.933 121.823 85.300  1.00 58.96  ? 87  PRO B O     1 
ATOM   4390 C CB    . PRO B 2 87  ? 130.881 119.504 84.343  1.00 48.46  ? 87  PRO B CB    1 
ATOM   4391 C CG    . PRO B 2 87  ? 131.873 118.434 84.661  1.00 51.61  ? 87  PRO B CG    1 
ATOM   4392 C CD    . PRO B 2 87  ? 131.541 117.995 86.056  1.00 55.52  ? 87  PRO B CD    1 
ATOM   4393 N N     . GLU B 2 88  ? 128.386 120.000 86.502  1.00 53.87  ? 88  GLU B N     1 
ATOM   4394 C CA    . GLU B 2 88  ? 127.013 120.421 86.748  1.00 49.34  ? 88  GLU B CA    1 
ATOM   4395 C C     . GLU B 2 88  ? 126.902 121.450 87.865  1.00 53.22  ? 88  GLU B C     1 
ATOM   4396 O O     . GLU B 2 88  ? 125.805 121.967 88.101  1.00 58.63  ? 88  GLU B O     1 
ATOM   4397 C CB    . GLU B 2 88  ? 126.144 119.204 87.077  1.00 51.57  ? 88  GLU B CB    1 
ATOM   4398 C CG    . GLU B 2 88  ? 126.062 118.181 85.955  1.00 63.36  ? 88  GLU B CG    1 
ATOM   4399 C CD    . GLU B 2 88  ? 127.211 117.191 85.980  1.00 72.48  ? 88  GLU B CD    1 
ATOM   4400 O OE1   . GLU B 2 88  ? 127.913 117.069 84.954  1.00 72.16  ? 88  GLU B OE1   1 
ATOM   4401 O OE2   . GLU B 2 88  ? 127.413 116.538 87.025  1.00 77.99  ? 88  GLU B OE2   1 
ATOM   4402 N N     . ASP B 2 89  ? 127.999 121.754 88.554  1.00 54.59  ? 89  ASP B N     1 
ATOM   4403 C CA    . ASP B 2 89  ? 128.019 122.781 89.585  1.00 51.07  ? 89  ASP B CA    1 
ATOM   4404 C C     . ASP B 2 89  ? 128.258 124.175 89.021  1.00 50.36  ? 89  ASP B C     1 
ATOM   4405 O O     . ASP B 2 89  ? 128.323 125.138 89.791  1.00 52.40  ? 89  ASP B O     1 
ATOM   4406 C CB    . ASP B 2 89  ? 129.090 122.450 90.631  1.00 51.47  ? 89  ASP B CB    1 
ATOM   4407 C CG    . ASP B 2 89  ? 128.830 121.131 91.331  1.00 54.25  ? 89  ASP B CG    1 
ATOM   4408 O OD1   . ASP B 2 89  ? 127.737 120.561 91.133  1.00 60.82  ? 89  ASP B OD1   1 
ATOM   4409 O OD2   . ASP B 2 89  ? 129.714 120.660 92.075  1.00 57.10  ? 89  ASP B OD2   1 
ATOM   4410 N N     . THR B 2 90  ? 128.391 124.301 87.703  1.00 49.79  ? 90  THR B N     1 
ATOM   4411 C CA    . THR B 2 90  ? 128.600 125.600 87.076  1.00 47.24  ? 90  THR B CA    1 
ATOM   4412 C C     . THR B 2 90  ? 127.331 126.439 87.175  1.00 55.74  ? 90  THR B C     1 
ATOM   4413 O O     . THR B 2 90  ? 126.313 126.115 86.554  1.00 60.34  ? 90  THR B O     1 
ATOM   4414 C CB    . THR B 2 90  ? 129.009 125.424 85.616  1.00 52.48  ? 90  THR B CB    1 
ATOM   4415 O OG1   . THR B 2 90  ? 130.257 124.724 85.547  1.00 55.12  ? 90  THR B OG1   1 
ATOM   4416 C CG2   . THR B 2 90  ? 129.146 126.777 84.931  1.00 53.56  ? 90  THR B CG2   1 
ATOM   4417 N N     . ALA B 2 91  ? 127.396 127.520 87.948  1.00 55.80  ? 91  ALA B N     1 
ATOM   4418 C CA    . ALA B 2 91  ? 126.260 128.412 88.144  1.00 50.69  ? 91  ALA B CA    1 
ATOM   4419 C C     . ALA B 2 91  ? 126.756 129.674 88.834  1.00 51.18  ? 91  ALA B C     1 
ATOM   4420 O O     . ALA B 2 91  ? 127.916 129.766 89.246  1.00 53.58  ? 91  ALA B O     1 
ATOM   4421 C CB    . ALA B 2 91  ? 125.152 127.745 88.965  1.00 52.55  ? 91  ALA B CB    1 
ATOM   4422 N N     . VAL B 2 92  ? 125.861 130.649 88.953  1.00 56.45  ? 92  VAL B N     1 
ATOM   4423 C CA    . VAL B 2 92  ? 126.119 131.850 89.738  1.00 53.89  ? 92  VAL B CA    1 
ATOM   4424 C C     . VAL B 2 92  ? 125.611 131.593 91.150  1.00 53.68  ? 92  VAL B C     1 
ATOM   4425 O O     . VAL B 2 92  ? 124.421 131.331 91.351  1.00 55.71  ? 92  VAL B O     1 
ATOM   4426 C CB    . VAL B 2 92  ? 125.438 133.082 89.123  1.00 52.05  ? 92  VAL B CB    1 
ATOM   4427 C CG1   . VAL B 2 92  ? 125.685 134.308 89.990  1.00 54.31  ? 92  VAL B CG1   1 
ATOM   4428 C CG2   . VAL B 2 92  ? 125.930 133.314 87.707  1.00 54.88  ? 92  VAL B CG2   1 
ATOM   4429 N N     . TYR B 2 93  ? 126.508 131.670 92.127  1.00 52.64  ? 93  TYR B N     1 
ATOM   4430 C CA    . TYR B 2 93  ? 126.183 131.342 93.508  1.00 49.26  ? 93  TYR B CA    1 
ATOM   4431 C C     . TYR B 2 93  ? 125.857 132.605 94.289  1.00 53.41  ? 93  TYR B C     1 
ATOM   4432 O O     . TYR B 2 93  ? 126.651 133.553 94.314  1.00 53.75  ? 93  TYR B O     1 
ATOM   4433 C CB    . TYR B 2 93  ? 127.329 130.585 94.173  1.00 49.78  ? 93  TYR B CB    1 
ATOM   4434 C CG    . TYR B 2 93  ? 127.415 129.135 93.757  1.00 49.61  ? 93  TYR B CG    1 
ATOM   4435 C CD1   . TYR B 2 93  ? 127.936 128.775 92.523  1.00 47.79  ? 93  TYR B CD1   1 
ATOM   4436 C CD2   . TYR B 2 93  ? 126.975 128.125 94.603  1.00 51.09  ? 93  TYR B CD2   1 
ATOM   4437 C CE1   . TYR B 2 93  ? 128.016 127.450 92.140  1.00 46.43  ? 93  TYR B CE1   1 
ATOM   4438 C CE2   . TYR B 2 93  ? 127.051 126.797 94.229  1.00 51.52  ? 93  TYR B CE2   1 
ATOM   4439 C CZ    . TYR B 2 93  ? 127.573 126.465 92.997  1.00 50.03  ? 93  TYR B CZ    1 
ATOM   4440 O OH    . TYR B 2 93  ? 127.651 125.144 92.619  1.00 56.19  ? 93  TYR B OH    1 
ATOM   4441 N N     . TYR B 2 94  ? 124.691 132.606 94.931  1.00 55.11  ? 94  TYR B N     1 
ATOM   4442 C CA    . TYR B 2 94  ? 124.193 133.752 95.676  1.00 49.08  ? 94  TYR B CA    1 
ATOM   4443 C C     . TYR B 2 94  ? 124.171 133.422 97.160  1.00 52.24  ? 94  TYR B C     1 
ATOM   4444 O O     . TYR B 2 94  ? 123.671 132.363 97.556  1.00 53.32  ? 94  TYR B O     1 
ATOM   4445 C CB    . TYR B 2 94  ? 122.790 134.155 95.214  1.00 52.60  ? 94  TYR B CB    1 
ATOM   4446 C CG    . TYR B 2 94  ? 122.700 134.550 93.759  1.00 53.43  ? 94  TYR B CG    1 
ATOM   4447 C CD1   . TYR B 2 94  ? 122.768 135.883 93.375  1.00 56.60  ? 94  TYR B CD1   1 
ATOM   4448 C CD2   . TYR B 2 94  ? 122.536 133.591 92.770  1.00 52.04  ? 94  TYR B CD2   1 
ATOM   4449 C CE1   . TYR B 2 94  ? 122.679 136.248 92.042  1.00 59.32  ? 94  TYR B CE1   1 
ATOM   4450 C CE2   . TYR B 2 94  ? 122.448 133.946 91.436  1.00 58.82  ? 94  TYR B CE2   1 
ATOM   4451 C CZ    . TYR B 2 94  ? 122.519 135.275 91.077  1.00 64.12  ? 94  TYR B CZ    1 
ATOM   4452 O OH    . TYR B 2 94  ? 122.433 135.631 89.750  1.00 71.32  ? 94  TYR B OH    1 
ATOM   4453 N N     . CYS B 2 95  ? 124.727 134.326 97.966  1.00 53.09  ? 95  CYS B N     1 
ATOM   4454 C CA    . CYS B 2 95  ? 124.658 134.251 99.417  1.00 50.51  ? 95  CYS B CA    1 
ATOM   4455 C C     . CYS B 2 95  ? 123.533 135.152 99.902  1.00 55.51  ? 95  CYS B C     1 
ATOM   4456 O O     . CYS B 2 95  ? 123.340 136.257 99.385  1.00 57.80  ? 95  CYS B O     1 
ATOM   4457 C CB    . CYS B 2 95  ? 126.000 134.663 100.015 1.00 54.56  ? 95  CYS B CB    1 
ATOM   4458 S SG    . CYS B 2 95  ? 126.206 134.634 101.773 1.00 70.54  ? 95  CYS B SG    1 
ATOM   4459 N N     . ASN B 2 96  ? 122.773 134.663 100.880 1.00 55.12  ? 96  ASN B N     1 
ATOM   4460 C CA    . ASN B 2 96  ? 121.503 135.285 101.241 1.00 49.32  ? 96  ASN B CA    1 
ATOM   4461 C C     . ASN B 2 96  ? 121.284 135.192 102.744 1.00 53.50  ? 96  ASN B C     1 
ATOM   4462 O O     . ASN B 2 96  ? 121.336 134.096 103.311 1.00 53.66  ? 96  ASN B O     1 
ATOM   4463 C CB    . ASN B 2 96  ? 120.352 134.610 100.485 1.00 47.20  ? 96  ASN B CB    1 
ATOM   4464 C CG    . ASN B 2 96  ? 118.987 134.998 101.018 1.00 49.61  ? 96  ASN B CG    1 
ATOM   4465 O OD1   . ASN B 2 96  ? 118.208 134.142 101.440 1.00 51.68  ? 96  ASN B OD1   1 
ATOM   4466 N ND2   . ASN B 2 96  ? 118.683 136.289 100.990 1.00 51.38  ? 96  ASN B ND2   1 
ATOM   4467 N N     . VAL B 2 97  ? 121.037 136.336 103.385 1.00 55.77  ? 97  VAL B N     1 
ATOM   4468 C CA    . VAL B 2 97  ? 120.573 136.386 104.768 1.00 46.77  ? 97  VAL B CA    1 
ATOM   4469 C C     . VAL B 2 97  ? 119.060 136.546 104.747 1.00 48.17  ? 97  VAL B C     1 
ATOM   4470 O O     . VAL B 2 97  ? 118.515 137.303 103.931 1.00 52.01  ? 97  VAL B O     1 
ATOM   4471 C CB    . VAL B 2 97  ? 121.257 137.518 105.563 1.00 47.95  ? 97  VAL B CB    1 
ATOM   4472 C CG1   . VAL B 2 97  ? 120.926 138.878 104.986 1.00 56.25  ? 97  VAL B CG1   1 
ATOM   4473 C CG2   . VAL B 2 97  ? 120.859 137.448 107.030 1.00 54.83  ? 97  VAL B CG2   1 
ATOM   4474 N N     . LYS B 2 98  ? 118.372 135.809 105.617 1.00 52.29  ? 98  LYS B N     1 
ATOM   4475 C CA    . LYS B 2 98  ? 116.930 135.677 105.491 1.00 47.76  ? 98  LYS B CA    1 
ATOM   4476 C C     . LYS B 2 98  ? 116.308 135.451 106.862 1.00 54.20  ? 98  LYS B C     1 
ATOM   4477 O O     . LYS B 2 98  ? 116.952 134.926 107.774 1.00 60.75  ? 98  LYS B O     1 
ATOM   4478 C CB    . LYS B 2 98  ? 116.594 134.528 104.533 1.00 51.02  ? 98  LYS B CB    1 
ATOM   4479 C CG    . LYS B 2 98  ? 115.123 134.298 104.274 1.00 53.38  ? 98  LYS B CG    1 
ATOM   4480 C CD    . LYS B 2 98  ? 114.936 133.227 103.213 1.00 54.59  ? 98  LYS B CD    1 
ATOM   4481 C CE    . LYS B 2 98  ? 115.254 131.850 103.746 1.00 59.32  ? 98  LYS B CE    1 
ATOM   4482 N NZ    . LYS B 2 98  ? 114.965 130.777 102.755 1.00 58.09  ? 98  LYS B NZ    1 
ATOM   4483 N N     . ASP B 2 99  ? 115.048 135.864 106.995 1.00 51.49  ? 99  ASP B N     1 
ATOM   4484 C CA    . ASP B 2 99  ? 114.259 135.622 108.194 1.00 51.53  ? 99  ASP B CA    1 
ATOM   4485 C C     . ASP B 2 99  ? 112.790 135.551 107.805 1.00 55.65  ? 99  ASP B C     1 
ATOM   4486 O O     . ASP B 2 99  ? 112.321 136.347 106.987 1.00 60.64  ? 99  ASP B O     1 
ATOM   4487 C CB    . ASP B 2 99  ? 114.476 136.714 109.247 1.00 55.66  ? 99  ASP B CB    1 
ATOM   4488 C CG    . ASP B 2 99  ? 114.071 136.271 110.638 1.00 66.54  ? 99  ASP B CG    1 
ATOM   4489 O OD1   . ASP B 2 99  ? 114.177 135.062 110.935 1.00 60.84  ? 99  ASP B OD1   1 
ATOM   4490 O OD2   . ASP B 2 99  ? 113.643 137.133 111.433 1.00 70.32  ? 99  ASP B OD2   1 
ATOM   4491 N N     . TYR B 2 100 ? 112.073 134.597 108.395 1.00 55.64  ? 100 TYR B N     1 
ATOM   4492 C CA    . TYR B 2 100 ? 110.666 134.385 108.080 1.00 53.18  ? 100 TYR B CA    1 
ATOM   4493 C C     . TYR B 2 100 ? 110.050 133.537 109.184 1.00 58.61  ? 100 TYR B C     1 
ATOM   4494 O O     . TYR B 2 100 ? 110.758 132.912 109.979 1.00 61.99  ? 100 TYR B O     1 
ATOM   4495 C CB    . TYR B 2 100 ? 110.503 133.731 106.704 1.00 56.71  ? 100 TYR B CB    1 
ATOM   4496 C CG    . TYR B 2 100 ? 111.158 132.372 106.582 1.00 54.49  ? 100 TYR B CG    1 
ATOM   4497 C CD1   . TYR B 2 100 ? 112.519 132.254 106.331 1.00 51.69  ? 100 TYR B CD1   1 
ATOM   4498 C CD2   . TYR B 2 100 ? 110.412 131.209 106.690 1.00 55.54  ? 100 TYR B CD2   1 
ATOM   4499 C CE1   . TYR B 2 100 ? 113.119 131.015 106.212 1.00 51.78  ? 100 TYR B CE1   1 
ATOM   4500 C CE2   . TYR B 2 100 ? 111.001 129.968 106.568 1.00 52.35  ? 100 TYR B CE2   1 
ATOM   4501 C CZ    . TYR B 2 100 ? 112.355 129.875 106.332 1.00 51.00  ? 100 TYR B CZ    1 
ATOM   4502 O OH    . TYR B 2 100 ? 112.947 128.639 106.215 1.00 55.20  ? 100 TYR B OH    1 
ATOM   4503 N N     . VAL B 2 101 ? 108.715 133.524 109.231 1.00 58.88  ? 101 VAL B N     1 
ATOM   4504 C CA    . VAL B 2 101 ? 108.016 132.797 110.288 1.00 61.94  ? 101 VAL B CA    1 
ATOM   4505 C C     . VAL B 2 101 ? 107.307 131.568 109.733 1.00 64.49  ? 101 VAL B C     1 
ATOM   4506 O O     . VAL B 2 101 ? 107.634 130.441 110.113 1.00 68.09  ? 101 VAL B O     1 
ATOM   4507 C CB    . VAL B 2 101 ? 107.031 133.712 111.038 1.00 59.36  ? 101 VAL B CB    1 
ATOM   4508 C CG1   . VAL B 2 101 ? 106.480 133.000 112.260 1.00 57.85  ? 101 VAL B CG1   1 
ATOM   4509 C CG2   . VAL B 2 101 ? 107.726 134.996 111.460 1.00 55.53  ? 101 VAL B CG2   1 
ATOM   4510 N N     . TYR B 2 102 ? 106.301 131.753 108.879 1.00 64.21  ? 102 TYR B N     1 
ATOM   4511 C CA    . TYR B 2 102 ? 105.789 130.619 108.114 1.00 63.33  ? 102 TYR B CA    1 
ATOM   4512 C C     . TYR B 2 102 ? 105.817 130.896 106.618 1.00 66.92  ? 102 TYR B C     1 
ATOM   4513 O O     . TYR B 2 102 ? 106.382 130.107 105.854 1.00 71.62  ? 102 TYR B O     1 
ATOM   4514 C CB    . TYR B 2 102 ? 104.368 130.263 108.569 1.00 72.32  ? 102 TYR B CB    1 
ATOM   4515 C CG    . TYR B 2 102 ? 103.657 129.286 107.658 1.00 70.57  ? 102 TYR B CG    1 
ATOM   4516 C CD1   . TYR B 2 102 ? 104.293 128.132 107.212 1.00 71.58  ? 102 TYR B CD1   1 
ATOM   4517 C CD2   . TYR B 2 102 ? 102.353 129.517 107.242 1.00 70.27  ? 102 TYR B CD2   1 
ATOM   4518 C CE1   . TYR B 2 102 ? 103.650 127.238 106.376 1.00 75.22  ? 102 TYR B CE1   1 
ATOM   4519 C CE2   . TYR B 2 102 ? 101.703 128.627 106.408 1.00 73.53  ? 102 TYR B CE2   1 
ATOM   4520 C CZ    . TYR B 2 102 ? 102.355 127.490 105.978 1.00 76.64  ? 102 TYR B CZ    1 
ATOM   4521 O OH    . TYR B 2 102 ? 101.710 126.602 105.148 1.00 83.60  ? 102 TYR B OH    1 
ATOM   4522 N N     . ASN B 2 103 ? 105.227 132.007 106.185 1.00 66.99  ? 103 ASN B N     1 
ATOM   4523 C CA    . ASN B 2 103 ? 105.323 132.459 104.808 1.00 64.44  ? 103 ASN B CA    1 
ATOM   4524 C C     . ASN B 2 103 ? 105.483 133.968 104.726 1.00 67.81  ? 103 ASN B C     1 
ATOM   4525 O O     . ASN B 2 103 ? 105.526 134.512 103.617 1.00 73.28  ? 103 ASN B O     1 
ATOM   4526 C CB    . ASN B 2 103 ? 104.086 132.022 104.003 1.00 64.28  ? 103 ASN B CB    1 
ATOM   4527 C CG    . ASN B 2 103 ? 104.277 130.677 103.328 1.00 72.98  ? 103 ASN B CG    1 
ATOM   4528 O OD1   . ASN B 2 103 ? 105.113 130.529 102.439 1.00 78.01  ? 103 ASN B OD1   1 
ATOM   4529 N ND2   . ASN B 2 103 ? 103.503 129.686 103.755 1.00 72.35  ? 103 ASN B ND2   1 
ATOM   4530 N N     . THR B 2 104 ? 105.570 134.654 105.862 1.00 65.53  ? 104 THR B N     1 
ATOM   4531 C CA    . THR B 2 104 ? 105.807 136.089 105.915 1.00 66.91  ? 104 THR B CA    1 
ATOM   4532 C C     . THR B 2 104 ? 107.308 136.304 106.056 1.00 62.72  ? 104 THR B C     1 
ATOM   4533 O O     . THR B 2 104 ? 107.897 135.970 107.089 1.00 65.01  ? 104 THR B O     1 
ATOM   4534 C CB    . THR B 2 104 ? 105.049 136.729 107.076 1.00 67.34  ? 104 THR B CB    1 
ATOM   4535 O OG1   . THR B 2 104 ? 105.508 136.172 108.314 1.00 70.29  ? 104 THR B OG1   1 
ATOM   4536 C CG2   . THR B 2 104 ? 103.555 136.477 106.940 1.00 64.05  ? 104 THR B CG2   1 
ATOM   4537 N N     . TYR B 2 105 ? 107.923 136.857 105.016 1.00 59.64  ? 105 TYR B N     1 
ATOM   4538 C CA    . TYR B 2 105 ? 109.367 137.057 104.992 1.00 56.82  ? 105 TYR B CA    1 
ATOM   4539 C C     . TYR B 2 105 ? 109.687 138.394 105.649 1.00 60.03  ? 105 TYR B C     1 
ATOM   4540 O O     . TYR B 2 105 ? 109.397 139.456 105.087 1.00 62.86  ? 105 TYR B O     1 
ATOM   4541 C CB    . TYR B 2 105 ? 109.874 136.993 103.554 1.00 59.86  ? 105 TYR B CB    1 
ATOM   4542 C CG    . TYR B 2 105 ? 110.297 135.605 103.130 1.00 63.44  ? 105 TYR B CG    1 
ATOM   4543 C CD1   . TYR B 2 105 ? 109.421 134.531 103.233 1.00 66.69  ? 105 TYR B CD1   1 
ATOM   4544 C CD2   . TYR B 2 105 ? 111.558 135.371 102.605 1.00 65.10  ? 105 TYR B CD2   1 
ATOM   4545 C CE1   . TYR B 2 105 ? 109.798 133.259 102.845 1.00 68.88  ? 105 TYR B CE1   1 
ATOM   4546 C CE2   . TYR B 2 105 ? 111.940 134.105 102.208 1.00 68.77  ? 105 TYR B CE2   1 
ATOM   4547 C CZ    . TYR B 2 105 ? 111.059 133.053 102.332 1.00 70.75  ? 105 TYR B CZ    1 
ATOM   4548 O OH    . TYR B 2 105 ? 111.444 131.792 101.938 1.00 68.22  ? 105 TYR B OH    1 
ATOM   4549 N N     . LEU B 2 106 ? 110.271 138.344 106.848 1.00 59.57  ? 106 LEU B N     1 
ATOM   4550 C CA    . LEU B 2 106 ? 110.537 139.569 107.597 1.00 58.86  ? 106 LEU B CA    1 
ATOM   4551 C C     . LEU B 2 106 ? 111.606 140.411 106.912 1.00 56.48  ? 106 LEU B C     1 
ATOM   4552 O O     . LEU B 2 106 ? 111.452 141.629 106.766 1.00 58.59  ? 106 LEU B O     1 
ATOM   4553 C CB    . LEU B 2 106 ? 110.943 139.232 109.034 1.00 56.11  ? 106 LEU B CB    1 
ATOM   4554 C CG    . LEU B 2 106 ? 109.818 138.960 110.042 1.00 56.28  ? 106 LEU B CG    1 
ATOM   4555 C CD1   . LEU B 2 106 ? 108.969 140.206 110.244 1.00 62.45  ? 106 LEU B CD1   1 
ATOM   4556 C CD2   . LEU B 2 106 ? 108.951 137.780 109.633 1.00 55.56  ? 106 LEU B CD2   1 
ATOM   4557 N N     . TYR B 2 107 ? 112.700 139.781 106.489 1.00 55.82  ? 107 TYR B N     1 
ATOM   4558 C CA    . TYR B 2 107 ? 113.668 140.443 105.629 1.00 56.99  ? 107 TYR B CA    1 
ATOM   4559 C C     . TYR B 2 107 ? 114.366 139.391 104.780 1.00 58.55  ? 107 TYR B C     1 
ATOM   4560 O O     . TYR B 2 107 ? 114.458 138.220 105.156 1.00 62.82  ? 107 TYR B O     1 
ATOM   4561 C CB    . TYR B 2 107 ? 114.685 141.277 106.427 1.00 58.76  ? 107 TYR B CB    1 
ATOM   4562 C CG    . TYR B 2 107 ? 115.557 140.508 107.398 1.00 59.13  ? 107 TYR B CG    1 
ATOM   4563 C CD1   . TYR B 2 107 ? 116.724 139.884 106.972 1.00 58.83  ? 107 TYR B CD1   1 
ATOM   4564 C CD2   . TYR B 2 107 ? 115.234 140.439 108.747 1.00 58.32  ? 107 TYR B CD2   1 
ATOM   4565 C CE1   . TYR B 2 107 ? 117.529 139.192 107.857 1.00 59.18  ? 107 TYR B CE1   1 
ATOM   4566 C CE2   . TYR B 2 107 ? 116.036 139.753 109.640 1.00 62.19  ? 107 TYR B CE2   1 
ATOM   4567 C CZ    . TYR B 2 107 ? 117.181 139.130 109.189 1.00 65.62  ? 107 TYR B CZ    1 
ATOM   4568 O OH    . TYR B 2 107 ? 117.981 138.443 110.074 1.00 72.79  ? 107 TYR B OH    1 
ATOM   4569 N N     . ASP B 2 108 ? 114.858 139.831 103.621 1.00 63.08  ? 108 ASP B N     1 
ATOM   4570 C CA    . ASP B 2 108 ? 115.478 138.920 102.661 1.00 62.84  ? 108 ASP B CA    1 
ATOM   4571 C C     . ASP B 2 108 ? 116.491 139.734 101.858 1.00 60.66  ? 108 ASP B C     1 
ATOM   4572 O O     . ASP B 2 108 ? 116.107 140.489 100.961 1.00 65.04  ? 108 ASP B O     1 
ATOM   4573 C CB    . ASP B 2 108 ? 114.433 138.280 101.761 1.00 60.02  ? 108 ASP B CB    1 
ATOM   4574 C CG    . ASP B 2 108 ? 114.931 137.011 101.100 1.00 62.16  ? 108 ASP B CG    1 
ATOM   4575 O OD1   . ASP B 2 108 ? 116.068 136.588 101.397 1.00 65.95  ? 108 ASP B OD1   1 
ATOM   4576 O OD2   . ASP B 2 108 ? 114.184 136.436 100.280 1.00 61.79  ? 108 ASP B OD2   1 
ATOM   4577 N N     . TYR B 2 109 ? 117.769 139.574 102.187 1.00 55.76  ? 109 TYR B N     1 
ATOM   4578 C CA    . TYR B 2 109 ? 118.845 140.315 101.546 1.00 54.19  ? 109 TYR B CA    1 
ATOM   4579 C C     . TYR B 2 109 ? 119.720 139.353 100.757 1.00 54.30  ? 109 TYR B C     1 
ATOM   4580 O O     . TYR B 2 109 ? 120.165 138.331 101.290 1.00 53.22  ? 109 TYR B O     1 
ATOM   4581 C CB    . TYR B 2 109 ? 119.678 141.072 102.580 1.00 60.46  ? 109 TYR B CB    1 
ATOM   4582 C CG    . TYR B 2 109 ? 118.919 142.168 103.289 1.00 64.48  ? 109 TYR B CG    1 
ATOM   4583 C CD1   . TYR B 2 109 ? 118.619 143.360 102.645 1.00 65.66  ? 109 TYR B CD1   1 
ATOM   4584 C CD2   . TYR B 2 109 ? 118.490 142.006 104.600 1.00 64.19  ? 109 TYR B CD2   1 
ATOM   4585 C CE1   . TYR B 2 109 ? 117.922 144.364 103.289 1.00 67.73  ? 109 TYR B CE1   1 
ATOM   4586 C CE2   . TYR B 2 109 ? 117.793 143.004 105.253 1.00 69.37  ? 109 TYR B CE2   1 
ATOM   4587 C CZ    . TYR B 2 109 ? 117.511 144.180 104.592 1.00 73.74  ? 109 TYR B CZ    1 
ATOM   4588 O OH    . TYR B 2 109 ? 116.816 145.177 105.238 1.00 79.32  ? 109 TYR B OH    1 
ATOM   4589 N N     . TRP B 2 110 ? 119.961 139.683 99.494  1.00 57.92  ? 110 TRP B N     1 
ATOM   4590 C CA    . TRP B 2 110 ? 120.751 138.866 98.589  1.00 54.76  ? 110 TRP B CA    1 
ATOM   4591 C C     . TRP B 2 110 ? 122.085 139.534 98.291  1.00 59.44  ? 110 TRP B C     1 
ATOM   4592 O O     . TRP B 2 110 ? 122.280 140.729 98.528  1.00 64.54  ? 110 TRP B O     1 
ATOM   4593 C CB    . TRP B 2 110 ? 120.002 138.624 97.273  1.00 52.49  ? 110 TRP B CB    1 
ATOM   4594 C CG    . TRP B 2 110 ? 118.801 137.743 97.394  1.00 48.13  ? 110 TRP B CG    1 
ATOM   4595 C CD1   . TRP B 2 110 ? 117.526 138.131 97.681  1.00 48.58  ? 110 TRP B CD1   1 
ATOM   4596 C CD2   . TRP B 2 110 ? 118.754 136.327 97.189  1.00 49.11  ? 110 TRP B CD2   1 
ATOM   4597 N NE1   . TRP B 2 110 ? 116.690 137.041 97.689  1.00 49.14  ? 110 TRP B NE1   1 
ATOM   4598 C CE2   . TRP B 2 110 ? 117.420 135.921 97.388  1.00 50.85  ? 110 TRP B CE2   1 
ATOM   4599 C CE3   . TRP B 2 110 ? 119.712 135.361 96.866  1.00 46.00  ? 110 TRP B CE3   1 
ATOM   4600 C CZ2   . TRP B 2 110 ? 117.019 134.592 97.275  1.00 49.27  ? 110 TRP B CZ2   1 
ATOM   4601 C CZ3   . TRP B 2 110 ? 119.312 134.042 96.753  1.00 47.10  ? 110 TRP B CZ3   1 
ATOM   4602 C CH2   . TRP B 2 110 ? 117.978 133.669 96.957  1.00 49.76  ? 110 TRP B CH2   1 
ATOM   4603 N N     . GLY B 2 111 ? 123.011 138.735 97.767  1.00 58.25  ? 111 GLY B N     1 
ATOM   4604 C CA    . GLY B 2 111 ? 124.216 139.250 97.162  1.00 61.94  ? 111 GLY B CA    1 
ATOM   4605 C C     . GLY B 2 111 ? 124.075 139.304 95.648  1.00 71.12  ? 111 GLY B C     1 
ATOM   4606 O O     . GLY B 2 111 ? 123.115 138.806 95.066  1.00 73.18  ? 111 GLY B O     1 
ATOM   4607 N N     . GLN B 2 112 ? 125.064 139.924 95.011  1.00 71.33  ? 112 GLN B N     1 
ATOM   4608 C CA    . GLN B 2 112 ? 125.060 140.016 93.557  1.00 72.22  ? 112 GLN B CA    1 
ATOM   4609 C C     . GLN B 2 112 ? 125.599 138.759 92.889  1.00 72.17  ? 112 GLN B C     1 
ATOM   4610 O O     . GLN B 2 112 ? 125.623 138.693 91.656  1.00 76.77  ? 112 GLN B O     1 
ATOM   4611 C CB    . GLN B 2 112 ? 125.860 141.239 93.102  1.00 72.03  ? 112 GLN B CB    1 
ATOM   4612 C CG    . GLN B 2 112 ? 125.463 142.520 93.816  1.00 78.91  ? 112 GLN B CG    1 
ATOM   4613 C CD    . GLN B 2 112 ? 124.234 143.165 93.204  1.00 87.15  ? 112 GLN B CD    1 
ATOM   4614 O OE1   . GLN B 2 112 ? 124.161 143.365 91.992  1.00 87.18  ? 112 GLN B OE1   1 
ATOM   4615 N NE2   . GLN B 2 112 ? 123.258 143.489 94.044  1.00 91.20  ? 112 GLN B NE2   1 
ATOM   4616 N N     . GLY B 2 113 ? 126.030 137.775 93.666  1.00 67.42  ? 113 GLY B N     1 
ATOM   4617 C CA    . GLY B 2 113 ? 126.437 136.497 93.132  1.00 60.37  ? 113 GLY B CA    1 
ATOM   4618 C C     . GLY B 2 113 ? 127.882 136.483 92.668  1.00 63.37  ? 113 GLY B C     1 
ATOM   4619 O O     . GLY B 2 113 ? 128.525 137.515 92.478  1.00 64.04  ? 113 GLY B O     1 
ATOM   4620 N N     . THR B 2 114 ? 128.396 135.270 92.486  1.00 62.92  ? 114 THR B N     1 
ATOM   4621 C CA    . THR B 2 114 ? 129.727 135.052 91.945  1.00 60.04  ? 114 THR B CA    1 
ATOM   4622 C C     . THR B 2 114 ? 129.684 133.838 91.030  1.00 56.74  ? 114 THR B C     1 
ATOM   4623 O O     . THR B 2 114 ? 129.037 132.834 91.346  1.00 56.18  ? 114 THR B O     1 
ATOM   4624 C CB    . THR B 2 114 ? 130.772 134.866 93.059  1.00 56.15  ? 114 THR B CB    1 
ATOM   4625 O OG1   . THR B 2 114 ? 132.056 134.606 92.478  1.00 64.03  ? 114 THR B OG1   1 
ATOM   4626 C CG2   . THR B 2 114 ? 130.387 133.724 93.994  1.00 53.00  ? 114 THR B CG2   1 
ATOM   4627 N N     . GLN B 2 115 ? 130.357 133.939 89.888  1.00 52.74  ? 115 GLN B N     1 
ATOM   4628 C CA    . GLN B 2 115 ? 130.287 132.891 88.880  1.00 53.17  ? 115 GLN B CA    1 
ATOM   4629 C C     . GLN B 2 115 ? 131.253 131.762 89.208  1.00 57.17  ? 115 GLN B C     1 
ATOM   4630 O O     . GLN B 2 115 ? 132.443 131.994 89.443  1.00 60.24  ? 115 GLN B O     1 
ATOM   4631 C CB    . GLN B 2 115 ? 130.591 133.455 87.493  1.00 53.81  ? 115 GLN B CB    1 
ATOM   4632 C CG    . GLN B 2 115 ? 130.675 132.388 86.410  1.00 52.76  ? 115 GLN B CG    1 
ATOM   4633 C CD    . GLN B 2 115 ? 129.312 131.923 85.937  1.00 54.18  ? 115 GLN B CD    1 
ATOM   4634 O OE1   . GLN B 2 115 ? 128.393 132.725 85.773  1.00 59.63  ? 115 GLN B OE1   1 
ATOM   4635 N NE2   . GLN B 2 115 ? 129.173 130.620 85.719  1.00 54.07  ? 115 GLN B NE2   1 
ATOM   4636 N N     . VAL B 2 116 ? 130.733 130.539 89.219  1.00 58.19  ? 116 VAL B N     1 
ATOM   4637 C CA    . VAL B 2 116 ? 131.526 129.327 89.377  1.00 55.26  ? 116 VAL B CA    1 
ATOM   4638 C C     . VAL B 2 116 ? 131.375 128.509 88.106  1.00 53.31  ? 116 VAL B C     1 
ATOM   4639 O O     . VAL B 2 116 ? 130.252 128.187 87.701  1.00 53.56  ? 116 VAL B O     1 
ATOM   4640 C CB    . VAL B 2 116 ? 131.093 128.516 90.608  1.00 54.23  ? 116 VAL B CB    1 
ATOM   4641 C CG1   . VAL B 2 116 ? 131.894 127.233 90.701  1.00 53.03  ? 116 VAL B CG1   1 
ATOM   4642 C CG2   . VAL B 2 116 ? 131.282 129.342 91.867  1.00 54.82  ? 116 VAL B CG2   1 
ATOM   4643 N N     . THR B 2 117 ? 132.498 128.187 87.472  1.00 53.56  ? 117 THR B N     1 
ATOM   4644 C CA    . THR B 2 117 ? 132.511 127.382 86.261  1.00 51.70  ? 117 THR B CA    1 
ATOM   4645 C C     . THR B 2 117 ? 133.457 126.206 86.447  1.00 55.86  ? 117 THR B C     1 
ATOM   4646 O O     . THR B 2 117 ? 134.592 126.375 86.905  1.00 63.75  ? 117 THR B O     1 
ATOM   4647 C CB    . THR B 2 117 ? 132.935 128.209 85.043  1.00 52.97  ? 117 THR B CB    1 
ATOM   4648 O OG1   . THR B 2 117 ? 132.038 129.315 84.879  1.00 61.85  ? 117 THR B OG1   1 
ATOM   4649 C CG2   . THR B 2 117 ? 132.898 127.357 83.784  1.00 51.32  ? 117 THR B CG2   1 
ATOM   4650 N N     . VAL B 2 118 ? 132.983 125.015 86.097  1.00 53.77  ? 118 VAL B N     1 
ATOM   4651 C CA    . VAL B 2 118 ? 133.749 123.783 86.231  1.00 51.08  ? 118 VAL B CA    1 
ATOM   4652 C C     . VAL B 2 118 ? 133.997 123.246 84.828  1.00 50.26  ? 118 VAL B C     1 
ATOM   4653 O O     . VAL B 2 118 ? 133.051 122.872 84.122  1.00 50.57  ? 118 VAL B O     1 
ATOM   4654 C CB    . VAL B 2 118 ? 133.025 122.750 87.103  1.00 54.39  ? 118 VAL B CB    1 
ATOM   4655 C CG1   . VAL B 2 118 ? 133.947 121.591 87.429  1.00 56.43  ? 118 VAL B CG1   1 
ATOM   4656 C CG2   . VAL B 2 118 ? 132.513 123.406 88.377  1.00 51.19  ? 118 VAL B CG2   1 
ATOM   4657 N N     . SER B 2 119 ? 135.264 123.203 84.424  1.00 49.48  ? 119 SER B N     1 
ATOM   4658 C CA    . SER B 2 119 ? 135.627 122.789 83.079  1.00 49.93  ? 119 SER B CA    1 
ATOM   4659 C C     . SER B 2 119 ? 135.585 121.267 82.960  1.00 55.39  ? 119 SER B C     1 
ATOM   4660 O O     . SER B 2 119 ? 135.350 120.542 83.931  1.00 58.56  ? 119 SER B O     1 
ATOM   4661 C CB    . SER B 2 119 ? 137.006 123.333 82.711  1.00 52.94  ? 119 SER B CB    1 
ATOM   4662 O OG    . SER B 2 119 ? 137.026 124.750 82.771  1.00 65.61  ? 119 SER B OG    1 
ATOM   4663 N N     . SER B 2 120 ? 135.818 120.776 81.747  1.00 54.24  ? 120 SER B N     1 
ATOM   4664 C CA    . SER B 2 120 ? 135.763 119.346 81.474  1.00 43.32  ? 120 SER B CA    1 
ATOM   4665 C C     . SER B 2 120 ? 136.888 118.917 80.538  1.00 45.60  ? 120 SER B C     1 
ATOM   4666 O O     . SER B 2 120 ? 138.067 119.083 80.850  1.00 50.29  ? 120 SER B O     1 
ATOM   4667 C CB    . SER B 2 120 ? 134.408 118.970 80.873  1.00 43.28  ? 120 SER B CB    1 
ATOM   4668 O OG    . SER B 2 120 ? 133.382 119.040 81.846  1.00 48.75  ? 120 SER B OG    1 
HETATM 4669 P PB    . ADP C 3 .   ? 118.569 123.615 141.161 1.00 61.95  ? 701 ADP A PB    1 
HETATM 4670 O O1B   . ADP C 3 .   ? 119.804 123.294 141.887 1.00 60.57  ? 701 ADP A O1B   1 
HETATM 4671 O O2B   . ADP C 3 .   ? 118.045 124.940 141.497 1.00 60.67  ? 701 ADP A O2B   1 
HETATM 4672 O O3B   . ADP C 3 .   ? 118.703 123.441 139.717 1.00 61.34  ? 701 ADP A O3B   1 
HETATM 4673 P PA    . ADP C 3 .   ? 117.268 121.121 141.173 1.00 57.42  ? 701 ADP A PA    1 
HETATM 4674 O O1A   . ADP C 3 .   ? 115.865 120.881 140.886 1.00 70.52  ? 701 ADP A O1A   1 
HETATM 4675 O O2A   . ADP C 3 .   ? 118.277 120.871 140.168 1.00 63.68  ? 701 ADP A O2A   1 
HETATM 4676 O O3A   . ADP C 3 .   ? 117.426 122.618 141.627 1.00 57.02  ? 701 ADP A O3A   1 
HETATM 4677 O "O5'" . ADP C 3 .   ? 117.595 120.191 142.387 1.00 56.55  ? 701 ADP A "O5'" 1 
HETATM 4678 C "C5'" . ADP C 3 .   ? 116.557 119.564 143.088 1.00 59.99  ? 701 ADP A "C5'" 1 
HETATM 4679 C "C4'" . ADP C 3 .   ? 116.958 119.691 144.518 1.00 58.32  ? 701 ADP A "C4'" 1 
HETATM 4680 O "O4'" . ADP C 3 .   ? 118.259 119.181 144.608 1.00 56.00  ? 701 ADP A "O4'" 1 
HETATM 4681 C "C3'" . ADP C 3 .   ? 117.034 121.145 144.849 1.00 53.84  ? 701 ADP A "C3'" 1 
HETATM 4682 O "O3'" . ADP C 3 .   ? 116.379 121.431 146.066 1.00 58.43  ? 701 ADP A "O3'" 1 
HETATM 4683 C "C2'" . ADP C 3 .   ? 118.468 121.386 145.075 1.00 50.96  ? 701 ADP A "C2'" 1 
HETATM 4684 O "O2'" . ADP C 3 .   ? 118.558 122.304 146.142 1.00 56.96  ? 701 ADP A "O2'" 1 
HETATM 4685 C "C1'" . ADP C 3 .   ? 119.001 120.032 145.435 1.00 51.25  ? 701 ADP A "C1'" 1 
HETATM 4686 N N9    . ADP C 3 .   ? 120.406 120.056 145.091 1.00 42.74  ? 701 ADP A N9    1 
HETATM 4687 C C8    . ADP C 3 .   ? 120.869 119.951 143.876 1.00 42.94  ? 701 ADP A C8    1 
HETATM 4688 N N7    . ADP C 3 .   ? 122.194 120.047 143.892 1.00 41.52  ? 701 ADP A N7    1 
HETATM 4689 C C5    . ADP C 3 .   ? 122.571 120.236 145.139 1.00 38.56  ? 701 ADP A C5    1 
HETATM 4690 C C6    . ADP C 3 .   ? 123.818 120.437 145.828 1.00 37.97  ? 701 ADP A C6    1 
HETATM 4691 N N6    . ADP C 3 .   ? 124.965 120.440 145.165 1.00 41.19  ? 701 ADP A N6    1 
HETATM 4692 N N1    . ADP C 3 .   ? 123.786 120.607 147.127 1.00 40.18  ? 701 ADP A N1    1 
HETATM 4693 C C2    . ADP C 3 .   ? 122.657 120.608 147.799 1.00 40.74  ? 701 ADP A C2    1 
HETATM 4694 N N3    . ADP C 3 .   ? 121.487 120.433 147.230 1.00 41.20  ? 701 ADP A N3    1 
HETATM 4695 C C4    . ADP C 3 .   ? 121.385 120.245 145.926 1.00 41.60  ? 701 ADP A C4    1 
HETATM 4696 P P     . PO4 D 4 .   ? 119.068 123.296 135.320 1.00 73.49  ? 702 PO4 A P     1 
HETATM 4697 O O1    . PO4 D 4 .   ? 120.508 123.499 134.743 1.00 68.00  ? 702 PO4 A O1    1 
HETATM 4698 O O2    . PO4 D 4 .   ? 118.056 123.157 134.132 1.00 61.93  ? 702 PO4 A O2    1 
HETATM 4699 O O3    . PO4 D 4 .   ? 119.038 121.996 136.198 1.00 71.86  ? 702 PO4 A O3    1 
HETATM 4700 O O4    . PO4 D 4 .   ? 118.670 124.526 136.206 1.00 66.43  ? 702 PO4 A O4    1 
# 
